|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5232 |
| Enzyme 1 Name |
Cytosolic 5'-nucleotidase 1B |
| Enzyme 1 Synonyms |
- Cytosolic 5'-nucleotidase IB
- cN1B
- cN-IB
- Autoimmune infertility-related protein
|
| Enzyme 1 Gene Name |
NT5C1B |
| Enzyme 1 Protein Sequence |
>Cytosolic 5'-nucleotidase 1B
MSQTSLKQKKNEPGMRSSKESLEAEKRKESDKTGVRLSNQMRRAVNPNHSLRCCPFQGHS
SCRRCLCAAEGTALGPCHTIRIYIHMCLLWEQGQQITMMRGSQESSLRKTDSRGYLVRSQ
WSRISRSPSTKAPSIDEPRSRNTSAKLPSSSTSSRTPSTSPSLHDSSPPPLSGQPSLQPP
ASPQLPRSLDSRPPTPPEPDPGSRRSTKMQENPEAWAQGIVREIRQTRDSQPLEYSRTSP
TEWKSSSQRRGIYPASTQLDRNSLSEQQQQQREDEDDYEAAYWASMRSFYEKNPSCSRPW
PPKPKNAITIALSSCALFNMVDGRKIYEQEGLEKYMEYQLTNENVILTPGPAFRFVKALQ
YVNARLRDLYPDEQDLFDIVLMTNNHAQVGVRLINSVNHYGLLIDRFCLTGGKDPIGYLK
AYLTNLYIAADSEKVQEAIQEGIASATMFDGAKDMAYCDTQLRVAFDGDAVLFSDESEHF
TKEHGLDKFFQYDTLCESKPLAQGPLKGFLEDLGRLQKKFYAKNERLLCPIRTYLVTARS
AASSGARVLKTLRRWGLEIDEALFLAGAPKSPILVKIRPHIFFDDHMFHIEGAQRLGSIA
AYGFNKKFSS
|
| Enzyme 1 Number of Residues |
610 |
| Enzyme 1 Molecular Weight |
68804 |
| Enzyme 1 Theoretical pI |
9.03 |
| Enzyme 1 GO Classification |
| Function |
- 5'-nucleotidase activity
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- magnesium ion binding
- metal ion binding
- nucleotidase activity
- nucleotide binding
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 1 General Function |
Not Available |
| Enzyme 1 Specific Function |
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Helps to regulate adenosine levels |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
13774961  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q96P26  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
5NT1B_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1699 bp
GGGCAAAAATGTGGATAACAACAAAAGAATTTCAACAGGTAAAAAAATGAGTCAAACATC
TCTCAAACAGAAAAAGAATGAGCCCGGAATGAGGTCCTCAAAAGAGAGTCTAGAAGCAGA
AAAAAGAAAGGAATCTGACAAAACAGGAGTTCGTCTGAGCAATCAGGGATCACAAGAATC
ATCACTGCGGAAGACAGACTCTCGAGGGTACCTTGTGCGCAGTCAATGGTCTAGAATATC
CCGGAGCCCATCCACCAAGGCTCCATCCATAGATGAGCCTAGAAGCAGGAACACCAGTGC
TAAGCTCCCCAGCAGCTCCACGAGCTCCCGGACTCCATCCACCTCCCCAAGCCTGCATGA
CTCCTCACCGCCGCCGCTGTCCGGGCAGCCCTCGCTCCAGCCACCCGCGTCGCCCCAGCT
GCCCCGGTCGCTGGACTCGCGGCCTCCCACGCCCCCAGAGCCCGATCCTGGCTCCCGGCG
CAGCACCAAAATGCAAGAAAATCCGGAGGCCTGGGCCCAAGGCATCGTGCGGGAAATCCG
CCAGACCCGGGACTCGCAGCCGCTGGAATATTCGCGCACGTCCCCCACCGAGTGGAAGTC
CTCCAGCCAGCGCAGGGGGATCTACCCCGCCTCCACCCAGCTGGACCGCAACTCTCTGTC
CGAGCAGCAGCAGCAGCAGCGGGAGGACGAAGACGACTACGAAGCTGCCTACTGGGCATC
CATGAAGTCGTTCTACGAAAAGAACCCGAGCTGCTGGCGCCCCTGGCCGCCCAAACCCAA
GAACGCCATCACCATTGCTCTCTCATCCTGCGCGCTCTTCAACATGGTGGACGGCAGGAA
AATCTACGAGCAAGAGGGTCTGGAAAAGTACATGGAGTATCAGCTCACCAATGAGAACGT
CATCCTGACCCCGGGCCCGGCGTTCCGTTTCGTCAAGGCACTACAGTATGTCAATGCTAG
ACTCCGTGATCTATATCCTGATGAACAGGACTTATTTGATATTGTACTGATGACTAATAA
CCATGCCCAAGTGGGAGTGCGGCTTATAAACAGCGTCAATCACTACGGCTTACTGATTGA
CCGCTTCTGTCTGACCGGGGGAAAAGACCCCATTGGCTATTTGAAGGCATATCTTACCAA
CTTGTATATTGCTGCAGATTCTGAAAAAGTGCAAGAGGCAATACAAGAAGGTATTGCCTC
TGCGACAATGTTTGATGGAGCCAAAGACATGGCTTACTGTGACACTCAGCTCCGTGTAGC
CTTTGATGGGGATGCTGTCCTCTTCTCTGATGAGTCTGAACATTTTACCAAGGAGCATGG
GCTGGACAAATTCTTCCAGTATGATACATTATGTGAAAGTAAGCCTCTTGCTCAGGGTCC
CCTAAAAGGCTTTCTGGAAGATTTAGGCAGACTGCAAAAGAAGTTCTATGCCAAAAATGA
ACGGTTACTTTGTCCTATCAGGACCTACCTGGTTACAGCTAGGAGTGCAGCCAGTTCAGG
CGCCCGTGTGCTGAAAACCTTCCGACGCTGGGGTCTAGAGATAGACGAAGCTCTTTTCCT
TGCTGGAGCCCCCAAAAGTCCCATCTTGGTGAAGATCCGGCCCCACATCTTCTTTGATGA
CCACATGTTCCACATTGAAGGGGCACAGAGGTTAGGTTCCATCGCAGCTTATGGCTTTAA
TAAAAAATTCAGTAGTTAG
|
| Enzyme 1 GenBank Gene ID |
AF356185  |
| Enzyme 1 GeneCard ID |
NT5C1B  |
| Enzyme 1 GenAtlas ID |
NT5C1B  |
| Enzyme 1 HGNC ID |
HGNC:17818  |
| Enzyme 1 Chromosome Location |
2 |
| Enzyme 1 Locus |
2p24.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Sala-Newby GB, Newby AC: Cloning of a mouse cytosolic 5'-nucleotidase-I identifies a new gene related to human autoimmune infertility-related protein. Biochim Biophys Acta. 2001 Oct 31;1521(1-3):12-8. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5233 |
| Enzyme 2 Name |
Cytosolic 5'-nucleotidase 1A |
| Enzyme 2 Synonyms |
- Cytosolic 5'-nucleotidase IA
- cN1A
- cN-IA
- cN-I
|
| Enzyme 2 Gene Name |
NT5C1A |
| Enzyme 2 Protein Sequence |
>Cytosolic 5'-nucleotidase 1A
MEPGQPREPQEPREPGPGAETAAAPVWEEAKIFYDNLAPKKKPKSPKPQNAVTIAVSSRA
LFRMDEEQQIYTEQGVEEYVRYQLEHENEPFSPGPAFPFVKALEAVNRRLRELYPDSEDV
FDIVLMTNNHAQVGVRLINSINHYDLFIERFCMTGGNSPICYLKAYHTNLYLSADAEKVR
EAIDEGIAAATIFSPSRDVVVSQSQLRVAFDGDAVLFSDESERIVKAHGLDRFFEHEKAH
ENKPLAQGPLKGFLEALGRLQKKFYSKGLRLECPIRTYLVTARSAASSGARALKTLRSWG
LETDEALFLAGAPKGPLLEKIRPHIFFDDQMFHVAGAQEMGTVAAHVPYGVAQTPRRTAP
AKQAPSAQ
|
| Enzyme 2 Number of Residues |
368 |
| Enzyme 2 Molecular Weight |
41021 |
| Enzyme 2 Theoretical pI |
6.52 |
| Enzyme 2 GO Classification |
| Function |
- 5'-nucleotidase activity
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- magnesium ion binding
- metal ion binding
- nucleotidase activity
- nucleotide binding
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides and has a broad substrate specificity. Helps to regulate adenosine levels in heart during ischemia and hypoxia |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
12659324  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q9BXI3  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
5NT1A_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1107 bp
ATGGAACCTGGGCAGCCCCGGGAGCCCCAGGAGCCCCGCGAGCCCGGGCCAGGAGCGGAG
ACCGCTGCGGCCCCGGTCTGGGAGGAAGCCAAGATTTTCTACGACAACCTCGCGCCCAAG
AAGAAACCCAAATCGCCCAAGCCTCAGAATGCAGTCACCATCGCTGTGTCCTCCCGAGCC
TTGTTTCGCATGGACGAGGAGCAGCAGATCTACACGGAGCAGGGCGTGGAGGAGTACGTG
CGCTACCAGCTGGAACATGAGAACGAACCCTTCAGTCCCGGGCCAGCCTTCCCTTTTGTG
AAGGCTCTGGAGGCCGTGAACAGGCGGCTGCGGGAGCTGTACCCTGATAGTGAGGACGTC
TTCGACATCGTCCTCATGACTAACAACCATGCTCAAGTGGGTGTCCGCCTCATCAACAGT
ATCAACCACTATGACCTGTTCATCGAGAGGTTCTGCATGACAGGTGGGAACAGCCCGATC
TGCTACCTCAAGGCCTATCACACCAACCTCTACTTGTCAGCCGATGCGGAAAAAGTGCGA
GAAGCCATTGATGAGGGGATCGCAGCTGCCACCATCTTCAGCCCCAGCAGGGATGTGGTT
GTGTCCCAGAGTCAGCTGCGCGTGGCCTTCGATGGGGACGCCGTGCTCTTCTCGGACGAG
TCGGAGCGCATCGTCAAGGCCCACGGGCTGGACCGATTCTTCGAGCATGAGAAGGCCCAC
GAGAACAAGCCTCTGGCTCAGGGCCCCTTAAAGGGCTTTCTGGAGGCACTGGGTAGGTTG
CAGAAGAAGTTCTACTCCAAAGGCCTGCGGCTGGAGTGCCCAATTCGTACCTACTTGGTG
ACAGCACGCAGTGCAGCCAGTTCCGGGGCCCGGGCTCTCAAGACCCTGCGCAGCTGGGGC
CTGGAGACAGATGAAGCCTTGTTCCTTGCTGGAGCGCCCAAGGGCCCTCTCCTTGAGAAG
ATCCGCCCACACATCTTCTTTGATGACCAGATGTTCCATGTGGCTGGGGCTCAGGAGATG
GGCACTGTGGCCGCCCATGTGCCTTATGGTGTGGCACAGACACCCCGGCGGACTGCACCT
GCAAAGCAGGCCCCATCTGCACAGTAG
|
| Enzyme 2 GenBank Gene ID |
AF331801  |
| Enzyme 2 GeneCard ID |
NT5C1A  |
| Enzyme 2 GenAtlas ID |
NT5C1A  |
| Enzyme 2 HGNC ID |
HGNC:17819  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1p34.3-p33 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Hunsucker SA, Spychala J, Mitchell BS: Human cytosolic 5'-nucleotidase I: characterization and role in nucleoside analog resistance. J Biol Chem. 2001 Mar 30;276(13):10498-504. Epub 2000 Dec 22. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5234 |
| Enzyme 3 Name |
5'(3')-deoxyribonucleotidase, cytosolic type |
| Enzyme 3 Synonyms |
- Cytosolic 5',3'-pyrimidine nucleotidase
- Deoxy-5'-nucleotidase 1
- dNT-1
|
| Enzyme 3 Gene Name |
NT5C |
| Enzyme 3 Protein Sequence |
>5'(3')-deoxyribonucleotidase, cytosolic type
MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADK
VASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHL
GPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFTCCHNRHLVLPPTRRRL
LSWSDNWREILDSKRGAAQRE
|
| Enzyme 3 Number of Residues |
201 |
| Enzyme 3 Molecular Weight |
23383 |
| Enzyme 3 Theoretical pI |
6.63 |
| Enzyme 3 GO Classification |
Not Available |
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 Specific Function |
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
7524492  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q8TCD5  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
NT5C_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>606 bp
ATGGCGCGGAGCGTGCGCGTGCTGGTGGACATGGACGGCGTCCTGGCCGACTTCGAGGCC
GGCCTCCTGCGGGGCTTCCGCCGCCGCTTCCCTGAGGAGCCGCACGTGCCGCTGGAGCAA
CGCCGCGGCTTCCTGGCCCGCGAGCAGTACCGCGCCCTGCGGCCCGACCTGGCGGATAAA
GTGGCCAGTGTGTACGAAGCCCCGGGCTTTTTCCTGGACCTGGAGCCCATCCCGGGAGCC
TTGGACGCTGTGCGGGAGATGAACGACCTACCGGACACGCAGGTCTTCATCTGCACCAGC
CCCCTGCTGAAGTACCACCACTGTGTGGGTGAGAAGTACCGCTGGGTGGAGCAGCACCTG
GGGCCCCAGTTCGTAGAACGAATTATCCTGACAAGGGACAAGACGGTGGTCTTGGGGGAC
CTGCTCATTGATGACAAGGACACAGTTCGAGGCCAGGAGGAGACCCCAAGCTGGGAGCAC
ATCTTGTTCACCTGCTGCCACAATCGGCACCTGGTCCTGCCCCCGACAAGGAGACGGCTG
CTCTCCTGGAGTGACAACTGGAGGGAGATCTTAGATAGCAAGCGCGGAGCTGCGCAGCGG
GAATGA
|
| Enzyme 3 GenBank Gene ID |
AF154829  |
| Enzyme 3 GeneCard ID |
NT5C  |
| Enzyme 3 GenAtlas ID |
NT5C  |
| Enzyme 3 HGNC ID |
HGNC:17144  |
| Enzyme 3 Chromosome Location |
17 |
| Enzyme 3 Locus |
17q25.1 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Rampazzo C, Johansson M, Gallinaro L, Ferraro P, Hellman U, Karlsson A, Reichard P, Bianchi V: Mammalian 5'(3')-deoxyribonucleotidase, cDNA cloning, and overexpression of the enzyme in Escherichia coli and mammalian cells. J Biol Chem. 2000 Feb 25;275(8):5409-15. [PubMed
]
- Rampazzo C, Kost-Alimova M, Ruzzenente B, Dumanski JP, Bianchi V: Mouse cytosolic and mitochondrial deoxyribonucleotidases: cDNA cloning of the mitochondrial enzyme, gene structures, chromosomal mapping and comparison with the human orthologs. Gene. 2002 Jul 10;294(1-2):109-17. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5236 |
| Enzyme 4 Name |
5'(3')-deoxyribonucleotidase, mitochondrial precursor |
| Enzyme 4 Synonyms |
- 5',3'-nucleotidase, mitochondrial
- Deoxy-5'-nucleotidase 2
- dNT-2
|
| Enzyme 4 Gene Name |
NT5M |
| Enzyme 4 Protein Sequence |
>5'(3')-deoxyribonucleotidase, mitochondrial precursor
MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRAR
FPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMAS
LQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDI
TGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC
|
| Enzyme 4 Number of Residues |
228 |
| Enzyme 4 Molecular Weight |
25862 |
| Enzyme 4 Theoretical pI |
8.12 |
| Enzyme 4 GO Classification |
Not Available |
| Enzyme 4 General Function |
Not Available |
| Enzyme 4 Specific Function |
Dephosphorylates specifically the 5' and 2'(3')- phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
Not Available |
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
9408106  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q9NPB1  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
NT5M_HUMAN  |
| Enzyme 4 PDB ID |
1Q92  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>687 bp
ATGATCCGGCTGGGCGGCTGGTGTGCGCGGCGGCTCTGCAGCGCGGCGGTTCCCGCGGGG
CGGCGCGGGGCGGCGGGCGGGCTGGGCCTGGCGGGAGGCCGCGCCCTACGGGTGCTGGTG
GACATGGACGGCGTGCTGGCTGACTTCGAGGGCGGATTCCTCAGGAAGTTCCGCGCGCGC
TTTCCCGACCAGCCCTTCATCGCGCTGGAGGACCGGCGCGGCTTCTGGGTGTCGGAGCAG
TACGGCCGCCTGCGGCCAGGGCTGAGCGAGAAGGCCATCAGCATTTGGGAGTCAAAGAAT
TTCTTTTTTGAACTTGAGCCTCTGCCAGGGGCCGTGGAAGCTGTCAAGGAGATGGCCAGC
CTACAAAACACTGACGTCTTCATCTGCACAAGCCCCATCAAGATGTTCAAGTACTGTCCC
TATGAGAAGTATGCCTGGGTGGAGAAGTACTTTGGCCCTGACTTTCTGGAGCAGATTGTG
CTGACCAGAGACAAGACCGTGGTCTCTGCTGACCTTCTCATAGACGACCGGCCGGACATC
ACAGGGGCCGAGCCAACCCCCAGCTGGGAGCATGTCCTCTTCACCGCCTGCCACAACCAG
CACCTGCAGCTGCAGCCCCCCCGCCGCAGGCTGCACTCGTGGGCGGACGACTGGAAGGCC
ATTCTGGACAGCAAGCGGCCCTGCTGA
|
| Enzyme 4 GenBank Gene ID |
AJ277557  |
| Enzyme 4 GeneCard ID |
NT5M  |
| Enzyme 4 GenAtlas ID |
NT5M  |
| Enzyme 4 HGNC ID |
HGNC:15769  |
| Enzyme 4 Chromosome Location |
17 |
| Enzyme 4 Locus |
17p11.2 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Rampazzo C, Gallinaro L, Milanesi E, Frigimelica E, Reichard P, Bianchi V: A deoxyribonucleotidase in mitochondria: involvement in regulation of dNTP pools and possible link to genetic disease. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8239-44. [PubMed
]
- Rinaldo-Matthis A, Rampazzo C, Reichard P, Bianchi V, Nordlund P: Crystal structure of a human mitochondrial deoxyribonucleotidase. Nat Struct Biol. 2002 Oct;9(10):779-87. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5237 |
| Enzyme 5 Name |
Cytosolic purine 5'-nucleotidase |
| Enzyme 5 Synonyms |
- 5'-nucleotidase cytosolic II
|
| Enzyme 5 Gene Name |
NT5C2 |
| Enzyme 5 Protein Sequence |
>Cytosolic purine 5'-nucleotidase
MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
PQEITHCHDEDDDEEEEEEEE
|
| Enzyme 5 Number of Residues |
561 |
| Enzyme 5 Molecular Weight |
64970 |
| Enzyme 5 Theoretical pI |
6.05 |
| Enzyme 5 GO Classification |
Not Available |
| Enzyme 5 General Function |
Not Available |
| Enzyme 5 Specific Function |
May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5-prime-monophosphate (IMP) and other purine nucleotides |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
633071  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P49902  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
5NTC_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1686 bp
ATGTCGACCTCCTGGAGTGATCGGTTACAGAATGCAGCAGATATGCCTGCTAACATGGAT
AAGCATGCCCTGAAAAAGTATCGTCGAGAAGCCTATCATCGGGTGTTTGTGAACCGAAGT
TTAGCAATGGAAAAGATAAAGTGTTTTGGTTTTGATATGGATTATACCCTTGCTGTGTAC
AAGTCCCCAGAGTATGAGTCCCTTGGTTTTGAGCTTACTGTGGAGAGATTAGTTTCTATT
GGCTATCCCCAGGAGTTGCTCAGCTTTGCTTATGATTCTACATTCCCTACCAGGGGACTT
GTCTTTGACACACTGTATGGAAATCTTTTGAAAGTCGATGCCTATGGAAACCTCTTGGTC
TGTGCACATGGATTTAACTTTATAAGGGGACCAGAAACTAGAGAACAGTATCCAAATAAA
TTTATCCAGCGAGATGATACTGAAAGATTTTACATTCTGAACACACTATTCAACCTACCA
GAGACCTACCTGTTGGCCTGCCTAGTAGATTTTTTTACTAATTGTCCCAGATATACCAGT
TGTGAAACAGGATTTAAAGATGGGGACCTCTTCATGTCCTACCGGAGTATGTTCCAGGAT
GTAAGAGATGCTGTTGACTGGGTTCATTACAAGGGCTCCCTTAAGGAAAAGACAGTTGAA
AATCTTGAGAAGTATGTAGTCAAAGATGGAAAACTGCCTTTGCTTCTGAGCCGGATGAAG
GAAGTAGGGAAAGTATTTCTTGCTACCAACAGTGACTATAAATATACAGATAAAATTATG
ACTTACCTGTTTGACTTCCCACATGGCCCCAAGCCTGGGAGCTCCCATCGACCATGGCAG
TCCTACTTTGACTTGATCTTGGTGGATGCACGGAAACCACTCTTTTTTGGAGAAGGCACA
GTACTGCGTCAGGTGGATACTAAAACTGGCAAGCTGAAAATTGGTACCTACACAGGGCCC
CTACAGCATGGTATCGTCTACTCAGGAGGTTCTTCTGATACGATCTGTGACCTGTTGGGA
GCCAAGGGAAAAGACATTTTGTATATTGGAGATCACATTTTTGGGGACATTTTAAAATCA
AAGAAACGGCAAGGGTGGCGAACTTTTTTGGTGATTCCTGAACTCGCACAGGAGCTACAT
GTCTGGACTGACAAGAGTTCACTTTTCGAAGAACTTCAGAGCTTGGATATTTTCTTGGCT
GAACTCTACAAGCATCTTGACAGCAGTAGCAATGAGCGTCCAGACATCAGTTCCATCCAG
AGACGTATTAAGAAAGTAACTCATGACATGGACATGTGCTATGGGATGATGGGAAGCCTG
TTTCGCAGTGGCTCCCGGCAGACCCTTTTTGCCAGTCAAGTGATGCGTTATGCTGACCTC
TATGCAGCATCTTTCATCAACCTGCTGTATTACCCTTTCAGCTACCTCTTCAGGGCTGCC
CATGTCTTGATGCCTCATGAATCAACGGTGGAGCACACACACGTAGATATCAATGAGATG
GAGTCTCCTCTTGCCACCCGGAACCGCACATCAGTGGATTTCAAAGACACTGACTACAAG
CGGCACCAGCTGACACGGTCAATTAGTGAGATTAAACCTCCCAACCTCTTCCCACTGGCC
CCCCAGGAAATTACACACTGCCATGACGAAGATGATGATGAAGAGGAGGAGGAGGAGGAA
GAATAA
|
| Enzyme 5 GenBank Gene ID |
D38524  |
| Enzyme 5 GeneCard ID |
NT5C2  |
| Enzyme 5 GenAtlas ID |
NT5C2  |
| Enzyme 5 HGNC ID |
HGNC:8022  |
| Enzyme 5 Chromosome Location |
10 |
| Enzyme 5 Locus |
10q24.32-q24.33 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Oka J, Matsumoto A, Hosokawa Y, Inoue S: Molecular cloning of human cytosolic purine 5'-nucleotidase. Biochem Biophys Res Commun. 1994 Nov 30;205(1):917-22. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5313 |
| Enzyme 6 Name |
Ectonucleoside triphosphate diphosphohydrolase 1 |
| Enzyme 6 Synonyms |
- NTPDase 1
- Ecto-ATP diphosphohydrolase
- ATPDase
- Lymphoid cell activation antigen
- Ecto-apyrase
- CD39 antigen
|
| Enzyme 6 Gene Name |
ENTPD1 |
| Enzyme 6 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
|
| Enzyme 6 Number of Residues |
510 |
| Enzyme 6 Molecular Weight |
57965 |
| Enzyme 6 Theoretical pI |
6.29 |
| Enzyme 6 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 6 General Function |
Not Available |
| Enzyme 6 Specific Function |
In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation. Hydrolyzes ATP and ADP equally well |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- ATP + 2 H2O = AMP + 2 phosphate
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
765256  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P49961  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
ENTP1_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1533 bp
ATGGAAGATACAAAGGAGTCTAACGTGAAGACATTTTGCTCCAAGAATATCCTAGCCATC
CTTGGCTTCTCCTCTATCATAGCTGTGATAGCTTTGCTTGCTGTGGGGTTGACCCAGAAC
AAAGCATTGCCAGAAAACGTTAAGTATGGGATTGTGCTGGATGCGGGTTCTTCTCACACA
AGTTTATACATCTATAAGTGGCCAGCAGAAAAGGAGAATGACACAGGCGTGGTGCATCAA
GTAGAAGAATGCAGGGTTAAAGGTCCTGGAATCTCAAAATTTGTTCAGAAAGTAAATGAA
ATAGGCATTTACCTGACTGATTGCATGGAAAGAGCTAGGGAAGTGATTCCAAGGTCCCAG
CACCAAGAGACACCCGTTTACCTGGGAGCCACGGCAGGCATGCGGTTGCTCAGGATGGAA
AGTGAAGAGTTGGCAGACAGGGTTCTGGATGTGGTGGAGAGGAGCCTCAGCAACTACCCC
TTTGACTTCCAGGGTGCCAGGATCATTACTGGCCAAGAGGAAGGTGCCTATGGCTGGATT
ACTATCAACTATCTGCTGGGCAAATTCAGTCAGAAAACAAGGTGGTTCAGCATAGTCCCA
TATGAAACCAATAATCAGGAAACCTTTGGAGCTTTGGACCTTGGGGGAGCCTCTACACAA
GTCACTTTTGTACCCCAAAACCAGACTATCGAGTCCCCAGATAATGCTCTGCAATTTCGC
CTCTATGGCAAGGACTACAATGTCTACACACATAGCTTCTTGTGCTATGGGAAGGATCAG
GCACTCTGGCAGAAACTGGCCAAGGACATTCAGGTTGCAAGTAATGAAATTCTCAGGGAC
CCATGCTTTCATCCTGGATATAAGAAGGTAGTGAACGTAAGTGACCTTTACAAGACCCCC
TGCACCAAGAGATTTGAGATGACTCTTCCATTCCAGCAGTTTGAAATCCAGGGTATTGGA
AACTATCAACAATGCCATCAAAGCATCCTGGAGCTCTTCAACACCAGTTACTGCCCTTAC
TCCCAGTGTGCCTTCAATGGGATTTTCTTGCCACCACTCCAGGGGGATTTTGGGGCATTT
TCAGCTTTTTACTTTGTGATGAAGTTTTTAAACTTGACATCAGAGAAAGTCTCTCAGGAA
AAGGTGACTGAGATGATGAAAAAGTTCTGTGCTCAGCCTTGGGAGGAGATAAAAACATCT
TACGCTGGAGTAAAGGAGAAGTACCTGAGTGAATACTGCTTTTCTGGTACCTACATTCTC
TCCCTCCTTCTGCAAGGCTATCATTTCACAGCTGATTCCTGGGAGCACATCCATTTCATT
GGCAAGATCCAGGGCAGCGACGCCGGCTGGACTTTGGGCTACATGCTGAACCTGACCAAC
ATGATCCCAGCTGAGCAACCATTGTCCACACCTCTCTCCCACTCCACCTATGTCTTCCTC
ATGGTTCTATTCTCCCTGGTCCTTTTCACAGTGGCCATCATAGGCTTGCTTATCTTTCAC
AAGCCTTCATATTTCTGGAAAGATATGGTATAG
|
| Enzyme 6 GenBank Gene ID |
S73813  |
| Enzyme 6 GeneCard ID |
ENTPD1  |
| Enzyme 6 GenAtlas ID |
ENTPD1  |
| Enzyme 6 HGNC ID |
HGNC:3363  |
| Enzyme 6 Chromosome Location |
10 |
| Enzyme 6 Locus |
10q24 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed
]
- Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed
]
- Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [PubMed
]
- Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed
]
- Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed
]
- Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed
]
- Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed
]
- Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5314 |
| Enzyme 7 Name |
Soluble calcium-activated nucleotidase 1 |
| Enzyme 7 Synonyms |
- SCAN-1
- Apyrase homolog
- Putative NF-kappa-B-activating protein 107
- Putative MAPK-activating protein PM09
|
| Enzyme 7 Gene Name |
CANT1 |
| Enzyme 7 Protein Sequence |
>Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
|
| Enzyme 7 Number of Residues |
401 |
| Enzyme 7 Molecular Weight |
44840 |
| Enzyme 7 Theoretical pI |
5.98 |
| Enzyme 7 GO Classification |
Not Available |
| Enzyme 7 General Function |
Not Available |
| Enzyme 7 Specific Function |
Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- A nucleoside diphosphate + H2O = a nucleotide + phosphate
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
22218108  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q8WVQ1  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
CANT1_HUMAN  |
| Enzyme 7 PDB ID |
1S1D  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1116 bp
ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA
|
| Enzyme 7 GenBank Gene ID |
AF328554  |
| Enzyme 7 GeneCard ID |
CANT1  |
| Enzyme 7 GenAtlas ID |
CANT1  |
| Enzyme 7 HGNC ID |
HGNC:19721  |
| Enzyme 7 Chromosome Location |
17 |
| Enzyme 7 Locus |
17q25.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [PubMed
]
- Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed
]
- Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5668 |
| Enzyme 8 Name |
Inosine triphosphate pyrophosphatase |
| Enzyme 8 Synonyms |
- ITPase
- Inosine triphosphatase
- Putative oncogene protein hlc14-06-p
|
| Enzyme 8 Gene Name |
ITPA |
| Enzyme 8 Protein Sequence |
>Inosine triphosphate pyrophosphatase
MAASLVGKKIVFVTGNAKKLEEVVQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEA
VRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLLAGFEDKSAYALCTFAL
STGDPSQPVRLFRGRTSGRIVAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFR
ALLELQEYFGSLAA
|
| Enzyme 8 Number of Residues |
194 |
| Enzyme 8 Molecular Weight |
21446 |
| Enzyme 8 Theoretical pI |
5.34 |
| Enzyme 8 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 8 General Function |
Nucleotide transport and metabolism |
| Enzyme 8 Specific Function |
Hydrolyzes ITP and dITP to their respective monophosphate derivatives. Xanthosine 5'-triphosphate (XTP) is also a potential substrate. May be the major enzyme responsible for regulating ITP concentration in cells |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- A nucleoside triphosphate + H2O = a nucleotide + diphosphate
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
13398328  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q9BY32  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
ITPA_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>585 bp
ATGGCGGCCTCATTGGTGGGGAAGAAGATCGTGTTTGTAACGGGGAACGCCAAGAAGCTG
GAGGAGGTCGTTCAGATTCTAGGAGATAAGTTTCCACGCACTTTGGTGGCACAGAAAATT
GACCTGCCGGAGTACCAGGGGGAGCCGGATGAGATTTCCATACAGAAATGTCAGGAGGCA
GTTCGCCAGGTACAGGGGCCCGTGCTGGTTGAGGACACTTGTCTGTGCTTCAATGCCCTT
GGAGGGCTCCCCGGCCCCTACATAAAGTGGTTTCTGGAGAAGTTAAAGCCTGAAGGTCTC
CACCAGCTCCTGGCCGGGTTCGAGGACAAGTCAGCCTATGCGCTCTGCACGTTTGCACTC
AGCACCGGGGACCCAAGCCAGCCCGTGCGCCTGTTCAGGGGCCGGACCTCGGGCCGGATC
GTGGCACCCAGAGGCTGCCAGGACTTTGGCTGGGACCCCTGCTTTCAGCCTGATGGATAT
GAGCAGACGTACGCAGAGATGCCTAAGGCGGAGAAGAACGCTGTCTCCCATCGCTTCCGG
GCCCTGCTGGAGCTGCAGGAGTACTTTGGCAGTTTGGCAGCTTGA
|
| Enzyme 8 GenBank Gene ID |
AF219116  |
| Enzyme 8 GeneCard ID |
ITPA  |
| Enzyme 8 GenAtlas ID |
ITPA  |
| Enzyme 8 HGNC ID |
HGNC:6176  |
| Enzyme 8 Chromosome Location |
20 |
| Enzyme 8 Locus |
20p |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Lin S, McLennan AG, Ying K, Wang Z, Gu S, Jin H, Wu C, Liu W, Yuan Y, Tang R, Xie Y, Mao Y: Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa gene. J Biol Chem. 2001 Jun 1;276(22):18695-701. Epub 2001 Mar 13. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Sumi S, Marinaki AM, Arenas M, Fairbanks L, Shobowale-Bakre M, Rees DC, Thein SL, Ansari A, Sanderson J, De Abreu RA, Simmonds HA, Duley JA: Genetic basis of inosine triphosphate pyrophosphohydrolase deficiency. Hum Genet. 2002 Oct;111(4-5):360-7. Epub 2002 Aug 15. [PubMed
]
- Cao H, Hegele RA: DNA polymorphisms in ITPA including basis of inosine triphosphatase deficiency. J Hum Genet. 2002;47(11):620-2. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5676 |
| Enzyme 9 Name |
Adenine phosphoribosyltransferase |
| Enzyme 9 Synonyms |
- APRT
|
| Enzyme 9 Gene Name |
APRT |
| Enzyme 9 Protein Sequence |
>Adenine phosphoribosyltransferase
MADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHGGRIDY
IAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYSLEYGKAELEIQKDALEPG
QRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE
|
| Enzyme 9 Number of Residues |
180 |
| Enzyme 9 Molecular Weight |
19608 |
| Enzyme 9 Theoretical pI |
5.82 |
| Enzyme 9 GO Classification |
| Function |
- adenine phosphoribosyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring pentosyl groups
|
| Process |
- adenine salvage
- cellular metabolism
- metabolism
- nucleobase metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside metabolism
- physiological process
- purine base metabolism
- purine base salvage
|
| Component |
| — |
|
| Enzyme 9 General Function |
Nucleotide transport and metabolism |
| Enzyme 9 Specific Function |
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
28819  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P07741  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
APT_HUMAN  |
| Enzyme 9 PDB ID |
1ORE  |
| Enzyme 9 PDB File |
Show |
| Enzyme 9 3D Structure |
|
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>543 bp
ATGGCCGACTCCGAGCTGCAGCTGGTTGAGCAGCGGATCCGCAGCTTCCCCGACTTCCCC
ACCCCAGGCGTGGTATTCAGGGACATCTCGCCCGTCCTGAAGGACCCCGCCTCCTTCCGC
GCCGCCATCGGCCTCCTGGCGCGACACCTGAAGGCGACCCACGGGGGCCGCATCGACTAC
ATCGCAGGCCTAGACTCCCGAGGCTTCCTCTTTGGCCCCTCCCTGGCCCAGGAGCTTGGA
CTGGGCTGCGTGCTCATCCGAAAGCGGGGGAAGCTGCCAGGCCCCACTCTGTGGGCCTCC
TATTCCCTGGAGTACGGGAAGGCTGAGCTGGAGATTCAGAAAGACGCCCTGGAGCCAGGA
CAGAGGGTGGTCGTCGTGGATGATCTGCTGGCCACTGGTGGAACCATGAACGCTGCCTGT
GAGCTGCTGGGCCGCCTGCAGGCTGAGGTCCTGGAGTGCGTGAGCCTGGTGGAGCTGACC
TCGCTTAAGGGCAGGGAGAAGCTGGCACCTGTACCCTTCTTCTCTCTCCTGCAGTATGAG
TGA
|
| Enzyme 9 GenBank Gene ID |
Y00486  |
| Enzyme 9 GeneCard ID |
APRT  |
| Enzyme 9 GenAtlas ID |
APRT  |
| Enzyme 9 HGNC ID |
HGNC:626  |
| Enzyme 9 Chromosome Location |
16 |
| Enzyme 9 Locus |
16q24 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Hidaka Y, Tarle SA, O'Toole TE, Kelley WN, Palella TD: Nucleotide sequence of the human APRT gene. Nucleic Acids Res. 1987 Nov 11;15(21):9086. [PubMed
]
- Broderick TP, Schaff DA, Bertino AM, Dush MK, Tischfield JA, Stambrook PJ: Comparative anatomy of the human APRT gene and enzyme: nucleotide sequence divergence and conservation of a nonrandom CpG dinucleotide arrangement. Proc Natl Acad Sci U S A. 1987 May;84(10):3349-53. [PubMed
]
- Wilson JM, O'Toole TE, Argos P, Shewach DS, Daddona PE, Kelley WN: Human adenine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme. J Biol Chem. 1986 Oct 15;261(29):13677-83. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Chen J, Sahota A, Laxdal T, Scrine M, Bowman S, Cui C, Stambrook PJ, Tischfield JA: Identification of a single missense mutation in the adenine phosphoribosyltransferase (APRT) gene from five Icelandic patients and a British patient. Am J Hum Genet. 1991 Dec;49(6):1306-11. [PubMed
]
- Sahota A, Chen J, Boyadjiev SA, Gault MH, Tischfield JA: Missense mutation in the adenine phosphoribosyltransferase gene causing 2,8-dihydroxyadenine urolithiasis. Hum Mol Genet. 1994 May;3(5):817-8. [PubMed
]
- Hidaka Y, Palella TD, O'Toole TE, Tarle SA, Kelley WN: Human adenine phosphoribosyltransferase. Identification of allelic mutations at the nucleotide level as a cause of complete deficiency of the enzyme. J Clin Invest. 1987 Nov;80(5):1409-15. [PubMed
]
- Hidaka Y, Tarle SA, Fujimori S, Kamatani N, Kelley WN, Palella TD: Human adenine phosphoribosyltransferase deficiency. Demonstration of a single mutant allele common to the Japanese. J Clin Invest. 1988 Mar;81(3):945-50. [PubMed
]
- Kamatani N, Hakoda M, Otsuka S, Yoshikawa H, Kashiwazaki S: Only three mutations account for almost all defective alleles causing adenine phosphoribosyltransferase deficiency in Japanese patients. J Clin Invest. 1992 Jul;90(1):130-5. [PubMed
]
- Deng L, Yang M, Frund S, Wessel T, De Abreu RA, Tischfield JA, Sahota A: 2,8-Dihydroxyadenine urolithiasis in a patient with considerable residual adenine phosphoribosyltransferase activity in cell extracts but with mutations in both copies of APRT. Mol Genet Metab. 2001 Mar;72(3):260-4. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5715 |
| Enzyme 10 Name |
Hypoxanthine-guanine phosphoribosyltransferase |
| Enzyme 10 Synonyms |
- HGPRT
- HGPRTase
|
| Enzyme 10 Gene Name |
HPRT1 |
| Enzyme 10 Protein Sequence |
>Hypoxanthine-guanine phosphoribosyltransferase
MATRSPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGH
HIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGD
DLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVG
FEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA
|
| Enzyme 10 Number of Residues |
218 |
| Enzyme 10 Molecular Weight |
24580 |
| Enzyme 10 Theoretical pI |
6.67 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- hypoxanthine phosphoribosyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring pentosyl groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside metabolism
- physiological process
- purine ribonucleoside salvage
- purine salvage
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 10 General Function |
Nucleotide transport and metabolism |
| Enzyme 10 Specific Function |
IMP + diphosphate = hypoxanthine + 5-phospho- alpha-D-ribose 1-diphosphate |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
306885  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P00492  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
HPRT_HUMAN  |
| Enzyme 10 PDB ID |
1BZY  |
| Enzyme 10 PDB File |
Show |
| Enzyme 10 3D Structure |
|
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>657 bp
ATGGCGACCCGCAGCCCTGGCGTCGTGATTAGTGATGATGAACCAGGTTATGACCTTGAT
TTATTTTGCATACCTAATCATTATGCTGAGGATTTGGAAAGGGTGTTTATTCCTCATGGA
CTAATTATGGACAGGACTGAACGTCTTGCTCGAGATGTGATGAAGGAGATGGGAGGCCAT
CACATTGTAGCCCTCTGTGTGCTCAAGGGGGGCTATAAATTCTTTGCTGACCTGCTGGAT
TACATCAAAGCACTGAATAGAAATAGTGATAGATCCATTCCTATGACTGTAGATTTTATC
AGACTGAAGAGCTATTGTAATGACCAGTCAACAGGGGACATAAAAGTAATTGGTGGAGAT
GATCTCTCAACTTTAACTGGAAAGAATGTCTTGATTGTGGAAGATATAATTGACACTGGC
AAAACAATGCAGACTTTGCTTTCCTTGGTCAGGCAGTATAATCCAAAGATGGTCAAGGTC
GCAAGCTTGCTGGTGAAAAGGACCCCACGAAGTGTTGGATATAAGCCAGACTTTGTTGGA
TTTGAAATTCCAGACAAGTTTGTTGTAGGATATGCCCTTGACTATAATGAATACTTCAGG
GATTTGAATCATGTTTGTGTCATTAGTGAAACTGGAAAAGCAAAATACAAAGCCTAA
|
| Enzyme 10 GenBank Gene ID |
M31642  |
| Enzyme 10 GeneCard ID |
HPRT1  |
| Enzyme 10 GenAtlas ID |
HPRT1  |
| Enzyme 10 HGNC ID |
HGNC:5157  |
| Enzyme 10 Chromosome Location |
X |
| Enzyme 10 Locus |
Xq26.1 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Jolly DJ, Okayama H, Berg P, Esty AC, Filpula D, Bohlen P, Johnson GG, Shively JE, Hunkapillar T, Friedmann T: Isolation and characterization of a full-length expressible cDNA for human hypoxanthine phosphoribosyl transferase. Proc Natl Acad Sci U S A. 1983 Jan;80(2):477-81. [PubMed
]
- Edwards A, Voss H, Rice P, Civitello A, Stegemann J, Schwager C, Zimmermann J, Erfle H, Caskey CT, Ansorge W: Automated DNA sequencing of the human HPRT locus. Genomics. 1990 Apr;6(4):593-608. [PubMed
]
- Wilson JM, Tarr GE, Mahoney WC, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme. J Biol Chem. 1982 Sep 25;257(18):10978-85. [PubMed
]
- Patel PI, Framson PE, Caskey CT, Chinault AC: Fine structure of the human hypoxanthine phosphoribosyltransferase gene. Mol Cell Biol. 1986 Feb;6(2):393-403. [PubMed
]
- Eads JC, Scapin G, Xu Y, Grubmeyer C, Sacchettini JC: The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP. Cell. 1994 Jul 29;78(2):325-34. [PubMed
]
- Shi W, Li CM, Tyler PC, Furneaux RH, Grubmeyer C, Schramm VL, Almo SC: The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor. Nat Struct Biol. 1999 Jun;6(6):588-93. [PubMed
]
- Balendiran GK, Molina JA, Xu Y, Torres-Martinez J, Stevens R, Focia PJ, Eakin AE, Sacchettini JC, Craig SP 3rd: Ternary complex structure of human HGPRTase, PRPP, Mg2+, and the inhibitor HPP reveals the involvement of the flexible loop in substrate binding. Protein Sci. 1999 May;8(5):1023-31. [PubMed
]
- Sculley DG, Dawson PA, Emmerson BT, Gordon RB: A review of the molecular basis of hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. Hum Genet. 1992 Nov;90(3):195-207. [PubMed
]
- Wilson JM, Kobayashi R, Fox IH, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. J Biol Chem. 1983 May 25;258(10):6458-60. [PubMed
]
- Wilson JM, Kelley WN: Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome. J Clin Invest. 1983 May;71(5):1331-5. [PubMed
]
- Wilson JM, Tarr GE, Kelley WN: Human hypoxanthine (guanine) phosphoribosyltransferase: an amino acid substitution in a mutant form of the enzyme isolated from a patient with gout. Proc Natl Acad Sci U S A. 1983 Feb;80(3):870-3. [PubMed
]
- Wilson JM, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. Structural alteration in a dysfunctional enzyme variant (HPRTMunich) isolated from a patient with gout. J Biol Chem. 1984 Jan 10;259(1):27-30. [PubMed
]
- Cariello NF, Scott JK, Kat AG, Thilly WG, Keohavong P: Resolution of a missense mutant in human genomic DNA by denaturing gradient gel electrophoresis and direct sequencing using in vitro DNA amplification: HPRT Munich. Am J Hum Genet. 1988 May;42(5):726-34. [PubMed
]
- Davidson BL, Pashmforoush M, Kelley WN, Palella TD: Genetic basis of hypoxanthine guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome (HPRTFlint). Gene. 1988 Mar 31;63(2):331-6. [PubMed
]
- Davidson BL, Palella TD, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland). Gene. 1988 Aug 15;68(1):85-91. [PubMed
]
- Fujimori S, Hidaka Y, Davidson BL, Palella TD, Kelley WN: Identification of a single nucleotide change in a mutant gene for hypoxanthine-guanine phosphoribosyltransferase (HPRT Ann Arbor). Hum Genet. 1988 May;79(1):39-43. [PubMed
]
- Davidson BL, Chin SJ, Wilson JM, Kelley WN, Palella TD: Hypoxanthine-guanine phosphoribosyltransferase. Genetic evidence for identical mutations in two partially deficient subjects. J Clin Invest. 1988 Dec;82(6):2164-7. [PubMed
]
- Keough DT, Gordon RB, de Jersey J, Emmerson BT: Biochemical basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in nine families. J Inherit Metab Dis. 1988;11(3):229-38. [PubMed
]
- Igarashi T, Minami M, Nishida Y: Molecular analysis of hypoxanthine-guanine phosphoribosyltransferase mutations in five unrelated Japanese patients. Acta Paediatr Jpn. 1989 Jun;31(3):303-13. [PubMed
]
- Davidson BL, Pashmforoush M, Kelley WN, Palella TD: Human hypoxanthine-guanine phosphoribosyltransferase deficiency. The molecular defect in a patient with gout (HPRTAshville). J Biol Chem. 1989 Jan 5;264(1):520-5. [PubMed
]
- Fujimori S, Davidson BL, Kelley WN, Palella TD: Identification of a single nucleotide change in the hypoxanthine-guanine phosphoribosyltransferase gene (HPRTYale) responsible for Lesch-Nyhan syndrome. J Clin Invest. 1989 Jan;83(1):11-3. [PubMed
]
- Davidson BL, Tarle SA, Palella TD, Kelley WN: Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in ten subjects determined by direct sequencing of amplified transcripts. J Clin Invest. 1989 Jul;84(1):342-6. [PubMed
]
- Gibbs RA, Nguyen PN, McBride LJ, Koepf SM, Caskey CT: Identification of mutations leading to the Lesch-Nyhan syndrome by automated direct DNA sequencing of in vitro amplified cDNA. Proc Natl Acad Sci U S A. 1989 Mar;86(6):1919-23. [PubMed
]
- Gibbs RA, Nguyen PN, Edwards A, Civitello AB, Caskey CT: Multiplex DNA deletion detection and exon sequencing of the hypoxanthine phosphoribosyltransferase gene in Lesch-Nyhan families. Genomics. 1990 Jun;7(2):235-44. [PubMed
]
- Skopek TR, Recio L, Simpson D, Dallaire L, Melancon SB, Ogier H, O'Neill JP, Falta MT, Nicklas JA, Albertini RJ: Molecular analyses of a Lesch-Nyhan syndrome mutation (hprtMontreal) by use of T-lymphocyte cultures. Hum Genet. 1990 Jun;85(1):111-6. [PubMed
]
- Gordon RB, Sculley DG, Dawson PA, Beacham IR, Emmerson BT: Identification of a single nucleotide substitution in the coding sequence of in vitro amplified cDNA from a patient with partial HPRT deficiency (HPRTBRISBANE). J Inherit Metab Dis. 1990;13(5):692-700. [PubMed
]
- Davidson BL, Tarle SA, Van Antwerp M, Gibbs DA, Watts RW, Kelley WN, Palella TD: Identification of 17 independent mutations responsible for human hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. Am J Hum Genet. 1991 May;48(5):951-8. [PubMed
]
- Tarle SA, Davidson BL, Wu VC, Zidar FJ, Seegmiller JE, Kelley WN, Palella TD: Determination of the mutations responsible for the Lesch-Nyhan syndrome in 17 subjects. Genomics. 1991 Jun;10(2):499-501. [PubMed
]
- Sculley DG, Dawson PA, Beacham IR, Emmerson BT, Gordon RB: Hypoxanthine-guanine phosphoribosyltransferase deficiency: analysis of HPRT mutations by direct sequencing and allele-specific amplification. Hum Genet. 1991 Oct;87(6):688-92. [PubMed
]
- Yamada Y, Goto H, Ogasawara N: Identification of two independent Japanese mutant HPRT genes using the PCR technique. Adv Exp Med Biol. 1991;309B:121-4. [PubMed
]
- Lightfoot T, Joshi R, Nuki G, Snyder FF: The point mutation of hypoxanthine-guanine phosphoribosyltransferase (HPRTEdinburgh) and detection by allele-specific polymerase chain reaction. Hum Genet. 1992 Mar;88(6):695-6. [PubMed
]
- Sege-Peterson K, Chambers J, Page T, Jones OW, Nyhan WL: Characterization of mutations in phenotypic variants of hypoxanthine phosphoribosyltransferase deficiency. Hum Mol Genet. 1992 Sep;1(6):427-32. [PubMed
]
- Burgemeister R, Rotzer E, Gutensohn W, Gehrke M, Schiel W: Identification of a new missense mutation in exon 2 of the human hypoxanthine phosphoribosyltransferase gene (HPRTIsar): a further example of clinical heterogeneity in HPRT deficiencies. Hum Mutat. 1995;5(4):341-4. [PubMed
]
- Fujimori S, Sakuma R, Yamaoka N, Hakoda M, Yamanaka H, Kamatani N: An asymptomatic germline missense base substitution in the hypoxanthine phosphoribosyltransferase (HPRT) gene that reduces the amount of enzyme in humans. Hum Genet. 1997 Jan;99(1):8-10. [PubMed
]
- Liu G, Aral B, Zabot MT, Kamoun P, Ceballos-Picot I: The molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in French families; report of two novel mutations. Hum Mutat. 1998;Suppl 1:S88-90. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5833 |
| Enzyme 11 Name |
Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma |
| Enzyme 11 Synonyms |
- GMP-PDE gamma
|
| Enzyme 11 Gene Name |
PDE6H |
| Enzyme 11 Protein Sequence |
>Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
MSDNTTLPAPASNQGPTTPRKGPPKFKQRQTRQFKSKPPKKGVKGFGDDIPGMEGLGTDI
TVICPWEAFSHLELHELAQFGII
|
| Enzyme 11 Number of Residues |
83 |
| Enzyme 11 Molecular Weight |
9074 |
| Enzyme 11 Theoretical pI |
9.98 |
| Enzyme 11 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 11 General Function |
Not Available |
| Enzyme 11 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 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 |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
1311544  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q13956  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
CNCG_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>252 bp
ATGAGTGACAACACTACTCTGCCTGCTCCAGCTTCAAACCAGGGTCCTACCACCCCACGC
AAAGGCCCTCCCAAGTTCAAGCAGAGGCAGACTCGCCAATTCAAGAGTAAACCTCCAAAG
AAAGGTGTGAAAGGATTTGGAGATGACATTCCAGGAATGGAGGGGCTAGGAACAGATATC
ACAGTGATTTGTCCATGGGAGGCATTCAGCCACCTGGAATTGCATGAGCTCGCTCAGTTT
GGGATTATCTGA
|
| Enzyme 11 GenBank Gene ID |
D45399  |
| Enzyme 11 GeneCard ID |
PDE6H  |
| Enzyme 11 GenAtlas ID |
PDE6H  |
| Enzyme 11 HGNC ID |
HGNC:8790  |
| Enzyme 11 Chromosome Location |
12 |
| Enzyme 11 Locus |
12p13 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 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 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5843 |
| Enzyme 12 Name |
Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A |
| Enzyme 12 Synonyms |
- Cam-PDE 1A
- 61 kDa Cam-PDE
- hCam-1
|
| Enzyme 12 Gene Name |
PDE1A |
| Enzyme 12 Protein Sequence |
>Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
MGSSATEIEELENTTFKYLTGEQTEKMWQRLKGILRCLVKQLERGDVNVVDLKKNIEYAA
SVLEAVYIDETRRLLDTEDELSDIQTDSVPSEVRDWLASTFTRKMGMTKKKPEEKPKFRS
IVHAVQAGIFVERMYRKTYHMVGLAYPAAVIVTLKDVDKWSFDVFALNEASGEHSLKFMI
YELFTRYDLINRFKIPVSCLITFAEALEVGYSKYKNPYHNLIHAADVTQTVHYIMLHTGI
MHWLTELEILAMVFAAAIHDYEHTGTTNNFHIQTRSDVAILYNDRSVLENHHVSAAYRLM
QEEEMNILINLSKDDWRDLRNLVIEMVLSTDMSGHFQQIKNIRNSLQQPEGIDRAKTMSL
ILHAADISHPAKSWKLHYRWTMALMEEFFLQGDKEAELGLPFSPLCDRKSTMVAQSQIGF
IDFIVEPTFSLLTDSTEKIVIPLIEEASKAETSSYVASSSTTIVGLHIADALRRSNTKGS
MSDGSYSPDYSLAAVDLKSFKNNLVDIIQQNKERWKELAAQEARTSSQKCEFIHQ
|
| Enzyme 12 Number of Residues |
535 |
| Enzyme 12 Molecular Weight |
61253 |
| Enzyme 12 Theoretical pI |
6.02 |
| 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 |
Has a higher affinity for cGMP than 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 |
1151109  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P54750  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
PDE1A_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 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 12 GenBank Gene ID |
U40370  |
| Enzyme 12 GeneCard ID |
PDE1A  |
| Enzyme 12 GenAtlas ID |
PDE1A  |
| Enzyme 12 HGNC ID |
HGNC:8774  |
| Enzyme 12 Chromosome Location |
2 |
| Enzyme 12 Locus |
2q32.1 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 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 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5847 |
| Enzyme 13 Name |
High-affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A |
| Enzyme 13 Synonyms |
Not Available |
| Enzyme 13 Gene Name |
PDE8A |
| Enzyme 13 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 13 Number of Residues |
829 |
| Enzyme 13 Molecular Weight |
93305 |
| Enzyme 13 Theoretical pI |
6.03 |
| Enzyme 13 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 13 General Function |
Signal transduction mechanisms |
| Enzyme 13 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 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 |
16417190  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
O60658  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
PDE8A_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 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 13 GenBank Gene ID |
AF388183  |
| Enzyme 13 GeneCard ID |
PDE8A  |
| Enzyme 13 GenAtlas ID |
PDE8A  |
| Enzyme 13 HGNC ID |
HGNC:8793  |
| Enzyme 13 Chromosome Location |
15 |
| Enzyme 13 Locus |
15q25.3 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 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 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
5848 |
| Enzyme 14 Name |
Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B |
| Enzyme 14 Synonyms |
- Cam-PDE 1B
- 63 kDa Cam-PDE
|
| Enzyme 14 Gene Name |
PDE1B |
| Enzyme 14 Protein Sequence |
>Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
MELSPRSPPEMLEESDCPSPLELKSAPSKKMWIKLRSLLRYMVKQLENGEINIEELKKNL
EYTASLLEAVYIDETRQILDTEDELQELRSDAVPSEVRDWLASTFTQQARAKGRRAEEKP
KFRSIVHAVQAGIFVERMFRRTYTSVGPTYSTAVLNCLKNLDLWCFDVFSLNQAADDHAL
RTIVFELLTRHNLISRFKIPTVFLMSFLDALETGYGKYKNPYHNQIHAADVTQTVHCFLL
RTGMVHCLSEIELLAIIFAAAIHDYEHTGTTNSFHIQTKSECAIVYNDRSVLENHHISSV
FRLMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKTMKTALQQLERIDKPK
ALSLLLHAADISHPTKQWLVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQS
QIGFIDFIVEPTFSVLTDVAEKSVQPLADEDSKSKNQPSFQWRQPSLDVEVGDPNPDVVS
FRSTWVKRIQENKQKWKERAASGITNQMSIDELSPCEEEAPPSPAEDEHNQNGNLD
|
| Enzyme 14 Number of Residues |
536 |
| Enzyme 14 Molecular Weight |
61380 |
| Enzyme 14 Theoretical pI |
5.22 |
| 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 |
Has a preference for cGMP as a substrate |
| 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 |
1621592  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q01064  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
PDE1B_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 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 14 GenBank Gene ID |
U56976  |
| Enzyme 14 GeneCard ID |
PDE1B  |
| Enzyme 14 GenAtlas ID |
PDE1B  |
| Enzyme 14 HGNC ID |
HGNC:8775  |
| Enzyme 14 Chromosome Location |
12 |
| Enzyme 14 Locus |
12q13 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 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 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
5850 |
| Enzyme 15 Name |
cGMP-inhibited 3',5'-cyclic phosphodiesterase B |
| Enzyme 15 Synonyms |
- Cyclic GMP-inhibited phosphodiesterase B
- CGI-PDE B
- CGIPDE1
- CGIP1
|
| Enzyme 15 Gene Name |
PDE3B |
| Enzyme 15 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 15 Number of Residues |
1112 |
| Enzyme 15 Molecular Weight |
124335 |
| Enzyme 15 Theoretical pI |
5.75 |
| Enzyme 15 GO Classification |
Not Available |
| Enzyme 15 General Function |
Not Available |
| Enzyme 15 Specific Function |
May play a role in fat metabolism |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 15 Pfam Domain Function |
Not Available |
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
- 88-108
117-137
152-172
192-212
220-240
247-267
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
1145302  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q13370  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
PDE3B_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 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 15 GenBank Gene ID |
U38178  |
| Enzyme 15 GeneCard ID |
PDE3B  |
| Enzyme 15 GenAtlas ID |
PDE3B  |
| Enzyme 15 HGNC ID |
HGNC:8779  |
| Enzyme 15 Chromosome Location |
11 |
| Enzyme 15 Locus |
11p15.1 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 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 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
5854 |
| Enzyme 16 Name |
Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha' |
| Enzyme 16 Synonyms |
- cGMP phosphodiesterase 6C
|
| Enzyme 16 Gene Name |
PDE6C |
| Enzyme 16 Protein Sequence |
>Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'
MGEINQVAVEKYLEENPQFAKEYFDRKLRVEVLGEIFKNSQVPVQSSMSFSELTQVEESA
LCLELLWTVQEEGGTPEQGVHRALQRLAHLLQADRCSMFLCRSRNGIPEVASRLLDVTPT
SKFEDNLVGPDKEVVFPLDIGIVGWAAHTKKTHNVPDVKKNSHFSDFMDKQTGYVTKNLL
ATPIVVGKEVLAVIMAVNKVNASEFSKQDEEVFSKYLNFVSIILRLHHTSYMYNIESRRS
QILMWSANKVFEELTDVERQFHKALYTVRSYLNCERYSIGLLDMTKEKEFYDEWPIKLGE
VEPYKGPKTPDGREVNFYKIIDYILHGKEEIKVIPTPPADHWTLISGLPTYVAENGFICN
MMNAPADEYFTFQKGPVDETGWVIKNVLSLPIVNKKEDIVGVATFYNRKDGKPFDEHDEY
ITETLTQFLGWSLLNTDTYDKMNKLENRKDIAQEMLMNQTKATPEEIKSILKFQEKLNVD
VIDDCEEKQLVAILKEDLPDPRSAELYEFRFSDFPLTEHGLIKCGIRLFFEINVVEKFKV
PVEVLTRWMYTVRKGYRAVTYHNWRHGFNVGQTMFTLLMTGRLKKYYTDLEAFAMLAAAF
CHDIDHRGTNNLYQMKSTSPLARLHGSSILERHHLEYSKTLLQDESLNIFQNLNKRQFET
VIHLFEVAIIATDLALYFKKRTMFQKIVDACEQMQTEEEAIKYVTVDPTKKEIIMAMMMT
ACDLSAITKPWEVQSQVALMVANEFWEQGDLERTVLQQQPIPMMDRNKRDELPKLQVGFI
DFVCTFVYKEFSRFHKEITPMLSGLQNNRVEWKSLADEYDAKMKVIEEEAKKQEGGAEKA
AEDSGGGDDKKSKTCLML
|
| Enzyme 16 Number of Residues |
858 |
| Enzyme 16 Molecular Weight |
99148 |
| Enzyme 16 Theoretical pI |
5.45 |
| 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 |
Guanosine 3',5'-cyclic phosphate + H(2)O = guanosine 5'-phosphate |
| 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 |
940231  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P51160  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
PDE6C_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>2577 bp
ATGGGTGAGATCAACCAAGTTGCCGTGGAGAAATACCTGGAGGAGAACCCTCAGTTTGCC
AAGGAGTACTTTGACAGGAAGTTGCGGGTGGAGGTGCTGGGAGAAATCTTCAAGAACAGC
CAGGTGCCAGTCCAGTCCAGCATGTCCTTCTCTGAGCTGACCCAGGTGGAGGAGTCAGCC
CTGTGCTTGGAGCTGCTGTGGACCGTGCAGGAGGAGGGGGGCACCCCAGAGCAGGGGGTT
CACAGGGCCCTACAGAGGCTGGCCCACCTGCTCCAGGCTGACCGCTGCAGCATGTTCCTG
TGCCGGTCCCGGAACGGCATACCTGAGGTGGCCTCTAGGTTGCTGGTAGTCACCCCCACC
TCCAAGTTTGAGGACAACCTGGTGGGCCCTGACAAAGAAGTTGTGTTTCCATTGGACATT
GGGATAGTGGGTTGGGCTGCTCACACGAAGAAAACTCATAATGTCCCAGATGTGAAAAAG
AACAGCCATTTTTCTGACTTCATGGACAAGCAAACTGGGTATGTCACTAAGAACCTGCTG
GCAACCCCGATCGTGGTGGGCAAGGAGGTTCTTGCTGTGATCATGGCAGTTAACAAAGTA
AATGCATCTGAATTTTCCAAACAGGATGAAGAGGTCTTTTCCAAATACCTCAACTTTGTG
TCTATCATCCTAAGGCTTCATCACACCAGCTACATGTACAATATTGAATCCCGAAGAAGC
CAGATCCTTATGTGGTCAGCCAATAAAGTATTTGAAGAACTCACAGATGTTGAGCGACAG
TTTCACAAAGCGCTCTACACGGTTAGATCATATCTGAACTGTGAACGATACTCCATTGGA
CTGCTGGACATGACCAAGGAGAAGGAATTCTACGATGAATGGCCAATCAAGCTTGGAGAA
GTAGAGCCTTATAAAGGTCCAAAGACACCTGATGGCAGGGAAGTCAACTTTTATAAAATC
ATTGATTACATTTTACATGGAAAAGAAGAGATCAAAGTGATTCCGACGCCTCCTGCAGAC
CACTGGACACTCATTAGTGGGTTGCCAACATATGTTGCTGAAAATGGATTTATCTGTAAC
ATGATGAATGCCCCTGCGGATGAATACTTCACATTTCCGAAAGGACCTGTAGACGAAACT
GGTTGGGTCATTAAGAATGTTTTGTCCCTGCCTATTGTCAACAAGAAAGAAGATATTGTG
GGAGTGGCTACATTTTACAACAGGAAGGATGGAAAACCTTTCGATGAGCATGATGAATAC
ATTACCGAGACTCTCACACAATTTCTTGGATGGTCTCTTTTAAATACTGACACCTACGAT
AAGATGAATAAGCTAGAAAACAGAAAGGACATTGCTCAGGAAATGCTCATGAACCAAACC
AAAGCCACTCTTGAAGAAATTAAGTCCATTTTGAAATTTCAAGAGAAGTTAAATGTTGAT
GTAATTGACGACTGTGAAGAAAAACAACTTGTTGCAATTTTGAAAGAGGACTTGCCAGAC
CCACGCTCAGCAGAACTGTACGAATTCCGCTTCAGTGACTTCCCCCTTACAGAGCACGGA
TTGATTAAATGTGGAATACGACTGTTTTTTGAAATAAATGTGGTGGAGAAATTCAAAGTA
CCTGTAGAGGTTCTTACCAGATGGATGTACACTGTGAGGAAAGGGTACCGAGCTGTCACT
TACCACAATTGGCAGCATGGGTTCAACGTGGGGCAGACCATGTTTACTTTGCTGATGACA
GGAAGATTAAAGAAGTACTACACAGATCTCGAAGCCTTTGCCATGCTTGCTGCTGCTTTC
TGCCATGATATTGACCACAGAGGCACCAATAATTTGTACCAGATGAAATCCACGTCTCCA
TTAGCAAGACTTCATGGTTCTTCTATTTTGGAGAGGCACCACCTGGAGTACAGTAAGACT
CTGTTGCAGGATGAGAGTTTAAACATCTTCCAGAACCTAAATAAGCGGCAGTTTGAAACA
GTTATTCATTTGTTCGAGGTCGCAATAATAGCAACTGACCTGGCTTTATATTTCAAGAAG
AGGACCATGTTTCAAAAAATTGTTGATGCCTGTGAACAAATGCAAACGGAAGAAGAAGCC
ATCAAATATGTAACTGTTGATCCAACCAAGAAAGAGATTATCATGGCAATGATGATGACG
GCATGTGACTTGTCTGCTATTACCAAGCCCTGGGAGGTGCAAAGTCAGGTAGCACTTATG
GTTGCAAATGAATTTTGGGAACAAGGAGATCTGGAGAGAACAGTGTTGCAGCAACAACCC
ATTCCTATGATGGACAGAAACAAAAGAGATGAATTACCTAAACTTCAAGTTGGATTTATT
GATTTTGTTTGTACTTTTGTATATAAGGAGTTCTCACGGTTTCACAAAGAAATCACACCT
ATGCTGAGTGGTCTTCAGAATAACAGAGTAGAATGGAAATCACTAGCTGATGAGTATGAT
GCAAAGATGAAGGTCATTGAAGAGGAGGCAAAAAAGCAAGAAGGAGGAGCCGAAAAAGCT
GCTGAAGATTCAGGAGGTGGTGATGACAAAAAGTCCAAAACATGTTTAATGTTGTAA
|
| Enzyme 16 GenBank Gene ID |
U31973  |
| Enzyme 16 GeneCard ID |
PDE6C  |
| Enzyme 16 GenAtlas ID |
PDE6C  |
| Enzyme 16 HGNC ID |
HGNC:8787  |
| Enzyme 16 Chromosome Location |
10 |
| Enzyme 16 Locus |
10q24 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Piriev NI, Viczian AS, Ye J, Kerner B, Korenberg JR, Farber DB: Gene structure and amino acid sequence of the human cone photoreceptor cGMP-phosphodiesterase alpha' subunit (PDEA2) and its chromosomal localization to 10q24. Genomics. 1995 Aug 10;28(3):429-35. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
5864 |
| Enzyme 17 Name |
GMP synthase [glutamine-hydrolyzing] |
| Enzyme 17 Synonyms |
- Glutamine amidotransferase
- GMP synthetase
|
| Enzyme 17 Gene Name |
GMPS |
| Enzyme 17 Protein Sequence |
>GMP synthase [glutamine-hydrolyzing]
MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETP
AFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHK
KSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANE
SKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAA
HSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPE
EVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVR
ILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPH
TLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDW
ESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVE
VVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
|
| Enzyme 17 Number of Residues |
693 |
| Enzyme 17 Molecular Weight |
76716 |
| Enzyme 17 Theoretical pI |
6.86 |
| Enzyme 17 GO Classification |
| Function |
- ATP binding
- GMP synthase (glutamine-hydrolyzing) activity
- GMP synthase (glutamine-hydrolyzing) activity
- adenyl nucleotide binding
- binding
- carbon-nitrogen ligase activity, with glutamine as amido-N-donor
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- molecular function unknown
- nucleotide binding
- purine nucleotide binding
|
| Process |
- GMP biosynthesis
- amino acid and derivative metabolism
- amino acid metabolism
- biosynthesis
- cellular metabolism
- glutamine family amino acid metabolism
- glutamine metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside monophosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside monophosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 17 General Function |
Nucleotide transport and metabolism |
| Enzyme 17 Specific Function |
Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
595410  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
P49915  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
GUAA_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>2082 bp
ATGGCTCTGTGCAACGGAGACTCCAAGCTGGAGAATGCTGGAGGAGACCTTAAGGATGGC
CACCACCACTATGAAGGAGCTGTTGTCATTCTGGATGCTGGTGCTCAGTACGGGAAAGTC
ATAGACCGAAGAGTGAGGGAACTGTTCGTGCAGTCTGAAATTTTCCCCTTGGAAACACCA
GCATTTGCTATAAAGGAACAAGGATTCCGTGCTATTATCATCTCTGGAGGACCTAATTCT
GTGTATGCTGAAGATGCTCCCTGGTTTGATCCAGCAATATTCACTATTGGCAAGCCTGTT
CTTGGAATTTGCTATGGTATGCAGATGATGAATAAGGTATTTGGAGGTACTGTGCACAAA
AAAAGTGTCAGAGAAGATGGAGTTTTCAACATTAGTGTGGATAATACATGTTCATTATTC
AGGGGCCTTCAGAAGGAAGAAGTTGTTTTGCTTACACATGGAGATAGTGTAGACAAAGTA
GCTGATGGATTCAAGGTTGTGGCACGTTCTGGAAACATAGTAGCAGGCATAGCAAATGAA
TCTAAAAAGTTATATGGAGCACAGTTCCACCCTGAAGTTGGCCTTACAGAAAATGGAAAA
GTAATACTGAAGAATTTCCTTTATGATATAGCTGGATGCAGTGGAACCTTCACCGTGCAG
AACAGAGAACTTGAGTGTATTCGAGAGATCAAAGAGAGAGTAGGCACGTCAAAAGTTTTG
GTTTTACTCAGTGGTGGAGTAGACTCAACAGTTTGTACAGCTTTGCTAAATCGTGCTTTG
AACCAAGAACAAGTCATTGCTGTGCACATTGATAATGGCTTTATGAGAAAACGAGAAAGC
CAGTCTGTTGAAGAGGCCCTCAAAAAGCTTGGAATTCAGGTCAAAGTGATAAATGCTGCT
CATTCTTTCTACAATGGAACAACAACCCTACCAATATCAGATGAAGATAGAACCCCACGG
AAAAGAATTAGCAAAACGTTAAATATGACCACAAGTCCTGAAGAGAAAAGAAAAATCATT
GGGGATACTTTTGTTAAGATTGCCAATGAAGTAATTGGAGAAATGAACTTGAAACCAGAG
GAGGTTTTCCTTGCCCAAGGTACTTTACGGCCTGATCTAATTGAAAGTGCATCCCTTGTT
GCAAGTGGCAAAGCTGAACTCATCAAAACCCATCACAATGACACAGAGCTCATCAGAAAG
TTGAGAGAGGAGGGAAAAGTAATAGAACCTCTGAAAGATTTTCATAAAGATGAAGTGAGA
ATTTTGGGCAGAGAACTTGGACTTCCAGAAGAGTTAGTTTCCAGGCATCCATTTCCAGGT
CCTGGCCTGGCAATCAGAGTAATATGTGCTGAAGAACCTTATATTTGTAAGGACTTTCCT
GAAACCAACAATATTTTGAAAATAGTAGCTGATTTTTCTGCAAGTGTTAAAAAGCCACAT
ACCCTATTACAGAGAGTCAAAGCCTGCACAACAGAAGAGGATCAGGAGAAGCTGATGCAA
ATTACCAGTCTGCATTCACTGAATGCCTTCTTGCTGCCAATTAAAACTGTAGGTGTGCAG
GGTGACTGTCGTTCCTACAGTTACGTGTGTGGAATCTCCAGTAAAGATGAACCTGACTGG
GAATCACTTATTTTTCTGGCTAGGCTTATACCTCGCATGTGTCACAACGTTAACAGAGTT
GTTTATATATTTGGCCCACCAGTTAAAGAACCTCCTACAGATGTTACTCCCACTTTCTTG
ACAACAGGGGTGCTCAGTACTTTACGCCAAGCTGATTTTGAGGCCCATAACATTCTCAGG
GAGTCTGGGTATGCTGGGAAAATCAGCCAGATGCCGGTGATTTTGACACCATTACATTTT
GATCGGGACCCACTTCAAAAGCAGCCTTCATGCCAGAGATCTGTGGTTATTCGAACCTTT
ATTACTAGTGACTTCATGACTGGTATACCTGCAACACCTGGCAATGAGATCCCTGTAGAG
GTGGTATTAAAGATGGTCACTGAGATTAAGAAGATTCCTGGTATTTCTCGAATTATGTAT
GACTTAACATCAAAGCCCCCAGGAACTACTGAGTGGGAGTAA
|
| Enzyme 17 GenBank Gene ID |
U10860  |
| Enzyme 17 GeneCard ID |
GMPS  |
| Enzyme 17 GenAtlas ID |
GMPS  |
| Enzyme 17 HGNC ID |
HGNC:4378  |
| Enzyme 17 Chromosome Location |
3 |
| Enzyme 17 Locus |
3q24 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Hirst M, Haliday E, Nakamura J, Lou L: Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA. J Biol Chem. 1994 Sep 23;269(38):23830-7. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
5872 |
| Enzyme 18 Name |
cGMP-inhibited 3',5'-cyclic phosphodiesterase A |
| Enzyme 18 Synonyms |
- Cyclic GMP-inhibited phosphodiesterase A
- CGI-PDE A
|
| Enzyme 18 Gene Name |
PDE3A |
| Enzyme 18 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 18 Number of Residues |
1141 |
| Enzyme 18 Molecular Weight |
124980 |
| Enzyme 18 Theoretical pI |
5.87 |
| Enzyme 18 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 18 General Function |
Not Available |
| Enzyme 18 Specific Function |
Hydrolyzes both cyclic AMP (cAMP) and cyclic GMP (cGMP) |
| 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 |
- 61-83
- 129-151
- 158-180
- 184-206
- 238-255
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
38201493  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q14432  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
PDE3A_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 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 18 GenBank Gene ID |
M91667  |
| Enzyme 18 GeneCard ID |
PDE3A  |
| Enzyme 18 GenAtlas ID |
PDE3A  |
| Enzyme 18 HGNC ID |
HGNC:8778  |
| Enzyme 18 Chromosome Location |
Not Available |
| Enzyme 18 Locus |
Not Available |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 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 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
5876 |
| Enzyme 19 Name |
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A |
| Enzyme 19 Synonyms |
Not Available |
| Enzyme 19 Gene Name |
PDE10A |
| Enzyme 19 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 19 Number of Residues |
779 |
| Enzyme 19 Molecular Weight |
88413 |
| Enzyme 19 Theoretical pI |
6.57 |
| 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 |
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 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 |
4958858  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9Y233  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
PDE10_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 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 19 GenBank Gene ID |
AB020593  |
| Enzyme 19 GeneCard ID |
PDE10A  |
| Enzyme 19 GenAtlas ID |
PDE10A  |
| Enzyme 19 HGNC ID |
HGNC:8772  |
| Enzyme 19 Chromosome Location |
Not Available |
| Enzyme 19 Locus |
Not Available |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 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 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
5877 |
| Enzyme 20 Name |
Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C |
| Enzyme 20 Synonyms |
- Cam-PDE 1C
- hCam-3
|
| Enzyme 20 Gene Name |
PDE1C |
| Enzyme 20 Protein Sequence |
>Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
MESPTKEIEEFESNSLKYLQPEQIEKIWLRLRGLRKYKKTSQRLRSLVKQLERGEASVVD
LKKNLEYAATVLESVYIDETRRLLDTEDELSDIQSDAVPSEVRDWLASTFTRQMGMMLRR
SDEKPRFKSIVHAVQAGIFVERMYRRTSNMVGLSYPPAVIEALKDVDKWSFDVFSLNEAS
GDHALKFIFYELLTRYDLISRFKIPISALVSFVEALEVGYSKHKNPYHNLMHAADVTQTV
HYLLYKTGVANWLTELEIFAIIFSAAIHDYEHTGTTNNFHIQTRSDPAILYNDRSVLENH
HLSAAYRLLQDDEEMNILINLSKDDWREFRTLVIEMVMATDMSCHFQQIKAMKTALQQPE
AIEKPKALSLMLHTADISHPAKAWDLHHRWTMSLLEEFFRQGDREAELGLPFSPLCDRKS
TMVAQSQVGFIDFIVEPTFTVLTDMTEKIVSPLIDETSQTGGTGQRRSSLNSISSSDAKR
SGVKTSGSEGSAPINNSVISVDYKSFKATWTEVVHINRERWRAKVPKEEKAKKEAEEKAR
LAAEEQQKEMEAKSQAEEGASGKAEKKTSGETKNQVNGTRANKSDNPRGKNSKAEKSSGE
QQQNGDFKDGKNKTDKKDHSNIGNDSKKTDGTKQRSHGSPAPSTSSTCRLTLPVIKPPLR
HFKRPAYASSSYAPSVSKKTDEHPARYKMLDQRIKMKKIQNISHNWNRK
|
| Enzyme 20 Number of Residues |
709 |
| Enzyme 20 Molecular Weight |
80761 |
| Enzyme 20 Theoretical pI |
9.31 |
| 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 |
Not Available |
| Enzyme 20 Specific Function |
Has a high affinity for both cAMP and cGMP |
| 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 |
1151111  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q14123  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
PDE1C_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 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 20 GenBank Gene ID |
U40371  |
| Enzyme 20 GeneCard ID |
PDE1C  |
| Enzyme 20 GenAtlas ID |
PDE1C  |
| Enzyme 20 HGNC ID |
HGNC:8776  |
| Enzyme 20 Chromosome Location |
Not Available |
| Enzyme 20 Locus |
Not Available |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 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 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
5881 |
| Enzyme 21 Name |
cAMP-specific 3',5'-cyclic phosphodiesterase 4B |
| Enzyme 21 Synonyms |
- DPDE4
- PDE32
|
| Enzyme 21 Gene Name |
PDE4B |
| Enzyme 21 Protein Sequence |
>cAMP-specific 3',5'-cyclic phosphodiesterase 4B
MKKSRSVMTVMADDNVKDYFECSLSKSYSSSSNTLGIDLWRGRRCCSGNLQLPPLSQRQS
ERARTPEGDGISRPTTLPLTTLPSIAITTVSQECFDVENGPSPGRSPLDPQASSSAGLVL
HATFPGHSQRRESFLYRSDSDYDLSPKAMSRNSSLPSEQHGDDLIVTPFAQVLASLRSVR
NNFTILTNLHGTSNKRSPAASQPPVSRVNPQEESYQKLAMETLEELDWCLDQLETIQTYR
SVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQNDVEIPSPTQKDREKKK
KQQLMTQISGVKKLMHSSSLNNTSISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSH
NRPLTCIMYAIFQERDLLKTFRISSDTFITYMMTLEDHYHSDVAYHNSLHAADVAQSTHV
LLSTPALDAVFTDLEILAAIFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHL
AVGFKLLQEEHCDIFMNLTKKQRQTLRKMVIDMVLATDMSKHMSLLADLKTMVETKKVTS
SGVLLLDNYTDRIQVLRNMVHCADLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEI
SPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILDTLEDNRNWYQSMIPQSP
SPPLDEQNRDCQGLMEKFQFELTLDEEDSEGPEKEGEGHSYFSSTKTLCVIDPENRDSLG
ETDIDIATEDKSPVDT
|
| Enzyme 21 Number of Residues |
736 |
| Enzyme 21 Molecular Weight |
83344 |
| Enzyme 21 Theoretical pI |
4.89 |
| Enzyme 21 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 21 General Function |
Not Available |
| Enzyme 21 Specific Function |
May be involved in mediating central nervous system effects of therapeutic agents ranging from antidepressants to antiasthmatic and anti-inflammatory agents |
| 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 |
347122  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q07343  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
PDE4B_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 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 21 GenBank Gene ID |
L20966  |
| Enzyme 21 GeneCard ID |
PDE4B  |
| Enzyme 21 GenAtlas ID |
PDE4B  |
| Enzyme 21 HGNC ID |
HGNC:8781  |
| Enzyme 21 Chromosome Location |
Not Available |
| Enzyme 21 Locus |
Not Available |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 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 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
5888 |
| Enzyme 22 Name |
High-affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A |
| Enzyme 22 Synonyms |
Not Available |
| Enzyme 22 Gene Name |
PDE9A |
| Enzyme 22 Protein Sequence |
>High-affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAM
VSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRRE
GAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANH
LAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDV
PTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLF
CVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYN
NTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLI
LATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCL
LEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIML
QPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA
|
| Enzyme 22 Number of Residues |
593 |
| Enzyme 22 Molecular Weight |
68493 |
| Enzyme 22 Theoretical pI |
6.10 |
| Enzyme 22 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 22 General Function |
Not Available |
| Enzyme 22 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 22 Pathways |
Not Available |
| Enzyme 22 Reactions |
- guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
3242777  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
O76083  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
PDE9A_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 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 22 GenBank Gene ID |
AF048837  |
| Enzyme 22 GeneCard ID |
PDE9A  |
| Enzyme 22 GenAtlas ID |
PDE9A  |
| Enzyme 22 HGNC ID |
HGNC:8795  |
| Enzyme 22 Chromosome Location |
Not Available |
| Enzyme 22 Locus |
Not Available |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 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 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
5889 |
| Enzyme 23 Name |
cGMP-dependent 3',5'-cyclic phosphodiesterase |
| Enzyme 23 Synonyms |
- Cyclic GMP-stimulated phosphodiesterase
- CGS-PDE
- cGSPDE
|
| Enzyme 23 Gene Name |
PDE2A |
| Enzyme 23 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 23 Number of Residues |
941 |
| Enzyme 23 Molecular Weight |
105718 |
| Enzyme 23 Theoretical pI |
5.08 |
| 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 |
Hydrolyzes both cyclic AMP (cAMP) and cyclic GMP (cGMP) |
| 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 |
2108052  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
O00408  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
PDE2A_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 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 23 GenBank Gene ID |
U67733  |
| Enzyme 23 GeneCard ID |
PDE2A  |
| Enzyme 23 GenAtlas ID |
PDE2A  |
| Enzyme 23 HGNC ID |
HGNC:8777  |
| Enzyme 23 Chromosome Location |
11 |
| Enzyme 23 Locus |
11q13.4 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 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 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
5893 |
| Enzyme 24 Name |
Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] |
| Enzyme 24 Synonyms |
- Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase
- Diadenosine tetraphosphatase
- Ap4A hydrolase
- Ap4Aase
- Nucleoside diphosphate-linked moiety X motif 2
- Nudix motif 2
|
| Enzyme 24 Gene Name |
NUDT2 |
| Enzyme 24 Protein Sequence |
>Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
MALRACGLIIFRRCLIPKVDNNAIEFLLLQASDGIHHWTPPKGHVEPGEDDLETALRETQ
EEAGIEAGQLTIIEGFKRELNYVARNKPKTVIYWLAEVKDYDVEIRLSHEHQAYRWLGLE
EACQLAQFKEMKAALQEGHQFLCSIEA
|
| Enzyme 24 Number of Residues |
147 |
| Enzyme 24 Molecular Weight |
16829 |
| Enzyme 24 Theoretical pI |
5.06 |
| Enzyme 24 GO Classification |
| Function |
- bis(5'-nucleosyl)-tetraphosphatase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
- nucleotide diphosphatase activity
- pyrophosphatase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 24 General Function |
Replication, recombination and repair |
| Enzyme 24 Specific Function |
Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis |
| Enzyme 24 Pathways |
|
| Enzyme 24 Reactions |
- P1,P4-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
1050960  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
P50583  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
AP4A_HUMAN  |
| Enzyme 24 PDB ID |
1XSC  |
| Enzyme 24 PDB File |
Show |
| Enzyme 24 3D Structure |
|
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>60 bp
ATGCCAGCCCTGTTTTACAGGGAGCCCTGGAGGAGTTGGGATAGAGGCCACATTGACTGA
|
| Enzyme 24 GenBank Gene ID |
U30313  |
| Enzyme 24 GeneCard ID |
NUDT2  |
| Enzyme 24 GenAtlas ID |
NUDT2  |
| Enzyme 24 HGNC ID |
HGNC:8049  |
| Enzyme 24 Chromosome Location |
Not Available |
| Enzyme 24 Locus |
Not Available |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Thorne NM, Hankin S, Wilkinson MC, Nunez C, Barraclough R, McLennan AG: Human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase is a member of the MutT family of nucleotide pyrophosphatases. Biochem J. 1995 Nov 1;311 ( Pt 3):717-21. [PubMed
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
5896 |
| Enzyme 25 Name |
Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha |
| Enzyme 25 Synonyms |
- GMP-PDE alpha
- PDE V-B1
|
| Enzyme 25 Gene Name |
PDE6A |
| Enzyme 25 Protein Sequence |
>Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
MGEVTAEEVEKFLDSNIGFAKQYYNLHYRAKLISDLLGAKEAAVDFSNYHSPSSMEESEI
IFDLLRDFQENLQTEKCIFNVMKKLCFLLQADRMSLFMYRTRNGIAELATRLFNVHKDAV
LEDCLVMPDQEIVFPLDMGIVGHVAHSKKIANVPNTEEDEHFCDFVDILTEYKTKNILAS
PIMNGKDVVAIIMAVNKVDGSHFTKRDEEILLKYLNFANLIMKWYHLSYLHNCETRRGQI
LLWSGSKVFEELTDIERQFHKALYTVRAFLNCDRYSVGLLDMTKQKEFFDVWPVLMGEVP
PYSGPRTPDGREINFYKVIDYILHGKEDIKVIPNPPPDHWALVSGLPAYVAQNGLICNIM
NAPAEDFFAFQKEPLDESGWMIKNVLSMPIVNKKEEIVGVATFYNRKDGKPFDEMDETLM
ESLTQFLGWSVLNPDTYESMNKLENRKDIFQDIVKYHVKCDNEEIQKILKTREVYGKEPW
ECEEEELAEILQAELPDADKYEINKFHFSDLPLTELELVKCGIQMYYELKVVDKFHIPQE
ALVRFMYSLSKGYRKITYHNWRHGFNVGQTMFSLLVTGKLKRYFTDLEALAMVTAAFCHD
IDHRGTNNLYQMKSQNPLAKLHGSSILERHHLEFGKTLLRDESLNIFQNLNRRQHEHAIH
MMDIAIIATDLALYFKKRTMFQKIVDQSKTYESEQEWTQYMMLEQTRKEIVMAMMMTACD
LSAITKPWEVQSQVALLVAAEFWEQGDLERTVLQQNPIPMMDRNKADELPKLQVGFIDFV
CTFVYKEFSRFHEEITPMLDGITNNRKEWKALADEYDAKMKVQEEKKQKQQSAKSAAAGN
QPGGNPSPGGATTSKSCCIQ
|
| Enzyme 25 Number of Residues |
860 |
| Enzyme 25 Molecular Weight |
99636 |
| Enzyme 25 Theoretical pI |
5.48 |
| Enzyme 25 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 25 General Function |
Not Available |
| Enzyme 25 Specific Function |
This protein participates in processes of transmission and amplification of the visual signal |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
- guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
2366987  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
P16499  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
PDE6A_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>2583 bp
ATGGGCGAGGTGACAGCAGAGGAGGTGGAGAAGTTCCTGGACTCGAATATTGGCTTTGCC
AAACAGTACTACAACCTCCACTACCGGGCCAAGCTCATCTCCGACCTCCTTGGGGCCAAG
GAGGCTGCCGTGGACTTCAGCAACTACCACTCCCCGAGCAGCATGGAGGAGAGCGAAATC
ATCTTTGATCTCCTGCGGGACTTTCAGGAGAATTTACAGACAGAGAAATGCATCTTCAAT
GTCATGAAGAAGCTGTGCTTCCTCCTGCAGGCAGACCGCATGAGCCTGTTCATGTACCGG
ACCCGCAATGGCATCGCAGAGCTGGCCACCAGGCTTTTCAATGTCCACAAGGATGCTGTC
CTCGAGGACTGCCTGGTGATGCCCGACCAAGAGATCGTCTTCCCTTTGGACATGGGCATC
GTGGGCCATGTCGCACACTCTAAGAAGATTGCTAACGTCCCCAACACAGAGGAGGATGAG
CATTTCTGTGACTTTGTGGACATCCTCACAGAGTACAAGACCAAGAACATCTTGGCTTCC
CCCATAATGAATGGGAAGGATGTGGTGGCCATAATCATGGCTGTGAATAAAGTGGATGGA
TCCCACTTCACCAAGAGAGATGAAGAGATTCTTCTCAAGTACCTCAATTTTGCAAATCTA
ATCATGAAGTGGTACCACCTGAGTTACCTGCACAACTGTGAAACTCGACGTGGCCAGATA
CTGCTGTGGTCTGGGAGCAAAGTCTTTGAAGAACTTACGGACATCGAACGACAGTTCCAC
AAAGCCCTGTACACAGTCCGTGCTTTCCTCAACTGTGACAGATACTCTGTGGGTCTCTTA
GACATGACCAAGCAGAAGGAATTTTTTGATGTGTGGCCGGTTCTGATGGGTGAAGTTCCA
CCTTACTCTGGTCCCAGGACTCCGGATGGAAGAGAAATTAACTTTTACAAGGTCATTGAC
TACATCCTGCATGGCAAAGAGGACATCAAAGTCATCCCGAATCCACCTCCTGACCATTGG
GCTTTAGTAAGCGGTCTCCCCGCTTATGTTGCCCAGAATGGCCTGATTTGCAACATCATG
AACGCGCCTGCGGAGGACTTTTTTGCATTTCAGAAAGAACCTCTGGATGAGTCTGGATGG
ATGATTAAAAATGTGCTTTCAATGCCGATTGTGAACAAGAAGGAAGAAATTGTTGGAGTG
GCCACATTTTACAATCGTAAAGATGGGAAGCCCTTTGATGAAATGGATGAGACGCTCATG
GAGTCTTTGACTCAATTTCTGGGCTGGTCTGTCTTAAATCCTGACACCTATGAGTCAATG
AATAAACTTGAAAATAGGAAGGATATTTTCCAGGACATAGTAAAATATCATGTGAAGTGT
GACAATGAAGAAATTCAGAAAATCTTGAAAACCAGAGAGGTGTATGGGAAGGAGCCATGG
GAGTGTGAGGAAGAGGAGCTGGCTGAGATCCTGCAAGCGGAGCTGCCAGATGCAGATAAA
TACGAAATTAATAAATTTCACTTCAGTGACTTACCCCTAACAGAACTGGAGCTGGTAAAA
TGTGGAATACAGATGTATTATGAGCTCAAAGTGGTGGATAAATTTCACATTCCACAAGAG
GCCCTGGTGCGGTTCATGTACTCCCTGAGTAAGGGCTACCGCAAGATCACCTACCACAAC
TGGCGGCACGGCTTCAACGTGGGGCAGACCATGTTCTCCCTGCTGGTGACGGGAAAGCTG
AAGCGCTACTTCACGGACCTAGAGGCCTTGGCCATGGTCACTGCTGCTTTCTGCCATGAC
ATTGACCACAGAGGCACCAATAACCTCTACCAGATGAAATCCCAGAACCCACTGGCCAAG
CTCCATGGGTCCTCTATCTTGGAAAGACACCACTTGGAGTTTGGCAAAACACTGCTCAGA
GACGAGAGCCTGAATATCTTTCAAAACCTCAATCGTCGACAGCATGAGCATGCCATCCAC
ATGATGGACATTGCAATCATTGCCACAGACCTCGCCCTGTATTTCAAGAAGAGGACGATG
TTCCAAAAGATCGTGGATCAGTCTAAGACATATGAGAGTGAACAGGAGTGGACACAGTAC
ATGATGCTGGAGCAGACACGGAAGGAAATCGTTATGGCCATGATGATGACCGCCTGTGAT
CTCTCAGCCATCACCAAACCCTGGGAGGTGCAGAGCCAGGTAGCTCTGCTGGTGGCTGCT
GAATTCTGGGAACAAGGTGACCTGGAGCGCACGGTGCTGCAACAGAATCCCATTCCCATG
ATGGACAGAAACAAAGCAGATGAACTCCCTAAGCTTCAAGTCGGCTTCATTGACTTTGTT
TGCACCTTCGTCTACAAGGAATTCTCCCGTTTCCACGAGGAGATCACCCCAATGTTGGAC
GGGATCACCAACAATCGCAAGGAGTGGAAGGCGCTTGCTGATGAGTACGATGCCAAGATG
AAGGTGCAGGAGGAGAAGAAGCAGAAACAGCAGTCGGCCAAGTCAGCAGCCGCAGGAAAT
CAGCCGGGGGGAAACCCCAGCCCAGGGGGTGCAACTACATCCAAGTCCTGCTGCATCCAG
TAA
|
| Enzyme 25 GenBank Gene ID |
M26061  |
| Enzyme 25 GeneCard ID |
PDE6A  |
| Enzyme 25 GenAtlas ID |
PDE6A  |
| Enzyme 25 HGNC ID |
HGNC:8785  |
| Enzyme 25 Chromosome Location |
Not Available |
| Enzyme 25 Locus |
Not Available |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Pittler SJ, Baehr W, Wasmuth JJ, McConnell DG, Champagne MS, vanTuinen P, Ledbetter D, Davis RL: Molecular characterization of human and bovine rod photoreceptor cGMP phosphodiesterase alpha-subunit and chromosomal localization of the human gene. Genomics. 1990 Feb;6(2):272-83. [PubMed
]
- Huang SH, Pittler SJ, Huang X, Oliveira L, Berson EL, Dryja TP: Autosomal recessive retinitis pigmentosa caused by mutations in the alpha subunit of rod cGMP phosphodiesterase. Nat Genet. 1995 Dec;11(4):468-71. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
5902 |
| Enzyme 26 Name |
High-affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B |
| Enzyme 26 Synonyms |
- HSPDE8B
|
| Enzyme 26 Gene Name |
PDE8B |
| Enzyme 26 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 26 Number of Residues |
885 |
| Enzyme 26 Molecular Weight |
98980 |
| Enzyme 26 Theoretical pI |
6.81 |
| Enzyme 26 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 26 General Function |
Signal transduction mechanisms |
| Enzyme 26 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 26 Pathways |
|
| Enzyme 26 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
32261241  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
O95263  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
PDE8B_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 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 26 GenBank Gene ID |
AY129948  |
| Enzyme 26 GeneCard ID |
PDE8B  |
| Enzyme 26 GenAtlas ID |
PDE8B  |
| Enzyme 26 HGNC ID |
HGNC:8794  |
| Enzyme 26 Chromosome Location |
5 |
| Enzyme 26 Locus |
5q14.1 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 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 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
5906 |
| Enzyme 27 Name |
Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta precursor |
| Enzyme 27 Synonyms |
- GMP-PDE beta
|
| Enzyme 27 Gene Name |
PDE6B |
| Enzyme 27 Protein Sequence |
>Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta precursor
MSLSEEQARSFLDQNPDFARQYFGKKLSPENVGRGCEDGCPPDCDSLRDLCQVEESTALL
ELVQDMQESINMERVVFKVLRRLCTLLQADRCSLFMYRQRNGVAELATRLFSVQPDSVLE
DCLVPPDSEIVFPLDIGVVGHVAQTKKMVNVEDVAECPHFSSFADELTDYKTKNMLATPI
MNGKDVVAVIMAVNKLNGPFFTSEDEDVFLKYLNFATLYLKIYHLSYLHNCETRRGQVLL
WSANKVFEELTDIERQFHKAFYTVRAYLNCERYSVGLLDMTKEKEFFDVWSVLMGESQPY
SGPRTPDGREIVFYKVIDYILHGKEEIKVIPTPSADHWALASGLPSYVAESGFICNIMNA
SADEMFKFQEGALDDSGWLIKNVLSMPIVNKKEEIVGVATFYNRKDGKPFDEQDEVLMES
LTQFLGWSVMNTDTYDKMNKLENRKDIAQDMVLYHVKCDRDEIQLILPTRARLGKEPADC
DEDELGEILKEELPGPTTFDIYEFHFSDLECTELDLVKCGIQMYYELGVVRKFQIPQEVL
VRFLFSISKGYRRITYHNWRHGFNVAQTMFTLLMTGKLKSYYTDLEAFAMVTAGLCHDID
HRGTNNLYQMKSQNPLAKLHGSSILERHHLEFGKFLLSEETLNIYQNLNRRQHEHVIHLM
DIAIIATDLALYFKKRAMFQKIVDESKNYQDKKSWVEYLSLETTRKEIVMAMMMTACDLS
AITKPWEVQSKVALLVAAEFWEQGDLERTVLDQQPIPMMDRNKAAELPKLQVGFIDFVCT
FVYKEFSRFHEEILPMFDRLQNNRKEWKALADEYEAKVKALEEKEEEERVAAKKVGTEIC
NGGPAPKSSTCCIL
|
| Enzyme 27 Number of Residues |
854 |
| Enzyme 27 Molecular Weight |
98408 |
| Enzyme 27 Theoretical pI |
4.91 |
| Enzyme 27 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 27 General Function |
Not Available |
| Enzyme 27 Specific Function |
This protein participates in processes of transmission and amplification of the visual signal. Necessary for the formation of a functional phosphodiesterase holoenzyme |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
- guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate
|
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
252253  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
P35913  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
PDE6B_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>2565 bp
ATGAGCCTCAGTGAGGAGCAGGCCCGGAGCTTTCTGGACCAGAACCCCGATTTTGCCCGC
CAGTACTTTGGGAAGAAACTGAGCCCTGAGAATGTTGGCCGCGGCTGCGAGGACGGGTGC
CCGCCGGACTGCGACAGCCTCCGGGACCTCTGCCAGGTGGAGGAGAGCACGGCGCTGCTG
GAGCTGGTGCAGGATATGCAGGAGAGCATCAACATGGAGCGCGTGGTCTTCAAGGTCCTG
CGGCGCCTCTGCACCCTCCTGCAGGCCGACCGCTGCAGCCTCTTCATGTACCGCCAGCGC
AACGGCGTGGCCGAGCTGGCCACCAGGCTTTTCAGCGTGCAGCCGGACAGCGTCCTGGAG
GACTGCCTGGTGCCCCCCGACTCCGAGATCGTCTTCCCACTGGACATCGGGGTCGTGGGC
CACGTGGCTCAGACCAAAAAGATGGTGAACGTCGAGGACGTGGCCGAGTGCCCTCACTTC
AGCTCATTTGCTGACGAGCTCACTGACTACAAGACAAAGAATATGCTGGCCACACCCATC
ATGAATGGCAAAGACGTCGTGGCGGTGATCATGGCAGTGAACAAGCTCAACGGCCCATTC
TTCACCAGCGAAGACGAAGATGTGTTCTTGAAGTACCTGAATTTTGCCACGTTGTACCTG
AAGATCTATCACCTGAGCTACCTCCACAACTGCGAGACGCGCCGCGGCCAGGTGCTGCTG
TGGTCGGCCAACAAGGTGTTTGAGGAGCTGACGGACATCGAGAGGCAGTTCCACAAGGCC
TTCTACACGGTGCGGGCCTACCTCAACTGCGAGCGGTACTCCGTGGGCCTCCTGGACATG
ACCAAGGAGAAGGAATTTTTTGACGTGTGGTCTGTGCTGATGGGAGAGTCCCAGCCGTAC
TCGGGCCCACGCACGCCTGATGGCCGGGAAATTGTCTTCTACAAAGTGATCGACTACATC
CTCCACGGCAAGGAGGAGATCAAGGTCATTCCCACACCCTCAGCCGATCACTGGGCCCTG
GCCAGCGGCCTTCCAAGCTACGTGGCAGAAAGCGGCTTTATTTGTAACATCATGAATGCT
TCCGCTGACGAAATGTTCAAATTTCAGGAAGGGGCCCTGGACGACTCCGGGTGGCTCATC
AAGAATGTGCTGTCCATGCCCATCGTCAACAAGAAGGAGGAGATTGTGGGAGTCGCCACA
TTTTACAACAGGAAAGACGGGAAGCCCTTTGACGAACAGGACGAGGTTCTCATGGAGTCC
CTGACACAGTTCCTGGGCTGGTCAGTGATGAACACCGACACCTACGACAAGATGAACAAG
CTGGAGAACCGCAAGGACATCGCACAGGACATGGTCCTTTACCACGTGAAGTGCGACAGG
GACGAGATCCAGCTCATCCTGCCAACCAGAGCGCGCCTGGGGAAGGAGCCTGCTGACTGC
GATGAGGACGAGCTGGGCGAAATCCTGAAGGAGGAGCTGCCAGGGCCCACCACATTTGAC
ATCTACGAATTCCACTTCTCTGACCTGGAGTGCACCGAACTGGACCTGGTCAAATGTGGC
ATCCAGATGTACTACGAGCTGGGCGTGGTCCGAAAGTTCCAGATCCCCCAGGAGGTCCTG
GTGCGGTTCCTGTTCTCCATCAGCAAAGGGTACCGGAGAATCACCTACCACAACTGGCGC
CACGGCTTCAACGTGGCCCAGACGATGTTCACGCTGCTCATGACCGGCAAACTGAAGAGC
TACTACACGGACCTGGAGGCCTTCGCCATGGTGACAGCCGGCCTGTGCCATGACATCGAC
CACCGCGGCACCAACAACCTGTACCAGATGAAGTCCCAGAACCCCTTGGCTAAGCTCCAC
GGCTCCTCGATTTTGGAGCGGCACCACCTGGAGTTTGGGAAGTTCCTGCTCTCGGAGGAG
ACCCTGAACATCTACCAGAACCTGAACCGGCGGCAGCACGAGCACGTGATCCACCTGATG
GACATCGCCATCATCGCCACGGACCTGGCCCTGTACTTCAAGAAGAGAGCGATGTTTCAG
AAGATCGTGGATGAGTCCAAGAACTACCAGGACAAGAAGAGCTGGGTGGAGTACCTGTCC
CTGGAGACGACCCGGAAGGAGATCGTCATGGCCATGATGATGACAGCCTGCGACCTGTCT
GCCATCACCAAGCCCTGGGAAGTCCAGAGCAAGGTCGCACTTCTCGTGGCTGCTGAGTTC
TGGGAGCAAGGTGACTTGGAAAGGACAGTCTTGGATCAGCAGCCCATTCCTATGATGGAC
CGGAACAAGGCGGCCGAGCTCCCCAAGCTGCAAGTGGGCTTCATCGACTTCGTGTGCACA
TTCGTGTACAAGGAGTTCTCTCGTTTCCACGAAGAGATCCTGCCCATGTTCGACCGACTG
CAGAACAATAGGAAAGAGTGGAAGGCGCTGGCTGATGAGTATGAGGCCAAAGTGAAGGCT
CTGGAGGAGAAGGAGGAGGAGGAGAGGGTGGCAGCCAAGAAAGTAGGCACAGAAATTTGC
AATGGCGGCCCAGCACCCAAGTCTTCAACCTGCTGTATCCTGTGA
|
| Enzyme 27 GenBank Gene ID |
S41458  |
| Enzyme 27 GeneCard ID |
PDE6B  |
| Enzyme 27 GenAtlas ID |
PDE6B  |
| Enzyme 27 HGNC ID |
HGNC:8786  |
| Enzyme 27 Chromosome Location |
4 |
| Enzyme 27 Locus |
4p16.3 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Khramtsov NV, Feshchenko EA, Suslova VA, Shmukler BE, Terpugov BE, Rakitina TV, Atabekova NV, Lipkin VM: The human rod photoreceptor cGMP phosphodiesterase beta-subunit. Structural studies of its cDNA and gene. FEBS Lett. 1993 Aug 2;327(3):275-8. [PubMed
]
- Khramtsov NV, Feshchenko EA, Suslova VA, Terpugov BE, Rakitina TV, Atabekova NV, Shmukler BE, Lipkin VM: [Structural studies of cDNA and the gene for the beta-subunit of cGMP phosphodiesterase from human retina] Bioorg Khim. 1992 Dec;18(12):1551-4. [PubMed
]
- Collins C, Hutchinson G, Kowbel D, Riess O, Weber B, Hayden MR: The human beta-subunit of rod photoreceptor cGMP phosphodiesterase: complete retinal cDNA sequence and evidence for expression in brain. Genomics. 1992 Jul;13(3):698-704. [PubMed
]
- Weber B, Riess O, Hutchinson G, Collins C, Lin BY, Kowbel D, Andrew S, Schappert K, Hayden MR: Genomic organization and complete sequence of the human gene encoding the beta-subunit of the cGMP phosphodiesterase and its localisation to 4p 16.3. Nucleic Acids Res. 1991 Nov 25;19(22):6263-8. [PubMed
]
- Suslova VA, Suslov ON, Kim EE, Lipkin VM: [Organization of the gene for the beta-subunit of human photoreceptor cyclic GMP phosphodiesterase] Bioorg Khim. 1996 Apr;22(4):256-63. [PubMed
]
- McLaughlin ME, Sandberg MA, Berson EL, Dryja TP: Recessive mutations in the gene encoding the beta-subunit of rod phosphodiesterase in patients with retinitis pigmentosa. Nat Genet. 1993 Jun;4(2):130-4. [PubMed
]
- Gal A, Orth U, Baehr W, Schwinger E, Rosenberg T: Heterozygous missense mutation in the rod cGMP phosphodiesterase beta-subunit gene in autosomal dominant stationary night blindness. Nat Genet. 1994 May;7(1):64-8. [PubMed
]
- Gal A, Orth U, Baehr W, Schwinger E, Rosenberg T: Heterozygous missense mutation in the rod cGMP phosphodiesterase beta-subunit gene in autosomal dominant stationary night blindness. Nat Genet. 1994 Aug;7(4):551. [PubMed
]
- Danciger M, Blaney J, Gao YQ, Zhao DY, Heckenlively JR, Jacobson SG, Farber DB: Mutations in the PDE6B gene in autosomal recessive retinitis pigmentosa. Genomics. 1995 Nov 1;30(1):1-7. [PubMed
]
- Gao YQ, Danciger M, Zhao DY, Blaney J, Piriev NI, Shih J, Jacobson SG, Heckenlively JH, Farber DB: Screening of the PDE6B gene in patients with autosomal dominant retinitis pigmentosa. Exp Eye Res. 1996 Feb;62(2):149-54. [PubMed
]
- Valverde D, Solans T, Grinberg D, Balcells S, Vilageliu L, Bayes M, Chivelet P, Besmond C, Goossens M, Gonzalez-Duarte R, Baiget M: A novel mutation in exon 17 of the beta-subunit of rod phosphodiesterase in two RP sisters of a consanguineous family. Hum Genet. 1996 Jan;97(1):35-8. [PubMed
]
- Valverde D, Baiget M, Seminago R, del Rio E, Garcia-Sandoval B, del Rio T, Bayes M, Balcells S, Martinez A, Grinberg D, Ayuso C: Identification of a novel R552O mutation in exon 13 of the beta-subunit of rod phosphodiesterase gene in a Spanish family with autosomal recessive retinitis pigmentosa. Hum Mutat. 1996;8(4):393-4. [PubMed
]
- Saga M, Mashima Y, Akeo K, Kudoh J, Oguchi Y, Shimizu N: A novel homozygous Ile535Asn mutation in the rod cGMP phosphodiesterase beta-subunit gene in two brothers of a Japanese family with autosomal recessive retinitis pigmentosa. Curr Eye Res. 1998 Mar;17(3):332-5. [PubMed
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
5908 |
| Enzyme 28 Name |
cAMP-specific 3',5'-cyclic phosphodiesterase 4D |
| Enzyme 28 Synonyms |
- DPDE3
- PDE43
|
| Enzyme 28 Gene Name |
PDE4D |
| Enzyme 28 Protein Sequence |
>cAMP-specific 3',5'-cyclic phosphodiesterase 4D
MEAEGSSAPARAGSGEGSDSAGGATLKAPKHLWRHEQHHQYPLRQPQFRLLHPHHHLPPP
PPPSPQPQPQCPLQPPPPPPLPPPPPPPGAARGRYASSGATGRVRHRGYSDTERYLYCRA
MDRTSYAVETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTSAGRSPLDPMTSPGSGLILQA
NFVHSQRRESFLYRSDSDYDLSPKSMSRNSSIASDIHGDDLIVTPFAQVLASLRTVRNNF
AALTNLQDRAPSKRSPMCNQPSINKATITEEAYQKLASETLEELDWCLDQLETLQTRHSV
SEMASNKFKRMLNRELTHLSEMSRSGNQVSEFISNTFLDKQHEVEIPSPTQKEKEKKKRP
MSQISGVKKLMHSSSLTNSSIPRFGVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPL
TVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLST
PALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGF
KLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVL
LLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMC
DKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQSPSPAP
DDPEEGRQGQTEKFQFELTLEEDGESDTEKDSGSQVEEDTSCSDSKTLCTQDSESTEIPL
DEQVEEEAVGEEEESQPEACVIDDRSPDT
|
| Enzyme 28 Number of Residues |
809 |
| Enzyme 28 Molecular Weight |
91116 |
| Enzyme 28 Theoretical pI |
5.25 |
| Enzyme 28 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 28 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 28 Specific Function |
Regulates the levels of cAMP in the cell |
| Enzyme 28 Pathways |
|
| Enzyme 28 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
347130  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
Q08499  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
PDE4D_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 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 28 GenBank Gene ID |
L20970  |
| Enzyme 28 GeneCard ID |
PDE4D  |
| Enzyme 28 GenAtlas ID |
PDE4D  |
| Enzyme 28 HGNC ID |
HGNC:8783  |
| Enzyme 28 Chromosome Location |
5 |
| Enzyme 28 Locus |
5q12 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 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 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
5909 |
| Enzyme 29 Name |
Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma |
| Enzyme 29 Synonyms |
- GMP-PDE gamma
|
| Enzyme 29 Gene Name |
PDE6G |
| Enzyme 29 Protein Sequence |
>Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
MNLEPPKAEFRSATRVAGGPVTPRKGPPKFKQRQTRQFKSKPPKKGVQGFGDDIPGMEGL
GTDITVICPWEAFNHLELHELAQYGII
|
| Enzyme 29 Number of Residues |
87 |
| Enzyme 29 Molecular Weight |
9643 |
| Enzyme 29 Theoretical pI |
10.16 |
| Enzyme 29 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 29 General Function |
Not Available |
| Enzyme 29 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 29 Pathways |
|
| Enzyme 29 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
189703  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
P18545  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
CNRG_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>264 bp
ATGAACCTGGAACCGCCCAAGGCTGAGTTCCGGTCAGCCACCAGGGTGGCCGGGGGACCT
GTCACCCCCAGGAAAGGGCCCCCTAAATTTAAGCAGCGACAGACCAGGCAGTTCAAGAGC
AAGCCCCCAAAGAAAGGCGTTCAAGGGTTTGGGGACGACATCCCTGGAATGGAAGGCCTG
GGAACAGACATCACAGTCATCTGCCCTTGGGAGGCCTTCAACCACCTGGAGCTGCACGAG
CTGGCCCAATATGGCATCATCTAG
|
| Enzyme 29 GenBank Gene ID |
M36476  |
| Enzyme 29 GeneCard ID |
PDE6G  |
| Enzyme 29 GenAtlas ID |
PDE6G  |
| Enzyme 29 HGNC ID |
HGNC:8789  |
| Enzyme 29 Chromosome Location |
17 |
| Enzyme 29 Locus |
17q25 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 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 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
5913 |
| Enzyme 30 Name |
Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta |
| Enzyme 30 Synonyms |
- GMP-PDE delta
- p17 protein
|
| Enzyme 30 Gene Name |
PDE6D |
| Enzyme 30 Protein Sequence |
>Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
MSAKDERAREILRGFKLNWMNLRDAETGKILWQGTEDLSVPGVEHEARVPKKILKCKAVS
RELNFSSTEQMEKFRLEQKVYFKGQCLEEWFFEFGFVIPNSTNTWQSLIEAAPESQMMPA
SVLTGNVIIETKFFDDDLLVSTSRVRLFYV
|
| Enzyme 30 Number of Residues |
150 |
| Enzyme 30 Molecular Weight |
17420 |
| Enzyme 30 Theoretical pI |
5.35 |
| Enzyme 30 GO Classification |
Not Available |
| Enzyme 30 General Function |
Not Available |
| Enzyme 30 Specific Function |
Guanosine 3',5'-cyclic phosphate + H(2)O = guanosine 5'-phosphate |
| Enzyme 30 Pathways |
|
| Enzyme 30 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
2896020  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
O43924  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
PDE6D_HUMAN  |
| Enzyme 30 PDB ID |
1KSG  |
| Enzyme 30 PDB File |
Show |
| Enzyme 30 3D Structure |
|
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>453 bp
ATGTCAGCCAAGGACGAGCGGGCCAGGGAGATCCTGAGGGGCTTCAAACTAAATTGGATG
AACCTTCGGGATGCTGAGACAGGGAAGATACTCTGGCAAGGAACAGAAGACCTGTCTGTC
CCTGGTGTGGAGCATGAAGCCCGTGTTCCCAAGAAAATCCTCAAGTGCAAGGCAGTGTCT
CGAGAACTTAATTTTTCTTCGACAGAACAAATGGAAAAATTCCGCCTGGAACAAAAAGTT
TACTTCAAAGGGCAATGCCTAGAAGAATGGTTCTTCGAGTTTGGCTTTGTGATCCCTAAC
TCCACAAATACCTGGCAGTCCTTGATAGAGGCAGCACCCGAGTCCCAGATGATGCCAGCA
AGCGTCTTAACTGGGAACGTTATCATAGAAACAAAGTTTTTTGACGACGATCTTCTTGTA
AGCACATCCAGAGTGAGACTTTTCTATGTTTGA
|
| Enzyme 30 GenBank Gene ID |
AF045999  |
| Enzyme 30 GeneCard ID |
PDE6D  |
| Enzyme 30 GenAtlas ID |
PDE6D  |
| Enzyme 30 HGNC ID |
HGNC:8788  |
| Enzyme 30 Chromosome Location |
2 |
| Enzyme 30 Locus |
2q35-q36 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 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 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
5922 |
| Enzyme 31 Name |
cAMP-specific 3',5'-cyclic phosphodiesterase 4A |
| Enzyme 31 Synonyms |
- DPDE2
- PDE46
|
| Enzyme 31 Gene Name |
PDE4A |
| Enzyme 31 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 31 Number of Residues |
886 |
| Enzyme 31 Molecular Weight |
98144 |
| Enzyme 31 Theoretical pI |
4.87 |
| Enzyme 31 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 31 General Function |
Not Available |
| Enzyme 31 Specific Function |
Adenosine 3',5'-cyclic phosphate + H(2)O = adenosine 5'-phosphate |
| Enzyme 31 Pathways |
|
| Enzyme 31 Reactions |
- nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
347120  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
P27815  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
PDE4A_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 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 31 GenBank Gene ID |
L20965  |
| Enzyme 31 GeneCard ID |
PDE4A  |
| Enzyme 31 GenAtlas ID |
PDE4A  |
| Enzyme 31 HGNC ID |
HGNC:8780  |
| Enzyme 31 Chromosome Location |
19 |
| Enzyme 31 Locus |
19p13.2 |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 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 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
5927 |
| Enzyme 32 Name |
cGMP-specific 3',5'-cyclic phosphodiesterase |
| Enzyme 32 Synonyms |
- CGB-PDE
- cGMP-binding cGMP-specific phosphodiesterase
|
| Enzyme 32 Gene Name |
PDE5A |
| Enzyme 32 Protein Sequence |
>cGMP-specific 3',5'-cyclic phosphodiesterase
MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAE
RVHTIPVCKEGIRGHTESCSCPLQQSPRADNSVPGTPTRKISASEFDRPLRPIVVKDSEG
TVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLI
SADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPL
NIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDE
KDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIIS
FMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTME
PLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGK
VKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETREL
QSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWIL
SVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGV
NNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAI
LATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAE
LVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCF
PLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRN
|
| Enzyme 32 Number of Residues |
875 |
| Enzyme 32 Molecular Weight |
100014 |
| Enzyme 32 Theoretical pI |
6.00 |
| Enzyme 32 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 32 General Function |
Not Available |
| Enzyme 32 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 32 Pathways |
Not Available |
| Enzyme 32 Reactions |
- guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate
|
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
3420185  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
O76074  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
PDE5A_HUMAN  |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 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 32 GenBank Gene ID |
AF043731  |
| Enzyme 32 GeneCard ID |
PDE5A  |
| Enzyme 32 GenAtlas ID |
PDE5A  |
| Enzyme 32 HGNC ID |
HGNC:8784  |
| Enzyme 32 Chromosome Location |
4 |
| Enzyme 32 Locus |
4q25-q27 |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 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 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
5951 |
| Enzyme 33 Name |
GMP reductase 2 |
| Enzyme 33 Synonyms |
- Guanosine 5'-monophosphate oxidoreductase 2
- Guanosine monophosphate reductase 2
|
| Enzyme 33 Gene Name |
GMPR2 |
| Enzyme 33 Protein Sequence |
>GMP reductase 2
MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPIIAANMDTVGT
FEMAKVLCKFSLFTAVHKHYSLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAI
PQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGI
GPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVM
LGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGD
VEHTIRDILGGIRSTCTYVGAAKLKELSRRTTFIRVTQQVNPIFSEAC
|
| Enzyme 33 Number of Residues |
348 |
| Enzyme 33 Molecular Weight |
37875 |
| Enzyme 33 Theoretical pI |
7.25 |
| Enzyme 33 GO Classification |
| Function |
- GMP reductase activity
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on NADH or NADPH
- oxidoreductase activity, acting on NADH or NADPH, nitrogenous group as acceptor
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 33 General Function |
Nucleotide transport and metabolism |
| Enzyme 33 Specific Function |
Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. Plays a role in modulating cellular differentiation |
| Enzyme 33 Pathways |
|
| Enzyme 33 Reactions |
- inosine 5'-phosphate + ammonia + NADP+ = guanosine 5'-phosphate + NADPH + H+
|
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
23451216  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
Q9P2T1  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
GMPR2_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>1047 bp
ATGCCTCATATTGACAACGATGTGAAACTGGACTTCAAGGATGTCCTTTTGAGGCCCAAA
CGCAGTACCCTTAAGTCTCGAAGTGAGGTGGATCTCACAAGATCCTTTTCATTTCGGAAC
TCAAAGCAGACATACTCTGGGGTTCCCATCATTGCTGCCAATATGGATACTGTGGGCACC
TTTGAGATGGCCAAGGTTCTCTGTAAGTTCTCTCTCTTCACTGCTGTCCATAAGCACTAT
AGCCTCGTTCAGTGGCAAGAGTTTGCTGGCCAGAATCCTGACTGTCTTGAGCATCTGGCT
GCCAGCTCAGGCACAGGCTCTTCTGACTTTGAGCAGCTGGAACAGATCCTGGAAGCTATT
CCCCAGGTGAAGTATATATGCCTGGATGTGGCAAATGGCTACTCTGAACACTTTGTTGAA
TTTGTAAAAGATGTACGGAAGCGCTTCCCCCAGCACACCATCATGGCAGGGAATGTGGTA
ACAGGAGAGATGGTAGAAGAGCTCATCCTTTCTGGGGCTGACATCATCAAAGTGGGAATT
GGGCCAGGCTCTGTGTGTACTACTCGGAAGAAAACTGGAGTGGGGTATCCACAGCTCAGC
GCAGTGATGGAGTGTGCAGATGCTGCTCATGGCCTCAAAGGCCACATCATTTCAGATGGA
GGTTGCAGCTGTCCTGGGGATGTGGCCAAGGCTTTTGGGGCAGGAGCTGACTTCGTGATG
CTGGGTGGCATGCTGGCTGGGCACAGTGAGTCAGGTGGTGAGCTCATCGAGAGGGATGGC
AAGAAGTACAAGCTCTTCTATGGAATGAGTTCTGAAATGGCCATGAAGAAGTATGCTGGG
GGCGTGGCTGAGTACAGAGCCTCAGAGGGAAAGACAGTGGAAGTTCCTTTTAAAGGAGAT
GTGGAACATACCATCCGAGACATCCTAGGAGGGATCCGCTCTACGTGTACCTATGTGGGA
GCAGCTAAGCTCAAAGAGTTGAGCAGGAGAACTACCTTCATCCGAGTCACCCAGCAGGTG
AATCCAATCTTCAGTGAGGCGTGCTAG
|
| Enzyme 33 GenBank Gene ID |
AF419346  |
| Enzyme 33 GeneCard ID |
GMPR2  |
| Enzyme 33 GenAtlas ID |
GMPR2  |
| Enzyme 33 HGNC ID |
HGNC:4377  |
| Enzyme 33 Chromosome Location |
14 |
| Enzyme 33 Locus |
14q12 |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
- Deng Y, Wang Z, Ying K, Gu S, Ji C, Huang Y, Gu X, Wang Y, Xu Y, Li Y, Xie Y, Mao Y: NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression, purification, and kinetic properties. Int J Biochem Cell Biol. 2002 Sep;34(9):1035-50. [PubMed
]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
5958 |
| Enzyme 34 Name |
GMP reductase 1 |
| Enzyme 34 Synonyms |
- Guanosine 5'-monophosphate oxidoreductase 1
- Guanosine monophosphate reductase 1
|
| Enzyme 34 Gene Name |
GMPR |
| Enzyme 34 Protein Sequence |
>GMP reductase 1
MPRIDADLKLDFKDVLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPIIVANMDTVGT
FEMAAVMSQHSMFTAIHKHYSLDDWKLFATNHPECLQNVAVSSGSGQNDLEKMTSILEAV
PQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKVGV
GPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVM
LGGMFSGHTECAGEVFERNGRKLKLFYGMSSDTAMNKHAGGVAEYRASEGKTVEVPYKGD
VENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQQHNTVFS
|
| Enzyme 34 Number of Residues |
345 |
| Enzyme 34 Molecular Weight |
37419 |
| Enzyme 34 Theoretical pI |
7.08 |
| Enzyme 34 GO Classification |
| Function |
- GMP reductase activity
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on NADH or NADPH
- oxidoreductase activity, acting on NADH or NADPH, nitrogenous group as acceptor
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 34 General Function |
Nucleotide transport and metabolism |
| Enzyme 34 Specific Function |
Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides |
| Enzyme 34 Pathways |
|
| Enzyme 34 Reactions |
- inosine 5'-phosphate + ammonia + NADP+ = guanosine 5'-phosphate + NADPH + H+
|
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
529232  |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
P36959  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
GMPR1_HUMAN  |
| Enzyme 34 PDB ID |
2BLE  |
| Enzyme 34 PDB File |
Show |
| Enzyme 34 3D Structure |
|
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>87 bp
ATGCCCCGCATAGATGCGGACCTCAAGCTCGACTTCAAGGATGTCCTGCTCCGACCTAAG
CGGAGCAGCCTCAAGAGCCGAGCCGAG
|
| Enzyme 34 GenBank Gene ID |
L35304  |
| Enzyme 34 GeneCard ID |
GMPR  |
| Enzyme 34 GenAtlas ID |
GMPR  |
| Enzyme 34 HGNC ID |
HGNC:4376  |
| Enzyme 34 Chromosome Location |
6 |
| Enzyme 34 Locus |
6p23 |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
- Kanno H, Huang IY, Kan YW, Yoshida A: Two structural genes on different chromosomes are required for encoding the major subunit of human red cell glucose-6-phosphate dehydrogenase. Cell. 1989 Aug 11;58(3):595-606. [PubMed
]
- Kondoh T, Kanno H, Chang L, Yoshida A: Genomic structure and expression of human guanosine monophosphate reductase. Hum Genet. 1991 Dec;88(2):219-24. [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
]
- Kondoh T, Kanno H, Chang LF, Yoshida A: Identification of common variant alleles of the human guanosine monophosphate reductase gene. Hum Genet. 1991 Dec;88(2):225-7. [PubMed
]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
6218 |
| Enzyme 35 Name |
Guanylate kinase |
| Enzyme 35 Synonyms |
- GMP kinase
|
| Enzyme 35 Gene Name |
GUK1 |
| Enzyme 35 Protein Sequence |
>Guanylate kinase
MSGPRPVVLSGPSGAGKSTLLKRLLQEHSGIFGFSVSHTTRNPRPGEENGKDYYFVTREV
MQRDIAAGDFIEHAEFSGNLYGTSKVAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYI
SVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEPGLFDVVIINDSLDQAYAE
LKEALSEEIKKAQRTGA
|
| Enzyme 35 Number of Residues |
197 |
| Enzyme 35 Molecular Weight |
21726 |
| Enzyme 35 Theoretical pI |
6.53 |
| Enzyme 35 GO Classification |
Not Available |
| Enzyme 35 General Function |
Nucleotide transport and metabolism |
| Enzyme 35 Specific Function |
Essential for recycling GMP and indirectly, cGMP |
| Enzyme 35 Pathways |
|
| Enzyme 35 Reactions |
|
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
1196436  |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
Q16774  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
KGUA_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>594 bp
ATGTCGGGCCCCAGGCCTGTGGTGCTGAGCGGGCCTTCGGGAGCTGGGAAGAGCACCCTG
CTGAAGAGGCTGCTCCAGGAGCACAGCGGCATCTTTGGCTTCAGCGTGTCCCATACCACG
AGGAACCCGAGGCCCGGCGAGGAGAACGGCAAAGATTACTACTTTGTAACCAGGGAGGTG
ATGCAGCGTGACATAGCAGCCGGCGACTTCATCGAGCATGCCGAGTTCTCGGGGAACCTG
TATGGCACGAGCAAGGTGGCGGTGCAGGCCGTGCAGGCCATGAACCGCATCTGTGTGCTG
GACGTGGACCTGCAGGGTGTGCGGAACATCAAGGCCACCGATCTGCGGCCCATCTACATC
TCTGTGCAGCCGCCTTCACTGCACGTGCTGGAGCAGCGGCTGCGGCAGCGCAACACTGAA
ACCGAGGAGAGCCTGGTGAAGCGGCTGGCTGCTGCCCAGGCCGACATGGAGAGCAGCAAG
GAGCCCGGCCTGTTTGATGTGGTCATCATTAACGACAGCCTGGACCAGGCCTACGCAGAG
CTGAAGGAGGCGCTCTCTGAGGAAATCAAGAAAGCTCAAAGGACCGGCGCCTGA
|
| Enzyme 35 GenBank Gene ID |
L76200  |
| Enzyme 35 GeneCard ID |
GUK1  |
| Enzyme 35 GenAtlas ID |
GUK1  |
| Enzyme 35 HGNC ID |
HGNC:4693  |
| Enzyme 35 Chromosome Location |
1 |
| Enzyme 35 Locus |
1q32-q41 |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 General References |
- Fitzgibbon J, Katsanis N, Wells D, Delhanty J, Vallins W, Hunt DM: Human guanylate kinase (GUK1): cDNA sequence, expression and chromosomal localisation. FEBS Lett. 1996 May 6;385(3):185-8. [PubMed
]
- Brady WA, Kokoris MS, Fitzgibbon M, Black ME: Cloning, characterization, and modeling of mouse and human guanylate kinases. J Biol Chem. 1996 Jul 12;271(28):16734-40. [PubMed
]
|
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
6352 |
| Enzyme 36 Name |
Atrial natriuretic peptide receptor B precursor |
| Enzyme 36 Synonyms |
- ANP-B
- ANPRB
- GC-B
- Guanylate cyclase B
- NPR-B
- Atrial natriuretic peptide B-type receptor
|
| Enzyme 36 Gene Name |
NPR2 |
| Enzyme 36 Protein Sequence |
>Atrial natriuretic peptide receptor B precursor
MALPSLLLLVAALAGGVRPPGARNLTLAVVLPEHNLSYAWAWPRVGPAVALAVEALGRAL
PVDLRFVSSELEGACSEYLAPLSAVDLKLYHDPDLLLGPGCVYPAASVARFASHWRLPLL
TAGAVASGFSAKNDHYRTLVRTGPSAPKLGEFVVTLHGHFNWTARAALLYLDARTDDRPH
YFTIEGVFEALQGSNLSVQHQVYAREPGGPEQATHFIRANGRIVYICGPLEMLHEILLQA
QRENLTNGDYVFFYLDVFGESLRAGPTRATGRPWQDNRTREQAQALREAFQTVLVITYRE
PPNPEYQEFQNRLLIRAREDFGVELGPSLMNLIAGCFYDGILLYAEVLNETIQEGGTRED
GLRIVEKMQGRRYHGVTGLVVMDKNNDRETDFVLWAMGDLDSGDFQPAAHYSGAEKQIWW
TGRPIPWVKGAPPSDNPPCAFDLDDPSCDKTPLSTLAIVALGTGITFIMFGVSSFLIFRK
LMLEKELASMLWRIRWEELQFGNSERYHKGAGSRLTLSLRGSSYGSLMTAHGKYQIFANT
GHFKGNVVAIKHVNKKRIELTRQVLFELKHMRDVQFNHLTRFIGACIDPPNICIVTEYCP
RGSLQDILENDSINLDWMFRYSLINDLVKGMAFLHNSIISSHGSLKSSNCVVDSRFVLKI
TDYGLASFRSTAEPDDSHALYAKKLWTAPELLSGNPLPTTGMQKADVYSFGIILQEIALR
SGPFYLEGLDLSPKEIVQKVRNGQRPYFRPSIDRTQLNEELVLLMERCWAQDPAERPDFG
QIKGFIRRFNKEGGTSILDNLLLRMEQYANNLEKLVEERTQAYLEEKRKAEALLYQILPH
SVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTLLNDLYTCFDAIIDNF
DVYKVETIGDAYMVVSGLPGRNGQRHAPEIARMALALLDAVSSFRIRHRPHDQLRLRIGV
HTGPVCAGVVGLKMPRYCLFGDTVNTASRMESNGQALKIHVSSTTKDALDELGCFQLELR
GDVEMKGKGKMRTYWLLGERKGPPGLL
|
| Enzyme 36 Number of Residues |
1047 |
| Enzyme 36 Molecular Weight |
117024 |
| Enzyme 36 Theoretical pI |
6.86 |
| Enzyme 36 GO Classification |
| Function |
- ATP binding
- G-protein coupled receptor activity
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- lyase activity
- nucleotide binding
- peptide receptor activity, G-protein coupled
- phosphorus-oxygen lyase activity
- protein kinase activity
- purine nucleotide binding
- receptor activity
- rhodopsin-like receptor activity
- signal transducer activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transmembrane receptor activity
|
| Process |
- biopolymer metabolism
- biopolymer modification
- cell communication
- cellular metabolism
- cellular process
- cyclic nucleotide biosynthesis
- intracellular signaling cascade
- macromolecule metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide biosynthesis
- nucleotide metabolism
- physiological process
- protein amino acid phosphorylation
- protein modification
- signal transduction
|
| Component |
|
|
| Enzyme 36 General Function |
Signal transduction mechanisms |
| Enzyme 36 Specific Function |
Receptor for atrial natriuretic peptide (ANP), brain natriuretic peptide (BNP), and C-type natriuretic peptide (CNP). Has guanylate cyclase activity on binding of ligand. The activation order seems to be CNP > BNP > ANP |
| Enzyme 36 Pathways |
|
| Enzyme 36 Reactions |
- GTP = 3',5'-cyclic GMP + diphosphate
|
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
5139790  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
P20594  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
ANPRB_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>3144 bp
ATGGCGCTGCCATCACTTCTGCTGTTGGTGGCAGCCCTGGCAGGTGGGGTGCGTCCTCCC
GGGGCGCGGAACCTGACGCTGGCGGTGGTGCTGCCAGAACACAACCTGAGCTATGCCTGG
GCCTGGCCACGGGTGGGACCCGCTGTGGCACTAGCTGTGGAGGCTCTGGGCCGGGCACTG
CCCGTGGACCTGCGGTTTGTCAGCTCCGAACTGGAAGGCGCCTGCTCTGAGTACCTGGCA
CCGCTGAGCGCTGTGGACCTCAAGCTGTACCATGACCCCGACCTGCTGTTAGGTCCCGGT
TGCGTGTACCCTGCTGCCTCTGTGGCCCGCTTTGCCTCCCACTGGCGCCTTCCCCTGCTG
ACTGCGGGTGCTGTGGCCTCTGGTTTTTCGGCTAAGAATGACCATTATCGTACCCTGGTT
CGCACTGGCCCCTCTGCTCCCAAGCTGGGTGAGTTTGTGGTGACACTACACGGGCACTTC
AATTGGACTGCCCGTGCTGCCTTGCTGTACCTGGATGCTCGCACAGATGACCGGCCTCAC
TACTTCACCATCGAGGGCGTCTTTGAGGCCCTGCAGGGCAGCAACCTCAGTGTGCAGCAC
CAGGTGTATGCCCGAGAGCCAGGGGGCCCCGAGCAGGCCACCCACTTCATCCGGGCCAAC
GGGCGCATTGTGTATATCTGCGGCCCTCTGGAGATGCTGCATGAGATCCTGCTTCAGGCC
CAGAGGGAGAATCTGACCAATGGGGATTATGTCTTCTTTTACCTGGATGTCTTTGGGGAG
AGTCTCCGTGCAGGCCCCACACGTGCTACAGGCCGGCCCTGGCAGGACAATCGCACCCGG
GAACAGGCCCAGGCCCTCAGAGAGGCCTTTCAGACTGTATTGGTGATCACGTACCGAGAA
CCCCCAAATCCTGAGTATCAGGAATTCCAGAATCGTCTGCTGATAAGAGCCCGGGAAGAC
TTTGGTGTGGAGCTGGGCCCTTCCCTGATGAACCTCATCGCTGGCTGCTTCTATGATGGG
ATCCTGCTATATGCTGAAGTCCTGAATGAGACAATACAGGAAGGAGGCACCCGGGAGGAT
GGACTTCGAATTGTGGAAAAGATGCAGGGACGAAGATATCACGGTGTAACTGGGCTGGTT
GTCATGGACAAGAACAATGACCGAGAGACTGACTTTGTCCTCTGGGCCATGGGAGACCTG
GATTCTGGGGACTTTCAGCCTGCAGCCCACTACTCGGGAGCTGAGAAGCAGATTTGGTGG
ACGGGACGGCCTATTCCCTGGGTGAAGGGGGCTCCTCCCTCGGACAATCCCCCCTGTGCC
TTTGACTTGGACGACCCATCCTGTGATAAAACTCCACTTTCAACCCTGGCAATTGTGGCT
CTGGGCACAGGAATCACCTTCATCATGTTTGGTGTTTCCAGCTTCCTAATTTTCCGAAAG
CTGATGCTGGAGAAGGAGCTGGCTAGCATGTTGTGGCGTATTCGCTGGGAAGAACTGCAG
TTTGGCAACTCAGAGCGTTATCACAAAGGTGCAGGCAGTCGCCTCACACTGTCGCTGCGG
GGATCCAGTTACGGCTCGCTCATGACAGCCCATGGGAAATACCAGATCTTTGCCAACACC
GGTCACTTCAAGGGAAATGTTGTCGCCATCAAACATGTGAATAAGAAGCGCATTGAGCTG
ACCCGGCAGGTTCTGTTTGAACTCAAACATATGAGAGATGTTCAGTTCAACCATCTCACT
CGCTTCATTGGCGCCTGCATAGACCCTCCCAACATTTGCATTGTCACTGAATACTGTCCT
CGTGGGAGTTTACAGGATATTCTAGAAAATGACAGCATCAACTTGGACTGGATGTTTCGT
TATTCACTCATTAATGACCTTGTTAAGGGCATGGCCTTTCTCCACAACAGCATTATTTCA
TCGCATGGGAGTCTCAAGTCCTCCAACTGTGTGGTGGATAGTCGTTTTGTGCTCAAAATC
ACAGACTATGGCCTGGCCAGCTTCCGATCAACTGCTGAACCTGATGACAGCCATGCCCTC
TATGCCAAGAAGCTGTGGACTGCCCCAGAACTGCTCAGTGGGAACCCCTTGCCAACCACA
GGCATGCAGAAGGCTGACGTCTATAGCTTTGGGATCATCCTGCAGGAGATAGCACTTCGC
AGTGGTCCTTTCTACTTGGAGGGCCTGGACCTCAGCCCCAAAGAGATTGTCCAGAAGGTA
CGAAATGGTCAGCGGCCATATTTCCGGCCAAGCATTGACCGGTCCCAACTGAATGAAGAG
CTAGTTTTGCTGATGGAGCGATGTTGGGCTCAGGACCCAGCTGAGCGGCCAGACTTTGGA
CAGATTAAGGGCTTCATTCGGCGCTTTAACAAGGAGGGTGGCACCAGCATATTGGACAAC
CTCCTGCTGCGCATGGAACAGTATGCCAATAACTTGGAGAAGCTGGTGGAGGAACGCACA
CAGGCCTATCTGGAGGAAAAACGCAAGGCTGAAGCTCTGCTCTACCAAATCCTACCCCAT
TCAGTGGCAGAGCAGTTAAAACGGGGAGAGACTGTACAGGCTGAGGCCTTTGACAGTGTT
ACCATCTACTTCAGTGACATTGTTGGCTTCACAGCATTGTCAGCAGAGAGCACCCCCATG
CAGGTAGTGACACTTCTTAATGACCTGTATACCTGCTTTGATGCCATAATTGACAACTTT
GATGTCTACAAGGTGGAGACGATTGGGGATGCTTACATGGTGGTATCTGGCCTCCCAGGC
CGAAATGGTCAACGCCATGCACCAGAAATTGCTCGTATGGCCCTAGCATTACTAGATGCA
GTTTCTTCCTTTCGCATCCGCCACCGACCCCATGACCAGCTGAGGCTACGCATAGGGGTC
CATACTGGGCCAGTCTGTGCTGGGGTTGTTGGCCTGAAGATGCCCCGTTATTGTCTTTTT
GGAGACACAGTGAACACTGCTTCTCGAATGGAGTCTAATGGTCAAGCGCTGAAGATCCAT
GTCTCCTCTACCACCAAGGATGCCCTAGATGAGCTAGGATGCTTCCAGCTAGAGCTTCGG
GGGGATGTGGAAATGAAGGGAAAAGGAAAGATGCGAACATACTGGCTCTTAGGAGAGCGG
AAAGGACCTCCTGGACTCCTGTAA
|
| Enzyme 36 GenBank Gene ID |
AB005647  |
| Enzyme 36 GeneCard ID |
NPR2  |
| Enzyme 36 GenAtlas ID |
NPR2  |
| Enzyme 36 HGNC ID |
HGNC:7944  |
| Enzyme 36 Chromosome Location |
9 |
| Enzyme 36 Locus |
9p21-p12 |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
- Chang MS, Lowe DG, Lewis M, Hellmiss R, Chen E, Goeddel DV: Differential activation by atrial and brain natriuretic peptides of two different receptor guanylate cyclases. Nature. 1989 Sep 7;341(6237):68-72. [PubMed
]
- Rehemudula D, Nakayama T, Soma M, Takahashi Y, Uwabo J, Sato M, Izumi Y, Kanmatsuse K, Ozawa Y: Structure of the type B human natriuretic peptide receptor gene and association of a novel microsatellite polymorphism with essential hypertension. Circ Res. 1999 Mar 19;84(5):605-10. [PubMed
]
- Hirsch JR, Meyer M, Magert HJ, Forssmann WG, Mollerup S, Herter P, Weber G, Cermak R, Ankorina-Stark I, Schlatter E, Kruhoffer M: cGMP-dependent and -independent inhibition of a K+ conductance by natriuretic peptides: molecular and functional studies in human proximal tubule cells. J Am Soc Nephrol. 1999 Mar;10(3):472-80. [PubMed
]
|
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
6358 |
| Enzyme 37 Name |
Atrial natriuretic peptide receptor A precursor |
| Enzyme 37 Synonyms |
- ANP-A
- ANPRA
- GC-A
- Guanylate cyclase
- NPR-A
- Atrial natriuretic peptide A-type receptor
|
| Enzyme 37 Gene Name |
NPR1 |
| Enzyme 37 Protein Sequence |
>Atrial natriuretic peptide receptor A precursor
MPGPRRPAGSRLRLLLLLLLPPLLLLLRGSHAGNLTVAVVLPLANTSYPWSWARVGPAVE
LALAQVKARPDLLPGWTVRTVLGSSENALGVCSDTAAPLAAVDLKWEHNPAVFLGPGCVY
AAAPVGRFTAHWRVPLLTAGAPALGFGVKDEYALTTRAGPSYAKLGDFVAALHRRLGWER
QALMLYAYRPGDEEHCFFLVEGLFMRVRDRLNITVDHLEFAEDDLSHYTRLLRTMPRKGR
VIYICSSPDAFRTLMLLALEAGLCGEDYVFFHLDIFGQSLQGGQGPAPRRPWERGDGQDV
SARQAFQAAKIITYKDPDNPEYLEFLKQLKHLAYEQFNFTMEDGLVNTIPASFHDGLLLY
IQAVTETLAHGGTVTDGENITQRMWNRSFQGVTGYLKIDSSGDRETDFSLWDMDPENGAF
RVVLNYNGTSQELVAVSGRKLNWPLGYPPPDIPKCGFDNEDPACNQDHLSTLEVLALVGS
LSLLGILIVSFFIYRKMQLEKELASELWRVRWEDVEPSSLERHLRSAGSRLTLSGRGSNY
GSLLTTEGQFQVFAKTAYYKGNLVAVKRVNRKRIELTRKVLFELKHMRDVQNEHLTRFVG
ACTDPPNICILTEYCPRGSLQDILENESITLDWMFRYSLTNDIVKGMLFLHNGAICSHGN
LKSSNCVVDGRFVLKITDYGLESFRDLDPEQGHTVYAKKLWTAPELLRMASPPVRGSQAG
DVYSFGIILQEIALRSGVFHVEGLDLSPKEIIERVTRGEQPPFRPSLALQSHLEELGLLM
QRCWAEDPQERPPFQQIRLTLRKFNRENSSNILDNLLSRMEQYANNLEELVEERTQAYLE
EKRKAEALLYQILPHSVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTL
LNDLYTCFDAVIDNFDVYKVETIGDAYMVVSGLPVRNGRLHACEVARMALALLDAVRSFR
IRHRPQEQLRLRIGIHTGPVCAGVVGLKMPRYCLFGDTVNTASRMESNGEALKIHLSSET
KAVLEEFGGFELELRGDVEMKGKGKVRTYWLLGERGSSTRG
|
| Enzyme 37 Number of Residues |
1061 |
| Enzyme 37 Molecular Weight |
118921 |
| Enzyme 37 Theoretical pI |
6.61 |
| Enzyme 37 GO Classification |
| Function |
- ATP binding
- G-protein coupled receptor activity
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- lyase activity
- nucleotide binding
- peptide receptor activity, G-protein coupled
- phosphorus-oxygen lyase activity
- protein kinase activity
- protein-tyrosine kinase activity
- purine nucleotide binding
- receptor activity
- rhodopsin-like receptor activity
- signal transducer activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transmembrane receptor activity
|
| Process |
- biopolymer metabolism
- biopolymer modification
- cell communication
- cellular metabolism
- cellular process
- cyclic nucleotide biosynthesis
- intracellular signaling cascade
- macromolecule metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide biosynthesis
- nucleotide metabolism
- physiological process
- protein amino acid phosphorylation
- protein modification
- signal transduction
|
| Component |
|
|
| Enzyme 37 General Function |
Signal transduction mechanisms |
| Enzyme 37 Specific Function |
Receptor for atrial natriuretic peptide. Has guanylate cyclase activity on binding of ANF |
| Enzyme 37 Pathways |
|
| Enzyme 37 Reactions |
- GTP = 3',5'-cyclic GMP + diphosphate
|
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
28230  |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
P16066  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
ANPRA_HUMAN  |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
>3186 bp
ATGCCGGGGCCCCGGCGCCCCGCTGGCTCCCGCCTGCGCCTGCTCCTGCTCCTGCTGCTG
CCGCCGCTGCTGCTGCTGCTCCGGGGCAGCCACGCGGGCAACCTGACGGTAGCCGTGGTA
CTGCCGCTGGCCAATACCTCGTACCCCTGGTCGTGGGCGCGCGTGGGACCCGCCGTGGAG
CTGGCCCTGGCCCAGGTGAAGGCGCGCCCCGACTTGCTGCCGGGCTGGACGGTCCGCACG
GTGCTGGGCAGCAGCGAAAACGCGCTGGGCGTCTGCTCCGACACCGCAGCGCCCCTGGCC
GCGGTGGACCTCAAGTGGGAGCACAACCCCGCTGTGTTCCTGGGCCCCGGCTGCGTGTAC
GCCGCCGCCCCAGTGGGGCGCTTCACCGCGCACTGGCGGGTCCCGCTGCTGACCGCCGGC
GCCCCGGCGCTGGGCTTCGGTGTCAAGGACGAGTATGCGCTGACCACCCGCGCGGGGCCC
AGCTACGCCAAGCTGGGGGACTTCGTGGCGGCGCTGCACCGACGGCTGGGCTGGGAGCGC
CAAGCGCTCATGCTCTACGCCTACCGGCCGGGTGACGAAGAGCACTGCTTCTTCCTCGTG
GAGGGGCTGTTCATGCGGGTCCGCGACCGCCTCAATATTACGGTGGACCACCTGGAGTTC
GCCGAGGACGACCTCAGCCACTACACCAGGCTGCTGCGGACCATGCCGCGCAAAGGCCGA
GTTATCTACATCTGCAGCTCCCCTGATGCCTTCAGAACCCTCATGCTCCTGGCCCTGGAA
GCTGGCTTGTGTGGGGAGGACTACGTTTTCTTCCACCTGGATATCTTTGGGCAAAGCCTG
CAAGGTGGACAGGGCCCTGCTCCCCGCAGGCCCTGGGAGAGAGGGGATGGGCAGGATGTC
AGTGCCCGCCAGGCCTTTCAGGCTGCCAAAATCATTACATATAAAGACCCAGATAATCCC
GAGTACTTGGAATTCCTGAAGCAGTTAAAACACCTGGCCTATGAGCAGTTCAACTTCACC
ATGGAGGATGGCCTGGTGAACACCATCCCAGCATCCTTCCACGACGGGCTCCTGCTCTAT
ATCCAGGCAGTGACGGAGACTCTGGCACATGGGGGAACTGTTACTGATGGGGAGAACATC
ACTCAGCGGATGTGGAACCGAAGCTTTCAAGGTGTGACAGGATACCTGAAAATTGATAGC
AGTGGCGATCGGGAAACAGACTTCTCCCTCTGGGATATGGATCCCGAGAATGGTGCCTTC
AGGGTTGTACTGAACTACAATGGGACTTCCCAAGAGCTGGTGGCTGTGTCGGGGCGCAAA
CTGAACTGGCCCCTGGGGTACCCTCCTCCTGACATCCCCAAATGTGGCTTTGACAACGAA
GACCCAGCATGCAACCAAGATCACCTTTCCACCCTGGAGGTGCTGGCTTTGGTGGGCAGC
CTCTCCTTGCTCGGCATTCTGATTGTCTCCTTCTTCATATACAGGAAGATGCAGCTGGAG
AAGGAACTGGCCTCGGAGCTGTGGCGGGTGCGCTGGGAGGACGTTGAGCCCAGTAGCCTT
GAGAGGCACCTGCGGAGTGCAGGCAGCCGGCTGACCCTGAGCGGGAGAGGCTCCAATTAC
GGCTCCCTGCTAACCACAGAGGGCCAGTTCCAAGTCTTTGCCAAGACAGCATATTATAAG
GGCAACCTCGTGGCTGTGAAACGTGTGAACCGTAAACGCATTGAGCTGACACGAAAAGTC
CTGTTTGAACTGAAGCATATGCGGGATGTGCAGAATGAACACCTGACCAGGTTTGTGGGA
GCCTGCACCGACCCCCCCAATATCTGCATCCTCACAGAGTACTGTCCCCGTGGGAGCCTG
CAGGACATTCTGGAGAATGAGAGCATCACCCTGGACTGGATGTTCCGGTACTCACTCACC
AATGACATCGTCAAGGGCATGCTGTTTCTACACAATGGGGCTATCTGTTCCCATGGGAAC
CTCAAGTCATCCAACTGCGTGGTAGATGGGCGCTTTGTGCTCAAGATCACCGACTATGGG
CTGGAGAGCTTCAGGGACCTGGACCCAGAGCAAGGACACACCGTTTATGCCAAAAAGCTG
TGGACGGCCCCTGAGCTCCTGCGAATGGCTTCACCCCCTGTGCGGGGCTCCCAGGCTGGT
GACGTATACAGCTTTGGGATCATCCTTCAGGAGATTGCCCTGAGGAGTGGGGTCTTCCAC
GTGGAAGGTTTGGACCTGAGCCCCAAAGAGATCATCGAGCGGGTGACTCGGGGTGAGCAG
CCCCCCTTCCGGCCCTCCCTGGCCCTGCAGAGTCACCTGGAGGAGTTGGGGCTGCTCATG
CAGCGGTGCTGGGCTGAGGACCCACAGGAGAGGCCACCATTCCAGCAGATCCGCCTGACG
TTGCGCAAATTTAACAGGGAGAACAGCAGCAACATCCTGGACAACCTGCTGTCCCGCATG
GAGCAGTACGCGAACAATCTGGAGGAACTGGTGGAGGAGCGGACCCAGGCATACCTGGAG
GAGAAGCGCAAGGCTGAGGCCCTGCTCTACCAGATCCTGCCTCACTCAGTGGCTGAGCAG
CTGAAGCGTGGGGAGACGGTGCAGGCCGAAGCCTTTGACAGTGTTACCATCTACTTCAGT
GACATTGTGGGTTTCACAGCGCTGTCGGCGGAGAGCACACCCATGCAGGTGGTGACCCTG
CTCAATGACCTGTACACTTGCTTTGATGCTGTCATAGACAACTTTGATGTGTACAAGGTG
GAGACAATTGGCGATGCCTACATGGTGGTGTCAGGGCTCCCTGTGCGGAACGGGCGGCTA
CACGCCTGCGAGGTAGCCCGCATGGCCCTGGCACTGCTGGATGCTGTGCGCTCCTTCCGA
ATCCGCCACCGGCCCCAGGAGCAGCTGCGCTTGCGCATTGGCATCCACACAGGACCTGTG
TGTGCTGGAGTGGTGGGACTGAAGATGCCCCGTTACTGTCTCTTTGGGGATACAGTCAAC
ACAGCCTCAAGAATGGAGTCTAATGGGGAAGCCCTGAAGATCCACTTGTCTTCTGAGACC
AAGGCTGTCCTGGAGGAGTTTGGTGGTTTCGAGCTGGAGCTTCGAGGGGATGTAGAAATG
AAGGGCAAAGGCAAGGTTCGGACCTACTGGCTCCTTGGGGAGAGGGGGAGTAGCACCCGA
GGCTGA
|
| Enzyme 37 GenBank Gene ID |
X15357  |
| Enzyme 37 GeneCard ID |
NPR1  |
| Enzyme 37 GenAtlas ID |
NPR1  |
| Enzyme 37 HGNC ID |
HGNC:7943  |
| Enzyme 37 Chromosome Location |
1 |
| Enzyme 37 Locus |
1q21-q22 |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
- Lowe DG, Chang MS, Hellmiss R, Chen E, Singh S, Garbers DL, Goeddel DV: Human atrial natriuretic peptide receptor defines a new paradigm for second messenger signal transduction. EMBO J. 1989 May;8(5):1377-84. [PubMed
]
- Takahashi Y, Nakayama T, Soma M, Izumi Y, Kanmatsuse K: Organization of the human natriuretic peptide receptor A gene. Biochem Biophys Res Commun. 1998 May 29;246(3):736-9. [PubMed
]
- Pardhasaradhi K, Kutty RK, Gentleman S, Krishna G: Expression of mRNA for atrial natriuretic peptide receptor guanylate cyclase (ANPRA) in human retina. Cell Mol Neurobiol. 1994 Feb;14(1):1-7. [PubMed
]
|
| Enzyme 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
6359 |
| Enzyme 38 Name |
Heat-stable enterotoxin receptor precursor |
| Enzyme 38 Synonyms |
- GC-C
- Intestinal guanylate cyclase
- STA receptor
- hSTAR
|
| Enzyme 38 Gene Name |
GUCY2C |
| Enzyme 38 Protein Sequence |
>Heat-stable enterotoxin receptor precursor
MKTLLLDLALWSLLFQPGWLSFSSQVSQNCHNGSYEISVLMMGNSAFAEPLKNLEDAVNE
GLEIVRGRLQNAGLNVTVNATFMYSDGLIHNSGDCRSSTCEGLDLLRKISNAQRMGCVLI
GPSCTYSTFQMYLDTELSYPMISAGSFGLSCDYKETLTRLMSPARKLMYFLVNFWKTNDL
PFKTYSWSTSYVYKNGTETEDCFWYLNALEASVSYFSHELGFKVVLRQDKEFQDILMDHN
RKSNVIIMCGGPEFLYKLKGDRAVAEDIVIILVDLFNDQYLEDNVTAPDYMKNVLVLTLS
PGNSLLNSSFSRNLSPTKRDFALAYLNGILLFGHMLKIFLENGENITTPKFAHAFRNLTF
EGYDGPVTLDDWGDVDSTMVLLYTSVDTKKYKVLLTYDTHVNKTYPVDMSPTFTWKNSKL
PNDITGRGPQILMIAVFTLTGAVVLLLLVALLMLRKYRKDYELRQKKWSHIPPENIFPLE
TNETNHVSLKIDDDKRRDTIQRLRQCKYDKKRVILKDLKHNDGNFTEKQKIELNKLLQID
YYNLTKFYGTVKLDTMIFGVIEYCERGSLREVLNDTISYPDGTFMDWEFKISVLYDIAKG
MSYLHSSKTEVHGRLKSTNCVVDSRMVVKITDFGCNSILPPKKDLWTAPEHLRQANISQK
GDVYSYGIIAQEIILRKETFYTLSCRDRNEKIFRVENSNGMKPFRPDLFLETAEEKELEV
YLLVKNCWEEDPEKRPDFKKIETTLAKIFGLFHDQKNESYMDTLIRRLQLYSRNLEHLVE
ERTQLYKAERDRADRLNFMLLPRLVVKSLKEKGFVEPELYEEVTIYFSDIVGFTTICKYS
TPMEVVDMLNDIYKSFDHIVDHHDVYKVETIGDAYMVASGLPKRNGNRHAIDIAKMALEI
LSFMGTFELEHLPGLPIWIRIGVHSGPCAAGVVGIKMPRYCLFGDTVNTASRMESTGLPL
RIHVSGSTIAILKRTECQFLYEVRGETYLKGRGNETTYWLTGMKDQKFNLPTPPTVENQQ
RLQAEFSDMIANSLQKRQAAGIRSQKPRRVASYKKGTLEYLQLNTTDKESTYF
|
| Enzyme 38 Number of Residues |
1073 |
| Enzyme 38 Molecular Weight |
123370 |
| Enzyme 38 Theoretical pI |
7.18 |
| Enzyme 38 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- lyase activity
- nucleotide binding
- phosphorus-oxygen lyase activity
- protein kinase activity
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- cell communication
- cellular metabolism
- cellular process
- cyclic nucleotide biosynthesis
- intracellular signaling cascade
- macromolecule metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide biosynthesis
- nucleotide metabolism
- physiological process
- protein amino acid phosphorylation
- protein modification
- signal transduction
|
| Component |
| — |
|
| Enzyme 38 General Function |
Signal transduction mechanisms |
| Enzyme 38 Specific Function |
Receptor for the E.coli heat-stable enterotoxin (E.coli enterotoxin markedly stimulates the accumulation of cGMP in mammalian cells expressing GC-C). Also activated by the endogenous peptide guanylin |
| Enzyme 38 Pathways |
|
| Enzyme 38 Reactions |
- GTP = 3',5'-cyclic GMP + diphosphate
|
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
338502  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
P25092  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
GUC2C_HUMAN  |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>3222 bp
ATGAAGACGTTGCTGTTGGACTTGGCTTTGTGGTCACTGCTCTTCCAGCCCGGGTGGCTG
TCCTTTAGTTCCCAGGTGAGTCAGAACTGCCACAATGGCAGCTATGAAATCAGCGTCCTG
ATGATGGGCAACTCAGCCTTTGCAGAGCCCCTGAAAAACTTGGAAGATGCGGTGAATGAG
GGGCTGGAAATAGTGAGAGGACGTCTGCAAAATGCTGGCCTAAATGTGACTGTGAACGCT
ACTTTCATGTATTCGGATGGTCTGATTCATAACTCAGGCGACTGCCGGAGTAGCACCTGT
GAAGGCCTCGACCTACTCAGGAAAATTTCAAATGCACAACGGATGGGCTGTGTCCTCATA
GGGCCCTCATGTACATACTCCACCTTCCAGATGTACCTTGACACAGAATTGAGCTACCCC
ATGATCTCAGCTGGAAGTTTTGGATTGTCATGTGACTATAAAGAAACCTTAACCAGGCTG
ATGTCTCCAGCTAGAAAGTTGATGTACTTCTTGGTTAACTTTTGGAAAACCAACGATCTG
CCCTTCAAAACTTATTCCTGGAGCACTTCGTATGTTTACAAGAATGGTACAGAAACTGAG
GACTGTTTCTGGTACCTTAATGCTCTGGAGGCTAGCGTTTCCTATTTCTCCCACGAACTC
GGCTTTAAGGTGGTGTTAAGACAAGATAAGGAGTTTCAGGATATCTTAATGGACCACAAC
AGGAAAAGCAATGTGATTATTATGTGTGGTGGTCCAGAGTTCCTCTACAAGCTGAAGGGT
GACCGAGCAGTGGCTGAAGACATTGTCATTATTCTAGTGGATCTTTTCAATGACCAGTAC
TTGGAGGACAATGTCACAGCCCCTGACTATATGAAAAATGTCCTTGTTCTGACGCTGTCT
CCTGGGAATTCCCTTCTAAATAGCTCTTTCTCCAGGAATCTATCACCAACAAAACGAGAC
TTTGCTCTTGCCTATTTGAATGGAATCCTGCTCTTTGGACATATGCTGAAGATATTTCTT
GAAAATGGAGAAAATATTACCACCCCCAAATTTGCTCATGCTTTCAGGAATCTCACTTTT
GAAGGGTATGACGGTCCAGTGACCTTGGATGACTGGGGGGATGTTGACAGTACCATGGTG
CTTCTGTATACCTCTGTGGACACCAAGAAATACAAGGTTCTTTTGACCTATGATACCCAC
GTAAATAAGACCTATCCTGTGGATATGAGCCCCACATTCACTTGGAAGAACTCTAAACTT
CCTAATGATATTACAGGCCGGGGCCCTCAGATCCTGATGATTGCAGTCTTCACCCTCACT
GGAGCTGTGGTGCTGCTCCTGCTCGTCGCTCTCCTGATGCTCAGAAAATATAGAAAAGAT
TATGAACTTCGTCAGAAAAAATGGTCCCACATTCCTCCTGAAAATATCTTTCCTCTGGAG
ACCAATGAGACCAATCATGTTAGCCTCAAGATCGATGATGACAAAAGACGAGATACAATC
CAGAGACTACGACAGTGCAAATACGACAAAAAGCGAGTGATTCTCAAAGATCTCAAGCAC
AATGATGGTAATTTCACTGAAAAACAGAAGATAGAATTGAACAAGTTGCTTCAGATTGAC
TATTACAACCTGACCAAGTTCTACGGCACAGTGAAACTTGATACCATGATCTTCGGGGTG
ATAGAATACTGTGAGAGAGGATCCCTCCGGGAAGTTTTAAATGACACAATTTCCTACCCT
GATGGCACATTCATGGATTGGGAGTTTAAGATCTCTGTCTTGTATGACATTGCTAAGGGA
ATGTCATATCTGCACTCCAGTAAGACAGAAGTCCATGGTCGTCTGAAATCTACCAACTGC
GTAGTGGACAGTAGAATGGTGGTGAAGATCACTGATTTTGGCTGCAATTCCATTTTACCT
CCAAAAAAGGACCTGTGGACAGCTCCAGAGCACCTCCGCCAAGCCAACATCTCTCAGAAA
GGAGATGTGTACAGCTATGGGATCATCGCACAGGAGATCATTCTGCGGAAAGAAACCTTC
TACACTTTGAGCTGTCGGGACCGGAATGAGAAGATTTTCAGAGTGGAAAATTCCAATGGA
ATGAAACCCTTCCGCCCAGATTTATTCTTGGAAACAGCAGAGGAAAAAGAGCTAGAAGTG
TACCTACTTGTAAAAAACTGTTGGGAGGAAGATCCAGAAAAGAGACCAGATTTCAAAAAA
ATTGAGACTACACTTGCCAAGATATTTGGACTTTTTCATGACCAAAAAAATGAAAGCTAT
ATGGATACCTTGATCCGACGTCTACAGCTATATTCTCGAAACCTGGAACATCTGGTAGAG
GAAAGGACACAGCTGTACAAGGCAGAGAGGGACAGGGCTGACAGACTTAACTTTATGTTG
CTTCCAAGGCTAGTGGTAAAGTCTCTGAAGGAGAAAGGCTTTGTGGAGCCGGAACTATAT
GAGGAAGTTACAATCTACTTCAGTGACATTGTAGGTTTCACTACTATCTGCAAATACAGC
ACCCCCATGGAAGTGGTGGACATGCTTAATGACATCTATAAGAGTTTTGACCACATTGTT
GATCATCATGATGTCTACAAGGTGGAAACCATCGGTGATGCGTACATGGTGGCTAGTGGT
TTGCCTAAGAGAAATGGCAATCGGCATGCAATAGACATTGCCAAGATGGCCTTGGAAATC
CTCAGCTTCATGGGGACCTTTGAGCTGGAGCATCTTCCTGGCCTCCCAATATGGATTCGC
ATTGGAGTTCACTCTGGTCCCTGTGCTGCTGGAGTTGTGGGAATCAAGATGCCTCGTTAT
TGTCTATTTGGAGATACGGTCAACACAGCCTCTAGGATGGAATCCACTGGCCTCCCTTTG
AGAATTCACGTGAGTGGCTCCACCATAGCCATCCTGAAGAGAACTGAGTGCCAGTTCCTT
TATGAAGTGAGAGGAGAAACATACTTAAAGGGAAGAGGAAATGAGACTACCTACTGGCTG
ACTGGGATGAAGGACCAGAAATTCAACCTGCCAACCCCTCCTACTGTGGAGAATCAACAG
CGTTTGCAAGCAGAATTTTCAGACATGATTGCCAACTCTTTACAGAAAAGACAGGCAGCA
GGGATAAGAAGCCAAAAACCCAGACGGGTAGCCAGCTATAAAAAAGGCACTCTGGAATAC
TTGCAGCTGAATACCACAGACAAGGAGAGCACCTATTTTTAA
|
| Enzyme 38 GenBank Gene ID |
M73489  |
| Enzyme 38 GeneCard ID |
GUCY2C  |
| Enzyme 38 GenAtlas ID |
GUCY2C  |
| Enzyme 38 HGNC ID |
HGNC:4688  |
| Enzyme 38 Chromosome Location |
12 |
| Enzyme 38 Locus |
12p12 |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 General References |
- de Sauvage FJ, Camerato TR, Goeddel DV: Primary structure and functional expression of the human receptor for Escherichia coli heat-stable enterotoxin. J Biol Chem. 1991 Sep 25;266(27):17912-8. [PubMed
]
- Singh S, Singh G, Heim JM, Gerzer R: Isolation and expression of a guanylate cyclase-coupled heat stable enterotoxin receptor cDNA from a human colonic cell line. Biochem Biophys Res Commun. 1991 Sep 30;179(3):1455-63. [PubMed
]
- Mann EA, Jump ML, Glenella RA: Cell line-specific transcriptional activation of the promoter of the human guanylyl cyclase C/heat-stable enterotoxin/receptor gene. Biochim Biophys Acta. 1996 Feb 7;1305(1-2):7-10. [PubMed
]
- Mann EA, Cohen MB, Giannella RA: Comparison of receptors for Escherichia coli heat-stable enterotoxin: novel receptor present in IEC-6 cells. Am J Physiol. 1993 Jan;264(1 Pt 1):G172-8. [PubMed
]
- Scott RO, Thelin WR, Milgram SL: A novel PDZ protein regulates the activity of guanylyl cyclase C, the heat-stable enterotoxin receptor. J Biol Chem. 2002 Jun 21;277(25):22934-41. Epub 2002 Apr 11. [PubMed
]
|
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
6413 |
| Enzyme 39 Name |
Cyclic nucleotide-gated cation channel alpha 3 |
| Enzyme 39 Synonyms |
- CNG channel alpha 3
- CNG-3
- CNG3
- Cyclic nucleotide-gated channel alpha 3
- Cone photoreceptor cGMP-gated channel subunit alpha
|
| Enzyme 39 Gene Name |
CNGA3 |
| Enzyme 39 Protein Sequence |
>Cyclic nucleotide-gated cation channel alpha 3
MAKINTQYSHPSRTHLKVKTSDRDLNRAENGLSRAHSSSEETSSVLQPGIAMETRGLADS
GQGSFTGQGIARLSRLIFLLRRWAARHVHHQDQGPDSFPDRFRGAELKEVSSQESNAQAN
VGSQEPADRGRSAWPLAKCNTNTSNNTEEEKKTKKKDAIVVDPSSNLYYRWLTAIALPVF
YNWYLLICRACFDELQSEYLMLWLVLDYSADVLYVLDVLVRARTGFLEQGLMVSDTNRLW
QHYKTTTQFKLDVLSLVPTDLAYLKVGTNYPEVRFNRLLKFSRLFEFFDRTETRTNYPNM
FRIGNLVLYILIIIHWNACIYFAISKFIGFGTDSWVYPNISIPEHGRLSRKYIYSLYWST
LTLTTIGETPPPVKDEEYLFVVVDFLVGVLIFATIVGNVGSMISNMNASRAEFQAKIDSI
KQYMQFRKVTKDLETRVIRWFDYLWANKKTVDEKEVLKSLPDKLKAEIAINVHLDTLKKV
RIFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGKEMYIINEGKLAVVADDGVTQFVV
LSDGSYFGEISILNIKGSKSGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPEAKKALEE
KGRQILMKDNLIDEELARAGADPKDLEEKVEQLGSSLDTLQTRFARLLAEYNATQMKMKQ
RLSQLESQVKGGGDKPLADGEVPGDATKTEDKQQ
|
| Enzyme 39 Number of Residues |
694 |
| Enzyme 39 Molecular Weight |
78839 |
| Enzyme 39 Theoretical pI |
7.80 |
| Enzyme 39 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 39 General Function |
Signal transduction mechanisms |
| Enzyme 39 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 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 |
3153887  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
Q16281  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
CNGA3_HUMAN  |
| Enzyme 39 PDB ID |
Not Available |
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 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 39 GenBank Gene ID |
AF065314  |
| Enzyme 39 GeneCard ID |
CNGA3  |
| Enzyme 39 GenAtlas ID |
CNGA3  |
| Enzyme 39 HGNC ID |
HGNC:2150  |
| Enzyme 39 Chromosome Location |
2 |
| Enzyme 39 Locus |
2q11.2 |
| Enzyme 39 SNPs |
SNPJam Report  |
| Enzyme 39 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 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
6417 |
| Enzyme 40 Name |
Rap guanine nucleotide exchange factor 2 |
| Enzyme 40 Synonyms |
- Neural RAP guanine nucleotide exchange protein
- nRap GEP
- PDZ domain-containing guanine nucleotide exchange factor 1
- PDZ-GEF1
- RA-GEF
|
| Enzyme 40 Gene Name |
RAPGEF2 |
| Enzyme 40 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 40 Number of Residues |
1499 |
| Enzyme 40 Molecular Weight |
167419 |
| Enzyme 40 Theoretical pI |
6.64 |
| Enzyme 40 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 40 General Function |
Not Available |
| Enzyme 40 Specific Function |
Guanine nucleotide exchange factor (GEF) for Rap1A, Rap1B and Rap2B GTPases. Does not interact with cAMP or cGMP |
| 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 |
40788210  |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
Q9Y4G8  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
RPGF2_HUMAN  |
| Enzyme 40 PDB ID |
Not Available |
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 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 40 GenBank Gene ID |
AB002311  |
| Enzyme 40 GeneCard ID |
RAPGEF2  |
| Enzyme 40 GenAtlas ID |
RAPGEF2  |
| Enzyme 40 HGNC ID |
HGNC:16854  |
| Enzyme 40 Chromosome Location |
4 |
| Enzyme 40 Locus |
4q32.1 |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 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 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
7002 |
| Enzyme 41 Name |
Rho guanine nucleotide exchange factor 1 |
| Enzyme 41 Synonyms |
- p115-RhoGEF
- p115RhoGEF
- 115 kDa guanine nucleotide exchange factor
- Sub1.5
|
| Enzyme 41 Gene Name |
ARHGEF1 |
| Enzyme 41 Protein Sequence |
>Rho guanine nucleotide exchange factor 1
MEDFARGAASPGPSRPGLVPVSIIGAEDEDFENELETNSEEQNSQFQSLEQVKRRPAHLM
ALLQHVALQFEPGPLLCCLHADMLGSLGPKEAKKAFLDFYHSFLEKTAVLRVPVPPNVAF
ELDRTRADLISEDVQRRFVQEVVQSQQVAVGRQLEDFRSKRLMGMTPWEQELAQLEAWVG
RDRASYEARERHVAERLLMHLEEMQHTISTDEEKSAAVVNAIGLYMRHLGVRTKSGDKKS
GRNFFRKKVMGNRRSDEPAKTKKGLSSILDAARWNRGEPQVPDFRHLKAEVDAEKPGATD
RKGGVGMPSRDRNIGAPGQDTPGVSLHPLSLDSPDREPGADAPLELGDSSPQGPMSLESL
APPESTDEGAETESPEPGDEGEPGRSGLELEPEEPPGWRELVPPDTLHSLPKSQVKRQEV
ISELLVTEAAHVRMLRVLHDLFFQPMAECLFFPLEELQNIFPSLDELIEVHSLFLDRLMK
RRQESGYLIEEIGDVLLARFDGAEGSWFQKISSRFCSRQSFALEQLKAKQRKDPRFCAFV
QEAESRPRCRRLQLKDMIPTEMQRLTKYPLLLQSIGQNTEEPTEREKVELAAECCREILH
HVNQAVRDMEDLLRLKDYQRRLDLSHLRQSSDPMLSEFKNLDITKKKLVHEGPLTWRVTK
DKAVEVHVLLLDDLLLLLQRQDERLLLKSHSRTLTPTPDGKTMLRPVLRLTSAMTREVAT
DHKAFYVLFTWDQEAQIYELVAQTVSERKNWCALITETAGSLKVPAPASRPKPRPSPSST
REPLLSSSENGNGGRETSPADARTERILSDLLPFCRPGPEGQLAATALRKVLSLKQLLFP
AEEDNGAGPPRDGDGVPGGGPLSPARTQEIQENLLSLEETMKQLEELEEEFCRLRPLLSQ
LGGNSVPQPGCT
|
| Enzyme 41 Number of Residues |
912 |
| Enzyme 41 Molecular Weight |
102437 |
| Enzyme 41 Theoretical pI |
5.37 |
| Enzyme 41 GO Classification |
| Function |
- GTPase regulator activity
- enzyme regulator activity
- guanyl-nucleotide exchange factor activity
- small GTPase regulator activity
|
| Process |
- cell communication
- cellular process
- intracellular signaling cascade
- signal transduction
|
| Component |
| — |
|
| Enzyme 41 General Function |
Not Available |
| Enzyme 41 Specific Function |
Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase. Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12 |
| 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 |
1654344  |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
Q92888  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
ARHG1_HUMAN  |
| Enzyme 41 PDB ID |
Not Available |
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
>2739 bp
ATGGAAGACTTCGCCCGAGGGGCGGCCTCCCCAGGCCCCTCCCGGCCTGGCCTGGTTCCC
GTCAGCATCATCGGGGCTGAGGATGAGGATTTTGAGAACGAGCTGGAGACAAACTCAGAA
GAGCAAAACAGCCAGTTCCAGAGCCTGGAGCAGGTGAAGCGGCGCCCAGCCCACCTCATG
GCCCTCCTGCAGCACGTGGCCCTGCAGTTTGAGCCAGGACCCCTGCTTTGCTGTCTGCAT
GCCGACATGCTGGGCTCACTGGGCCCCAAGGAGGCCAAGAAGGCCTTCCTGGACTTCTAC
CACAGCTTCCTGGAGAAGACAGCGGTTCTCCGGGTGCCGGTCCCTCCCAACGTCGCCTTT
GAACTTGACCGCACTAGGGCTGACCTCATCTCCGAGGATGTCCAGCGGCGGTTCGTGCAG
GAGGTGGTGCAAAGCCAGCAGGTAGCCGTGGGCCGGCAGCTGGAGGACTTCCGTTCCAAG
CGGCTCATGGGCATGACGCCCTGGGAGCAGGAGCTGGCCCAGCTGGAGGCTTGGGTTGGG
CGGGACCGAGCCAGCTACGAGGCCCGGGAGCGGCACGTGGCGGAGCGGCTGCTCATGCAC
CTGGAGGAGATGCAACATACCATCTCTACCGACGAAGAAAAGAGTGCTGCCGTGGTCAAC
GCCATTGGGCTGTACATGCGCCACCTTGGGGTGCGGACCAAGAGTGGAGACAAGAAGTCG
GGGAGGAACTTCTTCCGGAAAAAGGTGATGGGGAACCGGCGGTCGGACGACCCTCCCAAG
ACCAAGAAGGGGCTGAGCAGCATCCTGGATGCCGCCCGCTGGAACCGGGGAGAGCCCCAG
GTTCCAGATTTTCGACACCTCAAAGCAGAGGTTGATGCCGAGAAGCCAGGTGCTACAGAC
CGGAAGGGAGGCGTGGGGATGCCCTCTCGGGACCGGAATATCGGGGCTCCTGGGCAGGAC
ACCCCTGGAGTCTCTCTGCACCCTCTGTCCCTGGACAGCCCAGACCGGGAACCAGGTGCT
GACGCCCCCCTGGAGCTGGGGGACTCATCCCCGCAGGGCCCAATGAGCCTGGAGTCCTTG
GCGCCCCCAGAGAGTACCGACGAGGGGGCCGAAACCGAGAGCCCCGAGCCTGGAGATGAG
GGGGAGCCGGGGCGGTCGGGACTGGAGCTTGAACCAGAAGAGCCTCCCGGCTGGCGGGAA
CTCGTCCCCCCAGACACCCTGCACAGCCTGCCCAAGAGCCAGGTGAAGCGGCAGGAGGTC
ATCAGCGAGCTGCTGGTGACAGAGGCGGCCCACGTGCGCATGCTGCGGGTGCTGCACGAC
CTCTTCTTCCAGCCCATGGCAGAATGCCTGTTCTTCCCCTTGGAGGAGCTGCAGAACATC
TTCCCCAGCCTGGACGAGCTCATCGAGGTGCATTCCCTGTTCCTCGATCGCCTGATGAAG
CGGAGGCAGGAGAGTGGCTACCTCATCGAGGAGATCGGAGACGTGCTGCTGGCCCGGTTT
GATGGTGCTGAGGGCTCCTGGTTCCAGAAAATCTCCTCCCGCTTCTGCAGCCGCCAGTCA
TTTGCCTTAGAGCAGCTCAAAGCCAAGCAACGCAAGGACCCTCGGTTCTGTGCCTTCGTG
CAGGAAGCTGAGAGCCGCCCGCGGTGCCGCCGCCTGCAGCTGAAGGACATGATCCCCACG
GAGATGCAGCGGCTGACCAAGTACCCCCTGCTCCTGCAGAGCATCGGGCAGAACACAGAA
GAGCCCACAGAACGGGAGAAAGTGGAGCTGGCAGCCGAGTGCTGCCGGGAAATTCTACAC
CACGTCAACCAAGCCGTGCGTGACATGGAGGACCTGCTGAGGCTCAAGGACTATCAGCGG
CGCCTGGACTTGTCCCACCTTCGGCAGAGCAGCGACCCTATGCTGAGCGAGTTCAAGAAC
CTGGACATCACCAAGAAGAAATTGGTCCACGAGGGCCCACTGACGTGGCGGGTGACTAAG
GACAAGGCAGTGGAGGTGCATGTGCTGCTGCTGGACGACCTGCTGCTGCTGCTCCAGCGC
CAGGACGAGCGGCTGCTGCTCAAGTCCCATAGCCGGACACTGACGCCCACGCCCGATGGC
AAGACCATGCTGCGGCCCGTGCTGCGGCTCACCTCCGCCATGACCCGCGAGGTGGCCACC
GATCACAAAGCCTTCTACGTCCTTTTTACCTGGGACCAGGAGGCCCAGATATACGAGCTG
GTGGCACAGACTGTGTCGGAGCGGAAAAACTGGTGTGCTCTCATCACTGAGACTGCCGGA
TCCCTGAAAGTCCCTGCCCCTGCCTCTCGCCCTAAGCCCCGGCCCAGGCCGAGCAGCACC
CGAGAACCCCTCCTCAGCAGCTCTGAGAACGGGAATGGTGGCCGAGAGACGTCTCCAGCT
GATGCCCGGACCGAGAGAATCCTCAGTGACCTCCTGCCCTTCTGCAGACCAGGCCCCGAG
GGCCAGCTCGCTGCCACGGCCCTTCGGAAAGTGCTGTCCCTGAAGCAGCTTCTGTTTCCG
GCGGAGGAAGACAATGGGGCGGGGCCTCCTCGAGATGGGGATGGGGTCCCAGGGGGCGGG
CCCCTGAGCCCAGCACGGACCCAGGAAATCCAGGAGAACCTGCTCAGCTTGGAGGAGACC
ATGAAGCAGCTGGAGGAGTTGGAGGAGGAATTTTGCCGCCTGAGACCCCTCCTGTCTCAG
CTTGGGGGGAACTCTGTCCCCCAGCCTGGCTGCACTTGA
|
| Enzyme 41 GenBank Gene ID |
U64105  |
| Enzyme 41 GeneCard ID |
ARHGEF1  |
| Enzyme 41 GenAtlas ID |
ARHGEF1  |
| Enzyme 41 HGNC ID |
HGNC:681  |
| Enzyme 41 Chromosome Location |
19 |
| Enzyme 41 Locus |
19q13.13 |
| Enzyme 41 SNPs |
SNPJam Report  |
| Enzyme 41 General References |
- Hart MJ, Sharma S, elMasry N, Qiu RG, McCabe P, Polakis P, Bollag G: Identification of a novel guanine nucleotide exchange factor for the Rho GTPase. J Biol Chem. 1996 Oct 11;271(41):25452-8. [PubMed
]
- Aasheim HC, Pedeutour F, Smeland EB: Characterization, expression and chromosomal localization of a human gene homologous to the mouse Lsc oncogene, with strongest expression in hematopoetic tissues. Oncogene. 1997 Apr 10;14(14):1747-52. [PubMed
]
- Kozasa T, Jiang X, Hart MJ, Sternweis PM, Singer WD, Gilman AG, Bollag G, Sternweis PC: p115 RhoGEF, a GTPase activating protein for Galpha12 and Galpha13. Science. 1998 Jun 26;280(5372):2109-11. [PubMed
]
- Hart MJ, Jiang X, Kozasa T, Roscoe W, Singer WD, Gilman AG, Sternweis PC, Bollag G: Direct stimulation of the guanine nucleotide exchange activity of p115 RhoGEF by Galpha13. Science. 1998 Jun 26;280(5372):2112-4. [PubMed
]
- Bhattacharyya R, Wedegaertner PB: Galpha 13 requires palmitoylation for plasma membrane localization, Rho-dependent signaling, and promotion of p115-RhoGEF membrane binding. J Biol Chem. 2000 May 19;275(20):14992-9. [PubMed
]
- Holinstat M, Mehta D, Kozasa T, Minshall RD, Malik AB: Protein kinase Calpha-induced p115RhoGEF phosphorylation signals endothelial cytoskeletal rearrangement. J Biol Chem. 2003 Aug 1;278(31):28793-8. Epub 2003 May 16. [PubMed
]
- Chen Z, Wells CD, Sternweis PC, Sprang SR: Structure of the rgRGS domain of p115RhoGEF. Nat Struct Biol. 2001 Sep;8(9):805-9. [PubMed
]
|
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
7120 |
| Enzyme 42 Name |
Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-2 subunit precursor |
| Enzyme 42 Synonyms |
- G gamma-I
|
| Enzyme 42 Gene Name |
GNG2 |
| Enzyme 42 Protein Sequence |
>Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-2 subunit precursor
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL
|
| Enzyme 42 Number of Residues |
71 |
| Enzyme 42 Molecular Weight |
7850 |
| Enzyme 42 Theoretical pI |
8.22 |
| Enzyme 42 GO Classification |
| Function |
- signal transducer activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- signal transduction
|
| Component |
- cell
- extrinsic to membrane
- extrinsic to plasma membrane
- heterotrimeric G-protein complex
- membrane
|
|
| Enzyme 42 General Function |
Not Available |
| Enzyme 42 Specific Function |
Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction |
| 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 |
20147633  |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
P59768  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
GBG2_HUMAN  |
| Enzyme 42 PDB ID |
1GP2  |
| Enzyme 42 PDB File |
Show |
| Enzyme 42 3D Structure |
|
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
>216 bp
ATGGCCAGCAACAACACCGCCAGCATAGCACAAGCCAGGAAGCTGGTAGAGCAGCTTAAG
ATGGAAGCCAATATCGACAGGATAAAGGTGTCCAAGGCAGCTGCAGATTTGATGGCCTAC
TGTGAAGCACATGCCAAGGAAGACCCCCTCCTGACCCCTGTTCCGGCTTCAGAAAACCCG
TTTAGGGAGAAGAAGTTTTTCTGTGCCATCCTTTAA
|
| Enzyme 42 GenBank Gene ID |
AF493870  |
| Enzyme 42 GeneCard ID |
GNG2  |
| Enzyme 42 GenAtlas ID |
GNG2  |
| Enzyme 42 HGNC ID |
HGNC:4404  |
| Enzyme 42 Chromosome Location |
14 |
| Enzyme 42 Locus |
14q21 |
| Enzyme 42 SNPs |
SNPJam Report  |
| Enzyme 42 General References |
- Modarressi MH, Taylor KE, Wolfe J: Cloning, characterization, and mapping of the gene encoding the human G protein gamma 2 subunit. Biochem Biophys Res Commun. 2000 Jun 7;272(2):610-5. [PubMed
]
|
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
7131 |
| Enzyme 43 Name |
Ras-related C3 botulinum toxin substrate 1 precursor |
| Enzyme 43 Synonyms |
- p21-Rac1
- Ras- like protein TC25
- Cell migration-inducing gene 5 protein
|
| Enzyme 43 Gene Name |
RAC1 |
| Enzyme 43 Protein Sequence |
>Ras-related C3 botulinum toxin substrate 1 precursor
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLR
DDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPP
PVKKRKRKCLLL
|
| Enzyme 43 Number of Residues |
192 |
| Enzyme 43 Molecular Weight |
21450 |
| Enzyme 43 Theoretical pI |
8.65 |
| Enzyme 43 GO Classification |
| Function |
- GTP binding
- binding
- guanyl nucleotide binding
- nucleotide binding
- purine nucleotide binding
|
| Process |
- cell communication
- cellular process
- intracellular signaling cascade
- signal transduction
- small GTPase mediated signal transduction
|
| Component |
| — |
|
| Enzyme 43 General Function |
Not Available |
| Enzyme 43 Specific Function |
Isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP- dependent manner, suggesting that the insertion does not completely abolish effector interaction |
| 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 |
190824  |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
P63000  |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
RAC1_HUMAN  |
| Enzyme 43 PDB ID |
1I4L  |
| Enzyme 43 PDB File |
Show |
| Enzyme 43 3D Structure |
|
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
>579 bp
ATGCAGGCCATCAAGTGTGTGGTGGTGGGAGACGGAGCTGTAGGTAAAACTTGCCTACTG
ATCAGTTACACAACCAATGCATTTCCTGGAGAATATATCCCTACTGTCTTTGACAATTAT
TCTGCCAATGTTATGGTAGATGGAAAACCGGTGAATCTGGGCTTATGGGATACAGCTGGA
CAAGAAGATTATGACAGATTACGCCCCCTATCCTATCCGCAAACAGATGTGTTCTTAATT
TGCTTTTCCCTTGTGAGTCCTGCATCATTTGAAAATGTCCGTGCAAAGTGGTATCCTGAG
GTGCGGCACCACTGTCCCAACACTCCCATCATCCTAGTGGGAACTAAACTTGATCTTAGG
GATGATAAAGACACGATCGAGAAACTGAAGGAGAAGAAGCTGACTCCCATCACCTATCCG
CAGGGTCTAGCCATGGCTAAGGAGATTGGTGCTGTAAAATACCTGGAGTGCTCGGCGCTC
ACACAGCGAGGCCTCAAGACAGTGTTTGACGAAGCGATCCGAGCAGTCCTCTGCCCGCCT
CCCGTGAAGAAGAGGAAGAGAAAATGCCTGCTGTTGTAA
|
| Enzyme 43 GenBank Gene ID |
M29870  |
| Enzyme 43 GeneCard ID |
RAC1  |
| Enzyme 43 GenAtlas ID |
RAC1  |
| Enzyme 43 HGNC ID |
HGNC:9801  |
| Enzyme 43 Chromosome Location |
7 |
| Enzyme 43 Locus |
7p22 |
| Enzyme 43 SNPs |
SNPJam Report  |
| Enzyme 43 General References |
- Didsbury J, Weber RF, Bokoch GM, Evans T, Snyderman R: rac, a novel ras-related family of proteins that are botulinum toxin substrates. J Biol Chem. 1989 Oct 5;264(28):16378-82. [PubMed
]
- Drivas GT, Shih A, Coutavas E, Rush MG, D'Eustachio P: Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line. Mol Cell Biol. 1990 Apr;10(4):1793-8. [PubMed
]
- Matos P, Skaug J, Marques B, Beck S, Verissimo F, Gespach C, Boavida MG, Scherer SW, Jordan P: Small GTPase Rac1: structure, localization, and expression of the human gene. Biochem Biophys Res Commun. 2000 Nov 2;277(3):741-51. [PubMed
]
- Jordan P, Brazao R, Boavida MG, Gespach C, Chastre E: Cloning of a novel human Rac1b splice variant with increased expression in colorectal tumors. Oncogene. 1999 Nov 18;18(48):6835-9. [PubMed
]
- 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
]
- Kinsella BT, Erdman RA, Maltese WA: Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA. J Biol Chem. 1991 May 25;266(15):9786-94. [PubMed
]
- Jullien-Flores V, Dorseuil O, Romero F, Letourneur F, Saragosti S, Berger R, Tavitian A, Gacon G, Camonis JH: Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity. J Biol Chem. 1995 Sep 22;270(38):22473-7. [PubMed
]
- Nishihara H, Kobayashi S, Hashimoto Y, Ohba F, Mochizuki N, Kurata T, Nagashima K, Matsuda M: Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins. Biochim Biophys Acta. 1999 Nov 11;1452(2):179-87. [PubMed
]
- Johansson A, Driessens M, Aspenstrom P: The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1. J Cell Sci. 2000 Sep;113 ( Pt 18):3267-75. [PubMed
]
- Vikis HG, Li W, He Z, Guan KL: The semaphorin receptor plexin-B1 specifically interacts with active Rac in a ligand-dependent manner. Proc Natl Acad Sci U S A. 2000 Nov 7;97(23):12457-62. [PubMed
]
- Noda Y, Takeya R, Ohno S, Naito S, Ito T, Sumimoto H: Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C. Genes Cells. 2001 Feb;6(2):107-19. [PubMed
]
- Welch HC, Coadwell WJ, Ellson CD, Ferguson GJ, Andrews SR, Erdjument-Bromage H, Tempst P, Hawkins PT, Stephens LR: P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac. Cell. 2002 Mar 22;108(6):809-21. [PubMed
]
- Brugnera E, Haney L, Grimsley C, Lu M, Walk SF, Tosello-Trampont AC, Macara IG, Madhani H, Fink GR, Ravichandran KS: Unconventional Rac-GEF activity is mediated through the Dock180-ELMO complex. Nat Cell Biol. 2002 Aug;4(8):574-82. [PubMed
]
- Hirshberg M, Stockley RW, Dodson G, Webb MR: The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue. Nat Struct Biol. 1997 Feb;4(2):147-52. [PubMed
]
- Lapouge K, Smith SJ, Walker PA, Gamblin SJ, Smerdon SJ, Rittinger K: Structure of the TPR domain of p67phox in complex with Rac.GTP. Mol Cell. 2000 Oct;6(4):899-907. [PubMed
]
- Worthylake DK, Rossman KL, Sondek J: Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1. Nature. 2000 Dec 7;408(6813):682-8. [PubMed
]
- Stebbins CE, Galan JE: Modulation of host signaling by a bacterial mimic: structure of the Salmonella effector SptP bound to Rac1. Mol Cell. 2000 Dec;6(6):1449-60. [PubMed
]
- Wurtele M, Wolf E, Pederson KJ, Buchwald G, Ahmadian MR, Barbieri JT, Wittinghofer A: How the Pseudomonas aeruginosa ExoS toxin downregulates Rac. Nat Struct Biol. 2001 Jan;8(1):23-6. [PubMed
]
- Grizot S, Faure J, Fieschi F, Vignais PV, Dagher MC, Pebay-Peyroula E: Crystal structure of the Rac1-RhoGDI complex involved in nadph oxidase activation. Biochemistry. 2001 Aug 28;40(34):10007-13. [PubMed
]
- Tarricone C, Xiao B, Justin N, Walker PA, Rittinger K, Gamblin SJ, Smerdon SJ: The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. Nature. 2001 May 10;411(6834):215-9. [PubMed
]
|
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
7134 |
| Enzyme 44 Name |
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short |
| Enzyme 44 Synonyms |
- Adenylate cyclase-stimulating G alpha protein
|
| Enzyme 44 Gene Name |
GNAS |
| Enzyme 44 Protein Sequence |
>Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQM
RILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA
NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD
KIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFND
VTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEK
VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY
PHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL
|
| Enzyme 44 Number of Residues |
394 |
| Enzyme 44 Molecular Weight |
45665 |
| Enzyme 44 Theoretical pI |
5.56 |
| Enzyme 44 GO Classification |
| Function |
- GTP binding
- binding
- guanyl nucleotide binding
- nucleotide binding
- purine nucleotide binding
- signal transducer activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 44 General Function |
Not Available |
| Enzyme 44 Specific Function |
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase:it activates the cyclase in response to beta-adrenergic stimuli |
| 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 |
31915  |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
P63092  |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
GNAS2_HUMAN  |
| Enzyme 44 PDB ID |
1U0H  |
| Enzyme 44 PDB File |
Show |
| Enzyme 44 3D Structure |
|
| Enzyme 44 Cellular Location |
Not Available |
| Enzyme 44 Gene Sequence |
>1185 bp
ATGGGCTGCCTCGGGAACAGTAAGACCGAGGACCAGCGCAACGAGGAGAAGGCGCAGCGT
GAGGCCAACAAAAAGATCGAGAAGCAGCTGCAGAAGGACAAGCAGGTCTACCGGGCCACG
CACCGCCTGCTGCTGCTGGGTGCTGGAGAATCTGGTAAAAGCACCATTGTGAAGCAGATG
AGGATCCTGCATGTTAATGGGTTTAATGGAGAGGGCGGCGAAGAGGACCCGCAGGCTGCA
AGGAGCAACAGCGATGGTGAGAAGGCAACCAAAGTGCAGGACATCAAAAACAACCTGAAA
GAGGCGATTGAAACCATTGTGGCCGCCATGAGCAACCTGGTGCCCCCCGTGGAGCTGGCC
AACCCCGAGAACCAGTTCAGAGTGGACTACATCCTGAGTGTGATGAACGTGCCTGACTTT
GACTTCCCTCCCGAATTCTATGAGCATGCCAAGGCTCTGTGGGAGGATGAAGGAGTGCGT
GCCTGCTACGAACGCTCCAACGAGTACCAGCTGATTGACTGTGCCCAGTACTTCCTGGAC
AAGATCGACGTGATCAAGCAGGCTGACTATGTGCCGAGCGATCAGGACCTGCTTCGCTGC
CGTGTCCTGACTTCTGGAATCTTTGAGACCAAGTTCCAGGTGGACAAAGTCAACTTCCAC
ATGTTTGACGTGGGTGGCCAGCGCGATGAACGCCGCAAGTGGATCCAGTGCTTCAACGAT
GTGACTGCCATCATCTTCGTGGTGGCCAGCAGCAGCTACAACATGGTCATCCGGGAGGAC
AACCAGACCAACCGCCTGCAGGAGGCTCTGAACCTCTTCAAGAGCATCTGGAACAACAGA
TGGCTGCGCACCATCTCTGTGATCCTGTTCCTCAACAAGCAAGATCTGCTCGCTGAGAAA
GTCCTTGCTGGGAAATCGAAGATTGAGGACTACTTTCCAGAATTTGCTCGCTACACTACT
CCTGAGGATGCTACTCCCGAGCCCGGAGAGGACCCACGCGTGACCCGGGCCAAGTACTTC
ATTCGAGATGAGTTTCTGAGGATCAGCACTGCCAGTGGAGATGGGCGTCACTACTGCTAC
CCTCATTTCACCTGCGCTGTGGACACTGAGAACATCCGCCGTGTGTTCAACGACTGCCGT
GACATCATTCAGCGCATGCACCTTCGTCAGTACGAGCTGCTCTAA
|
| Enzyme 44 GenBank Gene ID |
X04408  |
| Enzyme 44 GeneCard ID |
GNAS  |
| Enzyme 44 GenAtlas ID |
GNAS  |
| Enzyme 44 HGNC ID |
HGNC:4392  |
| Enzyme 44 Chromosome Location |
20 |
| Enzyme 44 Locus |
20q13.3 |
| Enzyme 44 SNPs |
SNPJam Report  |
| Enzyme 44 General References |
- Mattera R, Codina J, Crozat A, Kidd V, Woo SL, Birnbaumer L: Identification by molecular cloning of two forms of the alpha-subunit of the human liver stimulatory (GS) regulatory component of adenylyl cyclase. FEBS Lett. 1986 Sep 29;206(1):36-42. [PubMed
]
- Harris BA: Complete cDNA sequence of a human stimulatory GTP-binding protein alpha subunit. Nucleic Acids Res. 1988 Apr 25;16(8):3585. [PubMed
]
- Kozasa T, Itoh H, Tsukamoto T, Kaziro Y: Isolation and characterization of the human Gs alpha gene. Proc Natl Acad Sci U S A. 1988 Apr;85(7):2081-5. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Bray P, Carter A, Simons C, Guo V, Puckett C, Kamholz J, Spiegel A, Nirenberg M: Human cDNA clones for four species of G alpha s signal transduction protein. Proc Natl Acad Sci U S A. 1986 Dec;83(23):8893-7. [PubMed
]
- Miric A, Vechio JD, Levine MA: Heterogeneous mutations in the gene encoding the alpha-subunit of the stimulatory G protein of adenylyl cyclase in Albright hereditary osteodystrophy. J Clin Endocrinol Metab. 1993 Jun;76(6):1560-8. [PubMed
]
- Schwindinger WF, Francomano CA, Levine MA: Identification of a mutation in the gene encoding the alpha subunit of the stimulatory G protein of adenylyl cyclase in McCune-Albright syndrome. Proc Natl Acad Sci U S A. 1992 Jun 1;89(11):5152-6. [PubMed
]
- Weinstein LS, Shenker A, Gejman PV, Merino MJ, Friedman E, Spiegel AM: Activating mutations of the stimulatory G protein in the McCune-Albright syndrome. N Engl J Med. 1991 Dec 12;325(24):1688-95. [PubMed
]
- Landis CA, Masters SB, Spada A, Pace AM, Bourne HR, Vallar L: GTPase inhibiting mutations activate the alpha chain of Gs and stimulate adenylyl cyclase in human pituitary tumours. Nature. 1989 Aug 31;340(6236):692-6. [PubMed
]
- Schwindinger WF, Miric A, Zimmerman D, Levine MA: A novel Gs alpha mutant in a patient with Albright hereditary osteodystrophy uncouples cell surface receptors from adenylyl cyclase. J Biol Chem. 1994 Oct 14;269(41):25387-91. [PubMed
]
- Warner DR, Weng G, Yu S, Matalon R, Weinstein LS: A novel mutation in the switch 3 region of Gsalpha in a patient with Albright hereditary osteodystrophy impairs GDP binding and receptor activation. J Biol Chem. 1998 Sep 11;273(37):23976-83. [PubMed
]
|
| Enzyme 44 Metabolite References |
Not Available |
|
Enzyme 45
[top]
|
| Enzyme 45 ID |
7136 |
| Enzyme 45 Name |
Proto-oncogene DBL |
| Enzyme 45 Synonyms |
- Proto-oncogene MCF-2[Contains: MCF2-transforming protein
- DBL-transforming protein]
|
| Enzyme 45 Gene Name |
MCF2 |
| Enzyme 45 Protein Sequence |
>Proto-oncogene DBL
MAEANPRRGKMRFRRNAASFPGNLHLVLVLRPTSFLQRTFTDIGFWFSQEDFMLKLPVVM
LSSVSDLLTYIDDKQLTPELGGTLQYCHSEWIIFRNAIENFALTVKEMAQMLQSFGTELA
ETELPDDIPSIEEILAIRAERYHLLKNDITAVTKEGKILLTNLEVPDTEGAVSSRLECHR
QISGDWQTINKLLTQVHDMETAFDGFWEKHQLKMEQYLQLWKFEQDFQQLVTEVEFLLNQ
QAELADVTGTIAQVKQKIKKLENLDENSQELLSKAQFVILHGHKLAANHHYALDLICQRC
NELRYLSDILVNEIKAKRIQLSRTFKMHKLLQQARQCCDEGECLLANQEIDKFQSKEDAQ
KALQDIENFLEMALPFINYEPETLQYEFDVILSPELKVQMKTIQLKLENIRSIFENQQAG
FRNLADKHVRPIQFVVPTPENLVTSGTPFFSSKQGKKTWRQNQSNLKIEVVPDCQEKRSS
GPSSSLDNGNSLDVLKNHVLNELIQTERVYVRELYTVLLGYRAEMDNPEMFDLMPPLLRN
KKDILFGNMAEIYEFHNDIFLSSLENCAHAPERVGPCFLERKDDFQMYAKYCQNKPRSET
IWRKYSECAFFQECQRKLKHRLRLDSYLLKPVQRITKYQLLLKELLKYSKDCEGSALLKK
ALDAMLDLLKSVNDSMHQIAINGYIGNLNELGKMIMQGGFSVWIGHKKGATKMKDLARFK
PMQRHLFLYEKAIVFCKRRVESGEGSDRYPSYSFKHCWKMDEVGITEYVKGDNRKFEIWY
GEKEEVYIVQASNVDVKMTWLKEIRNILLKQQELLTVKKRKQQDQLTERDKFQISLQQND
EKQQGAFISTEETELEHTSTVVEVCEAIASVQAEANTVWTEASQSAEISEEPAEWSSNYF
YPTYDENEEENRPLMRPVSEMALLY
|
| Enzyme 45 Number of Residues |
925 |
| Enzyme 45 Molecular Weight |
107675 |
| Enzyme 45 Theoretical pI |
5.87 |
| Enzyme 45 GO Classification |
| Function |
- GTPase regulator activity
- enzyme regulator activity
- guanyl-nucleotide exchange factor activity
- small GTPase regulator activity
|
| Process |
- cell communication
- cellular process
- intracellular signaling cascade
- signal transduction
|
| Component |
| — |
|
| Enzyme 45 General Function |
Not Available |
| Enzyme 45 Specific Function |
Guanine nucleotide exchange factor (GEF) that modulates the Rho family of GTPases. Promotes the conversion of some member of the Rho family GTPase from the GDP-bound to the GTP-bound form. Isoform 1 exhibits no activity toward RHOA, RAC1 or CDC42. Isoform 2 exhibits decreased GEF activity toward CDC42. Isoform 3 exhibits a weak but significant activity toward RAC1 and CDC42. Isoform 4 exhibits significant activity toward RHOA and CDC42. The truncated DBL oncogene is active toward RHOA, RAC1 and CDC42 |
| Enzyme 45 Pathways |
Not Available |
| Enzyme 45 Reactions |
Not Available |
| Enzyme 45 Pfam Domain Function |
|
| Enzyme 45 Signals |
|
| Enzyme 45 Transmembrane Regions |
|
| Enzyme 45 Essentiality |
Not Available |
| Enzyme 45 GenBank ID Protein |
30482  |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
P10911  |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
MCF2_HUMAN  |
| Enzyme 45 PDB ID |
Not Available |
| Enzyme 45 Cellular Location |
Not Available |
| Enzyme 45 Gene Sequence |
>2778 bp
ATGGCAGAAGCAAATCCCCGGAGAGGCAAGATGAGGTTCAGAAGGAATGCGGCTTCCTTC
CCTGGGAACTTGCACTTGGTTTTGGTTTTACGTCCTACCAGCTTTCTTCAACGAACGTTC
ACAGACATTGGATTTTGGTTTAGTCAGGAGGATTTTATGCCTAAATTACCAGTTGTTATG
CTGAGCTCAGTTAGTGATTTGCTGACATACATTGATGACAAGCAATTAACCCCTGAGTTA
GGCGGCACCTTGCAGTACTGCCACAGTGAATGGATCATCTTCAGAAATGCTATAGAAAAT
TTTGCCCTCACAGTGAAAGAAATGGCTCAGATGTTACAGTCCTTTGGAACTGAACTGGCT
GAGACAGAACTACCAGATGATATTCCCTCAATAGAAGAAATTCTGGCAATTCGTGCTGAA
AGGTATCATCTGTTGAAGAATGATATTACAGCTGTAACCAAAGAAGGAAAAATTCTGCTA
ACAAATCTGGAAGTGCCTGACACTGAAGGAGCTGTCAGTTCAAGACTAGAATGTCATCGG
CAAATAAGTGGTGACTGGCAAACTATTAATAAGTTGCTGACTCAAGTACATGATATGGAA
ACAGCTTTTGATGGATTTTGGGAAAAACATCAATTAAAAATGGAGCAGTATCTGCAACTA
TGGAAGTTTGAGCAGGATTTTCAACAGCTTGTGACTGAAGTTGAATTTCTATTAAACCAA
CAAGCAGAACTGGCTGATGTAACAGGGACTATAGCTCAAGTAAAACAAAAAATAAAAAAA
TTGGAAAACTTAGATGAAAATTCTCAGGAGCTATTATCAAAGGCCCAGTTTGTGATATTA
CATGGACACAAGCTTGCAGCAAATCACCATTATGCACTTGATTTAATCTGCCAGAGGTGC
AATGAGCTACGTTACCTTTCTGATATTTTGGTTAATGAGATAAAAGCAAAACGGATACAA
CTCAGCAGGACCTTCAAAATGCATAAACTCCTACAGCAGGCTCGTCAATGCTGTGATGAA
GGGGAATGTCTTCTAGCTAATCAGGAAATAGATAAGTTTCAGTCTAAAGAAGATGCTCAG
AAAGCTCTCCAAGACATTGAAAATTTTCTTGAAATGGCTCTACCCTTTATAAATTATGAA
CCTGAAACACTGCAGTATGAATTTGATGTAATATTATCTCCTGAGCTTAAGGTTCAAATG
AAGACTATACAACTCAAGCTTGAAAACATTCGAAGTATATTTGAGAACCAGCAGGCTGGT
TTCAGGAACCTGGCAGATAAGCATGTGAGGCCAATCCAATTTGTGGTACCCACACCTGAA
AATTTGGTCACATCTGGGACACCATTTTTTTCATCTAAACAAGGGAAGAAGACTTGGAGA
CAAAATCAGAGCAACTTAAAAATTGAAGTGGTGCCTGATTGTCAGGAGAAGAGAAGTTCT
GGTCCATCCTCCAGTTTGGACAATGGCAATAGCTTGGATGTTTTAAAGAACCACGTACTA
AATGAACTGATACAGACTGAGAGAGTTTATGTTCGAGAACTGTATACTGTTTTGTTGGGT
TATAGAGCGGAGATGGATAATCCAGAGATGTTTGATCTTATGCCACCTCTCCTGAGAAAT
AAAAAGGACATTCTCTTTGGAAACATGGCAGAAATATATGAATTCCATAACGACATTTTC
TTGAGCAGCCTGGAAAATTGTGCTCATGCTCCAGAAAGAGTGGGACCTTGTTTCCTGGAA
AGGAAGGATGATTTTCAGATGTATGCAAAATATTGTCAGAATAAGCCCAGATCAGAAACA
ATTTGGAGGAAGTATTCAGAATGCGCATTTTTCCAGGAATGTCAAAGAAAGTTAAAACAC
AGACTTAGACTGGATTCCTATTTACTCAAACCAGTGCAACGAATCACTAAATATCAGTTA
TTGTTGAAGGAGCTATTAAAATATAGCAAAGACTGTGAAGGTTCTGCTCTGTTGAAGAAG
GCACTCGATGCAATGCTGGATTTACTGAAGTCAGTTAATGATTCTATGCATCAGATTGCA
ATAAATGGCTATATTGGAAACTTAAATGAACTGGGCAAGATGATAATGCAAGGTGGATTC
AGCGTTTGGATAGGGCACAAGAAAGGTGCTACAAAAATGAAGGATTTGGCTAGATTCAAA
CCAATGCAGCGACACCTTTTCTTGTATGAAAAAGCCATTGTTTTTTGCAAAAGGCGTGTT
GAAAGTGGAGAAGGCTCTGACAGATACCCGTCATACAGTTTTAAACACTGTTGGAAAATG
GATGAAGTTGGAATCACTGAATATGTAAAAGGTGATAACCGCAAGTTTGAAATCTGGTAT
GGTGAAAAGGAAGAAGTTTATATTGTCCAGGCTTCTAATGTAGATGTGAAGATGACGTGG
CTAAAAGAAATAAGAAATATTTTGTTGAAGCAGCAGGAACTTTTGACAGTTAAAAAAAGA
AAGCAACAGGATCAATTAACAGAACGGGATAAGTTTCAGATTTCTCTTCAGCAGAATGAT
GAAAAGCAACAGGGAGCTTTTATAAGTACTGAGGAAACTGAATTGGAACACACCAGCACT
GTGGTGGAGGTCTGTGAGGCAATTGCGTCAGTTCAGGCAGAAGCAAATACAGTTTGGACT
GAGGCATCACAATCTGCAGAAATCTCTGAAGAACCTGCGGAATGGTCAAGCAACTATTTC
TACCCTACTTATGATGAAAATGAAGAAGAAAATAGGCCCCTCATGAGACCTGTGTCGGAG
ATGGCTCTCCTATATTGA
|
| Enzyme 45 GenBank Gene ID |
X12556  |
| Enzyme 45 GeneCard ID |
MCF2  |
| Enzyme 45 GenAtlas ID |
MCF2  |
| Enzyme 45 HGNC ID |
HGNC:6940  |
| Enzyme 45 Chromosome Location |
X |
| Enzyme 45 Locus |
Xq27 |
| Enzyme 45 SNPs |
SNPJam Report  |
| Enzyme 45 General References |
- Ron D, Tronick SR, Aaronson SA, Eva A: Molecular cloning and characterization of the human dbl proto-oncogene: evidence that its overexpression is sufficient to transform NIH/3T3 cells. EMBO J. 1988 Aug;7(8):2465-73. [PubMed
]
- Komai K, Okayama R, Kitagawa M, Yagi H, Chihara K, Shiozawa S: Alternative splicing variants of the human DBL (MCF-2) proto-oncogene. Biochem Biophys Res Commun. 2002 Dec 6;299(3):455-8. [PubMed
]
- Eva A, Vecchio G, Rao CD, Tronick SR, Aaronson SA: The predicted DBL oncogene product defines a distinct class of transforming proteins. Proc Natl Acad Sci U S A. 1988 Apr;85(7):2061-5. [PubMed
]
- Noguchi T, Galland F, Batoz M, Mattei MG, Birnbaum D: Activation of a mcf.2 oncogene by deletion of amino-terminal coding sequences. Oncogene. 1988 Dec;3(6):709-15. [PubMed
]
- Ron D, Zannini M, Lewis M, Wickner RB, Hunt LT, Graziani G, Tronick SR, Aaronson SA, Eva A: A region of proto-dbl essential for its transforming activity shows sequence similarity to a yeast cell cycle gene, CDC24, and the human breakpoint cluster gene, bcr. New Biol. 1991 Apr;3(4):372-9. [PubMed
]
- Hart MJ, Eva A, Zangrilli D, Aaronson SA, Evans T, Cerione RA, Zheng Y: Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product. J Biol Chem. 1994 Jan 7;269(1):62-5. [PubMed
]
|
| Enzyme 45 Metabolite References |
Not Available |
|
Enzyme 46
[top]
|
| Enzyme 46 ID |
7137 |
| Enzyme 46 Name |
Cell division control protein 42 homolog precursor |
| Enzyme 46 Synonyms |
- G25K GTP-binding protein
|
| Enzyme 46 Gene Name |
CDC42 |
| Enzyme 46 Protein Sequence |
>Cell division control protein 42 homolog precursor
MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG
QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR
DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQRGLKNVFDEAILAALEPP
ETQPKRKCCIF
|
| Enzyme 46 Number of Residues |
191 |
| Enzyme 46 Molecular Weight |
21311 |
| Enzyme 46 Theoretical pI |
5.83 |
| Enzyme 46 GO Classification |
| Function |
- GTP binding
- binding
- guanyl nucleotide binding
- nucleotide binding
- purine nucleotide binding
|
| Process |
- cell communication
- cellular process
- intracellular signaling cascade
- signal transduction
- small GTPase mediated signal transduction
|
| Component |
| — |
|
| Enzyme 46 General Function |
Not Available |
| Enzyme 46 Specific Function |
Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Causes the formation of thin, actin-rich surface projections called filopodia |
| Enzyme 46 Pathways |
Not Available |
| Enzyme 46 Reactions |
Not Available |
| Enzyme 46 Pfam Domain Function |
|
| Enzyme 46 Signals |
|
| Enzyme 46 Transmembrane Regions |
|
| Enzyme 46 Essentiality |
Not Available |
| Enzyme 46 GenBank ID Protein |
182857  |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
P60953  |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
CDC42_HUMAN  |
| Enzyme 46 PDB ID |
1GRN  |
| Enzyme 46 PDB File |
Show |
| Enzyme 46 3D Structure |
|
| Enzyme 46 Cellular Location |
Not Available |
| Enzyme 46 Gene Sequence |
>576 bp
ATGCAGACAATTAAGTGTGTTGTTGTGGGCGATGGTGCTGTTGGTAAAACATGTCTCCTG
ATATCCTACACAACAAACAAATTTCCATCGGAATATGTACCGACTGTTTTTGACAACTAT
GCAGTCACAGTTATGATTGGTGGAGAACCATATACTCTTGGACTTTTTGATACTGCAGGG
CAAGAGGATTATGACAGATTACGACCGCTGAGTTATCCACAAACAGATGTATTTCTAGTC
TGTTTTTCAGTGGTCTCTCCATCTTCATTTGAAAACGTGAAAGAAAAGTGGGTGCCTGAG
ATAACTCACCACTGTCCAAAGACTCCTTTCTTGCTTGTTGGGACTCAAATTGATCTCAGA
GATGACCCCTCTACTATTGAGAAACTTGCCAAGAACAAACAGAAGCCTATCACTCCAGAG
ACTGCTGAAAAGCTGGCCCGTGACCTGAAGGCTGTCAAGTATGTGGAGTGTTCTGCACTT
ACACAGAGAGGTCTGAAGAATGTGTTTGATGAGGCTATCCTAGCTGCCCTCGAGCCTCCG
GAAACTCAACCCAAAAGGAAGTGCTGTATATTCTAA
|
| Enzyme 46 GenBank Gene ID |
M35543  |
| Enzyme 46 GeneCard ID |
CDC42  |
| Enzyme 46 GenAtlas ID |
CDC42  |
| Enzyme 46 HGNC ID |
HGNC:1736  |
| Enzyme 46 Chromosome Location |
1 |
| Enzyme 46 Locus |
1p36.1 |
| Enzyme 46 SNPs |
SNPJam Report  |
| Enzyme 46 General References |
- Munemitsu S, Innis MA, Clark R, McCormick F, Ullrich A, Polakis P: Molecular cloning and expression of a G25K cDNA, the human homolog of the yeast cell cycle gene CDC42. Mol Cell Biol. 1990 Nov;10(11):5977-82. [PubMed
]
- Shinjo K, Koland JG, Hart MJ, Narasimhan V, Johnson DI, Evans T, Cerione RA: Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42. Proc Natl Acad Sci U S A. 1990 Dec;87(24):9853-7. [PubMed
]
- Polakis PG, Snyderman R, Evans T: Characterization of G25K, a GTP-binding protein containing a novel putative nucleotide binding domain. Biochem Biophys Res Commun. 1989 Apr 14;160(1):25-32. [PubMed
]
- Yamane HK, Farnsworth CC, Xie HY, Evans T, Howald WN, Gelb MH, Glomset JA, Clarke S, Fung BK: Membrane-binding domain of the small G protein G25K contains an S-(all-trans-geranylgeranyl)cysteine methyl ester at its carboxyl terminus. Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):286-90. [PubMed
]
- Joberty G, Perlungher RR, Macara IG: The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins. Mol Cell Biol. 1999 Oct;19(10):6585-97. [PubMed
]
- Johansson A, Driessens M, Aspenstrom P: The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1. J Cell Sci. 2000 Sep;113 ( Pt 18):3267-75. [PubMed
]
- Noda Y, Takeya R, Ohno S, Naito S, Ito T, Sumimoto H: Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C. Genes Cells. 2001 Feb;6(2):107-19. [PubMed
]
- Meller N, Irani-Tehrani M, Kiosses WB, Del Pozo MA, Schwartz MA: Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins. Nat Cell Biol. 2002 Sep;4(9):639-47. [PubMed
]
- Feltham JL, Dotsch V, Raza S, Manor D, Cerione RA, Sutcliffe MJ, Wagner G, Oswald RE: Definition of the switch surface in the solution structure of Cdc42Hs. Biochemistry. 1997 Jul 22;36(29):8755-66. [PubMed
]
- Guo W, Sutcliffe MJ, Cerione RA, Oswald RE: Identification of the binding surface on Cdc42Hs for p21-activated kinase. Biochemistry. 1998 Oct 6;37(40):14030-7. [PubMed
]
- Rittinger K, Walker PA, Eccleston JF, Nurmahomed K, Owen D, Laue E, Gamblin SJ, Smerdon SJ: Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP. Nature. 1997 Aug 14;388(6643):693-7. [PubMed
]
- Rudolph MG, Wittinghofer A, Vetter IR: Nucleotide binding to the G12V-mutant of Cdc42 investigated by X-ray diffraction and fluorescence spectroscopy: two different nucleotide states in one crystal. Protein Sci. 1999 Apr;8(4):778-87. [PubMed
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