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Enzyme 1
[top]
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| Enzyme 1 ID |
5240 |
| Enzyme 1 Name |
Histone acetyltransferase p300 |
| Enzyme 1 Synonyms |
- E1A-associated protein p300
|
| Enzyme 1 Gene Name |
EP300 |
| Enzyme 1 Protein Sequence |
>Histone acetyltransferase p300
MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGD
INQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINS
MVKSPMTQAGLTSPNMGMGTSGPNQGPTQSTGMMNSPVNQPAMGMNTGTNAGMNPGMLAA
GNGQGIMPNQVMNGSIGAGRGRQDMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQ
PLKMGMMNNPNPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMP
NMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGE
VRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNA
GDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQIDPSSIERAYAALGLPYQVNQM
PTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQ
NPMMSENASVPSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAAL
KDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPN
AAGMVPVSMNPGPNMGQPQPGMTSNGPLPDPSMIRGSVPNQMMPRITPQSGLNQFGQMSM
AQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNI
PLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTP
TPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPS
LPAAPSADQPQQQPRSQQSTAASVPTPNAPLLPPQPATPLSQPAVSIEGQVSNPPSTSST
EVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELK
TEIKEEEDQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVD
PQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYK
YCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHF
CEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVL
HHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGE
VTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQE
YGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPP
SEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKE
LPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNK
SSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIP
CDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETR
WHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQ
SLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENK
CPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSPTPATPTTPTG
QQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPG
PPPTAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMAPMGMNPPPMTRGPSGHL
EPGMGPTGMQQQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISP
LKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPI
PGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGG
MSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYP
PQPQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSP
QQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHV
SPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNS
DLNSNLSQSTLDIH
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| Enzyme 1 Number of Residues |
2414 |
| Enzyme 1 Molecular Weight |
264147 |
| Enzyme 1 Theoretical pI |
8.56 |
| Enzyme 1 GO Classification |
| Function |
- binding
- cation binding
- ion binding
- protein binding
- transcription coactivator activity
- transcription cofactor activity
- transcription factor binding
- transition metal ion binding
- zinc ion binding
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| Process |
- regulation of biological process
- regulation of cellular metabolism
- regulation of metabolism
- regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- regulation of physiological process
- regulation of transcription
- regulation of transcription, DNA-dependent
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| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 1 General Function |
Not Available |
| Enzyme 1 Specific Function |
Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes |
| Enzyme 1 Pathways |
Not Available |
| Enzyme 1 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
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| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
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| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
495301  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q09472  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
EP300_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>7245 bp
ATGGCCGAGAATGTGGTGGAACCGGGGCCGCCTTCAGCCAAGCGGCCTAAACTCTCATCT
CCGGCCCTCTCGGCGTCCGCCAGCGATGGCACAGATTTTGGCTCTCTATTTGACTTGGAG
CACGACTTACCAGATGAATTAATCAACTCTACAGAATTGGGACTAACCAATGGTGGTGAT
ATTAATCAGCTTCAGACAAGTCTTGGCATGGTACAAGATGCAGCTTCTAAACATAAACAG
CTGTCAGAATTGCTGCGATCTGGTAGTTCCCCTAACCTCAATATGGGAGTTGGTGGCCCA
GGTCAAGTCATGGCCAGCCAGGCCCAACAGAGCAGTCCTGGATTAGGTTTGATAAATAGC
ATGGTCAAAAGCCCAATGACACAGGCAGGCTTGACTTCTCCCAACATGGGGATGGGCACT
AGTGGACCAAATCAGGGTCCTACGCAGTCAACAGGTATGATGAACAGTCCAGTAAATCAG
CCTGCCATGGGAATGAACACAGGGACGAATGCGGGCATGAATCCTGGAATGTTGGCTGCA
GGCAATGGACAAGGGATAATGCCTAATCAAGTCATGAACGGTTCAATTGGAGCAGGCCGA
GGGCGACAGGATATGCAGTACCCAAACCCAGGCATGGGAAGTGCTGGCAACTTACTGACT
GAGCCTCTTCAGCAGGGCTCTCCCCAGATGGGAGGACAAACAGGATTGAGAGGCCCCCAG
CCTCTTAAGATGGGAATGATGAACAACCCCAATCCTTATGGTTCACCATATACTCAGAAT
CCTGGACAGCAGATTGGAGCCAGTGGCCTTGGTCTCCAGATTCAGACAAAAACTGTACTA
TCAAATAACTTATCTCCATTTGCTATGGACAAAAAGGCAGTTCCTGGTGGAGGAATGCCC
AACATGGGTCAACAGCCAGCCCCGCAGGTCCAGCAGCCAGGTCTGGTGACTCCAGTTGCC
CAAGGGATGGGTTCTGGAGCACATACAGCTGATCCAGAGAAGCGCAAGCTCATCCAGCAG
CAGCTTGTTCTCCTTTTGCATGCTCACAAGTGCCAGCGCCGGGAACAGGCCAATGGGGAA
GTGAGGCAGTGCAACCTTCCCCACTGTCGCACAATGAAGAATGTCCTAAACCACATGACA
CACTGCCAGTCAGGCAAGTCTTGCCAAGTGGCACACTGTGCATCTTCTCGACAAATCATT
TCACACTGGAAGAATTGTACAAGACATGATTGTCCTGTGTGTCTCCCCCTCAAAAATGCT
GGTGATAAGAGAAATCAACAGCCAATTTTGACTGGAGCACCCGTTGGACTTGGAAATCCT
AGCTCTCTAGGGGTGGGTCAACAGTCTGCCCCCAACCTAAGCACTGTTAGTCAGATTGAT
CCCAGCTCCATAGAAAGAGCCTATGCAGCTCTTGGACTACCCTATCAAGTAAATCAGATG
CCGACACAACCCCAGGTGCAAGCAAAGAACCAGCAGAATCAGCAGCCTGGGCAGTCTCCC
CAAGGCATGCGGCCCATGAGCAACATGAGTGCTAGTCCTATGGGAGTAAATGGAGGTGTA
GGAGTTCAAACGCCGAGTCTTCTTTCTGACTCAATGTTGCATTCAGCCATAAATTCTCAA
AACCCAATGATGAGTGAAAATGCCAGTGTGCCCTCCCTGGGTCCTATGCCAACAGCAGCT
CAACCATCCACTACTGGAATTCGGAAACAGTGGCACGAAGATATTACTCAGGATCTTCGA
AATCATCTTGTTCACAAACTCGTCCAAGCCATATTTCCTACGCCGGATCCTGCTGCTTTA
AAAGACAGACGGATGGAAAACCTAGTTGCATATGCTCGGAAAGTTGAAGGGGACATGTAT
GAATCTGCAAACAATCGAGCGGAATACTACCACCTTCTAGCTGAGAAAATCTATAAGATC
CAGAAAGAACTAGAAGAAAAACGAAGGACCAGACTACAGAAGCAGAACATGCTACCAAAT
GCTGCAGGCATGGTTCCAGTTTCCATGAATCCAGGGCCTAACATGGGACAGCCGCAACCA
GGAATGACTTCTAATGGCCCTCTACCTGACCCAAGTATGATCCGTGGCAGTGTGCCAAAC
CAGATGATGCCTCGAATAACTCCACAATCTGGTTTGAATCAATTTGGCCAGATGAGCATG
GCCCAGCCCCCTATTGTACCCCGGCAAACCCCTCCTCTTCAGCACCATGGACAGTTGGCT
CAACCTGGAGCTCTCAACCCGCCTATGGGCTATGGGCCTCGTATGCAACAGCCTTCCAAC
CAGGGCCAGTTCCTTCCTCAGACTCAGTTCCCATCACAGGGAATGAATGTAACAAATATC
CCTTTGGCTCCGTCCAGCGGTCAAGCTCCAGTGTCTCAAGCACAAATGTCTAGTTCTTCC
TGCCCGGTGAACTCTCCTATAATGCCTCCAGGGTCTCAGGGGAGCCACATTCACTGTCCC
CAGCTTCCTCAACCAGCTCTTCATCAGAATTCACCCTCGCCTGTACCTAGTCGTACCCCC
ACCCCTCACCATACTCCCCCAAGCATAGGGGCTCAGCAGCCACCAGCAACAACAATTCCA
GCCCCTGTTCCTACACCACCAGCCATGCCACCTGGGCCACAGTCCCAGGCTCTACATCCC
CCTCCAAGGCAGACACCTACACCACCAACAACACAACTTCCCCAACAAGTGCAGCCTTCA
CTTCCTGCTGCACCTTCTGCTGACCAGCCCCAGCAGCAGCCTCGCTCACAGCAGAGCACA
GCAGCGTCTGTTCCTACCCCAAACGCACCGCTGCTTCCTCCGCAGCCTGCAACTCCACTT
TCCCAGCCAGCTGTAAGCATTGAAGGACAGGTATCAAATCCTCCATCTACTAGTAGCACA
GAAGTGAATTCTCAGGCCATTGCTGAGAAGCAGCCTTCCCAGGAAGTGAAGATGGAGGCC
AAAATGGAAGTGGATCAACCAGAACCAGCAGATACGCAGCCGGAGGATATTTCAGAGTCT
AAAGTGGAAGACTGTAAAATGGAATCTACCGAAACAGAAGAGAGAAGCACTGAGTTAAAA
ACTGAAATAAAAGAGGAGGAAGACCAGCCAAGTACTTCAGCTACCCAGTCATCTCCGGCT
CCAGGACAGTCAAAGAAAAAGATTTTCAAACCAGAAGAACTACGACAGGCACTGATGCCA
ACATTGGAGGCACTTTACCGTCAGGATCCAGAATCCCTTCCCTTTCGTCAACCTGTGGAC
CCTCAGCTTTTAGGAATCCCTGATTACTTTGATATTGTGAAGAGCCCCATGGATCTTTCT
ACCATTAAGAGGAAGTTAGACACTGGACAGTATCAGGAGCCCTGGCAGTATGTCGATGAT
ATTTGGCTTATGTTCAATAATGCCTGGTTATATAACCGGAAAACATCACGGGTATACAAA
TACTGCTCCAAGCTCTCTGAGGTCTTTGAACAAGAAATTGACCCAGTGATGCAAAGCCTT
GGATACTGTTGTGGCAGAAAGTTGGAGTTCTCTCCACAGACACTGTGTTGCTACGGCAAA
CAGTTGTGCACAATACCTCGTGATGCCACTTATTACAGTTACCAGAACAGGTATCATTTC
TGTGAGAAGTGTTTCAATGAGATCCAAGGGGAGAGCGTTTCTTTGGGGGATGACCCTTCC
CAGCCTCAAACTACAATAAATAAAGAACAATTTTCCAAGAGAAAAAATGACACACTGGAT
CCTGAACTGTTTGTTGAATGTACAGAGTGCGGAAGAAAGATGCATCAGATCTGTGTCCTT
CACCATGAGATCATCTGGCCTGCTGGATTCGTCTGTGATGGCTGTTTAAAGAAAAGTGCA
CGAACTAGGAAAGAAAATAAGTTTTCTGCTAAAAGGTTGCCATCTACCAGACTTGGCACC
TTTCTAGAGAATCGTGTGAATGACTTTCTGAGGCGACAGAATCACCCTGAGTCAGGAGAG
GTCACTGTTAGAGTAGTTCATGCTTCTGACAAAACCGTGGAAGTAAAACCAGGCATGAAA
GCAAGGTTTGTGGACAGTGGAGAGATGGCAGAATCCTTTCCATACCGAACCAAAGCCCTC
TTTGCCTTTGAAGAAATTGATGGTGTTGACCTGTGCTTCTTTGGCATGCATGTTCAAGAG
TATGGCTCTGACTGCCCTCCACCCAACCAGAGGAGAGTATACATATCTTACCTCGATAGT
GTTCATTTCTTCCGTCCTAAATGCTTGAGGACTGCAGTCTATCATGAAATCCTAATTGGA
TATTTAGAATATGTCAAGAAATTAGGTTACACAACAGGGCATATTTGGGCATGTCCACCA
AGTGAGGGAGATGATTATATCTTCCATTGCCATCCTCCTGACCAGAAGATACCCAAGCCC
AAGCGACTGCAGGAATGGTACAAAAAAATGCTTGACAAGGCTGTATCAGAGCGTATTGTC
CATGACTACAAGGATATTTTTAAACAAGCTACTGAAGATAGATTAACAAGTGCAAAGGAA
TTGCCTTATTTCGAGGGTGATTTCTGGCCCAATGTTCTGGAAGAAAGCATTAAGGAACTG
GAACAGGAGGAAGAAGAGAGAAAACGAGAGGAAAACACCAGCAATGAAAGCACAGATGTG
ACCAAGGGAGACAGCAAAAATGCTAAAAAGAAGAATAATAAGAAAACCAGCAAAAATAAG
AGCAGCCTGAGTAGGGGCAACAAGAAGAAACCCGGGATGCCCAATGTATCTAACGACCTC
TCACAGAAACTATATGCCACCATGGAGAAGCATAAAGAGGTCTTCTTTGTGATCCGCCTC
ATTGCTGGCCCTGCTGCCAACTCCCTGCCTCCCATTGTTGATCCTGATCCTCTCATCCCC
TGCGATCTGATGGATGGTCGGGATGCGTTTCTCACGCTGGCAAGGGACAAGCACCTGGAG
TTCTCTTCACTCCGAAGAGCCCAGTGGTCCACCATGTGCATGCTGGTGGAGCTGCACACG
CAGAGCCAGGACCGCTTTGTCTACACCTGCAATGAATGCAAGCACCATGTGGAGACACGC
TGGCACTGTACTGTCTGTGAGGATTATGACTTGTGTATCACCTGCTATAACACTAAAAAC
CATGACCACAAAATGGAGAAACTAGGCCTTGGCTTAGATGATGAGAGCAACAACCAGCAG
GCTGCAGCCACCCAGAGCCCAGGCGATTCTCGCCGCCTGAGTATCCAGCGCTGCATCCAG
TCTCTGGTCCATGCTTGCCAGTGTCGGAATGCCAATTGCTCACTGCCATCCTGCCAGAAG
ATGAAGCGGGTTGTGCAGCATACCAAGGGTTGCAAACGGAAAACCAATGGCGGGTGCCCC
ATCTGCAAGCAGCTCATTGCCCTCTGCTGCTACCATGCCAAGCACTGCCAGGAGAACAAA
TGCCCGGTGCCGTTCTGCCTAAACATCAAGCAGAAGCTCCGGCAGCAACAGCTGCAGCAC
CGACTACAGCAGGCCCAAATGCTTCGCAGGAGGATGGCCAGCATGCAGCGGACTGGTGTG
GTTGGGCAGCAACAGGGCCTCCCTTCCCCCACTCCTGCCACTCCAACGACACCAACTGGC
CAACAGCCAACCACCCCGCAGACGCCCCAGCCCACTTCTCAGCCTCAGCCTACCCCTCCC
AATAGCATGCCACCCTACTTGCCCAGGACTCAAGCTGCTGGCCCTGTGTCCCAGGGTAAG
GCAGCAGGCCAGGTGACCCCTCCAACCCCTCCTCAGACTGCTCAGCCACCCCTTCCAGGG
CCCCCACCTACAGCAGTGGAAATGGCAATGCAGATTCAGAGAGCAGCGGAGACGCAGCGC
CAGATGGCCCACGTGCAAATTTTTCAAAGGCCAATCCAACACCAGATGCCCCCGATGACT
CCCATGGCCCCCATGGGTATGAACCCACCTCCCATGACCAGAGGTCCCAGTGGGCATTTG
GAGCCAGGGATGGGACCGACAGGGATGCAGCAACAGCCACCCTGGAGCCAAGGAGGATTG
CCTCAGCCCCAGCAACTACAGTCTGGGATGCCAAGGCCAGCCATGATGTCAGTGGCCCAG
CATGGTCAACCTTTGAACATGGCTCCACAACCAGGATTGGGCCAGGTAGGTATCAGCCCA
CTCAAACCAGGCACTGTGTCTCAACAAGCCTTACAAAACCTTTTGCGGACTCTCAGGTCT
CCCAGCTCTCCCCTGCAGCAGCAACAGGTGCTTAGTATCCTTCACGCCAACCCCCAGCTG
TTGGCTGCATTCATCAAGCAGCGGGCTGCCAAGTATGCCAACTCTAATCCACAACCCATC
CCTGGGCAGCCTGGCATGCCCCAGGGGCAGCCAGGGCTACAGCCACCTACCATGCCAGGT
CAGCAGGGGGTCCACTCCAATCCAGCCATGCAGAACATGAATCCAATGCAGGCGGGCGTT
CAGAGGGCTGGCCTGCCCCAGCAGCAACCACAGCAGCAACTCCAGCCACCCATGGGAGGG
ATGAGCCCCCAGGCTCAGCAGATGAACATGAACCACAACACCATGCCTTCACAATTCCGA
GACATCTTGAGACGACAGCAAATGATGCAACAGCAGCAGCAACAGGGAGCAGGGCCAGGA
ATAGGCCCTGGAATGGCCAACCATAACCAGTTCCAGCAACCCCAAGGAGTTGGCTACCCA
CCACAGCCGCAGCAGCGGATGCAGCATCACATGCAACAGATGCAACAAGGAAATATGGGA
CAGATAGGCCAGCTTCCCCAGGCCTTGGGAGCAGAGGCAGGTGCCAGTCTACAGGCCTAT
CAGCAGCGACTCCTTCAGCAACAGATGGGGTCCCCTGTTCAGCCCAACCCCATGAGCCCC
CAGCAGCATATGCTCCCAAATCAGGCCCAGTCCCCACACCTACAAGGCCAGCAGATCCCT
AATTCTCTCTCCAATCAAGTGCGCTCTCCCCAGCCTGTCCCTTCTCCACGGCCACAGTCC
CAGCCCCCCCACTCCAGTCCTTCCCCAAGGATGCAGCCTCAGCCTTCTCCACACCACGTT
TCCCCACAGACAAGTTCCCCACATCCTGGACTGGTAGCTGCCCAGGCCAACCCCATGGAA
CAAGGGCATTTTGCCAGCCCGGACCAGAATTCAATGCTTTCTCAGCTTGCTAGCAATCCA
GGCATGGCAAACCTCCATGGTGCAAGCGCCACGGACCTGGGACTCAGCACCGATAACTCA
GACTTGAATTCAAACCTCTCACAGAGTACACTAGACATACACTAG
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| Enzyme 1 GenBank Gene ID |
U01877  |
| Enzyme 1 GeneCard ID |
EP300  |
| Enzyme 1 GenAtlas ID |
EP300  |
| Enzyme 1 HGNC ID |
HGNC:3373  |
| Enzyme 1 Chromosome Location |
22 |
| Enzyme 1 Locus |
22q13.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Eckner R, Ewen ME, Newsome D, Gerdes M, DeCaprio JA, Lawrence JB, Livingston DM: Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes Dev. 1994 Apr 15;8(8):869-84. [PubMed
]
- Xu W, Chen H, Du K, Asahara H, Tini M, Emerson BM, Montminy M, Evans RM: A transcriptional switch mediated by cofactor methylation. Science. 2001 Dec 21;294(5551):2507-11. Epub 2001 Nov 8. [PubMed
]
- Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y: The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell. 1996 Nov 29;87(5):953-9. [PubMed
]
- Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature. 1996 Jul 25;382(6589):319-24. [PubMed
]
- Arany Z, Huang LE, Eckner R, Bhattacharya S, Jiang C, Goldberg MA, Bunn HF, Livingston DM: An essential role for p300/CBP in the cellular response to hypoxia. Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12969-73. [PubMed
]
- Fryer CJ, Archer TK: Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex. Nature. 1998 May 7;393(6680):88-91. [PubMed
]
- Ko L, Cardona GR, Chin WW: Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator. Proc Natl Acad Sci U S A. 2000 May 23;97(11):6212-7. [PubMed
]
- Gizard F, Lavallee B, DeWitte F, Hum DW: A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression. J Biol Chem. 2001 Sep 7;276(36):33881-92. Epub 2001 May 10. [PubMed
]
- Vadlamudi RK, Wang RA, Mazumdar A, Kim Y, Shin J, Sahin A, Kumar R: Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha. J Biol Chem. 2001 Oct 12;276(41):38272-9. Epub 2001 Jul 31. [PubMed
]
- Yamamoto N, Yamamoto S, Inagaki F, Kawaichi M, Fukamizu A, Kishi N, Matsuno K, Nakamura K, Weinmaster G, Okano H, Nakafuku M: Role of Deltex-1 as a transcriptional regulator downstream of the Notch receptor. J Biol Chem. 2001 Nov 30;276(48):45031-40. Epub 2001 Sep 19. [PubMed
]
- Braganca J, Swingler T, Marques FI, Jones T, Eloranta JJ, Hurst HC, Shioda T, Bhattacharya S: Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2. J Biol Chem. 2002 Mar 8;277(10):8559-65. Epub 2001 Dec 14. [PubMed
]
- Shiseki M, Nagashima M, Pedeux RM, Kitahama-Shiseki M, Miura K, Okamura S, Onogi H, Higashimoto Y, Appella E, Yokota J, Harris CC: p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity. Cancer Res. 2003 May 15;63(10):2373-8. [PubMed
]
- Hecht A, Stemmler MP: Identification of a promoter-specific transcriptional activation domain at the C terminus of the Wnt effector protein T-cell factor 4. J Biol Chem. 2003 Feb 7;278(6):3776-85. Epub 2002 Nov 22. [PubMed
]
- Freedman SJ, Sun ZY, Poy F, Kung AL, Livingston DM, Wagner G, Eck MJ: Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha. Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5367-72. [PubMed
]
- Gayther SA, Batley SJ, Linger L, Bannister A, Thorpe K, Chin SF, Daigo Y, Russell P, Wilson A, Sowter HM, Delhanty JD, Ponder BA, Kouzarides T, Caldas C: Mutations truncating the EP300 acetylase in human cancers. Nat Genet. 2000 Mar;24(3):300-3. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
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Enzyme 2
[top]
|
| Enzyme 2 ID |
5243 |
| Enzyme 2 Name |
CREB-binding protein |
| Enzyme 2 Synonyms |
Not Available |
| Enzyme 2 Gene Name |
CREBBP |
| Enzyme 2 Protein Sequence |
>CREB-binding protein
MAENLLDGPPNPKRAKLSSPGFSANDSTDFGSLFDLENDLPDELIPNGGELGLLNSGNLV
PDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSANMASLSAMGK
SPLSQGDSSAPSLPKQAASTSGPTPAASQALNPQAQKQVGLATSSPATSQTGPGICMNAN
FNQTHPGLLNSNSGHSLINQASQGQAQVMNGSLGAAGRGRGAGMPYPTPAMQGASSSVLA
ETLTQVSPQMTGHAGLNTAQAGGMAKMGITGNTSPFGQPFSQAGGQPMGATGVNPQLASK
QSMVNSLPTFPTDIKNTSVTNVPNMSQMQTSVGIVPTQAIATGPTADPEKRKLIQQQLVL
LLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWK
NCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGTGQQNATSLSNPNPIDPSS
MQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPQTHQQMRTLNPLGNNPMNIPAGGITTDQ
QPPNLISESALPTSLGATNPLMNDGSNSGNIGTLSTIPTAAPPSSTGVRKGWHEHVTQDL
RSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYK
IQKELEEKRRSRLHKQGILGNQPALPAPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVSQG
MNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPNMMGAHT
NNMMAQAPAQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPLNMLGPQA
SQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTPVSSSGQTPT
PTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTP
LSQAAASIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRSE
MMEEDLQGASQVKEETDIAEQKSEPMEVDEKKPEVKVEVKEEEESSSNGTASQSTSPSQP
RKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKR
KLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCC
GRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQT
TISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRK
ENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFV
DSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDCPPPNTRRVYISYLDSIHFF
RPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQ
EWYKKMLDKAFAERIIHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEE
EERKKEESTAASETTEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQK
LYATMEKHKEVFFVIHLHAGPVINTLPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSS
LRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAH
KMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKR
VVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQ
QAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVSMSPAG
FPSVARTQPPTTVSTGKPTSQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRVNINNS
MPPGRTGMGTPGSQMAPVSLNVPRPNQVSGPVMPSMPPGQWQQAPLPQQQPMPGLPRPVI
SMQAQAAVAGPRMPSVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAF
IKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPQQQA
MGGLNPQGQALNIMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAG
MAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQHLPLQGSSMGQMAAQMGQLGQMGQPGLG
ADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLS
NQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSIDQGHL
GNPEQSAMLPQLNTPSRSALSSELSLVGDTTGDTLEKFVEGL
|
| Enzyme 2 Number of Residues |
2442 |
| Enzyme 2 Molecular Weight |
265354 |
| Enzyme 2 Theoretical pI |
8.63 |
| Enzyme 2 GO Classification |
| Function |
- binding
- cation binding
- ion binding
- protein binding
- transcription coactivator activity
- transcription cofactor activity
- transcription factor binding
- transition metal ion binding
- zinc ion binding
|
| Process |
- regulation of biological process
- regulation of cellular metabolism
- regulation of metabolism
- regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- regulation of physiological process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
Acetyltransferase enzyme. Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non- histone proteins, like NCOA3 coactivator. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. CREBBP, as coactivator, augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes |
| Enzyme 2 Pathways |
Not Available |
| Enzyme 2 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
4321116  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q92793  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
CBP_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>7329 bp
ATGGCTGAGAACTTGCTGGACGGACCGCCCAACCCCAAAAGAGCCAAACTCAGCTCGCCC
GGTTTCTCGGCGAATGACAGCACAGATTTTGGATCATTGTTTGACTTGGAAAATGATCTT
CCTGATGAGCTGATACCCAATGGAGGAGAATTAGGCCTTTTAAACAGTGGGAACCTTGTT
CCAGATGCTGCTTCCAAACATAAACAACTGTCGGAGCTTCTACGAGGAGGCAGCGGCTCT
AGTATCAACCCAGGAATAGGAAATGTGAGCGCCAGCAGCCCCGTGCAGCAGGGCCTGGGT
GGCCAGGCTCAAGGGCAGCCGAACAGTGCTAACATGGCCAGCCTCAGTGCCATGGGCAAG
AGCCCTCTGAGCCAGGGAGATTCTTCAGCCCCCAGCCTGCCTAAACAGGCAGCCAGCACC
TCTGGGCCCACCCCCGCTGCCTCCCAAGCACTGAATCCGCAAGCACAAAAGCAAGTGGGG
CTGGCGACTAGCAGCCCTGCCACGTCACAGACTGGACCTGGTATCTGCATGAATGCTAAC
TTTAACCAGACCCACCCAGGCCTCCTCAATAGTAACTCTGGCCATAGCTTAATTAATCAG
GCTTCACAAGGGCAGGCGCAAGTCATGAATGGATCTCTTGGGGCTGCTGGCAGAGGAAGG
GGAGCTGGAATGCCGTACCCTACTCCAGCCATGCAGGGCGCCTCGAGCAGCGTGCTGGCT
GAGACCCTAACGCAGGTTTCCCCGCAAATGACTGGTCACGCGGGACTGAACACCGCACAG
GCAGGAGGCATGGCCAAGATGGGAATAACTGGGAACACAAGTCCATTTGGACAGCCCTTT
AGTCAAGCTGGAGGGCAGCCAATGGGAGCCACTGGAGTGAACCCCCAGTTAGCCAGCAAA
CAGAGCATGGTCAACAGTTTGCCCACCTTCCCTACAGATATCAAGAATACTTCAGTCACC
AACGTGCCAAATATGTCTCAGATGCAAACATCAGTGGGAATTGTACCCACACAAGCAATT
GCAACAGGCCCCACTGCAGATCCTGAAAAACGCAAACTGATACAGCAGCAGCTGGTTCTA
CTGCTTCATGCTCATAAGTGTCAGAGACGAGAGCAAGCAAACGGAGAGGTTCGGGCCTGC
TCGCTCCCGCATTGTCGAACCATGAAAAACGTTTTGAATCACATGACGCATTGTCAGGCT
GGGAAAGCCTGCCAAGTTGCCCATTGTGCATCTTCACGACAAATCATCTCTCATTGGAAG
AACTGCACACGACATGACTGTCCTGTTTGCCTCCCTTTGAAAAATGCCAGTGACAAGCGA
AACCAACAAACCATCCTGGGGTCTCCAGCTAGTGGAATTCAAAACACAATTGGTTCTGTT
GGCACAGGGCAACAGAATGCCACTTCTTTAAGTAACCCAAATCCCATAGACCCCAGCTCC
ATGCAGCGAGCCTATGCTGCTCTCGGACTCCCCTACATGAACCAGCCCCAGACGCAGCTG
CAGCCTCAGGTTCCTGGCCAGCAACCAGCACAGCCTCAAACCCACCAGCAGATGAGGACT
CTCAACCCCCTGGGAAATAATCCAATGAACATTCCAGCAGGAGGAATAACAACAGATCAG
CAGCCCCCAAACTTGATTTCAGAATCAGCTCTTCCGACTTCCCTGGGGGCCACAAACCCA
CTGATGAACGATGGCTCCAACTCTGGTAACATTGGAACCCTCAGCACTATACCAACAGCA
GCTCCTCCTTCTAGCACCGGTGTAAGGAAAGGCTGGCACGAACATGTCACTCAGGACCTG
CGGAGCCATCTAGTGCATAAACTCGTCCAAGCCATCTTCCCAACACCTGATCCCGCAGCT
CTAAAGGATCGCCGCATGGAAAACCTGGTAGCCTATGCTAAGAAAGTGGAAGGGGACATG
TACGAGTCTGCCAACAGCAGGGATGAATATTATCACTTATTAGCAGAGAAAATCTACAAG
ATACAAAAAGAACTAGAAGAAAAACGGAGGTCGCGTTTACATAAACAAGGCATCTTGGGG
AACCAGCCAGCCTTACCAGCCCCGGGGGCTCAGCCCCCTGTGATTCCACAGGCACAACCT
GTGAGACCTCCAAATGGACCCCTGTCCCTGCCAGTGAATCGCATGCAAGTTTCTCAAGGG
ATGAATTCATTTAACCCCATGTCCTTGGGGAACGTCCAGTTGCCACAAGCACCCATGGGA
CCTCGTGCAGCCTCCCCAATGAACCACTCTGTCCAGATGAACAGCATGGGCTCAGTGCCA
GGGATGGCCATTTCTCCTTCCCGAATGCCTCAGCCTCCGAACATGATGGGTGCACACACC
AACAACATGATGGCCCAGGCGCCCGCTCAGAGCCAGTTTCTGCCACAGAACCAGTTCCCG
TCATCCAGCGGGGCGATGAGTGTGGGCATGGGGCAGCCGCCAGCCCAAACAGGCGTGTCA
CAGGGACAGGTGCCTGGTGCTGCTCTTCCTAACCCTCTCAACATGCTGGGGCCTCAGGCC
AGCCAGCTACCTTGCCCTCCAGTGACACAGTCACCACTGCACCCAACACCGCCTCCTGCT
TCCACGGCTGCTGGCATGCCATCTCTCCAGCACACGACACCACCTGGGATGACTCCTCCC
CAGCCAGCAGCTCCCACTCAGCCATCAACTCCTGTGTCGTCTTCCGGGCAGACTCCCACC
CCGACTCCTGGCTCAGTGCCCAGTGCTACCCAAACCCAGAGCACCCCTACAGTCCAGGCA
GCAGCCCAGGCCCAGGTGACCCCGCAGCCTCAAACCCCAGTTCAGCCCCCGTCTGTGGCT
ACCCCTCAGTCATCGCAGCAACAGCCGACGCCTGTGCACGCCCAGCCTCCTGGCACACCG
CTTTCCCAGGCAGCAGCCAGCATTGATAACAGAGTCCCTACCCCCTCCTCGGTGGCCAGC
GCAGAAACCAATTCCCAGCAGCCAGGACCTGACGTACCTGTGCTGGAAATGAAGACGGAG
ACCCAAGCAGAGGACACTGAGCCCGATCCTGGTGAATCCAAAGGGGAGCCCAGGTCTGAG
ATGATGGAGGAGGATTTGCAAGGAGCTTCCCAAGTTAAAGAAGAAACAGACATAGCAGAG
CAGAAATCAGAACCAATGGAAGTGGATGAAAAGAAACCTGAAGTGAAAGTAGAAGTTAAA
GAGGAAGAAGAGAGTAGCAGTAACGGCACAGCCTCTCAGTCAACATCTCCTTCGCAGCCG
CGCAAAAAAATCTTTAAACCAGAGGAGTTACGCCAGGCCCTCATGCCAACCCTAGAAGCA
CTGTATCGACAGGACCCAGAGTCATTACCTTTCCGGCAGCCTGTAGATCCCCAGCTCCTC
GGAATTCCAGACTATTTTGACATCGTAAAGAATCCCATGGACCTCTCCACCATCAAGCGG
AAGCTGGACACAGGGCAATACCAAGAGCCCTGGCAGTACGTGGACGACGTCTGGCTCATG
TTCAACAATGCCTGGCTCTATAATCGCAAGACATCCCGAGTCTATAAGTTTTGCAGTAAG
CTTGCAGAGGTCTTTGAGCAGGAAATTGACCCTGTCATGCAGTCCCTTGGATATTGCTGT
GGACGCAAGTATGAGTTTTCCCCACAGACTTTGTGCTGCTATGGGAAGCAGCTGTGTACC
ATTCCTCGCGATGCTGCCTACTACAGCTATCAGAATAGGTATCATTTCTGTGAGAAGTGT
TTCACAGAGATCCAGGGCGAGAATGTGACCCTGGGTGACGACCCTTCACAGCCCCAGACG
ACAATTTCAAAGGATCAGTTTGAAAAGAAGAAAAATGATACCTTAGACCCCGAACCTTTC
GTTGATTGCAAGGAGTGTGGCCGGAAGATGCATCAGATTTGCGTTCTGCACTATGACATC
ATTTGGCCTTCAGGTTTTGTGTGCGACAACTGCTTGAAGAAAACTGGCAGACCTCGAAAA
GAAAACAAATTCAGTGCTAAGAGGCTGCAGACCACAAGACTGGGAAACCACTTGGAAGAC
CGAGTGAACAAATTTTTGCGGCGCCAGAATCACCCTGAAGCCGGGGAGGTTTTTGTCCGA
GTGGTGGCCAGCTCAGACAAGACGGTGGAGGTCAAGCCCGGGATGAAGTCACGGTTTGTG
GATTCTGGGGAAATGTCTGAATCTTTCCCATATCGAACCAAAGCTCTGTTTGCTTTTGAG
GAAATTGACGGCGTGGATGTCTGCTTTTTTGGAATGCACGTCCAAGAATACGGCTCTGAT
TGCCCCCCTCCAAACACGAGGCGTGTGTACATTTCTTATCTGGATAGTATTCATTTCTTC
CGGCCACGTTGCCTCCGCACAGCCGTTTACCATGAGATCCTTATTGGATATTTAGAGTAT
GTGAAGAAATTAGGGTATGTGACAGGGCACATCTGGGCCTGTCCTCCAAGTGAAGGAGAT
GATTACATCTTCCATTGCCACCCACCTGATCAAAAAATACCCAAGCCAAAACGACTGCAG
GAGTGGTACAAAAAGATGCTGGACAAGGCGTTTGCAGAGCGGATCATCCATGACTACAAG
GATATTTTCAAACAAGCAACTGAAGACAGGCTCACCAGTGCCAAGGAACTGCCCTATTTT
GAAGGTGATTTCTGGCCCAATGTGTTAGAAGAGAGCATTAAGGAACTAGAACAAGAAGAA
GAGGAGAGGAAAAAGGAAGAGAGCACTGCAGCCAGTGAAACCACTGAGGGCAGTCAGGGC
GACAGCAAGAATGCCAAGAAGAAGAACAACAAGAAAACCAACAAGAACAAAAGCAGCATC
AGCCGCGCCAACAAGAAGAAGCCCAGCATGCCCAACGTGTCCAATGACCTGTCCCAGAAG
CTGTATGCCACCATGGAGAAGCACAAGGAGGTCTTCTTCGTGATCCACCTGCACGCTGGG
CCTGTCATCAACACCCTGCCCCCCATCGTCGACCCCGACCCCCTGCTCAGCTGTGACCTC
ATGGATGGGCGCGACGCCTTCCTCACCCTCGCCAGAGACAAGCACTGGGAGTTCTCCTCC
TTGCGCCGCTCCAAGTGGTCCACGCTCTGCATGCTGGTGGAGCTGCACACCCAGGGCCAG
GACCGCTTTGTCTACACCTGCAACGAGTGCAAGCACCACGTGGAGACGCGCTGGCACTGC
ACTGTGTGCGAGGACTACGACCTCTGCATCAACTGCTATAACACGAAGAGCCATGCCCAT
AAGATGGTGAAGTGGGGGCTGGGCCTGGATGACGAGGGCAGCAGCCAGGGCGAGCCACAG
TCAAAGAGCCCCCAGGAGTCACGCCGGCTGAGCATCCAGCGCTGCATCCAGTCGCTGGTG
CACGCGTGCCAGTGCCGCAACGCCAACTGCTCGCTGCCATCCTGCCAGAAGATGAAGCGG
GTGGTGCAGCACACCAAGGGCTGCAAACGCAAGACCAACGGGGGCTGCCCGGTGTGCAAG
CAGCTCATCGCCCTCTGCTGCTACCACGCCAAGCACTGCCAAGAAAACAAATGCCCCGTG
CCCTTCTGCCTCAACATCAAACACAAGCTCCGCCAGCAGCAGATCCAGCACCGCCTGCAG
CAGGCCCAGCTCATGCGCCGGCGGATGGCCACCATGAACACCCGCAACGTGCCTCAGCAG
AGTCTGCCTTCTCCTACCTCAGCACCGCCCGGGACCCCCACACAGCAGCCCAGCACACCC
CAGACGCCGCAGCCCCCTGCCCAGCCCCAACCCTCACCCGTGAGCATGTCACCAGCTGGC
TTCCCCAGCGTGGCCCGGACTCAGCCCCCCACCACGGTGTCCACAGGGAAGCCTACCAGC
CAGGTGCCGGCCCCCCCACCCCCGGCCCAGCCCCCTCCTGCAGCGGTGGAAGCGGCTCGG
CAGATCGAGCGTGAGGCCCAGCAGCAGCAGCACCTGTACCGGGTGAACATCAACAACAGC
ATGCCCCCAGGACGCACGGGCATGGGGACCCCGGGGAGCCAGATGGCCCCCGTGAGCCTG
AATGTGCCCCGACCCAACCAGGTGAGCGGGCCCGTCATGCCCAGCATGCCTCCCGGGCAG
TGGCAGCAGGCGCCCCTTCCCCAGCAGCAGCCCATGCCAGGCTTGCCCAGGCCTGTGATA
TCCATGCAGGCCCAGGCGGCCGTGGCTGGGCCCCGGATGCCCAGCGTGCAGCCACCCAGG
AGCATCTCACCCAGCGCTCTGCAAGACCTGCTGCGGACCCTGAAGTCGCCCAGCTCCCCT
CAGCAGCAACAGCAGGTGCTGAACATTCTCAAATCAAACCCGCAGCTAATGGCAGCTTTC
ATCAAACAGCGCACAGCCAAGTACGTGGCCAATCAGCCCGGCATGCAGCCCCAGCCTGGC
CTCCAGTCCCAGCCCGGCATGCAACCCCAGCCTGGCATGCACCAGCAGCCCAGCCTGCAG
AACCTGAATGCCATGCAGGCTGGCGTGCCGCGGCCCGGTGTGCCTCCACAGCAGCAGGCG
ATGGGAGGCCTGAACCCCCAGGGCCAGGCCTTGAACATCATGAACCCAGGACACAACCCC
AACATGGCGAGTATGAATCCACAGTACCGAGAAATGTTACGGAGGCAGCTGCTGCAGCAG
CAGCAGCAACAGCAGCAGCAACAACAGCAGCAACAGCAGCAGCAGCAAGGGAGTGCCGGC
ATGGCTGGGGGCATGGCGGGGCACGGCCAGTTCCAGCAGCCTCAAGGACCCGGAGGCTAC
CCACCGGCCATGCAGCAGCAGCAGCGCATGCAGCAGCATCTCCCCCTCCAGGGCAGCTCC
ATGGGCCAGATGGCGGCTCAGATGGGACAGCTTGGCCAGATGGGGCAGCCGGGGCTGGGG
GCAGACAGCACCCCCAACATCCAGCAAGCCCTGCAGCAGCGGATTCTGCAGCAACAGCAG
ATGAAGCAGCAGATTGGGTCCCCAGGCCAGCCGAACCCCATGAGCCCCCAGCAACACATG
CTCTCAGGACAGCCACAGGCCTCGCATCTCCCTGGCCAGCAGATCGCCACGTCCCTTAGT
AACCAGGTGCGGTCTCCAGCCCCTGTCCAGTCTCCACGGCCCCAGTCCCAGCCTCCACAT
TCCAGCCCGTCACCACGGATACAGCCCCAGCCTTCGCCACACCACGTCTCACCCCAGACT
GGTTCCCCCCACCCCGGACTCGCAGTCACCATGGCCAGCTCCATAGATCAGGGACACTTG
GGGAACCCCGAACAGAGTGCAATGCTCCCCCAGCTGAACACCCCCAGCAGGAGTGCGCTG
TCCAGCGAACTGTCCCTGGTCGGGGACACCACGGGGGACACGCTAGAGAAGTTTGTGGAG
GGCTTGTAG
|
| Enzyme 2 GenBank Gene ID |
U85962  |
| Enzyme 2 GeneCard ID |
CREBBP  |
| Enzyme 2 GenAtlas ID |
CREBBP  |
| Enzyme 2 HGNC ID |
HGNC:2348  |
| Enzyme 2 Chromosome Location |
16 |
| Enzyme 2 Locus |
16p13.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Sobulo OM, Borrow J, Tomek R, Reshmi S, Harden A, Schlegelberger B, Housman D, Doggett NA, Rowley JD, Zeleznik-Le NJ: MLL is fused to CBP, a histone acetyltransferase, in therapy-related acute myeloid leukemia with a t(11;16)(q23;p13.3). Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8732-7. [PubMed
]
- Giles RH, Petrij F, Dauwerse HG, den Hollander AI, Lushnikova T, van Ommen GJ, Goodman RH, Deaven LL, Doggett NA, Peters DJ, Breuning MH: Construction of a 1.2-Mb contig surrounding, and molecular analysis of, the human CREB-binding protein (CBP/CREBBP) gene on chromosome 16p13.3. Genomics. 1997 May 15;42(1):96-114. [PubMed
]
- Borrow J, Stanton VP Jr, Andresen JM, Becher R, Behm FG, Chaganti RS, Civin CI, Disteche C, Dube I, Frischauf AM, Horsman D, Mitelman F, Volinia S, Watmore AE, Housman DE: The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein. Nat Genet. 1996 Sep;14(1):33-41. [PubMed
]
- Panagopoulos I, Fioretos T, Isaksson M, Samuelsson U, Billstrom R, Strombeck B, Mitelman F, Johansson B: Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13). Hum Mol Genet. 2001 Feb 15;10(4):395-404. [PubMed
]
- Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature. 1996 Jul 25;382(6589):319-24. [PubMed
]
- Arany Z, Huang LE, Eckner R, Bhattacharya S, Jiang C, Goldberg MA, Bunn HF, Livingston DM: An essential role for p300/CBP in the cellular response to hypoxia. Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12969-73. [PubMed
]
- Doucas V, Tini M, Egan DA, Evans RM: Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling. Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):2627-32. [PubMed
]
- Chen H, Lin RJ, Xie W, Wilpitz D, Evans RM: Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell. 1999 Sep 3;98(5):675-86. [PubMed
]
- Mahajan MA, Samuels HH: A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein. Mol Cell Biol. 2000 Jul;20(14):5048-63. [PubMed
]
- Gizard F, Lavallee B, DeWitte F, Hum DW: A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression. J Biol Chem. 2001 Sep 7;276(36):33881-92. Epub 2001 May 10. [PubMed
]
- Vadlamudi RK, Wang RA, Mazumdar A, Kim Y, Shin J, Sahin A, Kumar R: Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha. J Biol Chem. 2001 Oct 12;276(41):38272-9. Epub 2001 Jul 31. [PubMed
]
- Braganca J, Swingler T, Marques FI, Jones T, Eloranta JJ, Hurst HC, Shioda T, Bhattacharya S: Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2. J Biol Chem. 2002 Mar 8;277(10):8559-65. Epub 2001 Dec 14. [PubMed
]
- Wu RC, Qin J, Hashimoto Y, Wong J, Xu J, Tsai SY, Tsai MJ, O'Malley BW: Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) Coactivator activity by I kappa B kinase. Mol Cell Biol. 2002 May;22(10):3549-61. [PubMed
]
- Watanabe N, Wachi S, Fujita T: Identification and characterization of BCL-3-binding protein: implications for transcription and DNA repair or recombination. J Biol Chem. 2003 Jul 11;278(28):26102-10. Epub 2003 May 2. [PubMed
]
- Dames SA, Martinez-Yamout M, De Guzman RN, Dyson HJ, Wright PE: Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response. Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5271-6. [PubMed
]
- Murata T, Kurokawa R, Krones A, Tatsumi K, Ishii M, Taki T, Masuno M, Ohashi H, Yanagisawa M, Rosenfeld MG, Glass CK, Hayashi Y: Defect of histone acetyltransferase activity of the nuclear transcriptional coactivator CBP in Rubinstein-Taybi syndrome. Hum Mol Genet. 2001 May 1;10(10):1071-6. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5351 |
| Enzyme 3 Name |
Ectonucleotide pyrophosphatase/phosphodiesterase family member 1 |
| Enzyme 3 Synonyms |
- E- NPP 1
- Phosphodiesterase I/nucleotide pyrophosphatase 1
- Plasma-cell membrane glycoprotein PC-1[Includes: Alkaline phosphodiesterase I
- NPPase]
|
| Enzyme 3 Gene Name |
ENPP1 |
| Enzyme 3 Protein Sequence |
>Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED
|
| Enzyme 3 Number of Residues |
925 |
| Enzyme 3 Molecular Weight |
104925 |
| Enzyme 3 Theoretical pI |
7.14 |
| Enzyme 3 GO Classification |
| Function |
- binding
- catalytic activity
- endonuclease activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- nuclease activity
- nucleic acid binding
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 Specific Function |
Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity |
| Enzyme 3 Pathways |
- Nicotinate and Nicotinamide Metabolism (map00760
)
- Pantothenate and CoA Biosynthesis (map00770
)
- Purine Metabolism (map00230
)
- Riboflavin Metabolism (map00740
)
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 3 Reactions |
- A dinucleotide + H2O = 2 mononucleotides
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
189650  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P22413  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
ENPP1_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>2622 bp
ATGGACGTGGGGGAGGAGCCGCTGGAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCC
AACACCTATAAAGTACTCTCGCTGGTATTGTCAGTATGTGTGTTAACAACAATACTTGGT
TGTATATTTGGGTTGAAACCAAGCTGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGT
TTCGAGAGAACATTTGGGAACTGTCGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGC
TGTTTAGATTACCAGGAGACGTGCATAGAACCAGAACATATATGGACTTGCAACAAATTC
AGGTGTGGTGAGAAAAGGTTGACCAGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGAC
AAGGGCGACTGCTGCATCAACTACAGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAA
GAACCATGTGAGAGCATTAATGAGCCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACC
CTCTTATTTTCTTTGGATGGATTCAGGGCAGAATATTTACACACTTGGGGTGGACTTCTT
CCTGTTATTAGCAAACTAAAAAAATGTGGAACATATACTAAAAACATGAGACCGGTATAT
CCAACAAAAACTTTCCCCAATCACTACAGCATTGTCACCGGATTGTATCCAGAATCTCAT
GGCATAATCGACAATAAAATGTATGATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGT
AAAGAGAAATTTAATCCTGAGTGGTACAAAGGAGAACCAATTTGGGTCACAGCTAAGTAT
CAAGGCCTCAAGTCTGGCACATTTTTCTGGCCAGGATCAGATGTGGAAATTAACGGAATT
TTCCCAGACATCTATAAAATGTATAATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCT
GTTCTTCAGTGGCTACAGCTTCCTAAAGATGAAAGACCACACTTTTACACTCTGTATTTA
GAAGAACCAGATTCTTCAGGTCATTCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCC
TTGCAGAGGGTTGATGGTATGGTTGGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTG
CACAGATGCCTGAACCTCATCCTTATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAG
AAATACATATATCTGAATAAATATTTGGGGGATGTTAAAAATATTAAAGTTATCTATGGA
CCTGCAGCTCGATTGAGACCCTCTGATGTCCCAGATAAATACTATTCATTTAACTATGAA
GGCATTGCCCGAAATCTTTCTTGCCGGGAACCAAACCAGCACTTCAAACCTTACCTGAAA
CATTTCTTACCTAAGCGTTTGCACTTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTC
TATTTGGACCCTCAGTGGCAACTTGCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGT
GGATTTCATGGCTCTGACAATGTATTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGA
CCTGGATTCAAGCATGGCATTGAGGCTGACACCTTTGAAAACATTGAAGTCTATAACTTA
ATGTGTGATTTACTGAATTTGACACCGGCTCCTAATAACGGAACTCATGGAAGTCTTAAC
CACCTTCTAAAGAATCCTGTTTATACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTA
CAGTGCCCCTTCACAAGAAACCCCAGAGATAACCTTGGCTGCTCATGTAACCCTTCGATT
TTGCCGATTGAGGATTTTCAAACACAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATT
AAGCATGAAACTTTACCCTATGGAAGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGT
CTTCTTTCCCAGCACCAGTTTATGAGTGGATACAGCCAAGACATCTTAATGCCCCTTTGG
ACATCCTATACCGTGGACAGAAATGACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTG
TACCAGGACTTTAGAATTCCTCTTAGTCCTGTCCATAAATGTTCATTTTATAAAAATAAC
ACCAAAGTGAGTTACGGGTTCCTCTCCCCACCACAACTAAATAAAAATTCAAGTGGAATA
TATTCTGAAGCTTTGCTTACTACAAATATAGTGCCAATGTACCAGAGTTTTCAAGTTATA
TGGCGCTACTTTCATGACACCCTACTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAAT
GTCGTCAGTGGTCCTGTGTTTGACTTTGATTATGATGGACGTTGTGATTCCTTAGAGAAT
CTGAGGCAAAAAAGAAGAGTCATCCGTAACCAAGAAATTTTGATTCCAACTCACTTCTTT
ATTGTGCTAACAAGCTGTAAAGATACATCTCAGACGCCTTTGCACTGTGAAAACCTAGAC
ACCTTAGCTTTCATTTTGCCTCACAGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAG
CATGACTCCTCATGGGTTGAAGAATTGTTAATGTTACACAGAGCACGGATCACAGATGTT
GAGCACATCACTGGACTCAGCTTCTATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTA
AAGTTGAAAACACATTTGCCAACCTTTAGCCAAGAAGACTGA
|
| Enzyme 3 GenBank Gene ID |
M57736  |
| Enzyme 3 GeneCard ID |
ENPP1  |
| Enzyme 3 GenAtlas ID |
ENPP1  |
| Enzyme 3 HGNC ID |
HGNC:3356  |
| Enzyme 3 Chromosome Location |
6 |
| Enzyme 3 Locus |
6q22-q23 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed
]
- Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed
]
- Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed
]
- Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed
]
- Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed
]
- Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5781 |
| Enzyme 4 Name |
Hormone-sensitive lipase |
| Enzyme 4 Synonyms |
- HSL
|
| Enzyme 4 Gene Name |
LIPE |
| Enzyme 4 Protein Sequence |
>Hormone-sensitive lipase
MEPGSKSVSRSDWQPEPHQRPITPLEPGPEKTPIAQPESKTLQGSNTQQKPASNQRPLTQ
QETPAQHDAESQKEPRAQQKSASQEEFLAPQKPAPQQSPYIQRVLLTQQEAASQQGPGLG
KESITQQEPALRQRHVAQPGPGPGEPPPAQQEAESTPAAQAKPGAKREPSAPTESTSQET
PEQSDKQTTPVQGAKSKQGSLTELGFLTKLQELSIQRSALEWKALSEWVTDSESESDVGS
SSDTDSPATMGGMVAQGVKLGFKGKSGYKVMSGYSGTSPHEKTSARNHRHYQDTASRLIH
NMDLRTMTQSLVTLAEDNIAFFSSQGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAH
LFDLDPETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRTSHNLAELEAYLAALT
QLRALVYYAQRLLVTNRPGVLFFEGDEGLTADFLREYVTLHKGCFYGRCLGFQFTPAIRP
FLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWK
AFWNITEMEVLSSLANMASATVRVSRLLSLPPEAFEMPLTADPTLTVTISPPLAHTGPGP
VLVRLISYDLREGQDSEELSSLIKSNGQRSLELWPRPQQAPRSRSLIVHFHGGGFVAQTS
RSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGSTGERIC
LAGDSAGGNLCFTVALRAAAYGVRVPDGIMAAYPATMLQPAASPSRLLSLMDPLLPLSVL
SKCVSAYAGAKTEDHSNSDQKALGMMGLVRRDTALLLRDFRLGASSWLNSFLELSGRKSQ
KMSEPIAEPMRRSVSEAALAQPQGPLGTDSLKNLTLRDLSLRGNSETSSDTPEMSLSAET
LSPSTPSDVNFLLPPEDAGEEAEAKNELSPMDRGLGVRAAFPEGFHPRRSSQGATQMPLY
SSPIVKNPFMSPLLAPDSMLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVE
DLPHGFLTLAALCRETRQAAELCVERIRLVLTPPAGAGPSGETGAAGVDGGCGGRH
|
| Enzyme 4 Number of Residues |
1076 |
| Enzyme 4 Molecular Weight |
116599 |
| Enzyme 4 Theoretical pI |
6.68 |
| Enzyme 4 GO Classification |
| Function |
- carboxylic ester hydrolase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipase activity
|
| Process |
- alcohol metabolism
- cellular metabolism
- cholesterol metabolism
- lipid catabolism
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
- sterol metabolism
|
| Component |
| — |
|
| Enzyme 4 General Function |
Lipid transport and metabolism |
| Enzyme 4 Specific Function |
In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
- (1) diacylglycerol + H2O = monoacylglycerol + a carboxylate
- (2) triacylglycerol + H2O = diacylglycerol + a carboxylate
- (3) monoacylglycerol + H2O = glycerol + a carboxylate
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
896476  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q05469  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
LIPS_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>2328 bp
ATGGACCTGCGCACAATGACACAGTCGCTGGTGACTCTGGCGGAGGACAACATAGCCTTC
TTCTCGAGCCAGGGTCCTGGGGAAACGGCCCAGCGGCTGTCAGGCGTTTTTGCCGGTGTA
CGGGAGCAGGCGCTGGGGCTGGAGCCGGCCCTGGGCCGCCTGCTGGGTGTGGCGCACCTC
TTTGACCTGGACCCAGAGACACCGGCCAACGGGTACCGCAGCCTAGTGCACACAGCCCGC
TGCTGCCTGGCGCACCTCCTGCACAAATCCCGCTATGTGGCCTCCAACCGCCGCAGCATC
TTCTTCCGCACCAGCCACAACCTGGCCGAGCTGGAGGCCTACCTGGCTGCCCTCACCCAG
CTCCGCGCTCTGGTCTACTACGCCCAGCGCCTGCTGGTTACCAATCGGCCGGGGGTACTC
TTCTTTGAGGGCGACGAGGGGCTCACCGCCGACTTCCTCCGGGAGTATGTCACGCTGCAT
AAGGGATGCTTCTATGGCCGCTGCCTGGGCTTCCAGTTCACGCCTGCCATCCGGCCATTC
CTGCAGACCATCTCCATTGGGCTGGTGTCCTTCGGGGAGCACTACAAACGCAACGAGACA
GGCCTCAGTGTGGCCGCCAGCTCTCTCTTCACCAGCGGCCGCTTTGCCATCGACCCCGAG
CTGCGTGGGGCTGAGTTTGAGCGGATCACACAGAACCTGGACGTGCACTTCTGGAAAGCC
TTCTGGAACATCACCGAGATGGAAGTGCTATCGTCTCTGGCCAACATGGCATCGGCCACC
GTGAGGGTAAGCCGCCTGCTCAGCCTGCCACCCGAAGCCTTTGAGATGCCACTGACTGCC
GACCCCACGCTCACGGTCACCATCTCACCCCCACTGGCCCACACAGGCCCTGGGCCCGTC
CTCGTCAGGCTCATCTCCTATGACCTGCGTGAAGGACAGGACAGTGAGGAGCTCAGCAGC
CTGATAAAGTCCAACGGCCAACGGAGCCTGGAGCTGTGGCCGCGCCCCCAGCAGGCACCC
CGCTCGCGGTCCCTGATAGTGCACTTCCACGGCGGTGGCTTTGTGGCCCAGACCTCCAGA
TCCCACGAGCCCTACCTCAAGAGCTGGGCCCAGGAGCTGGGCGCCCCCATCATCTCCATC
GACTACTCCCTGGCCCCTGAGGCCCCCTTCCCCCGTGCGCTGGAGGAGTGCTTCTTCGCC
TACTGCTGGGCCATCAAGCACTGCGCCCTCCTTGGCTCAACAGGGGAACGAATCTGCCTT
GCGGGGGACAGTGCAGGCGGGAACCTCTGCTTCACCGTGGCTCTTCGGGCAGCAGCCTAC
GGGGTGCGGGTGCCAGATGGCATCATGGCAGCCTACCCGGCCACAATGCTGCAGCCTGCC
GCCTCTCCCTCCCGCCTGCTGAGCCTCATGGACCCCTTGCTGCCCCTCAGTGTGCTCTCC
AAGTGTGTCAGCGCCTATGCTGGTGCAAAGACGGAGGACCACTCCAACTCAGACCAGAAA
GCCCTCGGCATGATGGGGCTGGTGCGGCGGGACACAGCCCTGCTCCTCCGAGACTTCCGC
CTGGGTGCCTCCTCATGGCTCAACTCCTTCCTGGAGTTAAGTGGGCGCAAGTCCCAGAAG
ATGTCGGAGCCCATAGCAGAGCCGATGCGCCGCAGTGTGTCTGAAGCAGCACTGGCCCAG
CCCCAGGGCCCACTGGGCACGGATTCCCTCAAGAACCTGACCCTGAGGGACTTGAGCCTG
AGGGGAAACTCCGAGACGTCGTCGGACACCCCCGAGATGTCGCTGTCAGCTGAGACACTT
AGCCCCTCCACACCCTCCGATGTCAACTTCTTATTACCACCTGAGGATGCAGGGGAAGAG
GCTGAGGCCAAAAATGAGCTGAGCCCCATGGACAGAGGCCTGGGCGTCCGTGCCGCCTTC
CCCGAGGGTTTCCACCCCCGACGCTCCAGCCAGGGTGCCACACAGATGCCCCTCTACTCC
TCACCCATAGTCAAGAACCCCTTCATGTCGCCGCTGCTGGCACCCGACAGCATGCTCAAG
AGCCTGCCACCTGTGCACATCGTGGCGTGCGCGCTGGACCCCATGCTGGACGACTCGGTC
ATGCTCGCGCGGCGACTGCGCAACCTGGGCCAGCCGGTGACGCTGCGCGTGGTGGAGGAC
CTGCCGCACGGCTTCCTGACCCTAGCGGCGCTGTGCCGCGAGACGCGCCAGGCCGCAGAG
CTGTGCGTGGAGCGCATCCGCCTCGTCCTCACTCCTCCCGCCGGAGCCGGGCCGAGCGGG
GAGACGGGGGCTGCGGGGGTAGACGGGGGCTGCGGGGGGCGACACTAA
|
| Enzyme 4 GenBank Gene ID |
L11706  |
| Enzyme 4 GeneCard ID |
LIPE  |
| Enzyme 4 GenAtlas ID |
LIPE  |
| Enzyme 4 HGNC ID |
HGNC:6621  |
| Enzyme 4 Chromosome Location |
19 |
| Enzyme 4 Locus |
19q13.2 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Langin D, Laurell H, Holst LS, Belfrage P, Holm C: Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):4897-901. [PubMed
]
- Holst LS, Langin D, Mulder H, Laurell H, Grober J, Bergh A, Mohrenweiser HW, Edgren G, Holm C: Molecular cloning, genomic organization, and expression of a testicular isoform of hormone-sensitive lipase. Genomics. 1996 Aug 1;35(3):441-7. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5833 |
| Enzyme 5 Name |
Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma |
| Enzyme 5 Synonyms |
- GMP-PDE gamma
|
| Enzyme 5 Gene Name |
PDE6H |
| Enzyme 5 Protein Sequence |
>Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
MSDNTTLPAPASNQGPTTPRKGPPKFKQRQTRQFKSKPPKKGVKGFGDDIPGMEGLGTDI
TVICPWEAFSHLELHELAQFGII
|
| Enzyme 5 Number of Residues |
83 |
| Enzyme 5 Molecular Weight |
9074 |
| Enzyme 5 Theoretical pI |
9.98 |
| Enzyme 5 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- cGMP-specific phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 5 General Function |
Not Available |
| Enzyme 5 Specific Function |
Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
1311544  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q13956  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
CNCG_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>252 bp
ATGAGTGACAACACTACTCTGCCTGCTCCAGCTTCAAACCAGGGTCCTACCACCCCACGC
AAAGGCCCTCCCAAGTTCAAGCAGAGGCAGACTCGCCAATTCAAGAGTAAACCTCCAAAG
AAAGGTGTGAAAGGATTTGGAGATGACATTCCAGGAATGGAGGGGCTAGGAACAGATATC
ACAGTGATTTGTCCATGGGAGGCATTCAGCCACCTGGAATTGCATGAGCTCGCTCAGTTT
GGGATTATCTGA
|
| Enzyme 5 GenBank Gene ID |
D45399  |
| Enzyme 5 GeneCard ID |
PDE6H  |
| Enzyme 5 GenAtlas ID |
PDE6H  |
| Enzyme 5 HGNC ID |
HGNC:8790  |
| Enzyme 5 Chromosome Location |
12 |
| Enzyme 5 Locus |
12p13 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Shimizu-Matsumoto A, Itoh K, Inazawa J, Nishida K, Matsumoto Y, Kinoshita S, Matsubara K, Okubo K: Isolation and chromosomal localization of the human cone cGMP phosphodiesterase gamma cDNA (PDE6H). Genomics. 1996 Feb 15;32(1):121-4. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5843 |
| Enzyme 6 Name |
Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A |
| Enzyme 6 Synonyms |
- Cam-PDE 1A
- 61 kDa Cam-PDE
- hCam-1
|
| Enzyme 6 Gene Name |
PDE1A |
| Enzyme 6 Protein Sequence |
>Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
MGSSATEIEELENTTFKYLTGEQTEKMWQRLKGILRCLVKQLERGDVNVVDLKKNIEYAA
SVLEAVYIDETRRLLDTEDELSDIQTDSVPSEVRDWLASTFTRKMGMTKKKPEEKPKFRS
IVHAVQAGIFVERMYRKTYHMVGLAYPAAVIVTLKDVDKWSFDVFALNEASGEHSLKFMI
YELFTRYDLINRFKIPVSCLITFAEALEVGYSKYKNPYHNLIHAADVTQTVHYIMLHTGI
MHWLTELEILAMVFAAAIHDYEHTGTTNNFHIQTRSDVAILYNDRSVLENHHVSAAYRLM
QEEEMNILINLSKDDWRDLRNLVIEMVLSTDMSGHFQQIKNIRNSLQQPEGIDRAKTMSL
ILHAADISHPAKSWKLHYRWTMALMEEFFLQGDKEAELGLPFSPLCDRKSTMVAQSQIGF
IDFIVEPTFSLLTDSTEKIVIPLIEEASKAETSSYVASSSTTIVGLHIADALRRSNTKGS
MSDGSYSPDYSLAAVDLKSFKNNLVDIIQQNKERWKELAAQEARTSSQKCEFIHQ
|
| Enzyme 6 Number of Residues |
535 |
| Enzyme 6 Molecular Weight |
61253 |
| Enzyme 6 Theoretical pI |
6.02 |
| Enzyme 6 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- cell communication
- cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 6 General Function |
Not Available |
| Enzyme 6 Specific Function |
Has a higher affinity for cGMP than for cAMP |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
1151109  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P54750  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
PDE1A_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1608 bp
ATGGGGTCTAGTGCCACAGAGATTGAAGAATTGGAAAACACCACTTTTAAGTATCTTACA
GGAGAACAGACTGAAAAAATGTGGCAGCGCCTGAAAGGAATACTAAGATGCTTGGTGAAG
CAGCTGGAAAGAGGTGATGTTAACGTCGTCGACTTAAAGAAGAATATTGAATATGCGGCA
TCTGTGCTGGAAGCAGTTTATATCGATGAAACAAGAAGACTTCTGGATACTGAAGATGAG
CTCAGTGACATTCAGACTGACTCAGTCCCATCTGAAGTCCGGGACTGGTTGGCTTCTACC
TTTACACGGAAAATGGGGATGACAAAAAAGAAACCTGAGGAAAAACCAAAATTTCGGAGC
ATTGTGCATGCTGTTCAAGCTGGAATTTTTGTGGAAAGAATGTACCGAAAAACATATCAT
ATGGTTGGTTTGGCATATCCAGCAGCTGTCATCGTAACATTAAAGGATGTTGATAAATGG
TCTTTCGATGTATTTGCCCTAAATGAAGCAAGTGGAGAGCATAGTCTGAAGTTTATGATT
TATGAACTGTTTACCAGATATGATCTTATCAACCGTTTCAAGATTCCTGTTTCTTGCCTA
ATCACCTTTGCAGAAGCTTTAGAAGTTGGTTACAGCAAGTACAAAAATCCATATCACAAT
TTGATTCATGCAGCTGATGTCACTCAAACTGTGCATTACATAATGCTTCATACAGGTATC
ATGCACTGGCTCACTGAACTGGAAATTTTAGCAATGGTCTTTGCTGCTGCCATTCATGAT
TATGAGCATACAGGGACAACAAACAACTTTCACATTCAGACAAGGTCAGATGTTGCCATT
TTGTATAATGATCGCTCTGTCCTTGAGAATCACCACGTGAGTGCAGCTTATCGACTTATG
CAAGAAGAAGAAATGAATATCTTGATAAATTTATCCAAAGATGACTGGAGGGATCTTCGG
AACCTAGTGATTGAAATGGTTTTATCTACAGACATGTCAGGTCACTTCCAGCAAATTAAA
AATATAAGAAACAGTTTGCAGCAGCCTGAAGGGATTGACAGAGCCAAAACCATGTCCCTG
ATTCTCCACGCAGCAGACATCAGCCACCCAGCCAAATCCTGGAAGCTGCATTATCGGTGG
ACCATGGCCCTAATGGAGGAGTTTTTCCTGCAGGGAGATAAAGAAGCTGAATTAGGGCTT
CCATTTTCCCCACTTTGTGATCGGAAGTCAACCATGGTGGCCCAGTCACAAATAGGTTTC
ATCGATTTCATAGTAGAGCCAACATTTTCTCTTCTGACAGACTCAACAGAGAAAATTGTT
ATTCCTCTTATAGAGGAAGCCTCAAAAGCCGAAACTTCTTCCTATGTGGCAAGCAGCTCA
ACCACCATTGTGGGGTTACACATTGCTGATGCACTAAGACGATCAAATACAAAAGGCTCC
ATGAGTGATGGGTCCTATTCCCCAGACTACTCCCTTGCAGCAGTGGACCTGAAGAGTTTC
AAGAACAACCTGGTGGACATCATTCAGCAGAACAAAGAGAGGTGGAAAGAGTTAGCTGCA
CAAGAAGCAAGAACCAGTTCACAGAAGTGTGAGTTTATTCATCAGTAA
|
| Enzyme 6 GenBank Gene ID |
U40370  |
| Enzyme 6 GeneCard ID |
PDE1A  |
| Enzyme 6 GenAtlas ID |
PDE1A  |
| Enzyme 6 HGNC ID |
HGNC:8774  |
| Enzyme 6 Chromosome Location |
2 |
| Enzyme 6 Locus |
2q32.1 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Loughney K, Martins TJ, Harris EA, Sadhu K, Hicks JB, Sonnenburg WK, Beavo JA, Ferguson K: Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3',5'-cyclic nucleotide phosphodiesterases. J Biol Chem. 1996 Jan 12;271(2):796-806. [PubMed
]
- Michibata H, Yanaka N, Kanoh Y, Okumura K, Omori K: Human Ca2+/calmodulin-dependent phosphodiesterase PDE1A: novel splice variants, their specific expression, genomic organization, and chromosomal localization. Biochim Biophys Acta. 2001 Jan 26;1517(2):278-87. [PubMed
]
- Fidock M, Miller M, Lanfear J: Isolation and differential tissue distribution of two human cDNAs encoding PDE1 splice variants. Cell Signal. 2002 Jan;14(1):53-60. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5847 |
| Enzyme 7 Name |
High-affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A |
| Enzyme 7 Synonyms |
Not Available |
| Enzyme 7 Gene Name |
PDE8A |
| Enzyme 7 Protein Sequence |
>High-affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A
MGCAPSIHISERLVAEDAPSPAAPPLSSGGPRLPQGQKTAALPRTRGAGLLESELRDGSG
KKVAVADVQFGPMRFHQDQLQVLLVFTKEDNQCNGFCRACEKAGFKCTVTKEAQAVLACF
LDKHHDIIIIDHRNPRQLDAEALCRSIRSSKLSENTVIVGVVRRVDREELSVMPFISAGF
TRRYVENPNIMACYNELLQLEFGEVRSQLKLRACNSVFTALENSEDAIEITSEDRFIQYA
NPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNI
QQNVKIIPVIGQGGKIRHYVSIIRVCNGNNKAEKISECVQSDTHTDNQTGKHKDRRKGSL
DVKAVASRATEVSSQRRHSSMARIHSMTIEAPITKVINIINAAQESSPMPVTEALDRVLE
ILRTTELYSPQFGAKDDDPHANDLVGGLMSDGLRRLSGNEYVLSTKNTQMVSSNIITPIS
LDDVPPRIARAMENEEYWDFDIFELEAATHNRPLIYLGLKMFARFGICEFLHCSESTLRS
WLQIIEANYHSSNPYHNSTHSADVLHATAYFLSKERIKETLDPIDEVAALIAATIHDVDH
PGRTNSFLCNAGSELAILYNDTAVLESHHAALAFQLTTGDDKCNIFKNMERNDYRTLRQG
IIDMVLATEMTKHFEHVNKFVNSINKPLATLEENGETDKNQEVINTMLRTPENRTLIKRM
LIKCADVSNPCRPLQYCIEWAARISEEYFSQTDEEKQQGLPVVMPVFDRNTCSIPKSQIS
FIDYFITDMFDAWDAFVDLPDLMQHLDNNFKYWKGLDEMKLRNLRPPPE
|
| Enzyme 7 Number of Residues |
829 |
| Enzyme 7 Molecular Weight |
93305 |
| Enzyme 7 Theoretical pI |
6.03 |
| Enzyme 7 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- DNA binding
- binding
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- kinase activity
- nucleic acid binding
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
- protein histidine kinase activity
- protein kinase activity
- signal transducer activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- two-component response regulator activity
- two-component sensor molecule activity
|
| Process |
- cell communication
- cellular process
- regulation of biological process
- regulation of cellular metabolism
- regulation of metabolism
- regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- regulation of physiological process
- regulation of transcription
- regulation of transcription, DNA-dependent
- signal transduction
- two-component signal transduction system (phosphorelay)
- two-component signal transduction system (phosphorelay)
|
| Component |
| — |
|
| Enzyme 7 General Function |
Signal transduction mechanisms |
| Enzyme 7 Specific Function |
Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase, which has a high affinity for cAMP, may be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
16417190  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
O60658  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
PDE8A_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>2490 bp
ATGGGCTGTGCCCCGAGCATCCACATTTCCGAGCGCCTGGTGGCCGAGGACGCGCCTAGC
CCCGCGGCACCGCCGCTGTCGTCCGGCGGGCCGCGCCTCCCGCAGGGCCAGAAGACGGCC
GCCTTGCCCCGGACCCGCGGCGCCGGCCTCTTGGAGTCGGAGCTTCGCGACGGCAGCGGC
AAGAAGGTAGCAGTAGCTGATGTGCAGTTTGGCCCCATGAGATTTCATCAAGATCAACTT
CAGGTACTTTTAGTGTTTACCAAAGAAGATAACCAATGTAATGGATTCTGCAGGGCATGT
GAAAAAGCAGGGTTTAAGTGTACAGTTACCAAGGAGGCTCAGGCTGTCCTTGCCTGTTTC
CTGGACAAACATCATGACATTATCATCATAGACCACAGAAATCCTCGACAGCTGGATGCA
GAGGCACTGTGCAGGTCTATCAGATCATCAAAACTCTCAGAAAACACAGTTATTGTTGGT
GTAGTACGCAGGGTGGATAGAGAAGAGTTGTCCGTAATGCCTTTCATTTCTGCTGGATTT
ACAAGGAGGTATGTAGAAAACCCCAACATCATGGCCTGCTACAATGAACTGCTCCAGCTG
GAGTTTGGAGAGGTGCGATCACAACTGAAACTCAGGGCTTGTAACTCAGTATTCACTGCA
TTAGAAAACAGTGAAGATGCAATTGAAATTACAAGCGAAGACCGTTTTATACAGTATGCA
AATCCTGCATTTGAAACAACAATGGGCTATCAGTCAGGTGAATTAATAGGGAAGGAGTTA
GGAGAAGTGCCTATAAATGAAAAAAAGGCTGACTTGCTCGATACTATAAATTCATGCATC
AGGATAGGCAAGGAGTGGCAAGGAATTTACTATGCAAAAAAGAAAAACGGAGATAATATA
CAACAAAATGTGAAGATAATACCTGTCATTGGACAGGGAGGAAAAATTAGACACTATGTG
TCCATTATCAGAGTGTGCAATGGCAACAATAAGGCTGAGAAAATATCCGAATGTGTTCAG
TCTGACACTCATACAGATAATCAGACAGGCAAACATAAAGACAGGAGAAAAGGCTCACTA
GACGTCAAAGCTGTTGCCTCCCGTGCAACTGAAGTTTCCAGCCAGAGACGACACTCTTCC
ATGGCCCGGATACATTCCATGACAATTGAGGCGCCCATCACCAAGGTAATCAATATTATC
AATGCTGCCCAGGAAAGTAGTCCCATGCCTGTGACAGAAGCCCTAGACCGTGTGCTGGAA
ATTCTAAGAACCACTGAGTTATATTCACCACAGTTTGGTGCTAAAGATGATGATCCCCAT
GCCAATGACCTTGTTGGGGGCTTAATGTCTGATGGTTTGCGAAGACTATCAGGGAATGAA
TATGTTCTTTCAACAAAAAACACTCAAATGGTTTCAAGCAATATAATCACTCCCATCTCC
CTTGATGATGTCCCACCACGGATAGCTCGGGCCATGGAAAATGAGGAATACTGGGACTTT
GATATTTTTGAACTGGAGGCTGCCACCCACAATAGGCCTTTGATTTATCTTGGTCTCAAA
ATGTTTGCTCGCTTTGGAATCTGTGAATTCTTACACTGCTCCGAGTCAACGCTAAGATCA
TGGTTACAAATTATCGAAGCCAATTATCATTCCTCCAATCCCTACCACAATTCTACACAT
TCTGCTGATGTGCTTCATGCCACTGCCTATTTTCTCTCCAAGGAGAGGATAAAGGAAACT
TTAGATCCAATTGATGAGGTCGCTGCACTCATCGCAGCCACCATTCATGATGTGGATCAC
CCTGGGAGAACCAACTCCTTCCTGTGTAATGCTGGAAGTGAGCTGGCCATTTTGTACAAT
GACACTGCTGTGCTGGAGAGCCACCATGCGGCCTTGGCCTTCCAGCTGACCACTGGAGAT
GATAAATGCAATATATTTAAAAACATGGAGAGGAATGATTATCGGACACTGCGCCAGGGG
ATTATCGACATGGTCTTAGCCACAGAAATGACAAAGCACTTTGAGCATGTCAACAAATTT
GTCAACAGCATCAACAAACCCTTGGCAACACTAGAAGAAAATGGGGAAACTGATAAAAAC
CAGGAAGTGATAAACACTATGCTTAGGACTCCAGAGAACCGGACCCTAATCAAACGAATG
CTGATTAAATGTGCTGATGTGTCCAATCCCTGCCGACCCCTGCAGTACTGCATCGAGTGG
GCTGCACGCATTTCGGAAGAATATTTTTCTCAGACTGATGAAGAGAAGCAGCAGGGCTTA
CCTGTGGTGATGCCAGTGTTTGACAGAAATACCTGCAGCATCCCCAAATCCCAAATCTCT
TTCATTGATTACTTCATCACAGACATGTTTGATGCTTGGGATGCCTTTGTAGACCTGCCT
GATTTAATGCAGCATCTTGACAACAACTTTAAATACTGGAAAGGACTGGACGAAATGAAG
CTGCGGAACCTCCGACCACCTCCTGAATAG
|
| Enzyme 7 GenBank Gene ID |
AF388183  |
| Enzyme 7 GeneCard ID |
PDE8A  |
| Enzyme 7 GenAtlas ID |
PDE8A  |
| Enzyme 7 HGNC ID |
HGNC:8793  |
| Enzyme 7 Chromosome Location |
15 |
| Enzyme 7 Locus |
15q25.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Wang P, Wu P, Egan RW, Billah MM: Human phosphodiesterase 8A splice variants: cloning, gene organization, and tissue distribution. Gene. 2001 Dec 12;280(1-2):183-94. [PubMed
]
- Fisher DA, Smith JF, Pillar JS, St Denis SH, Cheng JB: Isolation and characterization of PDE8A, a novel human cAMP-specific phosphodiesterase. Biochem Biophys Res Commun. 1998 May 29;246(3):570-7. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5848 |
| Enzyme 8 Name |
Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B |
| Enzyme 8 Synonyms |
- Cam-PDE 1B
- 63 kDa Cam-PDE
|
| Enzyme 8 Gene Name |
PDE1B |
| Enzyme 8 Protein Sequence |
>Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
MELSPRSPPEMLEESDCPSPLELKSAPSKKMWIKLRSLLRYMVKQLENGEINIEELKKNL
EYTASLLEAVYIDETRQILDTEDELQELRSDAVPSEVRDWLASTFTQQARAKGRRAEEKP
KFRSIVHAVQAGIFVERMFRRTYTSVGPTYSTAVLNCLKNLDLWCFDVFSLNQAADDHAL
RTIVFELLTRHNLISRFKIPTVFLMSFLDALETGYGKYKNPYHNQIHAADVTQTVHCFLL
RTGMVHCLSEIELLAIIFAAAIHDYEHTGTTNSFHIQTKSECAIVYNDRSVLENHHISSV
FRLMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKTMKTALQQLERIDKPK
ALSLLLHAADISHPTKQWLVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQS
QIGFIDFIVEPTFSVLTDVAEKSVQPLADEDSKSKNQPSFQWRQPSLDVEVGDPNPDVVS
FRSTWVKRIQENKQKWKERAASGITNQMSIDELSPCEEEAPPSPAEDEHNQNGNLD
|
| Enzyme 8 Number of Residues |
536 |
| Enzyme 8 Molecular Weight |
61380 |
| Enzyme 8 Theoretical pI |
5.22 |
| Enzyme 8 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- cell communication
- cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 8 General Function |
Not Available |
| Enzyme 8 Specific Function |
Has a preference for cGMP as a substrate |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
1621592  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q01064  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
PDE1B_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1611 bp
ATGGAGCTGTCCCCCCGCAGTCCTCCGGAGATGCTGGAGGAGTCGGATTGCCCGTCACCC
CTGGAGCTGAAGTCAGCCCCCAGCAAGAAGATGTGGATTAAGCTTCGGTCTCTGCTGCGC
TACATGGTGAAGCAGTTGGAGAATGGGGAGATAAACATTGAGGAGCTGAAGAAAAATCTG
GAGTACACAGCTTCTCTGCTGGAAGCCGTCTACATAGATGAGACACGGCAAATCTTGGAC
ACGGAGGACGAGCTGCAGGAGCTGCGGTCAGATGCCGTGCCTTCGGAGGTGCGGGACTGG
CTGGCCTCCACCTTCACCCAGCAGGCCCGGGCCAAAGGCCGCCGAGCAGAGGAGAAGCCC
AAGTTCCGAAGCATTGTGCACGCTGTGCAGGCTGGGATCTTCGTGGAACGGATGTTCCGG
AGAACATACACCTCTGTGGGCCCCACTTACTCTACTGCGGTTCTCAACTGTCTCAAGAAC
CTGGATCTCTGGTGCTTTGATGTCTTTTCCTTGAACCAGGCAGCAGATGACCATGCCCTG
AGGACCATTGTTTTTGAGTTGCTGACTCGGCATAACCTCATCAGCCGCTTCAAGATTCCC
ACTGTGTTTTTGATGAGTTTCCTGGATGCCTTGGAGACAGGCTATGGGAAGTACAAGAAT
CCTTACCACAACCAGATCCACGCAGCCGATGTTACCCAGACAGTCCATTGCTTCTTGCTC
CGCACAGGGATGGTGCACTGCCTGTCGGAGATTGAGCTCCTGGCCATCATCTTTGCTGCA
GCTATCCATGATTATGAGCACACGGGCACTACCAACAGCTTCCACATCCAGACCAAGTCA
GAATGTGCCATCGTGTACAATGATCGTTCAGTGCTGGAGAATCACCACATCAGCTCTGTT
TTCCGATTGATGCAGGATGATGAGATGAACATTTTCATCAACCTCACCAAGGATGAGTTT
GTAGAACTCCGAGCCCTGGTCATTGAGATGGTGTTGGCCACAGACATGTCCTGCCATTTC
CAGCAAGTGAAGACCATGAAGACAGCCTTGCAACAGCTGGAGAGGATTGACAAGCCCAAG
GCCCTGTCTCTACTGCTCCATGCTGCTGACATCAGCCACCCAACCAAGCAGTGGTTGGTC
CACAGCCGTTGGACCAAGGCCCTCATGGAGGAATTCTTCCGTCAGGGTGACAAGGAGGCA
GAGTTGGGCCTGCCCTTTTCTCCACTCTGTGACCGCACTTCCACTCTAGTGGCACAGTCT
CAGATAGGGTTCATCGACTTCATTGTGGAGCCCACATTCTCTGTGCTGACTGACGTGGCA
GAGAAGAGTGTTCAGCCCCTGGCGGATGAGGACTCCAAGTCTAAAAACCAGCCCAGCTTT
CAGTGGCGCCAGCCCTCTCTGGATGTGGAAGTGGGAGACCCCAACCCTGATGTGGTCAGC
TTTCGTTCCACCTGGGTCAAGCGCATTCAGGAGAACAAGCAGAAATGGAAGGAACGGGCA
GCAAGTGGCATCACCAACCAGATGTCCATTGACGAGCTGTCCCCCTGTGAAGAAGAGGCC
CCCCCATCCCCTGCCGAAGATGAACACAACCAGAATGGGAATCTGGATTAG
|
| Enzyme 8 GenBank Gene ID |
U56976  |
| Enzyme 8 GeneCard ID |
PDE1B  |
| Enzyme 8 GenAtlas ID |
PDE1B  |
| Enzyme 8 HGNC ID |
HGNC:8775  |
| Enzyme 8 Chromosome Location |
12 |
| Enzyme 8 Locus |
12q13 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Jiang X, Li J, Paskind M, Epstein PM: Inhibition of calmodulin-dependent phosphodiesterase induces apoptosis in human leukemic cells. Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):11236-41. [PubMed
]
- Yu J, Wolda SL, Frazier AL, Florio VA, Martins TJ, Snyder PB, Harris EA, McCaw KN, Farrell CA, Steiner B, Bentley JK, Beavo JA, Ferguson K, Gelinas R: Identification and characterisation of a human calmodulin-stimulated phosphodiesterase PDE1B1. Cell Signal. 1997 Nov;9(7):519-29. [PubMed
]
- Repaske DR, Swinnen JV, Jin SL, Van Wyk JJ, Conti M: A polymerase chain reaction strategy to identify and clone cyclic nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA encoding the 63-kDa calmodulin-dependent phosphodiesterase. J Biol Chem. 1992 Sep 15;267(26):18683-8. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5850 |
| Enzyme 9 Name |
cGMP-inhibited 3',5'-cyclic phosphodiesterase B |
| Enzyme 9 Synonyms |
- Cyclic GMP-inhibited phosphodiesterase B
- CGI-PDE B
- CGIPDE1
- CGIP1
|
| Enzyme 9 Gene Name |
PDE3B |
| Enzyme 9 Protein Sequence |
>cGMP-inhibited 3',5'-cyclic phosphodiesterase B
MRRDERDAKAMRSLQPPDGAGSPPESLRNGYVKSCVSPLRQDPPRGFFFHLCRFCNVELR
PPPASPQQPRRCSPFCRARLSLGALAAFVLALLLGAEPESWAAGAAWLRTLLSVCSHSLS
PLFSIACAFFFLTCFLTRTKRGPGPGRSCGSWWLLALPACCYLGDFLVWQWWSWPWGDGD
AGSAAPHTPPEAAAGRLLLVLSCVGLLLTLAHPLRLRHCVLVLLLASFVWWVSFTSLGSL
PSALRPLLSGLVGGAGCLLALGLDHFFQIREAPLHPRLSSAAEEKVPVIRPRRRSSCVSL
GETAASYYGSCKIFRRPSLPCISREQMILWDWDLKQWYKPHYQNSGGGNGVDLSVLNEAR
NMVSDLLTDPSLPPQVISSLRSISSLMGAFSGSCRPKINPLTPFPGFYPCSEIEDPAEKG
DRKLNKGLNRNSLPTPQLRRSSGTSGLLPVEQSSRWDRNNGKRPHQEFGISSQGCYLNGP
FNSNLLTIPKQRSSSVSLTHHVGLRRAGVLSSLSPVNSSNHGPVSTGSLTNRSPIEFPDT
ADFLNKPSVILQRSLGNAPNTPDFYQQLRNSDSNLCNSCGHQMLKYVSTSESDGTDCCSG
KSGEEENIFSKESFKLMETQQEEETEKKDSRKLFQEGDKWLTEEAQSEQQTNIEQEVSLD
LILVEEYDSLIEKMSNWNFPIFELVEKMGEKSGRILSQVMYTLFQDTGLLEIFKIPTQQF
MNYFRALENGYRDIPYHNRIHATDVLHAVWYLTTRPVPGLQQIHNGCGTGNETDSDGRIN
HGRIAYISSKSCSNPDESYGCLSSNIPALELMALYVAAAMHDYDHPGRTNAFLVATNAPQ
AVLYNDRSVLENHHAASAWNLYLSRPEYNFLLHLDHVEFKRFRFLVIEAILATDLKKHFD
FLAEFNAKANDVNSNGIEWSNENDRLLVCQVCIKLADINGPAKVRDLHLKWTEGIVNEFY
EQGDEEANLGLPISPFMDRSSPQLAKLQESFITHIVGPLCNSYDAAGLLPGQWLEAEEDN
DTESGDDEDGEELDTEDEEMENNLNPKPPRRKSRRRIFCQLMHHLTENHKIWKEIVEEEE
KCKADGNKLQVENSSLPQADEIQVIEEADEEE
|
| Enzyme 9 Number of Residues |
1112 |
| Enzyme 9 Molecular Weight |
124335 |
| Enzyme 9 Theoretical pI |
5.75 |
| Enzyme 9 GO Classification |
Not Available |
| Enzyme 9 General Function |
Not Available |
| Enzyme 9 Specific Function |
May play a role in fat metabolism |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 9 Pfam Domain Function |
Not Available |
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
- 88-108
117-137
152-172
192-212
220-240
247-267
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
1145302  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q13370  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
PDE3B_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>3339 bp
ATGAGGAGGGACGAGCGAGACGCCAAAGCCATGCGGTCCCTGCAGCCGCCGGATGGGGCC
GGCTCGCCCCCCGAGAGTCTGAGGAACGGCTACGTGAAGAGCTGCGTGAGCCCCTTGCGG
CAGGACCCTCCGCGCGGCTTCTTCTTCCACCTCTGCCGCTTCTGCAACGTGGAGCTGCGG
CCGCCGCCGGCCTCTCCCCAGCAGCCGCGGCGCTGCTCCCCCTTCTGCCGGGCGCGCCTC
TCGCTGGGCGACCTGGCTGCCTTTGTCCTCGCCCTGCTGCTGGGAGCGGAACCCGAGAGC
TGGGCTGCCGGGGCCGCCTGGCTGCGGACGCTGCTGAGCGTGTGTTCGCACAGCTTGAGC
CCCCTCTTCAGCATCGCCTGTGCCTTCTTCTTCCTCACCTGCTTCCTCACCCGGACCAAG
CGGGGACCCGGCCCGGGCCGGAGCTGCGGCTCCTGGTGGCTGCTGGCGCTGCCCGCCTGC
TGTTACCTGGGGGACTTCTTGGTGTGGCAGTGGTGGTCTTGGCCTTGGGGGGATGGCGAC
GCAGGGTCCGCGGCCCCGCACACGCCCCCGGAGGCGGCAGCGGGCAGGTTGCTGCTGGTG
CTGAGCTGCGTAGGGCTGCTGCTGACGCTCGCGCACCCGCTGCGGCTCCGGCACTGCGTT
CTGGTGCTGCTCCTGGCCAGCTTCGTCTGGTGGGTCTCCTTCACCAGCCTCGGGTCGCTG
CCCTCCGCCCTCAGGCCGCTGCTCTCCGGCCTGGTGGGGGGCGCTGGCTGCCTGCTGGCC
CTGGGGTTGGATCACTTCTTTCAAATCAGGGAAGCGCCTCTTCATCCTCGACTGTCCAGT
GCCGCCGAAGAAAAAGTGCCTGTGATCCGACCCCGGAGGAGGTCCAGCTGCGTGTCGTTA
GGAGAAACTGCAGCCAGTTACTATGGCAGTTGCAAAATATTCAGGAGACCGTCGTTGCCT
TGTATTTCCAGAGAACAGATGATTCTTTGGGATTGGGACTTAAAACAATGGTATAAGCCT
CATTATCAAAATTCTGGAGGTGGAAATGGAGTTGATCTTTCAGTGCTAAATGAGGCTCGC
AATATGGTGTCAGATCTTCTGACTGATCCAAGCCTTCCACCACAAGTCATTTCCTCTCTA
CGGAGTATTAGTAGCTTAATGGGTGCTTTCTCAGGTTCCTGTAGGCCAAAGATTAATCCT
CTCACACCATTTCCTGGATTTTACCCCTGTTCTGAAATAGAGGACCCAGCTGAGAAAGGG
GATAGAAAACTTAACAAGGGACTAAATAGGAATAGTTTGCCAACTCCACAGCTGAGGAGA
AGCTCAGGAACTTCAGGATTGCTACCTGTTGAACAGTCTTCAAGGTGGGATCGTAATAAT
GGCAAAAGGCCTCACCAAGAATTTGGCATTTCAAGTCAAGGATGCTATCTAAATGGGCCT
TTTAATTCAAATCTACTGACTATCCCGAAGCAAAGGTCATCTTCTGTATCACTGACTCAC
CATGTAGGTCTCAGAAGAGCTGGTGTTTTGTCCAGTCTGAGTCCTGTGAATTCTTCCAAC
CATGGACCAGTGTCTACTGGCTCTCTAACTAATCGATCACCCATAGAATTTCCTGATACT
GCTGATTTTCTTAATAAGCCAAGCGTTATCTTGCAGAGATCTCTGGGCAATGCACCTAAT
ACTCCAGATTTTTATCAGCAACTTAGAAATTCTGATAGCAATCTGTGTAACAGCTGTGGA
CATCAAATGCTGAAATATGTTTCAACATCTGAATCAGATGGTACAGATTGCTGCAGTGGA
AAATCAGGTGAAGAAGAAAACATTTTCTCGAAAGAATCATTCAAACTTATGGAAACTCAA
CAAGAAGAGGAAACAGAGAAGAAAGACAGCAGAAAATTATTTCAGGAAGGTGATAAGTGG
CTAACAGAAGAGGCACAGAGTGAACAGCAAACAAATATTGAACAGGAAGTATCACTGGAC
CTGATTTTAGTAGAAGAGTATGACTCATTAATAGAAAAGATGAGCAACTGGAATTTTCCA
ATTTTTGAACTTGTAGAAAAGATGGGAGAGAAATCAGGAAGGATTCTCAGTCAGGTTATG
TATACCTTATTTCAAGACACTGGTTTATTGGAAATATTTAAAATTCCCACTCAACAATTT
ATGAACTATTTTCGTGCATTAGAAAATGGCTATCGAGACATTCCTTATCACAATCGTATA
CATGCCACAGATGTGCTACATGCAGTTTGGTATCTGACAACACGGCCAGTTCCTGGCTTA
CAGCAGATCCACAATGGTTGTGGAACAGGAAATGAAACAGATTCTGATGGTAGAATTAAC
CATGGGCGAATTGCTTATATTTCTTCGAAGAGCTGCTCTAATCCTGATGAGAGTTATGGC
TGCCTGTCTTCAAACATTCCTGCATTAGAATTGATGGCTCTATACGTGGCAGCTGCCATG
CATGATTATGATCACCCAGGGAGGACAAATGCATTTCTAGTGGCTACAAATGCCCCTCAG
GCAGTTTTATACAATGACAGATCTGTTCTGGAAAATCATCATGCTGCGTCAGCTTGGAAT
CTATATCTTTCTCGCCCAGAATACAACTTCCTTCTTCATCTTGATCATGTGGAATTCAAG
CGCTTTCGTTTTTTAGTCATTGAAGCAATCCTTGCTACGGATCTTAAAAAGCATTTTGAT
TTTCTCGCAGAATTCAATGCCAAGGCAAATGATGTAAATAGTAATGGCATAGAATGGAGT
AATGAAAATGATCGCCTCTTGGTATGCCAGGTGTGCATCAAACTGGCAGATATAAATGGC
CCAGCAAAAGTTCGAGACTTGCATTTGAAATGGACAGAAGGCATTGTCAATGAATTTTAT
GAGCAGGGAGATGAAGAAGCAAATCTTGGTCTGCCCATCAGTCCATTCATGGATCGTTCT
TCTCCTCAACTAGCAAAACTCCAAGAATCTTTTATCACCCACATAGTGGGTCCCCTGTGT
AACTCCTATGATGCTGCTGGTTTGCTACCAGGTCAGTGGTTAGAAGCAGAAGAGGATAAT
GATACTGAAAGTGGTGATGATGAAGACGGTGAAGAATTAGATACAGAAGATGAAGAAATG
GAAAACAATCTAAATCCAAAACCACCAAGAAGGAAAAGCAGACGGCGAATATTTTGTCAG
CTAATGCACCACCTCACTGAAAACCACAAGATATGGAAGGAAATCGTAGAGGAAGAAGAA
AAATGTAAAGCTGATGGGAATAAACTGCAGGTGGAGAATTCCTCCTTACCTCAAGCAGAT
GAGATTCAGGTAATTGAAGAGGCAGATGAAGAGGAATAG
|
| Enzyme 9 GenBank Gene ID |
U38178  |
| Enzyme 9 GeneCard ID |
PDE3B  |
| Enzyme 9 GenAtlas ID |
PDE3B  |
| Enzyme 9 HGNC ID |
HGNC:8779  |
| Enzyme 9 Chromosome Location |
11 |
| Enzyme 9 Locus |
11p15.1 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Miki T, Taira M, Hockman S, Shimada F, Lieman J, Napolitano M, Ward D, Taira M, Makino H, Manganiello VC: Characterization of the cDNA and gene encoding human PDE3B, the cGIP1 isoform of the human cyclic GMP-inhibited cyclic nucleotide phosphodiesterase family. Genomics. 1996 Sep 15;36(3):476-85. [PubMed
]
- Lobbert RW, Winterpacht A, Seipel B, Zabel BU: Molecular cloning and chromosomal assignment of the human homologue of the rat cGMP-inhibited phosphodiesterase 1 (PDE3A)--a gene involved in fat metabolism located at 11p 15.1. Genomics. 1996 Oct 15;37(2):211-8. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5862 |
| Enzyme 10 Name |
High-affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A |
| Enzyme 10 Synonyms |
- HCP1
- TM22
|
| Enzyme 10 Gene Name |
PDE7A |
| Enzyme 10 Protein Sequence |
>High-affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A
MEVCYQLPVLPLDRPVPQHVLSRRGAISFSSSSALFGCPNPRQLSQRRGAISYDSSDQTA
LYIRMLGDVRVRSRAGFESERRGSHPYIDFRIFHSQSEIEVSVSARNIRRLLSFQRYLRS
SRFFRGTAVSNSLNILDDDYNGQAKCMLEKVGNWNFDIFLFDRLTNGNSLVSLTFHLFSL
HGLIEYFHLDMMKLRRFLVMIQEDYHSQNPYHNAVHAADVTQAMHCYLKEPKLANSVTPW
DILLSLIAAATHDLDHPGVNQPFLIKTNHYLATLYKNTSVLENHHWRSAVGLLRESGLFS
HLPLESRQQMETQIGALILATDISRQNEYLSLFRSHLDRGDLCLEDTRHRHLVLQMALKC
ADICNPCRTWELSKQWSEKVTEEFFHQGDIEKKYHLGVSPLCDRHTESIANIQIGFMTYL
VEPLFTEWARFSNTRLSQTMLGHVGLNKASWKGLQREQSSSEDTDAAFELNSQLLPQENR
LS
|
| Enzyme 10 Number of Residues |
482 |
| Enzyme 10 Molecular Weight |
55506 |
| Enzyme 10 Theoretical pI |
7.53 |
| Enzyme 10 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- cell communication
- cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 10 General Function |
Not Available |
| Enzyme 10 Specific Function |
Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase is highly specific for cAMP and may have a role in muscle signal transduction |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
5566609  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q13946  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
PDE7A_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1449 bp
ATGGAAGTGTGTTACCAGCTGCCGGTACTGCCCCTGGACAGGCCGGTCCCCCAGCACGTC
CTCAGCCGCCGAGGAGCCATCAGCTTCAGCTCCAGCTCCGCTCTCTTCGGCTGCCCCAAT
CCCCGGCAGCTCTCTCAGAGGCGTGGAGCTATTTCCTATGACAGTTCTGATCAGACTGCA
TTATACATTCGTATGCTAGGAGATGTACGTGTAAGGAGCCGAGCAGGATTTGAATCAGAA
AGAAGAGGTTCTCACCCATATATTGATTTTCGTATTTTCCACTCTCAATCTGAAATTGAA
GTGTCTGTCTCTGCAAGGAATATCAGAAGGCTACTAAGTTTCCAGCGATATCTTAGATCT
TCACGCTTTTTTCGTGGTACTGCGGTTTCAAATTCCCTAAACATTTTAGATGATGATTAT
AATGGACAAGCCAAGTGTATGCTGGAAAAAGTTGGAAATTGGAATTTTGATATCTTTCTA
TTTGATAGACTAACAAATGGAAATAGTCTAGTAAGCTTAACCTTTCATTTATTTAGTCTT
CATGGATTAATTGAGTACTTCCATTTAGATATGATGAAACTTCGTAGATTTTTAGTTATG
ATTCAAGAAGATTACCACAGTCAAAATCCTTACCATAACGCAGTCCACGCTGCGGATGTT
ACTCAGGCCATGCACTGTTACTTAAAGGAACCTAAGCTTGCCAATTCTGTAACTCCTTGG
GATATCTTGCTGAGCTTAATTGCAGCTGCCACTCATGATCTGGATCATCCAGGTGTTAAT
CAACCTTTCCTTATTAAAACTAACCATTACTTGGCAACTTTATACAAGAATACCTCAGTA
CTGGAAAATCACCACTGGAGATCTGCAGTGGGCTTATTGAGAGAATCAGGCTTATTCTCA
CATCTGCCATTAGAAAGCAGGCAACAAATGGAGACACAGATAGGTGCTCTGATACTAGCC
ACAGACATCAGTCGCCAGAATGAGTATCTGTCTTTGTTTAGGTCCCATTTGGATAGAGGT
GATTTATGCCTAGAAGACACCAGACACAGACATTTGGTTTTACAGATGGCTTTGAAATGT
GCTGATATTTGTAACCCATGTCGGACGTGGGAATTAAGCAAGCAGTGGAGTGAAAAAGTA
ACGGAGGAATTCTTCCATCAAGGAGATATAGAAAAAAAATATCATTTGGGTGTGAGTCCA
CTTTGCGATCGTCACACTGAATCTATTGCCAACATCCAGATTGGTTTTATGACTTACCTA
GTGGAGCCTTTATTTACAGAATGGGCCAGGTTTTCCAATACAAGGCTATCCCAGACAATG
CTTGGACACGTGGGGCTGAATAAAGCCAGCTGGAAGGGACTGCAGAGAGAACAGTCGAGC
AGTGAGGACACTGATGCTGCATTTGAGTTGAACTCACAGTTATTACCTCAGGAAAATCGG
TTATCATAA
|
| Enzyme 10 GenBank Gene ID |
L12052  |
| Enzyme 10 GeneCard ID |
PDE7A  |
| Enzyme 10 GenAtlas ID |
PDE7A  |
| Enzyme 10 HGNC ID |
HGNC:8791  |
| Enzyme 10 Chromosome Location |
Not Available |
| Enzyme 10 Locus |
Not Available |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Michaeli T, Bloom TJ, Martins T, Loughney K, Ferguson K, Riggs M, Rodgers L, Beavo JA, Wigler M: Isolation and characterization of a previously undetected human cAMP phosphodiesterase by complementation of cAMP phosphodiesterase-deficient Saccharomyces cerevisiae. J Biol Chem. 1993 Jun 15;268(17):12925-32. [PubMed
]
- Han P, Zhu X, Michaeli T: Alternative splicing of the high affinity cAMP-specific phosphodiesterase (PDE7A) mRNA in human skeletal muscle and heart. J Biol Chem. 1997 Jun 27;272(26):16152-7. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5872 |
| Enzyme 11 Name |
cGMP-inhibited 3',5'-cyclic phosphodiesterase A |
| Enzyme 11 Synonyms |
- Cyclic GMP-inhibited phosphodiesterase A
- CGI-PDE A
|
| Enzyme 11 Gene Name |
PDE3A |
| Enzyme 11 Protein Sequence |
>cGMP-inhibited 3',5'-cyclic phosphodiesterase A
MAVPGDAARVRDKPVHSGVSQAPTAGRDCHHRADPASPRDSGCRGCWGDLVLQPLRSSRK
LSSALCAGSLSFLLALLVRLVRGEVGCDLEQCKEAAAAEEEEAAPGAEGGVFPGPRGGAP
GGGARLSPWLQPSALLFSLLCAFFWMGLYLLRAGVRLPLAVALLAACCGGEALVQIGLGV
GEDHLLSLPAAGVVLSCLAAATWLVLRLRLGVLMIALTSAVRTVSLISLERFKVAWRPYL
AYLAGVLGILLARYVEQILPQSAEAAPREHLGSQLIAGTKEDIPVFKRRRRSSSVVSAEM
SGCSSKSHRRTSLPCIPREQLMGHSEWDHKRGPRGSQSSGTSITVDIAVMGEAHGLITDL
LADPSLPPNVCTSLRAVSNLLSTQLTFQAIHKPRVNPVTSLSENYTCSDSEESSEKDKLA
IPKRLRRSLPPGLLRRVSSTWTTTTSATGLPTLEPAPVRRDRSTSIKLQEAPSSSPDSWN
NPVMMTLTKSRSFTSSYAISAANHVKAKKQSRPGALAKISPLSSPCSSPLQGTPASSLVS
KISAVQFPESADTTAKQSLGSHRALTYTQSAPDLSPQILTPPVICSSCGRPYSQGNPADE
PLERSGVATRTPSRTDDTAQVTSDYETNNNSDSSDIVQNEDETECLREPLRKASACSTYA
PETMMFLDKPILAPEPLVMDNLDSIMEQLNTWNFPIFDLVENIGRKCGRILSQVSYRLFE
DMGLFEAFKIPIREFMNYFHALEIGYRDIPYHNRIHATDVLHAVWYLTTQPIPGLSTVIN
DHGSTSDSDSDSGFTHGHMGYVFSKTYNVTDDKYGCLSGNIPALELMALYVAAAMHDYDH
PGRTNAFLVATSAPQAVLYNDRSVLENHHAAAAWNLFMSRPEYNFLINLDHVEFKHFRFL
VIEAILATDLKKHFDFVAKFNGKVNDDVGIDWTNENDRLLVCQMCIKLADINGPAKCKEL
HLQWTDGIVNEFYEQGDEEASLGLPISPFMDRSAPQLANLQESFISHIVGPLCNSYDSAG
LMPGKWVEDSDESGDTDDPEEEEEEAPAPNEEETCENNESPKKKTFKRRKIYCQITQHLL
QNHKMWKKVIEEEQRLAGIENQSLDQTPQSHSSEQIQAIKEEEEEKGKPRGEEIPTQKPD
Q
|
| Enzyme 11 Number of Residues |
1141 |
| Enzyme 11 Molecular Weight |
124980 |
| Enzyme 11 Theoretical pI |
5.87 |
| Enzyme 11 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- cell communication
- cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 11 General Function |
Not Available |
| Enzyme 11 Specific Function |
Hydrolyzes both cyclic AMP (cAMP) and cyclic GMP (cGMP) |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
- 61-83
- 129-151
- 158-180
- 184-206
- 238-255
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
38201493  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q14432  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
PDE3A_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>3426 bp
ATGGCAGTGCCCGGCGACGCTGCACGAGTCAGGGACAAGCCCGTCCACAGTGGGGTGAGT
CAAGCCCCCACGGCGGGCCGGGACTGCCACCATCGTGCGGACCCCGCATCGCCGCGGGAC
TCGGGCTGCCGTGGCTGCTGGGGAGACCTGGTGCTGCAGCCGCTCCGGAGCTCTCGGAAA
CTTTCCTCCGCGCTGTGCGCGGGCTCCCTATCCTTTCTGCTGGCGCTGCTGGTGAGGCTG
GTCCGCGGGGAGGTCGGCTGTGACCTGGAGCAGTGTAAGGAGGCGGCGGCGGCGGAGGAG
GAGGAAGCAGCCCCGGGAGCAGAAGGGGGCGTCTTCCCGGGGCCTCGGGGAGGTGCTCCC
GGGGGCGGTGCGCGGCTCAGCCCCTGGCTGCAGCCCTCGGCGCTGCTCTTCAGTCTCCTG
TGTGCCTTCTTCTGGATGGGCTTGTACCTCCTGCGCGCCGGGGTGCGCCTGCCTCTGGCT
GTCGCGCTGCTGGCCGCCTGCTGCGGGGGGGAAGCGCTCGTCCAGATTGGGCTGGGCGTC
GGGGAGGATCACTTACTCTCACTCCCCGCTGCGGGGGTGGTGCTCAGCTGCTTGGCCGCC
GCGACATGGCTGGTGCTGAGGCTGAGGCTGGGCGTCCTCATGATCGCCTTGACTAGCGCG
GTCAGGACCGTGTCCCTCATTTCCTTAGAGAGGTTCAAGGTCGCCTGGAGACCTTACCTG
GCGTACCTGGCCGGCGTGCTGGGGATCCTCTTGGCCAGGTACGTGGAACAAATCTTGCCG
CAGTCCGCGGAGGCGGCTCCAAGGGAGCATTTGGGGTCCCAGCTGATTGCTGGGACCAAG
GAAGATATCCCGGTGTTTAAGAGGAGGAGGCGGTCCAGCTCCGTCGTGTCCGCCGAGATG
TCCGGCTGCAGCAGCAAGTCCCATCGGAGGACCTCCCTGCCCTGTATACCGAGGGAACAG
CTCATGGGGCATTCAGAATGGGACCACAAACGAGGGCCAAGAGGATCACAGTCTTCAGGA
ACCAGTATTACTGTGGACATCGCCGTCATGGGCGAAGCCCACGGCCTCATTACCGACCTC
CTGGCAGACCCTTCTCTTCCACCAAACGTGTGCACATCCTTGAGAGCCGTGAGCAACTTG
CTCAGCACACAGCTCACCTTCCAGGCCATTCACAAGCCCAGAGTGAATCCCGTTACTTCG
CTCAGTGAAAACTATACCTGTTCTGACTCTGAAGAGAGCTCTGAAAAAGACAAGCTTGCT
ATTCCAAAGCGCCTGAGAAGGAGTTTGCCTCCTGGCTTGTTGAGACGAGTTTCTTCCACT
TGGACCACCACCACCTCGGCCACAGGTCTACCCACCTTGGAGCCTGCACCAGTACGGAGA
GACCGCAGCACCAGCATCAAACTGCAGGAAGCACCTTCATCCAGTCCTGATTCTTGGAAT
AATCCAGTGATGATGACCCTCACCAAAAGCAGATCCTTTACTTCATCCTATGCTATTTCT
GCAGCTAACCATGTAAAGGCTAAAAAGCAAAGTCGACCAGGTGCCCTCGCTAAAATTTCA
CCTCTTTCATCGCCCTGCTCCTCACCTCTCCAAGGGACTCCTGCCAGCAGCCTGGTCAGC
AAAATTTCTGCAGTGCAGTTTCCAGAATCTGCTGACACAACTGCCAAACAAAGCCTAGGT
TCTCACAGGGCCTTAACTTACACTCAGAGTGCCCCAGACCTATCCCCTCAAATCCTGACT
CCACCTGTTATATGTAGCAGCTGTGGCAGACCATATTCCCAAGGGAATCCTGCTGATGAG
CCCCTGGAGAGAAGTGGGGTAGCCACTCGGACACCAAGTCGAACAGATGACACTGCTCAA
GTTACCTCTGATTATGAAACCAATAACAACAGTGACAGCAGTGACATTGTACAGAATGAA
GATGAAACAGAGTGCCTGAGAGAGCCTCTGAGGAAAGCATCGGCTTGCAGCACCTATGCT
CCTGAGACCATGATGTTTCTGGACAAACCAATTCTTGCTCCCGAACCTCTTGTCATGGAT
AACCTGGACTCAATTATGGAGCAGCTAAATACTTGGAATTTTCCAATTTTTGATTTAGTG
GAAAATATAGGAAGAAAATGTGGCCGTATTCTTAGTCAGGTATCTTACAGACTTTTTGAA
GACATGGGCCTCTTTGAAGCTTTTAAAATTCCAATTAGGGAATTTATGAATTATTTTCAT
GCTTTGGAGATTGGATATAGGGATATTCCTTATCATAACAGAATCCATGCCACTGATGTT
TTACATGCTGTTTGGTATCTTACTACACAGCCTATTCCAGGCCTCTCAACTGTGATTAAT
GATCATGGTTCAACCAGTGATTCAGATTCTGACAGTGGATTTACACATGGACATATGGGA
TATGTATTCTCAAAAACGTATAATGTGACAGATGATAAATACGGATGTCTGTCTGGGAAT
ATCCCTGCCTTGGAGTTGATGGCGCTGTATGTGGCTGCAGCCATGCACGATTATGATCAT
CCAGGAAGGACTAATGCTTTCCTGGTTGCAACTAGTGCTCCTCAGGCGGTGCTATATAAC
GATCGTTCAGTTTTGGAGAATCATCACGCAGCTGCTGCATGGAATCTTTTCATGTCCCGG
CCAGAGTATAACTTCTTAATTAACCTTGACCATGTGGAATTTAAGCATTTCCGTTTCCTT
GTCATTGAAGCAATTTTGGCCACTGACCTGAAGAAACACTTTGACTTCGTAGCCAAATTT
AATGGCAAGGTAAATGATGATGTTGGAATAGATTGGACCAATGAAAATGATCGTCTACTG
GTTTGTCAAATGTGTATAAAGTTGGCTGATATCAATGGTCCAGCTAAATGTAAAGAACTC
CATCTTCAGTGGACAGATGGTATTGTCAATGAATTTTATGAACAGGGTGATGAAGAGGCC
AGCCTTGGATTACCCATAAGCCCCTTCATGGATCGTTCTGCTCCTCAGCTGGCCAACCTT
CAGGAATCCTTCATCTCTCACATTGTGGGGCCTCTGTGCAACTCCTATGATTCAGCAGGA
CTAATGCCTGGAAAATGGGTGGAAGACAGCGATGAGTCAGGAGATACTGATGACCCAGAA
GAAGAGGAGGAAGAAGCACCAGCACCAAATGAAGAGGAAACCTGTGAAAATAATGAATCT
CCAAAAAAGAAGACTTTCAAAAGGAGAAAAATCTACTGCCAAATAACTCAGCACCTCTTA
CAGAACCACAAGATGTGGAAGAAAGTCATTGAAGAGGAGCAACGGTTGGCAGGCATAGAA
AATCAATCCCTGGACCAGACCCCTCAGTCGCACTCTTCAGAACAGATCCAGGCTATCAAG
GAAGAAGAAGAAGAGAAAGGGAAACCAAGAGGCGAGGAGATACCAACCCAAAAGCCAGAC
CAGTGA
|
| Enzyme 11 GenBank Gene ID |
M91667  |
| Enzyme 11 GeneCard ID |
PDE3A  |
| Enzyme 11 GenAtlas ID |
PDE3A  |
| Enzyme 11 HGNC ID |
HGNC:8778  |
| Enzyme 11 Chromosome Location |
Not Available |
| Enzyme 11 Locus |
Not Available |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Meacci E, Taira M, Moos M Jr, Smith CJ, Movsesian MA, Degerman E, Belfrage P, Manganiello V: Molecular cloning and expression of human myocardial cGMP-inhibited cAMP phosphodiesterase. Proc Natl Acad Sci U S A. 1992 May 1;89(9):3721-5. [PubMed
]
- Cheung PP, Xu H, McLaughlin MM, Ghazaleh FA, Livi GP, Colman RW: Human platelet cGI-PDE: expression in yeast and localization of the catalytic domain by deletion mutagenesis. Blood. 1996 Aug 15;88(4):1321-9. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5876 |
| Enzyme 12 Name |
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A |
| Enzyme 12 Synonyms |
Not Available |
| Enzyme 12 Gene Name |
PDE10A |
| Enzyme 12 Protein Sequence |
>cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
MRIEERKSQHLTGLTDEKVKAYLSLHPQVLDEFVSESVSAETVEKWLKRKNNKSEDESAP
KEVSRYQDTNMQGVVYELNSYIEQRLDTGGDNQLLLYELSSIIKIATKADGFALYFLGEC
NNSLCIFTPPGIKEGKPRLIPAGPITQGTTVSAYVAKSRKTLLVEDILGDERFPRGTGLE
SGTRIQSVLCLPIVTAIGDLIGILELYRHWGKEAFCLSHQEVATANLAWASVAIHQVQVC
RGLAKQTELNDFLLDVSKTYFDNIVAIDSLLEHIMIYAKNLVNADRCALFQVDHKNKELY
SDLFDIGEEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDAYADPRFNREVDLYT
GYTTRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHR
IRHSECIYRVTMEKLSYHSICTSEEWQGLMQFTLPVRLCKEIELFHFDIGPFENMWPGIF
VYMVHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAILQNNHTLFTD
LERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTVSILQLEGHNI
FSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLNNQSHRDRVIGLMM
TACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFY
NAVAIPCYTTLTQILPPTEPLLKACRDNLSQWEKVIRGEETATWISSPSVAQKAAASED
|
| Enzyme 12 Number of Residues |
779 |
| Enzyme 12 Molecular Weight |
88413 |
| Enzyme 12 Theoretical pI |
6.57 |
| Enzyme 12 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- cell communication
- cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 12 General Function |
Not Available |
| Enzyme 12 Specific Function |
Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This enzyme can hydrolyze both cAMP and cGMP, having a higher affinity for cAMP |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
4958858  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q9Y233  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
PDE10_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>2340 bp
ATGAGGATAGAAGAGAGGAAATCCCAACATTTAACAGGTTTGACAGATGAAAAAGTGAAG
GCATATCTTTCTCTTCACCCCCAGGTATTAGATGAATTTGTATCTGAAAGTGTTAGTGCA
GAGACAGTAGAGAAATGGCTGAAGAGGAAGAACAACAAATCAGAAGATGAATCAGCTCCT
AAGGAAGTCAGCAGGTACCAAGATACGAATATGCAGGGAGTTGTATATGAACTAAACAGC
TATATAGAACAACGGTTGGACACAGGAGGAGACAACCAGCTACTCCTCTATGAACTGAGC
AGCATCATTAAAATAGCCACAAAAGCCGATGGATTTGCACTGTATTTCCTTGGAGAGTGC
AATAATAGCCTGTGTATATTCACGCCACCTGGGATAAAGGAAGGAAAACCCCGCCTCATC
CCTGCTGGGCCCATCACTCAGGGCACCACCGTCTCTGCTTATGTGGCCAAGTCCAGGAAA
ACACTGCTAGTAGAAGACATCCTTGGAGATGAACGATTTCCAAGAGGTACTGGACTGGAA
TCAGGGACTCGTATCCAGTCTGTTCTTTGCTTACCAATTGTCACTGCAATTGGTGACTTG
ATTGGTATTCTCGAGCTGTATCGGCACTGGGGCAAAGAAGCCTTCTGTCTTAGTCACCAG
GAGGTTGCAACAGCAAATCTTGCCTGGGCTTCAGTAGCAATACATCAGGTGCAGGTATGC
AGAGGCCTTGCCAAACAGACAGAATTGAATGACTTCCTACTCGACGTATCAAAAACATAT
TTTGATAACATAGTTGCAATAGATTCTCTACTTGAACACATAATGATATATGCAAAAAAC
CTGGTGAATGCCGATCGTTGTGCGCTTTTCCAGGTGGACCATAAGAACAAGGAGTTATAT
TCAGACCTTTTTGATATTGGAGAGGAAAAGGAAGGAAAACCTGTCTTCAAGAAGACCAAA
GAGATAAGATTTTCAATTGAGAAAGGAATTGCTGGCCAAGTAGCAAGAACAGGGGAAGTC
CTGAACATTCCAGATGCCTATGCAGACCCACGCTTTAACAGAGAAGTAGACTTGTACACA
GGCTACACCACGCGGAACATCCTGTGCATGCCCATCGTCAGCCGAGGCAGCGTGATAGGT
GTGGTGCAGATGGTCAACAAAATCAGTGGCAGTGCCTTCTCTAAAACAGATGAAAACAAC
TTCAAAATGTTTGCCGTCTTTTGTGCTTTAGCCTTACACTGTGCTAATATGTATCATAGA
ATTCGCCACTCAGAGTGCATTTACCGGGTAACGATGGAAAAGCTGTCCTACCATAGCATT
TGTACTTCAGAAGAGTGGCAAGGTCTCATGCAATTCACCCTTCCCGTGCGTCTCTGCAAA
GAAATTGAATTATTCCACTTTGACATTGGTCCTTTTGAAAACATGTGGCCTGGAATTTTT
GTCTACATGGTTCATCGGTCCTGTGGGACATCCTGCTTTGAGCTTGAAAAGTTGTGTCGT
TTTATTATGTCTGTGAAGAAGAACTATCGGCGGGTTCCTTATCACAACTGGAAGCATGCG
GTCACTGTAGCACACTGCATGTATGCCATACTTCAGAACAATCACACGCTTTTCACAGAC
CTTGAGCGCAAAGGACTGCTGATTGCGTGTCTGTGTCATGACCTGGACCACAGGGGCTTC
AGTAACAGCTACCTGCAGAAGTTCGACCACCCTCTGGCCGCTCTCTACTCCACTTCCACC
ATGGAGCAGCACCACTTCTCCCAGACTGTGTCCATCCTTCAGTTGGAAGGGCACAATATC
TTCTCCACTCTGAGCTCCAGTGAATATGAGCAGGTGCTTGAGATCATCCGCAAAGCCATC
ATTGCCACAGACCTTGCTTTATACTTTGGAAACAGGAAGCAGTTGGAAGAGATGTACCAG
ACCGGATCACTAAACCTTAATAATCAATCACATAGAGACCGTGTAATTGGTTTGATGATG
ACTGCCTGTGACCTTTGTTCTGTGACAAAACTGTGGCCCGTTACAAAATTGACGGCAAAT
GATATATATGCAGAATTCTGGGCTGAGGGTGATGAAATGAAGAAATTGGGAATACAGCCT
ATTCCTATGATGGACAGAGACAAGAAGGATGAAGTCCCCCAAGGCCAGCTTGGGTTCTAC
AATGCCGTGGCCATTCCCTGCTATACAACCCTTACCCAGATCCTCCCTCCCACGGAGCCT
CTTCTGAAAGCATGCAGGGATAATCTCAGTCAGTGGGAGAAGGTGATTCGAGGGGAGGAG
ACTGCAACCTGGATTTCATCCCCATCCGTGGCTCAGAAGGCAGCTGCATCTGAAGATTGA
|
| Enzyme 12 GenBank Gene ID |
AB020593  |
| Enzyme 12 GeneCard ID |
PDE10A  |
| Enzyme 12 GenAtlas ID |
PDE10A  |
| Enzyme 12 HGNC ID |
HGNC:8772  |
| Enzyme 12 Chromosome Location |
Not Available |
| Enzyme 12 Locus |
Not Available |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Fujishige K, Kotera J, Michibata H, Yuasa K, Takebayashi S, Okumura K, Omori K: Cloning and characterization of a novel human phosphodiesterase that hydrolyzes both cAMP and cGMP (PDE10A). J Biol Chem. 1999 Jun 25;274(26):18438-45. [PubMed
]
- Loughney K, Snyder PB, Uher L, Rosman GJ, Ferguson K, Florio VA: Isolation and characterization of PDE10A, a novel human 3', 5'-cyclic nucleotide phosphodiesterase. Gene. 1999 Jun 24;234(1):109-17. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5877 |
| Enzyme 13 Name |
Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C |
| Enzyme 13 Synonyms |
- Cam-PDE 1C
- hCam-3
|
| Enzyme 13 Gene Name |
PDE1C |
| Enzyme 13 Protein Sequence |
>Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
MESPTKEIEEFESNSLKYLQPEQIEKIWLRLRGLRKYKKTSQRLRSLVKQLERGEASVVD
LKKNLEYAATVLESVYIDETRRLLDTEDELSDIQSDAVPSEVRDWLASTFTRQMGMMLRR
SDEKPRFKSIVHAVQAGIFVERMYRRTSNMVGLSYPPAVIEALKDVDKWSFDVFSLNEAS
GDHALKFIFYELLTRYDLISRFKIPISALVSFVEALEVGYSKHKNPYHNLMHAADVTQTV
HYLLYKTGVANWLTELEIFAIIFSAAIHDYEHTGTTNNFHIQTRSDPAILYNDRSVLENH
HLSAAYRLLQDDEEMNILINLSKDDWREFRTLVIEMVMATDMSCHFQQIKAMKTALQQPE
AIEKPKALSLMLHTADISHPAKAWDLHHRWTMSLLEEFFRQGDREAELGLPFSPLCDRKS
TMVAQSQVGFIDFIVEPTFTVLTDMTEKIVSPLIDETSQTGGTGQRRSSLNSISSSDAKR
SGVKTSGSEGSAPINNSVISVDYKSFKATWTEVVHINRERWRAKVPKEEKAKKEAEEKAR
LAAEEQQKEMEAKSQAEEGASGKAEKKTSGETKNQVNGTRANKSDNPRGKNSKAEKSSGE
QQQNGDFKDGKNKTDKKDHSNIGNDSKKTDGTKQRSHGSPAPSTSSTCRLTLPVIKPPLR
HFKRPAYASSSYAPSVSKKTDEHPARYKMLDQRIKMKKIQNISHNWNRK
|
| Enzyme 13 Number of Residues |
709 |
| Enzyme 13 Molecular Weight |
80761 |
| Enzyme 13 Theoretical pI |
9.31 |
| Enzyme 13 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- cell communication
- cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 13 General Function |
Not Available |
| Enzyme 13 Specific Function |
Has a high affinity for both cAMP and cGMP |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
1151111  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q14123  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
PDE1C_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1905 bp
ATGGAGTCGCCAACCAAGGAGATTGAAGAATTTGAGAGCAACTCTCTGAAATACCTGCAA
CCGGAACAGATCGAGAAAATCTGGCTTCGGCTCCGCGGGCTGAGGAAATATAAGAAAACG
TCCCAGAGATTACGGTCTTTGGTCAAACAATTAGAGAGAGGGGAAGCTTCAGTGGTAGAT
CTTAAGAAGAATTTGGAATATGCAGCCACAGTGCTTGAATCTGTGTATATTGATGAAACA
AGGAGACTCCTGGATACAGAGGATGAGCTCAGTGACATTCAGTCAGATGCTGTGCCTTCT
GAGGTCCGAGACTGGCTGGCCTCCACCTTCACGCGGCAGATGGGGATGATGCTCAGGAGG
AGCGACGAGAAGCCCCGGTTCAAGAGCATCGTTCACGCAGTGCAGGCTGGGATATTTGTG
GAGAGAATGTATAGACGGACATCAAACATGGTTGGACTGAGCTATCCACCAGCTGTTATT
GAGGCATTAAAGGATGTGGACAAGTGGTCCTTTGACGTCTTTTCCCTCAATGAGGCCAGT
GGGGATCATGCACTGAAATTTATTTTCTATGAACTACTCACACGTTATGATCTGATCAGC
CGTTTCAAGATCCCCATTTCTGCACTTGTCTCATTTGTGGAGGCCCTGGAAGTGGGATAC
AGCAAGCACAAAAATCCTTACCATAACTTAATGCACGCTGCCGATGTTACACAGACAGTG
CATTACCTCCTCTATAAGACAGGAGTGGCGAACTGGCTGACGGAGCTGGAGATCTTTGCT
ATAATCTTCTCAGCTGCCATCCATGACTACGAGCATACCGGAACCACCAACAATTTCCAC
ATTCAGACTCGGTCTGATCCAGCTATTCTGTATAATGACAGATCTGTACTGGAGAATCAC
CATTTAAGTGCAGCTTATCGCCTTCTGCAAGATGACGAGGAAATGAATATTTTGATTAAC
CTCTCAAAGGATGACTGGAGGGAGTTTCGAACCTTGGTAATTGAAATGGTGATGGCCACA
GATATGTCTTGTCACTTCCAACAAATCAAAGCAATGAAGACTGCTCTGCAGCAGCCAGAA
GCCATTGAAAAGCCAAAAGCCTTATCCCTTATGCTGCATACAGCAGATATTAGCCATCCA
GCAAAAGCATGGGACCTCCATCATCGCTGGACAATGTCACTCCTGGAGGAGTTCTTCAGA
CAGGGTGACAGAGAAGCAGAGCTGGGGCTGCCTTTTTCTCCTCTGTGTGACCGAAAGTCC
ACTATGGTTGCTCAGTCACAAGTAGGTTTCATTGATTTCATCGTGGAACCCACCTTCACT
GTGCTTACGGACATGACCGAGAAGATTGTGAGTCCATTAATCGATGAAACCTCTCAAACT
GGTGGGACAGGACAGAGGCGTTCGAGTTTGAATAGCATCAGCTCGTCAGATGCCAAGCGA
TCAGGTGTCAAGACCTCTGGTTCAGAGGGAAGTGCCCCGATCAACAATTCTGTCATCTCC
GTTGACTATAAGAGCTTTAAAGCTACTTGGACGGAAGTGGTGCACATCAATCGGGAGAGA
TGGAGGGCCAAGGTACCCAAAGAGGAGAAGGCCAAGAAGGAAGCAGAGGAAAAGGCTCGC
CTGGCCGCAGAGGAGCAGCAAAAGGAAATGGAAGCCAAAAGCCAGGCTGAAGAAGGCGCA
TCTGGCAAAGCTGAGAAAAAGACGTCTGGAGAAACTAAGAATCAAGTCAATGGAACACGG
GCAAACAAAAGTGACAACCCTCGTGGGAAAAATTCCAAAGCCGAGAAGTCATCAGGAGAA
CAGCAACAGAATGGTGACTTCAAAGATGGTAAAAATAAGACAGACAAGAAGGATCACTCT
AACATCGGAAATGATTCAAAGAAAACAGATGATTCACAAGAGTAA
|
| Enzyme 13 GenBank Gene ID |
U40371  |
| Enzyme 13 GeneCard ID |
PDE1C  |
| Enzyme 13 GenAtlas ID |
PDE1C  |
| Enzyme 13 HGNC ID |
HGNC:8776  |
| Enzyme 13 Chromosome Location |
Not Available |
| Enzyme 13 Locus |
Not Available |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Loughney K, Martins TJ, Harris EA, Sadhu K, Hicks JB, Sonnenburg WK, Beavo JA, Ferguson K: Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3',5'-cyclic nucleotide phosphodiesterases. J Biol Chem. 1996 Jan 12;271(2):796-806. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
5881 |
| Enzyme 14 Name |
cAMP-specific 3',5'-cyclic phosphodiesterase 4B |
| Enzyme 14 Synonyms |
- DPDE4
- PDE32
|
| Enzyme 14 Gene Name |
PDE4B |
| Enzyme 14 Protein Sequence |
>cAMP-specific 3',5'-cyclic phosphodiesterase 4B
MKKSRSVMTVMADDNVKDYFECSLSKSYSSSSNTLGIDLWRGRRCCSGNLQLPPLSQRQS
ERARTPEGDGISRPTTLPLTTLPSIAITTVSQECFDVENGPSPGRSPLDPQASSSAGLVL
HATFPGHSQRRESFLYRSDSDYDLSPKAMSRNSSLPSEQHGDDLIVTPFAQVLASLRSVR
NNFTILTNLHGTSNKRSPAASQPPVSRVNPQEESYQKLAMETLEELDWCLDQLETIQTYR
SVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQNDVEIPSPTQKDREKKK
KQQLMTQISGVKKLMHSSSLNNTSISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSH
NRPLTCIMYAIFQERDLLKTFRISSDTFITYMMTLEDHYHSDVAYHNSLHAADVAQSTHV
LLSTPALDAVFTDLEILAAIFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHL
AVGFKLLQEEHCDIFMNLTKKQRQTLRKMVIDMVLATDMSKHMSLLADLKTMVETKKVTS
SGVLLLDNYTDRIQVLRNMVHCADLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEI
SPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILDTLEDNRNWYQSMIPQSP
SPPLDEQNRDCQGLMEKFQFELTLDEEDSEGPEKEGEGHSYFSSTKTLCVIDPENRDSLG
ETDIDIATEDKSPVDT
|
| Enzyme 14 Number of Residues |
736 |
| Enzyme 14 Molecular Weight |
83344 |
| Enzyme 14 Theoretical pI |
4.89 |
| Enzyme 14 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- cell communication
- cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 14 General Function |
Not Available |
| Enzyme 14 Specific Function |
May be involved in mediating central nervous system effects of therapeutic agents ranging from antidepressants to antiasthmatic and anti-inflammatory agents |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
347122  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q07343  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
PDE4B_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>2211 bp
ATGAAGAAAAGCAGGAGTGTGATGACGGTGATGGCTGATGATAATGTTAAAGATTATTTT
GAATGTAGCTTGAGTAAATCCTACAGTTCTTCCAGTAACACACTTGGGATCGACCTCTGG
AGAGGGAGAAGGTGTTGCTCAGGAAACTTACAGTTACCACCACTGTCTCAAAGACAGAGT
GAAAGGGCAAGGACTCCTGAGGGAGATGGTATTTCCAGGCCGACCACACTGCCTTTGACA
ACGCTTCCAAGCATTGCTATTACAACTGTAAGCCAGGAGTGCTTTGATGTGGAAAATGGC
CCTTCCCCAGGTCGGAGTCCACTGGATCCCCAGGCCAGCTCTTCCGCTGGGCTGGTACTT
CACGCCACCTTTCCTGGGCACAGCCAGCGCAGAGAGTCATTTCTCTACAGATCAGACAGC
GACTATGACTTGTCACCAAAGGCGATGTCGAGAAACTCTTCTCTTCCAAGCGAGCAACAC
GGCGATGACTTGATTGTAACTCCTTTTGCCCAGGTCCTTGCCAGCTTGCGAAGTGTGAGA
AACAACTTCACTATACTGACAAACCTTCATGGTACATCTAACAAGAGGTCCCCAGCTGCT
AGTCAGCCTCCTGTCTCCAGAGTCAACCCACAAGAAGAATCTTATCAAAAATTAGCAATG
GAAACGCTGGAGGAATTAGACTGGTGTTTAGACCAGCTAGAGACCATACAGACCTACCGG
TCTGTCAGTGAGATGGCTTCTAACAAGTTCAAAAGAATGCTGAACCGGGAGCTGACACAC
CTCTCAGAGATGAGCCGATCAGGGAACCAGGTGTCTGAATACATTTCAAATACTTTCTTA
GACAAGCAGAATGATGTGGAGATCCCATCTCCTACCCAGAAAGACAGGGAGAAAAAGAAA
AAGCAGCAGCTCATGACCCAGATAAGTGGAGTGAAGAAATTAATGCATAGTTCAAGCCTA
AACAATACAAGCATCTCACGCTTTGGAGTCAACACTGAAAATGAAGATCACCTGGCCAAG
GAGCTGGAAGACCTGAACAAATGGGGTCTTAACATCTTTAATGTGGCTGGATATTCTCAC
AATAGACCCCTAACATGCATCATGTATGCTATATTCCAGGAAAGAGACCTCCTAAAGACA
TTCAGAATCTCATCTGACACATTTATAACCTACATGATGACTTTAGAAGACCATTACCAT
TCTGACGTGGCATATCACAACAGCCTGCACGCTGCTGATGTAGCCCAGTCGACCCATGTT
CTCCTTTCTACACCAGCATTAGACGCTGTCTTCACAGATTTGGAGATCCTGGCTGCCATT
TTTGCAGCTGCCATCCATGACGTTGATCATCCTGGAGTCTCCAATCAGTTTCTCATCAAC
ACAAATTCAGAACTTGCTTTGATGTATAATGATGAATCTGTGTTGGAAAATCATCACCTT
GCTGTGGGTTTCAAACTGCTGCAAGAAGAACACTGTGACATCTTCATGAATCTCACCAAG
AAGCAGCGTCAGACACTCAGGAAGATGGTTATTGACATGGTGTTAGCAACTGATATGTCT
AAACATATGAGCCTGCTGGCAGACCTGAAGACAATGGTAGAAACGAAGAAAGTTACAAGT
TCAGGCGTTCTTCTCCTAGACAACTATACCGATCGCATTCAGGTCCTTCGCAACATGGTA
CACTGTGCAGACCTGAGCAACCCCACCAAGTCCTTGGAATTGTATCGGCAATGGACAGAC
CGCATCATGGAGGAATTTTTCCAGCAGGGAGACAAAGAGCGGGAGAGGGGAATGGAAATT
AGCCCAATGTGTGATAAACACACAGCTTCTGTGGAAAAATCCCAGGTTGGTTTCATCGAC
TACATTGTCCATCCATTGTGGGAGACATGGGCAGATTTGGTACAGCCTGATGCTCAGGAC
ATTCTCGATACCTTAGAAGATAACAGGAACTGGTATCAGAGCATGATACCTCAAAGTCCC
TCACCACCACTGGACGAGCAGAACAGGGACTGCCAGGGTCTGATGGAGAAGTTTCAGTTT
GAACTGACTCTCGATGAGGAAGATTCTGAAGGACCTGAGAAGGAGGGAGAGGGACACAGC
TATTTCAGCAGCACAAAGACGCTTTGTGTGATTGATCCAGAAAACAGAGATTCCCTGGGA
GAGACTGACATAGACATTGCAACAGAAGACAAGTCCCCCGTGGATACATAA
|
| Enzyme 14 GenBank Gene ID |
L20966  |
| Enzyme 14 GeneCard ID |
PDE4B  |
| Enzyme 14 GenAtlas ID |
PDE4B  |
| Enzyme 14 HGNC ID |
HGNC:8781  |
| Enzyme 14 Chromosome Location |
Not Available |
| Enzyme 14 Locus |
Not Available |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed
]
- Huston E, Lumb S, Russell A, Catterall C, Ross AH, Steele MR, Bolger GB, Perry MJ, Owens RJ, Houslay MD: Molecular cloning and transient expression in COS7 cells of a novel human PDE4B cAMP-specific phosphodiesterase, HSPDE4B3. Biochem J. 1997 Dec 1;328 ( Pt 2):549-58. [PubMed
]
- McLaughlin MM, Cieslinski LB, Burman M, Torphy TJ, Livi GP: A low-Km, rolipram-sensitive, cAMP-specific phosphodiesterase from human brain. Cloning and expression of cDNA, biochemical characterization of recombinant protein, and tissue distribution of mRNA. J Biol Chem. 1993 Mar 25;268(9):6470-6. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
5884 |
| Enzyme 15 Name |
cAMP-specific 3',5'-cyclic phosphodiesterase 7B |
| Enzyme 15 Synonyms |
Not Available |
| Enzyme 15 Gene Name |
PDE7B |
| Enzyme 15 Protein Sequence |
>cAMP-specific 3',5'-cyclic phosphodiesterase 7B
MSCLMVERCGEILFENPDQNAKCVCMLGDIRLRGQTGVRAERRGSYPFIDFRLLNSTTYS
GEIGTKKKVKRLLSFQRYFHASRLLRGIIPQAPLHLLDEDYLGQARHMLSKVGMWDFDIF
LFDRLTNGNSLVTLLCHLFNTHGLIHHFKLDMVTLHRFLVMVQEDYHSQNPYHNAVHAAD
VTQAMHCYLKEPKLASFLTPLDIMLGLLAAAAHDVDHPGVNQPFLIKTNHHLANLYQNMS
VLENHHWRSTIGMLRESRLLAHLPKEMTQDIEQQLGSLILATDINRQNEFLTRLKAHLHN
KDLRLEDAQDRHFMLQIALKCADICNPCRIWEMSKQWSERVCEEFYRQGELEQKFELEIS
PLCNQQKDSIPSIQIGFMSYIVEPLFREWAHFTGNSTLSENMLGHLAHNKAQWKSLLPRQ
HRSRGSSGSGPDHDHAGQGTESEEQEGDSP
|
| Enzyme 15 Number of Residues |
450 |
| Enzyme 15 Molecular Weight |
51836 |
| Enzyme 15 Theoretical pI |
7.03 |
| Enzyme 15 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- cell communication
- cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 15 General Function |
Not Available |
| Enzyme 15 Specific Function |
May be involved in the control of cAMP-mediated neural activity and cAMP metabolism in the brain |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
8439497  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q9NP56  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
PDE7B_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1353 bp
ATGTCTTGTTTAATGGTTGAGAGGTGTGGCGAAATCTTGTTTGAGAACCCCGATCAGAAT
GCCAAATGTGTTTGCATGCTGGGAGATATACGACTAAGGGGTCAGACGGGGGTTCGTGCT
GAACGCCGTGGCTCCTACCCATTCATTGACTTCCGCCTACTTAACAGTACAACATACTCA
GGGGAGATTGGCACCAAGAAAAAGGTGAAAAGACTATTAAGCTTTCAAAGATACTTCCAT
GCATCAAGGCTGCTTCGTGGAATTATACCACAAGCCCCTCTGCACCTGCTGGATGAAGAC
TACCTTGGACAAGCAAGGCATATGCTCTCCAAAGTGGGAATGTGGGATTTTGACATTTTC
TTGTTTGATCGCTTGACAAATGGAAACAGCCTGGTAACACTGTTGTGCCACCTCTTCAAT
ACCCATGGACTCATTCACCATTTCAAGTTAGATATGGTGACCTTACACCGATTTTTAGTC
ATGGTTCAAGAAGATTACCACAGCCAAAACCCGTATCACAATGCTGTTCACGCAGCCGAC
GTCACCCAGGCCATGCACTGCTACCTGAAAGAGCCAAAGCTTGCCAGCTTCCTCACGCCT
CTGGACATCATGCTTGGACTGCTGGCTGCAGCAGCACACGATGTGGACCACCCAGGGGTG
AACCAGCCATTTTTGATAAAAACTAACCACCATCTTGCAAACCTATATCAGAATATGTCT
GTGCTGGAGAATCATCACTGGCGATCTACAATTGGCATGCTTCGAGAATCAAGGCTTCTT
GCTCATTTGCCAAAGGAAATGACACAGGATATTGAACAGCAGCTGGGCTCCTTGATCTTG
GCAACAGACATCAACAGGCAGAATGAATTTTTGACCAGATTGAAAGCTCACCTCCACAAT
AAAGACTTAAGACTGGAGGATGCACAGGACAGGCACTTTATGCTTCAGATCGCCTTGAAG
TGTGCTGACATTTGCAATCCTTGTAGAATCTGGGAGATGAGCAAGCAGTGGAGTGAAAGG
GTCTGTGAAGAATTCTACAGGCAAGGTGAACTTGAACAGAAATTTGAACTGGAAATCAGT
CCTCTTTGTAATCAACAGAAAGATTCCATCCCTAGTATACAAATTGGTTTCATGAGCTAC
ATCGTGGAGCCGCTCTTCCGGGAATGGGCCCATTTCACGGGTAACAGCACCCTGTCGGAG
AACATGCTGGGCCACCTCGCACACAACAAGGCCCAGTGGAAGAGCCTGTTGCCCAGGCAG
CACAGAAGCAGGGGCAGCAGTGGCAGCGGGCCTGACCACGACCACGCAGGCCAAGGGACT
GAGAGCGAGGAGCAGGAAGGCGACAGCCCCTAG
|
| Enzyme 15 GenBank Gene ID |
AB038040  |
| Enzyme 15 GeneCard ID |
PDE7B  |
| Enzyme 15 GenAtlas ID |
PDE7B  |
| Enzyme 15 HGNC ID |
HGNC:8792  |
| Enzyme 15 Chromosome Location |
Not Available |
| Enzyme 15 Locus |
Not Available |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Sasaki T, Kotera J, Yuasa K, Omori K: Identification of human PDE7B, a cAMP-specific phosphodiesterase. Biochem Biophys Res Commun. 2000 May 19;271(3):575-83. [PubMed
]
- Gardner C, Robas N, Cawkill D, Fidock M: Cloning and characterization of the human and mouse PDE7B, a novel cAMP-specific cyclic nucleotide phosphodiesterase. Biochem Biophys Res Commun. 2000 May 27;272(1):186-92. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
5888 |
| Enzyme 16 Name |
High-affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A |
| Enzyme 16 Synonyms |
Not Available |
| Enzyme 16 Gene Name |
PDE9A |
| Enzyme 16 Protein Sequence |
>High-affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAM
VSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRRE
GAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANH
LAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDV
PTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLF
CVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYN
NTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLI
LATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCL
LEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIML
QPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA
|
| Enzyme 16 Number of Residues |
593 |
| Enzyme 16 Molecular Weight |
68493 |
| Enzyme 16 Theoretical pI |
6.10 |
| Enzyme 16 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- cell communication
- cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 16 General Function |
Not Available |
| Enzyme 16 Specific Function |
Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase has a high affinity for cGMP |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
- guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
3242777  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
O76083  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
PDE9A_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1782 bp
ATGGGATCCGGCTCCTCCAGCTACCGGCCCAAGGCCATCTACCTGGACATCGATGGACGC
ATTCAGAAGGTAATCTTCAGCAAGTACTGCAACTCCAGCGACATCATGGACCTGTTCTGC
ATCGCCACCGGCCTGCCTCGGAACACGACCATCTCCCTGCTGACCACCGACGACGCCATG
GTCTCCATCGACCCCACCATGCCCGCGAATTCAGAACGCACTCCGTACAAAGTGAGACCT
GTGGCCATCAAGCAACTCTCCGCTGGTGTCGAGGACAAGAGAACCACAAGCCGTGGCCAG
TCTGCTGAGAGACCACTGAGGGACAGACGGGTTGTGGGCCTGGAGCAGCCCCGGAGGGAA
GGAGCATTTGAAAGTGGACAGGTAGAGCCCAGGCCCAGAGAGCCCCAGGGCTGCTACCAG
GAAGGCCAGCGCATCCCTCCAGAGAGAGAAGAATTAATCCAGAGCGTGCTGGCGCAGGTT
GCAGAGCAGTTCTCAAGAGCATTCAAAATCAATGAACTGAAAGCTGAAGTTGCAAATCAC
TTGGCTGTCCTAGAGAAACGCGTGGAATTGGAAGGACTAAAAGTGGTGGAGATTGAGAAA
TGCAAGAGTGACATTAAGAAGATGAGGGAGGAGCTGGCGGCCAGAAGCAGCAGGACCAAC
TGCCCCTGTAAGTACAGTTTTTTGGATAACCACAAGAAGTTGACTCCTCGACGCGATGTT
CCCACTTACCCCAAGTACCTGCTCTCTCCAGAGACCATCGAGGCCCTGCGGAAGCCGACC
TTTGACGTCTGGCTTTGGGAGCCCAATGAGATGCTGAGCTGCCTGGAGCACATGTACCAC
GACCTCGGGCTGGTCAGGGACTTCAGCATCAACCCTGTCACCCTCAGGAGGTGGCTGTTC
TGTGTCCACGACAACTACAGAAACAACCCCTTCCACAACTTCCGGCACTGCTTCTGCGTG
GCCCAGATGATGTACAGCATGGTCTGGCTCTGCAGTCTCCAGGAGAAGTTCTCACAAACG
GATATCCTGATCCTAATGACAGCGGCCATCTGCCACGATCTGGACCATCCCGGCTACAAC
AACACGTACCAGATCAATGCCCGCACAGAGCTGGCGGTCCGCTACAATGACATCTCACCG
CTGGAGAACCACCACTGCGCCGTGGCCTTCCAGATCCTCGCCGAGCCTGAGTGCAACATC
TTCTCCAACATCCCACCTGATGGGTTCAAGCAGATCCGACAGGGAATGATCACATTAATC
TTGGCCACTGACATGGCAAGACATGCAGAAATTATGGATTCTTTCAAAGAGAAAATGGAG
AATTTTGACTACAGCAACGAGGAGCACATGACCCTGCTGAAGATGATTTTGATAAAATGC
TGTGATATCTCTAACGAGGTCCGTCCAATGGAAGTCGCAGAGCCTTGGGTGGACTGTTTA
TTAGAGGAATATTTTATGCAGAGCGACCGTGAGAAGTCAGAAGGCCTTCCTGTGGCACCG
TTCATGGACCGAGACAAAGTGACCAAGGCCACAGCCCAGATTGGGTTCATCAAGTTTGTC
CTGATCCCAATGTTTGAAACAGTGACCAAGCTCTTCCCCATGGTTGAGGAGATCATGCTG
CAGCCACTTTGGGAATCCCGAGATCGCTACGAGGAGCTGAAGCGGATAGATGACGCCATG
AAAGAGTTACAGAAGAAGACTGACAGCTTGACGTCTGGGGCCACCGAGAAGTCCAGAGAG
AGAAGCAGAGATGTGAAAAACAGTGAAGGAGACTGTGCCTGA
|
| Enzyme 16 GenBank Gene ID |
AF048837  |
| Enzyme 16 GeneCard ID |
PDE9A  |
| Enzyme 16 GenAtlas ID |
PDE9A  |
| Enzyme 16 HGNC ID |
HGNC:8795  |
| Enzyme 16 Chromosome Location |
Not Available |
| Enzyme 16 Locus |
Not Available |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Fisher DA, Smith JF, Pillar JS, St Denis SH, Cheng JB: Isolation and characterization of PDE9A, a novel human cGMP-specific phosphodiesterase. J Biol Chem. 1998 Jun 19;273(25):15559-64. [PubMed
]
- Guipponi M, Scott HS, Kudoh J, Kawasaki K, Shibuya K, Shintani A, Asakawa S, Chen H, Lalioti MD, Rossier C, Minoshima S, Shimizu N, Antonarakis SE: Identification and characterization of a novel cyclic nucleotide phosphodiesterase gene (PDE9A) that maps to 21q22.3: alternative splicing of mRNA transcripts, genomic structure and sequence. Hum Genet. 1998 Oct;103(4):386-92. [PubMed
]
- Rentero C, Monfort A, Puigdomenech P: Identification and distribution of different mRNA variants produced by differential splicing in the human phosphodiesterase 9A gene. Biochem Biophys Res Commun. 2003 Feb 14;301(3):686-92. [PubMed
]
- Wang P, Wu P, Egan RW, Billah MM: Identification and characterization of a new human type 9 cGMP-specific phosphodiesterase splice variant (PDE9A5). Differential tissue distribution and subcellular localization of PDE9A variants. Gene. 2003 Sep 18;314:15-27. [PubMed
]
- Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
5889 |
| Enzyme 17 Name |
cGMP-dependent 3',5'-cyclic phosphodiesterase |
| Enzyme 17 Synonyms |
- Cyclic GMP-stimulated phosphodiesterase
- CGS-PDE
- cGSPDE
|
| Enzyme 17 Gene Name |
PDE2A |
| Enzyme 17 Protein Sequence |
>cGMP-dependent 3',5'-cyclic phosphodiesterase
MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADSLQDALLSLGSVIDI
SGLQRAVKEALSAVLPRVETVYTYLLDGESQLVCEDPPHELPQEGKVREAIISQKRLGCN
GLGFSDLPGKPLARLVAPLAPDTQVLVMPLADKEAGAVAAVILVHCGQLSDNEEWSLQAV
EKHTLVALRRVQVLQQRGPREAPRAVQNPPEGTAEDQKGGAAYTDRDRKILQLCGELYDL
DASSLQLKVLQYLQQETRASRCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPLTGCLGQVV
EDKKSIQLKDLTSEDVQQLQSMLGCELQAMLCVPVISRATDQVVALACAFNKLEGDLFTD
EDEHVIQHCFHYTSTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITE
ARNLSNAEICSVFLLDQNELVAKVFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPD
AYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELVNKINGPWFSKFDEDLATAF
SIYCGISIAHSLLYKKVNEAQYRSHLANEMMMYHMKVSDDEYTKLLHDGIQPVAAIDSNF
ASFTYTPRSLPEDDTSMAILSMLQDMNFINNYKIDCPTLARFCLMVKKGYRDPPYHNWMH
AFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYS
SEGSVMERHHFAQAIAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDL
QKMAEVGYDRNNKQHHRLLLCLLMTSCDLSDQTKGWKTTRKIAELIYKEFFSQGDLEKAM
GNRPMEMMDREKAYIPELQISFMEHIAMPIYKLLQDLFPKAAELYERVASNREHWTKVSH
KFTIRGLPSNNSLDFLDEEYEVPDLDGTRAPINGCCSLDAE
|
| Enzyme 17 Number of Residues |
941 |
| Enzyme 17 Molecular Weight |
105718 |
| Enzyme 17 Theoretical pI |
5.08 |
| Enzyme 17 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- cell communication
- cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 17 General Function |
Not Available |
| Enzyme 17 Specific Function |
Hydrolyzes both cyclic AMP (cAMP) and cyclic GMP (cGMP) |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
2108052  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
O00408  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
PDE2A_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>2826 bp
ATGGGGCAGGCATGCGGCCACTCCATCCTCTGCAGGAGCCAGCAGTACCCGGCAGCGCGA
CCGGCTGAGCCGCGGGGCCAGCAGGTCTTCCTCAAGCCGGACGAGCCGCCGCCGCCGCCG
CAGCCATGCGCCGACAGCCTGCAGGACGCCTTGCTGAGTCTGGGCTCTGTCATCGACATT
TCAGGCCTGCAACGTGCTGTCAAGGAGGCCCTGTCAGCTGTGCTCCCCCGAGTGGAAACT
GTCTACACCTACCTACTGGATGGTGAGTCCCAGCTGGTGTGTGAGGACCCCCCACATGAG
CTGCCCCAGGAGGGGAAAGTCCGGGAGGCTATCATCTCCCAGAAGCGGCTGGGCTGCAAT
GGGCTGGGCTTCTCAGACCTGCCAGGGAAGCCCTTGGCCAGGCTGGTGGCTCCACTGGCT
CCTGATACCCAAGTGCTGGTCATGCCGCTAGCGGACAAGGAGGCTGGGGCCGTGGCAGCT
GTCATCTTGGTGCACTGTGGCCAGCTGAGTGATAATGAGGAATGGAGCCTGCAGGCGGTG
GAGAAGCATACCCTGGTCGCCCTGCGGAGGGTGCAGGTCCTGCAGCAGCGCGGGCCCAGG
GAGGCTCCCCGAGCCGTCCAGAACCCCCCGGAGGGGACGGCGGAAGACCAGAAGGGCGGG
GCGGCGTACACCGACCGCGACCGCAAGATCCTCCAACTGTGCGGGGAACTCTACGACCTG
GATGCCTCTTCCCTGCAGCTCAAAGTGCTCCAATACCTGCAGCAGGAGACCCGGGCATCC
CGCTGCTGCCTCCTGCTGGTGTCGGAGGACAATCTCCAGCTTTCTTGCAAGGTCATCGGA
GACAAAGTGCTCGGGGAAGAGGTCAGCTTTCCCTTGACAGGATGCCTGGGCCAGGTGGTG
GAAGACAAGAAGTCCATCCAGCTGAAGGACCTCACCTCCGAGGATGTACAACAGCTGCAG
AGCATGTTGGGCTGTGAGCTGCAGGCCATGCTCTGTGTCCCTGTCATCAGCCGGGCCACT
GACCAGGTGGTGGCCTTGGCCTGCGCCTTCAACAAGCTAGAAGGAGACTTGTTCACCGAC
GAGGACGAGCATGTGATCCAGCACTGCTTCCACTACACCAGCACCGTGCTCACCAGCACC
CTGGCCTTCCAGAAGGAACAGAAACTCAAGTGTGAGTGCCAGGCTCTTCTCCAAGTGGCA
AAGAACCTCTTCACCCACCTGGATGACGTCTCTGTCCTGCTCCAGGAGATCATCACGGAG
GCCAGAAACCTCAGCAACGCAGAGATCTGCTCTGTGTTCCTGCTGGATCAGAATGAGCTG
GTGGCCAAGGTGTTCGACGGGGGCGTGGTGGATGATGAGAGCTATGAGATCCGCATCCCG
GCCGATCAGGGCATCGCGGGACACGTGGCGACCACGGGCCAGATCCTGAACATCCCTGAC
GCATATGCCCATCCGCTTTTCTACCGCGGCGTGGACGACAGCACCGGCTTCCGCACGCGC
AACATCCTCTGCTTCCCCATCAAGAACGAGAACCAGGAGGTCATCGGTGTGGCCGAGCTG
GTGAACAAGATCAATGGGCCATGGTTCAGCAAGTTCGACGAGGACCTGGCGACGGCCTTC
TCCATCTACTGCGGCATCAGCATCGCCCATTCTCTCCTATACAAAAAAGTGAATGAGGCT
CAGTATCGCAGCCACCTGGCCAATGAGATGATGATGTACCACATGAAGGTCTCCGACGAT
GAGTATACCAAACTTCTCCATGATGGGATCCAGCCTGTGGCTGCCATTGACTCCAATTTT
GCAAGTTTCACCTATACCCCTCGTTCCCTGCCCGAGGATGACACGTCCATGGCCATCCTG
AGCATGCTGCAGGACATGAATTTCATCAACAACTACAAAATTGACTGCCCGACCCTGGCC
CGGTTCTGTTTGATGGTGAAGAAGGGCTACCGGGATCCCCCCTACCACAACTGGATGCAC
GCCTTTTCTGTCTCCCACTTCTGCTACCTGCTCTACAAGAACCTGGAGCTCACCAACTAC
CTCGAGGACATCGAGATCTTTGCCTTGTTTATTTCCTGCATGTGTCATGACCTGGACCAC
AGAGGCACAAACAACTCTTTCCAGGTGGCCTCGAAATCTGTGCTGGCTGCGCTCTACAGC
TCTGAGGGCTCCGTCATGGAGAGGCACCACTTTGCTCAGGCCATCGCCATCCTCAACACC
CACGGCTGCAACATCTTTGATCATTTCTCCCGGAAGGACTATCAGCGCATGCTGGATCTG
ATGCGGGACATCATCTTGGCCACAGACCTGGCCCACCATCTCCGCATCTTCAAGGACCTC
CAGAAGATGGCTGAGGTGGGCTACGACCGAAACAACAAGCAGCACCACAGACTTCTCCTC
TGCCTCCTCATGACCTCCTGTGACCTCTCTGACCAGACCAAGGGCTGGAAGACTACGAGA
AAGATCGCGGAGCTGATCTACAAAGAATTCTTCTCCCAGGGAGACCTGGAGAAGGCCATG
GGCAACAGGCCGATGGAGATGATGGACCGGGAGAAGGCCTATATCCCTGAGCTGCAAATC
AGCTTCATGGAGCACATTGCAATGCCCATCTACAAGCTGTTGCAGGACCTGTTCCCCAAA
GCGGCAGAGCTGTACGAGCGCGTGGCCTCCAACCGTGAGCACTGGACCAAGGTGTCCCAC
AAGTTCACCATCCGCGGCCTCCCAAGTAACAACTCGCTGGACTTCCTGGATGAGGAGTAC
GAGGTGCCTGATCTGGATGGCACTAGGGCCCCCATCAATGGCTGCTGCAGCCTTGATGCT
GAGTGA
|
| Enzyme 17 GenBank Gene ID |
U67733  |
| Enzyme 17 GeneCard ID |
PDE2A  |
| Enzyme 17 GenAtlas ID |
PDE2A  |
| Enzyme 17 HGNC ID |
HGNC:8777  |
| Enzyme 17 Chromosome Location |
11 |
| Enzyme 17 Locus |
11q13.4 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Rosman GJ, Martins TJ, Sonnenburg WK, Beavo JA, Ferguson K, Loughney K: Isolation and characterization of human cDNAs encoding a cGMP-stimulated 3',5'-cyclic nucleotide phosphodiesterase. Gene. 1997 May 20;191(1):89-95. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
5902 |
| Enzyme 18 Name |
High-affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B |
| Enzyme 18 Synonyms |
- HSPDE8B
|
| Enzyme 18 Gene Name |
PDE8B |
| Enzyme 18 Protein Sequence |
>High-affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B
MGCAPSIHVSQSGVIYCRDSDESSSPRQTTSVSQGPAAPLPGLFVQTDAADAIPPSRASG
PPSVARVRRARTELGSGSSAGSAAPAATTSRGRRRHCCSSAEAETQTCYTSVKQVSSAEV
RIGPMRLTQDPIQVLLIFAKEDSQSDGFWWACDRAGYRCNIARTPESALECFLDKHHEII
VIDHRQTQNFDAEAVCRSIRATNPSEHTVILAVVSRVSDDHEEASVLPLLHAGFNRRFME
NSSIIACYNELIQIEHGEVRSQFKLRACNSVFTALDHCHEAIEITSDDHVIQYVNPAFER
MMGYHKGELLGKELADLPKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVK
ITPVIGQGGKIRHFVSLKKLCCTTDNNKQIHKIHRDSGDNSQTEPHSFRYKNRRKESIDV
KSISSRGSDAPSLQNRRYPSMARIHSMTIEAPITKVINIINAAQENSPVTVAEALDRVLE
ILRTTELYSPQLGTKDEDPHTSDLVGGLMTDGLRRLSGNEYVFTKNVHQSHSHLAMPITI
NDVPPCISQLLDNEESWDFNIFELEAITHKRPLVYLGLKVFSRFGVCEFLNCSETTLRAW
FQVIEANYHSSNAYHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHP
GRTNSFLCNAGSELAVLYNDTAVLESHHTALAFQLTVKDTKCNIFKNIDRNHYRTLRQAI
IDMVLATEMTKHFEHVNKFVNSINKPMAAEIEGSDCECNPAGKNFPENQILIKRMMIKCA
DVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPVVMPVFDRNTCSIPKSQISFIDYF
ITDMFDAWDAFAHLPALMQHLADNYKHWKTLDDLKCKSLRLPSDS
|
| Enzyme 18 Number of Residues |
885 |
| Enzyme 18 Molecular Weight |
98980 |
| Enzyme 18 Theoretical pI |
6.81 |
| Enzyme 18 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- DNA binding
- binding
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- nucleic acid binding
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
- signal transducer activity
- two-component response regulator activity
|
| Process |
- cell communication
- cellular process
- regulation of biological process
- regulation of cellular metabolism
- regulation of metabolism
- regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- regulation of physiological process
- regulation of transcription
- regulation of transcription, DNA-dependent
- signal transduction
- two-component signal transduction system (phosphorelay)
|
| Component |
| — |
|
| Enzyme 18 General Function |
Signal transduction mechanisms |
| Enzyme 18 Specific Function |
Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase has high affinity for cAMP and may be involved in specific signaling in the thyroid gland |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
32261241  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
O95263  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
PDE8B_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>2517 bp
ATGGGCTGCGCCCCCAGCATCCATGTCTCGCAGAGCGGCGTGATCTACTGCCGGGACTCG
GACGAGTCCAGCTCGCCCCGCCAGACCACCAGCGTGTCGCAGGGCCCGGCGGCACCCCTG
CCCGGCCTCTTCGTCCAGACCGACGCCGCCGACGCCATCCCCCCGAGCCGCGCGTCGGGA
CCCCCCAGCGTAGCCCGCGTCCGCAGGGCCCGCACCGAGCTGGGCAGCGGTAGCAGCGCG
GGTTCCGCAGCCCCCGCCGCGACCACCAGCAGGGGCCGGAGGCGCCACTGCTGCAGCAGC
GCCGAGGCCGAGACTCAGACCTGCTACACCAGCGTGAAGCAGGTGTCTTCTGCGGAGGTG
CGCATCGGGCCCATGAGACTGACGCAGGACCCTATTCAGGTTTTGCTGATCTTTGCAAAG
GAAGATAGTCAGAGCGATGGCTTCTGGTGGGCCTGCGACAGAGCTGGTTATAGATGCAAT
ATTGCTCGGACTCCAGAGTCAGCCCTTGAATGCTTTCTTGATAAGCATCATGAAATTATT
GTAATTGATCATAGACAAACTCAGAACTTCGATGCAGAAGCAGTGTGCAGGTCGATCCGG
GCCACAAATCCCTCCGAGCACACGGTGATCCTCGCAGTGGTTTCGCGAGTATCGGATGAC
CATGAAGAGGCGTCAGTCCTTCCTCTTCTCCACGCAGGCTTCAACAGGAGATTTATGGAG
AATAGCAGCATAATTGCTTGCTATAATGAACTGATTCAAATAGAACATGGGGAAGTTCGC
TCCCAGTTCAAATTACGGGCCTGTAATTCAGTGTTTACAGCATTAGATCACTGTCATGAA
GCCATAGAAATAACAAGCGATGACCACGTGATTCAGGAGTGGCAGGGGGTTTACTATGCC
AGACGGAAATCCGGGGACAGCATCCAACAGCACGTGAAGATCACCCCAGTGATTGGCCAA
GGAGGGAAAATTAGGCATTTTGTCTCGCTCAAGAAACTGTGTTGTACCACTGACAATAAT
AAGCAGATTCACAAGATTCATCGTGATTCAGGAGATAATTCTCAGACAGAGCCTCATTCA
TTCAGATATAAGAACAGGAGGAAAGAGTCCATTGACGTGAAATCGATATCATCTCGAGGC
AGTGATGCACCAAGCCTGCAGAATCGTCGCTATCCGTCCATGGCGAGGATCCACTCCATG
ACCATCGAGGCTCCCATCACAAAGGTTATAAATATAATCAATGCAGCCCAAGAAAACAGC
CCAGTCACAGTAGCGGAAGCCTTGGACAGAGTTCTAGAGATTTTACGGACCACAGAACTG
TACTCCCCTCAGCTGGGTACCAAAGATGAAGATCCCCACACCAGTGATCTTGTTGGAGGC
CTGATGACTGACGGCTTGAGAAGACTGTCAGGAAACGAGTATGTGTTTACTAAGAATGTG
CACCAGAGTCACAGTCACCTTGCAATGCCAATAACCATCAATGATGTTCCCCCTTGTATC
TCTCAATTACTTGATAATGAGGAGAGTTGGGACTTCAACATCTTTGAATTGGAAGCCATT
ACGCATAAAAGGCCATTGGTTTATCTGGGCTTAAAGGTCTTCTCTCGGTTTGGAGTATGT
GAGTTTTTAAACTGTTCTGAAACCACTCTTCGGGCCTGGTTCCAAGTGATCGAAGCCAAC
TACCACTCTTCCAATGCCTACCACAACTCCACCCATGCTGCCGACGTCCTGCACGCCACC
GCTTTCTTTCTTGGAAAGGAAAGAGTAAAGGGAAGCCTCGATCAGTTGGATGAGGTGGCA
GCCCTCATTGCTGCCACAGTCCATGACGTGGATCACCCGGGAAGGACCAACTCTTTCCTC
TGCAATGCAGGCAGTGAGCTTGCTGTGCTCTACAATGACACTGCTGTTCTGGAGAGTCAC
CACACCGCCCTGGCCTTCCAGCTCACGGTCAAGGACACCAAATGCAACATTTTCAAGAAT
ATTGACAGGAACCATTATCGAACGCTGCGCCAGGCTATTATTGACATGGTTTTGGCAACA
GAGATGACAAAACACTTTGAACATGTGAATAAGTTTGTGAACAGCATCAACAAGCCAATG
GCAGCTGAGATTGAAGGCAGCGACTGTGAATGCAACCCTGCTGGGAAGAACTTCCCTGAA
AACCAAATCCTGATCAAACGCATGATGATTAAGTGTGCTGACGTGGCCAACCCATGCCGC
CCCTTGGACCTGTGCATTGAATGGGCTGGGAGGATCTCTGAGGAGTATTTTGCACAGACT
GATGAAGAGAAGAGACAGGGACTACCTGTGGTGATGCCAGTGTTTGACCGGAATACCTGT
AGCATCCCCAAGTCTCAGATCTCTTTCATTGACTACTTCATAACAGACATGTTTGATGCT
TGGGATGCCTTTGCACATCTACCAGCCCTGATGCAACATTTGGCTGACAACTACAAACAC
TGGAAGACACTAGATGACCTAAAGTGCAAAAGTTTGAGGCTTCCATCTGACAGCTAA
|
| Enzyme 18 GenBank Gene ID |
AY129948  |
| Enzyme 18 GeneCard ID |
PDE8B  |
| Enzyme 18 GenAtlas ID |
PDE8B  |
| Enzyme 18 HGNC ID |
HGNC:8794  |
| Enzyme 18 Chromosome Location |
5 |
| Enzyme 18 Locus |
5q14.1 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Hayashi M, Shimada Y, Nishimura Y, Hama T, Tanaka T: Genomic organization, chromosomal localization, and alternative splicing of the human phosphodiesterase 8B gene. Biochem Biophys Res Commun. 2002 Oct 11;297(5):1253-8. [PubMed
]
- Gamanuma M, Yuasa K, Sasaki T, Sakurai N, Kotera J, Omori K: Comparison of enzymatic characterization and gene organization of cyclic nucleotide phosphodiesterase 8 family in humans. Cell Signal. 2003 Jun;15(6):565-74. [PubMed
]
- Hayashi M, Matsushima K, Ohashi H, Tsunoda H, Murase S, Kawarada Y, Tanaka T: Molecular cloning and characterization of human PDE8B, a novel thyroid-specific isozyme of 3',5'-cyclic nucleotide phosphodiesterase. Biochem Biophys Res Commun. 1998 Sep 29;250(3):751-6. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
5903 |
| Enzyme 19 Name |
cAMP-specific 3',5'-cyclic phosphodiesterase 4C |
| Enzyme 19 Synonyms |
- DPDE1
- PDE21
|
| Enzyme 19 Gene Name |
PDE4C |
| Enzyme 19 Protein Sequence |
>cAMP-specific 3',5'-cyclic phosphodiesterase 4C
MENLGVGEGAEACSRLSRSRGRHSMTRAPKHLWRQPRRPIRIQQRFYSDPDKSAGCRERD
LSPRPELRKSRLSWPVSSCRRFDLENGLSCGRRALDPQSSPGLGRIMQAPVPHSQRRESF
LYRSDSDYELSPKAMSRNSSVASDLHGEDMIVTPFAQVLASLRTVRSNVAALARQQCLGA
AKQGPVGNPSSSNQLPPAEDTGQKLALETLDELDWCLDQLETLQTRHSVGEMASNKFKRI
LNRELTHLSETSRSGNQVSEYISRTFLDQQTEVELPKVTAEEAPQPMSRISGLHGLCHSA
SLSSATVPRFGVQTDQEEQLAKELEDTNKWGLDVFKVAELSGNRPLTAIIFSIFQERDLL
KTFQIPADTLATYLLMLEGHYHANVAYHNSLHAADVAQSTHVLLATPALEAVFTDLEILA
ALFASAIHDVDHPGVSNQFLINTNSELALMYNDASVLENHHLAVGFKLLQAENCDIFQNL
SAKQRLSLRRMVIDMVLATDMSKHMNLLADLKTMVETKKVTSLGVLLLDNYSDRIQVLQN
LVHCADLSNPTKPLPLYRQWTDRIMAEFFQQGDRERESGLDISPMCDKHTASVEKSQVGF
IDYIAHPLWETWADLVHPDAQDLLDTLEDNREWYQSKIPRSPSDLTNPERDGPDRFQFEL
TLEEAEEEDEEEEEEGEETALAKEALELPDTELLSPEAGPDPGDLPLDNQRT
|
| Enzyme 19 Number of Residues |
712 |
| Enzyme 19 Molecular Weight |
79902 |
| Enzyme 19 Theoretical pI |
4.84 |
| Enzyme 19 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- cell communication
- cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 19 General Function |
Not Available |
| Enzyme 19 Specific Function |
Adenosine 3',5'-cyclic phosphate + H(2)O = adenosine 5'-phosphate |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
727223  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q08493  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
PDE4C_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>2139 bp
ATGGAGAACCTGGGGGTCGGCGAAGGGGCAGAGGCTTGCAGCAGGTTGAGTCGCTCTCGC
GGCCGCCACAGCATGACCAGAGCCCCGAAGCACCTGTGGCGGCAACCCCGGCGCCCCATC
CGCATCCAACAGCGCTTCTATTCGGATCCGGACAAGTCCGCGGGCTGCCGCGAGAGGGAC
CTGAGCCCGCGGCCGGAGCTCAGGAAGTCGCGGCTCTCCTGGCCCGTTTCCTCCTGCAGG
CGCTTTGACCTGGAAAATGGGCTCTCGTGTGGGAGGAGGGCCCTGGACCCTCAGTCCAGC
CCTGGCCTGGGCCGGATTATGCAGGCTCCAGTCCCGCACAGCCAGCGGCGCGAGTCCTTC
CTGTACCGCTCAGATAGCGACTATGAACTCTCGCCCAAGGCCATGTCTCGGAACTCCTCT
GTGGCCAGCGACCTACATGGAGAGGACATGATTGTGACGCCCTTTGCCCAGGTCCTGGCC
AGTCTGCGGACCGTTCGGAGCAACGTGGCGGCCCTTGCCCGCCAGCAATGCCTAGGAGCA
GCCAAGCAGGGACCCGTCGGAAACCCTTCATCCAGCAATCAGCTCCCTCCTGCAGAGGAC
ACGGGGCAGAAGCTGGCATTGGAGACGCTAGACGAGCTGGACTGGTGCCTGGATCAGTTG
GAGACGCTGCAGACCCGGCACTCGGTGGGGGAGATGGCCTCCAACAAGTTCAAGCGGATC
CTGAACCGGGAGTTGACCCACCTGTCCGAAACCAGCCGCTCCGGGAACCAGGTGTCCGAG
TACATCTCCCGGACCTTCCTGGACCAGCAGACCGAGGTGGAGCTGCCCAAGGTGACCGCT
GAGGAGGCCCCACAGCCCATGTCCCGGATCAGTGGCCTACATGGGCTCTGCCACAGTGCC
AGCCTCTCCTCAGCCACTGTCCCACGCTTTGGGGTCCAGACTGACCAGGAGGAGCAACTG
GCCAAGGAGCTAGAAGACACCAACAAGTGGGGACTTGATGTGTTCAAGGTGGCGGACGTA
AGTGGGAACCGGCCCCTCACAGCTATCATATTCAGCATTTTTCAGGAGCGGGACCTGCTG
AAGACATTCCAGATCCCAGCAGACACACTGGCCACCTACCTGCTGATGCTGGAGGGTCAC
TACCACGCCAATGTGGCCTACCACAACAGCCTACATGCCGCCGACGTGGCCCAGTCCACG
CATGTGCTGCTGGCTACGCCCGCCCTCGAGGCTGTGTTCACAGACTTGGAAATCCTGGCT
GCCCTCTTTGCAAGCGCCATCCACGACGTGGACCATCCTGGGGTCTCCAACCAGTTTCTG
ATTAACACCAACTCAGACGTGGCGCTTATGTACAACGACGCCTCGGTGCTGGAGAACCAT
CACCTGGCTGTGGGCTTCAAGCTGCTGCAGGCAGAGAACTGCGATATCTTCCAGAACCTC
AGCGCCAAGCAGCGACTGAGTCTGCGCAGGATGGTCATTGACATGGTGCTGGCCACAGAC
ATGTCCAAACACATGAACCTCCTGGCCGACCTCAAGACCATGGTGGAGACCAAGAAGGTG
ACAAGCCTCGGTGTCCTCCTCCTGGACAACTATTCCGACCGAATCCAGGTCTTGCAGAAC
CTGGTGCACTGTGCTGATCTGAGCAACCCCACCAAGCCGCTGCCCCTGTACCGCCAGTGG
ACGGACCGCATCATGGCCGAGTTCTTCCAGCAGGGAGACCGCGAGCGTGAGTCGGGCCTG
GACATCAGTCCCATGTGTGACAAGCATACGGCCTCAGTGGAGAAGTCCCAGGTGGGTTTC
ATTGACTACATTGCTCACCCACTGTGGGAGACTTGGGCTGACCTGGTCCACCCAGATGCA
CAGGACCTGCTGGACACGCTGGAGGACAATCGAGAGTGGTACCAGAGCAAGATCCCCCGA
AGTCCCTCAGACCTCACCAACCCCGAGCGGGACGGGCCTGACAGATTCCAGTTTGAACTG
ACTCTGGAGGAGGCAGAGGAAGAGGATGAGGAGGAAGAAGAGGAGGGGGAAGAGACAGCT
TTAGCCAAAGAGGCCTTGGAGTTGCCTGACACTGAACTCCTGTCCCCTGAAGCCGGCCCA
GACCCTGGGGACTTACCCCTCGACAACCAGAGGACTTAG
|
| Enzyme 19 GenBank Gene ID |
Z46632  |
| Enzyme 19 GeneCard ID |
PDE4C  |
| Enzyme 19 GenAtlas ID |
PDE4C  |
| Enzyme 19 HGNC ID |
HGNC:8782  |
| Enzyme 19 Chromosome Location |
Not Available |
| Enzyme 19 Locus |
Not Available |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Engels P, Sullivan M, Muller T, Lubbert H: Molecular cloning and functional expression in yeast of a human cAMP-specific phosphodiesterase subtype (PDE IV-C). FEBS Lett. 1995 Jan 30;358(3):305-10. [PubMed
]
- Sullivan M, Olsen AS, Houslay MD: Genomic organisation of the human cyclic AMP-specific phosphodiesterase PDE4C gene and its chromosomal localisation to 19p13.1, between RAB3A and JUND. Cell Signal. 1999 Oct;11(10):735-42. [PubMed
]
- Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
5908 |
| Enzyme 20 Name |
cAMP-specific 3',5'-cyclic phosphodiesterase 4D |
| Enzyme 20 Synonyms |
- DPDE3
- PDE43
|
| Enzyme 20 Gene Name |
PDE4D |
| Enzyme 20 Protein Sequence |
>cAMP-specific 3',5'-cyclic phosphodiesterase 4D
MEAEGSSAPARAGSGEGSDSAGGATLKAPKHLWRHEQHHQYPLRQPQFRLLHPHHHLPPP
PPPSPQPQPQCPLQPPPPPPLPPPPPPPGAARGRYASSGATGRVRHRGYSDTERYLYCRA
MDRTSYAVETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTSAGRSPLDPMTSPGSGLILQA
NFVHSQRRESFLYRSDSDYDLSPKSMSRNSSIASDIHGDDLIVTPFAQVLASLRTVRNNF
AALTNLQDRAPSKRSPMCNQPSINKATITEEAYQKLASETLEELDWCLDQLETLQTRHSV
SEMASNKFKRMLNRELTHLSEMSRSGNQVSEFISNTFLDKQHEVEIPSPTQKEKEKKKRP
MSQISGVKKLMHSSSLTNSSIPRFGVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPL
TVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLST
PALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGF
KLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVL
LLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMC
DKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQSPSPAP
DDPEEGRQGQTEKFQFELTLEEDGESDTEKDSGSQVEEDTSCSDSKTLCTQDSESTEIPL
DEQVEEEAVGEEEESQPEACVIDDRSPDT
|
| Enzyme 20 Number of Residues |
809 |
| Enzyme 20 Molecular Weight |
91116 |
| Enzyme 20 Theoretical pI |
5.25 |
| Enzyme 20 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- cell communication
- cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 20 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 20 Specific Function |
Regulates the levels of cAMP in the cell |
| Enzyme 20 Pathways |
|
| Enzyme 20 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
347130  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q08499  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
PDE4D_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>2024 bp
ACATGATGCACGTGAATAATTTTCCCTTTAGAAGGCATTCCTGGATATGTTTTGATGTGG
ACAATGGCACATCTGCGGGACGGAGTCCCTTGGATCCCATGACCAGCCCAGGATCCGGGC
TAATTCTCCAAGCAAATTTTGTCCACAGTCAACGACGGGAGTCCTTCCTGTATCGATCCG
ACAGCGATTATGACCTCTCTCCAAAGTCTATGTCCCGGAACTCCTCCATTGCCAGTGATA
TACACGGAGATGACTTGATTGTGACTCCATTTGCTCAGGTCTTGGCCAGTCTGCGAACTG
TACGAAACAACTTTGCTGCATTAACTAATTTGCAAGATCGAGCACCTAGCAAAAGATCAC
CCATGTGCAACCAACCATCCATCAACAAAGCCACCATAACAGAGGAGGCCTACCAGAAAC
TGGCCAGCGAGACCCTGGAGGAGCTGGACTGGTGTCTGGACCAGCTAGAGACCCTACAGA
CCAGGCACTCCGTCAGTGAGATGGCCTCCAACAAGTTTAAAAGGATGCTTAATCGGGAGC
TCACCCATCTCTCTGAAATGAGTCGGTCTGGAAATCAAGTGTCAGAGTTTATATCAAACA
CATTCTTAGATAAGCAACATGAAGTGGAAATTCCTTCTCCAACTCAGAAGGAAAAGGAGA
AAAAGAAAAGACCAATGTCTCAGATCAGTGGAGTCAAGAAATTGATGCACAGCTCTAGTC
TGACTAATTCAAGTATCCCAAGGTTTGGAGTTAAAACTGAACAAGAAGATGTCCTTGCCA
AGGAACTAGAAGATGTGAACAAATGGGGTCTTCATGTTTTCAGAATAGCAGAGTTGTCTG
GTAACCGGCCCTTGACTGTTATCATGCACACCATTTTTCAGGAACGGGATTTATTAAAAA
CATTTAAAATTCCAGTAGATACTTTAATTACATATCTTATGACTCTCGAAGACCATTACC
ATGCTGATGTGGCCTATCACAACAATATCCATGCTGCAGATGTTGTCCAGTCTACTCATG
TGCTATTATCTACACCTGCTTTGGAGGCTGTGTTTACAGATTTGGAGATTCTTGCAGCAA
TTTTTGCCAGTGCAATACATGATGTAGATCATCCTGGTGTGTCCAATCAATTTCTGATCA
ATACAAACTCTGAACTTGCCTTGATGTACAATGATTCCTCAGTCTTAGAGAACCATCATT
TGGCTGTGGGCTTTAAATTGCTTCAGGAAGAAAACTGTGACATTTTCCAGAATTTGACCA
AAAAACAAAGACAATCTTTAAGGAAAATGGTCATTGACATCGTACTTGCAACAGATATGT
CAAAACACATGAATCTACTGGCTGATTTGAAGACTATGGTTGAAACTAAGAAAGTGACAA
GCTCTGGAGTTCTTCTTCTTGATAATTATTCCGATAGGATTCAGGTTCTTCAGAATATGG
TGCACTGTGCAGATCTGAGCAACCCAACAAAGCCTCTCCAGCTGTACCGCCAGTGGACGG
ACCGGATAATGGAGGAGTTCTTCCGCCAAGGAGACCGAGAGAGGGAACGTGGCATGGAGA
TAAGCCCCATGTGTGACAAGCACAATGCTTCCGTGGAAAAATCACAGGTGGGCTTCATAG
ACTATATTGTTCATCCCCTCTGGGAGACATGGGCAGACCTCGTCCACCCTGACGCCCAGG
ATATTTTGGACACTTTGGAGGACAATCGTGAATGGTACCAGAGCACAATCCCTCAGAGCC
CCTCTCCTGCACCTGATGACCCAGAGGAGGGCCGGCAGGGTCAAACTGAGAAATTCCAGT
TTGAACTAACTTTAGAGGAAGATGGTGAGTCAGACACGGAAAAGGACAGTGGCAGTCAAG
TGGAAGAAGACACTAGCTGCAGTGACTCCAAGACTCTTTGTACTCAAGACTCAGAGTCTA
CTGAAATTCCCCTTGATGAACAGGTTGAAGAGGAGGCAGTAGGGGAAGAAGAGGAAAGCC
AGCCTGAAGCCTGTGTCATAGATGATCGTTCTCCTGACACGTAA
|
| Enzyme 20 GenBank Gene ID |
L20970  |
| Enzyme 20 GeneCard ID |
PDE4D  |
| Enzyme 20 GenAtlas ID |
PDE4D  |
| Enzyme 20 HGNC ID |
HGNC:8783  |
| Enzyme 20 Chromosome Location |
5 |
| Enzyme 20 Locus |
5q12 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed
]
- Nemoz G, Zhang R, Sette C, Conti M: Identification of cyclic AMP-phosphodiesterase variants from the PDE4D gene expressed in human peripheral mononuclear cells. FEBS Lett. 1996 Apr 8;384(1):97-102. [PubMed
]
- Baecker PA, Obernolte R, Bach C, Yee C, Shelton ER: Isolation of a cDNA encoding a human rolipram-sensitive cyclic AMP phosphodiesterase (PDE IVD). Gene. 1994 Jan 28;138(1-2):253-6. [PubMed
]
- Bolger GB, Erdogan S, Jones RE, Loughney K, Scotland G, Hoffmann R, Wilkinson I, Farrell C, Houslay MD: Characterization of five different proteins produced by alternatively spliced mRNAs from the human cAMP-specific phosphodiesterase PDE4D gene. Biochem J. 1997 Dec 1;328 ( Pt 2):539-48. [PubMed
]
- Miro X, Casacuberta JM, Gutierrez-Lopez MD, de Landazuri MO, Puigdomenech P: Phosphodiesterases 4D and 7A splice variants in the response of HUVEC cells to TNF-alpha(1). Biochem Biophys Res Commun. 2000 Aug 2;274(2):415-21. [PubMed
]
- Wang D, Deng C, Bugaj-Gaweda B, Kwan M, Gunwaldsen C, Leonard C, Xin X, Hu Y, Unterbeck A, De Vivo M: Cloning and characterization of novel PDE4D isoforms PDE4D6 and PDE4D7. Cell Signal. 2003 Sep;15(9):883-91. [PubMed
]
- Gretarsdottir S, Thorleifsson G, Reynisdottir ST, Manolescu A, Jonsdottir S, Jonsdottir T, Gudmundsdottir T, Bjarnadottir SM, Einarsson OB, Gudjonsdottir HM, Hawkins M, Gudmundsson G, Gudmundsdottir H, Andrason H, Gudmundsdottir AS, Sigurdardottir M, Chou TT, Nahmias J, Goss S, Sveinbjornsdottir S, Valdimarsson EM, Jakobsson F, Agnarsson U, Gudnason V, Thorgeirsson G, Fingerle J, Gurney M, Gudbjartsson D, Frigge ML, Kong A, Stefansson K, Gulcher JR: The gene encoding phosphodiesterase 4D confers risk of ischemic stroke. Nat Genet. 2003 Oct;35(2):131-8. Epub 2003 Sep 21. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
5909 |
| Enzyme 21 Name |
Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma |
| Enzyme 21 Synonyms |
- GMP-PDE gamma
|
| Enzyme 21 Gene Name |
PDE6G |
| Enzyme 21 Protein Sequence |
>Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
MNLEPPKAEFRSATRVAGGPVTPRKGPPKFKQRQTRQFKSKPPKKGVQGFGDDIPGMEGL
GTDITVICPWEAFNHLELHELAQYGII
|
| Enzyme 21 Number of Residues |
87 |
| Enzyme 21 Molecular Weight |
9643 |
| Enzyme 21 Theoretical pI |
10.16 |
| Enzyme 21 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- cGMP-specific phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 21 General Function |
Not Available |
| Enzyme 21 Specific Function |
Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
189703  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
P18545  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
CNRG_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>264 bp
ATGAACCTGGAACCGCCCAAGGCTGAGTTCCGGTCAGCCACCAGGGTGGCCGGGGGACCT
GTCACCCCCAGGAAAGGGCCCCCTAAATTTAAGCAGCGACAGACCAGGCAGTTCAAGAGC
AAGCCCCCAAAGAAAGGCGTTCAAGGGTTTGGGGACGACATCCCTGGAATGGAAGGCCTG
GGAACAGACATCACAGTCATCTGCCCTTGGGAGGCCTTCAACCACCTGGAGCTGCACGAG
CTGGCCCAATATGGCATCATCTAG
|
| Enzyme 21 GenBank Gene ID |
M36476  |
| Enzyme 21 GeneCard ID |
PDE6G  |
| Enzyme 21 GenAtlas ID |
PDE6G  |
| Enzyme 21 HGNC ID |
HGNC:8789  |
| Enzyme 21 Chromosome Location |
17 |
| Enzyme 21 Locus |
17q25 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Tuteja N, Danciger M, Klisak I, Tuteja R, Inana G, Mohandas T, Sparkes RS, Farber DB: Isolation and characterization of cDNA encoding the gamma-subunit of cGMP phosphodiesterase in human retina. Gene. 1990 Apr 16;88(2):227-32. [PubMed
]
- Piriev NI, Purishko VA, Khramtsov NV, Lipkin VM: [The organization of the gamma-subunit gene of human photoreceptor cyclic GMP phosphodiesterase] Dokl Akad Nauk SSSR. 1990;315(1):229-31. [PubMed
]
- Hahn LB, Berson EL, Dryja TP: Evaluation of the gene encoding the gamma subunit of rod phosphodiesterase in retinitis pigmentosa. Invest Ophthalmol Vis Sci. 1994 Mar;35(3):1077-82. [PubMed
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
5913 |
| Enzyme 22 Name |
Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta |
| Enzyme 22 Synonyms |
- GMP-PDE delta
- p17 protein
|
| Enzyme 22 Gene Name |
PDE6D |
| Enzyme 22 Protein Sequence |
>Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
MSAKDERAREILRGFKLNWMNLRDAETGKILWQGTEDLSVPGVEHEARVPKKILKCKAVS
RELNFSSTEQMEKFRLEQKVYFKGQCLEEWFFEFGFVIPNSTNTWQSLIEAAPESQMMPA
SVLTGNVIIETKFFDDDLLVSTSRVRLFYV
|
| Enzyme 22 Number of Residues |
150 |
| Enzyme 22 Molecular Weight |
17420 |
| Enzyme 22 Theoretical pI |
5.35 |
| Enzyme 22 GO Classification |
Not Available |
| Enzyme 22 General Function |
Not Available |
| Enzyme 22 Specific Function |
Guanosine 3',5'-cyclic phosphate + H(2)O = guanosine 5'-phosphate |
| Enzyme 22 Pathways |
|
| Enzyme 22 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
2896020  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
O43924  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
PDE6D_HUMAN  |
| Enzyme 22 PDB ID |
1KSG  |
| Enzyme 22 PDB File |
Show |
| Enzyme 22 3D Structure |
|
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>453 bp
ATGTCAGCCAAGGACGAGCGGGCCAGGGAGATCCTGAGGGGCTTCAAACTAAATTGGATG
AACCTTCGGGATGCTGAGACAGGGAAGATACTCTGGCAAGGAACAGAAGACCTGTCTGTC
CCTGGTGTGGAGCATGAAGCCCGTGTTCCCAAGAAAATCCTCAAGTGCAAGGCAGTGTCT
CGAGAACTTAATTTTTCTTCGACAGAACAAATGGAAAAATTCCGCCTGGAACAAAAAGTT
TACTTCAAAGGGCAATGCCTAGAAGAATGGTTCTTCGAGTTTGGCTTTGTGATCCCTAAC
TCCACAAATACCTGGCAGTCCTTGATAGAGGCAGCACCCGAGTCCCAGATGATGCCAGCA
AGCGTCTTAACTGGGAACGTTATCATAGAAACAAAGTTTTTTGACGACGATCTTCTTGTA
AGCACATCCAGAGTGAGACTTTTCTATGTTTGA
|
| Enzyme 22 GenBank Gene ID |
AF045999  |
| Enzyme 22 GeneCard ID |
PDE6D  |
| Enzyme 22 GenAtlas ID |
PDE6D  |
| Enzyme 22 HGNC ID |
HGNC:8788  |
| Enzyme 22 Chromosome Location |
2 |
| Enzyme 22 Locus |
2q35-q36 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Li N, Florio SK, Pettenati MJ, Rao PN, Beavo JA, Baehr W: Characterization of human and mouse rod cGMP phosphodiesterase delta subunit (PDE6D) and chromosomal localization of the human gene. Genomics. 1998 Apr 1;49(1):76-82. [PubMed
]
- Ershova G, Derre J, Chetelin S, Nancy V, Berger R, Kaplan J, Munnich A, de Gunzburg J: cDNA sequence, genomic organization and mapping of PDE6D, the human gene encoding the delta subunit of the cGMP phosphodiesterase of retinal rod cells to chromosome 2q36. Cytogenet Cell Genet. 1997;79(1-2):139-41. [PubMed
]
- Lorenz B, Migliaccio C, Lichtner P, Meyer C, Strom TM, D'Urso M, Becker J, Ciccodicola A, Meitinger T: Cloning and gene structure of the rod cGMP phosphodiesterase delta subunit gene (PDED) in man and mouse. Eur J Hum Genet. 1998 May-Jun;6(3):283-90. [PubMed
]
- Linari M, Hanzal-Bayer M, Becker J: The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta, interacts with the Arf-like protein Arl3 in a GTP specific manner. FEBS Lett. 1999 Sep 10;458(1):55-9. [PubMed
]
- Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC: The complex of Arl2-GTP and PDE delta: from structure to function. EMBO J. 2002 May 1;21(9):2095-106. [PubMed
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
5922 |
| Enzyme 23 Name |
cAMP-specific 3',5'-cyclic phosphodiesterase 4A |
| Enzyme 23 Synonyms |
- DPDE2
- PDE46
|
| Enzyme 23 Gene Name |
PDE4A |
| Enzyme 23 Protein Sequence |
>cAMP-specific 3',5'-cyclic phosphodiesterase 4A
MEPPTVPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYSDSAERAERERQ
PHRPIERADAMDTSDRPGLRTTRMSWPSSFHGTGTGSGGAGGGSSRRFEAENGPTPSPGR
SPLDSQASPGLVLHAGAATSQRRESFLYRSDSDYDMSPKTMSRNSSVTSEAHAEDLIVTP
FAQVLASLRSVRSNFSLLTNVPVPSNKRSPLGGPTPVCKATLSEETCQQLARETLEELDW
CLEQLETMQTYRSVSEMASHKFKRMLNRELTHLSEMSRSGNQVSEYISTTFLDKQNEVEI
PSPTMKEREKQQAPRPRPSQPPPPPVPHLQPMSQITGLKKLMHSNSLNNSNIPRFGVKTD
QEELLAQELENLNKWGLNIFCVSDYAGGRSLTCIMYMIFQERDLLKKFRIPVDTMVTYML
TLEDHYHADVAYHNSLHAADVLQSTHVLLATPALDAVFTDLEILAALFAAAIHDVDHPGV
SNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEDNCDIFQNLSKRQRQSLRKMVIDM
VLATDMSKHMTLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLRNMVHCADLSNPTKPLE
LYRQWTDRIMAEFFQQGDRERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADL
VHPDAQEILDTLEDNRDWYYSAIRQSPSPPPEEESRGPGHPPLPDKFQFELTLEEEEEEE
ISMAQIPCTAQEALTAQGLSGVEEALDATIAWEASPAQESLEVMAQEASLEAELEAVYLT
QQAQSTGSAPVAPDEFSSREEFVVAVSHSSPSALALQSPLLPAWRTLSVSEHAPGLPGLP
STAAEVEAQREHQAAKRACSACAGTFGEDTSALPAPGGGGSGGDPT
|
| Enzyme 23 Number of Residues |
886 |
| Enzyme 23 Molecular Weight |
98144 |
| Enzyme 23 Theoretical pI |
4.87 |
| Enzyme 23 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- cell communication
- cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 23 General Function |
Not Available |
| Enzyme 23 Specific Function |
Adenosine 3',5'-cyclic phosphate + H(2)O = adenosine 5'-phosphate |
| Enzyme 23 Pathways |
|
| Enzyme 23 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
347120  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
P27815  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
PDE4A_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>2661 bp
ATGGAACCCCCGACCGTCCCCTCGGAAAGGAGCCTGTCTCTGTCACTGCCCGGGCCCCGG
GAGGGCCAGGCCACCCTGAAGCCTCCCCCGCAGCACCTGTGGCGGCAGCCTCGGACCCCC
ATCCGTATCCAGCAGCGCGGCTACTCCGACAGCGCGGAGCGCGCCGAGCGGGAGCGGCAG
CCGCACCGGCCCATAGAGCGCGCCGATGCCATGGACACCAGCGACCGGCCCGGCCTGCGC
ACGACCCGCATGTCCTGGCCCTCGTCCTTCCATGGCACTGGCACCGGCAGCGGCGGCGCG
GGCGGAGGCAGCAGCAGGCGCTTCGAGGCAGAGAATGGGCCGACACCATCTCCTGGCCGC
AGCCCCCTGGACTCGCAGGCGAGCCCAGGACTCGTGCTGCACGCCGGGGCGGCCACCAGC
CAGCGCCGGGAGTCCTTCCTGTACCGCTCAGACAGCGACTATGACATGTCACCCAAGACC
ATGTCCCGGAACTCATCGGTCACCAGCGAGGCGCACGCTGAAGACCTCATCGTAACACCA
TTTGCTCAGGTGCTGGCCAGCCTCCGGAGCGTCCGTAGCAACTTCTCACTCCTGACCAAT
GTGCCCGTTCCCAGTAACAAGCGGTCCCCGCTGGGCGGCCCCACCCCTGTCTGCAAGGCC
ACGCTGTCAGAAGAAACGTGTCAGCAGTTGGCCCGGGAGACTCTGGAGGAGCTGGACTGG
TGTCTGGAGCAGCTGGAGACCATGCAGACCTATCGCTCTGTCAGCGAGATGGCCTCGCAC
AAGTTCAAAAGGATGTTGAACCGTGAGCTCACACACCTGTCAGAAATGAGCAGGTCCGGA
AACCAGGTCTCAGAGTACATTTCCACAACATTCCTGGACAAACAGAATGAAGTGGAGATC
CCATCACCCACGATGAAGGAACGAGAAAAACAGCAAGCGCCGCGACCAAGACCCTCCCAG
CCGCCCCCGCCCCCTGTACCACACTTACAGCCCATGTCCCAAATCACAGGGTTGAAAAAG
TTGATGCATAGTAACAGCCTGAACAACTCTAACATTCCCCGATTTGGGGTGAAGACCGAT
CAAGAAGAGCTCCTGGCCCAAGAACTGGAGAACCTGAACAAGTGGGGCCTGAACATCTTT
TGCGTGTCGGATTACGCTGGAGGCCGCTCACTCACCTGCATCATGTACATGATATTCCAG
GAGCGGGACCTGCTGAAGAAATTCCGCATCCCGGTGGACACGATGGTGACATACATGCTG
ACGCTGGAGGATCACTACCACGCTGACGTGGCCTACCATAACAGCCTGCACGCAGCTGAC
GTGCTGCAGTCCACCCACGTACTGCTGGCCACGCCTGCACTAGATGCAGTGTTCACGGAC
CTGGAGATTCTCGCCGCCCTCTTCGCGGCTGCCATCCACGATGTGGATCACCCTGGGGTC
TCCAACCAGTTCCTCATCAACACCAATTCGGAGCTGGCGCTCATGTACAACGATGAGTCG
GTGCTCGAGAATCACCACCTGGCCGTGGGCTTCAAGCTGCTGCAGGAGGACAACTGCGAC
ATCTTCCAGAACCTCAGCAAGCGCCAGCGGCAGAGCCTACGCAAGATGGTCATCGACATG
GTGCTGGCCACGGACATGTCCAAGCACATGACCCTCCTGGCTGACCTGAAGACCATGGTG
GAGACCAAGAAAGTGACCAGCTCAGGGGTCCTCCTGCTAGATAACTACTCCGACCGCATC
CAGGTCCTCCGGAACATGGTGCACTGTGCCGACCTCAGCAACCCCACCAAGCCGCTGGAG
CTGTACCGCCAGTGGACAGACCGCATCATGGCCGAGTTCTTCCAGCAGGGTGACCGAGAG
CGCGAGCGTGGCATGGAAATCAGCCCCATGTGTGACAAGCACACTGCCTCCGTGGAGAAG
TCTCAGGTGGGTTTTATTGACTACATTGTGCACCCATTGTGGGAGACCTGGGCGGACCTT
GTCCACCCAGATGCCCAGGAGATCTTGGACACTTTGGAGGACAACCGGGACTGGTACTAC
AGCGCCATCCGGCAGAGCCCATCTCCGCCACCCGAGGAGGAGTCAAGGGGGCCAGGCCAC
CCACCCCTGCCTGACAAGTTCCAGTTTGAGCTGACGCTGGAGGAGGAAGAGGAGGAAGAA
ATATCAATGGCCCAGATACCGTGCACAGCCCAAGAGGCATTGACTGCGCAGGGATTGTCA
GGAGTCGAGGAAGCTCTGGATGCAACCATAGCCTGGGAGGCATCCCCGGCCCAGGAGTCG
TTGGAAGTTATGGCACAGGAAGCATCCCTGGAGGCCGAGCTGGAGGCAGTGTATTTGACA
CAGCAGGCACAGTCCACAGGCAGTGCACCTGTGGCTCCGGATGAGTTCTCGTCCCGGGAG
GAATTCGTGGTTGCTGTAAGCCACAGCAGCCCCTCTGCCCTGGCTCTTCAAAGCCCCCTT
CTCCCTGCTTGGAGGACCCTGTCTGTTTCAGAGCATGCCCCGGGCCTCCCGGGCCTCCCC
TCCACGGCGGCCGAGGTGGAGGCCCAACGAGAGCACCAGGCTGCCAAGAGGGCTTGCAGT
GCCTGCGCAGGGACATTTGGGGAGGACACATCCGCACTCCCAGCTCCTGGTGGCGGGGGG
TCAGGTGGAGACCCTACCTGA
|
| Enzyme 23 GenBank Gene ID |
L20965  |
| Enzyme 23 GeneCard ID |
PDE4A  |
| Enzyme 23 GenAtlas ID |
PDE4A  |
| Enzyme 23 HGNC ID |
HGNC:8780  |
| Enzyme 23 Chromosome Location |
19 |
| Enzyme 23 Locus |
19p13.2 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed
]
- Sullivan M, Rena G, Begg F, Gordon L, Olsen AS, Houslay MD: Identification and characterization of the human homologue of the short PDE4A cAMP-specific phosphodiesterase RD1 (PDE4A1) by analysis of the human HSPDE4A gene locus located at chromosome 19p13.2. Biochem J. 1998 Aug 1;333 ( Pt 3):693-703. [PubMed
]
- Livi GP, Kmetz P, McHale MM, Cieslinski LB, Sathe GM, Taylor DP, Davis RL, Torphy TJ, Balcarek JM: Cloning and expression of cDNA for a human low-Km, rolipram-sensitive cyclic AMP phosphodiesterase. Mol Cell Biol. 1990 Jun;10(6):2678-86. [PubMed
]
- Horton YM, Sullivan M, Houslay MD: Molecular cloning of a novel splice variant of human type IVA (PDE-IVA) cyclic AMP phosphodiesterase and localization of the gene to the p13.2-q12 region of human chromosome 19 [corrected] Biochem J. 1995 Jun 1;308 ( Pt 2):683-91. [PubMed
]
- Sullivan M, Egerton M, Shakur Y, Marquardsen A, Houslay MD: Molecular cloning and expression, in both COS-1 cells and S. cerevisiae, of a human cytosolic type-IVA, cyclic AMP specific phosphodiesterase (hPDE-IVA-h6.1). Cell Signal. 1994 Sep;6(7):793-812. [PubMed
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
5927 |
| Enzyme 24 Name |
cGMP-specific 3',5'-cyclic phosphodiesterase |
| Enzyme 24 Synonyms |
- CGB-PDE
- cGMP-binding cGMP-specific phosphodiesterase
|
| Enzyme 24 Gene Name |
PDE5A |
| Enzyme 24 Protein Sequence |
>cGMP-specific 3',5'-cyclic phosphodiesterase
MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAE
RVHTIPVCKEGIRGHTESCSCPLQQSPRADNSVPGTPTRKISASEFDRPLRPIVVKDSEG
TVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLI
SADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPL
NIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDE
KDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIIS
FMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTME
PLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGK
VKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETREL
QSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWIL
SVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGV
NNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAI
LATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAE
LVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCF
PLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRN
|
| Enzyme 24 Number of Residues |
875 |
| Enzyme 24 Molecular Weight |
100014 |
| Enzyme 24 Theoretical pI |
6.00 |
| Enzyme 24 GO Classification |
| Function |
- 3',5'-cyclic-nucleotide phosphodiesterase activity
- catalytic activity
- cyclic-nucleotide phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- cell communication
- cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 24 General Function |
Not Available |
| Enzyme 24 Specific Function |
Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'- GMP |
| Enzyme 24 Pathways |
Not Available |
| Enzyme 24 Reactions |
- guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
3420185  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
O76074  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
PDE5A_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>2628 bp
ATGGAGCGGGCCGGCCCCAGCTTCGGGCAGCAGCGACAGCAGCAGCAGCCCCAGCAGCAG
AAGCAGCAGCAGAGGGATCAGGACTCGGTCGAAGCATGGCTGGACGATCACTGGGACTTT
ACCTTCTCATACTTTGTTAGAAAAGCCACCAGAGAAATGGTCAATGCATGGTTTGCTGAG
AGAGTTCACACCATCCCTGTGTGCAAGGAAGGTATCAGAGGCCACACCGAATCTTGCTCT
TGTCCCTTGCAGCAGAGTCCTCGTGCAGATAACAGTGTCCCTGGAACACCAACCAGGAAA
ATCTCTGCCTCTGAATTTGACCGGCCTCTTAGACCCATTGTTGTCAAGGATTCTGAGGGA
ACTGTGAGCTTCCTCTCTGACTCAGAAAAGAAGGAACAGATGCCTCTAACCCCTCCAAGG
TTTGATCATGATGAAGGGGACCAGTGCTCAAGACTCTTGGAATTAGTGAAGGATATTTCT
AGTCATTTGGATGTCACAGCCTTATGTCACAAAATTTTCTTGCATATCCATGGACTGATA
TCTGCTGACCGCTATTCCCTGTTCCTTGTCTGTGAAGACAGCTCCAATGACAAGTTTCTT
ATCAGCCGCCTCTTTGATGTTGCTGAAGGTTCAACACTGGAAGAAGTTTCAAATAACTGT
ATCCGCTTAGAATGGAACAAAGGCATTGTGGGACATGTGGCAGCGCTTGGTGAGCCCTTG
AACATCAAAGATGCATATGAGGATCCTCGGTTCAATGCAGAAGTTGACCAAATTACAGGC
TACAAGACACAAAGCATTCTTTGTATGCCAATTAAGAATCATAGGGAAGAGGTTGTTGGT
GTAGCCCAGGCCATCAACAAGAAATCAGGAAACGGTGGGACATTTACTGAAAAAGATGAA
AAGGACTTTGCTGCTTATTTGGCATTTTGTGGTATTGTTCTTCATAATGCTCAGCTCTAT
GAGACTTCACTGCTGGAGAACAAGAGAAATCAGGTGCTGCTTGACCTTGCTAGTTTAATT
TTTGAAGAACAACAATCATTAGAAGTAATTTTGAAGAAAATAGCTGCCACTATTATCTCT
TTCATGCAAGTGCAGAAATGCACCATTTTCATAGTGGATGAAGATTGCTCCGATTCTTTT
TCTAGTGTGTTTCACATGGAGTGTGAGGAATTAGAAAAATCATCTGATACATTAACAAGG
GAACATGATGCAAACAAAATCAATTACATGTATGCTCAGTATGTCAAAAATACTATGGAA
CCACTTAATATCCCAGATGTCAGTAAGGATAAAAGATTTCCCTGGACAACTGAAAATACA
GGAAATGTAAACCAGCAGTGCATTAGAAGTTTGCTTTGTACACCTATAAAAAATGGAAAG
AAGAATAAAGTTATAGGGGTTTGCCAACTTGTTAATAAGATGGAGGAGAATACTGGCAAG
GTTAAGCCTTTCAACCGAAATGACGAACAGTTTCTGGAAGCTTTTGTCATCTTTTGTGGC
TTGGGGATCCAGAACACGCAGATGTATGAAGCAGTGGAGAGAGCCATGGCCAAGCAAATG
GTCACATTGGAGGTTCTGTCGTATCATGCTTCAGCAGCAGAGGAAGAAACAAGAGAGCTA
CAGTCGTTAGCGGCTGCTGTGGTGCCATCTGCCCAGACCCTTAAAATTACTGACTTTAGC
TTCAGTGACTTTGAGCTGTCTGATCTGGAAACAGCACTGTGTACAATTCGGATGTTTACT
GACCTCAACCTTGTGCAGAACTTCCAGATGAAACATGAGGTTCTTTGCAGATGGATTTTA
AGTGTTAAGAAGAATTATCGGAAGAATGTTGCCTATCATAATTGGAGACATGCCTTTAAT
ACAGCTCAGTGCATGTTTGCTGCTCTAAAAGCAGGCAAAATTCAGAACAAGCTGACTGAC
CTGGAGATACTTGCATTGCTGATTGCTGCACTAAGCCACGATTTGGATCACCGTGGTGTG
AATAACTCTTACATACAGCGAAGTGAACATCCACTTGCCCAGCTTTACTGCCATTCAATC
ATGGAACACCATCATTTTGACCAGTGCCTGATGATTCTTAATAGTCCAGGCAATCAGATT
CTCAGTGGCCTCTCCATTGAAGAATATAAGACCACGTTGAAAATAATCAAGCAAGCTATT
TTAGCTACAGACCTAGCACTGTACATTAAGAGGCGAGGAGAATTTTTTGAACTTATAAGA
AAAAATCAATTCAATTTGGAAGATCCTCATCAAAAGGAGTTGTTTTTGGCAATGCTGATG
ACAGCTTGTGATCTTTCTGCAATTACAAAACCCTGGCCTATTCAACAACGGATAGCAGAA
CTTGTAGCAACTGAATTTTTTGATCAAGGAGACAGAGAGAGAAAAGAACTCAACATAGAA
CCCACTGATCTAATGAACAGGGAGAAGAAAAACAAAATCCCAAGTATGCAAGTTGGGTTC
ATAGATGCCATCTGCTTGCAACTGTATGAGGCCCTGACCCACGTGTCAGAGGACTGTTTC
CCTTTGCTAGATGGCTGCAGAAAGAACAGGCAGAAATGGCAGGCCCTTGCAGAACAGCAG
GAGAAGATGCTGATTAATGGGGAAAGCGGCCAGGCCAAGCGGAACTGA
|
| Enzyme 24 GenBank Gene ID |
AF043731  |
| Enzyme 24 GeneCard ID |
PDE5A  |
| Enzyme 24 GenAtlas ID |
PDE5A  |
| Enzyme 24 HGNC ID |
HGNC:8784  |
| Enzyme 24 Chromosome Location |
4 |
| Enzyme 24 Locus |
4q25-q27 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Loughney K, Hill TR, Florio VA, Uher L, Rosman GJ, Wolda SL, Jones BA, Howard ML, McAllister-Lucas LM, Sonnenburg WK, Francis SH, Corbin JD, Beavo JA, Ferguson K: Isolation and characterization of cDNAs encoding PDE5A, a human cGMP-binding, cGMP-specific 3',5'-cyclic nucleotide phosphodiesterase. Gene. 1998 Aug 17;216(1):139-47. [PubMed
]
- Yanaka N, Kotera J, Ohtsuka A, Akatsuka H, Imai Y, Michibata H, Fujishige K, Kawai E, Takebayashi S, Okumura K, Omori K: Expression, structure and chromosomal localization of the human cGMP-binding cGMP-specific phosphodiesterase PDE5A gene. Eur J Biochem. 1998 Jul 15;255(2):391-9. [PubMed
]
- Stacey P, Rulten S, Dapling A, Phillips SC: Molecular cloning and expression of human cGMP-binding cGMP-specific phosphodiesterase (PDE5). Biochem Biophys Res Commun. 1998 Jun 18;247(2):249-54. [PubMed
]
- Zhou L, Thompson WJ, Potter DE: Multiple cyclic nucleotide phosphodiesterases in human trabecular meshwork cells. Invest Ophthalmol Vis Sci. 1999 Jul;40(8):1745-52. [PubMed
]
- Sung BJ, Hwang KY, Jeon YH, Lee JI, Heo YS, Kim JH, Moon J, Yoon JM, Hyun YL, Kim E, Eum SJ, Park SY, Lee JO, Lee TG, Ro S, Cho JM: Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules. Nature. 2003 Sep 4;425(6953):98-102. [PubMed
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
5977 |
| Enzyme 25 Name |
Adenylate cyclase type 7 |
| Enzyme 25 Synonyms |
- Adenylate cyclase type VII
- ATP pyrophosphate-lyase 7
- Adenylyl cyclase 7
|
| Enzyme 25 Gene Name |
ADCY7 |
| Enzyme 25 Protein Sequence |
>Adenylate cyclase type 7
MPAKGRYFLNEGEEGPDQDALYEKYQLTSQHGPLLLTLLLVAATACVALIIIAFSQGDPS
RHQAILGMAFLVLAVFAALSVLMYVECLLRRWLRALALLTWACLVALGYVLVFDAWTKAA
CAWEQVPFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVLGSLMGGFTTPSVRVGLQL
LANAVIFLCGNLTGAFHKHQMQDASRDLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAH
ISMGMKLAIIERLKEHGDRRCMPDNNFHSLYVKRHQNVSILYADIVGFTQLASDCSPKEL
VVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQAIKQ
VREATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEAT
LKHLDKAYEVEDGHGQQRDPYLKEMNIRTYLVIDPRSQQPPPPSQHLPRPKGDAALKMRA
SVRMTRYLESWGAARPFAHLNHRESVSSGETHVPNGRRPKSVPQRHRRTPDRSMSPKGRS
EDDSYDDEMLSAIEGLSSTRPCCSKSDDFYTFGSIFLEKGFEREYRLAPIPRARHDFACA
SLIFVCILLVHVLLMPRTAALGVSFGLVACVLGLVLGLCFATKFSRCCPARGTLCTISER
VETQPLLRLTLAVLTIGSLLTVAIINLPLMPFQVPELPVGNETGLLAASSKTRALCEPLP
YYTCSCVLGFIACSVFLRMSLEPKVVLLTVALVAYLVLFNLSPCWQWDCCGQGLGNLTKP
NGTTSGTPSCSWKDLKTMTNFYLVLFYITLLTLSRQIDYYCRLDCLWKKKFKKEHEEFET
MENVNRLLLENVLPAHVAAHFIGDKLNEDWYHQSYDCVCVMFASVPDFKVFYTECDVNKE
GLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSVASGHENQELERQHAH
IGVMVEFSIALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVAS
RMESTGELGKIQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFVCTDTAKFQGLGLN
|
| Enzyme 25 Number of Residues |
1080 |
| Enzyme 25 Molecular Weight |
120310 |
| Enzyme 25 Theoretical pI |
8.16 |
| Enzyme 25 GO Classification |
| Function |
- adenylate cyclase activity
- catalytic activity
- cyclase activity
- lyase activity
- phosphorus-oxygen lyase activity
|
| Process |
- cell communication
- cellular metabolism
- cellular process
- cyclic nucleotide biosynthesis
- intracellular signaling cascade
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide biosynthesis
- nucleotide metabolism
- physiological process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 25 General Function |
Signal transduction mechanisms |
| Enzyme 25 Specific Function |
This is a membrane-bound, calcium-inhibitable adenylyl cyclase |
| Enzyme 25 Pathways |
|
| Enzyme 25 Reactions |
- ATP = 3',5'-cyclic AMP + diphosphate
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
- 34-54
63-83
95-117
122-142
147-167
176-196
595-615
620-640
669-688
718-737
746-773
794-814
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
40788941  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
P51828  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
ADCY7_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>3267 bp
CGACACGCGTGCCAAGGGTGGAGGATGCCAGCCAAGGGGCGCTACTTCCTCAACGAGGGC
GAGGAGGGCCCTGACCAAGATGCGCTCTACGAGAAGTACCAGCTCACCAGCCAGCATGGG
CCGCTGCTGCTCACGCTCCTGCTGGTGGCCGCCACTGCCTGCGTGGCCCTCATCATCATT
GCCTTCAGCCAGGGGGACCCCTCCAGACACCAGGCCATTCTGGGCATGGCGTTCCTGGTG
CTGGCGGTGTTTGCGGCCCTCTCTGTGCTGATGTACGTCGAGTGTCTCCTGCGGCGCTGG
CTCAGGGCCTTGGCGCTGCTCACCTGGGCCTGCTTGGTGGCGCTGGGCTATGTGCTGGTG
TTCGACGCATGGACAAAGGCGGCCTGTGCGTGGGAGCAGGTGCCCTTCTTCCTGTTCATT
GTCTTCGTGGTGTACACACTACTGCCCTTCAGCATGCGGGGCGCTGTCGCCGTTGGGGCC
GTCTCCACTGCCTCCCACCTCCTGGTGCTCGGTTCTTTGATGGGAGGCTTCACGACACCC
AGTGTCCGGGTGGGGCTGCAGCTGCTGGCCAACGCAGTCATCTTCCTGTGTGGGAACCTG
ACAGGCGCCTTCCACAAGCACCAAATGCAGGATGCGTCCCGGGACCTCTTCACCTACACT
GTGAAGTGCATCCAGATCCGCCGGAAGCTGCGCATCGAGAAGCGCCAGCAGGAGAACCTG
CTGCTGTCAGTGCTTCCGGCCCACATCTCCATGGGCATGAAGCTGGCCATCATCGAACGG
CTCAAGGAGCATGGTGACCGTCGCTGCATGCCTGACAACAACTTCCACAGCCTCTACGTC
AAGAGGCACCAGAATGTCAGCATCCTCTATGCGGACATCGTGGGCTTCACGCAGCTGGCC
AGCGACTGTTCTCCCAAGGAGCTGGTGGTGGTGCTGAATGAGCTCTTTGGCAAGTTCGAC
CAGATCGCCAAGGCCAACGAGTGCATGCGAATCAAGATCCTCGGCGACTGCTACTACTGT
GTATCGGGCCTGCCCGTGTCGCTGCCTACCCACGCCCGGAACTGCGTGAAGATGGGGCTG
GACATGTGCCAGGCCATCAAGCAGGTGCGGGAGGCCACGGGCGTGGACATCAACATGCGT
GTGGGCATACACTCGGGGAATGTGCTGTGCGGGGTCATCGGGCTGCGCAAGTGGCAGTAT
GACGTGTGGTCCCACGACGTGTCCCTGGCCAACCGGATGGAGGCAGCCGGAGTACCCGGC
CGGGTGCACATCACGGAGGCCACGCTAAAGCACCTGGACAAGGCGTACGAGGTGGAGGAT
GGGCACGGGCAGCAGCGGGACCCCTACCTCAAGGAGATGAACATCCGCACCTACCTGGTC
ATCGACCCCCGGAGCCAGCAGCCACCCCCGCCCAGCCAACACCTCCCCAGGCCCAAGGGG
GACGCGGCCCTGAAGATGCGGGCGTCAGTGCGCATGACCCGGTACCTCGAGTCCTGGGGG
GCGGCACGGCCCTTTGCACATCTCAACCACCGTGAGAGCGTGAGCAGTGGTGAGACCCAC
GTCCCCAACGGGCGGAGGCCTAAGAGCGTTCCCCAGCGCCACCGCCGGACCCCAGACAGA
AGCATGTCCCCCAAGGGGCGGTCGGAGGATGACTCGTACGATGACGAGATGCTGTCAGCC
ATTGAGGGGCTCAGCTCCACGAGGCCCTGCTGCTCCAAGTCCGATGACTTCTACACCTTT
GGGTCCATCTTCCTGGAGAAGGGCTTTGAGCGCGAGTACCGCCTGGCACCCATCCCCCGG
GCCCGCCACGACTTTGCCTGCGCCAGCCTGATCTTCGTCTGCATCCTGCTCGTCCATGTC
CTGCTCATGCCCAGGACGGCGGCACTGGGTGTGTCCTTCGGGCTGGTGGCCTGTGTACTG
GGGCTGGTGCTGGGCCTGTGCTTTGCCACCAAGTTCTCGAGGTGCTGCCCAGCTCGGGGG
ACGCTCTGCACTATCTCTGAGAGGGTGGAGACACAGCCCCTGCTGAGGCTGACCCTGGCC
GTCCTGACCATCGGCAGCCTGCTCACTGTGGCCATCATCAACCTGCCCCTGATGCCTTTC
CAAGTTCCAGAGCTGCCTGTTGGCAATGAGACAGGCCTACTGGCCGCGAGCAGCAAGACA
AGAGCCCTGTGTGAGCCCCTCCCGTACTACACCTGCAGCTGTGTCCTGGGCTTCATCGCC
TGCTCGGTCTTCCTGAGGATGAGCCTGGAGCCAAAGGTTGTGCTGCTGACAGTGGCCCTG
GTGGCCTACCTGGTGCTCTTCAACCTCTCCCCATGCTGGCAGTGGGACTGCTGCGGCCAA
GGCCTGGGCAACCTCACCAAGCCCAACGGCACCACCAGTGGCACCCCTAGCTGTTCCTGG
AAGGACCTGAAGACCATGACCAATTTCTACCTGGTCCTGTTCTACATCACCCTGCTTACA
CTCTCCAGACAGATTGACTATTACTGCCGCTTGGACTGCCTATGGAAGAAGAAGTTCAAG
AAGGAGCACGAGGAGTTTGAGACCATGGAGAACGTGAACCGCCTTCTTCTGGAGAACGTC
CTGCCAGCCCACGTGGCTGCCCACTTTATCGGTGACAAGTTAAACGAGGACTGGTACCAT
CAGTCCTATGACTGCGTCTGTGTCATGTTTGCCTCCGTGCCGGACTTCAAAGTGTTCTAC
ACAGAGTGCGATGTCAACAAAGAAGGGCTGGAGTGCCTACGCCTGCTCAATGAGATCATT
GCCGACTTCGACGAGCTCCTACTGAAGCCCAAGTTCAGCGGCGTGGAGAAGATCAAGACC
ATCGGCAGCACGTACATGGCAGCTGCAGGGCTCAGCGTCGCCTCAGGGCACGAGAACCAG
GAGCTGGAGCGGCAGCATGCCCACATTGGTGTCATGGTGGAGTTCAGCATCGCCCTGATG
AGTAAGCTGGACGGCATCAACAGGCACTCCTTCAACTCCTTCCGCCTCCGCGTCGGCATA
AACCATGGGCCTGTGATTGCTGGAGTGATTGGGGCCCGAAAACCTCAGTATGACATCTGG
GGAAACACTGTCAATGTGGCCAGCCGAATGGAAAGCACTGGAGAACTTGGGAAAATCCAG
GTTACCGAGGAGACCTGCACCATCCTCCAGGGCCTCGGGTACTCTTGTGAATGCCGTGGC
CTGATCAACGTCAAAGGCAAAGGCGAGCTGAGGACTTACTTTGTCTGTACGGACACTGCC
AAGTTTCAGGGGCTGGGGCTGAACTGA
|
| Enzyme 25 GenBank Gene ID |
D25538  |
| Enzyme 25 GeneCard ID |
ADCY7  |
| Enzyme 25 GenAtlas ID |
ADCY7  |
| Enzyme 25 HGNC ID |
HGNC:238  |
| Enzyme 25 Chromosome Location |
16 |
| Enzyme 25 Locus |
16q12-q13 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
5979 |
| Enzyme 26 Name |
Adenylate cyclase type 6 |
| Enzyme 26 Synonyms |
- Adenylate cyclase type VI
- ATP pyrophosphate-lyase 6
- Adenylyl cyclase 6
- Ca(2+-inhibitable adenylyl cyclase
|
| Enzyme 26 Gene Name |
ADCY6 |
| Enzyme 26 Protein Sequence |
>Adenylate cyclase type 6
MSWFSGLLVPKVDERKTAWGERNGQKRSRRRGTRAGGFCTPRYMSCLRDAEPPSPTPAGP
PRCPWQDDAFIRRGGPGKGKELGLRAVALGFEDTEVTTTAGGTAEVAPDAVPRSGRSCWR
RLVQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLTAVLLAFHAAPARPQPAY
VALLACAAALFVGLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAADPRSPSAGLW
CPVFFVYIAYTLLPIRMRAAVLSGLGLSTLHLILAWQLNRGDAFLWKQLGANVLLFLCTN
VIGICTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINT
KKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHC
LRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRV
HCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNGDYEVEPGRGGERNA
YLKEQHIETFLILGASQKRKEEKAMLAKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFR
QMGIDDSSKDNRGTQDALNPEDEVDEFLSRAIDARSIDQLRKDHVRRFLLTFQREDLEKK
YSRKVDPRFGAYVACALLVFCFICFIQLLIFPHSTLMLGIYASIFLLLLITVLICAVYSC
GSLFPKALQRLSRSIVRSRAHSTAVGIFSVLLVFTSAIANMFTCNHTPIRSCAARMLNLT
PADITACHLQQLNYSLGLDAPLCEGTMPTCSFPEYFIGNMLLSLLASSVFLHISSIGKLA
MIFVLGLIYLVLLLLGPPATIFDNYDLLLGVHGLASSNETFDGLDCPAAGRVALKYMTPV
ILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHF
LARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIIS
EERFRQLEKIKTIGSTYMAASGLNASTYDQVGRSHITALADYAMRLMEQMKHINEHSFNN
FQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKG
YQLECRGVVKVKGKGEMTTYFLNGGPSS
|
| Enzyme 26 Number of Residues |
1168 |
| Enzyme 26 Molecular Weight |
130617 |
| Enzyme 26 Theoretical pI |
8.27 |
| Enzyme 26 GO Classification |
| Function |
- adenylate cyclase activity
- catalytic activity
- cyclase activity
- lyase activity
- phosphorus-oxygen lyase activity
|
| Process |
- cell communication
- cellular metabolism
- cellular process
- cyclic nucleotide biosynthesis
- intracellular signaling cascade
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide biosynthesis
- nucleotide metabolism
- physiological process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 26 General Function |
Signal transduction mechanisms |
| Enzyme 26 Specific Function |
Membrane-bound, calcium-inhibitable adenylyl cyclase |
| Enzyme 26 Pathways |
|
| Enzyme 26 Reactions |
- ATP = 3',5'-cyclic AMP + diphosphate
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
- 152-168
181-197
214-230
239-255
259-275
289-305
674-691
702-718
743-759
820-836
839-855
897-913
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
9049783  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
O43306  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
ADCY6_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>3507 bp
ATGTCATGGTTTAGTGGCCTCCTGGTCCCTAAAGTGGATGAACGGAAAACAGCCTGGGGC
GAACGCAATGGGCAGAAGCGTTCGCGGCGCCGTGGCACTCGGGCAGGTGGCTTCTGCACG
CCCCGCTATATGAGCTGCCTCCGGGATGCAGAGCCACCCAGCCCCACCCCTGCCGGCCCC
CCTCGGTGCCCCTGGCAGGATGACGCCTTCATCCGGAGGGGCGGCCCAGGCAAGGGCAAG
GAGCTGGGGCTGCGGGCAGTGGCCCTGGGCTTCGAGGATACCGAGGTGACAACGACAGCG
GGCGGGACGGCTGAGGTGGCGCCCGACGCGGTGCCCAGGAGTGGGCGATCCTGCTGGCGC
CGTCTGGTGCAGGTGTTCCAGTCGAAGCAGTTCCGTTCGGCCAAGCTGGAGCGCCTGTAC
CAGCGGTACTTCTTCCAGATGAACCAGAGCAGCCTGACGCTGCTGATGGCGGTGCTGGTG
CTGCTCACAGCGGTGCTGCTGGCTTTCCACGCCGCACCCGCCCGCCCTCAGCCTGCCTAT
GTGGCACTGTTGGCCTGTGCCGCCGCCCTGTTCGTGGGGCTCATGGTGGTGTGTAACCGG
CATAGCTTCCGCCAGGACTCCATGTGGGTGGTGAGCTACGTGGTGCTGGGCATCCTGGCG
GCAGTGCAGGTCGGGGGCGCTCTCGCAGCAGACCCGCGCAGCCCCTCTGCGGGCCTCTGG
TGCCCTGTGTTCTTTGTCTACATCGCCTACACGCTCCTCCCCATCCGCATGCGGGCTGCC
GTCCTCAGCGGCCTGGGCCTCTCCACCTTGCATTTGATCTTGGCCTGGCAACTTAACCGT
GGTGATGCCTTCCTCTGGAAGCAGCTCGGTGCCAATGTGCTGCTGTTCCTCTGCACCAAC
GTCATTGGCATCTGCACACACTATCCAGCAGAGGTGTCTCAGCGCCAGGCCTTTCAGGAG
ACCCGCGGTTACATCCAGGCCCGGCTCCACCTGCAGCATGAGAATCGGCAGCAGGAGCGG
CTGCTGCTGTCGGTATTGCCCCAGCACGTTGCCATGGAGATGAAAGAAGACATCAACACA
AAAAAAGAAGACATGATGTTCCACAAGATCTACATACAGAAGCATGACAATGTCAGCATC
CTGTTTGCAGACATTGAGGGCTTCACCAGCCTGGCATCCCAGTGCACTGCGCAGGAGCTG
GTCATGACCCTGAATGAGCTCTTTGCCCGGTTTGACAAGCTGGCTGCGGAGAATCACTGC
CTGAGGATCAAGATCTTGGGGGACTGTTACTACTGTGTGTCAGGGCTGCCGGAGGCCCGG
GCCGACCATGCCCACTGCTGTGTGGAGATGGGGGTAGACATGATTGAGGCCATCTCGCTG
GTACGTGAGGTGACAGGTGTGAATGTGAACATGCGCGTGGGCATCCACAGCGGGCGCGTG
CACTGCGGCGTCCTTGGCTTGCGGAAATGGCAGTTCGATGTGTGGTCCAATGATGTGACC
CTGGCCAACCACATGGAGGCAGGAGGCCGGGCTGGCCGCATCCACATCACTCGGGCAACA
CTGCAGTACCTGAACGGGGACTACGAGGTGGAGCCAGGCCGTGGTGGCGAGCGCAACGCG
TACCTCAAGGAGCAGCACATTGAGACTTTCCTCATCCTGGGCGCCAGCCAGAAACGGAAA
GAGGAGAAGGCCATGCTGGCCAAGCTGCAGCGGACTCGGGCCAACTCCATGGAAGGGCTG
ATGCCGCGCTGGGTTCCTGATCGTGCCTTCTCCCGGACCAAGGACTCCAAGGCCTTCCGC
CAGATGGGCATTGATGATTCCAGCAAAGACAACCGGGGCACCCAAGATGCCCTGAACCCT
GAGGATGAGGTGGATGAGTTCCTGAGCCGTGCCATCGATGCCCGCAGCATTGATCAGCTG
CGGAAGGACCATGTGCGCCGGTTTCTGCTCACCTTCCAGAGAGAGGATCTTGAGAAGAAG
TACTCCCGGAAGGTGGATCCCCGCTTCGGAGCCTACGTTGCCTGTGCCCTGTTGGTCTTC
TGCTTCATCTGCTTCATCCAGCTTCTCATCTTCCCACACTCCACCCTGATGCTTGGGATC
TATGCCAGCATCTTCCTGCTGCTGCTAATCACCGTGCTGATCTGTGCTGTGTACTCCTGT
GGTTCTCTGTTCCCTAAGGCCCTGCAACGTCTGTCCCGCAGCATTGTCCGCTCACGGGCA
CATAGCACCGCAGTTGGCATCTTTTCCGTCCTGCTTGTGTTTACTTCTGCCATTGCCAAC
ATGTTCACCTGTAACCACACCCCCATACGGAGCTGTGCAGCCCGGATGCTGAATTTAACA
CCTGCTGACATCACTGCCTGCCACCTGCAGCAGCTCAATTACTCTCTGGGCCTGGATGCT
CCCCTGTGTGAGGGCACCATGCCCACCTGCAGCTTTCCTGAGTACTTCATCGGGAACATG
CTGCTGAGTCTCTTGGCCAGCTCTGTCTTCCTGCACATCAGCAGCATCGGGAAGTTGGCC
ATGATCTTTGTCTTGGGGCTCATCTATTTGGTGCTGCTTCTGCTGGGTCCCCCAGCCACC
ATCTTTGACAACTATGACCTACTGCTTGGCGTCCATGGCTTGGCTTCTTCCAATGAGACC
TTTGATGGGCTGGACTGTCCAGCTGCAGGGAGGGTGGCCCTCAAATATATGACCCCTGTG
ATTCTGCTGGTGTTTGCGCTGGCGCTGTATCTGCATGCTCAGCAGGTGGAGTCGACTGCC
CGCCTAGACTTCCTCTGGAAACTACAGGCAACAGGGGAGAAGGAGGAGATGGAGGAGCTA
CAGGCATACAACCGGAGGCTGCTGCATAACATTCTGCCCAAGGACGTGGCGGCCCACTTC
CTGGCCCGGGAGCGCCGCAATGATGAACTCTACTATCAGTCGTGTGAGTGTGTGGCTGTT
ATGTTTGCCTCCATTGCCAACTTCTCTGAGTTCTATGTGGAGCTGGAGGCAAACAATGAG
GGTGTCGAGTGCCTGCGGCTGCTCAACGAGATCATCGCTGACTTTGATGAGATTATCAGC
GAGGAGCGGTTCCGGCAGCTGGAAAAGATCAAGACGATTGGTAGCACCTACATGGCTGCC
TCAGGGCTGAACGCCAGCACCTACGATCAGGTGGGCCGCTCCCACATCACTGCCCTGGCT
GACTACGCCATGCGGCTCATGGAGCAGATGAAGCACATCAATGAGCACTCCTTCAACAAT
TTCCAGATGAAGATTGGGCTGAACATGGGCCCAGTCGTGGCAGGTGTCATCGGGGCTCGG
AAGCCACAGTATGACATCTGGGGGAACACAGTGAATGTCTCTAGTCGTATGGACAGCACG
GGGGTCCCCGACCGAATCCAGGTGACCACGGACCTGTACCAGGTTCTAGCTGCCAAGGGC
TACCAGCTGGAGTGTCGAGGGGTGGTCAAGGTGAAGGGCAAGGGGGAGATGACCACCTAC
TTCCTCAATGGGGGCCCCAGCAGTTAA
|
| Enzyme 26 GenBank Gene ID |
AF250226  |
| Enzyme 26 GeneCard ID |
ADCY6  |
| Enzyme 26 GenAtlas ID |
ADCY6  |
| Enzyme 26 HGNC ID |
HGNC:237  |
| Enzyme 26 Chromosome Location |
12 |
| Enzyme 26 Locus |
12q12-q13 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- Wicker R, Catalan AG, Cailleux A, Starenki D, Stengel D, Sarasin A, Suarez HG: Cloning and expression of human adenylyl cyclase type VI in normal thyroid tissues. Biochim Biophys Acta. 2000 Sep 7;1493(1-2):279-83. [PubMed
]
- Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1997 Oct 31;4(5):307-13. [PubMed
]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
5980 |
| Enzyme 27 Name |
Adenylate cyclase type 5 |
| Enzyme 27 Synonyms |
- Adenylate cyclase type V
- ATP pyrophosphate-lyase 5
- Adenylyl cyclase 5
|
| Enzyme 27 Gene Name |
ADCY5 |
| Enzyme 27 Protein Sequence |
>Adenylate cyclase type 5
MSGSKSVSPPGYAAQKTAAPAPRGGPEHRSAWGEADSRANGYPHAPGGSARGSTKKPGGA
VTPQQQQRLASRWRSDDDDDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDCGRGSRRQRR
GAASGGSTRAPPAGGGGGSAAAAASAGGTEVRPRSVEVGLEERRGKGRAADELEAGAVEG
GEGSGDGGSSADSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQS
SLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGL
ACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSAL
HLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLH
SQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTS
LASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEM
GMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGK
AGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMN
RQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFL
GRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQI
TIVPHSIFMLSFYLTCSLLLTLVVFVSVIYSCVKLFPSPLQTLSRKIVRSKMNSTLVGVF
TITLVFLAAFVNMFTCNSRDLLGCLAQEHNISASQVNACHVAESAVNYSLGDEQGFCGSP
WPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLIVEVPGVTLFDNADL
LVTANAIDFFNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKL
QATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANF
SEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTY
DKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWG
NTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPL
S
|
| Enzyme 27 Number of Residues |
1261 |
| Enzyme 27 Molecular Weight |
138909 |
| Enzyme 27 Theoretical pI |
7.25 |
| Enzyme 27 GO Classification |
| Function |
- adenylate cyclase activity
- catalytic activity
- cyclase activity
- lyase activity
- phosphorus-oxygen lyase activity
|
| Process |
- cell communication
- cellular metabolism
- cellular process
- cyclic nucleotide biosynthesis
- intracellular signaling cascade
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide biosynthesis
- nucleotide metabolism
- physiological process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 27 General Function |
Signal transduction mechanisms |
| Enzyme 27 Specific Function |
This is a membrane-bound, calcium-inhibitable adenylyl cyclase |
| Enzyme 27 Pathways |
|
| Enzyme 27 Reactions |
- ATP = 3',5'-cyclic AMP + diphosphate
|
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
- 196-216
242-262
268-288
299-319
325-345
349-369
374-394
770-790
792-812
836-856
910-930
935-955
984-1004
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
Not Available |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
O95622  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
ADCY5_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
Not Available |
| Enzyme 27 GenBank Gene ID |
AC025571  |
| Enzyme 27 GeneCard ID |
ADCY5  |
| Enzyme 27 GenAtlas ID |
ADCY5  |
| Enzyme 27 HGNC ID |
HGNC:236  |
| Enzyme 27 Chromosome Location |
3 |
| Enzyme 27 Locus |
3q13.2-q21 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Ludwig MG, Seuwen K: Characterization of the human adenylyl cyclase gene family: cDNA, gene structure, and tissue distribution of the nine isoforms. J Recept Signal Transduct Res. 2002 Feb-Nov;22(1-4):79-110. [PubMed
]
- Raimundo S, Giray J, Volff JN, Schwab M, Altenbuchner J, Ratge D, Wisser H: Cloning and sequence of partial cDNAs encoding the human type V and VI adenylyl cyclases and subsequent RNA-quantification in various tissues. Clin Chim Acta. 1999 Jul;285(1-2):155-61. [PubMed
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
5981 |
| Enzyme 28 Name |
Adenylate cyclase type 8 |
| Enzyme 28 Synonyms |
- Adenylate cyclase type VIII
- ATP pyrophosphate-lyase 8
- Adenylyl cyclase 8
- Ca(2+/calmodulin- activated adenylyl cyclase
|
| Enzyme 28 Gene Name |
ADCY8 |
| Enzyme 28 Protein Sequence |
>Adenylate cyclase type 8
MELSDVRCLTGSEELYTIHPTPPAGDGRSASRPQRLLWQTAVRHITEQRFIHGHRGGSGS
GSGGSGKASDPAGGGPNHHAPQLSGDSALPLYSLGPGERAHSTCGTKVFPERSGSGSASG
SGGGGDLGFLHLDCAPSNSDFFLNGGYSYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRK
SEVVMNVLDVLTKLTLLVLHLSLASAPMDPLKGILLGFFTGIEVVICALVVVRKDTTSHT
YLQYSGVVTWVAMTTQILAAGLGYGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLGTS
LLQVILQVVIPRLAVISINQVVAQAVLFMCMNTAGIFISYLSDRAQRQAFLETRRCVEAR
LRLETENQRQERLVLSVLPRFVVLEMINDMTNVEDEHLQHQFHRIYIHRYENVSILFADV
KGFTNLSTTLSAQELVRMLNELFARFDRLAHEHHCLRIKILGDCYYCVSGLPEPRQDHAH
CCVEMGLSMIKTIRYVRSRTKHDVDMRIGIHSGSVLCGVLGLRKWQFDVWSWDVDIANKL
ESGGIPGRIHISKATLDCLNGDYNVEEGHGKERNEFLRKHNIETYLIKQPEDSLLSLPED
IVKESVSSSDRRNSGATFTEGSWSPELPFDNIVGKQNTLAALTRNSINLLPNHLAQALHV
QSGPEEINKRIEHTIDLRSGDKLRREHIKPFSLMFKDSSLEHKYSQMRDEVFKSNLVCAF
IVLLFITAIQSLLPSSRVMPMTIQFSILIMLHSALVLITTAEDYKCLPLILRKTCCWINE
TYLARNVIIFASILINFLGAILNILWCDFDKSIPLKNLTFNSSAVFTDICSYPEYFVFTG
VLAMVTCAVFLRLNSVLKLAVLLIMIAIYALLTETVYAGLFLRYDNLNHSGEDFLGTKEV
SLLLMAMFLLAVFYHGQQLEYTARLDFLWRVQAKEEINEMKELREHNENMLRNILPSHVA
RHFLEKDRDNEELYSQSYDAVGVMFASIPGFADFYSQTEMNNQGVECLRLLNEIIADFDE
LLGEDRFQDIEKIKTIGSTYMAVSGLSPEKQQCEDKWGHLCALADFSLALTESIQEINKH
SFNNFELRIGISHGSVVAGVIGAKKPQYDIWGKTVNLASRMDSTGVSGRIQVPEETYLIL
KDQGFAFDYRGEIYVKGISEQEGKIKTYFLLGRVQPNPFILPPRRLPGQYSLAAVVLGLV
QSLNRQRQKQLLNENNNTGIIKGHYNRRTLLSPSGTEPGAQAEGTDKSDLP
|
| Enzyme 28 Number of Residues |
1251 |
| Enzyme 28 Molecular Weight |
140124 |
| Enzyme 28 Theoretical pI |
6.99 |
| Enzyme 28 GO Classification |
| Function |
- adenylate cyclase activity
- catalytic activity
- cyclase activity
- lyase activity
- phosphorus-oxygen lyase activity
|
| Process |
- cell communication
- cellular metabolism
- cellular process
- cyclic nucleotide biosynthesis
- intracellular signaling cascade
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide biosynthesis
- nucleotide metabolism
- physiological process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 28 General Function |
Signal transduction mechanisms |
| Enzyme 28 Specific Function |
This is a membrane-bound, calcium-inhibitable adenylyl cyclase. May be involved in learning, in memory and in drug dependence |
| Enzyme 28 Pathways |
|
| Enzyme 28 Reactions |
- ATP = 3',5'-cyclic AMP + diphosphate
|
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
- 183-203
212-232
247-267
274-294
296-316
321-341
716-736
738-758
787-807
831-851
861-881
894-914
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
516263  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
P40145  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
ADCY8_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>3756 bp
ATGGAGCTCTCCGATGTGCGCTGCCTTACAGGCAGCGAGGAACTCTACACCATCCACCCG
ACGCCCCCGGCCGGCGACGGCAGGAGCGCCTCCCGGCCGCAGCGGCTGCTGTGGCAGACG
GCGGTGCGACACATCACGGAGCAGCGCTTCATTCACGGGCACCGGGGAGGCAGCGGCAGC
GGGAGTGGAGGCTCGGGCAAAGCCTCGGACCCTGCGGGCGGCGGCCCCAACCACCACGCG
CCGCAGCTGTCAGGCGACTCGGCGCTGCCCCTCTACTCGCTGGGCCCGGGAGAGCGAGCG
CACAGCACCTGCGGCACCAAAGTCTTCCCGGAACGCAGCGGGAGCGGCAGTGCCAGCGGC
AGCGGAGGCGGGGGCGACCTGGGCTTCCTGCACCTTGACTGTGCCCCTAGCAACTCGGAT
TTCTTTCTTAATGGGGGCTATAGCTACCGAGGGGTCATTTTCCCCACCCTGCGCAACTCC
TTCAAATCTCGGGATTTGGAACGCCTCTACCAGCGCTATTTCTTGGGCCAAAGGCGCAAA
TCGGAAGTGGTGATGAACGTGCTGGACGTGCTGACCAAACTCACTCTCTTGGTCCTACAC
TTGAGCCTGGCCTCGGCCCCCATGGACCCGCTCAAGGGCATCCTGCTGGGCTTCTTCACC
GGCATTGAGGTAGTGATCTGCGCCCTGGTGGTGGTCAGGAAGGACACCACCTCCCACACG
TACCTGCAGTACAGCGGCGTGGTCACCTGGGTGGCCATGACCACCCAGATCCTGGCAGCA
GGCCTCGGCTACGGGCTCCTGGGCGACGGCATAGGCTACGTGCTCTTCACGCTCTTCGCC
ACCTACAGTATGCTGCCGCTGCCGCTCACCTGGGCCATCCTGGCCGGCCTGGGCACCTCG
CTGCTGCAGGTCATCCTCCAAGTGGTCATACCCCGGCTGGCGGTCATTTCCATCAACCAG
GTTGTGGCCCAGGCAGTGCTATTCATGTGTATGAACACAGCTGGAATCTTCATCAGTTAC
CTGTCAGACCGGGCCCAGCGCCAAGCTTTCCTGGAGACTCGGAGGTGTGTGGAGGCCAGG
CTGCGCCTGGAGACAGAGAACCAAAGACAGGAGCGGCTCGTGCTTTCTGTGCTCCCCCGG
TTTGTTGTCCTGGAAATGATCAACGACATGACCAATGTGGAAGATGAGCACCTGCAGCAC
CAGTTCCATCGGATCTACATCCATCGCTATGAGAACGTCAGTATTCTTTTTGCAGATGTT
AAAGGATTTACCAACCTCTCCACGACCTTGTCTGCTCAGGAGCTGGTCAGGATGCTCAAC
GAGCTCTTTGCCAGATTTGATCGACTGGCCCATGAGCATCACTGCCTTCGTATTAAAATC
CTGGGGGACTGCTACTACTGCGTGTCTGGACTTCCTGAGCCCCGCCAGGACCATGCCCAC
TGCTGTGTTGAAATGGGTCTCAGCATGATCAAAACCATCAGGTATGTGCGGTCAAGGACA
AAACACGATGTTGACATGAGGATTGGAATCCACTCCGGCTCGGTGCTGTGCGGTGTTTTG
GGACTACGGAAGTGGCAGTTTGATGTCTGGTCTTGGGATGTGGATATTGCAAACAAACTC
GAATCTGGAGGAATCCCCGGGAGGATTCACATTTCCAAAGCCACGCTGGACTGTCTCAAC
GGTGACTATAACGTGGAAGAGGGCCATGGTAAAGAGAGGAATGAATTCCTGAGGAAGCAT
AATATCGAAACTTACTTAATTAAGCAGCCTGAGGACAGTCTGCTGTCCTTGCCTGAAGAT
ATCGTCAAGGAGTCAGTGAGCTCCTCAGACCGGAGAAACAGTGGGGCCACATTCACTGAA
GGATCCTGGAGCCCTGAACTGCCCTTTGATAATATCGTGGGGAAACAGAATACTCTGGCT
GCCCTAACAAGAAATTCAATAAATCTGCTTCCAAACCATCTTGCACAAGCTTTGCATGTC
CAGTCTGGGCCTGAGGAAATTAACAAGAGAATAGAACATACCATCGACTTGCGGAGTGGC
GATAAATTGAGAAGAGAGCATATCAAGCCATTCTCACTGATGTTTAAAGACTCCAGCCTG
GAGCACAAGTATTCTCAAATGAGGGATGAAGTGTTCAAGTCAAACTTGGTCTGTGCATTT
ATCGTTCTTCTATTTATCACGGCAATACAAAGTTTGCTTCCTTCTTCAAGAGTGATGCCA
ATGACCATCCAGTTCTCCATTCTGATTATGCTGCACTCGGCTCTGGTCCTCATCACCACA
GCAGAGGATTATAAATGTTTGCCCCTCATCCTCCGGAAAACTTGCTGTTGGATTAATGAG
ACCTATTTGGCCCGGAACGTCATCATCTTTGCATCCATTTTGATTAATTTCCTGGGTGCC
ATCTTAAATATCCTGTGGTGTGATTTTGACAAGTCGATACCCTTGAAGAACCTGACTTTC
AATTCCTCAGCTGTGTTTACAGATATCTGCTCCTACCCAGAGTACTTTGTCTTCACGGGG
GTGTTGGCCATGGTGACCTGTGCAGTTTTCCTCCGGCTGAACTCCGTCCTGAAGCTGGCA
GTGCTGCTGATCATGATTGCCATCTATGCCCTGCTCACTGAGACCGTCTACGCAGGCCTC
TTTCTGCGTTATGACAACCTCAACCACAGTGGAGAAGATTTCCTGGGGACCAAGGAGGTA
TCACTGCTACTGATGGCCATGTTCCTCCTGGCTGTGTTCTACCATGGACAGCAGCTGGAG
TACACAGCCCGCCTGGACTTCCTTTGGCGAGTACAGGCCAAAGAGGAGATCAATGAGATG
AAGGAGCTGAGGGAACACAATGAGAACATGCTCCGGAATATCTTACCCAGCCATGTGGCC
CGCCATTTCCTAGAGAAGGACCGAGACAATGAGGAGCTGTATTCTCAATCCTATGATGCT
GTTGGGGTGATGTTTGCCTCCATCCCAGGATTTGCGGACTTTTACTCTCAGACTGAAATG
AATAACCAGGGAGTGGAATGCCTGCGCTTGCTCAATGAGATCATTGCTGACTTCGATGAG
TTGCTTGGTGAAGACCGATTTCAAGACATTGAAAAGATTAAGACCATTGGCAGCACCTAC
ATGGCCGTGTCAGGCCTGTCACCTGAAAAACAGCAATGTGAAGACAAGTGGGGACATTTG
TGTGCTCTGGCTGACTTCTCACTCGCCCTGACAGAAAGCATACAGGAGATCAACAAGCAT
TCATTCAACAATTTTGAACTCCGGATTGGCATCAGCCACGGCTCAGTGGTAGCTGGCGTT
ATCGGCGCTAAGAAACCACAGTATGACATTTGGGGCAAAACTGTGAACCTGGCAAGCCGA
ATGGACAGCACGGGGGTTAGTGGCCGGATCCAAGTCCCAGAGGAGACCTATCTCATCCTG
AAGGACCAGGGCTTTGCCTTTGATTACCGAGGGGAGATCTATGTGAAGGGTATCAGTGAA
CAGGAAGGAAAAATCAAAACGTACTTTCTTCTGGGAAGAGTCCAACCCAACCCATTCATC
TTGCCCCCAAGAAGACTGCCTGGGCAGTACTCCCTGGCCGCGGTTGTCCTGGGACTTGTC
CAGTCCCTCAATAGGCAAAGGCAGAAGCAGCTACTCAATGAGAACAACAACACAGGAATC
ATCAAGGGTCATTACAACCGGCGGACTTTGTTGTCACCCAGCGGCACAGAGCCTGGAGCC
CAGGCTGAAGGCACCGACAAATCTGATTTGCCATAA
|
| Enzyme 28 GenBank Gene ID |
Z35309  |
| Enzyme 28 GeneCard ID |
ADCY8  |
| Enzyme 28 GenAtlas ID |
ADCY8  |
| Enzyme 28 HGNC ID |
HGNC:239  |
| Enzyme 28 Chromosome Location |
8 |
| Enzyme 28 Locus |
8q24 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- Defer N, Marinx O, Stengel D, Danisova A, Iourgenko V, Matsuoka I, Caput D, Hanoune J: Molecular cloning of the human type VIII adenylyl cyclase. FEBS Lett. 1994 Aug 29;351(1):109-13. [PubMed
]
- Parma J, Stengel D, Gannage MH, Poyard M, Barouki R, Hanoune J: Sequence of a human brain adenylyl cyclase partial cDNA: evidence for a consensus cyclase specific domain. Biochem Biophys Res Commun. 1991 Aug 30;179(1):455-62. [PubMed
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
5982 |
| Enzyme 29 Name |
Adenylate cyclase type 9 |
| Enzyme 29 Synonyms |
- Adenylate cyclase type IX
- ATP pyrophosphate-lyase 9
- Adenylyl cyclase 9
|
| Enzyme 29 Gene Name |
ADCY9 |
| Enzyme 29 Protein Sequence |
>Adenylate cyclase type 9
MASPPHQQLLHHHSTEVSCDSSGDSNSVRVKINPKQLSSNSHPKHCKYSISSSCSSSGDS
GGVPRRVGGGGRLRRQKKLPQLFERASSRWWDPKFDSVNLEEACLERCFPQTQRRFRYAL
FYIGFACLLWSIYFAVHMRSRLIVMVAPALCFLLVCVGFFLFTFTKLYARHYAWTSLALT
LLVFALTLAAQFQVLTPVSGRGDSSNLTATARPTDTCLSQVGSFSMCIEVLFLLYTVMHL
PLYLSLCLGVAYSVLFETFGYHFRDEACFPSPGAGALHWELLSRGLLHGCIHAIGVHLFV
MSQVRSRSTFLKVGQSIMHGKDLEVEKALKERMIHSVMPRIIADDLMKQGDEESENSVKR
HATSSPKNRKKKSSIQKAPIAFRPFKMQQIEEVSILFADIVGFTKMSANKSAHALVGLLN
DLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIKAIEQFCQEK
KEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLD
DRYEMEDGKVIERLGQSVVADQLKGLKTYLISGQRAKESRCSCAEALLSGFEVIDGSQVS
SGPRGQGTASSGNVSDLAQTVKTFDNLKTCPSCGITFAPKSEAGAEGGAPQNGCQDEHKN
STKASGGPNPKTQNGLLSPPQEEKLTNSQTSLCEILQEKGRWAGVSLDQSALLPLRFKNI
REKTDAHFVDVIKEDSLMKDYFFKPPINQFSLNFLDQELERSYRTSYQEEVIKNSPVKTF
ASPTFSSLLDVFLSTTVFLTLSTTCFLKYEAATVPPPPAALAVFSAALLLEVLSLAVSIR
MVFFLEDVMACTKRLLEWIAGWLPRHCIGAILVSLPALAVYSHVTSEYETNIHFPVFTGS
AALIAVVHYCNFCQLSSWMRSSLATVVGAGPLLLLYVSLCPDSSVLTSPLDAVQNFSSER
NPCNSSVPRDLRRPASLIGQEVVLVFFLLLLLVWFLNREFEVSYRLHYHGDVEADLHRTK
IQSMRDQADWLLRNIIPYHVAEQLKVSQTYSKNHDSGGVIFASIVNFSEFYEENYEGGKE
CYRVLNELIGDFDELLSKPDYSSIEKIKTIGATYMAASGLNTAQAQDGSHPQEHLQILFE
FAKEMMRVVDDFNNNMLWFNFKLRVGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTT
GVECRIQVSEESYRVLSKMGYDFDYRGTVNVKGKGQMKTYLYPKCTDHRVIPQHQLSISP
DIRVQVDGSIGRSPTDEIANLVPSVQYVDKTSLGSDSSTQAKDAHLSPKRPWKEPVKAEE
RGRFGKAIEKDDCDETGIEEANELTKLNVSKSV
|
| Enzyme 29 Number of Residues |
1353 |
| Enzyme 29 Molecular Weight |
150702 |
| Enzyme 29 Theoretical pI |
7.35 |
| Enzyme 29 GO Classification |
| Function |
- catalytic activity
- lyase activity
- phosphorus-oxygen lyase activity
|
| Process |
- cell communication
- cellular metabolism
- cellular process
- cyclic nucleotide biosynthesis
- intracellular signaling cascade
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide biosynthesis
- nucleotide metabolism
- physiological process
- signal transduction
|
| Component |
| — |
|
| Enzyme 29 General Function |
Signal transduction mechanisms |
| Enzyme 29 Specific Function |
May play a fundamental role in situations where fine interplay between intracellular calcium and cAMP determines the cellular function. May be a physiologically relevant docking site for calcineurin |
| Enzyme 29 Pathways |
|
| Enzyme 29 Reactions |
- ATP = 3',5'-cyclic AMP + diphosphate
|
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
- 118-138
142-162
172-192
216-235
242-259
281-301
787-807
819-839
868-888
892-912
921-941
976-996
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
3138932  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
O60503  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
ADCY9_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>3885 bp
ATGGCTTCCCCGCCCCACCAGCAGCTGCTGCATCACCACAGCACCGAGGTGAGCTGCGAC
TCCAGCGGGGACAGCAACAGCGTGCGCGTCAAGATCAACCCCAAGCAGCTGTCCTCCAAC
AGCCACCCCAAGCACTGCAAATACAGCATCTCCTCTAGCTGCAGCAGCTCTGGGGACTCC
GGGGGCGTCCCCCGGCGAGTGGGCGGCGGAGGCCGGCTGCGCAGGCAGAAGAAGCTGCCC
CAGCTGTTCGAGAGGGCCTCCAGCCGCTGGTGGGACCCCAAGTTCGACTCGGTGAACCTG
GAGGAGGCCTGCCTGGAGCGCTGCTTCCCGCAGACCCAGCGCCGGTTCCGGTATGCGCTC
TTCTACATCGGCTTCGCCTGCCTTCTGTGGAGCATCTATTTTGCGGTCCACATGAGATCC
AGACTGATCGTCATGGTCGCCCCCGCGCTGTGCTTCCTCCTGGTGTGTGTGGGCTTCTTT
CTGTTTACCTTCACCAAGCTGTACGCCCGGCATTACGCGTGGACCTCGCTGGCTCTCACC
CTGCTGGTGTTCGCCCTGACCCTGGCTGCGCAGTTCCAGGTCTTGACGCCTGTCTCAGGA
CGCGGCGACAGCTCCAACCTTACGGCCACAGCCCGGCCCACAGATACTTGCTTATCTCAA
GTGGGGAGCTTCTCCATGTGCATCGAAGTGCTCTTTTTGCTCTATACCGTCATGCACTTA
CCTTTGTACCTGAGTTTGTGTCTGGGGGTGGCCTACTCTGTCCTTTTCGAGACCTTTGGC
TACCATTTCCGGGATGAAGCCTGCTTCCCCTCGCCCGGAGCCGGGGCCCTGCACTGGGAG
CTGCTGAGCAGGGGGCTGCTCCACGGCTGCATCCACGCCATCGGGGTCCACCTGTTCGTC
ATGTCCCAGGTGAGGTCCAGGAGCACCTTCCTCAAGGTGGGGCAATCCATTATGCACGGG
AAGGACCTGGAAGTGGAAAAAGCCCTCAAAGAGAGGATGATTCATTCCGTGATGCCAAGA
ATCATAGCCGATGACTTAATGAAGCAGGGAGATGAGGAGAGTGAGAATTCTGTCAAGAGG
CATGCCACCTCGAGCCCCAAGAACAGGAAGAAAAAGTCTTCCATCCAAAAAGCTCCTATA
GCCTTCCGCCCTTTTAAGATGCAGCAGATCGAAGAAGTCAGTATTTTATTTGCAGATATC
GTGGGCTTCACCAAGATGAGTGCCAACAAGTCTGCCCACGCCCTGGTGGGTCTCCTGAAC
GATCTGTTCGGTCGCTTCGACCGCCTGTGTGAGGAGACCAAGTGTGAGAAAATCAGCACC
CTGGGAGACTGTTACTACTGCGTGGCGGGCTGTCCCGAGCCCCGGGCCGACCATGCCTAC
TGCTGCATCGAGATGGGCCTGGGCATGATCAAGGCCATCGAGCAGTTCTGCCAGGAGAAG
AAGGAGATGGTGAACATGAGAGTCGGGGTGCACACGGGCACCGTCCTTTGCGGCATCCTG
GGCATGAGGAGGTTTAAATTTGACGTGTGGTCCAACGATGTGAACCTGGCCAATCTCATG
GAGCAGCTGGGAGTGGCCGGCAAAGTTCACATTTCTGAGGCCACCGCAAAATACTTAGAT
GACCGGTACGAAATGGAAGATGGGAAAGTTATTGAACGGCTGGGCCAGAGCGTGGTTGCT
GACCAGTTGAAAGGTTTGAAGACATACCTGATATCGGGTCAGAGAGCCAAGGAGTCTCGC
TGCAGCTGTGCAGAGGCCTTGCTTTCTGGCTTTGAGGTCATTGACGGCTCACAGGTGTCC
TCAGGCCCTAGGGGACAGGGGACAGCGTCATCAGGGAATGTCAGTGACTTGGCGCAGACT
GTCAAAACCTTTGATAACCTTAAGACCTGCCCTTCGTGCGGAATCACATTTGCTCCCAAA
TCTGAAGCCGGCGCCGAGGGAGGAGCACCTCAAAACGGCTGCCAAGACGAGCATAAAAAC
AGCACCAAGGCTTCTGGAGGACCTAATCCCAAAACTCAGAACGGGCTCCTCAGCCCTCCC
CAAGAGGAGAAGCTCACCAACAGTCAGACTTCTCTGTGTGAGATCTTGCAGGAGAAGGGA
AGGTGGGCAGGGGTGAGCCTGGACCAGTCGGCTCTCCTTCCGCTGAGGTTCAAGAACATC
CGGGAGAAAACGGACGCCCACTTTGTGGACGTTATCAAAGAAGACAGCCTGATGAAAGAT
TACTTTTTTAAGCCGCCCATTAATCAGTTCAGCCTGAACTTCCTGGATCAGGAGCTGGAG
CGATCCTACAGGACCAGCTATCAGGAAGAGGTCATAAAGAACTCCCCCGTGAAGACGTTT
GCTAGTCCCACCTTCAGCTCCCTCCTGGATGTGTTTCTGTCGACCACAGTGTTTCTGACG
CTGTCCACCACCTGCTTCCTGAAGTACGAGGCGGCCACCGTGCCTCCCCCGCCCGCCGCC
CTGGCGGTCTTCAGTGCAGCCCTGCTGCTGGAGGTGCTGTCCCTCGCGGTGTCCATCAGG
ATGGTGTTCTTCCTGGAGGACGTCATGGCCTGCACCAAGCGCCTGCTGGAGTGGATCGCC
GGCTGGCTACCACGTCACTGCATCGGGGCCATCCTGGTGTCGCTTCCCGCACTGGCCGTC
TACTCCCATGTCACCTCCGAATATGAGACCAACATACACTTCCCAGTGTTCACAGGCTCG
GCCGCACTGATTGCCGTCGTGCACTACTGTAACTTCTGCCAGCTCAGCTCCTGGATGAGG
TCCTCCCTCGCCACCGTCGTGGGGGCCGGGCCGCTGCTCCTGCTCTACGTCTCCCTGTGC
CCAGACAGTTCTGTATTAACTTCGCCCCTTGACGCAGTACAGAATTTCAGTTCCGAGAGG
AACCCGTGCAATAGTTCGGTGCCGCGTGACCTCCGGCGGCCCGCCAGCCTCATCGGCCAG
GAGGTGGTTCTCGTCTTCTTTCTCCTGCTCTTGTTGGTCTGGTTCCTGAATCGCGAATTT
GAAGTCAGCTACCGCCTCCACTACCACGGAGACGTGGAAGCGGATCTTCACCGCACCAAG
ATCCAGAGCATGCGGGACCAGGCAGACTGGCTGCTGAGGAACATCATCCCCTACCACGTG
GCTGAGCAGCTGAAGGTGTCCCAGACCTACTCCAAGAACCACGACAGCGGAGGGGTGATC
TTCGCCAGCATCGTCAACTTCAGCGAGTTCTACGAGGAGAACTACGAGGGCGGCAAGGAG
TGCTACCGGGTCCTCAACGAGCTCATCGGGGACTTTGACGAGCTCCTAAGCAAGCCGGAC
TACAGCAGCATCGAGAAGATCAAGACCATCGGAGCCACGTACATGGCGGCGTCAGGGCTG
AACACCGCGCAGGCCCAGGACGGCAGCCACCCGCAGGAGCACCTGCAGATCCTGTTCGAG
TTCGCCAAGGAGATGATGCGCGTGGTGGACGACTTCAACAACAACATGCTGTGGTTCAAC
TTCAAGCTCCGCGTCGGCTTCAACCATGGGCCCCTCACGGCCGGGGTCATCGGCACCACC
AAGCTGCTGTACGACATCTGGGGAGACACCGTCAACATCGCCAGCAGGATGGACACCACC
GGCGTGGAGTGCCGCATCCAGGTGAGCGAAGAGAGCTACCGCGTCTTGAGCAAGATGGGC
TATGACTTCGACTACAGAGGGACCGTGAATGTCAAGGGGAAAGGCCAGATGAAGACCTAC
CTGTACCCAAAGTGCACGGATCACAGGGTCATCCCAGCACCAGCTGTCCATCTCCCCAGA
CATCCGCGTCCAGGTGGATGGCAGCATCGGACGGTCTCCCACAGACGAGATTGCCAACCT
GGTGCCTTCTGTCCAGTATGTGGACAAGACATCTCTGGGTTCTGA
|
| Enzyme 29 GenBank Gene ID |
AF036927  |
| Enzyme 29 GeneCard ID |
ADCY9  |
| Enzyme 29 GenAtlas ID |
ADCY9  |
| Enzyme 29 HGNC ID |
HGNC:240  |
| Enzyme 29 Chromosome Location |
16 |
| Enzyme 29 Locus |
16p13.3 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- Hacker BM, Tomlinson JE, Wayman GA, Sultana R, Chan G, Villacres E, Disteche C, Storm DR: Cloning, chromosomal mapping, and regulatory properties of the human type 9 adenylyl cyclase (ADCY9). Genomics. 1998 May 15;50(1):97-104. [PubMed
]
- Small KM, Brown KM, Theiss CT, Seman CA, Weiss ST, Liggett SB: An Ile to Met polymorphism in the catalytic domain of adenylyl cyclase type 9 confers reduced beta2-adrenergic receptor stimulation. Pharmacogenetics. 2003 Sep;13(9):535-41. [PubMed
]
- Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed
]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed
]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
5983 |
| Enzyme 30 Name |
Adenylate cyclase type 3 |
| Enzyme 30 Synonyms |
- Adenylate cyclase type III
- ATP pyrophosphate-lyase 3
- Adenylyl cyclase 3
- AC-III
- AC3
- Adenylate cyclase, olfactive type
|
| Enzyme 30 Gene Name |
ADCY3 |
| Enzyme 30 Protein Sequence |
>Adenylate cyclase type 3
MPRNQGFSEPEYSAEYSAEYSVSLPSDPDRGVGRTHEISVRNSGSCLCLPRFMRLTFVPE
SLENLYQTYFKRQRHETLLVLVVFAALFDCYVVVMCAVVFSSDKLASLAVAGIGLVLDII
LFVLCKKGLLPDRVTRRVLPYVLWLLITAQIFSYLGLNFARAHAASDTVGWQVFFVFSFF
ITLPLSLSPIVIISVVSCVVHTLVLGVTVAQQQQEELKGMQLLREILANVFLYLCAIAVG
IMSYYMADRKHRKAFLEARQSLEVKMNLEEQSQQQENLMLSILPKHVADEMLKDMKKDES
QKDQQQFNTMYMYRHENVSILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQ
LRIKILGDCYYCICGLPDYREDHAVCSILMGLAMVEAISYVREKTKTGVDMRVGVHTGTV
LGGVLGQKRWQYDVWSTDVTVANKMEAGGIPGRVHISQSTMDCLKGEFDVEPGDGGSRCD
YLEEKGIETYLIIASKPEVKKTATQNGLNGSALPNGAPASSKSSSPALIETKEPNGSAHS
SGSTSEKPEEQDAQADNPSFPNPRRRLRLQDLADRVVDASEDEHELNQLLNEALLERESA
QVVKKRNTFLLSMRFMDPEMETRYSVEKEKQSGAAFSCSCVVLLCTALVEILIDPWLMTN
YVTFMVGEILLLILTICSLAAIFPRAFPKKLVAFSTWIDRTRWARNTWAMLAIFILVMAN
VVDMLSCLQYYTGPSNATAGMETEGSCLENPKYYNYVAVLSLIATIMLVQVSHMVKLTLM
LLVAGAVATINLYAWRPVFDEYDHKRFREHDLPMVALEQMQGFNPGLNGTDRLPLVPSKY
SMTVMVFLMMLSFYYFSRHVEKLARTLFLWKIEVHDQKERVYEMRRWNEALVTNMLPEHV
ARHFLGSKKRDEELYSQTYDEIGVMFASLPNFADFYTEESINNGGIECLRFLNEIISDFD
SLLDNPKFRVITKIKTIGSTYMAASGVTPDVNTNGFASSNKEDKSERERWQHLADLADFA
LAMKDTLTNINNQSFNNFMLRIGMNKGGVLAGVIGARKPHYDIWGNTVNVASRMESTGVM
GNIQVVEETQVILREYGFRFVRRGPIFVKGKGELLTFFLKGRDKLATFPNGPSVTLPHQV
VDNS
|
| Enzyme 30 Number of Residues |
1144 |
| Enzyme 30 Molecular Weight |
128962 |
| Enzyme 30 Theoretical pI |
6.55 |
| Enzyme 30 GO Classification |
| Function |
- catalytic activity
- lyase activity
- phosphorus-oxygen lyase activity
|
| Process |
- cell communication
- cellular metabolism
- cellular process
- cyclic nucleotide biosynthesis
- intracellular signaling cascade
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide biosynthesis
- nucleotide metabolism
- physiological process
- signal transduction
|
| Component |
| — |
|
| Enzyme 30 General Function |
Signal transduction mechanisms |
| Enzyme 30 Specific Function |
Mediates odorant detection (possibly) via modulation of intracellular cAMP concentration |
| Enzyme 30 Pathways |
|
| Enzyme 30 Reactions |
- ATP = 3',5'-cyclic AMP + diphosphate
|
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
- 80-100
105-125
139-159
173-193
226-246
381-401
633-653
664-684
708-728
754-774
775-795
833-853
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
4104226  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
O60266  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
ADCY3_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>3435 bp
ATGCCGAGGAACCAGGGCTTCTCCGAGCCCGAATACTCGGCCGAGTACTCAGCCGAGTAC
TCCGTCAGCCTGCCCTCCGACCCTGACCGCGGGGTGGGCCGGACCCATGAAATCTCGGTC
CGGAACTCGGGCTCCTGCCTGTGCCTGCCTCGCTTCATGCGGCTGACTTTCGTGCCGGAG
TCCTTGGAGAACCTCTACCAGACCTACTTCAAAAGGCAGCGCCACGAGACCCTGCTGGTG
CTGGTGGTCTTTGCAGCCCTCTTTGACTGCTACGTGGTGGTCATGTGTGCTGTGGTCTTC
TCCAGCGACAAGCTGGCTCCCCTCGCCGTGGCTGGAATTGGACTGGTGTTGGACATCATC
CTCTTCGTGCTCTGCAAAAAGGGGCTGCTCCCGGACCGGGTCACCCGCAGAGTGCTGCCC
TACGTGCTGTGGCTGCTCATAACCGCCCAGATCTTCTCCTACCTGGGCCTGAACTTCGCG
CGTGCCCACGCGGCTAGTGACACGGTGGGCTGGCAGGTCTTCTTTGTCTTCTCCTTCTTC
ATCACGCTGCCCCTCAGCCTCAGCCCCATCGTGATCATCTCCGTGGTCTCCTGTGTGGTG
CACACGTTGGTCCTGGGGGTCACCGTGGCCCAGCAGCAGCAGGAGGAGCTCAAGGGGATG
CAGCTGCTGCGGGAGATCCTGGCCAACGTCTTCCTCTACCTGTGCGCCATCGCTGTGGGC
ATCATGTCCTACTACATGGCTGACCGCAAGCACCGCAAGGCCTTCCTGGAGGCCCGCCAG
TCGCTGGAGGTGAAGATGAACCTGGAAGAGCAGAGCCAGCAGCAGGAGAACCTCATGCTT
TCCATCCTGCCCAAGCACGTGGCTGACGAGATGCTGAAAGACATGAAGAAAGACGAGAGC
CAGAAGGACCAGCAGCAGTTCAACACCATGTACATGTACCGTCACGAGAACGTCAGCATC
CTCTTTGCCGACATCGTGGGCTTTACCCAGCTGTCTTCTGCCTGCAGTGCCCAGGAGCTT
GTGAAGCTGCTCAACGAGCTCTTTGCCCGCTTTGACAAGCTGGCAGCTAAATACCACCAG
CTGCGGATTAAGATCCTGGGCGACTGCTACTACTGCATCTGCGGCTTGCCTGACTACCGG
GAGGACCACGCCGTCTGCTCCATCCTCATGGGGCTGGCCATGGTGGAGGCCATCTCGTAT
GTGCGGGAGAAGACCAAGACTGGGGTGGACATGCGTGTGGGGGTGCACACGGGCACCGTG
CTGGGGGGCGTCCTGGGCCAGAAGCGCTGGCAGTACGACGTGTGGTCGACTGATGTCACT
GTAGCCAACAAGATGGAGGCCGGCGGCATCCCTGGGCGCGTGCACATCTCCCAGAGCACC
ATGGACTGCCTGAAAGGGGAGTTTGATGTGGAGCCAGGCGATGGGGGCAGCCGCTGTGAT
TACCTAGAAGAGAAGGGTATTGAAACCTACCTCATCATTGCCTCCAAGCCAGAGGTGAAG
AAAACAGCCACCCAGAATGGCCTCAATGGCTCGGCCCTGCCCAATGGAGCACCAGCTTCC
TCAAAGTCCAGCTCCCCTGCCCTCATTGAGACCAAGGAGCCCAACGGGAGTGCCCACAGC
AGTGGGTCCACGTCGGAGAAGCCCGAGGAGCAGGATGCCCAGGCCGACAACCCCTCATTC
CCCAACCCACGCCGGAGGCTGCGCCTGCAGGACCTGGCTGACCGAGTGGTGGATGCCTCT
GAAGATGAGCACGAGCTCAACCAGCTGCTCAACGAGGCCCTGCTTGAGCGAGAGTCCGCC
CAAGTAGTAAAGAAGAGAAACACCTTCCTCTTGTCCATGCGGTTCATGGACCCCGAGATG
GAAACCCGCTACTCGGTGGAGAAGGAGAAGCAGAGTGGGGCTGCCTTCAGCTGCTCCTGC
GTCGTCCTGCTCTGCACGGCCCTGGTCGAGATACTCATCGACCCCTGGCTAATGACAAAC
TATGTGACCTTCATGGTGGGGGAGATTCTGCTCCTCATCCTGACCATCTGCTCCCTGGCT
GCCATCTTTCCCCGGGCCTTTCCTAAGAAGCTTGTGGCCTTCTCAACTTGGATTGACCGG
ACCCGCTGGGCCAGGAACACCTGGGCCATGCTCGCCATCTTCATCCTGGTGATGGCAAAT
GTCGTGGACATGCTCAGCTGTCTCCAGTACTACACGGGACCCAGCAATGCAACGGCAGGG
ATGGAGACGGAGGGCAGCTGCCTGGAGAACCCCAAGTATTACAACTATGTGGCCGTGCTG
TCCCTCATCGCCACCATCATGCTGGTGCAGGTCAGCCACATGGTGAAGCTCACGCTCATG
CTGCTCGTCGCAGGCGCCGTGGCCACCATCAACCTCTATGCCTGGCGTCCCGTCTTTGAT
GAATACGACCACAAGCGTTTTCGGGAGCACGACTTACCTATGGTGGCCTTAGAGCAGATG
CAAGGATTCAACCCTGGGCTCAATGGCACTGACAGGCTGCCCCTGGTGCCTTCCAAGTAC
TCTATGACGGTGATGGTGTTCCTCATGATGCTCAGCTTCTACTACTTCTCCCGCCACGTA
GAAAAACTGGCACGGACACTTTTCTTGTGGAAGATTGAGGTCCACGACCAGAAGGAACGT
GTCTATGAGATGCGACGCTGGAACGAGGCCTTGGTCACCAACATGTTGCCTGAGCACGTG
GCACGCCATTTCCTGGGGTCCAAGAAGAGAGATGAGGAGCTGTATAGCCAGACGTATGAT
GAGATTGGAGTCATGTTTGCCTCCCTGCCCAACTTTGCTGACTTCTACACAGAGGAGAGC
ATCAACAATGGTGGTATTGAGTGTCTGCGTTTCCTCAATGAAATCATCTCAGATTTTGAC
TCTCTCCTGGACAATCCCAAGTTCCGGGTGATCACCAAGATCAAAACCATTGGCAGCACG
TATATGGCGGCTTCAGGAGTCACCCCCGATGTCAACACCAATGGCTTTGCCAGCTCCAAC
AAGGAAGACAAGTCCGAGAGAGAGCGCTGGCAGCACCTGGCTGACCTGGCCGACTTCGCG
CTGGCCATGAAGGATACGCTCACCAACATCAACAACCAGTCCTTCAATAACTTCATGCTG
CGCATAGGCATGAACAAAGGCGGGGTTCTGGCTGGGGTCATCGGAGCCCGGAAACCACAC
TACGACATCTGGGGCAATACAGTCAATGTAGCCAGCAGGATGGAGTCCACGGGGGTCATG
GGCAACATTCAGGTGGTAGAAGAAACCCAAGTCATCCTCCGAGAGTACGGCTTCCGCTTT
GTGAGGCGAGGCCCCATCTTTGTGAAGGGGAAGGGGGAGCTGCTGACCTTCTTCTTGAAG
GGGCGGGATAAGCTAGCCACCTTCCCCAATGGCCCCTCTGTCACACTGCCCCACCAGGTG
GTGGACAACTCCTGA
|
| Enzyme 30 GenBank Gene ID |
AF033861  |
| Enzyme 30 GeneCard ID |
ADCY3  |
| Enzyme 30 GenAtlas ID |
ADCY3  |
| Enzyme 30 HGNC ID |
HGNC:234  |
| Enzyme 30 Chromosome Location |
2 |
| Enzyme 30 Locus |
2p24-p22 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Yang B, He B, Abdel-Halim SM, Tibell A, Brendel MD, Bretzel RG, Efendic S, Hillert J: Molecular cloning of a full-length cDNA for human type 3 adenylyl cyclase and its expression in human islets. Biochem Biophys Res Commun. 1999 Jan 27;254(3):548-51. [PubMed
]
- Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed
]
- Hellevuo K, Yoshimura M, Kao M, Hoffman PL, Cooper DM, Tabakoff B: A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line. Biochem Biophys Res Commun. 1993 Apr 15;192(1):311-8. [PubMed
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
5984 |
| Enzyme 31 Name |
Adenylate cyclase type 1 |
| Enzyme 31 Synonyms |
- Adenylate cyclase type I
- ATP pyrophosphate-lyase 1
- Adenylyl cyclase 1
- Ca(2+/calmodulin- activated adenylyl cyclase
|
| Enzyme 31 Gene Name |
ADCY1 |
| Enzyme 31 Protein Sequence |
>Adenylate cyclase type 1
MAGAPRGGGGGGGGAGEPGGAERAAGTSRRRGLRACDEEFACPELEALFRGYTLRLEQAA
TLKALAVLSLLAGALALAELLGAPGPAPGLAKGSHPVHCVLFLALLVVTNVRSLQVPQLQ
QVGQLALLFSLTFALLCCPFALGGPARGSAGAAGGPATAEQGVWQLLLVTFVSYALLPVR
SLLAIGFGLVVAASHLLVTATLVPAKRPRLWRTLGANALLFVGVNMYGVFVRILTERSQR
KAFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHD
NVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGL
TQPKTDHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWS
NDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEPGYGHERNSFLKTHNIETFFIVPSH
RRKIFPGLILSDIKPAKRMKFKTVCYLLVQLMHCRKMFKAEIPFSNVMTCEDDDKRRALR
TASEKLRNRSSFSTNVVYTTPGTRVNRYISRLLEARQTELEMADLNFFTLKYKHVEREQK
YHQLQDEYFTSAVVLTLILAALFGLVYLLIFPQSVVVLLLLVFCICFLVACVLYLHITRV
QCFPGCLTIQIRTVLCIFIVVLIYSVAQGCVVGCLPWAWSSKPNSSLVVLSSGGQRTALP
TLPCESTHHALLCCLVGTLPLAIFFRVSSLPKMILLSGLTTSYILVLELSGYTRTGGGAV
SGRSYEPIVAILLFSCALALHARQVDIRLRLDYLWAAQAEEEREDMEKVKLDNRRILFNL
LPAHVAQHFLMSNPRNMDLYYQSYSQVGVMFASIPNFNDFYIELDGNNMGVECLRLLNEI
IADFDELMEKDFYKDIEKIKTIGSTYMAAVGLAPTSGTKAKKSISSHLSTLADFAIEMFD
VLDEINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMDSTGVQGRIQV
TEEVHRLLRRCPYHFVCRGKVSVKGKGEMLTYFLEGRTDGNGSQIRSLGLDRKMCPFGRA
GLQGRRPPVCPMPGVSVRAGLPPHSPGQYLPSAAAGKEA
|
| Enzyme 31 Number of Residues |
1119 |
| Enzyme 31 Molecular Weight |
123442 |
| Enzyme 31 Theoretical pI |
8.49 |
| Enzyme 31 GO Classification |
| Function |
- catalytic activity
- lyase activity
- phosphorus-oxygen lyase activity
|
| Process |
- cell communication
- cellular metabolism
- cellular process
- cyclic nucleotide biosynthesis
- intracellular signaling cascade
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide biosynthesis
- nucleotide metabolism
- physiological process
- signal transduction
|
| Component |
| — |
|
| Enzyme 31 General Function |
Signal transduction mechanisms |
| Enzyme 31 Specific Function |
This is a calmodulin-sensitive adenylyl cyclase. May be involved in regulatory processes in the central nervous system. It may play a role in memory acquisition and learning |
| Enzyme 31 Pathways |
|
| Enzyme 31 Reactions |
- ATP = 3',5'-cyclic AMP + diphosphate
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
- 64-84
88-108
125-145
158-178
183-203
214-234
611-631
635-655
674-694
725-745
753-773
775-794
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
41472630  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
Q08828  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
ADCY1_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>314 bp
ATGAAGGAGGACTTCCTGAAGCCCCCTGAGAGGATTTTCCACAAGATTTACATCCAGAGG
CACGACAATGTGAGCATCCTGTTTGCTGACATCGTGGGTTTCACGGGCTTGGCATCCCAG
TGCACAGCCCAGGAGCTGGTGAAACTCCTCAATGAGCTCTTCGGCAAGTTCGATGAATTA
GCCACGGAGAACCACTGTCGCCGCATCAAGATTCTCGGGGACTGCTACTACTGCGTGTCG
GGCCTCACCCAGCCCAAGACTGACCATGCCCACTGCTGTGTGGAGATGGGACTCGACATG
ATTGATACCATCAC
|
| Enzyme 31 GenBank Gene ID |
AC069008  |
| Enzyme 31 GeneCard ID |
ADCY1  |
| Enzyme 31 GenAtlas ID |
ADCY1  |
| Enzyme 31 HGNC ID |
HGNC:232  |
| Enzyme 31 Chromosome Location |
7 |
| Enzyme 31 Locus |
7p13-p12 |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- Villacres EC, Xia Z, Bookbinder LH, Edelhoff S, Disteche CM, Storm DR: Cloning, chromosomal mapping, and expression of human fetal brain type I adenylyl cyclase. Genomics. 1993 May;16(2):473-8. [PubMed
]
|
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
6209 |
| Enzyme 32 Name |
Adenylate cyclase type 2 |
| Enzyme 32 Synonyms |
- Adenylate cyclase type II
- ATP pyrophosphate-lyase 2
- Adenylyl cyclase 2
|
| Enzyme 32 Gene Name |
ADCY2 |
| Enzyme 32 Protein Sequence |
>Adenylate cyclase type 2
MWQEAMRRRRYLRDRSEEAAGGGDGLPRSRDWLYESYYCMSQQHPLIVFLLLIVMGSCLA
LLAVFFALGLEVEDHVAFLITVPTALAIFFAIFILVCIESVFKKLLRLFSLVIWICLVAM
GYLFMCFGGTVSPWDQVSFFLFIIFVVYTMLPFNMRDAIIASVLTSSSHTIVLSVCLSAT
PGGKEHLVWQILANVIIFICGNLAGAYHKHLMELALQQTYQDTCNCIKSRIKLEFEKRQQ
ERLLLSLLPAHIAMEMKAEIIQRLQGPKAGQMENTNNFHNLYVKRHTNVSILYADIVGFT
RLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVK
MGLDMCEAIKKVRDATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGG
VPGRVHISSVTLEHLNGAYKVEEGDGDIRDPYLKQHLVKTYFVINPKGERRSPQHLFRPR
HTLDGAKMRASVRMTRYLESWGAAKPFAHLHHRDSMTTENGKISTTDVPMGQHNFQNRTL
RTKSQKKRFEEELNERMIQAIDGINAQKQWLKSEDIQRISLLFYNKVLEKEYRATALPAF
KYYVTCACLIFFCIFIVQILVLPKTSVLGISFGAAFLLLAFILFVCFAGQLLQCSKKASP
LLMWLLKSSGIIANRPWPRISLTIITTAIILMMAVFNMFFLSDSEETIPPTANTTNTSFS
ASNNQVAILRAQNLFFLPYFIYSCILGLISCSVFLRVNYELKMLIMMVALVGYNTILLHT
HAHVLGDYSQVLFERPGIWKDLKTMGSVSLSIFFITLLVLGRQNEYYCRLDFLWKNKFKK
EREEIETMENLNRVLLENVLPAHVAEHFLARSLKNEELYHQSYDCVCVMFASIPDFKEFY
TESDVNKEGLECLRLLNEIIADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSAVPSQEHS
QEPERQYMHIGTMVEFAFALVGKLDAINKHSFNDFKLRVGINHGPVIAGVIGAQKPQYDI
WGNTVNVASRMDSTGVLDKIQVTEETSLVLQTLGYTCTCRGIINVKGKGDLKTYFVNTEM
SRSLSQSNVAS
|
| Enzyme 32 Number of Residues |
1091 |
| Enzyme 32 Molecular Weight |
123605 |
| Enzyme 32 Theoretical pI |
8.15 |
| Enzyme 32 GO Classification |
| Function |
- adenylate cyclase activity
- catalytic activity
- cyclase activity
- lyase activity
- phosphorus-oxygen lyase activity
|
| Process |
- cell communication
- cellular metabolism
- cellular process
- cyclic nucleotide biosynthesis
- intracellular signaling cascade
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide biosynthesis
- nucleotide metabolism
- physiological process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 32 General Function |
Signal transduction mechanisms |
| Enzyme 32 Specific Function |
This is a membrane-bound, calmodulin-insensitive adenylyl cyclase |
| Enzyme 32 Pathways |
|
| Enzyme 32 Reactions |
- ATP = 3',5'-cyclic AMP + diphosphate
|
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
- 46-66
76-96
108-128
133-153
159-179
187-207
602-622
628-652
680-701
734-755
763-780
801-821
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
33150814  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
Q08462  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
ADCY2_HUMAN  |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>3276 bp
ATGTGGCAGGAGGCGATGCGGCGCCGCCGCTACCTGCGGGACCGCTCCGAGGAGGCGGCG
GGCGGCGGAGACGGGCTGCCGCGGTCCCGGGACTGGCTCTACGAGTCCTACTACTGCATG
AGCCAGCAGCACCCGCTCATCGTCTTCCTGCTGCTCATCGTCATGGGCTCCTGCCTCGCC
CTGCTCGCCGTCTTCTTCGCGCTCGGGCTGGAAGTTGAAGACCATGTGGCGTTTCTAATA
ACAGTTCCAACTGCCCTGGCGATTTTCTTTGCGATATTTATCCTGGTCTGCATCGAGTCT
GTGTTTAAGAAGCTGCTGCGCCTCTTCTCGTTGGTGATATGGATATGCCTTGTTGCCATG
GGATACCTGTTCATGTGTTTTGGAGGCACCGTCTCTCCCTGGGACCAGGTATCGTTCTTC
CTCTTCATCATCTTCGTGGTGTACACCATGCTGCCCTTCAACATGCGAGACGCCATCATT
GCCAGCGTCCTCACCTCCTCCTCCCACACCATCGTGCTTAGCGTCTGCCTGTCTGCAACA
CCGGGAGGCAAGGAGCACCTTGGTCTGGCAGATCCTGGCCAATGTGATCATTTTCATCTG
TGGGAACCTGGCNGGACTAACCATAAGCACCTCATGGAACTCGCTCTTCAGCAAACATAT
CAGGACACCTGTAATTGCATCAAGTCGCGGATCAAGTTGGAATTTGAAAAACGTCAACAG
GAGCGGCTTCTGCTCTCCCTGCTGCCGGCCCACATCGCCATGGAGATGAAAGCGGAGATC
ATCCAGAGGCTGCAGGGCCCCAAGGCGGGCCAGATGGAGAACACAAATAACTTCCACAAC
CTGTATGTGAAGCGGCATACAAACGTGAGCATCTTATACGCTGACATCGTTGGCTTTACC
CGGCTGGCAAGTGACTGCTCCCCGGGAGAACTAGTCCACATGCTGAATGAGCTCTTTGGA
AAGTTTGATCAAATTGCAAAGGAGAATGAATGCATGAGAATTAAAATTTTAGGAGACTGC
TACTACTGTGTATCTGGACTCCCTATATCTCTCCCTAACCATGCCAAGAACTGTGTGAAA
ATGGGGCTGGACATGTGTGAAGCCATAAAGAAAGTGAGGGATGCTACTGGAGTTGATATC
AACATGCGCGTGGGCGTGCATTCTGGGAATGTCCTGTGTGGCGTGATTGGTCTGCAGAAG
TGGCAATATGATGTGTGGTCACATGATGTGACCTTGGCCAACCACATGGAAGCTGGAGGG
GTCCCTGGACGTGTTCACATTTCTTCTGTCACCCTGGAGCACTTGAATGGCGCTTATAAA
GTGGAGGAGGGAGATGGTGACATTAGGGACCCATATTTAAAACAGCACCTGGTGAAAACC
TACTTTGTGATCAACCCCAAGGGAGAACGACGGAGCCCCCAGCATCTCTTCAGACCTCGC
CACACCCTTGATGGAGCCAAAATGAGGGCCTCGGTCCGCATGACCCGGTACTTGGAGTCC
TGGGGGGCAGCCAAGCCCTTTGCACACCTACATCACAGGGACAGCATGACCACAGAGAAC
GGCAAGATCAGCACCACGGATGTACCCATGGGTCAGCATAATTTTCAAAATCGCACCTTA
AGAACCAAGTCACAAAAGAAGAGATTTGAAGAAGAATTGAATGAAAGGATGATTCAAGCA
ATTGATGGGATTAATGCACAGAAGCAATGGCTCAAGTCTGAAGACATTCAGAGAATCTCA
CTGCTTTTCTATAACAAAGTACTAGAAAAAGAGTACCGGGCCACGGCACTGCCAGCGTTC
AAGTATTATGTGACTTGTGCCTGTCTCATATTCTTCTGCATCTTCATTGTGCAGATTCTC
GTGCTGCCAAAAACGTCTGTCCTGGGCATCTCCTTTGGGGCTGCGTTTCTCTTGCTGGCC
TTCATCCTCTTCGTCTGCTTTGCTGGACAGCTTCTGCAATGCAGCAAAAAAGCCTCTCCC
CTGCTCATGTGGCTTTTGAAGTCCTCGGGCATCATTGCCAACCGCCCCTGGCCACGGATC
TCTCTCACGATCATCACCACAGCCATCATATTAATGATGGCCGTGTTCAACATGTTTTTC
CTGAGTGACTCAGAGGAAACAATCCCTCCAACTGCCAACACAACAAACACAAGCTTTTCA
GCCTCAAATAATCAGGTGGCGATTCTGCGTGCGCAGAATTTATTTTTCCTCCCGTACTTT
ATCTACAGCTGCATTCTGGGACTGATATCCTGTTCCGTGTTCCTGCGGGTAAACTATGAG
CTGAAGATGTTGATCATGATGGTGGCCTTGGTGGGCTACAACACCATCCTACTCCACACC
CACGCCCACGTCCTGGGCGACTACAGCCAGGTCTTATTTGAGAGACCAGGCATTTGGAAA
GACCTGAAGACCATGGGCTCTGTGTCTCTCTCTATATTCTTCATCACACTGCTTGTTCTG
GGTAGACAGAATGAATATTACTGTAGGTTAGACTTCTTATGGAAGAACAAATTCAAAAAA
GAGCGGGAGGAGATAGAGACCATGGAGAACCTGAACCGCGTGCTGCTGGAGAACGTGCTT
CCCGCGCACGTGGCTGAGCACTTCCTGGCCAGGAGCCTGAAGAATGAGGAGCTATACCAC
CAGTCCTATGACTGCGTCTGCGTCATGTTTGCCTCCATTCCGGATTTCAAAGAATTTTAT
ACAGAATCCGACGTGAACAAGGAGGGCTTGGAATGCCTTCGGCTCCTGAACGAGATCATC
GCTGACTTTGATGATCTTCTTTCCAAGCCAAAATTCAGTGGAGTTGAAAAGATTAAGACC
ATTGGCAGCACATACATGGCAGCAACAGGTCTGAGCGCTGTGCCCAGCCAGGAGCACTCC
CAGGAGCCCGAGCGGCAGTACATGCACATTGGCACCATGGTGGAGTTTGCTTTTGCCCTG
GTAGGGAAGCTGGATGCCATCAACAAGCACTCCTTCAACGACTTCAAATTGCGAGTGGGT
ATTAACCATGGACCTGTGATAGCTGGTGTGATTGGAGCTCAGAAGCCACAATATGATATC
TGGGGCAACACTGTCAATGTGGCCAGTAGGATGGACAGCACCGGAGTCCTGGACAAAATA
CAGGTTACCGAGGAGACGAGCCTCGTCCTGCAGACCCTCGGATACACGTGCACCTGTCGA
GGAATAATCAACGTGAAAGGAAAGGGGGACCTGAAGACGTACTTTGTAAACACAGAAATG
TCAAGGTCCCTTTCCCAGAGCAACGTGGCATCCTGA
|
| Enzyme 32 GenBank Gene ID |
AF410885  |
| Enzyme 32 GeneCard ID |
ADCY2  |
| Enzyme 32 GenAtlas ID |
ADCY2  |
| Enzyme 32 HGNC ID |
HGNC:233  |
| Enzyme 32 Chromosome Location |
5 |
| Enzyme 32 Locus |
5p15.3 |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
- Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed
]
- Stengel D, Parma J, Gannage MH, Roeckel N, Mattei MG, Barouki R, Hanoune J: Different chromosomal localization of two adenylyl cyclase genes expressed in human brain. Hum Genet. 1992 Sep-Oct;90(1-2):126-30. [PubMed
]
|
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
6332 |
| Enzyme 33 Name |
Cytochrome P450 17A1 |
| Enzyme 33 Synonyms |
- CYPXVII
- P450-C17
- P450c17
- Steroid 17-alpha-monooxygenase
- Steroid 17-alpha-hydroxylase/17,20 lyase
|
| Enzyme 33 Gene Name |
CYP17A1 |
| Enzyme 33 Protein Sequence |
>Cytochrome P450 17A1
MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKY
GPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAH
WQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVIS
LICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRN
DLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIF
GAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVGFSRTPTISDRNRLLLLEATIREV
LRLRPVAPMLIPHKANVDSSIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNP
AGTQLISPSVSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIP
KVVFLIDSFKVKIKVRQAWREAQAEGST
|
| Enzyme 33 Number of Residues |
508 |
| Enzyme 33 Molecular Weight |
57371 |
| Enzyme 33 Theoretical pI |
8.87 |
| Enzyme 33 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 33 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 33 Specific Function |
Conversion of pregnenolone and progesterone to their 17- alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved in sexual development during fetal life and at puberty |
| Enzyme 33 Pathways |
- C21 Steroid Hormone Metabolism (map00140
)
|
| Enzyme 33 Reactions |
- a steroid + AH2 + O2 = a 17alpha-hydroxysteroid + A + H2O
|
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
Not Available |
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
181342  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
P05093  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
CP17A_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>1527 bp
ATGTGGGAGCTCGTGGCTCTCTTGCTGCTTACCCTAGCTTATTTGTTTTGGCCCAAGAGA
AGGTGCCCTGGTGCCAAGTACCCCAAGAGCCTCCTGTCCCTGCCCCTGGTGGGCAGCCTG
CCATTCCTCCCCAGACATGGCCATATGCATAACAACTTCTTCAAGCTGCAGAAAAAATAT
GGCCCCATCTATTCTGTTCGTATGGGCACCAAGACTACAGTGATTGTCGGCCACCACCAG
CTGGCCAAGGAGGTGCTTATTAAGAAGGGCAAGGACTTCTCTGGGCGGCCTCAAATGGCA
ACTCTAGACATCGCGTCCAACAACCGTAAGGGTATCGCCTTCGCTGACTCTGGCGCACAC
TGGCAGCTGCATCGAAGGCTGGCGATGGCCACCTTTGCCCTGTTCAAGGATGGCGATCAG
AAGCTGGAGAAGATCATTTGTCAGGAAATCAGTACATTGTGTGATATGCTGGCCACCCAC
AACGGACAGTCCATAGACATCTCCTTTCCTGTCTTCGTGGCGGTAACCAATGTCATCTCC
TTGATCTGCTTCAATACCTCCTACAAGAATGGGGACCCTGAGTTGAATGTCATACAGAAT
TACAATGAAGGCATCATAGACAACCTGAGCAAAGACAGCCTGGTGGACCTAGTCCCCTGG
TTGAAGATTTTCCCCAACAAAACCCTGGAAAAATTAAAGAGCCATGTTAAAATACGAAAT
GATCTGCTGAATAAAATACTTGAAAATTACAAGGAGAAATTCCGGAGTGACTCTATCACC
AACATGCTGGACACACTGATGCAAGCCAAGATGAACTCAGATAATGGCAATGCTGGCCCA
GATCAAGATTCAGAGCTGCTTTCAGATAACCACATTCTCACCACCATAGGGGACATCTTT
GGGGCTGGCGTGGAGACCACCACCTCTGTGGTTAAATGGACCCTGGCCTTCCTGCTGCAC
AATCCTCAGGTGAAGAAGAAGCTCTACGAGGAGATTGACCAGAATGTGGGTTTCAGCCGC
ACACCAACTATCAGTGACCGTAACCGTCTCCTCCTGCTGGAGGCCACCATCCGAGAGGTG
CTTCGCCTCAGGCCCGTGGCCCCTATGCTCATCCCCCACAAGGCCAACGTTGACTCCAGC
ATCGGTGAGTTTGCTGTGGACAAGGGCACAGAAGTTATCATCAATCTGTGGGCGCTGCAT
CACAATGAGAAGGAGTGGCACCAGCCGGATCAGTTCATGCCTGAGCGTTTCTTGAATCCA
GCGGGGACCCAGCTCATCTCACCGTCAGTAAGCTATTTGCCCTTCGGAGCAGGACCTCGC
TCCTGTATAGGTGAGATCCTGGCCCGCCAGGAGCTCTTCCTCATCATGGCCTGGCTGCTG
CAGAGGTTCGACCTGGAGGTGCCAGATGATGGGCAGCTGCCCTCCCTGGAAGGCATCCCC
AAGGTGGTCTTTCTGATCGACTCTTTCAAAGTGAAGATCAAGGTGCGCCAGGCCTGGAGG
GAAGCCCAGGCTGAGGGTAGCACCTAA
|
| Enzyme 33 GenBank Gene ID |
M14564  |
| Enzyme 33 GeneCard ID |
CYP17A1  |
| Enzyme 33 GenAtlas ID |
CYP17A1  |
| Enzyme 33 HGNC ID |
HGNC:2593  |
| Enzyme 33 Chromosome Location |
10 |
| Enzyme 33 Locus |
10q24.3 |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
- Chung BC, Picado-Leonard J, Haniu M, Bienkowski M, Hall PF, Shively JE, Miller WL: Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): cloning of human adrenal and testis cDNAs indicates the same gene is expressed in both tissues. Proc Natl Acad Sci U S A. 1987 Jan;84(2):407-11. [PubMed
]
- Picado-Leonard J, Miller WL: Cloning and sequence of the human gene for P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): similarity with the gene for P450c21. DNA. 1987 Oct;6(5):439-48. [PubMed
]
- Bradshaw KD, Waterman MR, Couch RT, Simpson ER, Zuber MX: Characterization of complementary deoxyribonucleic acid for human adrenocortical 17 alpha-hydroxylase: a probe for analysis of 17 alpha-hydroxylase deficiency. Mol Endocrinol. 1987 May;1(5):348-54. [PubMed
]
- Brentano ST, Picado-Leonard J, Mellon SH, Moore CC, Miller WL: Tissue-specific, cyclic adenosine 3',5'-monophosphate-induced, and phorbol ester-repressed transcription from the human P450c17 promoter in mouse cells. Mol Endocrinol. 1990 Dec;4(12):1972-9. [PubMed
]
- Kagimoto M, Winter JS, Kagimoto K, Simpson ER, Waterman MR: Structural characterization of normal and mutant human steroid 17 alpha-hydroxylase genes: molecular basis of one example of combined 17 alpha-hydroxylase/17,20 lyase deficiency. Mol Endocrinol. 1988 Jun;2(6):564-70. [PubMed
]
- Auchus RJ, Miller WL: Molecular modeling of human P450c17 (17alpha-hydroxylase/17,20-lyase): insights into reaction mechanisms and effects of mutations. Mol Endocrinol. 1999 Jul;13(7):1169-82. [PubMed
]
- Yanase T, Kagimoto M, Suzuki S, Hashiba K, Simpson ER, Waterman MR: Deletion of a phenylalanine in the N-terminal region of human cytochrome P-450(17 alpha) results in partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1989 Oct 25;264(30):18076-82. [PubMed
]
- Lin D, Harikrishna JA, Moore CC, Jones KL, Miller WL: Missense mutation serine106----proline causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1991 Aug 25;266(24):15992-8. [PubMed
]
- Yanase T, Waterman MR, Zachmann M, Winter JS, Simpson ER, Kagimoto M: Molecular basis of apparent isolated 17,20-lyase deficiency: compound heterozygous mutations in the C-terminal region (Arg(496)----Cys, Gln(461)----Stop) actually cause combined 17 alpha-hydroxylase/17,20-lyase deficiency. Biochim Biophys Acta. 1992 Aug 25;1139(4):275-9. [PubMed
]
- Ahlgren R, Yanase T, Simpson ER, Winter JS, Waterman MR: Compound heterozygous mutations (Arg 239----stop, Pro 342----Thr) in the CYP17 (P45017 alpha) gene lead to ambiguous external genitalia in a male patient with partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Clin Endocrinol Metab. 1992 Mar;74(3):667-72. [PubMed
]
- Imai T, Globerman H, Gertner JM, Kagawa N, Waterman MR: Expression and purification of functional human 17 alpha-hydroxylase/17,20-lyase (P450c17) in Escherichia coli. Use of this system for study of a novel form of combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1993 Sep 15;268(26):19681-9. [PubMed
]
- Monno S, Ogawa H, Date T, Fujioka M, Miller WL, Kobayashi M: Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1993 Dec 5;268(34):25811-7. [PubMed
]
- Fardella CE, Zhang LH, Mahachoklertwattana P, Lin D, Miller WL: Deletion of amino acids Asp487-Ser488-Phe489 in human cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1993 Aug;77(2):489-93. [PubMed
]
- Fardella CE, Hum DW, Homoki J, Miller WL: Point mutation of Arg440 to His in cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1994 Jul;79(1):160-4. [PubMed
]
- Laflamme N, Leblanc JF, Mailloux J, Faure N, Labrie F, Simard J: Mutation R96W in cytochrome P450c17 gene causes combined 17 alpha-hydroxylase/17-20-lyase deficiency in two French Canadian patients. J Clin Endocrinol Metab. 1996 Jan;81(1):264-8. [PubMed
]
- Biason-Lauber A, Kempken B, Werder E, Forest MG, Einaudi S, Ranke MB, Matsuo N, Brunelli V, Schonle EJ, Zachmann M: 17alpha-hydroxylase/17,20-lyase deficiency as a model to study enzymatic activity regulation: role of phosphorylation. J Clin Endocrinol Metab. 2000 Mar;85(3):1226-31. [PubMed
]
- Gupta MK, Geller DH, Auchus RJ: Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency. J Clin Endocrinol Metab. 2001 Sep;86(9):4416-23. [PubMed
]
- Di Cerbo A, Biason-Lauber A, Savino M, Piemontese MR, Di Giorgio A, Perona M, Savoia A: Combined 17alpha-Hydroxylase/17,20-lyase deficiency caused by Phe93Cys mutation in the CYP17 gene. J Clin Endocrinol Metab. 2002 Feb;87(2):898-905. [PubMed
]
- Van Den Akker EL, Koper JW, Boehmer AL, Themmen AP, Verhoef-Post M, Timmerman MA, Otten BJ, Drop SL, De Jong FH: Differential inhibition of 17alpha-hydroxylase and 17,20-lyase activities by three novel missense CYP17 mutations identified in patients with P450c17 deficiency. J Clin Endocrinol Metab. 2002 Dec;87(12):5714-21. [PubMed
]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
6413 |
| Enzyme 34 Name |
Cyclic nucleotide-gated cation channel alpha 3 |
| Enzyme 34 Synonyms |
- CNG channel alpha 3
- CNG-3
- CNG3
- Cyclic nucleotide-gated channel alpha 3
- Cone photoreceptor cGMP-gated channel subunit alpha
|
| Enzyme 34 Gene Name |
CNGA3 |
| Enzyme 34 Protein Sequence |
>Cyclic nucleotide-gated cation channel alpha 3
MAKINTQYSHPSRTHLKVKTSDRDLNRAENGLSRAHSSSEETSSVLQPGIAMETRGLADS
GQGSFTGQGIARLSRLIFLLRRWAARHVHHQDQGPDSFPDRFRGAELKEVSSQESNAQAN
VGSQEPADRGRSAWPLAKCNTNTSNNTEEEKKTKKKDAIVVDPSSNLYYRWLTAIALPVF
YNWYLLICRACFDELQSEYLMLWLVLDYSADVLYVLDVLVRARTGFLEQGLMVSDTNRLW
QHYKTTTQFKLDVLSLVPTDLAYLKVGTNYPEVRFNRLLKFSRLFEFFDRTETRTNYPNM
FRIGNLVLYILIIIHWNACIYFAISKFIGFGTDSWVYPNISIPEHGRLSRKYIYSLYWST
LTLTTIGETPPPVKDEEYLFVVVDFLVGVLIFATIVGNVGSMISNMNASRAEFQAKIDSI
KQYMQFRKVTKDLETRVIRWFDYLWANKKTVDEKEVLKSLPDKLKAEIAINVHLDTLKKV
RIFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGKEMYIINEGKLAVVADDGVTQFVV
LSDGSYFGEISILNIKGSKSGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPEAKKALEE
KGRQILMKDNLIDEELARAGADPKDLEEKVEQLGSSLDTLQTRFARLLAEYNATQMKMKQ
RLSQLESQVKGGGDKPLADGEVPGDATKTEDKQQ
|
| Enzyme 34 Number of Residues |
694 |
| Enzyme 34 Molecular Weight |
78839 |
| Enzyme 34 Theoretical pI |
7.80 |
| Enzyme 34 GO Classification |
| Function |
- ion channel activity
- ion transporter activity
- transporter activity
- voltage-gated ion channel activity
- voltage-gated potassium channel activity
|
| Process |
- cation transport
- cellular physiological process
- ion transport
- monovalent inorganic cation transport
- physiological process
- potassium ion transport
- transport
|
| Component |
|
|
| Enzyme 34 General Function |
Signal transduction mechanisms |
| Enzyme 34 Specific Function |
Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of cone photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficacy of the channel when coexpressed with CNGB3. Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones |
| Enzyme 34 Pathways |
Not Available |
| Enzyme 34 Reactions |
Not Available |
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
3153887  |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
Q16281  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
CNGA3_HUMAN  |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>2085 bp
ATGGCCAAGATCAACACCCAATACTCCCACCCCTCCAGGACCCACCTCAAGGTAAAGACC
TCAGACCGAGATCTCAATCGCGCTGAAAATGGCCTCAGCAGAGCCCACTCGTCAAGTGAG
GAGACATCGTCAGTGCTGCAGCCGGGGATCGCCATGGAGACCAGAGGACTGGCTGACTCC
GGGCAGGGCTCCTTCACCGGCCAGGGGATCGCCAGGCTGTCGCGCCTCATCTTCTTGCTG
CGCAGGTGGGCTGCCAGGCATGTGCACCACCAGGACCAGGGACCGGACTCTTTTCCTGAT
CGTTTCCGTGGAGCCGAGCTTAAGGAGGTGTCCAGCCAAGAAAGCAATGCCCAGGCAAAT
GTGGGCAGCCAGGAGCCAGCAGACAGAGGGAGAAGCGCCTGGCCCCTGGCCAAATGCAAC
ACTAACACCAGCAACAACACGGAGGAGGAGAAGAAGACGAAAAAGAAGGATGCGATCGTG
GTGGACCCGTCCAGCAACCTGTACTACCGCTGGCTGACCGCCATCGCCCTGCCTGTCTTC
TATAACTGGTATCTGCTTATTTGCAGGGCCTGTTTCGATGAGCTGCAGTCCGAGTACCTG
ATGCTGTGGCTGGTCCTGGACTACTCGGCAGATGTCCTGTATGTCTTGGATGTGCTTGTA
CGAGCTCGGACAGGTTTTCTCGAGCAAGGCTTAATGGTCAGTGATACCAACAGGCTGTGG
CAGCATTACAAGACGACCACGCAGTTCAAGCTGGATGTGTTGTCCCTGGTCCCCACCGAC
CTGGCTTACTTAAAGGTGGGCACAAACTACCCAGAAGTGAGGTTCAACCGCCTACTGAAG
TTTTCCCGGCTCTTTGAATTCTTTGACCGCACAGAGACAAGGACCAACTACCCCAATATG
TTCAGGATTGGGAACTTGGTCTTGTACATTCTCATCATCATCCACTGGAATGCCTGCATC
TACTTTGCCATTTCCAAGTTCATTGGTTTTGGGACAGACTCCTGGGTCTACCCAAACATC
TCAATCCCAGAGCATGGGCGCCTCTCCAGGAAGTACATTTACAGTCTCTACTGGTCCACC
TTGACCCTTACCACCATTGGTGAGACCCCACCCCCCGTGAAAGATGAGGAGTATCTCTTT
GTGGTCGTAGACTTCTTGGTGGGTGTTCTGATTTTTGCCACCATTGTGGGCAATGTGGGC
TCCATGATCTCGAATATGAATGCCTCACGGGCAGAGTTCCAGGCCAAGATTGATTCCATC
AAGCAGTACATGCAGTTCCGCAAGGTCACCAAGGACTTGGAGACGCGGGTTATCCGGTGG
TTTGACTACCTGTGGGCCAACAAGAAGACGGTGGATGAGAAGGAGGTGCTCAAGAGCCTC
CCAGACAAGCTGAAGGCTGAGATCGCCATCAACGTGCACCTGGACACGCTGAAGAAGGTT
CGCATCTTCCAGGACTGTGAGGCAGGGCTGCTGGTGGAGCTGGTGCTGAAGCTGCGACCC
ACTGTGTTCAGCCCTGGGGATTATATCTGCAAGAAGGGAGATATTGGGAAGGAGATGTAC
ATCATCAACGAGGGCAAGCTGGCCGTGGTGGCTGATGATGGGGTCACCCAGTTCGTGGTC
CTCAGCGATGGCAGCTACTTCGGGGAGATCAGCATTCTGAACATCAAGGGGAGCAAGTCG
GGGAACCGCAGGACGGCCAACATCCGCAGCATTGGCTACTCAGACCTGTTCTGCCTCTCA
AAGGACGATCTCATGGAGGCCCTCACCGAGTACCCCGAAGCCAAGAAGGCCCTGGAGGAG
AAAGGACGGCAGATCCTGATGAAAGACAACCTGATCGATGAGGAGCTGGCCAGGGCGGGC
GCGGACCCCAAGGACCTTGAGGAGAAAGTGGAGCAGCTGGGGTCCTCCCTGGACACCCTG
CAGACCAGGTTTGCACGCCTCCTGGCTGAGTACAACGCCACCCAGATGAAGATGAAGCAG
CGTCTCAGCCAACTGGAAAGCCAGGTGAAGGGTGGTGGGGACAAGCCCCTGGCTGATGGG
GAAGTTCCCGGGGATGCTACAAAAACAGAGGACAAACAACAGTGA
|
| Enzyme 34 GenBank Gene ID |
AF065314  |
| Enzyme 34 GeneCard ID |
CNGA3  |
| Enzyme 34 GenAtlas ID |
CNGA3  |
| Enzyme 34 HGNC ID |
HGNC:2150  |
| Enzyme 34 Chromosome Location |
2 |
| Enzyme 34 Locus |
2q11.2 |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
- Wissinger B, Muller F, Weyand I, Schuffenhauer S, Thanos S, Kaupp UB, Zrenner E: Cloning, chromosomal localization and functional expression of the gene encoding the alpha-subunit of the cGMP-gated channel in human cone photoreceptors. Eur J Neurosci. 1997 Dec;9(12):2512-21. [PubMed
]
- Distler M, Biel M, Flockerzi V, Hofmann F: Expression of cyclic nucleotide-gated cation channels in non-sensory tissues and cells. Neuropharmacology. 1994 Nov;33(11):1275-82. [PubMed
]
- Sundin OH, Yang JM, Li Y, Zhu D, Hurd JN, Mitchell TN, Silva ED, Maumenee IH: Genetic basis of total colourblindness among the Pingelapese islanders. Nat Genet. 2000 Jul;25(3):289-93. [PubMed
]
- Kohl S, Marx T, Giddings I, Jagle H, Jacobson SG, Apfelstedt-Sylla E, Zrenner E, Sharpe LT, Wissinger B: Total colourblindness is caused by mutations in the gene encoding the alpha-subunit of the cone photoreceptor cGMP-gated cation channel. Nat Genet. 1998 Jul;19(3):257-9. [PubMed
]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
6416 |
| Enzyme 35 Name |
Cyclic nucleotide-gated cation channel beta 3 |
| Enzyme 35 Synonyms |
- CNG channel beta 3
- Cyclic nucleotide-gated channel beta 3
- Cone photoreceptor cGMP- gated channel subunit beta
- Cyclic nucleotide-gated cation channel modulatory subunit
|
| Enzyme 35 Gene Name |
CNGB3 |
| Enzyme 35 Protein Sequence |
>Cyclic nucleotide-gated cation channel beta 3
MFKSLTKVNKVKPIGENNENEQSSRRNEEGSHPSNQSQQTTAQEENKGEEKSLKTKSTPV
TSEEPHTNIQDKLSKKNSSGDLTTNPDPQNAAEPTGTVPEQKEMDPGKEGPNSPQNKPPA
APVINEYADAQLHNLVKRMRQRTALYKKKLVEGDLSSPEASPQTAKPTAVPPVKESDDKP
TEHYYRLLWFKVKKMPLTEYLKRIKLPNSIDSYTDRLYLLWLLLVTLAYNWNCWFIPLRL
VFPYQTADNIHYWLIADIICDIIYLYDMLFIQPRLQFVRGGDIIVDSNELRKHYRTSTKF
QLDVASIIPFDICYLFFGFNPMFRANRMLKYTSFFEFNHHLESIMDKAYIYRVIRTTGYL
LFILHINACVYYWASNYEGIGTTRWVYDGEGNEYLRCYYWAVRTLITIGGLPEPQTLFEI
VFQLLNFFSGVFVFSSLIGQMRDVIGAATANQNYFRACMDDTIAYMNNYSIPKLVQKRVR
TWYEYTWDSQRMLDESDLLKTLPTTVQLALAIDVNFSIISKVDLFKGCDTQMIYDMLLRL
KSVLYLPGDFVCKKGEIGKEMYIIKHGEVQVLGGPDGTKVLVTLKAGSVFGEISLLAAGG
GNRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILMKKARVLLKQKAKTAEATPPRK
DLALLFPPKEETPKLFKTLLGGTGKASLARLLKLKREQAAQKKENSEGGEEEGKENEDKQ
KENEDKQKENEDKGKENEDKDKGREPEEKPLDRPECTASPIAVEEEPHSVRRTVLPRGTS
RQSLIISMAPSAEGGEEVLTIEVKEKAKQ
|
| Enzyme 35 Number of Residues |
809 |
| Enzyme 35 Molecular Weight |
92251 |
| Enzyme 35 Theoretical pI |
8.11 |
| Enzyme 35 GO Classification |
| Function |
- ion channel activity
- ion transporter activity
- transporter activity
|
| Process |
- cellular physiological process
- ion transport
- physiological process
- transport
|
| Component |
|
|
| Enzyme 35 General Function |
Signal transduction mechanisms |
| Enzyme 35 Specific Function |
Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cGMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficiency of the channel when coexpressed with CNGA3. Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones |
| Enzyme 35 Pathways |
Not Available |
| Enzyme 35 Reactions |
Not Available |
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
- 217-237
251-271
303-323
360-380
418-438
505-525
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
9247066  |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
Q9NQW8  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
CNGB3_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>2430 bp
ATGTTTAAATCGCTGACAAAAGTCAACAAGGTGAAGCCTATAGGAGAGAACAATGAGAAT
GAACAAAGTTCTCGTCGGAATGAAGAAGGCTCTCACCCAAGTAATCAGTCTCAGCAAACC
ACAGCACAGGAAGAAAACAAAGGTGAAGAGAAATCTCTCAAAACCAAGTCAACTCCAGTC
ACGTCTGAAGAGCCACACACCAACATACAAGACAAACTCTCCAAGAAAAATTCCTCTGGA
GATCTGACCACAAACCCTGACCCTCAAAATGCAGCAGAACCAACTGGAACAGTGCCAGAG
CAGAAGGAAATGGACCCCGGGAAAGAAGGTCCAAACAGCCCACAAAACAAACCGCCTGCA
GCTCCTGTTATAAATGAGTATGCCGATGCCCAGCTACACAACCTGGTGAAAAGAATGCGT
CAAAGAACAGCCCTCTACAAGAAAAAGTTGGTAGAGGGAGATCTCTCCTCACCCGAAGCC
AGCCCACAAACTGCAAAGCCCACGGCTGTACCACCAGTAAAAGAAAGCGATGATAAGCCA
ACAGAACATTACTACAGGCTGTTGTGGTTCAAAGTCAAAAAGATGCCTTTAACAGAGTAC
TTAAAGCGAATTAAACTTCCAAACAGCATAGATTCATACACAGATCGACTCTATCTCCTG
TGGCTCTTGCTTGTCACTCTTGCCTATAACTGGAACTGCTGGTTTATACCACTGCGCCTC
GTCTTCCCATATCAAACCGCAGACAACATACACTACTGGCTTATTGCGGACATCATATGT
GATATCATCTACCTTTATGATATGCTATTTATCCAGCCCAGACTCCAGTTTGTAAGAGGA
GGAGACATAATAGTGGATTCAAATGAGCTAAGGAAACACTACAGGACTTCTACAAAATTT
CAGTTGGATGTCGCATCAATAATACCATTTGATATTTGCTACCTCTTCTTTGGGTTTAAT
CCAATGTTTAGAGCAAATAGGATGTTAAAGTACACTTCATTTTTTGAATTTAATCATCAC
CTAGAGTCTATAATGGACAAAGCATATATCTACAGAGTTATTCGAACAACTGGATACTTG
CTGTTTATTCTGCACATTAATGCCTGTGTTTATTACTGGGCTTCAAACTATGAAGGAATT
GGCACTACTAGATGGGTGTATGATGGGGAAGGAAACGAGTATCTGAGATGTTATTATTGG
GCAGTTCGAACTTTAATTACCATTGGTGGCCTTCCAGAACCACAAACTTTATTTGAAATT
GTTTTTCAACTCTTGAATTTTTTTTCTGGAGTTTTTGTGTTCTCCAGTTTAATTGGTCAG
ATGAGAGATGTGATTGGAGCAGCTACAGCCAATCAGAACTACTTCCGCGCCTGCATGGAT
GACACCATTGCCTACATGAACAATTACTCCATTCCTAAACTTGTGCAAAAGCGAGTTCGG
ACTTGGTATGAATATACATGGGACTCTCAAAGAATGCTAGATGAGTCTGATTTGCTTAAG
ACCCTACCAACTACGGTCCAGTTAGCCCTCGCCATTGATGTGAACTTCAGCATCATCAGC
AAAGTCGACTTGTTCAAGGGTTGTGATACACAGATGATTTATGACATGTTGCTAAGATTG
AAATCCGTTCTCTATTTGCCTGGTGACTTTGTCTGCAAAAAGGGAGAAATTGGCAAGGAA
ATGTATATCATCAAGCATGGAGAAGTCCAAGTTCTTGGAGGCCCTGATGGTACTAAAGTT
CTGGTTACTCTGAAAGCTGGGTCGGTGTTTGGAGAAATCAGCCTTCTAGCAGCAGGAGGA
GGAAACCGTCGAACTGCCAATGTGGTGGCCCACGGGTTTGCCAATCTTTTAACTCTAGAC
AAAAAGACCCTCCAAGAAATTCTAGTGCATTATCCAGATTCTGAAAGGATCCTCATGAAG
AAAGCCAGAGTGCTTTTAAAGCAGAAGGCTAAGACCGCAGAAGCAACCCCTCCAAGAAAA
GATCTTGCCCTCCTCTTCCCACCGAAAGAAGAGACACCCAAACTGTTTAAAACTCTCCTA
GGAGGCACAGGAAAAGCAAGTCTTGCAAGACTACTCAAATTGAAGCGAGAGCAAGCAGCT
CAGAAGAAAGAAAATTCTGAAGGAGGAGAGGAAGAAGGAAAAGAAAATGAAGATAAACAA
AAAGAAAATGAAGATAAACAAAAAGAAAATGAAGATAAAGGAAAAGAAAATGAAGATAAA
GATAAAGGAAGAGAGCCAGAAGAGAAGCCACTGGACAGACCTGAATGTACAGCAAGTCCT
ATTGCAGTGGAGGAAGAACCCCACTCAGTTAGAAGGACAGTTTTACCCAGAGGGACTTCT
CGTCAATCACTCATTATCAGCATGGCTCCTTCTGCTGAGGGCGGAGAAGAGGTTCTTACT
ATTGAAGTCAAAGAAAAGGCTAAGCAATAA
|
| Enzyme 35 GenBank Gene ID |
AF272900  |
| Enzyme 35 GeneCard ID |
CNGB3  |
| Enzyme 35 GenAtlas ID |
CNGB3  |
| Enzyme 35 HGNC ID |
HGNC:2153  |
| Enzyme 35 Chromosome Location |
8 |
| Enzyme 35 Locus |
8q21-q22 |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 General References |
- Kohl S, Baumann B, Broghammer M, Jagle H, Sieving P, Kellner U, Spegal R, Anastasi M, Zrenner E, Sharpe LT, Wissinger B: Mutations in the CNGB3 gene encoding the beta-subunit of the cone photoreceptor cGMP-gated channel are responsible for achromatopsia (ACHM3) linked to chromosome 8q21. Hum Mol Genet. 2000 Sep 1;9(14):2107-16. [PubMed
]
- Sundin OH, Yang JM, Li Y, Zhu D, Hurd JN, Mitchell TN, Silva ED, Maumenee IH: Genetic basis of total colourblindness among the Pingelapese islanders. Nat Genet. 2000 Jul;25(3):289-93. [PubMed
]
|
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
6417 |
| Enzyme 36 Name |
Rap guanine nucleotide exchange factor 2 |
| Enzyme 36 Synonyms |
- Neural RAP guanine nucleotide exchange protein
- nRap GEP
- PDZ domain-containing guanine nucleotide exchange factor 1
- PDZ-GEF1
- RA-GEF
|
| Enzyme 36 Gene Name |
RAPGEF2 |
| Enzyme 36 Protein Sequence |
>Rap guanine nucleotide exchange factor 2
MKPLAIPANHGVMGQQEKHSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLS
DIYQATESEAGDMDLSGLPETAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTD
DDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAGTIVLNDGEELDSWSVILNGS
VEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEK
NMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLL
TYRTFLSSPMEVGKKLLEWFNDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENN
LEREKMGGHLRLLNIACAAKAKRRLMTLTKPSREAPLPFILLGGSEKGFGIFVDSVDSGS
KATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEE
KRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKT
RISILPQKPYNDIGIGQSQDDSIVGLRQTKHIPTALPVSGTLSSSNPDLLQSHHRILDFS
ATPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIREFAVTATPDQYSLCEVSVTPE
GVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVE
VATQLSMRNFELFRNIEPTEYIDDLFKLRSKTSCANLKRFEEVINQETFWVASEILRETN
QLKRMKIIKHFIKIALHCRECKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDL
QDLFDPSRNMAKYRNVLNSQNLQPPIIPLFPVIKKDLTFLHEGNDSKVDGLVNFEKLRMI
AKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSTNATVLDVAQTGGHKKRVRRSS
FLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATNTLPKNPGDKKPVKSE
TSPVAPRAGSQQKAQSLPQPQQQPPPAHKINQGLQVPAVSLYPSRKKVPVKDLPPFGINS
PQALKKILSLSEEGSLERHKKQAEDTISNASSQLSSPPTSPQSSPRKGYTLAPSGTVDNF
SDSGHSEISSRSSIVSNSSFDSVPVSLHDERRQRHSVSIVETNLGMGRMERRTMIEPDQY
SLGSYAPMSEGRGLYATATVISSPSTEELSQDQGDRASLDAADSGRGSWTSCSSGSHDNI
QTIQHQRSWETLPFGHTHFDYSGDPAGLWASSSHMDQIMFSDHSTKYNRQNQSRESLEQA
QSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSIEAESSSLTSVTTEETKPVPMPAHIAV
ASSTTKGLIARKEGRYREPPPTPPGYIGIPITDFPEGHSHPARKPPDYNVALQRSRMVAR
SSDTAGPSSVQQPHGHPTSSRPVNKPQWHKPNESDPRLAPYQSQGFSTEEDEDEQVSAV
|
| Enzyme 36 Number of Residues |
1499 |
| Enzyme 36 Molecular Weight |
167419 |
| Enzyme 36 Theoretical pI |
6.64 |
| Enzyme 36 GO Classification |
| Function |
- GTPase regulator activity
- binding
- enzyme regulator activity
- guanyl-nucleotide exchange factor activity
- protein binding
- small GTPase regulator activity
|
| Process |
- cell communication
- cellular process
- intracellular signaling cascade
- signal transduction
- small GTPase mediated signal transduction
|
| Component |
| — |
|
| Enzyme 36 General Function |
Not Available |
| Enzyme 36 Specific Function |
Guanine nucleotide exchange factor (GEF) for Rap1A, Rap1B and Rap2B GTPases. Does not interact with cAMP or cGMP |
| Enzyme 36 Pathways |
Not Available |
| Enzyme 36 Reactions |
Not Available |
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
40788210  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
Q9Y4G8  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
RPGF2_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>4527 bp
ATTCAGTTCAGCATATGTTTCTTCATTATGAAACCACTAGCAATCCCAGCTAACCATGGA
GTTATGGGCCAGCAGGAGAAACACTCACTTCCTGCAGATTTCACAAAACTGCATCTTACT
GACAGTCTCCACCCACAGGTGACCCACGTTTCTTCTAGCCATTCAGGATGTAGTATCACT
AGTGATTCTGGGAGCAGCAGTCTTTCTGATATCTACCAGGCCACAGAAAGCGAGGCTGGT
GATATGGACCTGAGTGGGTTGCCAGAAACAGCAGTGGATTCCGAAGACGACGACGATGAA
GAAGACATTGAGAGAGCATCAGATCCTCTGATGAGCAGGGACATTGTGAGAGACTGCCTA
GAGAAGGACCCAATTGACCGGACAGATGATGACATTGAACAACTCTTGGAATTTATGCAC
CAGTTGCCTGCTTTTGCCAATATGACAATGTCAGTGAGGCGAGAACTCTGTGCTGTGATG
GTGTTCGCAGTGGTGGAAAGAGCAGGGACCATAGTGTTAAATGATGGTGAAGAGCTGGAC
TCCTGGTCAGTGATTCTCAATGGATCTGTGGAAGTGACTTATCCAGATGGAAAAGCAGAA
ATACTGTGCATGGGAAATAGTTTTGGTGTCTCTCCTACCATGGACAAAGAATACATGAAA
GGAGTGATGAGAACAAAGGTGGATGACTGCCAGTTTGTCTGCATAGCCCAGCAAGATTAC
TGCCGTATTCTCAATCAAGTAGAAAAGAACATGCAAAAAGTTGAAGAGGAAGGAGAGATT
GTTATGGTGAAAGAACACCGAGAACTTGATCGAACTGGAACAAGAAAGGGACACATTGTC
ATCAAGGGTACCTCAGAAAGGTTAACAATGCATTTGGTGGAAGAGCATTCAGTAGTAGAT
CCAACATTCATAGAAGACTTTCTGTTGACCTATAGGACTTTTCTTTCTAGCCCAATGGAA
GTGGGCAAAAAGTTATTGGAGTGGTTTAATGACCCGAGCCTCAGGGATAAGGTTACACGG
GTAGTATTATTGTGGGTAAATAATCACTTCAATGACTTTGAAGGAGATCCTGCAATGACT
CGATTTTTAGAAGAATTTGAAAACAATCTGGAAAGAGAGAAAATGGGTGGACACCTAAGG
CTGTTGAATATCGCGTGTGCTGCTAAAGCAAAAAGAAGATTGATGACGTTAACAAAACCA
TCCCGAGAAGCTCCTTTGCCTTTTATCTTACTTGGAGGCTCTGAGAAGGGATTTGGAATC
TTTGTTGACAGTGTAGATTCAGGTAGCAAAGCAACTGAAGCAGGCTTGAAACGGGGGGAT
CAGATATTAGAAGTAAATGGCCAAAACTTTGAAAACATTCAGCTGTCAAAAGCTATGGAA
ATTCTTAGAAATAACACACATTTATCTATCACTGTGAAAACCAATTTATTTGTATTTAAA
GAACTTCTAACAAGATTGTCAGAAGAGAAAAGAAATGGTGCCCCCCACCTTCCTAAAATT
GGTGACATTAAAAAGGCCAGTCGCTACTCCATTCCAGATCTTGCTGTAGATGTAGAACAG
GTGATAGGACTTGAAAAAGTGAACAAAAAAAGTAAAGCCAACACTGTGGGAGGAAGGAAC
AAGCTGAAAAAGATACTCGACAAGACTCGGATCAGTATCTTGCCACAGAAACCATACAAT
GATATTGGGATTGGTCAGTCTCAAGATGACAGCATAGTAGGATTAAGGCAGACAAAGCAC
ATCCCAACTGCATTGCCTGTCAGTGGAACCTTATCATCCAGTAATCCTGATTTATTGCAG
TCACATCATCGCATTTTAGACTTCAGTGCTACTCCTGACTTGCCAGATCAAGTGCTAAGG
GTTTTTAAGGCTGATCAGCAAAGCCGCTACATCATGATCAGTAAGGACACTACAGCAAAG
GAAGTGGTCATTCAGGCTATCAGGGAGTTTGCTGTTACTGCCACCCCGGATCAATATTCA
CTATGTGAGGTCTCTGTCACACCTGAGGGAGTAATCAAACAAAGAAGACTTCCAGATCAG
CTTTCCAAACTTGCAGACAGAATACAACTGAGTGGAAGGTATTATCTGAAAAACAACATG
GAAACAGAAACTCTTTGTTCAGATGAAGATGCTCAGGAGTTGTTGAGAGAGAGTCAAATT
TCCCTCCTTCAGCTCAGCACTGTGGAAGTTGCAACACAGCTCTCTATGCGAAATTTTGAA
CTCTTTCGCAACATTGAACCTACTGAATATATAGATGATTTATTTAAACTCAGATCAAAA
ACCAGCTGTGCCAACCTGAAGAGATTTGAAGAAGTCATTAACCAGGAAACATTTTGGGTA
GCATCTGAAATTCTCAGAGAAACAAACCAGCTGAAGAGGATGAAGATCATTAAGCATTTC
ATCAAGATAGCACTGCACTGTAGGGAATGCAAGAATTTTAACTCAATGTTTGCAATCATC
AGTGGCCTAAACCTGGCACCAGTGGCAAGACTGCGAACGACCTGGGAGAAACTTCCCAAT
AAATACGAAAAACTATTTCAAGATCTCCAAGACCTGTTTGATCCTTCCAGAAACATGGCA
AAATATCGTAATGTTCTCAATAGTCAAAATCTACAACCTCCCATAATCCCTCTATTCCCA
GTTATCAAAAAGGATCTCACCTTCCTTCACGAAGGAAATGACTCAAAAGTAGACGGGCTG
GTCAATTTTGAGAAGCTAAGGATGATTGCAAAAGAAATTCGTCACGTTGGCCGAATGGCT
TCAGTGAACATGGACCCTGCCCTCATGTTCAGGACTCGGAAGAAGAAATGGCGGAGTTTG
GGGTCTCTCAGCCAGGGTAGTACAAATGCAACAGTGCTAGATGTTGCTCAGACAGGTGGT
CATAAAAAGCGGGTACGTCGTAGTTCCTTTCTCAATGCCAAAAAGCTTTATGAAGATGCC
CAAATGGCTCGAAAAGTGAAGCAGTACCTTTCCAATTTGGAGCTAGAAATGGACGAGGAG
AGTCTTCAGACATTATCTCTGCAGTGTGAGCCAGCAACCAACACATTGCCTAAGAATCCT
GGTGACAAAAAGCCTGTCAAATCCGAGACCTCTCCAGTAGCTCCAAGGGCAGGGTCACAA
CAGAAAGCTCAGTCCCTGCCACAGCCCCAGCAGCAGCCACCACCAGCACATAAAATCAAC
CAGGGACTACAGGTTCCCGCCGTGTCCCTTTATCCTTCACGGAAGAAAGTGCCCGTAAAG
GATCTCCCACCTTTTGGCATAAACTCTCCACAAGCTTTAAAAAAAATTCTTTCTTTGTCT
GAAGAAGGAAGTTTGGAACGTCACAAGAAACAGGCTGAAGATACAATATCAAATGCATCT
TCGCAGCTTTCTTCTCCTCCTACTTCTCCACAGAGTTCTCCAAGGAAAGGCTATACTTTG
GCTCCCAGTGGTACTGTGGATAATTTTTCAGATTCTGGTCACAGTGAAATTTCTTCACGA
TCCAGTATTGTTAGCAATTCGTCTTTTGACTCAGTGCCAGTCTCACTGCACGATGAGAGG
CGCCAGAGGCATTCTGTCAGCATCGTGGAAACAAACCTAGGGATGGGCAGGATGGAGAGG
CGGACCATGATTGAACCTGATCAGTATAGCTTGGGGTCCTATGCACCAATGTCCGAGGGC
CGAGGCTTATATGCTACAGCTACAGTAATTTCTTCTCCAAGCACAGAGGAACTTTCCCAG
GATCAGGGGGATCGCGCGTCACTTGATGCTGCTGACAGTGGCCGTGGGAGCTGGACGTCA
TGCTCAAGTGGCTCCCATGATAATATACAGACGATCCAGCACCAGAGAAGCTGGGAGACT
CTTCCATTCGGGCATACTCACTTTGATTATTCAGGGGATCCTGCAGGTTTATGGGCATCA
AGCAGCCATATGGACCAAATTATGTTTTCTGATCATAGCACAAAGTATAACAGGCAAAAT
CAAAGTAGAGAGAGCCTTGAACAAGCCCAGTCCCGAGCAAGCTGGGCGTCTTCCACAGGT
TACTGGGGAGAAGACTCAGAAGGTGACACAGGCACAATAAAGCGGAGGGGTGGAAAGGAT
GTTTCCATTGAAGCCGAAAGCAGTAGCCTAACGTCTGTGACTACGGAAGAAACCAAGCCT
GTCCCCATGCCTGCCCACATAGCTGTGGCATCAAGTACTACAAAGGGGCTCATTGCACGA
AAGGAGGGCAGGTATCGAGAGCCCCCGCCCACCCCTCCCGGCTACATTGGAATTCCCATT
ACTGACTTTCCAGAAGGGCACTCCCATCCAGCCAGGAAACCGCCGGACTACAACGTGGCC
CTTCAGAGATCGCGGATGGTCGCACGATCCTCCGACACAGCTGGGCCTTCATCCGTACAG
CAGCCACATGGGCATCCCACCAGCAGCAGGCCTGTGAACAAACCTCAGTGGCATAAACCG
AACGAGTCTGACCCGCGCCTCGCCCCTTATCAGTCCCAAGGGTTTTCCACCGAGGAGGAT
GAAGATGAACAAGTTTCTGCTGTTTGA
|
| Enzyme 36 GenBank Gene ID |
AB002311  |
| Enzyme 36 GeneCard ID |
RAPGEF2  |
| Enzyme 36 GenAtlas ID |
RAPGEF2  |
| Enzyme 36 HGNC ID |
HGNC:16854  |
| Enzyme 36 Chromosome Location |
4 |
| Enzyme 36 Locus |
4q32.1 |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
- Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed
]
- de Rooij J, Boenink NM, van Triest M, Cool RH, Wittinghofer A, Bos JL: PDZ-GEF1, a guanine nucleotide exchange factor specific for Rap1 and Rap2. J Biol Chem. 1999 Dec 31;274(53):38125-30. [PubMed
]
- Rebhun JF, Castro AF, Quilliam LA: Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction. J Biol Chem. 2000 Nov 10;275(45):34901-8. [PubMed
]
|
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
6420 |
| Enzyme 37 Name |
Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 |
| Enzyme 37 Synonyms |
- Brain cyclic nucleotide-gated channel 1
- BCNG-1
|
| Enzyme 37 Gene Name |
HCN1 |
| Enzyme 37 Protein Sequence |
>Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
MEGGGKPNSSSNSRDDGNSVFPAKASATGAGPAAAEKRLGTPPGGGGAGAKEHGNSVCFK
VDGGGGGGGGGGGGEEPAGGFEDAEGPRRQYGFMQRQFTSMLQPGVNKFSLRMFGSQKAV
EKEQERVKTAGFWIIHPYSDFRFYWDLIMLIMMVGNLVIIPVGITFFTEQTTTPWIIFNV
ASDTVFLLDLIMNFRTGTVNEDSSEIILDPKVIKMNYLKSWFVVDFISSIPVDYIFLIVE
KGMDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFN
LIGMMLLLCHWDGCLQFLVPLLQDFPPDCWVSLNEMVNDSWGKQYSYALFKAMSHMLCIG
YGAQAPVSMSDLWITMLSMIVGATCYAMFVGHATALIQSLDSSRRQYQEKYKQVEQYMSF
HKLPADMRQKIHDYYEHRYQGKIFDEENILNELNDPLREEIVNFNCRKLVATMPLFANAD
PNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVITKSSKEMKLTDGSYFGE
ICLLTKGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSI
LLQKFQKDLNTGVFNNQENEILKQIVKHDREMVQAIAPINYPQMTTLNSTSSTTTPTSRM
RTQSPPVYTATSLSHSNLHSPSPSTQTPQPSAILSPCSYTTAVCSPPVQSPLAARTFHYA
SPTASQLSLMQQQPQQQVQQSQPPQTQPQQPSPQPQTPGSSTPKNEVHKSTQALHNTNLT
REVRPFSAWQPSLPHEVSTLISRPHPTVGESLASIPQPVTAVPGTGLQAGGRSTVPQRVT
LFRQMSSGAIPPNRGVPPAPPPPAAALPRESSSVLNTDPDAEKPRFASNL
|
| Enzyme 37 Number of Residues |
890 |
| Enzyme 37 Molecular Weight |
98930 |
| Enzyme 37 Theoretical pI |
8.54 |
| Enzyme 37 GO Classification |
| Function |
- ion channel activity
- ion transporter activity
- transporter activity
- voltage-gated ion channel activity
- voltage-gated potassium channel activity
|
| Process |
- cation transport
- cellular physiological process
- ion transport
- monovalent inorganic cation transport
- physiological process
- potassium ion transport
- transport
|
| Component |
|
|
| Enzyme 37 General Function |
Signal transduction mechanisms |
| Enzyme 37 Specific Function |
Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Activated by cAMP, and at 10-100 times higher concentrations, also by cGMP. May mediate responses to sour stimuli |
| Enzyme 37 Pathways |
Not Available |
| Enzyme 37 Reactions |
Not Available |
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
- 147-167
174-194
220-240
249-269
301-321
345-366
372-392
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
Not Available |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
O60741  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
HCN1_HUMAN  |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
Not Available |
| Enzyme 37 GenBank Gene ID |
AC114975  |
| Enzyme 37 GeneCard ID |
HCN1  |
| Enzyme 37 GenAtlas ID |
HCN1  |
| Enzyme 37 HGNC ID |
HGNC:4845  |
| Enzyme 37 Chromosome Location |
5 |
| Enzyme 37 Locus |
5p12 |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
- Santoro B, Liu DT, Yao H, Bartsch D, Kandel ER, Siegelbaum SA, Tibbs GR: Identification of a gene encoding a hyperpolarization-activated pacemaker channel of brain. Cell. 1998 May 29;93(5):717-29. [PubMed
]
|
| Enzyme 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
6503 |
| Enzyme 38 Name |
cAMP-dependent protein kinase, gamma-catalytic subunit |
| Enzyme 38 Synonyms |
- PKA C-gamma
|
| Enzyme 38 Gene Name |
PRKACG |
| Enzyme 38 Protein Sequence |
>cAMP-dependent protein kinase, gamma-catalytic subunit
MGNAPAKKDTEQEESVNEFLAKARGDFLYRWGNPAQNTASSDQFERLRTLGMGSFGRVML
VRHQETGGHYAMKILNKQKVVKMKQVEHILNEKRILQAIDFPFLVKLQFSFKDNSYLYLV
MEYVPGGEMFSRLQRVGRFSEPHACFYAAQVVLAVQYLHSLDLIHRDLKPENLLIDQQGY
LQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAVGFPPFY
ADQPIQIYEKIVSGRVRFPSKLSSDLKHLLRSLLQVDLTKRFGNLRNGVGDIKNHKWFAT
TSWIAIYEKKVEAPFIPKYTGPGDASNFDDYEEEELRISINEKCAKEFSEF
|
| Enzyme 38 Number of Residues |
351 |
| Enzyme 38 Molecular Weight |
40435 |
| Enzyme 38 Theoretical pI |
8.89 |
| Enzyme 38 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleotide binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid phosphorylation
- protein modification
|
| Component |
| — |
|
| Enzyme 38 General Function |
Not Available |
| Enzyme 38 Specific Function |
Phosphorylates a large number of substrates in the cytoplasm and the nucleus |
| Enzyme 38 Pathways |
Not Available |
| Enzyme 38 Reactions |
Not Available |
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
189987  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
P22612  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
KAPCG_HUMAN  |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>1083 bp
ATGGCGGCCCCTGCCGCCGCCACCGCCATGGGCAACGCCCCCGCCAAGAAGGACACCGAG
CAGGAGGAGAGCGTGAACGAGTTCCTAGCCAAAGCCAGAGGAGATTTCCTCTACAGATGG
GGAAACCCCGCTCAAAACACCGCCAGCTCGGATCAGTTCGAACGGCTCAGGACGCTGGGC
ATGGGCTCCTTCGGGCGGGTGATGCTGGTGAGGCACCAGGAGACCGGCGGCCACTACGCC
ATGAAGATCCTCAACAAGCAGAAGGTGGTGAAGATGAAGCAGGTCGAGCACATACTGAAC
GAGAAGCGCATCCTGCAGGCGATCGACTTTCCGTTCCTCGTCAAGCTCCAGTTCTCCTTT
AAGGACAACTCCTACCTGTACCTGGTGATGGAGTACGTGCCGGGTGGGGAGATGTTCTCC
CGCCTACAGCGCGTCGGAAGGTTTAGCGAGCCCCATGCCTGTTTCTATGCCGCCCAGGTC
GTCCTGGCCGTCCAGTACCTACACTCGCTCGACCTCATCCACCGCGACCTGAAGCCCGAG
AATCTCCTCATCGACCAGCAGGGCTACCTGCAGGTGACGGACTTCGGTTTCGCCAAGCGC
GTGAAGGGCCGCACTTGGACCTTGTGCGGGACCCCAGAGTACCTGGCCCCCGAGATCATC
CTGAGCAAAGGCTACAACAAGGCCGTGGACTGGTGGGCCCTAGGGGTGCTCATCTATGAG
ATGGCCGTGGGCTTCCCACCCTTCTACGCCGACCAGCCCATCCAGATCTACGAGAAGATC
GTCTCTGGGAGGGTGCGGTTTCCCTCCAAACTCAGCTCTGACCTCAAGGATCTGCTGCGG
AGCCTGCTGCAGGTGGACCTCACCAAGCGCTTCGGAAACCTCAGGAACGGGGTTGGCGAC
ATCAAGAACCACAAGTGGTTCGCCACAACCAGCTGGATCGCCATCTATGAGAAGAAGGTG
GAAGCTCCCTTCATCCCGAAGTACACAGGCCCTGGGGATGCCAGTAACTTTGACGACTAC
GAGGAGGAAGAGCTCCGGATCTCCATCAATGAGAAGTGTGCCAAGGAGTTTTCTGAGTTT
TAG
|
| Enzyme 38 GenBank Gene ID |
M34182  |
| Enzyme 38 GeneCard ID |
PRKACG  |
| Enzyme 38 GenAtlas ID |
PRKACG  |
| Enzyme 38 HGNC ID |
HGNC:9382  |
| Enzyme 38 Chromosome Location |
9 |
| Enzyme 38 Locus |
9q13 |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 General References |
- Beebe SJ, Oyen O, Sandberg M, Froysa A, Hansson V, Jahnsen T: Molecular cloning of a tissue-specific protein kinase (C gamma) from human testis--representing a third isoform for the catalytic subunit of cAMP-dependent protein kinase. Mol Endocrinol. 1990 Mar;4(3):465-75. [PubMed
]
- Reinton N, Haugen TB, Orstavik S, Skalhegg BS, Hansson V, Jahnsen T, Tasken K: The gene encoding the C gamma catalytic subunit of cAMP-dependent protein kinase is a transcribed retroposon. Genomics. 1998 Apr 15;49(2):290-7. [PubMed
]
|
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
6648 |
| Enzyme 39 Name |
cAMP-dependent protein kinase, alpha-catalytic subunit |
| Enzyme 39 Synonyms |
- PKA C-alpha
|
| Enzyme 39 Gene Name |
PRKACA |
| Enzyme 39 Protein Sequence |
>cAMP-dependent protein kinase, alpha-catalytic subunit
MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVML
VKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMV
MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGY
IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF
ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFAT
TDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
|
| Enzyme 39 Number of Residues |
351 |
| Enzyme 39 Molecular Weight |
40590 |
| Enzyme 39 Theoretical pI |
9.22 |
| Enzyme 39 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleotide binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid phosphorylation
- protein modification
|
| Component |
| — |
|
| Enzyme 39 General Function |
Not Available |
| Enzyme 39 Specific Function |
Phosphorylates a large number of substrates in the cytoplasm and the nucleus |
| Enzyme 39 Pathways |
Not Available |
| Enzyme 39 Reactions |
Not Available |
| Enzyme 39 Pfam Domain Function |
|
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
35479  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
P17612  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
KAPCA_HUMAN  |
| Enzyme 39 PDB ID |
1CTP  |
| Enzyme 39 PDB File |
Show |
| Enzyme 39 3D Structure |
|
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>1056 bp
ATGGGCAACGCCGCCGCCGCCAAGAAGGGCAGCGAGCAGGAGAGCGTGAAAGAATTCTTA
GCCAAAGCCAAAGAAGATTTTCTTAAAAAATGGGAAAGTCCCGCTCAGAACACAGCCCAC
TTGGATCAGTTTGAACGAATCAAGACCCTCGGCACGGGCTCCTTCGGGCGGGTGATGCTG
GTGAAACACAAGGAGACCGGGAACCACTATGCCATGAAGATCCTCGACAAACAGAAGGTG
GTGAAACTGAAACAGATCGAACACACCCTGAATGAAAAGCGCATCCTGCAAGCTGTCAAC
TTTCCGTTCCTCGTCAAACTCGAGTTCTCCTTCAAGGACAACTCAAACTTATACATGGTC
ATGGAGTACGTGCCCGGCGGGGAGATGTTCTCACACCTACGGCGGATCGGAAGGTTCAGT
GAGCCCCATGCCCGTTTCTACGCGGCCCAGATCGTCCTGACCTTTGAGTATCTGCACTCG
CTGGATCTCATCTACAGGGACCTGAAGCCGGAGAATCTGCTCATTGACCAGCAGGGCTAC
ATTCAGGTGACAGACTTCGGTTTCGCCAAGCGCGTGAAGGGCCGCACTTGGACCTTGTGC
GGCACCCCTGAGTACCTGGCCCCTGAGATTATCCTGAGCAAAGGCTACAACAAGGCCGTG
GACTGGTGGGCCCTGGGGGTTCTTATCTATGAAATGGCCGCTGGCTACCCGCCCTTCTTC
GCAGACCAGCCCATCCAGATCTATGAGAAGATCGTCTCTGGGAAGGTGCGCTTCCCTTCC
CACTTCAGCTCTGACTTGAAGGACCTGCTGCGGAACCTCCTGCAGGTAGATCTCACCAAG
CGCTTTGGGAACCTCAAGAATGGGGTCAACGATATCAAGAACCACAAGTGGTTTGCCACA
ACTGACTGGATTGCCATCTACCAGAGGAAGGTGGAAGCTCCCTTCATACCAAAGTTTAAA
GGCCCTGGGGATACGAGTAACTTTGACGACTATGAGGAAGAAGAAATCCGGGTCTCCATC
AATGAGAAGTGTGGCAAGGAGTTTTCTGAGTTTTAG
|
| Enzyme 39 GenBank Gene ID |
X07767  |
| Enzyme 39 GeneCard ID |
PRKACA  |
| Enzyme 39 GenAtlas ID |
PRKACA  |
| Enzyme 39 HGNC ID |
HGNC:9380  |
| Enzyme 39 Chromosome Location |
19 |
| Enzyme 39 Locus |
19p13.1 |
| Enzyme 39 SNPs |
SNPJam Report  |
| Enzyme 39 General References |
- Maldonado F, Hanks SK: A cDNA clone encoding human cAMP-dependent protein kinase catalytic subunit C alpha. Nucleic Acids Res. 1988 Aug 25;16(16):8189-90. [PubMed
]
- Agustin JT, Wilkerson CG, Witman GB: The unique catalytic subunit of sperm cAMP-dependent protein kinase is the product of an alternative Calpha mRNA expressed specifically in spermatogenic cells. Mol Biol Cell. 2000 Sep;11(9):3031-44. [PubMed
]
- Desseyn JL, Burton KA, McKnight GS: Expression of a nonmyristylated variant of the catalytic subunit of protein kinase A during male germ-cell development. Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6433-8. [PubMed
]
|
| Enzyme 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
6695 |
| Enzyme 40 Name |
Serine/threonine-protein kinase PRKY |
| Enzyme 40 Synonyms |
Not Available |
| Enzyme 40 Gene Name |
PRKY |
| Enzyme 40 Protein Sequence |
>Serine/threonine-protein kinase PRKY
MEAPGPAQAAAAESNSREVTEDAADWAPALCPSPEARSPEAPAYRLQDCDALVTMGTGTF
GRVHLVKEKTAKHFFALKVMSIPDVIRRKQEQHVHNEKSVLKEVSHPFLIRLFWTWHEER
FLYMLMEYVPGGELFSYLRNRGHFSSTTGLFYSAEIICAIEYLHSKEIVYRDLKPENILL
DRDGHIKLTDFGFAKKLVDRTWTLCGTPEYLAPEVIQSKGHGRAVDWWALGILIFEMLSG
FPPFFDDNPFGIYQKILAGKLYFPRHLDFHVKTGRMM
|
| Enzyme 40 Number of Residues |
277 |
| Enzyme 40 Molecular Weight |
31709 |
| Enzyme 40 Theoretical pI |
6.96 |
| Enzyme 40 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleotide binding
- protein kinase activity
- protein serine/threonine kinase activity
- protein-tyrosine kinase activity
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid phosphorylation
- protein modification
|
| Component |
| — |
|
| Enzyme 40 General Function |
Not Available |
| Enzyme 40 Specific Function |
ATP + a protein = ADP + a phosphoprotein |
| Enzyme 40 Pathways |
Not Available |
| Enzyme 40 Reactions |
Not Available |
| Enzyme 40 Pfam Domain Function |
|
| Enzyme 40 Signals |
|
| Enzyme 40 Transmembrane Regions |
|
| Enzyme 40 Essentiality |
Not Available |
| Enzyme 40 GenBank ID Protein |
2695984  |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
O43930  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
PRKY_HUMAN  |
| Enzyme 40 PDB ID |
Not Available |
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
>166 bp
ATGGAGGCGCCCGGGCCGGCCCAGGCGGCCGCGGCGGAGAGCAACTCCCGAGAGGTGACG
GAGGATGCCGCCGACTGGGCGCCCGCGCTCTGCCCCAGCCCCGAGGCGCGGTCGCCGGAG
GCGCCTGCCTACCGCCTGCAGGACTGCGACGCGCTGGTCACCATGG
|
| Enzyme 40 GenBank Gene ID |
Y13927  |
| Enzyme 40 GeneCard ID |
PRKY  |
| Enzyme 40 GenAtlas ID |
PRKY  |
| Enzyme 40 HGNC ID |
HGNC:9444  |
| Enzyme 40 Chromosome Location |
Y |
| Enzyme 40 Locus |
Yp11.2 |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 General References |
- Schiebel K, Winkelmann M, Mertz A, Xu X, Page DC, Weil D, Petit C, Rappold GA: Abnormal XY interchange between a novel isolated protein kinase gene, PRKY, and its homologue, PRKX, accounts for one third of all (Y+)XX males and (Y-)XY females. Hum Mol Genet. 1997 Oct;6(11):1985-9. [PubMed
]
- Schiebel K, Mertz A, Winkelmann M, Glaser B, Schempp W, Rappold G: FISH localization of the human Y-homolog of protein kinase PRKX (PRKY) to Yp11.2 and two pseudogenes to 15q26 and Xq12-->q13. Cytogenet Cell Genet. 1997;76(1-2):49-52. [PubMed
]
|
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
6711 |
| Enzyme 41 Name |
cAMP-dependent protein kinase, beta-catalytic subunit |
| Enzyme 41 Synonyms |
- PKA C-beta
|
| Enzyme 41 Gene Name |
PRKACB |
| Enzyme 41 Protein Sequence |
>cAMP-dependent protein kinase, beta-catalytic subunit
MGNAATAKKGSEVESVKEFLAKAKEDFLKKWENPTQNNAGLEDFERKKTLGTGSFGRVML
VKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVRLEYAFKDNSNLYMV
MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY
IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF
ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFAT
TDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEDIRVSITEKCAKEFGEF
|
| Enzyme 41 Number of Residues |
351 |
| Enzyme 41 Molecular Weight |
40623 |
| Enzyme 41 Theoretical pI |
9.19 |
| Enzyme 41 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleotide binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid phosphorylation
- protein modification
|
| Component |
| — |
|
| Enzyme 41 General Function |
Not Available |
| Enzyme 41 Specific Function |
Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux |
| Enzyme 41 Pathways |
Not Available |
| Enzyme 41 Reactions |
Not Available |
| Enzyme 41 Pfam Domain Function |
|
| Enzyme 41 Signals |
|
| Enzyme 41 Transmembrane Regions |
|
| Enzyme 41 Essentiality |
Not Available |
| Enzyme 41 GenBank ID Protein |
189983  |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
P22694  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
KAPCB_HUMAN  |
| Enzyme 41 PDB ID |
1CTP  |
| Enzyme 41 PDB File |
Show |
| Enzyme 41 3D Structure |
|
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
>1056 bp
ATGGGGAACGCGGCGACCGCCAAGAAAGGCAGCGAGGTGGAGAGCGTGAAAGAGTTTCTA
GCCAAAGCCAAAGAAGACTTTTTGAAAAAATGGGAGAATCCAACTCAGAATAATGCCGGA
CTTGAAGATTTTGAAAGGAAAAAAACCCTTGGAACAGGTTCATTTGGAAGAGTCATGTTG
GTAAAACACAAAGCCACTGAACAGTATTATGCCATGAAGATCTTAGATAAGCAGAAGGTT
GTTAAACTGAAGCAAATAGAGCATACTTTGAATGAGAAAAGAATATTACAGGCAGTGAAT
TTTCCTTTCCTTGTTCGACTGGAGTATGCTTTTAAGGATAATTCTAATTTATACATGGTT
ATGGAATATGTCCCTGGGGGTGAAATGTTTTCACATCTAAGAAGAATTGGAAGGTTCAGT
GAGCCCCATGCACGGTTCTATGCAGCTCAGATAGTGCTAACATTCGAGTACCTCCATTCA
CTAGACCTCATCTACAGAGATCTAAAACCTGAAAATCTCTTAATTGACCATCAAGGCTAT
ATCCAGGTCACAGACTTTGGGTTTGCCAAAAGAGTTAAAGGCAGAACTTGGACATTATGT
GGAACTCCAGAGTATTTGGCTCCAGAAATAATTCTCAGCAAGGGCTACAATAAGGCAGTG
GATTGGTGGGCATTAGGAGTGCTAATCTATGAAATGGCAGCTGGCTATCCCCCATTCTTT
GCAGACCAACCAATTCAGATTTATGAAAAGATTGTTTCTGGAAAGGTCCGATTCCCATCC
CACTTCAGTTCAGATCTCAAGGACCTTCTACGGAACCTGCTGCAGGTGGATTTGACCAAG
AGATTTGGAAATCTAAAGAATGGTGTCAGTGATATAAAAACTCACAAGTGGTTTGCCACG
ACAGATTGGATTGCTATTTACCAGAGGAAGGTTGAAGCTCCATTCATACCAAAGTTTAGA
GGCTCTGGAGATACCAGCAACTTTGATGACTATGAAGAAGAAGATATCCGTGTCTCTATA
ACAGAAAAATGTGCAAAAGAATTTGGTGAATTTTAA
|
| Enzyme 41 GenBank Gene ID |
M34181  |
| Enzyme 41 GeneCard ID |
PRKACB  |
| Enzyme 41 GenAtlas ID |
PRKACB  |
| Enzyme 41 HGNC ID |
HGNC:9381  |
| Enzyme 41 Chromosome Location |
1 |
| Enzyme 41 Locus |
1p36.1 |
| Enzyme 41 SNPs |
SNPJam Report  |
| Enzyme 41 General References |
- Beebe SJ, Oyen O, Sandberg M, Froysa A, Hansson V, Jahnsen T: Molecular cloning of a tissue-specific protein kinase (C gamma) from human testis--representing a third isoform for the catalytic subunit of cAMP-dependent protein kinase. Mol Endocrinol. 1990 Mar;4(3):465-75. [PubMed
]
- Orstavik S, Reinton N, Frengen E, Langeland BT, Jahnsen T, Skalhegg BS: Identification of novel splice variants of the human catalytic subunit Cbeta of cAMP-dependent protein kinase. Eur J Biochem. 2001 Oct;268(19):5066-73. [PubMed
]
|
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
6787 |
| Enzyme 42 Name |
Ribosomal protein S6 kinase alpha-5 |
| Enzyme 42 Synonyms |
- Nuclear mitogen- and stress-activated protein kinase 1
- 90 kDa ribosomal protein S6 kinase 5
- RSK-like protein kinase
- RSKL
|
| Enzyme 42 Gene Name |
RPS6KA5 |
| Enzyme 42 Protein Sequence |
>Ribosomal protein S6 kinase alpha-5
MEEEGGSSGGAAGTSADGGDGGEQLLTVKHELRTANLTGHAEKVGIENFELLKVLGTGAY
GKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYA
FQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKL
ENILLDSNGHVVLTDFGLSKEFVADETERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWS
LGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQRLLMKDPKK
RLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYS
PAALPQSSEKLFQGYSFVAPSILFKRNAAVIDPLQFHMGVERPGVTNVARSAMMKDSPFY
QHYDLDLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEGHPN
IVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGV
VHRDLKPENLLFTDENDNLEIKIIDFGFARLKPPDNQPLKTPCFTLHYAAPELLNQNGYD
ESCDLWSLGVILYTMLSGQVPFQSHDRSLTCTSAVEIMKKIKKGDFSFEGEAWKNVSQEA
KDLIQGLLTVDPNKRLKMSGLRYNEWLQDGSQLSSNPLMTPDILGSSGAAVHTCVKATFH
AFNKYKREGFCLQNVDKAPLAKRRKMKKTSTSTETRSSSSESSHSSSSHSHGKTTPTKTL
QPSNPADSNNPETLFQFSDSVA
|
| Enzyme 42 Number of Residues |
802 |
| Enzyme 42 Molecular Weight |
89866 |
| Enzyme 42 Theoretical pI |
7.10 |
| Enzyme 42 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleotide binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid phosphorylation
- protein modification
|
| Component |
| — |
|
| Enzyme 42 General Function |
Not Available |
| Enzyme 42 Specific Function |
Serine/threonine kinase required for the mitogen or stress-induced phosphorylation of the transcription factors CREB (cAMP response element-binding protein) and ATF1 (activating transcription factor-1). Essential role in the control of RELA transcriptional activity in response to TNF. Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and epidemal growth-factor (EGF), which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 14 (HMG-14) |
| Enzyme 42 Pathways |
Not Available |
| Enzyme 42 Reactions |
Not Available |
| Enzyme 42 Pfam Domain Function |
|
| Enzyme 42 Signals |
|
| Enzyme 42 Transmembrane Regions |
|
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
3411157  |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
O75582  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
KS6A5_HUMAN  |
| Enzyme 42 PDB ID |
Not Available |
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
>2409 bp
ATGGAGGAGGAGGGTGGCAGCAGCGGCGGCGCCGCGGGGACCAGCGCGGACGGCGGCGAC
GGAGGAGAGCAGCTCCTCACTGTCAAGCACGAGCTGCGGACTGCTAATTTGACAGGACAT
GCTGAGAAGGTGGGAATAGAAAATTTTGAGCTCCTGAAGGTCCTAGGAACTGGAGCTTAT
GGAAAAGTATTTCTAGTTCGTAAAATAAGTGGCCATGATACTGGAAAGCTGTATGCCATG
AAAGTTTTGAAAAAGGCAACAATCGTTCAAAAGGCCAAAACCACAGAGCATACAAGGACA
GAACGACAAGTCCTGGAACACATTAGGCAGTCGCCATTTTTGGTAACATTACATTATGCT
TTCCAGACAGAAACCAAACTTCATCTCATTTTAGATTATATAAATGGTGGTGAACTTTTT
ACTCATCTTTCTCAAAGAGAGCGTTTCACAGAGCATGAGGTGCAGATTTATGTTGGAGAG
ATTGTGCTTGCCCTCGAACATCTCCACAAGTTGGGGATTATATATCGTGATATTAAGCTT
GAGAATATTCTACTTGATTCTAATGGCCATGTGGTGCTGACAGATTTTGGTCTGAGTAAG
GAGTTTGTGGCTGATGAAACTGAAAGAGCATATTCCTTTTGTGGAACTATTGAATACATG
GCACCAGATATTGTCAGAGGGGGAGATTCAGGACATGACAAGGCAGTTGACTGGTGGAGT
TTGGGTGTTCTAATGTATGAATTACTAACTGGAGCATCTCCTTTCACTGTTGATGGAGAA
AAAAATTCCCAAGCTGAGATATCTAGGAGAATATTAAAAAGTGAGCCTCCATATCCCCAA
GAAATGAGTGCTTTAGCGAAAGACCTAATTCAGCGTCTTTTGATGAAAGATCCCAAGAAG
AGATTGGGATGTGGTCCACGTGATGCAGATGAAATCAAAGAACATCTCTTCTTTCAGAAA
ATAAATTGGGATGATTTAGCCGCCAAAAAAGTGCCTGCACCATTTAAGCCAGTCATTCGA
GATGAATTAGATGTGAGTAACTTTGCAGAAGAGTTCACAGAAATGGATCCCACTTATTCT
CCCGCAGCCCTGCCCCAGAGTTCTGAGAAGCTGTTTCAGGGCTATTCCTTTGTTGCTCCT
TCCATCCTATTCAAGCGTAATGCAGCTGTCATAGACCCTCTTCAGTTTCACATGGGAGTT
GAACGTCCTGGAGTGACAAATGTTGCCAGGAGTGCAATGATGAAGGACTCTCCATTCTAT
CAACACTATGACCTAGATTTGAAGGACAAACCCCTGGGAGAAGGTAGTTTTTCAATTTGT
CGAAAGTGTGTGCATAAAAAAAGTAACCAAGCTTTTGCAGTCAAAATAATCAGCAAAAGG
ATGGAAGCCAATACTCAAAAGGAAATAACAGCTCTGAAACTCTGTGAAGGACACCCCAAT
ATTGTGAAGTTGCATGAAGTTTTTCATGATCAGCTTCACACGTTTCTAGTGATGGAACTT
CTGAATGGAGGAGAACTGTTTGAGCGCATTAAGAAAAAGAAGCACTTCAGTGAGACGGAA
GCCAGCTACATCATGAGGAAGCTTGTTTCAGCTGTAAGCCACATGCATGATGTTGGAGTG
GTGCACAGGGATCTGAAACCTGAGAATTTATTGTTCACCGATGAAAATGACAATTTGGAA
ATTAAAATAATTGATTTTGGATTTGCACGGCTAAAGCCACCGGATAATCAGCCCCTGAAG
ACTCCATGCTTCACCCTTCATTATGCCGCCCCAGAGCTCTTGAATCAGAACGGCTACGAT
GAGTCCTGTGACCTGTGGAGCTTGGGCGTCATTTTGTACACAATGTTGTCAGGACAGGTT
CCCTTCCAATCTCATGACCGAAGTTTGACGTGTACCAGCGCGGTGGAAATCATGAAGAAA
ATTAAAAAGGGAGATTTCTCCTTTGAAGGAGAAGCCTGGAAGAATGTATCCCAAGAGGCT
AAAGATTTGATCCAAGGACTTCTCACAGTAGATCCAAACAAAAGGCTTAAAATGTCTGGC
TTGAGGTACAATGAATGGCTACAAGATGGAAGTCAGCTGTCCTCCAATCCTCTGATGACT
CCGGATATTCTAGGATCTTCCGGAGCTGCCGTGCATACCTGTGTGAAAGCAACCTTCCAC
GCCTTTAACAAATACAAGAGAGAGGGGTTTTGCCTTCAGAATGTTGATAAGGCCCCTTTG
GCTAAGAGAAGAAAAATGAAAAAGACTAGCACCAGTACCGAGACGCGCAGCAGTTCCAGT
GAGAGTTCCCATTCTTCTTCCTCTCATTCTCACGGTAAAACTACACCCACCAAGACACTG
CAGCCCAGCAATCCTGCCGACAGCAATAACCCGGAGACCCTCTTCCAGTTCTCGGACTCA
GTAGCTTAG
|
| Enzyme 42 GenBank Gene ID |
AF074393  |
| Enzyme 42 GeneCard ID |
RPS6KA5  |
| Enzyme 42 GenAtlas ID |
RPS6KA5  |
| Enzyme 42 HGNC ID |
HGNC:10434  |
| Enzyme 42 Chromosome Location |
14 |
| Enzyme 42 Locus |
14q31-q32.1 |
| Enzyme 42 SNPs |
SNPJam Report  |
| Enzyme 42 General References |
- Deak M, Clifton AD, Lucocq LM, Alessi DR: Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. EMBO J. 1998 Aug 3;17(15):4426-41. [PubMed
]
- New L, Zhao M, Li Y, Bassett WW, Feng Y, Ludwig S, Padova FD, Gram H, Han J: Cloning and characterization of RLPK, a novel RSK-related protein kinase. J Biol Chem. 1999 Jan 8;274(2):1026-32. [PubMed
]
- Jiang C, Yu L, Tu Q, Zhao Y, Zhang H, Zhao S: Assignment of a member of the ribosomal protein S6 kinase family, RPS6KA5, to human chromosome 14q31-->q32.1 by radiation hybrid mapping. Cytogenet Cell Genet. 1999;87(3-4):261-2. [PubMed
]
- Vermeulen L, De Wilde G, Van Damme P, Vanden Berghe W, Haegeman G: Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1). EMBO J. 2003 Mar 17;22(6):1313-24. [PubMed
]
|
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
6794 |
| Enzyme 43 Name |
Serine/threonine-protein kinase PRKX |
| Enzyme 43 Synonyms |
- Protein kinase PKX1
|
| Enzyme 43 Gene Name |
PRKX |
| Enzyme 43 Protein Sequence |
>Serine/threonine-protein kinase PRKX
MEAPGLAQAAAAESDSRKVAEETPDGAPALCPSPEALSPEPPVYSLQDFDTLATVGTGTF
GRVHLVKEKTAKHFFALKVMSIPDVIRLKQEQHVHNEKSVLKEVSHPFLIRLFWTWHDER
FLYMLMEYVPGGELFSYLRNRGRFSSTTGLFYSAEIICAIEYLHSKEIVYRDLKPENILL
DRDGHIKLTDFGFAKKLVDRTWTLCGTPEYLAPEVIQSKGHGRAVDWWALGILIFEMLSG
FPPFFDDNPFGIYQKILAGKIDFPRHLDFHVKDLIKKLLVVDRTRRLGNMKNGANDVKHH
RWFRSVDWEAVPQRKLKPPIVPKIAGDGDTSNFETYPENDWDTAAPVPQKDLEIFKNF
|
| Enzyme 43 Number of Residues |
358 |
| Enzyme 43 Molecular Weight |
40896 |
| Enzyme 43 Theoretical pI |
6.85 |
| Enzyme 43 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleotide binding
- protein kinase activity
- protein serine/threonine kinase activity
- protein-tyrosine kinase activity
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid phosphorylation
- protein modification
|
| Component |
| — |
|
| Enzyme 43 General Function |
Not Available |
| Enzyme 43 Specific Function |
ATP + a protein = ADP + a phosphoprotein |
| Enzyme 43 Pathways |
Not Available |
| Enzyme 43 Reactions |
Not Available |
| Enzyme 43 Pfam Domain Function |
|
| Enzyme 43 Signals |
|
| Enzyme 43 Transmembrane Regions |
|
| Enzyme 43 Essentiality |
Not Available |
| Enzyme 43 GenBank ID Protein |
1052737  |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
P51817  |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
PRKX_HUMAN  |
| Enzyme 43 PDB ID |
Not Available |
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
>1077 bp
ATGGAGGCGCCCGGGCTGGCCCAGGCGGCCGCGGCGGAGAGCGACTCCCGCAAGGTGGCG
GAGGAGACCCCCGACGGGGCGCCCGCGCTCTGCCCCAGCCCTGAGGCGCTGTCGCCGGAG
CCGCCTGTGTACAGCCTGCAGGACTTTGACACGCTGGCCACCGTGGGCACTGGGACGTTC
GGGCGGGTGCACCTGGTGAAGGAGAAGACAGCCAAGCATTTCTTCGCCCTCAAGGTGATG
AGCATTCCTGACGTCATCCGCCTAAAGCAGGAGCAACACGTACACAATGAGAAGTCTGTC
CTGAAGGAAGTCAGCCACCCGTTCCTCATCAGGCTGTTCTGGACGTGGCATGACGAGCGC
TTCCTCTACATGCTCATGGAGTACGTGCCGGGCGGCGAGCTCTTCAGCTACCTGCGCAAC
CGGGGGCGCTTCTCCAGCACCACGGGGCTCTTCTACTCTGCAGAGATCATCTGTGCCATC
GAGTACCTGCACTCCAAAGAGATCGTCTACAGGGACTTGAAGCCAGAGAACATCCTGCTG
GATAGGGATGGCCACATTAAGCTCACGGACTTTGGGTTCGCCAAGAAGCTGGTAGACAGG
ACTTGGACCCTCTGTGGAACACCCGAGTACCTAGCCCCCGAAGTCATTCAGAGCAAGGGC
CACGGAAGGGCCGTGGACTGGTGGGCCCTCGGCATCCTGATATTCGAGATGCTTTCGGGG
TTTCCTCCGTTTTTTGATGACAACCCGTTTGGCATTTATCAGAAAATTCTTGCAGGCAAA
ATAGATTTCCCCAGACATTTGGATTTCCATGTAAAAGACCTCATTAAGAAACTGCTCGTG
GTTGACAGAACAAGGCGATTAGGAAACATGAAGAACGGGGCGAATGATGTGAAGCATCAT
CGGTGGTTCCGCTCCGTGGACTGGGAAGCTGTTCCGCAGAGAAAACTGAAGCCTCCCATC
GTGCCCAAGATAGCTGGTGACGGCGACACTTCCAACTTCGAAACTTACCCTGAGAATGAC
TGGGACACAGCCGCGCCCGTGCCGCAGAAGGATTTAGAAATCTTCAAGAATTTCTGA
|
| Enzyme 43 GenBank Gene ID |
X85545  |
| Enzyme 43 GeneCard ID |
PRKX  |
| Enzyme 43 GenAtlas ID |
PRKX  |
| Enzyme 43 HGNC ID |
HGNC:9441  |
| Enzyme 43 Chromosome Location |
X |
| Enzyme 43 Locus |
Xp22.3 |
| Enzyme 43 SNPs |
SNPJam Report  |
| Enzyme 43 General References |
- Klink A, Schiebel K, Winkelmann M, Rao E, Horsthemke B, Ludecke HJ, Claussen U, Scherer G, Rappold G: The human protein kinase gene PKX1 on Xp22.3 displays Xp/Yp homology and is a site of chromosomal instability. Hum Mol Genet. 1995 May;4(5):869-78. [PubMed
]
- Schiebel K, Winkelmann M, Mertz A, Xu X, Page DC, Weil D, Petit C, Rappold GA: Abnormal XY interchange between a novel isolated protein kinase gene, PRKY, and its homologue, PRKX, accounts for one third of all (Y+)XX males and (Y-)XY females. Hum Mol Genet. 1997 Oct;6(11):1985-9. [PubMed
]
|
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
6826 |
| Enzyme 44 Name |
Serine/threonine-protein kinase 11 |
| Enzyme 44 Synonyms |
- Serine/threonine- protein kinase LKB1
- Renal carcinoma antigen NY-REN-19
|
| Enzyme 44 Gene Name |
STK11 |
| Enzyme 44 Protein Sequence |
>Serine/threonine-protein kinase 11
MEVVDPQQLGMFTEGELMSVGMDTFIHRIDSTEVIYQPRRKRAKLIGKYLMGDLLGEGSY
GKVKEVLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRHKNVIQLVDVLYNE
EKQKMYMVMEYCVCGMQEMLDSVPEKRFPVCQAHGYFCQLIDGLEYLHSQGIVHKDIKPG
NLLLTTGGTLKISDLGVAEALHPFAADDTCRTSQGSPAFQPPEIANGLDTFSGFKVDIWS
AGVTLYNITTGLYPFEGDNIYKLFENIGKGSYAIPGDCGPPLSDLLKGMLEYEPAKRFSI
RQIRQHSWFRKKHPPAEAPVPIPPSPDTKDRWRSMTVVPYLEDLHGADEDEDLFDIEDDI
IYTQDFTVPGQVPEEEASHNGQRRGLPKAVCMNGTEAAQLSTKSRAEGRAPNPARKACSA
SSKIRRLSACKQQ
|
| Enzyme 44 Number of Residues |
433 |
| Enzyme 44 Molecular Weight |
48636 |
| Enzyme 44 Theoretical pI |
7.47 |
| Enzyme 44 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleotide binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid phosphorylation
- protein modification
|
| Component |
| — |
|
| Enzyme 44 General Function |
Not Available |
| Enzyme 44 Specific Function |
Essential role in G1 cell cycle arrest. Phosphorylates and activates members of the AMPK-related subfamily of protein kinases. Tumor suppressor |
| Enzyme 44 Pathways |
Not Available |
| Enzyme 44 Reactions |
Not Available |
| Enzyme 44 Pfam Domain Function |
|
| Enzyme 44 Signals |
|
| Enzyme 44 Transmembrane Regions |
|
| Enzyme 44 Essentiality |
Not Available |
| Enzyme 44 GenBank ID Protein |
2754827  |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
Q15831  |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
STK11_HUMAN  |
| Enzyme 44 PDB ID |
Not Available |
| Enzyme 44 Cellular Location |
Not Available |
| Enzyme 44 Gene Sequence |
>1302 bp
ATGGAGGTGGTGGACCCGCAGCAGC |