|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5313 |
| Enzyme 1 Name |
Ectonucleoside triphosphate diphosphohydrolase 1 |
| Enzyme 1 Synonyms |
- NTPDase 1
- Ecto-ATP diphosphohydrolase
- ATPDase
- Lymphoid cell activation antigen
- Ecto-apyrase
- CD39 antigen
|
| Enzyme 1 Gene Name |
ENTPD1 |
| Enzyme 1 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
|
| Enzyme 1 Number of Residues |
510 |
| Enzyme 1 Molecular Weight |
57965 |
| Enzyme 1 Theoretical pI |
6.29 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 1 General Function |
Not Available |
| Enzyme 1 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 1 Pathways |
|
| Enzyme 1 Reactions |
- ATP + 2 H2O = AMP + 2 phosphate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
765256  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P49961  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
ENTP1_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 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 1 GenBank Gene ID |
S73813  |
| Enzyme 1 GeneCard ID |
ENTPD1  |
| Enzyme 1 GenAtlas ID |
ENTPD1  |
| Enzyme 1 HGNC ID |
HGNC:3363  |
| Enzyme 1 Chromosome Location |
10 |
| Enzyme 1 Locus |
10q24 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 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 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5314 |
| Enzyme 2 Name |
Soluble calcium-activated nucleotidase 1 |
| Enzyme 2 Synonyms |
- SCAN-1
- Apyrase homolog
- Putative NF-kappa-B-activating protein 107
- Putative MAPK-activating protein PM09
|
| Enzyme 2 Gene Name |
CANT1 |
| Enzyme 2 Protein Sequence |
>Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
|
| Enzyme 2 Number of Residues |
401 |
| Enzyme 2 Molecular Weight |
44840 |
| Enzyme 2 Theoretical pI |
5.98 |
| Enzyme 2 GO Classification |
Not Available |
| Enzyme 2 General Function |
Not Available |
| Enzyme 2 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 2 Pathways |
|
| Enzyme 2 Reactions |
- A nucleoside diphosphate + H2O = a nucleotide + phosphate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
22218108  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q8WVQ1  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
CANT1_HUMAN  |
| Enzyme 2 PDB ID |
1S1D  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1116 bp
ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA
|
| Enzyme 2 GenBank Gene ID |
AF328554  |
| Enzyme 2 GeneCard ID |
CANT1  |
| Enzyme 2 GenAtlas ID |
CANT1  |
| Enzyme 2 HGNC ID |
HGNC:19721  |
| Enzyme 2 Chromosome Location |
17 |
| Enzyme 2 Locus |
17q25.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 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 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5338 |
| Enzyme 3 Name |
Nucleoside diphosphate kinase, mitochondrial precursor |
| Enzyme 3 Synonyms |
- NDP kinase, mitochondrial
- NDK
- nm23-H4
- Nucleoside diphosphate kinase D
- NDPKD
|
| Enzyme 3 Gene Name |
NME4 |
| Enzyme 3 Protein Sequence |
>Nucleoside diphosphate kinase, mitochondrial precursor
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
|
| Enzyme 3 Number of Residues |
187 |
| Enzyme 3 Molecular Weight |
20659 |
| Enzyme 3 Theoretical pI |
10.75 |
| Enzyme 3 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- ion binding
- magnesium ion binding
- metal ion binding
- nucleoside diphosphate kinase activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthesis
- GTP biosynthesis
- UTP biosynthesis
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside triphosphate biosynthesis
- nucleoside triphosphate metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside triphosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside triphosphate biosynthesis
- pyrimidine ribonucleoside triphosphate biosynthesis
- ribonucleoside triphosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 3 General Function |
Nucleotide transport and metabolism |
| Enzyme 3 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
Not Available |
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
1945762  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
O00746  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
NDKM_HUMAN  |
| Enzyme 3 PDB ID |
1EHW  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCA
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
|
| Enzyme 3 GenBank Gene ID |
Y07604  |
| Enzyme 3 GeneCard ID |
NME4  |
| Enzyme 3 GenAtlas ID |
NME4  |
| Enzyme 3 HGNC ID |
HGNC:7852  |
| Enzyme 3 Chromosome Location |
16 |
| Enzyme 3 Locus |
16p13.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Milon L, Rousseau-Merck MF, Munier A, Erent M, Lascu I, Capeau J, Lacombe ML: nm23-H4, a new member of the family of human nm23/nucleoside diphosphate kinase genes localised on chromosome 16p13. Hum Genet. 1997 Apr;99(4):550-7. [PubMed
]
- Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed
]
- Milon L, Meyer P, Chiadmi M, Munier A, Johansson M, Karlsson A, Lascu I, Capeau J, Janin J, Lacombe ML: The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate kinase. J Biol Chem. 2000 May 12;275(19):14264-72. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5341 |
| Enzyme 4 Name |
Nucleoside diphosphate kinase A |
| Enzyme 4 Synonyms |
- NDK A
- NDP kinase A
- Tumor metastatic process-associated protein
- Metastasis inhibition factor nm23
- nm23-H1
- Granzyme A-activated DNase
- GAAD
|
| Enzyme 4 Gene Name |
NME1 |
| Enzyme 4 Protein Sequence |
>Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
|
| Enzyme 4 Number of Residues |
152 |
| Enzyme 4 Molecular Weight |
17149 |
| Enzyme 4 Theoretical pI |
6.11 |
| Enzyme 4 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- ion binding
- magnesium ion binding
- metal ion binding
- nucleoside diphosphate kinase activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthesis
- GTP biosynthesis
- UTP biosynthesis
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside triphosphate biosynthesis
- nucleoside triphosphate metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside triphosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside triphosphate biosynthesis
- pyrimidine ribonucleoside triphosphate biosynthesis
- ribonucleoside triphosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 4 General Function |
Nucleotide transport and metabolism |
| Enzyme 4 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
35068  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P15531  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
NDKA_HUMAN  |
| Enzyme 4 PDB ID |
1JXV  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>543 bp
TGCTGCGAACCACGTGGGTCCCGGGCGCGTTTCGGGTGCTGGCGGCTGCAGCCGGAGTTC
AAACCTAAGCAGCTGGAAGGAACCATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAA
CCAGATGGGGTCCAGCGGGGTCTTGTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGA
TTCCGCCTTGTTGGTCTGAAATTCATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTAC
GTTGACCTGAAGGACCGTCCATTCTTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCG
GTAGTTGCCATGGTCTGGGAGGGGCTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGG
GAGACCAACCCTGCAGACTCCAAGCCTGGGACCATCCGTGGAGACTTCTGCATACAAGTT
GGCAGGAACATTATACATGGCAGTGATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTG
TGGTTTCACCCTGAGGAACTGGTAGATTACACGAGCTGTGCTCAGAACTGGATCTATGAA
TGA
|
| Enzyme 4 GenBank Gene ID |
X17620  |
| Enzyme 4 GeneCard ID |
NME1  |
| Enzyme 4 GenAtlas ID |
NME1  |
| Enzyme 4 HGNC ID |
HGNC:7849  |
| Enzyme 4 Chromosome Location |
17 |
| Enzyme 4 Locus |
17q21.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Rosengard AM, Krutzsch HC, Shearn A, Biggs JR, Barker E, Margulies IM, King CR, Liotta LA, Steeg PS: Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development. Nature. 1989 Nov 9;342(6246):177-80. [PubMed
]
- Dooley S, Seib T, Engel M, Theisinger B, Janz H, Piontek K, Zang KD, Welter C: Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1. Hum Genet. 1994 Jan;93(1):63-6. [PubMed
]
- Wang L, Patel U, Ghosh L, Chen HC, Banerjee S: Mutation in the nm23 gene is associated with metastasis in colorectal cancer. Cancer Res. 1993 Feb 15;53(4):717-20. [PubMed
]
- Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed
]
- Hailat N, Keim DR, Melhem RF, Zhu XX, Eckerskorn C, Brodeur GM, Reynolds CP, Seeger RC, Lottspeich F, Strahler JR, et al.: High levels of p19/nm23 protein in neuroblastoma are associated with advanced stage disease and with N-myc gene amplification. J Clin Invest. 1991 Jul;88(1):341-5. [PubMed
]
- Manda R, Kohno T, Matsuno Y, Takenoshita S, Kuwano H, Yokota J: Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display. Genomics. 1999 Oct 1;61(1):5-14. [PubMed
]
- Min K, Song HK, Chang C, Kim SY, Lee KJ, Suh SW: Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor. Proteins. 2002 Feb 15;46(3):340-2. [PubMed
]
- Chen Y, Gallois-Montbrun S, Schneider B, Veron M, Morera S, Deville-Bonne D, Janin J: Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases. J Mol Biol. 2003 Sep 26;332(4):915-26. [PubMed
]
- Fan Z, Beresford PJ, Oh DY, Zhang D, Lieberman J: Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell. 2003 Mar 7;112(5):659-72. [PubMed
]
- Chang CL, Zhu XX, Thoraval DH, Ungar D, Rawwas J, Hora N, Strahler JR, Hanash SM, Radany E: Nm23-H1 mutation in neuroblastoma. Nature. 1994 Aug 4;370(6488):335-6. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5342 |
| Enzyme 5 Name |
Nucleoside diphosphate kinase 7 |
| Enzyme 5 Synonyms |
- NDK 7
- NDP kinase 7
- nm23-H7
|
| Enzyme 5 Gene Name |
NME7 |
| Enzyme 5 Protein Sequence |
>Nucleoside diphosphate kinase 7
MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN
|
| Enzyme 5 Number of Residues |
376 |
| Enzyme 5 Molecular Weight |
42492 |
| Enzyme 5 Theoretical pI |
6.44 |
| Enzyme 5 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside diphosphate kinase activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthesis
- GTP biosynthesis
- UTP biosynthesis
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside triphosphate biosynthesis
- nucleoside triphosphate metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside triphosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside triphosphate biosynthesis
- pyrimidine ribonucleoside triphosphate biosynthesis
- ribonucleoside triphosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 5 General Function |
Nucleotide transport and metabolism |
| Enzyme 5 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
4960169  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9Y5B8  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
NDK7_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1131 bp
ATGAATCATAGTGAAAGATTCGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
|
| Enzyme 5 GenBank Gene ID |
AF153191  |
| Enzyme 5 GeneCard ID |
NME7  |
| Enzyme 5 GenAtlas ID |
NME7  |
| Enzyme 5 HGNC ID |
HGNC:20461  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
1q24 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
Not Available |
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5344 |
| Enzyme 6 Name |
Nucleoside diphosphate kinase B |
| Enzyme 6 Synonyms |
- NDK B
- NDP kinase B
- nm23-H2
- C-myc purine-binding transcription factor PUF
|
| Enzyme 6 Gene Name |
NME2 |
| Enzyme 6 Protein Sequence |
>Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
|
| Enzyme 6 Number of Residues |
152 |
| Enzyme 6 Molecular Weight |
17298 |
| Enzyme 6 Theoretical pI |
8.69 |
| Enzyme 6 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- ion binding
- magnesium ion binding
- metal ion binding
- nucleoside diphosphate kinase activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthesis
- GTP biosynthesis
- UTP biosynthesis
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside triphosphate biosynthesis
- nucleoside triphosphate metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside triphosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside triphosphate biosynthesis
- pyrimidine ribonucleoside triphosphate biosynthesis
- ribonucleoside triphosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 6 General Function |
Nucleotide transport and metabolism |
| Enzyme 6 Specific Function |
Acts as a transcriptional activator of the c-Myc gene; binds DNA nonspecifically (Ref.3) |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
4467843  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P22392  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
NDKB_HUMAN  |
| Enzyme 6 PDB ID |
1NSK  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
|
| Enzyme 6 GenBank Gene ID |
X58965  |
| Enzyme 6 GeneCard ID |
NME2  |
| Enzyme 6 GenAtlas ID |
NME2  |
| Enzyme 6 HGNC ID |
HGNC:7850  |
| Enzyme 6 Chromosome Location |
17 |
| Enzyme 6 Locus |
17q21.3 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed
]
- Stahl JA, Leone A, Rosengard AM, Porter L, King CR, Steeg PS: Identification of a second human nm23 gene, nm23-H2. Cancer Res. 1991 Jan 1;51(1):445-9. [PubMed
]
- Postel EH, Berberich SJ, Flint SJ, Ferrone CA: Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. Science. 1993 Jul 23;261(5120):478-80. [PubMed
]
- Webb PA, Perisic O, Mendola CE, Backer JM, Williams RL: The crystal structure of a human nucleoside diphosphate kinase, NM23-H2. J Mol Biol. 1995 Aug 25;251(4):574-87. [PubMed
]
- Morera S, Lacombe ML, Xu Y, LeBras G, Janin J: X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution. Structure. 1995 Dec 15;3(12):1307-14. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5345 |
| Enzyme 7 Name |
Nucleoside diphosphate kinase 3 |
| Enzyme 7 Synonyms |
- NDK 3
- NDP kinase 3
- Nucleoside diphosphate kinase C
- NDPKC
- nm23-H3
- DR-nm23
|
| Enzyme 7 Gene Name |
NME3 |
| Enzyme 7 Protein Sequence |
>Nucleoside diphosphate kinase 3
MICLVLTIFANLFPAACTGAHERTFLAVKPDGVQRRLVGEIVRRFERKGFKLVALKLVQA
SEELLREHYAELRERPFYGRLVKYMASGPVVAMVWQGLDVVRTSRALIGATNPADAPPGT
IRGDFCIEVGKNLIHGSDSVESARREIALWFRADELLCWEDSAGHWLYE
|
| Enzyme 7 Number of Residues |
169 |
| Enzyme 7 Molecular Weight |
19015 |
| Enzyme 7 Theoretical pI |
7.97 |
| Enzyme 7 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- ion binding
- magnesium ion binding
- metal ion binding
- nucleoside diphosphate kinase activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthesis
- GTP biosynthesis
- UTP biosynthesis
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside triphosphate biosynthesis
- nucleoside triphosphate metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside triphosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside triphosphate biosynthesis
- pyrimidine ribonucleoside triphosphate biosynthesis
- ribonucleoside triphosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 7 General Function |
Nucleotide transport and metabolism |
| Enzyme 7 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
Not Available |
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
1051256  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q13232  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
NDK3_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>507 bp
ATGATCTGCCTGGTGCTGACCATCTTCGCTAACCTCTTCCCCGCGGCCTGCACCGGCGCA
CACGAACGCACCTTCCTGGCCGTGAAGCCGGACGGCGTGCAGCGGCGGCTGGTGGGCGAG
ATTGTGCGGCGCTTCGAGAGGAAGGGCTTCAAGTTGGTGGCGCTGAAGCTGGTGCAGTCC
TCCGAGGAGCTGCTGCGTGAGCACTACGCCGAGCTGCGTGAACGCCCGTTCTACGGCCGC
CTTGTCAAGTATATGGCCTCCGGGCCGGTGGTGGCCATGGTTTGGCAGGGGCTGGACGTG
GTGCGCACCTCGCGGGCGCTCATCGGAGCCACGAACCCGGCCGACGCCCCGCCCGGCACC
ATCCGCGGGGATTTCTGCATCGAGGTTGGCAACCTGATTCACGGCAGCGACTCGGTGGAG
AGTGCCCGCCGCGAGATCGCTCTCTGGTTCCGCGCAGACGAGCTCCTCTGCTGGGAGGAC
AGCGCTGGGCACTGGCTGTATGAGTAG
|
| Enzyme 7 GenBank Gene ID |
U29656  |
| Enzyme 7 GeneCard ID |
NME3  |
| Enzyme 7 GenAtlas ID |
NME3  |
| Enzyme 7 HGNC ID |
HGNC:7851  |
| Enzyme 7 Chromosome Location |
16 |
| Enzyme 7 Locus |
16q13 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Venturelli D, Martinez R, Melotti P, Casella I, Peschle C, Cucco C, Spampinato G, Darzynkiewicz Z, Calabretta B: Overexpression of DR-nm23, a protein encoded by a member of the nm23 gene family, inhibits granulocyte differentiation and induces apoptosis in 32Dc13 myeloid cells. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7435-9. [PubMed
]
- Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5346 |
| Enzyme 8 Name |
Nucleoside diphosphate kinase 6 |
| Enzyme 8 Synonyms |
- NDK 6
- NDP kinase 6
- nm23-H6
- Inhibitor of p53-induced apoptosis-alpha
- IPIA-alpha
|
| Enzyme 8 Gene Name |
NME6 |
| Enzyme 8 Protein Sequence |
>Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
|
| Enzyme 8 Number of Residues |
186 |
| Enzyme 8 Molecular Weight |
21142 |
| Enzyme 8 Theoretical pI |
8.49 |
| Enzyme 8 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- ion binding
- magnesium ion binding
- metal ion binding
- nucleoside diphosphate kinase activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthesis
- GTP biosynthesis
- UTP biosynthesis
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside triphosphate biosynthesis
- nucleoside triphosphate metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside triphosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside triphosphate biosynthesis
- pyrimidine ribonucleoside triphosphate biosynthesis
- ribonucleoside triphosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 8 General Function |
Nucleotide transport and metabolism |
| Enzyme 8 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Inhibitor of p53-induced apoptosis |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
Not Available |
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
3228530  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
O75414  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
NDK6_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
|
| Enzyme 8 GenBank Gene ID |
AF051941  |
| Enzyme 8 GeneCard ID |
NME6  |
| Enzyme 8 GenAtlas ID |
NME6  |
| Enzyme 8 HGNC ID |
HGNC:20567  |
| Enzyme 8 Chromosome Location |
3 |
| Enzyme 8 Locus |
3p21 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Mehus JG, Deloukas P, Lambeth DO: NME6: a new member of the nm23/nucleoside diphosphate kinase gene family located on human chromosome 3p21.3. Hum Genet. 1999 Jun;104(6):454-9. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5668 |
| Enzyme 9 Name |
Inosine triphosphate pyrophosphatase |
| Enzyme 9 Synonyms |
- ITPase
- Inosine triphosphatase
- Putative oncogene protein hlc14-06-p
|
| Enzyme 9 Gene Name |
ITPA |
| Enzyme 9 Protein Sequence |
>Inosine triphosphate pyrophosphatase
MAASLVGKKIVFVTGNAKKLEEVVQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEA
VRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLLAGFEDKSAYALCTFAL
STGDPSQPVRLFRGRTSGRIVAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFR
ALLELQEYFGSLAA
|
| Enzyme 9 Number of Residues |
194 |
| Enzyme 9 Molecular Weight |
21446 |
| Enzyme 9 Theoretical pI |
5.34 |
| Enzyme 9 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 9 General Function |
Nucleotide transport and metabolism |
| Enzyme 9 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 9 Pathways |
|
| Enzyme 9 Reactions |
- A nucleoside triphosphate + H2O = a nucleotide + diphosphate
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
13398328  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q9BY32  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
ITPA_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>585 bp
ATGGCGGCCTCATTGGTGGGGAAGAAGATCGTGTTTGTAACGGGGAACGCCAAGAAGCTG
GAGGAGGTCGTTCAGATTCTAGGAGATAAGTTTCCACGCACTTTGGTGGCACAGAAAATT
GACCTGCCGGAGTACCAGGGGGAGCCGGATGAGATTTCCATACAGAAATGTCAGGAGGCA
GTTCGCCAGGTACAGGGGCCCGTGCTGGTTGAGGACACTTGTCTGTGCTTCAATGCCCTT
GGAGGGCTCCCCGGCCCCTACATAAAGTGGTTTCTGGAGAAGTTAAAGCCTGAAGGTCTC
CACCAGCTCCTGGCCGGGTTCGAGGACAAGTCAGCCTATGCGCTCTGCACGTTTGCACTC
AGCACCGGGGACCCAAGCCAGCCCGTGCGCCTGTTCAGGGGCCGGACCTCGGGCCGGATC
GTGGCACCCAGAGGCTGCCAGGACTTTGGCTGGGACCCCTGCTTTCAGCCTGATGGATAT
GAGCAGACGTACGCAGAGATGCCTAAGGCGGAGAAGAACGCTGTCTCCCATCGCTTCCGG
GCCCTGCTGGAGCTGCAGGAGTACTTTGGCAGTTTGGCAGCTTGA
|
| Enzyme 9 GenBank Gene ID |
AF219116  |
| Enzyme 9 GeneCard ID |
ITPA  |
| Enzyme 9 GenAtlas ID |
ITPA  |
| Enzyme 9 HGNC ID |
HGNC:6176  |
| Enzyme 9 Chromosome Location |
20 |
| Enzyme 9 Locus |
20p |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 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 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6012 |
| Enzyme 10 Name |
DNA-directed RNA polymerase II 140 kDa polypeptide |
| Enzyme 10 Synonyms |
- RNA polymerase II subunit 2
- RPB2
|
| Enzyme 10 Gene Name |
POLR2B |
| Enzyme 10 Protein Sequence |
>DNA-directed RNA polymerase II 140 kDa polypeptide
MYDADEDMQYDEDDDEITPDLWQEACWIVISSYFDEKGLVRQQLDSFDEFIQMSVQRIVE
DAPPIDLQAEAQHASGEVEEPPRYLLKFEQIYLSKPTHWERDGAPSPMMPNEARLRNLTY
SAPLYVDITKTVIKEGEEQLQTQHQKTFIGKIPIMLRSTYCLLNGLTDRDLCELNECPLD
PGGYFIINGSEKVLIAQEKMATNTVYVFAKKDSKYAYTGECRSCLENSSRPTSTIWVSML
ARGGQGAKKSAIGQRIVATLPYIKQEVPIIIVFRALGFVSDRDILEHIIYDFEDPEMMEM
VKPSLDEAFVIQEQNVALNFIGSRGAKPGVTKEKRIKYAKEVLQKEMLPHVGVSDFCETK
KAYFLGYMVHRLLLAALGRRELDDRDHYGNKRLDLAGPLLAFLFRGMFKNLLKEVRIYAQ
KFIDRGKDFNLELAIKTRIISDGLKYSLATGNWGDQKKAHQARAGVSQVLNRLTFASTLS
HLRRLNSPIGRDGKLAKPRQLHNTLWGMVCPAETPEGHAVGLVKNLALMAYISVGSQPSP
ILEFLEEWSMENLEEISPAAIADATKIFVNGCWVGIHKDPEQLMNTLRKLRRQMDIIVSE
VSMIRDIREREIRIYTDAGRICRPLLIVEKQKLLLKKRHIDQLKEREYNNYSWQDLVASG
VVEYIDTLEEETVMLAMTPDDLQEKEVAYCSTYTHCEIHPSMILGVCASIIPFPDHNQSP
RNTYQSAMGKQAMGVYITNFHVRMDTLAHVLYYPQKPLVTTRSMEYLRFRELPAGINSIV
AIASYTGYNQEDSVIMNRSAVDRGFFRSVFYRSYKEQESKKGFDQEEVFEKPTRETCQGM
RHAIYDKLDDDGLIAPGVRVSGDDVIIGKTVTLPENEDELESTNRRYTKRDCSTFLRTSE
TGIVDQVMVTLNQEGYKFCKIRVRSVRIPQIGDKFASRHGQKGTCGIQYRQEDMPFTCEG
ITPDIIINPHAIPSRMTIGHLIECLQGKVSANKGEIGDATPFNDAVNVQKISNLLSDYGY
HLRGNEVLYNGFTGRKITSQIFIGPTYYQRLKHMVDDKIHSRARGPIQILNRQPMEGRSR
DGGLRFGEMERDCQIAHGAAQFLRERLFEASDPYQVHVCNLCGIMAIANTRTHTYECRGC
RNKTQISLVRMPYACKLLFQELMSMSIAPRMMSV
|
| Enzyme 10 Number of Residues |
1174 |
| Enzyme 10 Molecular Weight |
133898 |
| Enzyme 10 Theoretical pI |
6.87 |
| Enzyme 10 GO Classification |
| Function |
- DNA binding
- DNA-directed RNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- transcription
|
| Component |
| — |
|
| Enzyme 10 General Function |
Transcription |
| Enzyme 10 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
36122  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P30876  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
RPB2_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>3525 bp
ATGTACGACGCGGATGAGGATATGCAATATGATGAGGATGATGATGAAATCACCCCGGAT
TTGTGGCAAGAAGCATGCTGGATTGTAATCAGTTCCTATTTTGACGAGAAAGGCTTGGTT
AGACAACAGCTGGATTCTTTTGATGAGTTTATTCAGATGTCTGTTCAAAGAATTGTGGAA
GACGCTCCTCCTATAGACCTACAGGCTGAAGCTCAGCATGCTAGTGGAGAAGTTGAAGAA
CCGCCACGATATTTGCTGAAGTTTGAACAAATTTATCTTTCCAAGCCTACCCATTGGGAA
AGAGATGGTGCTCCTTCACCAATGATGCCCAATGAAGCTAGATTAAGGAATCTCACGTAT
TCTGCTCCGCTTTATGTTGATATAACAAAAACAGTCATTAAAGAAGGTGAAGAACAACTT
CAGACTCAGCATCAGAAAACTTTTATAGGAAAAATTCCAATTATGTTGCGGTCAACTTAC
TGCCTTTTGAATGGCTTGACAGATCGTGATCTTTGTGAGTTAAATGAATGCCCTTTGGAT
CCTGGTGGCTATTTCATTATTAATGGATCAGAAAAGGTTCTGATTGCCCAAGAGAAAATG
GCAACAAACACAGTTTATGTGTTTGCCAAAAAGGATTCTAAATATGCCTACACAGGAGAG
TGTAGATCATGTCTTGAGAATTCTTCCCGACCCACCAGTACTATATGGGTTAGCATGCTG
GCAAGAGGAGGACAGGGTGCCAAGAAGAGTGCTATTGGTCAGCGCATTGTGGCAACTCTA
CCATATATCAAGCAAGAAGTTCCCATCATTATTGTGTTCAGAGCATTAGGTTTTGTGTCC
GACAGAGATATTTTAGAACATATTATTTATGATTTTGAAGATCCAGAGATGATGGAAATG
GTTAAACCTTCTCTCGATGAAGCTTTTGTCATCCAAGAACAGAATGTTGCACTAAATTTC
ATTGGTTCACGAGGAGCAAAGCCTGGTGTTACTAAAGAGAAAAGAATTAAATATGCAAAG
GAAGTTTTACAAAAAGAAATGCTCCCTCATGTTGGTGTCAGTGATTTTTGTGAGACCAAA
AAAGCCTATTTCTTGGGATACATGGTTCATAGGTTACTTCTGGCAGCTTTGGGTAGAAGA
GAACTAGATGACAGAGATCACTATGGAAACAAGAGATTGGATCTTGCTGGGCCGCTGCTT
GCATTCTTATTTAGAGGTATGTTTAAGAATTTGCTTAAAGAAGTGCGGATCTATGCACAG
AAATTTATTGATCGAGGAAAGGATTTTAACTTGGAGTTGGCAATTAAAACACGGATCATA
TCTGATGGCCTAAAATACTCTTTAGCTACTGGAAACTGGGGTGATCAAAAGAAAGCTCAT
CAAGCCAGAGCTGGAGTATCTCAGGTGTTAAACCGCCTGACTTTTGCGTCTACTCTTTCT
CACCTGCGTCGTTTAAATTCTCCTATTGGTAGAGACGGCAAGCTAGCAAAACCAAGACAG
TTGCATAATACGTTGTGGGGAATGGTGTGTCCTGCCGAGACCCCAGAGGGCCATGCTGTA
GGACTTGTGAAGAATTTAGCCTTGATGGCGTATATTTCAGTTGGATCTCAACCATCTCCA
ATTCTGGAATTTTTAGAAGAATGGAGTATGGAAAATTTAGAAGAAATTTCTCCTGCAGCT
ATTGCTGATGCAACCAAGATTTTTGTTAATGGCTGCTGGGTTGGAATACATAAAGATCCC
GAACAACTTATGAACACCCTAAGGAAATTGAGACGTCAGATGGACATCATTGTGTCTGAA
GTTTCTATGATCAGAGATATTCGAGAGAGGGAGATTCGGATCTATACGGATGCAGGCCGT
ATTTGTAGACCACTTCTGATTGTGGAAAAACAAAAGCTACTTTTGAAGAAGAGGCATATT
GACCAATTGAAAGAGAGAGAATATAACAACTATAGTTGGCAGGATCTTGTGGCCAGTGGG
GTAGTGGAGTATATTGATACCCTGGAAGAAGAAACAGTGATGCTTGCAATGACTCCAGAT
GATTTACAGGAGAAAGAAGTAGCTTATTGTTCCACATATACACACTGTGAGATTCATCCC
TCAATGATCCTTGGTGTCTGTGCATCTATTATTCCCTTTCCTGATCATAACCAGTCCCCT
AGAAACACATACCAGTCTGCTATGGGTAAGCAGGCTATGGGAGTTTACATCACCAACTTC
CATGTTCGCATGGACACATTGGCCCATGTTCTCTATTATCCTCAAAAGCCACTTGTGACT
ACACGGTCTATGGAATATCTACGATTTAGAGAGCTGCCAGCAGGCATCAACTCAATTGTG
GCCATTGCATCATACACTGGATATAATCAGGAAGACTCTGTTATCATGAATCGTTCAGCT
GTAGACCGCGGCTTCTTCAGGTCTGTTTTCTATCGCTCATACAAAGAACAGGAGTCTAAA
AAAGGATTTGATCAAGAAGAAGTTTTTGAGAAGCCTACACGTGAAACATGCCAGGGCATG
AGGCATGCCATTTACGACAAGCTGGATGATGATGGTTTGATAGCTCCAGGGGTTCGTGTA
TCAGGAGATGATGTTATTATAGGCAAAACAGTCACCTTGCCTGAAAATGAAGATGAATTG
GAGAGCACCAATAGACGCTATACCAAGAGAGACTGTAGCACTTTTCTCAGAACTAGTGAG
ACGGGCATTGTGGATCAGGTTATGGTAACTCTCAATCAGGAAGGATATAAATTTTGTAAA
ATAAGGGTACGCTCTGTTAGGATTCCACAGATTGGAGACAAATTTGCTAGTCGACATGGT
CAAAAGGGTACTTGTGGTATTCAGTATAGACAAGAGGATATGCCTTTCACCTGTGAAGGT
ATCACCCCTGATATCATCATCAATCCCCATGCCATCCCCTCTCGTATGACTATTGGTCAC
TTAATTGAATGCCTTCAAGGGAAGGTATCGGCTAACAAGGGTGAAATTGGTGATGCCACT
CCATTTAATGATGCTGTTAACGTGCAGAAGATTTCTAATCTTTTATCTGATTATGGCTAT
CATCTCAGAGGAAATGAGGTCCTGTACAATGGGTTCACTGGTCGAAAAATCACATCACAA
ATATTTATTGGCCCCACTTATTACCAGCGTTTGAAGCATATGGTGGATGATAAGATTCAC
TCTCGTGCTAGGGGACCTATTCAGATCCTCAATAGACAGCCCATGGAGGGTAGATCTCGT
GATGGTGGCCTGCGTTTTGGAGAAATGGAACGAGATTGTCAGATTGCCCATGGAGCAGCC
CAGTTTTTAAGGGAAAGATTGTTTGAGGCATCAGATCCATATCAGGTTCATGTTTGCAAT
CTTTGTGGAATAATGGCGATTGCCAACACCAGGACCCATACATATGAATGCAGGGGCTGC
CGCAATAAAACCCAGATTTCTTTGGTGCGAATGCCTTACGCATGCAAACTATTGTTTCAG
GAACTTATGTCTATGAGTATTGCACCGCGAATGATGAGTGTTTAG
|
| Enzyme 10 GenBank Gene ID |
X63563  |
| Enzyme 10 GeneCard ID |
POLR2B  |
| Enzyme 10 GenAtlas ID |
POLR2B  |
| Enzyme 10 HGNC ID |
HGNC:9188  |
| Enzyme 10 Chromosome Location |
4 |
| Enzyme 10 Locus |
4q12 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Acker J, Wintzerith M, Vigneron M, Kedinger C: Primary structure of the second largest subunit of human RNA polymerase II (or B). J Mol Biol. 1992 Aug 20;226(4):1295-9. [PubMed
]
- Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6014 |
| Enzyme 11 Name |
DNA-directed RNA polymerase II largest subunit |
| Enzyme 11 Synonyms |
- RPB1
|
| Enzyme 11 Gene Name |
POLR2A |
| Enzyme 11 Protein Sequence |
>DNA-directed RNA polymerase II largest subunit
MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDP
RQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVD
SNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKG
HGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEP
RYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAA
HVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVD
FSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYII
RDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWS
TFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQD
TLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHI
NCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEM
GHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKA
HNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKIN
ISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHA
MGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGES
VEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMR
EDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKL
VIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAI
AHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLT
VFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMP
DFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIR
IMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKI
IITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALER
ELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLM
EAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTG
MFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPG
YSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSP
SYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSP
TSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPS
YSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPT
SPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPTSPKYTPTSPSYSPSSPEYTPTSPKY
SPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTS
PKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDEEN
|
| Enzyme 11 Number of Residues |
1970 |
| Enzyme 11 Molecular Weight |
217208 |
| Enzyme 11 Theoretical pI |
7.38 |
| Enzyme 11 GO Classification |
| Function |
- DNA binding
- DNA-directed RNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- transcription
- transcription from RNA polymerase II promoter
- transcription, DNA-dependent
|
| Component |
- DNA-directed RNA polymerase II, core complex
- RNA polymerase complex
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
- protein complex
|
|
| Enzyme 11 General Function |
Transcription |
| Enzyme 11 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
36124  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
P24928  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
RPB1_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>5913 bp
ATGCACGGGGGTGGCCCCCCCTCGGGGGACAGCGCATGCCCGCTGCGCACCATCAAGAGA
GTCCAGTTCGGAGTCCTGAGTCCGGATGAACTGAAGCGAATGTCTGTGACGGAGGGTGGC
ATCAAATACCCAGAGACGACTGAGGGAGGCCGCCCCAAGCTTGGGGGGCTGATGGACCCG
AGGCAGGGGGTGATTGAGCGGACTGGCCGCTGCCAAACATGTGCAGGAAACATGACAGAG
TGTCCTGGCCACTTTGGCCACATTGAACTGGCCAAGCCTGTGTTTCACGTGGGCTTCCTG
GTGAAGACAATGAAAGTTTTGCGCTGTGTCTGCTTCTTCTGCTCCAAACTGCTTGTGGAC
TCTAACAACCCAAAGATCAAGGATATCCTGGCTAAGTCCAAGGGACAGCCCAAGAAGCGG
CTCACACATGTCTACGACCTTTGCAAGGGCAAAAACATATGCGAGGGTGGGGAGGAGATG
GACAACAAGTTCGGTGTGGAACAACCTGAGGGTGACGAGGATCTGACCAAAGAAAAGGGC
CATGGTGGCTGTGGGCGGTACCAGCCCAGGATCCGGCGTTCTGGCCTAGAGCTGTATGCG
GAATGGAAGCACGTTAATGAGGACTCTCAGGAGAAGAAGATCCTGCTGAGTCCAGAGCGA
GTGCATGAGATCTTCAAACGCATCTCAGATGAGGAGTGTTTTGTGCTGGGCATGGAGCCC
CGCTATGCACGGCCAGAGTGGATGATTGTCACAGTGCTGCCTGTGCCCCCGCTCTCCGTG
CGGCCTGCTGTTGTGATGCAGGGCTCTGCCCGTAACCAGGATGACCTGACTCACAAACTG
GCTGACATCGTGAAGATCAACAATCAGCTGCGGCGCAATGAGCAGAACGGCGCAGCGGCC
CATGTCATTGCAGAGGATGTGAAGCTCCTCCAGTTCCATGTGGCCACCATGGTGGACAAT
GAGCTGCCTGGCTTGCCCCGTGCCATGCAGAAGTCTGGGCGTCCCCTCAAGTCCCTGAAG
CAGCGGTTGAAGGGCAAGGAAGGCCGGGTGCGAGGGAACCTGATGGGCAAAAGAGTGGAC
TTCTCGGCCCGTACTGTCATCACCCCCGACCCCAACCTCTCCATTGACCAGGTTGGCGTG
CCCCGCTCCATTGCTGCCAACATGACCTTTGCGGAGATTGTCACCCCCTTCAACATTGAC
AGACTTCAAGAACTAGTGCGCAGGGGGAACAGTCAGTACCCAGGCGCCAAGTACATCATC
CGAGACAATGGTGATCGCATTGACTTGCGTTTCCACCCCAAGCCCAGTGACCTTCACCTG
CAGACCGGCTATAAGGTGGAACGGCACATGTGTGATGGGGACATTGTTATCTTCAACCGG
CAGCCAACTCTGCACAAAATGTCCATGATGGGGCATCGGGTCCGCATTCTCCCATGGTCT
ACCTTTCGCTTGAATCTTAGCGTGACAACTCCGTACAATGCAGACTTTGACGGGGATGAG
ATGAACTTGCACCTGCCACAGTCTCTGGAGACGCGAGCAGAGATCCAGGAGCTGGCCATG
GTTCCTCGCATGATTGTCACCCCCCAGAGCAATCGGCCTGTCATGGGTATTGTGCAGGAC
ACACTCACAGCAGTGCGCAAATTCACCAAGAGAGACGTCTTCCTGGAGCGGGGTGAAGTG
ATGAACCTCCTGATGTTCCTGTCGACGTGGGATGGGAAGGTCCCACAGCCGGCCATCCTA
AAGCCCCGGCCCCTGTGGACAGGCAAGCAAATCTTCTCCCTCATCATACCTGGTCACATC
AATTGTATCCGTACCCACAGCACCCATCCCGATGATGAAGACAGTGGCCCTTACAAGCAC
ATCTCTCCTGGGGACACCAAGGTGGTGGTGGAGAATGGGGAGCTGATCATGGGCATCCTG
TGTAAGAAGTCTCTGGGCACGTCAGCTGGCTCCCTGGTCCACATCTCCTACCTAGAGATG
GGTCATGACATCACTCGCCTCTTCTACTCCAACATTCAGACTGTCATTAACAACTGGCTC
CTCATCGAGGGTCATACTATTGGCATTGGGGACTCCATTGCTGATTCTAAGACTTACCAG
GACATTCAGAACACTATTAAGAAGGCCAAGCAGGACGTAATAGAGGTCATCGAGAAGGCA
CACAACAATGAGCTGGAGCCCACCCCAGGGAACACTCTGCGGCAGACGTTTGAGAATCAG
GTGAACCGCATTCTTAACGATGCCCGAGACAAGACTGGCTCCTCTGCTCAGAAATCCCTG
TCTGAATACAACAACTTCAAGTCTATGGTCGTGTCCGGAGCTAAAGGTTCCAAGATTAAC
ATCTCCCAGGTCATTGCTGTCGTTGGACAGCAGAACGTCGAGGGCAAGCGGATTCCATTT
GGCTTCAAGCACCGGACTCTGCCTCACTTCATCAAGGATGACTACGGGCCTGAGAGCCGT
GGCTTTGTGGAGAACTCCTACCTAGCCGGCCTCACACCCACTGAGTTCTTTTTCCACGCC
ATGGGGGGTCGTGAGGGGCTCATTGACACGGCTGTCAAGACTGCTGAGACTGGATACATC
CAGCGGCGGCTGATCAAGTCCATGGAGTCAGTGATGGTGAAGTACGACGCGACTGTGCGG
AACTCCATCAACCAGGTGGTGCAGCTGCGCTACGGCGAAGACGGCCTGGCAGGCGAGAGC
GTTGAGTTCCAGAACCTGGCTACGCTTAAGCCTTCCAACAAGGCTTTTGAGAAGAAGTTC
CGCTTTGATTATACCAATGAGAGGGCCCTGCGGCGCACTCTGCAGGAGGACCTGGTGAAG
GACGTGCTGAGCAACGCACACATCCAGAACGAGTTGGAGCGGGAATTTGAGCGGATGCGG
GAGGATCGGGAGGTGCTCAGGGTCATCTTCCCAACTGGAGACAGCAAGGTCGTCCTCCCC
TGTAACCTGCTGCGGATGATCTGGAATGCTCAGAAAATCTTCCACATCAACCCACGCCTT
CCCTCCGACCTGCACCCCATCAAAGTGGTGGAGGGAGTCAAGGAATTGAGCAAGAAGCTG
GTGATTGTGAATGGGGATGACCCACTAAGTCGACAGGCCCAGGAAAATGCCACGCTGCTC
TTCAACATCCACCTGCGGTCCACGTTGTGTTCCCGCCGCATGGCAGAGGAGTTTCGGCTC
AGTGGGGAGGCCTTCGACTGGCTGCTTGGGGAGATTGAGTCCAAGTTCAACCAAGCCATT
GCGCATCCCGGGGAAATGGTGGGGGCTCTGGCTGCGCAGTCCCTTGGAGAACCTGCCACC
CAGATGACCTTGAATACCTTCCACTATGCTGGTGTGTCTGCCAAGAATGTGACGCTGGGT
GTGCCCCGACTTAAGGAGCTCATCAACATTTCCAAGAAGCCAAAGACTCCTTCGCTTACT
GTCTTCCTGTTGGGCCAGTCCGCTCGAGATGCTGAGAGAGCCAAGGATATTCTGTGCCGT
CTGGAGCATACAACGTTGAGGAAGGTGACTGCCAACACAGCCATCTACTATGACCCCAAC
CCCCAGAGCACGGTGGTGGCAGAGGATCAGGAATGGGTGAATGTCTACTATGAAATGCCT
GACTTTGATGTGGCCCGAATCTCCCCCTGGCTGTTGCGGGTGGAGCTGGATCGGAAGCAC
ATGACTGACCGGAAGCTCACCATGGAGCAGATTGCTGAAAAGATCAATGCTGGTTTTGGT
GACGACTTGAACTGCATCTTTAATGATGACAATGCAGAGAAGCTGGTGCTCCGTATTCGC
ATCATGAACAGCGATGAGAACAAGATGCAAGAGGAGGAAGAGGTGGTGGACAAGATGGAT
GATGATGTCTTCCTGCGCTGCATCGAGTCCAACATGCTGACAGATATGACCCTGCAGGGC
ATCGAGCAGATCAGCAAGGTGTACATGCACTTGCCACAGACAGACAACAAGAAGAAGATC
ATCATCACGGAGGATGGGGAATTCAAGGCCCTGCAGGAGTGGATCCTGGAGACGGACGGC
GTGAGCTTGATGCGGGTGCTGAGTGAGAAGGACGTGGACCCCGTACGCACCACGTCCAAT
GACATTGTGGAGATCTTCACGGTGCTGGGCATTGAAGCCGTGCGGAAGGCCCTGGAGCGG
GAGCTGTACCACGTCATCTCCTTTGATGGCTCCTATGTCAATTACCGACACTTGGCTCTC
TTGTGTGATACCATGACCTGTCGTGGCCACTTGATGGCCATCACCCGACACGGAGTCAAC
CGCCAGGACACAGGACCACTCATGAAGTGTTCCTTTGAGGAAACGGTGGACGTGCTTATG
GAAGCAGCCGCACACGGTGAGAGTGACCCCATGAAGGGGGTCTCTGAGAATATCATGCTG
GGCCAGCTGGCTCCGGCCGGCACTGGCTGCTTTGACCTCCTGCTTGATGCAGAGAAGTGC
AAGTATGGCATGGAGATCCCCACCAATATCCCCGGCCTGGGGGCTGCTGGACCCACCGGC
ATGTTCTTTGGTTCAGCACCCAGTCCCATGGGTGGAATCTCTCCTGCCATGACACCTTGG
AACCAGGGTGCAACCCCTGCCTATGGCGCCTGGTCCCCCAGTGTTGGGAGTGGAATGACC
CCAGGGGCAGCCGGTTTCTCTCCCAGTGCTGCGTCAGATGCCAGCGGCTTCAGCCCAGGT
TACTCCCCTGCCTGGTCTCCCACACCGGGCTCCCCGGGGTCCCCAGGTCCCTCAAGCCCC
TACATCCCTTCACCAGGTGGCGCCATGTCTCCCAGCTACTCGCCAACGTCACCTGCCTAC
GAGCCCCGCTCTCCTGGGGGCTACACACCCCAGAGTCCCTCTTATTCCCCCACTTCACCC
TCCTACTCCCCTACCTCTCCATCCTATTCTCCAACCAGTCCCAACTATAGTCCCACATCA
CCCAGCTATTCGCCAACGTCACCCAGCTACTCACCGACCTCTCCCAGCTACTCACCCACC
TCTCCCAGCTACTCGCCCACCTCTCCCAGCTATTCGCCCACCTCTCCCAGCTACTCACCC
ACTTCCCCTAGCTATTCGCCCACTTCCCCTAGCTACTCGCCAACGTCTCCCAGCTACTCG
CCGACATCTCCCAGCTACTCGCCAACTTCACCCAGCTATTCTCCCACTTCTCCCAGCTAC
TCACCTACCTCTCCAAGCTATTCACCCACCTCCCCCAGCTACTCACCCACTTCCCCAAGT
TACTCACCCACCAGCCCGAACTATTCTCCAACCAGTCCCAATTACACCCCAACATCACCC
AGCTACAGCCCGACATCACCCAGCTATTCCCCTACTAGTCCCAACTACACACCTACCAGC
CCTAACTACAGCCCAACCTCTCCAAGCTACTCTCCAACATCACCCAGCTATTCCCCGACC
TCACCAAGTTACTCCCCTTCCAGCCCACGATACACACCACAGTCTCCAACCTATACCCCA
AGCTCACCCAGCTACAGCCCCAGTTCGCCCAGCTACAGCCCAACCTCACCCAAGTACACC
CCAACCAGTCCTTCTTATAGTCCCAGCTCCCCAGAGTATACCCCAACCTCTCCCAAGTAC
TCACCTACCAGTCCCAAATATTCACCCACCTCTCCCAAGTACTCGCCTACCAGTCCCACC
TATTCACCCACCACCCCAAAATACTCCCCAACATCTCCTACTTATTCCCCAACCTCTCCA
GTCTACACCCCAACCTCTCCCAAGTACTCACCTACTAGCCCCACTTACTCGCCCACTTCC
CCCAAGTACTCGCCCACCAGCCCCACCTACTCGCCCACCTCCCCCAAAGGCTCAACCTAC
TCTCCCACTTCCCCTGGTTACTCGCCCACCAGCCCCACCTACAGTCTCACAAGCCCGGCT
ATCAGCCCGGATGACAGTGACGAGGAGAACTGA
|
| Enzyme 11 GenBank Gene ID |
X63564  |
| Enzyme 11 GeneCard ID |
POLR2A  |
| Enzyme 11 GenAtlas ID |
POLR2A  |
| Enzyme 11 HGNC ID |
HGNC:9187  |
| Enzyme 11 Chromosome Location |
17 |
| Enzyme 11 Locus |
17p13.1 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Wintzerith M, Acker J, Vicaire S, Vigneron M, Kedinger C: Complete sequence of the human RNA polymerase II largest subunit. Nucleic Acids Res. 1992 Feb 25;20(4):910. [PubMed
]
- Mita K, Tsuji H, Morimyo M, Takahashi E, Nenoi M, Ichimura S, Yamauchi M, Hongo E, Hayashi A: The human gene encoding the largest subunit of RNA polymerase II. Gene. 1995 Jul 4;159(2):285-6. [PubMed
]
- Nayler O, Stratling W, Bourquin JP, Stagljar I, Lindemann L, Jasper H, Hartmann AM, Fackelmayer FO, Ullrich A, Stamm S: SAF-B protein couples transcription and pre-mRNA splicing to SAR/MAR elements. Nucleic Acids Res. 1998 Aug 1;26(15):3542-9. [PubMed
]
- Allen M, Friedler A, Schon O, Bycroft M: The structure of an FF domain from human HYPA/FBP11. J Mol Biol. 2002 Oct 25;323(3):411-6. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6017 |
| Enzyme 12 Name |
DNA-directed RNA polymerase, mitochondrial precursor |
| Enzyme 12 Synonyms |
- MtRPOL
|
| Enzyme 12 Gene Name |
POLRMT |
| Enzyme 12 Protein Sequence |
>DNA-directed RNA polymerase, mitochondrial precursor
MSALCWGRGAAGLKRALRPCGRPGLPGKEGTAGGVCGPRRSSSASPQEQDQDRRKDWGHV
ELLEVLQARVRQLQAESVSEVVVNRVDVARLPECGSGDGSLQPPRKVQMGAKDATPVPCG
RWAKILEKDKRTQQMRMQRLKAKLQMPFQSGEFKALTRRLQVEPRLLSKQMAGCLEDCTR
QAPESPWEEQLARLLQEAPGKLSLDVEQAPSGQHSQAQLSGQQQRLLAFFKCCLLTDQLP
LAHHLLVVHHGQRQKRKLLTLDMYNAVMLGWARQGAFKELVYVLFMVKDAGLTPDLLSYA
AALQCMGRQDQDAGTIERCLEQMSQEGLKLQALFTAVLLSEEDRATVLKAVHKVKPTFSL
PPQLPPPVNTSKLLRDVYAKDGRVSYPKLHLPLKTLQCLFEKQLHMELASRVCVVSVEKP
TLPSKEVKHARKTLKTLRDQWEKALCRALRETKNRLEREVYEGRFSLYPFLCLLDEREVV
RMLLQVLQALPAQGESFTTLARELSARTFSRHVVQRQRVSGQVQALQNHYRKYLCLLASD
AEVPEPCLPRQYWEELGAPEALREQPWPLPVQMELGKLLAEMLVQATQMPCSLDKPHRSS
RLVPVLYHVYSFRNVQQIGILKPHPAYVQLLEKAAEPTLTFEAVDVPMLCPPLPWTSPHS
GAFLLSPTKLMRTVEGATQHQELLETCPPTALHGALDALTQLGNCAWRVNGRVLDLVLQL
FQAKGCPQLGVPAPPSEAPQPPEAHLPHSAAPARKAELRRELAHCQKVAREMHSLRAEAL
YRLSLAQHLRDRVFWLPHNMDFRGRTYPCPPHFNHLGSDVARALLEFAQGRPLGPHGLDW
LKIHLVNLTGLKKREPLRKRLAFAEEVMDDILDSADQPLTGRKWWMGAEEPWQTLACCME
VANAVRASDPAAYVSHLPVHQDGSCNGLQHYAALGRDSVGAASVNLEPSDVPQDVYSGVA
AQVEVFRRQDAQRGMRVAQVLEGFITRKVVKQTVMTVVYGVTRYGGRLQIEKRLRELSDF
PQEFVWEASHYLVRQVFKSLQEMFSGTRAIQHWLTESARLISHMGSVVEWVTPLGVPVIQ
PYRLDSKVKQIGGGIQSITYTHNGDISRKPNTRKQKNGFPPNFIHSLDSSHMMLTALHCY
RKGLTFVSVHDCYWTHAADVSVMNQVCREQFVRLHSEPILQDLSRFLVKRFCSEPQKILE
ASQLKETLQAVPKPGAFDLEQVKRSTYFFS
|
| Enzyme 12 Number of Residues |
1230 |
| Enzyme 12 Molecular Weight |
138622 |
| Enzyme 12 Theoretical pI |
9.25 |
| Enzyme 12 GO Classification |
| Function |
- DNA binding
- DNA-directed RNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- transcription
|
| Component |
| — |
|
| Enzyme 12 General Function |
Not Available |
| Enzyme 12 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
2114396  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
O00411  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
RPOM_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>3693 bp
ATGTCGGCACTTTGCTGGGGCCGCGGAGCGGCGGGGCTCAAACGAGCCCTACGGCCTTGC
GGCCGCCCGGGACTCCCCGGCAAAGAAGGGACCGCCGGTGGCGTCTGCGGCCCCAGGAGG
AGCTCGTCCGCCAGCCCCCAGGAGCAAGACCAAGACCGCAGGAAGGACTGGGGCCACGTG
GAGCTGCTGGAGGTGCTCCAGGCGCGGGTGCGGCAGCTGCAGGCTGAGAGCGTGTCGGAG
GTGGTGGTGAACAGGGTGGATGTGGCGCGGCTCCCAGAATGTGGCAGTGGAGATGGTAGC
CTCCAGCCACCCAGGAAGGTCCAGATGGGGGCCAAGGATGCCACCCCGGTGCCCTGTGGC
CGCTGGGCAAAGATACTGGAGAAGGATAAGCGGACCCAGCAGATGCGTATGCAGCGGTTG
AAGGCGAAGCTGCAGATGCCATTCCAGAGCGGGGAGTTCAAGGCGCTGACCAGGCGCCTG
CAGGTGGAGCCCCGGCTCCTGAGCAAGCAGATGGCCGGGTGCCTGGAGGACTGCACGCGC
CAGGCCCCCGAGAGCCCCTGGGAGGAGCAGCTGGCCCGGCTGCTGCAGGAGGCCCCTGGG
AAGCTGAGCCTCGATGTGGAGCAGGCCCCGTCGGGGCAGCACTCGCAGGCCCAGCTCTCA
GGTCAGCAGCAGAGGCTCCTGGCCTTCTTCAAGTGCTGCCTGCTCACTGACCAGCTGCCC
CTCGCCCACCACCTGCTGGTCGTCCACCACGGCCAGCGGCAGAAGCGGAAGCTGCTCACG
CTGGACATGTACAACGCCGTGATGCTTGGCTGGGCGCGGCAGGGTGCTTTCAAGGAGCTG
GTATATGTGTTATTCATGGTGAAGGATGCCGGCTTGACCCCGGACCTGCTGTCCTATGCG
GCTGCCCTCCAGTGCATGGGGAGGCAGGACCAGGACGCCGGGACCATCGAAAGGTGTCTG
GAACAGATGAGCCAGGAGGGGCTGAAGCTGCAGGCACTCTTCACCGCCGTTCTGCTGTCT
GAGGAGGATCGGGCCACTGTTCTGAAGGCCGTGCACAAGGTGAAGCCCACCTTCAGCCTC
CCGCCGCAGCTGCCGCCCCCGGTCAACACCTCCAAGCTGCTCAGGGACGTGTATGCCAAG
GATGGGCGTGTGTCCTACCCGAAGCTGCACCTGCCCTTGAAGACCCTGCAGTGCTTCTTT
GAGAAGCAGCTCCACATGGAGCTGGCCAGCAGGGTGTGCGTGGTGTCCGTGGAGAAGCCC
ACGTTGCCAAGCAAGGAGGTCAAGCACGCGCGGAAGACCCTGAAGACCCTGCGGGACCAA
TGGGAGAAAGCACTGTGCCGGGCGCTGCGGGAGACCAAGAACCGCCTAGAGCGCGAGGTG
TACGAGGGCCGGTTCTCACTTTACCCCTTCCTGTGCCTGCTGGACGAGCGCGAGGTGGTG
CGGATGCTCCTGCAGGTCCTGCAGGCGCTGCCCGCCCAAGGTGAGTCCTTCACCACCCTG
GCCCGGGAGCTGAGTGCGCGCACTTTCAGCCGGCACGTGGTGCAGAGGCAGCGGGTCAGT
GGCCAGGTGCAGGCGCTGCAGAACCACTACAGGAAGTACCTCTGCTTGCTGGCCTCCGAC
GCCGAGGTGCCCGAGCCCTGCCTGCCGCGGCAGTACTGGGAGGAGCTGGGGGCGCCCGAG
GCCCTGCGGGAGCAGCCCTGGCCCCTGCCAGTGCAGATGGAGCTGGGCAAGCTGCTGGCG
GAGATGCTGGTGCAGGCTACGCAGATGCCATGCAGCCTGGACAAGCCGCATCGTTCCTCT
CGGCTTGTCCCCGTGCTCTACCACGTGTATTCCTTCCGCAACGTCCAGCAAATCGGCATC
CTGAAGCCGCACCCGGCCTACGTGCAGCTGCTGGAGAAGGCCGCGGAACCCACGCTGACC
TTCGAGGCGGTGGATGTACCCATGCTTTGCCCCCCGCTGCCCTGGACATCGCCGCACTCT
GGTGCTTTCCTGCTCAGCCCCACCAAGCTGATGCGCACGGTGGAAGGCGCCACGCAACAC
CAGGAGCTGCTGGAAACCTGCCCACCCACCGCGCTGCATGGCGCACTGGACGCCCTCACC
CAACTGGGCAACTGCGCCTGGCGCGTCAACGGGCGCGTGCTGGACCTGGTGCTGCAGCTC
TTCCAGGCCAAGGGCTGCCCCCAGCTAGGCGTGCCGGCCCCGCCCTCCGAGGCGCCCCAG
CCGCCCGAGGCCCACCTGCCGCACAGCGCCGCGCCCGCCCGCAAGGCCGAGCTGCGCCGT
GAGCTGGCGCACTGCCAGAAGGTGGCCCGGGAGATGCACAGCCTGCGGGCGGAGGCGCTG
TACCGCCTCTCGCTGGCGCAGCACCTGCGGGACCGCGTCTTCTGGCTGCCGCACAACATG
GACTTCCGCGGCCGCACCTACCCCTGCCCGCCGCACTTCAACCACCTGGGCAGCGACGTG
GCGCGGGCCCTGCTGGAGTTCGCCCAGGGCCGCCCGCTCGGCCCGCACGGCCTGGATTGG
CTCAAGATCCACCTGGTCAATCTCACGGGGTTGAAGAAGCGGGAGCCGCTGCGGAAGCGC
CTGGCCTTTGCGGAGGAGGTGATGGATGACATCCTGGACTCCGCGGACCAACCCTTGACG
GGCCGAAAGTGGTGGATGGGCGCGGAGGAACCCTGGCAGACGCTGGCCTGCTGTATGGAG
GTGGCGAACGCTGTGCGCGCCTCCGACCCTGCCGCCTATGTCTCCCACCTCCCCGTCCAT
CAGGACGGCTCTTGCAACGGCCTGCAGCATTATGCTGCTCTGGGCCGCGACAGCGTGGGC
GCCGCCTCCGTCAACCTGGAGCCCTCGGATGTGCCGCAGGACGTGTACAGCGGCGTGGCC
GCGCAGGTGGAGGTGTTCCGTAGGCAGGACGCCCAGCGGGGCATGCGGGTGGCACAGGTG
CTGGAAAGTTTCATCACCCGCAAGGTGGTGAAGCAGACGGTGATGACGGTGGTGTACGGG
GTCACGCGCTATGGCGGGCGCCTGCAGATTGAGAAGCGCCTCCGGGAGCTGAGCGACTTT
CCCCAGGAGTTCGTGTGGGAGGCCTCTCACTATCTCGTACGCCAGGTCTTCAAGAGTCTA
CAGGAGATGTTCTCGGGGACCCGGGCCATCCAGCACTGGCTGACCGAGAGTGCCCGCCTC
ATCTCCCACATGGGCTCTGTGGTGGAGTGGGTCACACCCCTGGGCGTCCCCGTCATCCAG
CCGTATCGCCTGGACTCCAAGGTCAAGCAAATAGGAGGTGGAATTCAGAGCATCACCTAC
ACCCACAACGGAGACATCAGCCGAAAGCCCAACACACGTAAGCAGAAGAACGGCTTCCCG
CCCAACTTCATCCACTCGCTGGACTCCTCCCACATGATGCTCACCGCCCTGCACTGCTAC
AGGAAGGGCCTGACCTTCGTCTCTGTGCACGACTGTTACTGGACTCACGCAGCTGATGTC
TCCGTCATGAACCAGGTGTGCCGGGAGCAGTTTGTCCGCTTGCACAGCGAGCCCATCCTG
CAGGACCTGTCCAGATTCCTGGTCAAGCGGTTCTGCTCTGAGCCCCAGAAGATCTTGGAG
GCCAGCCAGCTGAAGGAGACACTGCAGGCGGTGCCCAAGCCAGGGGCCTTCGACCTGGAG
CAGGTGAAGCGTTCCACCTACTTCTTCAGCTGA
|
| Enzyme 12 GenBank Gene ID |
U75370  |
| Enzyme 12 GeneCard ID |
POLRMT  |
| Enzyme 12 GenAtlas ID |
POLRMT  |
| Enzyme 12 HGNC ID |
HGNC:9200  |
| Enzyme 12 Chromosome Location |
19 |
| Enzyme 12 Locus |
19p13.3 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Tiranti V, Savoia A, Forti F, D'Apolito MF, Centra M, Rocchi M, Zeviani M: Identification of the gene encoding the human mitochondrial RNA polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence Tags database. Hum Mol Genet. 1997 Apr;6(4):615-25. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6018 |
| Enzyme 13 Name |
DNA-directed RNA polymerase I 135 kDa polypeptide |
| Enzyme 13 Synonyms |
- RNA polymerase I subunit 2
- RPA135
|
| Enzyme 13 Gene Name |
POLR1B |
| Enzyme 13 Protein Sequence |
>DNA-directed RNA polymerase I 135 kDa polypeptide
MDPGSRWRNLPSGPSLKHLTDPSYGIPREQQKAALQELTRAHVESFNYAVHEGLGLAVQA
IPPFEFAFKDERISFTILDAVISPPTVPKGTICKEANVYPAECRGRRSTYRGKLTADINW
AVNGISKGIIKQFLGYVPIMVKSKLCNLRNLPPQALIEHHEEAEEMGGYFIINGIEKVIR
MLIMPRRNFPIAMIRPKWKTRGPGYTQYGVSMHCVREEHSAVNMNLHYLENGTVMLNFIY
RKELFFLPLGFALKALVSFSDYQIFQELIKGKEDDSFLRNSVSQMLRIVMEEGCSTQKQV
LNYLGECFRVKLNVPDWYPNEQAAEFLFNQCICIHLKSNTEKFYMLCLMTRKLFALAKGE
CMEDNPDSLVNQEVLTPGQLFLMFLKEKLEGWLVSIKIAFDKKAQKTSVSMNTDNLMRIF
TMGIDLTKPFEYLFATGNLRSKTGLGLLQDSGLCVVADKLNFIRYLSHFRCVHRGADFAK
MRTTTVRRLLPESWGFLCPVHTPDGEPCGLMNHLTAVCEVVTQFVYTASIPALLCNLGVT
PIDGAPHRSYSECYPVLLDGVMVGWVDKDLAPGIADSLRHFKVLREKRIPPWMEVVLIPM
TGKPSLYPGLFLFTTPCRLVRPVQNLALGKEELIGTMEQIFMNVAIFEDEVFAGVTTHQE
LFPHSLLSVIANFIPFSDHNQSPRNMYQCQMGKQTMGFPLLTYQDRSDNKLYRLQTPQSP
LVRPSMYDYYDMDNYPIGTNAIVAVISYTGYDMEDAMIVNKASWERGFAHGSVYKSEFID
LSEKIKQGDSSLVFGIKPGDPRVLQKLDDDGLPFIGAKLQYGDPYYSYLNLNTGESFVMY
YKSKENCVVDNIKVCSNDTGSGKFKCVCITMRVPRNPTIGDKFASRHGQKGILSRLWPAE
DMPFTESGMVPDILFNPHGFPSRMTIGMLIESMAGKSAALHGLCHDATPFIFSEENSALE
YFGEMLKAAGYNFYGTERLYSGISGLELEADIFIGVVYYQRLRHMVSDKFQVRTTGARDR
VTNQPIGGRNVQGGIRFGEMERDALLAHGTSFLLHDRLFNCSDRSVAHVCVKCGSLLSPL
LEKPPPSWSAMRNRKYNCTLCSRSDTIDTVSVPYVFRYFVAELAAMNIKVKLDVV
|
| Enzyme 13 Number of Residues |
1135 |
| Enzyme 13 Molecular Weight |
128231 |
| Enzyme 13 Theoretical pI |
7.88 |
| Enzyme 13 GO Classification |
| Function |
- DNA binding
- DNA-directed RNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- transcription
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 13 General Function |
Transcription |
| Enzyme 13 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. RNA polymerase I is essentially used to transcribe ribosomal DNA units |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
10433976  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q9H9Y6  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
RPA2_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>3240 bp
ATGGATCCTGGCAGCCGGTGGCGGAACCTGCCCAGCGGGCCTAGCCTAAAGCACTTGACT
GACCCCTCTTATGGAATCCCGCGGGAACAGCAAAAGGCAGCGTTGCAGGAGCTGACGCGG
GCGCACGTGGAGTCCTTCAACTACGCTGTGCACGAGGGTCTCGGCCTCGCGGTGCAGGCT
GATATCAACTGGGCAGTGAATGGAATCTCAAAAGGAATCATTAAGCAGTTTCTTGGCTAC
GTTCCCATCATGGTGAAATCCAAGCTTTGCAACTTACGTAACCTTCCCCCACAAGCCCTC
ATTGAGCACCATGAGGAGGCAGAGGAAATGGGGGGCTATTTTATAATCAATGGCATTGAA
AAAGTCATCCGAATGTTGATTATGCCTCGGAGAAATTTTCCCATTGCAATGATAAGACCA
AAATGGAAAACCAGAGGGCCTGGTTATACTCAGTATGGAGTTTCAATGCACTGTGTGAGG
GAAGAACATTCCGCTGTCAATATGAACCTCCACTACTTGGAAAATGGCACAGTTATGTTG
AACTTTATTTACCGAAAAGAACTGTTCTTTCGTCCTTTGGGATTTGCACTTAAGGCACTT
GTCAGCTTTTCTGATTATCAGATCTTTCAGGAGCTCATCAAAGGAAAAGAGGATGATTCT
TTCCTTAGGAACTCTGTTTCTCAGATGTTAAGGATTGTAATGGAAGAGGGTTGTTTGACA
CAAAAACAGGTCCTTAACTACCTAGGTGAATGCTTCAGAGTAAAACTCAATGTTCCTGAC
TGGTACCCAAATGAGCAAGCTGCGGAGTTCCTGTTTAACCAGTGCATCTGTATCCACTTG
AAATCCAATACTGAAAAGTTTTATATGCTTTGTCTCATGACGCGAAAGCTCTTTGCTTTA
GCCAAAGGAGAGTGCATGGAGGACAATCCTGATAGTTTGGTGAACCAGGAAGTCCTCACA
CCGGGTCAGCTCTTCCTTATGTTCCTGAAGGAAAAACTGGAAGGTTGGTTAGTGTCTATT
AAAATAGCTTTTGATAAGAAGGCTCAGAAGACCAGTGTTTCCATGAACACTGACAATTTG
ATGAGGATTTTTACAATGGGCATAGACCTTACAAAACCATTTGAATACCTTTTTGCTACT
GGGAATCTGCGTTCTAAAACAGGTCTTGGCCTCCTACAAGATTCTGGACTTTGTGTTGTG
GCTGACAAGCTGAACTTCATACGCTACCTCTCCCATTTCCGCTGCGTGCACAGAGGGGCT
GATTTTGCCAAGATGAGGACCACCACAGTACGCAGGCTGCTGCCAGAGTCCTGGGGCTTC
CTTTGTCCCGTGCATACCCCAGACGGGGAGCCCTGTGGCCTGATGAACCACCTAACTGCC
GTATGTGAGGTTGTCACACAGTTTGTGTATACGGCATCTATTCCAGCTTTACTGTGCAAC
TTGGGGGTCACTCCCATTGATGGAGCTCCCCACCGATCATACAGTGAGTGCTACCCTGTC
CTGCTGGACGGTGTCATGGTTGGCTGGGTGGATAAGGATCTTGCTCCAGGCATCGCAGAT
TCTCTTCGTCATTTTAAGGTGTTGAGAGAGAAAAGAATTCCTCCCTGGATGGAAGTGGTC
CTTATACCCATGACAGGAAAACCAAGTCTGTACCCAGGATTGTTCCTTTTTACCACTCCT
TGTAGACTGGTACGGCCTGTGCAGAACTTAGCATTGGGCAAAGAAGAGCTAATTGGAACT
ATGGAACAGATCTTCATGAATGTCGCTATCTTTGAGGATGAAGTTTTTGCTGGAGTTACC
ACACACCAGGAACTCTTTCCACACAGCCTGCTGAGTGTGATTGCCAACTTCATCCCTTTC
TCTGATCACAACCAGAGTCCACGGAACATGTACCAATGCCAGATGGGTAAGCAAACTATG
GGCTTTCCACTTCTCACTTATCAAGACCGATCGGATAACAAACTGTATCGTCTTCAGACT
CCTCAGAGTCCCTTGGTGAGACCCTCCATGTATGATTATTATGACATGGATAACTATCCA
ATTGGGACCAATGCCATCGTTGCTGTGATTTCTTACACTGGCTATGATATGGAAGATGCC
ATGATTGTGAATAAGGCCTCTTGGGAACGAGGCTTTGCCCATGGAAGTGTCTACAAGTCT
GAGTTCATAGACCTCTCTGAAAAAATTAAACAAGGAGATAGTAGCCTGGTGTTTGGCATC
AAACCTGGTGACCCACGCGTTCTGCAGAAGTTAGATGACGATGGATTGCCGTTTATAGGA
GCAAAACTGCAGTACGGAGATCCGTATTACAGCTACCTCAACCTCAACACCGGGGAAAGT
TTTGTGATGTACTATAAGAGTAAAGAAAATTGTGTTGTGGATAACATCAAAGTGTGCAGT
AATGACACTGGGAGTGGAAAATTCAAGTGTGTTCGCATCACTATGAGAGTGCCTCGGAAC
CCAACTATCGGAGATAAATTTGCCAGTCGCCATGGGCGGAAGGGCATTTTAAGCAGATTG
TGGCCGGCTGAGGACATGCCTTTTACTGAGAGTGGGATGGTCCCAGACATTCTGTTCAAT
CCCCATGGTTTTCCATCCCGCATGACCATTGGGATGTTAATTGAGAGTATGGCCGGGAAG
TCTGCAGCTTTGCATGGTCTCTGCCATGATGCTACACCCTTCATCTTCTCAGAGGAGAAC
TCGGCCTTAGAATACTTTGGTGAGATGTTAAAGGCTGCTGGCTACAATTTCTATGGCACC
GAGAGGTTATATAGTGGCATCAGTGGGCTAGAACTGGAAGCAGACATCTTCATAGGAGTG
GTTTATTATCAGCGCTTACGCCATATGGTCTCAGACAAATTTCAAGTAAGGACAACTGGA
GCCCGAGACAGAGTCACCAACCAGCCTATTGGGGGAAGAAATGTCCAGGGTGGAATCCGT
TTTGGGGAGATGGAACGGGATGCGCTTTTAGCTCATGGTACATCTTTTCTCCTTCATGAC
CGCCTCTTCAACTGCTCAGATCGGTCGGTAGCCCATGTGTGTGTGAAGTGTGGCAGTTTA
CTCTCTCCACTGTTGGAGAAGCCACCCCCTTCTTGGTCTGCCATGCGCAACAGAAAATAC
AACTGTACTCTGTGTAGTCGCAGTGACACTATCGATACTGTTTCTGTGCCTTATGTTTTT
CGGTATTTTGTAGCTGAACTGGCAGCTATGAACATCAAAGTGAAACTGGATGTTGTTTAA
|
| Enzyme 13 GenBank Gene ID |
AK022533  |
| Enzyme 13 GeneCard ID |
POLR1B  |
| Enzyme 13 GenAtlas ID |
POLR1B  |
| Enzyme 13 HGNC ID |
HGNC:20454  |
| Enzyme 13 Chromosome Location |
2 |
| Enzyme 13 Locus |
2q13 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
Not Available |
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
6027 |
| Enzyme 14 Name |
DNA-directed RNA polymerase III subunit 127.6 kDa polypeptide |
| Enzyme 14 Synonyms |
- RNA polymerase III subunit 2
- RPC2
|
| Enzyme 14 Gene Name |
POLR3B |
| Enzyme 14 Protein Sequence |
>DNA-directed RNA polymerase III subunit 127.6 kDa polypeptide
MDVLAEEFGNLTPEQLAAPIPTVEEKWRLLPAFLKVKGLVKQHIDSFNYFINVEIKKIMK
ANEKVTSDADPMWYLKYLNIYVGLPDVEESFNVTRPVSPHECRLRDMTYSAPITVDIEYT
RGSQRIIRNALPIGRMPIMLRSSNCVLTGKTPAEFAKLNECPLDPGGYFIVKGVEKVILI
QEQLSKNRIIVEADRKGAVGASVTSSTHEKKSRTNMAVKQGRFYLRHNTLSEDIPIVIIF
KAMGVESDQEIVQMIGTEEHVMAAFGPSLEECQKAQIFTQMQALKYIGNKVRRQRMWGGG
PKKTKIEEARELLASTILTHVPVKEFNFRAKCIYTAVMVRRVILAQGDNKVDDRDYYGNK
RLELAGQLLSLLFEDLFKKFNSEMKKIADQVIPKQRAAQFDVVKHMRQDQITNGMVNAIS
TGNWSLKRFKMDRQGVTQVLSRLSYISALGMMTRISSQFEKTRKVSGPRSLQPSQWGMLC
PSDTPEGEACGLVKNLALMTHITTDMEDGPIVKLASNLGVEDVNLLCGEELSYPNVFLVF
LNGNILGVIRDHKKLVNTFRLMRRAGYINEFVSISTNLTDRCVYISSDGGRLCRPYIIVK
KQKPAVTNKHMEELAQGYRNFEDFLHESLVEYLDVNEENDCNIALYEHTINKDTTHLEIE
PFTLLGVCAGLIPYPHHNQSPRNTYQCAMGKQAMGTIGYNQRNRIDTLMYLLAYPQKPMV
KTKTIELIEFEKLPAGQNATVAVMSYSGYDIEDALVLNKASLDRGFGRCLVYKNAKCTLK
RYTNQTFDKVMGPMLDAATRKPIWRHEILDADGICSPGEKVENKQVLVNKSMPTVTQIPL
EGSNVPQQPQYKDVPITYKGATDSYIEKVMISSNAEDAFLIKMLLRQTRRPEIGDKFSSR
HGQKGVCGLIVPQEDMPFCDSGICPDIIMNPHGFPSRMTVGKLIELLAGKAGVLDGRFHY
GTAFGGSKVKDVCEDLVRHGYNYLGKDYVTSGITGEPLEAYIYFGPVYYQKLKHMVLDKM
HARARGPRAVLTRQPTEGRSRDGGLRLGEMERDCLIGYGASMLLLERLMISSDAFEVDVC
GQCGLLGYSGWCHYCKSSCHVSSLRIPYACKLLFQELQSMNIIPRLKLSKYNE
|
| Enzyme 14 Number of Residues |
1133 |
| Enzyme 14 Molecular Weight |
127787 |
| Enzyme 14 Theoretical pI |
8.64 |
| Enzyme 14 GO Classification |
| Function |
- DNA binding
- DNA-directed RNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- transcription
|
| Component |
| — |
|
| Enzyme 14 General Function |
Transcription |
| Enzyme 14 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
24429617  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q9NW08  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
RPC2_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>3402 bp
ATGGACGTGCTAGCGGAGGAGTTTGGGAACCTGACTCCGGAGCAGCTGGCGGCGCCGATC
CCGACTGTAGAGGAAAAATGGAGGCTGCTTCCAGCATTTTTAAAGGTGAAAGGCCTTGTG
AAACAGCATATAGATTCATTTAACTATTTCATTAATGTAGAGATAAAGAAGATAATGAAA
GCCAATGAAAAGGTTACAAGTGACGCTGACCCTATGTGGTACTTAAAATATCTTAATATC
TATGTTGGGCTTCCTGATGTTGAAGAAAGCTTCAATGTAACTAGACCAGTGTCCCCTCAT
GAGTGCCGTTTGAGAGACATGACATACTCTGCCCCTATTACAGTGGATATTGAATATACC
CGAGGCAGCCAGAGGATCATCCGCAATGCCTTACCTATCGGCAGAATGCCCATAATGCTA
CGTAGTTCAAACTGTGTTCTTACAGGAAAAACGCCAGCAGAATTTGCCAAACTGAACGAA
TGTCCCTTAGATCCAGGTGGCTACTTCATTGTTAAAGGAGTAGAAAAAGTTATTCTTATC
CAAGAGCAGCTGTCTAAGAACAGGATCATCGTGGAGGCTGATAGAAAAGGGGCTGTTGGA
GCTTCAGTTACCAGCTCTACCCATGAGAAAAAAAGCAGAACCAATATGGCTGTGAAACAA
GGACGATTTTATTTGAGGCATAATACTTTGTCAGAAGATATACCCATTGTCATCATATTT
AAGGCCATGGGTGTTGAGAGTGACCAGGAAATTGTGCAGATGATTGGAACAGCGGAGCAC
GTGATGGCTGCATTTGGGCCCAGTCTGGAAGAGTGCCAGAAAGCTCAGATTTTCACACAG
ATGCAGGCATTAAAATATATAGGGAACAAAGTAAGAAGGCAAAGGATGTGGGGAGGTGGA
CCAAAGAAAACCAAAATAGAAGAAGCAAGAGAGCTCCTGGCTTCCACCATTCTGACCCAT
GTCCCAGTTAAGGAATTCAATTTCCGAGCCAAATGTATCTATACTGCAGTGATGGTGCGA
AGAGTTATTCTGGCCCAAGGAGATAATAAAGTTGACGACAGAGATTATTATGGTAACAAG
CGACTGGAATTGGCAGGACAGCTTTTATCTCTTCTTTTTGAAGACTTGTTCAAAAAATTT
AATTCTGAAATGAAAAAGATTGCCGACCAGGTGATTCCTAAGCAAAGAGCAGCCCAGTTT
GATGTTGTCAAACACATGCGCCAAGACCAGATCACCAATGGCATGGTGAATGCTATTTCT
ACCGGAAATTGGTCTTTAAAGAGATTTAAAATGGACCGCCAGGGTGTAACCCAAGTGCTG
TCTCGCTTGTCATATATATCCGCACTGGGCATGATGACAAGAATCTCTTCCCAGTTTGAA
AAAACGAGAAAAGTGAGTGGTCCTCGCTCCCTCCAGCCATCTCAGTGGGGAATGCTGTGT
CCTTCGGACACTCCTGAAGGAGAGGCATGTGGTTTGGTTAAAAACTTGGCCCTTATGACA
CACATCACAACTGATATGGAAGATGGACCCATTGTTAAATTAGCCAGTAACTTGGGAGTA
GAAGATGTGAATTTATTATGTGGGGAAGAGCTCTCTTACCCAAATGTGTTTCTTGTCTTT
CTTAATGGTAACATCTTAGGTGTCATTCGAGACCACAAAAAGCTAGTGAATACATTTCGA
CTCATGAGAAGAGCAGGATATATCAATGAATTTGTTTCCATCTCAACAAATCTTACAGAT
CGATGTGTCTATATTTCTTCTGATGGGGGAAGGCTATGCAGACCCTACATAATTGTCAAG
AAACAGAAGCCAGCAGTCACAAATAAACATATGGAAGAGCTGGCCCAAGGGTACAGGAAT
TTTGAAGATTTCTTACATGAGAGTCTGGTTGAATATTTAGATGTGAATGAAGAAAATGAT
TGTAACATTGCACTGTACGAACACACAATTAATAAAGACACCACCCACTTGGAGATTGAA
CCCTTCACTCTTCTCGGCGTGTGTGCTGGACTTATCCCATACCCTCACCATAACCAGTCA
CCGAGAAACACTTATCAGTGTGCCATGGGGAAACAAGCCATGGGTACTATAGGATACAAC
CAGCGAAACAGAATTGATACTCTCATGTATCTACTAGCATATCCACAAAAACCCATGGTT
AAGACAAAAACCATTGAATTGATAGAATTTGAGAAACTGCCAGCTGGACAGAATGCAACA
GTTGCTGTGATGAGCTATAGTGGCTATGATATTGAAGATGCTCTTGTTTTAAACAAGGCC
TCTTTAGACAGAGGCTTTGGGCGTTGCCTTGTATATAAAAATGCTAAATGTACGTTGAAA
CGATACACCAATCAGACTTTTGATAAAGTGATGGGGCCCATGTTGGATGCTGCTACAAGG
AAACCTATCTGGCGACATGAAATCTTAGATGCAGATGGTATTTGTTCTCCAGGTGAGAAA
GTAGAAAACAAACAAGTGCTTGTAAATAAGTCCATGCCCACAGTGACTCAGATTCCTTTG
GAAGGAAGTAATGTACCACAGCAACCACAGTACAAAGATGTACCCATAACCTACAAAGGA
GCAACAGACTCATATATTGAAAAAGTGATGATATCTTCAAATGCTGAAGATGCTTTTCTG
ATCAAAATGCTGCTGAGACAGACAAGGCGTCCAGAAATTGGAGACAAATTCAGCAGTCGT
CATGGGCAAAAAGGTGTTTGTGGCTTGATCGTCCCCCAGGAAGACATGCCATTTTGTGAT
TCTGGCATCTGTCCGGACATCATCATGAACCCACACGGCTTCCCATCACGAATGACGGTG
GGGAAGCTCATTGAGCTGCTGGCTGGCAAGGCCGGTGTGCTGGACGGCAGATTCCACTAC
GGCACTGCGTTTGGAGGCAGTAAAGTGAAGGATGTGTGTGAGGACCTCGTTCGCCATGGT
TATAACTACTTGGGGAAAGACTATGTTACATCCGGCATCACAGGTGAGCCCTTAGAAGCA
TACATCTATTTTGGCCCCGTGTACTATCAGAAGCTGAAACACATGGTGCTAGATAAAATG
CATGCCCGGGCCCGGGGCCCACGAGCCGTCCTTACCAGGCAACCCACTGAAGGACGGTCT
CGTGATGGTGGCTTGCGTCTCGGGGAAATGGAACGTGACTGTTTAATCGGTTATGGAGCC
AGTATGCTTTTGCTAGAGAGACTAATGATTTCAAGTGATGCCTTTGAGGTTGATGTCTGT
GGGCAGTGTGGACTTCTGGGGTATTCTGGCTGGTGCCATTACTGCAAGTCATCCTGCCAC
GTGTCTTCCCTCCGTATTCCGTATGCCTGCAAGCTGCTCTTCCAGGAACTACAGTCTATG
AACATCATCCCCAGGTTAAAACTGTCCAAGTACAATGAATGA
|
| Enzyme 14 GenBank Gene ID |
AY092084  |
| Enzyme 14 GeneCard ID |
POLR3B  |
| Enzyme 14 GenAtlas ID |
POLR3B  |
| Enzyme 14 HGNC ID |
HGNC:30348  |
| Enzyme 14 Chromosome Location |
12 |
| Enzyme 14 Locus |
12q23.3 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N: Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits. Mol Cell Biol. 2002 Nov;22(22):8044-55. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
6238 |
| Enzyme 15 Name |
DNA polymerase beta |
| Enzyme 15 Synonyms |
Not Available |
| Enzyme 15 Gene Name |
POLB |
| Enzyme 15 Protein Sequence |
>DNA polymerase beta
MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAK
KLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIK
TLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGS
FRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQ
LPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRP
LGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE
|
| Enzyme 15 Number of Residues |
335 |
| Enzyme 15 Molecular Weight |
38178 |
| Enzyme 15 Theoretical pI |
9.41 |
| Enzyme 15 GO Classification |
| Function |
- DNA binding
- DNA-directed DNA polymerase activity
- beta DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA repair
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
|
|
| Enzyme 15 General Function |
Replication, recombination and repair |
| Enzyme 15 Specific Function |
Repair polymerase. Conducts "gap-filling" DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. Has a 5'-deoxyribose-5- phosphate lyase (dRP lyase) activity |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 15 Pfam Domain Function |
Not Available |
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
292397  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P06746  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
DPOLB_HUMAN  |
| Enzyme 15 PDB ID |
8ICK  |
| Enzyme 15 PDB File |
Show |
| Enzyme 15 3D Structure |
|
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1008 bp
ATGAGCAAACGGAAGGCGCCGCAGGAGACTCTCAACGGGGGAATCACCGACATGCTCACA
GAACTCGCAAACTTTGAGAAGAACGTGAGCCAAGCTATCCACAAGTACAATGCTTACAGA
AAAGCAGCATCTGTTATAGCAAAATACCCACACAAAATAAAGAGTGGAGCTGAAGCTAAG
AAATTGCCTGGAGTAGGAACAAAAATTGCTGAAAAGATTGATGAGTTTTTAGCAACTGGA
AAATTACGTAAACTGGAAAAGATTCGGCAGGATGATACGAGTTCATCCATCAATTTCCTG
ACTCGAGTTAGTGGCATTGGTCCATCTGCTGCAAGGAAGTTTGTAGATGAAGGAATTAAA
ACACTAGAAGATCTCAGAAAAAATGAAGATAAATTGAACCATCATCAGCGAATTGGGCTG
AAATATTTTGGGGACTTTGAAAAAAGAATTCCTCGTGAAGAGATGTTACAAATGCAAGAT
ATTGTACTAAATGAAGTTAAAAAAGTGGATTCTGAATACATTGCTACAGTCTGTGGCAGT
TTCAGAAGAGGTGCAGAGTCCAGTGGTGACATGGATGTTCTCCTGACCCATCCCAGCTTC
ACTTCAGAATCAACCAAACAGCCAAAACTGTTACATCAGGTTGTGGAGCAGTTACAAAAG
GTTCATTTTATCACAGATACCCTGTCAAAGGGTGAGACAAAGTTCATGGGTGTTTGCCAG
CTTCCCAGTAAAAATGATGAAAAAGAATATCCACACAGAAGAATTGATATCAGGTTGATA
CCCAAAGATCAGTATTACTGTGGTGTTCTCTATTTCACTGGGAGTGATATTTTCAATAAG
AATATGAGGGCTCATGCCCTAGAAAAGGGTTTCACAATCAATGAGTACACCATCCGTCCC
TTGGGAGTCACTGGAGTTGCAGGAGAACCCCTGCCAGTGGATAGTGAAAAAGACATCTTT
GATTACATCCAGTGGAAATACCGGGAACCCAAGGACCGGAGCGAATGA
|
| Enzyme 15 GenBank Gene ID |
L11607  |
| Enzyme 15 GeneCard ID |
POLB  |
| Enzyme 15 GenAtlas ID |
POLB  |
| Enzyme 15 HGNC ID |
HGNC:9174  |
| Enzyme 15 Chromosome Location |
8 |
| Enzyme 15 Locus |
8p11.2 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Chyan YJ, Ackerman S, Shepherd NS, McBride OW, Widen SG, Wilson SH, Wood TG: The human DNA polymerase beta gene structure. Evidence of alternative splicing in gene expression. Nucleic Acids Res. 1994 Jul 25;22(14):2719-25. [PubMed
]
- SenGupta DN, Zmudzka BZ, Kumar P, Cobianchi F, Skowronski J, Wilson SH: Sequence of human DNA polymerase beta mRNA obtained through cDNA cloning. Biochem Biophys Res Commun. 1986 Apr 14;136(1):341-7. [PubMed
]
- Abbotts J, SenGupta DN, Zmudzka B, Widen SG, Notario V, Wilson SH: Expression of human DNA polymerase beta in Escherichia coli and characterization of the recombinant enzyme. Biochemistry. 1988 Feb 9;27(3):901-9. [PubMed
]
- Widen SG, Kedar P, Wilson SH: Human beta-polymerase gene. Structure of the 5'-flanking region and active promoter. J Biol Chem. 1988 Nov 15;263(32):16992-8. [PubMed
]
- Matsumoto Y, Kim K, Katz DS, Feng JA: Catalytic center of DNA polymerase beta for excision of deoxyribose phosphate groups. Biochemistry. 1998 May 5;37(18):6456-64. [PubMed
]
- DeMott MS, Beyret E, Wong D, Bales BC, Hwang JT, Greenberg MM, Demple B: Covalent trapping of human DNA polymerase beta by the oxidative DNA lesion 2-deoxyribonolactone. J Biol Chem. 2002 Mar 8;277(10):7637-40. Epub 2002 Jan 22. [PubMed
]
- Pelletier H, Sawaya MR, Wolfle W, Wilson SH, Kraut J: A structural basis for metal ion mutagenicity and nucleotide selectivity in human DNA polymerase beta. Biochemistry. 1996 Oct 1;35(39):12762-77. [PubMed
]
- Pelletier H, Sawaya MR: Characterization of the metal ion binding helix-hairpin-helix motifs in human DNA polymerase beta by X-ray structural analysis. Biochemistry. 1996 Oct 1;35(39):12778-87. [PubMed
]
- Sawaya MR, Prasad R, Wilson SH, Kraut J, Pelletier H: Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: evidence for an induced fit mechanism. Biochemistry. 1997 Sep 16;36(37):11205-15. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
6239 |
| Enzyme 16 Name |
DNA polymerase alpha catalytic subunit |
| Enzyme 16 Synonyms |
Not Available |
| Enzyme 16 Gene Name |
POLA1 |
| Enzyme 16 Protein Sequence |
>DNA polymerase alpha catalytic subunit
MAPVHGDDSLSDSGSFVSSRARREKKSKKGRQEALERLKKAKAGEKYKYEVEDFTGVYEE
VDEEQYSKLVQARQDDDWIVDDDGIGYVEDGREIFDDDLEDDALDADEKGKDGKARNKDK
RNVKKLAVTKPNNIKSMFIACAGKKTADKAVDLSKDGLLGDILQDLNTETPQITPPPVMI
LKKKRSIGASPNPFSVHTATAVPSGKIASPVSRKEPPLTPVPLKRAEFAGDDVQVESTEE
EQESGAMEFEDGDFDEPMEVEEVDLEPMAAKAWDKESEPAEEVKQEADSGKGTVSYLGSF
LPDVSCWDIDQEGDSSFSVQEVQVDSSHLPLVKGADEEQVFHFYWLDAYEDQYNQPGVVF
LFGKVWIESAETHVSCCVMVKNIERTLYFLPREMKIDLNTGKETGTPISMKDVYEEFDEK
IATKYKIMKFKSKPVEKNYAFEIPDVPEKSEYLEVKYSAEMPQLPQDLKGETFSHVFGTN
TSSLELFLMNRKIKGPCWLEVKSPQLLNQPVSWCKVEAMALKPDLVNVIKDVSPPPLVVM
AFSMKTMQNAKNHQNEIIAMAALVHHSFALDKAAPKPPFQSHFCVVSKPKDCIFPYAFKE
VIEKKNVKVEVAATERTLLGFFLAKVHKIDPDIIVGHNIYGFELEVLLQRINVCKAPHWS
KIGRLKRSNMPKLGGRSGFGERNATCGRMICDVEISAKELIRCKSYHLSELVQQILKTER
VVIPMENIQNMYSESSQLLYLLEHTWKDAKFILQIMCELNVLPLALQITNIAGNIMSRTL
MGGRSERNEFLLLHAFYENNYIVPDKQIFRKPQQKLGDEDEEIDGDTNKYKKGRKKAAYA
GGLVLDPKVGFYDKFILLLDFNSLYPSIIQEFNICFTTVQRVASEAQKVTEDGEQEQIPE
LPDPSLEMGILPREIRKLVERRKQVKQLMKQQDLNPDLILQYDIRQKALKLTANSMYGCL
GFSYSRFYAKPLAALVTYKGREILMHTKEMVQKMNLEVIYGDTDSIMINTNSTNLEEVFK
LGNKVKSEVNKLYKLLEIDIDGVFKSLLLLKKKKYAALVVEPTSDGNYVTKQELKGLDIV
RRDWCDLAKDTGNFVIGQILSDQSRDTIVENIQKRLIEIGENVLNGSVPVSQFEINKALT
KDPQDYPDKKSLPHVHVALWINSQGGRKVKAGDTVSYVICQDGSNLTASQRAYAPEQLQK
QDNLTIDTQYYLAQQIHPVVARICEPIDGIDAVLIATWLGLDPTQFRVHHYHKDEENDAL
LGGPAQLTDEEKYRDCERFKCPCPTCGTENIYDNVFDGSGTDMEPSLYRCSNIDCKASPL
TFTVQLSNKLIMDIRRFIKKYYDGWLICEEPTCRNRTRHLPLQFSRTGPLCPACMKATLQ
PEYSDKSLYTQLCFYRYIFDAECALEKLTTDHEKDKLKKQFFTPKVLQDYRKLKNTAEQF
LSRSGYSEVNLSKLFAGCAVKS
|
| Enzyme 16 Number of Residues |
1462 |
| Enzyme 16 Molecular Weight |
165914 |
| Enzyme 16 Theoretical pI |
5.59 |
| Enzyme 16 GO Classification |
| Function |
- 3'-5' exonuclease activity
- DNA binding
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- exonuclease activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- nuclease activity
- nucleic acid binding
- nucleotide binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 16 General Function |
Replication, recombination and repair |
| Enzyme 16 Specific Function |
Polymerase alpha in a complex with DNA primase is a replicative polymerase |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
35568  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P09884  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
DPOLA_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>4389 bp
ATGGCACCTGTGCACGGCGACGACTCTCTGTCAGATTCAGGGAGTTTTGTATCTTCTCGA
GCCCGGCGAGAAAAAAAATCAAAGAAGGGGCGCCAAGAAGCCCTAGAAAGACTGAAAAAG
GCTAAAGCTGGTGAGAAGTATAAATATGAAGTCGAGGACTTCACAGGTGTTTATGAAGAA
GTTGATGAAGAACAGTATTCGAAGCTGGTTCAGGCACGCCAGGATGATGACTGGATTGTG
GATGATGATGGTATTGGCTATGTGGAAGATGGCCGAGAGATTTTTGATGATGACCTTGAA
GATGATGCCCTTGATGCTGATGAGAAAGGAAAAGATGGTAAAGCACGCAATAAAGACAAG
AGGAATGTAAAGAAGCTCGCAGTGACAAAACCGAACAACATTAAGTCAATGTTCATTGCT
TGTGCTGGAAAGAAAACTGCAGATAAAGCTGTAGACTTGTCCAAGGATGGTCTGCTAGGT
GACATTCTACAGGATCTTAACACTGAGACACCTCAAATAACTCCACCACCTGTAATGATA
CTGAAGAAGAAAAGATCCATTGGAGCTTCACCGAATCCTTTCTCTGTGCACACCGCCACG
GCAGTTCCTTCAGGAAAAATTGCTTCCCCTGTCTCCAGAAAGGAGCCTCCATTAACTCCT
GTTCCTCTTAAACGTGCTGAATTTGCTGGCGATGATGTACAGGTCGAGAGTACAGAAGAA
GAGCAGGAGTCAGGGGCAATGGAGTTTGAAGATGGTGACTTTGATGAGCCCATGGAAGTT
GAAGAGGTGGACCTGGAGCCTATGGCTGCCAAGGCTTGGGACAAAGAGAGTGAGCCAGCA
GAGGAAGTGAAACAAGAGGCGGATTCTGGGAAAGGGACCGTGTCCTACTTAGGAAGTTTT
CTCCCGGATGTCTCTTGTTGGGACATTGATCAAGAAGGTGATAGCAGTTTCTCAGTGCAA
GAAGTTCAAGTGGATTCCAGTCACCTCCCATTGGTAAAAGGGGCAGATGAGGAACAAGTA
TTCCACTTTTATTGGTTGGATGCTTATGAGGATCAGTACAACCAACCAGGTGTGGTATTT
CTGTTTGGGAAAGTTTGGATTGAATCAGCCGAGACCCATGTGAGCTGTTGTGTCATGGTG
AAAAATATCGAGCGAACGCTTTACTTCCTTCCCCGTGAAATGAAAATTGATCTAAATACG
GGGAAAGAAACAGGAACTCCAATTTCAATGAAGGATGTTTATGAGGAATTTGATGAGAAA
ATAGCAACAAAATATAAAATTATGAAGTTCAAGTCTAAGCCAGTGGAAAAGAACTATGCT
TTTGAGATACCTGATGTTCCAGAAAAATCTGAGTACTTGGAAGTTAAATACTCGGCTGAA
ATGCCACAGCTTCCTCAAGATTTGAAAGGAGAAACTTTTTCTCATGTATTTGGGACCAAC
ACATCTAGCCTGGAACTGTTCTTGATGAACAGAAAGATCAAAGGACCTTGTTGGCTTGAA
GTAAAAAAGTCCACAGCTCTTAATCAGCCAGTCAGTTGGTGTAAAGTTGAGGCAATGGCT
TTGAAACCAGACCTGGTGAATGTAATTAAGGATGTCAGTCCACCACCGCTTGTCGTGATG
GCTTTCAGCATGAAGACAATGCAGAATGCAAAGAACCATCAAAATGAGATTATTGCTATG
GCAGCTTTGGTCCATCACAGTTTTGCATTGGATAAAGCAGCCCCAAAGCCTCCCTTTCAG
TCACACTTCTGTGTTGTGTCTAAACCAAAGGACTGTATTTTTCCATATGCTTTCAAAGAA
GTCATTGAGAAAAAGAATGTGAAGGTTGAGGTTGCTGCAACAGAAAGAACACTGCTAGGT
TTTTTCCTTGCAAAAGTTCACAAAATTGATCCTGATATCATTGTGGGTCATAATATTTAT
GGGTTTGAACTGGAAGTACTACTGCAGAGAATTAATGTGTGCAAAGCTCCTCACTGGTCC
AAGATAGGTCGACTGAAGCGATCCAACATGCCAAAGCTTGGGGGCCGGAGTGGATTTGGT
GAAAGAAATGCTACCTGTGGTCGAATGATCTGTGATGTGGAAATTTCAGCAAAGGAATTG
ATTCGTTGTAAAAGCTACCATCTGTCTGAACTTGTTCAGCAGATTCTAAAAACTGAAAGG
GTTGTAATCCCAATGGAAAATATACAAAATATGTACAGTGAATCTTCTCAACTGTTATAC
CTGTTGGAACACACCTGGAAAGATGCCAAGTTCATTTTGCAGATCATGTGTGAGCTAAAT
GTTCTTCCATTAGCATTGCAGATCACTAACATCGCTGGGAACATTATGTCCAGGACGCTG
ATGGGTGGACGATCCGAGCGTAACGAGTTCTTGTTGCTTCATGCATTTTACGAAAACAAC
TATATTGTGCCTGACAAGCAGATTTTCAGAAAGCCTCAGCAAAAACTGGGAGATGAAGAT
GAAGAAATTGATGGAGATACCAATAAATACAAGAAAGGACGTAAGAAAGGAGCTTATGCT
GGAGGCTTGGTTTTGGACCCCAAAGTTGGTTTTTATGATAAGTTCATTTTGCTTCTGGAC
TTCAACAGTCTATATCCTTCCATCATTCAGGAATTTAACATTTGTTTTACAACAGTACAA
AGAGTTGCTTCAGAGGCACAGAAAGTTACAGAGGATGGAGAACAAGAACAGATCCCTGAG
TTGCCAGATCCAAGCTTAGAAATGGGCATTTTGCCCAGAGAGATCCGGAAACTGGTAGAA
CGGAGAAAACAAGTCAAACAGCTAATGAAACAGCAAGACTTAAATCCAGACCTTATTCTT
CAGTATGACATTCGACAGAAGGCTTTGAAGCTCACAGCGAACAGTATGTATGGTTGCCTG
GGATTTTCCTATAGCAGATTTTACGCCAAACCACTGGCTGCCTTGGTGACATACAAAGGA
AGGGAGATTTTGATGCATACGAAAGAGATGGTACAAAAGATGAATCTTGAAGTTATTTAT
GGAGATACAGATTCAATTATGATAAACACCAATAGCACCAATCTGGAAGAAGTATTTAAG
TTGGGAAACAAGGTAAAAAGTGAAGTGAATAAGTTGTACAAACTGCTTGAAATAGACATT
GATGGGGTTTTCAAGTCTCTGCTACTGCTGAAAAAAAAGAAGTACGCTGCTCTGGTTGTT
GAGCCAACGTCGGATGGGAATTATGTCACCAAACAGGAGCTCAAAGGATTAGATATAGTT
AGAAGAGATTGGTGTGATCTTGCTAAAGACACTGGAAACTTTGTGATTGGCCAGATTCTT
TCTGATCAAAGCCGGGACACTATAGTGGAAAACATTCAGAAGAGGCTGATAGAAATTGGA
GAAAATGTGCTAAATGGCAGTGTCCCAGTGAGCCAGTTTGAAATTAACAAGGCATTGACA
AAGGATCCCCAGGATTACCCTGATAAAAAAAGCCTACCTCATGTACATGTTGCCCTCTGG
ATAAATTCTCAAGGAGGCAGAAAGGTGAAAGCTGGAGATACTGTGTCATATGTCATCTGT
CAGGATGGATCAAACCTCACTGCAAGTCAGAGGGCCTATGCGCCTGAGCAGCTGCAGAAA
CAGGATAATCTAACCATTGACACCCAGTACTACCTGGCCCAGCAGATCCACCCAGTCGTG
GCTCGGATCTGTGAACCAATAGACGGAATTGATGCTGTCCTCATTGCAACGTGGTTGGGA
CTTGACCCCACCCAATTTAGAGTTCATCATTATCATAAAGATGAAGAGAATGATGCTCTA
CTTGGTGGCCCAGCACAGCTCACTGATGAAGAGAAATACAGGGACTGTGAAAGATTCAAA
TGTCCATGCCCTACATGTGGAACTGAGAATATTTATGATAATGTCTTTGATGGTTCGGGA
ACAGATATGGAGCCCAGCTTGTATCGTTGCAGTAACATCGATTGTAAGGCTTCACCTCTG
ACCTTTACAGTACAACTGAGCAACAAATTGATCATGGACATTAGACGTTTCATTAAAAAG
TACTATGATGGCTGGTTGATATGTGAAGAGCCAACCTGTCGCAATCGAACTCGTCACCTT
CCCCTTCAATTCTCCCGAACTGGGCCTCTTTGCCCAGCCTGCATGAAAGCTACACTTCAA
CCAGAGTATTCTGACAAGTCCCTGTACACCCAGCTGTGCTTTTACCGGTACATTTTTGAT
GCGGAGTGTGCACTGGAGAAACTTACTACCGATCATGAGAAAGATAAATTGAAGAAGCAA
TTTTTTACCCCCAAAGTTCTGCAGGACTACAGAAAACTCAAGAACACAGCAGAGCAATTC
TTGTCCCGAAGTGGCTACTCCGAAGTGAATCTGAGCAAACTCTTCGCTGGTTGTGCCGTG
AAATCCTAA
|
| Enzyme 16 GenBank Gene ID |
X06745  |
| Enzyme 16 GeneCard ID |
POLA1  |
| Enzyme 16 GenAtlas ID |
POLA1  |
| Enzyme 16 HGNC ID |
HGNC:9173  |
| Enzyme 16 Chromosome Location |
X |
| Enzyme 16 Locus |
Xp22.1-p21.3 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Wong SW, Wahl AF, Yuan PM, Arai N, Pearson BE, Arai K, Korn D, Hunkapiller MW, Wang TS: Human DNA polymerase alpha gene expression is cell proliferation dependent and its primary structure is similar to both prokaryotic and eukaryotic replicative DNA polymerases. EMBO J. 1988 Jan;7(1):37-47. [PubMed
]
- Pearson BE, Nasheuer HP, Wang TS: Human DNA polymerase alpha gene: sequences controlling expression in cycling and serum-stimulated cells. Mol Cell Biol. 1991 Apr;11(4):2081-95. [PubMed
]
- Hsi KL, Copeland WC, Wang TS: Human DNA polymerase alpha catalytic polypeptide binds ConA and RCA and contains a specific labile site in the N-terminus. Nucleic Acids Res. 1990 Nov 11;18(21):6231-7. [PubMed
]
- Evanics F, Maurmann L, Yang WW, Bose RN: Nuclear magnetic resonance structures of the zinc finger domain of human DNA polymerase-alpha. Biochim Biophys Acta. 2003 Sep 23;1651(1-2):163-71. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
6240 |
| Enzyme 17 Name |
DNA polymerase subunit delta 3 |
| Enzyme 17 Synonyms |
- DNA polymerase subunit delta p66
|
| Enzyme 17 Gene Name |
POLD3 |
| Enzyme 17 Protein Sequence |
>DNA polymerase subunit delta 3
MADQLYLENIDEFVTDQNKIVTYKWLSYTLGVHVNQAKQMLYDYVERKRKENSGAQLHVT
YLVSGSLIQNGHSCHKVAVVREDKLEAVKSKLAVTASIHVYSIQKAMLKDSGPLFNTDYD
ILKSNLQNCSKFSAIQCAAAVPRAPAESSSSSKKFEQSHLHMSSETQANNELTTNGHGPP
ASKQVSQQPKGIMGMFASKAAAKTQETNKETKTEAKEVTNASAAGNKAPGKGNMMSNFFG
KAAMNKFKVNLDSEQAVKEEKIVEQPTVSVTEPKLATPAGLKKSSKKAEPVKVLQKEKKR
GKRVALSDDETKETENMRKKRRRIKLPESDSSEDEVFPDSPGAYEAESPSPPPPPSPPLE
PVPKTEPEPPSVKSSSGENKRKRKRVLKSKTYLDGEGCIVTEKVYESESCTDSEEELNMK
TSSVHRPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK
|
| Enzyme 17 Number of Residues |
466 |
| Enzyme 17 Molecular Weight |
51401 |
| Enzyme 17 Theoretical pI |
9.96 |
| Enzyme 17 GO Classification |
Not Available |
| Enzyme 17 General Function |
Not Available |
| Enzyme 17 Specific Function |
The function of subunit 3 is not clear |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
Not Available |
| Enzyme 17 Pfam Domain Function |
Not Available |
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
436222  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q15054  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
DPOD3_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>1476 bp
AGACGTTTCCCGCCGGCGGGAGCTGTGGCTGTGATTGAGAGAGGGGTTAGAGGCGGGTCC
CAGCGCTGCCGCACCATGGCGGACCAGCTTTATCTGGAAAATATAGACGAGTTCGTCACG
GACCAAAACAAGATCGTGACATACAAATGGCTGAGCTATACACTAGGGGTTCATGTTAAC
CAGGCCAAACAGATGCTGTATGATTATGTTGAAAGGAAACGAAAAGAAAATTCAGGAGCC
CAACTGCATGTTACCTACTTGGTGTCTGGCAGTCTCATTCAGAATGGACATTCCTGCCAC
AAGGTTGCAGTAGTGAGAGAAGATAAATTGGAAGCAGTGAAGTCCAAGCTAGCTGTGACT
GCCAGCATCCATGTGTACAGCATCCAGAAAGCCATGCTAAAGGACAGTGGGCCTCTGTTC
AATACTGACTATGACATCCTTAAAAGCAACTTGCAGAACTGCAGCAAATTTAGTGCTATA
CAATGTGCAGCTGCCGTCCCTAGAGCTCCTGCTGAATCCTCTTCGTCTTCCAAAAAGTTT
GAGCAGTCACATCTTCACATGTCAAGTGAGACACAAGCCAACAATGAGCTGACCACCAAT
GGTCATGGCCCACCTGCATCCAAGCAGGTTTCCCAGCAGCCCAAAGGAATTATGGGAATG
TTTGCCTCCAAAGCTGCTGCTAAAACCCAAGAAACCAACAAGGAAACGAAAACAGAGGCT
AAAGAAGTAACAAATGCATCTGCAGCAGGCAACAAGGCACCAGGGAAAGGGAATATGATG
AGCAACTTTTTTGGAAAAGCTGCTATGAATAAATTTAAAGTCAATTTGGACTCAGAACAA
GCAGTGAAAGAAGAAAAAATAGTGGAGCAGCCTACAGTGTCTGTCACGGAACCAAAGCTG
GCAACTCCTGCAGGCCTGAAAAAATCCAGCAAAAAAGCAGAGCCTGTTAAGGTGCTGCAG
AAGGAAAAAAAAAGGGGGAAGCGAGTAGCATTATCTGATGATGAGACAAAGGAAACTGAA
AACATGAGGAAAAAGAGGAGAAGAATCAAACTTCCTGAATCTGATAGCAGTGAAGATGAA
GTCTTTCCAGACTCTCCTGGGGCTTATGAAGCTGAGTCACCATCCCCACCTCCTCCTCCG
TCTCCACCTCTTGAACCAGTGCCAAAGACTGAGCCTGAACCTCCTTCTGTCAAGAGCTCA
AGTGGAGAAAACAAAAGAAAACGAAAACGCGTACTAAAATCTAAAACTTACCTGGATGGG
GAAGGCTGCATAGTGACTGAAAAAGTCTACGAGAGTGAATCCTGCACAGATAGTGAAGAG
GAGCTTAACATGAAGACATCCTCAGTACACAGACCCCCTGCCATGACTGTGAAAAAAGAA
CCCAGAGAGGAACGAAAGGGCCCCAAGAAAGGGACTGCTGCTCTGGGCAAAGCCAACAGA
CAGGTGTCCATTACTGGCTTCTTCCAGAGGAAATAA
|
| Enzyme 17 GenBank Gene ID |
D26018  |
| Enzyme 17 GeneCard ID |
POLD3  |
| Enzyme 17 GenAtlas ID |
POLD3  |
| Enzyme 17 HGNC ID |
HGNC:20932  |
| Enzyme 17 Chromosome Location |
11 |
| Enzyme 17 Locus |
11q14 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed
]
- Hughes P, Tratner I, Ducoux M, Piard K, Baldacci G: Isolation and identification of the third subunit of mammalian DNA polymerase delta by PCNA-affinity chromatography of mouse FM3A cell extracts. Nucleic Acids Res. 1999 May 15;27(10):2108-14. [PubMed
]
- Mo J, Liu L, Leon A, Mazloum N, Lee MY: Evidence that DNA polymerase delta isolated by immunoaffinity chromatography exhibits high-molecular weight characteristics and is associated with the KIAA0039 protein and RPA. Biochemistry. 2000 Jun 20;39(24):7245-54. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
6243 |
| Enzyme 18 Name |
DNA polymerase lambda |
| Enzyme 18 Synonyms |
- Pol Lambda
- DNA polymerase kappa
- DNA polymerase beta-2
- Pol beta2
|
| Enzyme 18 Gene Name |
POLL |
| Enzyme 18 Protein Sequence |
>DNA polymerase lambda
MDPRGILKAFPKRQKIHADASSKVLAKIPRREEGEEAEEWLSSLRAHVVRTGIGRARAEL
FEKQIVQHGGQLCPAQGPGVTHIVVDEGMDYERALRLLRLPQLPPGAQLVKSAWLSLCLQ
ERRLVDVAGFSIFIPSRYLDHPQPSKAEQDASIPPGTHEALLQTALSPPPPPTRPVSPPQ
KAKEAPNTQAQPISDDEASDGEETQVSAADLEALISGHYPTSLEGDCEPSPAPAVLDKWV
CAQPSSQKATNHNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSFHKPVTSYQEAC
SIPGIGKRMAEKIIEILESGHLRKLDHISESVPVLELFSNIWGAGTKTAQMWYQQGFRSL
EDIRSQASLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGLLCVACGSYRR
GKATCGDVDVLITHPDGRSHRGIFSRLLDSLRQEGFLTDDLVSQEENGQQQKYLGVCRLP
GPGRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTAVVRNT
HGCKVGPGRVLPTPTEKDVFRLLGLPYREPAERDW
|
| Enzyme 18 Number of Residues |
575 |
| Enzyme 18 Molecular Weight |
63483 |
| Enzyme 18 Theoretical pI |
7.94 |
| Enzyme 18 GO Classification |
| Function |
- DNA binding
- DNA-directed DNA polymerase activity
- beta DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA repair
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
|
|
| Enzyme 18 General Function |
Replication, recombination and repair |
| Enzyme 18 Specific Function |
Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 18 Pfam Domain Function |
Not Available |
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
6687796  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q9UGP5  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
DPOLL_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>1728 bp
ATGGATCCCAGGGGTATCTTGAAGGCATTTCCCAAGCGGCAGAAAATTCATGCTGATGCA
TCATCAAAAGTACTTGCAAAGATTCCTAGGAGGGAAGAGGGAGAAGAAGCAGAAGAGTGG
CTGAGCTCCCTTCGGGCCCATGTTGTGCGCACTGGCATTGGACGAGCCCGGGCAGAACTC
TTTGAGAAGCAGATTGTTCAGCATGGCGGCCAGCTATGCCCTGCCCAGGGCCCAGGTGTC
ACTCACATTGTGGTGGATGAAGGCATGGACTATGAGCGAGCCCTCCGCCTTCTCAGACTA
CCCCAGCTGCCCCCGGGTGCTCAGCTGGTGAAGTCAGCCTGGCTGAGCTTGTGCCTTCAG
GAGAGGAGGCTGGTGGATGTAGCTGGATTCAGCATCTTCATCCCCAGTAGGTACTTGGAC
CATCCACAGCCCAGCAAGGCAGAGCAGGATGCTTCTATTCCTCCTGGCACCCATGAGGCC
CTGCTTCAGACAGCCCTTTCTCCTCCTCCTCCTCCCACCAGGCCTGTGTCTCCTCCCCAA
AAGGCAAAAGAGGCACCAAACACCCAAGCCCAGCCCATCTCTGATGATGAAGCCAGTGAT
GGGGAAGAAACCCAGGTTAGTGCAGCTGATCTGGAAGCCCTCATCAGTGGCCACTACCCC
ACCTCCCTTGAGGGAGATTGTGAGCCTAGCCCAGCCCCTGCTGTCCTGGATAAGTGGGTC
TGTGCACAGCCCTCAAGCCAGAAGGCGACCAATCACAACCTCCATATCACAGAGAAGCTG
GAAGTTCTGGCCAAAGCCTACAGTGTTCAGGGAGACAAGTGGAGGGCCCTGGGCTATGCC
AAGGCCATCAATGCCCTCAAGAGCTTCCATAAGCCTGTCACCTCGTACCAGGAGGCCTGC
AGTATCCCTGGGATTGGGAAGCGGATGGCTGAGAAAATCATAGAGATCCTGGAGAGCGGG
CATTTGCGGAAGCTGGACCATATCAGTGAGAGCGTGCCTGTCTTGGAGCTCTTCTCCAAC
ATCTGGGGAGCTGGGACCAAGACTGCCCAGATGTGGTACCAACAGGGCTTCCGAAGTCTG
GAAGACATCCGCAGCCAGGCCTCCCTGACAACCCAGCAGGCCATCGGCCTGAAGCATTAC
AGTGACTTCCTGGAACGTATGCCCAGGGAGGAGGCTACAGAGATTGAGCAGACAGTCCAG
AAAGCAGCCCAGGCCTTTAACTCTGGGCTGCTGTGTGTGGCATGTGGTTCATACCGACGG
GGAAAGGCGACCTGTGGTGATGTCGACGTGCTCATCACTCACCCAGATGGCCGGTCCCAC
CGGGGTATCTTCAGCCGCCTCCTTGACAGTCTTCGGCAGGAAGGGTTCCTCACAGATGAC
TTGGTGAGCCAAGAGGAGAATGGTCAGCAACAGAAGTACTTGGGGGTGTGCCGGCTCCCA
GGGCCAGGGCGGCGGCACCGGCGCCTGGACATCATCGTGGTGCCCTATAGCGAGTTTGCC
TGTGCCCTGCTCTACTTCACCGGCTCTGCACACTTCAACCGCTCCATGCGAGCCCTGGCC
AAAACCAAGGGCATGAGTCTGTCAGAACATGCCCTCAGCACTGCTGTGGTCCGGAACACC
CATGGCTGCAAGGTGGGGCCTGGCCGAGTGCTGCCCACTCCCACTGAGAAGGATGTCTTC
AGGCTCTTAGGCCTCCCCTACCGAGAACCTGCTGAGCGGGACTGGTGA
|
| Enzyme 18 GenBank Gene ID |
AJ131890  |
| Enzyme 18 GeneCard ID |
POLL  |
| Enzyme 18 GenAtlas ID |
POLL  |
| Enzyme 18 HGNC ID |
HGNC:9184  |
| Enzyme 18 Chromosome Location |
10 |
| Enzyme 18 Locus |
10q23 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Aoufouchi S, Flatter E, Dahan A, Faili A, Bertocci B, Storck S, Delbos F, Cocea L, Gupta N, Weill JC, Reynaud CA: Two novel human and mouse DNA polymerases of the polX family. Nucleic Acids Res. 2000 Sep 15;28(18):3684-93. [PubMed
]
- Nagasawa K, Kitamura K, Yasui A, Nimura Y, Ikeda K, Hirai M, Matsukage A, Nakanishi M: Identification and characterization of human DNA polymerase beta 2, a DNA polymerase beta -related enzyme. J Biol Chem. 2000 Oct 6;275(40):31233-8. [PubMed
]
- Garcia-Diaz M, Bebenek K, Kunkel TA, Blanco L: Identification of an intrinsic 5'-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair. J Biol Chem. 2001 Sep 14;276(37):34659-63. Epub 2001 Jul 16. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
6244 |
| Enzyme 19 Name |
DNA polymerase epsilon subunit 4 |
| Enzyme 19 Synonyms |
- DNA polymerase II subunit 4
- DNA polymerase epsilon subunit p12
|
| Enzyme 19 Gene Name |
POLE4 |
| Enzyme 19 Protein Sequence |
>DNA polymerase epsilon subunit 4
MAAAAAAGSGTPREEEGPAGEAAASQPQAPTSVPGARLSRLPLARVKALVKADPDVTLAG
QEAIFILARAAELFVETIAKDAYCCAQQGKRKTLQRRDLDNAIEAVDEFAFLEGTLD
|
| Enzyme 19 Number of Residues |
117 |
| Enzyme 19 Molecular Weight |
12209 |
| Enzyme 19 Theoretical pI |
4.55 |
| Enzyme 19 GO Classification |
| Function |
- DNA binding
- binding
- nucleic acid binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 19 General Function |
Not Available |
| Enzyme 19 Specific Function |
May play a role in allowing polymerase epsilon to carry out its replication and/or repair function |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
9623361  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9NR33  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
DPOE4_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>354 bp
ATGGCGGCGGCGGCGGCGGCAGGAAGCGGGACGCCCCGAGAGGAGGAGGTACCTGCTGGG
GAGGCAGCGGCCTCGCAGCCCCAGGCCCCAACGAGTGTGCCTGGGGCTCGTCTCTCGAGG
TTGCCTCTGGCGCGAGTGAAGGCCTTGGTGAAGGCAGATCCCGACGTGACGCTAGCGGGA
CAGGAAGCCATCTTCATTCTGGCACGAGCCGCGGAACTGTTTGTGGAGACCATTGCAAAA
GATGCCTACTGTTGCGCTCAGCAGGGAAAAAGGAAAACCCTTCAGAGGAGAGACTTGGAT
AATGCAATAGAAGCTGTGGATGAATTTGCTTTTCTGGAAGGTACTTTAGATTGA
|
| Enzyme 19 GenBank Gene ID |
AF261688  |
| Enzyme 19 GeneCard ID |
POLE4  |
| Enzyme 19 GenAtlas ID |
POLE4  |
| Enzyme 19 HGNC ID |
HGNC:18755  |
| Enzyme 19 Chromosome Location |
2 |
| Enzyme 19 Locus |
2p12 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Li Y, Pursell ZF, Linn S: Identification and cloning of two histone fold motif-containing subunits of HeLa DNA polymerase epsilon. J Biol Chem. 2000 Jul 28;275(30):23247-52. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
6245 |
| Enzyme 20 Name |
DNA polymerase eta |
| Enzyme 20 Synonyms |
- RAD30 homolog A
- Xeroderma pigmentosum variant type protein
|
| Enzyme 20 Gene Name |
POLH |
| Enzyme 20 Protein Sequence |
>DNA polymerase eta
MATGQDRVVALVDMDCFFVQVEQRQNPHLRNKPCAVVQYKSWKGGGIIAVSYEARAFGVT
RSMWADDAKKLCPDLLLAQVRESRGKANLTKYREASVEVMEIMSRFAVIERASIDEAYVD
LTSAVQERLQKLQGQPISADLLPSTYIEGLPQGPTTAEETVQKEGMRKQGLFQWLDSLQI
DNLTSPDLQLTVGAVIVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSH
GSVPQLFSQMPIRKIRSLGGKLGASVIEILGIEYMGELTQFTESQLQSHFGEKNGSWLYA
MCRGIEHDPVKPRQLPKTIGCSKNFPGKTALATREQVQWWLLQLAQELEERLTKDRNDND
RVATQLVVSIRVQGDKRLSSLRRCCALTRYDAHKMSHDAFTVIKNCNTSGIQTEWSPPLT
MLFLCATKFSASAPSSSTDITSFLSSDPSSLPKVPVTSSEAKTQGSGPAVTATKKATTSL
ESFFQKAAERQKVKEASLSSLTAPTQAPMSNSPSKPSLPFQTSQSTGTEPFFKQKSLLLK
QKQLNNSSVSSPQQNPWSNCKALPNSLPTEYPGCVPVCEGVSKLEESSKATPAEMDLAHN
SQSMHASSASKSVLEVTQKATPNPSLLAAEDQVPCEKCGSLVPVWDMPEHMDYHFALELQ
KSFLQPHSSNPQVVSAVSHQGKRNPKSPLACTNKRPRPEGMQTLESFFKPLTH
|
| Enzyme 20 Number of Residues |
713 |
| Enzyme 20 Molecular Weight |
78414 |
| Enzyme 20 Theoretical pI |
8.56 |
| Enzyme 20 GO Classification |
| Function |
| — |
| Process |
- DNA metabolism
- DNA repair
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 20 General Function |
Replication, recombination and repair |
| Enzyme 20 Specific Function |
DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Targets POLI to replication foci |
| Enzyme 20 Pathways |
|
| Enzyme 20 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
5138988  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q9Y253  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
POLH_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>2142 bp
ATGGCTACTGGACAGGATCGAGTGGTTGCTCTCGTGGACATGGACTGTTTTTTTGTTCAA
GTGGAGCAGCGGCAAAATCCTCATTTGAGGAATAAACCTTGTGCAGTTGTACAGTACAAA
TCATGGAAGGGTGGTGGAATAATTGCAGTGAGTTATGAAGCTCGTGCATTTGGAGTCACT
AGAAGTATGTGGGCAGATGATGCTAAGAAGTTATGTCCAGATCTTCTACTGGCACAAGTT
CGTGAGTCCCGTGGGAAAGCTAACCTCACCAAGTACCGGGAAGCCAGTGTTGAAGTGATG
GAGATAATGTCTCGTTTTGCTGTGATTGAACGTGCCAGCATTGATGAGGCTTACGTAGAT
CTGACCAGTGCTGTACAAGAGAGACTACAAAAGCTACAAGGTCAGCCTATCTCGGCAGAC
TTGTTGCCAAGCACTTACATTGAAGGGTTGCCCCAAGGCCCTACAACGGCAGAAGAGACT
GTTCAGAAAGAGGGGATGCGAAAACAAGGCTTATTTCAATGGCTCGATTCTCTTCAGATT
GATAACCTCACCTCTCCAGACCTGCAGCTCACCGTGGGAGCAGTGATTGTGGAGGAAATG
AGAGCAGCCATAGAGAGGGAGACTGGTTTTCAGTGTTCAGCTGGAATTTCACACAATAAG
GTCCTGGCAAAACTGGCCTGTGGACTAAACAAGCCCAACCGCCAAACCCTGGTTTCACAT
GGGTCAGTCCCACAGCTCTTCAGCCAAATGCCCATTCGCAAAATCCGTAGTCTTGGAGGA
AAGCTAGGGGCCTCTGTCATTGAGATCCTAGGGATAGAATACATGGGTGAACTGACCCAG
TTCACTGAATCCCAGCTCCAGAGTCATTTTGGGGAGAAGAATGGGTCTTGGCTATATGCC
ATGTGCCGAGGGATTGAACATGATCCAGTTAAACCCAGGCAACTACCCAAAACCATTGGC
TGTAGTAAGAACTTCCCAGGAAAAACAGCTCTTGCTACTCGGGAACAGGTACAATGGTGG
CTGTTGCAATTAGCCCAGGAACTAGAGGAGAGACTGACTAAAGACCGAAATGATAATGAC
AGGGTAGCCACCCAGCTGGTTGTGAGCATTCGTGTACAAGGAGACAAACGCCTCAGCAGC
CTGCGCCGCTGCTGTGCCCTTACCCGCTATGATGCTCACAAGATGAGCCATGATGCATTT
ACTGTCATCAAGAACTGTAATACTTCTGGAATCCAGACAGAATGGTCTCCTCCTCTCACA
ATGCTTTTCCTCTGTGCTACAAAATTTTCTGCCTCTGCCCCTTCATCTTCTACAGACATC
ACCAGCTTCTTGAGCAGTGACCCAAGTTCTCTGCCAAAGGTGCCAGTTACCAGCTCAGAA
GCTAAGACCCAGGGAAGTGGCCCAGCGGTGACAGCCACTAAGAAAGCAACCACGTCTCTG
GAATCATTCTTCCAAAAAGCTGCAGAAAGGCAGAAAGTTAAAGAAGCTTCGCTTTCATCT
CTTACTGCTCCCACTCAGGCTCCCATGAGCAATTCACCATCCAAGCCCTCATTACCTTTT
CAAACCAGTCAAAGTACAGGAACTGAGCCCTTCTTTAAGCAGAAAAGTCTGCTTCTAAAG
CAGAAACAGCTTAATAATTCTTCAGTTTCTTCCCCCCAACAAAACCCATGGTCCAACTGT
AAAGCATTACCAAACTCTTTACCAACAGAGTATCCAGGGTGTGTCCCTGTTTGTGAAGGG
GTGTCGAAGCTAGAAGAATCCTCTAAAGCAACTCCTGCAGAGATGGATTTGGCCCACAAC
AGCCAAAGCATGCACGCCTCTTCAGCTTCCAAATCTGTGCTGGAGGTGACTCAGAAAGCA
ACCCCAAATCCAAGTCTTCTAGCTGCTGAGGACCAAGTGCCCTGTGAGAAGTGTGGCTCC
CTGGTACCGGTATGGGATATGCCAGAACACATGGACTATCATTTTGCATTGGAGTTGCAG
AAATCCTTTTTGCAGCCCCACTCTTCAAACCCCCAGGTTGTTTCTGCCGTATCTCATCAA
GGCAAAAGAAATCCCAAGAGCCCTTTGGCCTGCACTAATAAACGCCCCAGGCCTGAGGGC
ATGCAAACATTGGAATCATTTTTTAAGCCATTAACACATTAG
|
| Enzyme 20 GenBank Gene ID |
AB024313  |
| Enzyme 20 GeneCard ID |
POLH  |
| Enzyme 20 GenAtlas ID |
POLH  |
| Enzyme 20 HGNC ID |
HGNC:9181  |
| Enzyme 20 Chromosome Location |
6 |
| Enzyme 20 Locus |
6p21.1 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Masutani C, Kusumoto R, Yamada A, Dohmae N, Yokoi M, Yuasa M, Araki M, Iwai S, Takio K, Hanaoka F: The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase eta. Nature. 1999 Jun 17;399(6737):700-4. [PubMed
]
- Johnson RE, Kondratick CM, Prakash S, Prakash L: hRAD30 mutations in the variant form of xeroderma pigmentosum. Science. 1999 Jul 9;285(5425):263-5. [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 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
6246 |
| Enzyme 21 Name |
DNA polymerase delta catalytic subunit |
| Enzyme 21 Synonyms |
- DNA polymerase subunit delta p125
|
| Enzyme 21 Gene Name |
POLD1 |
| Enzyme 21 Protein Sequence |
>DNA polymerase delta catalytic subunit
MDGKRRPGPGPGVPPKRARGGLWDDDDAPRPSQFEEDLALMEEMEAEHRLQEQEEEELQS
VLEGVADGQVPPSAIDPRWLRPTPPALDPQTEPLIFQQLEIDHYVGPAQPVPGGPPPSRG
SVPVLRAFGVTDEGFSVCCHIHGFAPYFYTPAPPGFGPEHMGDLQRELNLAISRDSRGGR
ELTGPAVLAVELCSRESMFGYHGHGPSPFLRITVALPRLVAPARRLLEQGIRVAGLGTPS
FAPYEANVDFEIRFMVDTDIVGCNWLELPAGKYALRLKEKATQCQLEADVLWSDVVSHPP
EGPWQRIAPLRVLSFDIECAGRKGIFPEPERDPVIQICSLGLRWGEPEPFLRLALTLRPC
APILGAKVQSYEKEEDLLQAWSTFIRIMDPDVITGYNIQNFDLPYLISRAQTLKVQTFPF
LGRVAGLCSNIRDSSFQSKQTGRRDTKVVSMVGRVQMDMLQVLLREYKLRSYTLNAVSFH
FLGEQKEDVQHSIITDLQNGNDQTRRRLAVYCLKDAYLPLRLLERLMVLVNAVEMARVTG
VPLSYLLSRGQQVKVVSQLLRQAMHEGLLMPVVKSEGGEDYTGATVIEPLKGYYDVPIAT
LDFSSLYPSIMMAHNLCYTTLLRPGTAQKLGLTEDQFIRTPTGDEFVKTSVRKGLLPQIL
ENLLSARKRAKAELAKETDPLRRQVLDGRQLALKVSANSVYGFTGAQVGKLPCLEISQSV
TGFGRQMIEKTKQLVESKYTVENGYSTSAKVVYGDTDSVMCRFGVSSVAEAMALGREAAD
WVSGHFPSPIRLEFEKVYFPYLLISKKRYAGLLFSSRPDAHDRMDCKGLEAVRRDNCPLV
ANLVTASLRRLLIDRDPEGAVAHAQDVISDLLCNRIDISQLVITKELTRAASDYAGKQAH
VELAERMRKRDPGSAPSLGDRVPYVIISAAKGVAAYMKSEDPLFVLEHSLPIDTQYYLEQ
QLAKPLLRIFEPILGEGRAEAVLLRGDHTRCKTVLTGKVGGLLAFAKRRNCCIGCRTVLS
HQGAVCEFCQPRESELYQKEVSHLNALEERFSRLWTQCQRCQGSLHEDVICTSRDCPIFY
MRKKVRKDLEDQEQLLRRFGPPGPEAW
|
| Enzyme 21 Number of Residues |
1107 |
| Enzyme 21 Molecular Weight |
123633 |
| Enzyme 21 Theoretical pI |
7.03 |
| Enzyme 21 GO Classification |
| Function |
- 3'-5' exonuclease activity
- DNA binding
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- exonuclease activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- nuclease activity
- nucleic acid binding
- nucleotide binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 21 General Function |
Replication, recombination and repair |
| Enzyme 21 Specific Function |
Possesses two enzymatic activities:DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction. Required with its accessory proteins (proliferating cell nuclear antigen (PCNA) and replication factor C (RFC) or activator 1) for leading strand synthesis. Also involved in completing Okazaki fragments initiated by the DNA polymerase alpha/primase complex |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
181620  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
P28340  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
DPOD1_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>3324 bp
ATGGATGGCAAGCGGCGGCCAGGCCCAGGGCCCGGGGTGCCCCCAAAGCGGGCCCGTGGG
GGCCTCTGGGATGATGATGATGCACCTTGGCCATCCCAATTCGAGGAGGACCTGGCACTG
ATGGAGGAGATGGAGGCAGAACACAGGCTGCAGGAGCAGGAGGAGGAGGAGCTGCAGTCA
GTCCTGGAGGGGGTTGCAGACGGGCAGGTCCCACCATCAGCCATAGATCCTCGCTGGCTT
CGGCCCACACCACCAGCGCTGGACCCCCAGACAGAGCCCCTCATCTTCCAACAGTTGGAG
ATTGACCATTATGTGGGCCCAGCGCAGCCTGTGCCTGGGGGGCCCCCACCATCCCGCGGC
TCCGTGCCTGTGCTCCGCGCCTTCGGGGTCACCGATGAGGGGTTCTCTGTCTGCTGCCAC
ATCCACGGCTTCGCTCCCTACTTCTACACCCCAGCGCCCCCTGGTTTCGGGCCCGAGCAC
ATGGGTGACCTGCAACGGGAGCTGAACTTGGCCATCAGCCGGGACAGTCGCGGGGGGAGG
GAGCTGACTGGGCCGGCCGTGCTGGCTGTGGAACTGTGCTCCCGAGAGAGCATGTTTGGG
TACCACGGGCACGGCCCCTCCCCGTTCCTGCGCATCACCGTGGCGCTGCCGCGCCTCGTG
GCCCCGGCCCGCCGTCTCCTGGAACAGGGCATCCGTGTGGCAGGCCTGGGCACGCCCAGC
TTCGCGCCCTACGAGGCCAACGTCGACTTTGAGATCCGGTTCATGGTGGACACGGACATC
GTCGGCTGCAACTGGCTGGAGCTCCCAGCTGGGAAATACGCCCTGAGGCTGAAGGAGAAG
GCTACGCAGTGCCAGCTGGAGGCGGACGTGCTGTGGTCTGACGTGGTCAGTCACCCACCG
GAAGGGCCATGGCAGCGCATTGCGCCCTTGCGCGTGCTCAGCTTCGATATCGAGTGCGCC
GGCCGCAAAGGCATCTTCCCTGAGCCTGAGCGGGACCCTGTCATCCAGATCTGCTCGCTG
GGCCTGCGCTGGGGGGAGCCGGAGCCCTTCCTACGCCTGGCGCTCACCCTGCGGCCCTGT
GCCCCCATCCTGGGTGCCAAGGTGCAGAGCTACGAGAAGGAGGAGGACCTGCTGCAGGCC
TGGTCCACCTTCATCCGTATCATGGACCCCGACGTGATCACCGGTTACAACATCCAGAAC
TTCGACCTTCCGTACCTCATCTCTCGGGCCCAGACCCTCAAGGTACAAACATTCCCTTTC
CTGGGCCGTGTGGCCGGCCTTTGCTCCAACATCCGGGACTCTTCATTCCAGTCCAAGCAG
ACGGGCCGGCGGGACACCAAGGTTGTCAGCATGGTGGGCCGCGTGCAGATGGACATGCTG
CAGGTGCTGCTGCGGGAGTACAAGCTCCGCTCCCACACGCTCAATGCCGTGAGCTTCCAC
TTCCTGGGCGAGCAGAAGGAGGACGTGCAGCACAGCATCATCACCGACCTGCAGAATGGG
AACGACCAGACCCGCCGCCGCCTGGCTGTGTACTGCCTGAAGGATGCCTACCTGCCACTG
CGGCTGCTGGAGCGGCTCATGGTGCTGGTGAACGCCGTGGAGATGGCGAGGGTCACTGGC
GTGCCCCTCAGCTACCTGCTCAGTCGTGGCCAGCAGGTCAAAGTCGTATCCCAGCTGTTG
CGGCAGGCCATGCACGAGGGGCTGCTGATGCCCGTGGTGAAGTCAGAGGGCGGCGAGGAC
TACACGGGAGCCACTGTCATCGAGCCCCTCAAAGGGTACTACGACGTCCCCATCGCCACC
CTGGACTTCTCCTCGCTGTACCCGTCCATCATGATGGCCCACAACCTGTGTTACACCACG
CTCCTTCGGCCCGGGACTGCACAGAAACTGGGCCTGACTGAGGATCAGTTCATCAGGACC
CCCACCGGGGACGAGTTTGTGAAGACCTCAGTGCGGAAGGGGCTGCTGCCCCAGATCCTG
GAGAACCTGCTCAGTGCCCGGAAGAGGGCCAAGGCCGAGCTGGCCAAGGAGACAGACCCC
CTCCGGCGCCAGGTCCTGGATGGACGGCAGCTGGCGCTGAAGGTGAGCGCCAACTCCGTA
TACGGCTTCACTGGCGCCCAGGTGGGCAAGTTGCCGTGCCTGGAGATCTCACAGAGCGTC
ACGGGGTTCGGACGTCAGATGATCGAGAAAACCAAGCAGCTGGTGGAGTCTAAGTACACA
GTGGAGAATGGCTACAGCACCAGTGCCAAGGTGGTGTATGGTGACACTGACTCCGTCATG
TGCCGATTCGGCGTGTCCTCGGTGGCTGAGGCGATGGCCCTGGGGCGGGAGGCCGCGGAC
TGGGTGTCAGGTCACTTCCCGTCGCCCATCCGGCTGGAGTTTGAGAAGGTCTACTTCCCA
TACCTGCTTATCAGCAAGAAGCGCTACGCGGGCCTGCTCTTCTCCTCCCGGCCCGACGCC
CACGACCGCATGGACTGCAAGGGCCTGGAGGCCGTGCGCAGGGACAACTGCCCCCTCGTG
GCCAACCTGGTCACTGCCTCACTGCGCCGCCTGCTCATCGACCGAGACCCTGAGGGCGCG
GTGGCTCACGCACAGGACGTCATCTCGGACCTGCTGTGCAACCGCATCGATATCTCCCAG
CTGGTCATCACCAAGGAGCTGACCCGCGCGGCCTCCGACTATGCCGGCAAGCAGGCCCAC
GTGGAGCTGGCCGAGAGGATGAGGAAGCGGGACCCCGGGAGTGCGCCCAGCCTGGGCGAC
CGCGTCCCCTACGTGATCATCAGTGCCGCCAAGGGTGTGGCCGCCTACATGAAGTCGGAG
GACCCGCTGTTCGTGCTGGAGCACAGCCTGCCCATTGACACGCAGTACTACCTGGAGCAG
CAGCTGGCCAAGCCCCTCCTGCGCATCTTCGAGCCCATCCTGGGCGAGGGCCGTGCCGAG
GCTGTGCTACTGCGGGGGGACCACACGCGCTGCAAGACGGTGCTCACGGGCAAGGTGGGC
GGCCTCCTGGCCTTCGCCAAACGCCGCAACTGCTGCATTGGCTGCCGCACAGTGCTCAGC
CACCAGGGAGCCGTGTGTGAGTTCTGCCAGCCCCGGGAGTCTGAGCTGTATCAGAAGGAG
GTATCCCATCTGAATGCCCTGGAGGAGCGCTTCTCGCGCCTCTGGACGCAGTGCCAGCGC
TGCCAGGGCAGCCTGCACGAGGACGTCATCTGCACCAGCCGGGACTGCCCCATCTTCTAC
ATGCGCAAGAAGGTGCGGAAGGACCTGGAAGACCAGGAGCAGCTCCTGCGGCGCTTCGGA
CCCCCTGGACCTGAGGCCTGGTGA
|
| Enzyme 21 GenBank Gene ID |
M80397  |
| Enzyme 21 GeneCard ID |
POLD1  |
| Enzyme 21 GenAtlas ID |
POLD1  |
| Enzyme 21 HGNC ID |
HGNC:9175  |
| Enzyme 21 Chromosome Location |
19 |
| Enzyme 21 Locus |
19q13.3 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Chung DW, Zhang JA, Tan CK, Davie EW, So AG, Downey KM: Primary structure of the catalytic subunit of human DNA polymerase delta and chromosomal location of the gene. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11197-201. [PubMed
]
- Yang CL, Chang LS, Zhang P, Hao H, Zhu L, Toomey NL, Lee MY: Molecular cloning of the cDNA for the catalytic subunit of human DNA polymerase delta. Nucleic Acids Res. 1992 Feb 25;20(4):735-45. [PubMed
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
6247 |
| Enzyme 22 Name |
DNA polymerase zeta catalytic subunit |
| Enzyme 22 Synonyms |
- hREV3
|
| Enzyme 22 Gene Name |
REV3L |
| Enzyme 22 Protein Sequence |
>DNA polymerase zeta catalytic subunit
MFSVRIVTADYYMASPLQGLDTCQSPLTQAPVKKVPVVRVFGATPAGQKTCLHLHGIFPY
LYVPYDGYGQQPESYLSQMAFSIDRALNVALGNPSSTAQHVFKVSLVSGMPFYGYHEKER
HFMKIYLYNPTMVKRICELLQSGAIMNKFYQPHEAHIPYLLQLFIDYNLYGMNLINLAAV
KFRKARRKSNTLHATGSCKNHLSGNSLADTLFRWEQDEIPSSLILEGVEPQSTCELEVDA
VAADILNRLDIEAQIGGNPGLQAIWEDEKQRRRNRNETSQMSQPESQDHRFVPATESEKK
FQKRLQEILKQNDFSVTLSGSVDYSDGSQEFSAELTLHSEVLSPEMLQCTPANMVEVHKD
KESSKGHTRHKVEEALINEEAILNLMENSQTFQPLTQRLSESPVFMDSSPDEALVHLLAG
LESDGYRGERNRMPSPCRSFGNNKYPQNSDDEENEPQIEKEEMELSLVMSQRWDSNIEEH
CAKKRSLCRNTHRSSTEDDDSSSGEEMEWSDNSLLLASLSIPQLDGTADENSDNPLNNEN
SRTHSSVIATSKLSVKPSIFHKDAATLEPSSSAKITFQCKHTSALSSHVLNKEDLIEDLS
QTNKNTEKGLDNSVTSFTNESTYSMKYPGSLSSTVHSENSHKENSKKEILPVSSCESSIF
DYEEDIPSVTRQVPSRKYTNIRKIEKDSPFIHMHRHPNENTLGKNSFNFSDLNHSKNKVS
SEGNEKGNSTALSSLFPSSFTENCELLSCSGENRTMVHSLNSTADESGLNKLKIRYEEFQ
EHKTEKPSLSQQAAHYMFFPSVVLSNCLTRPQKLSPVTYKLQPGNKPSRLKLNKRKLAGH
QETSTKSSETGSTKDNFIQNNPCNSNPEKDNALASDLTKTTRGAFENKTPTDGFIDCHFG
DGTLETEQSFGLYGNKYTLRAKRKVNYETEDSESSFVTHNSKISLPHPMEIGESLDGTLK
SRKRRKMSKKLPPVIIKYIIINRFRGRKNMLVKLGKIDSKEKQVILTEEKMELYKKLAPL
KDFWPKVPDSPATKYPIYPLTPKKSHRRKSKHKSAKKKTGKQQRTNNENIKRTLSFRKKR
SHAILSPPSPSYNAETEDCDLNYSDVMSKLGFLSERSTSPINSSPPRCWSPTDPRAEEIM
AAAEKEAMLFKGPNVYKKTVNSRIGKTSRARAQIKKSKAKLANPSIVTKKRNKRNQTNKL
VDDGKKKPRAKQKTNEKGTSRKHTTLKDEKIKSQSGAEVKFVLKHQNVSEFASSSGGSQL
LFKQKDMPLMGSAVDHPLSASLPTGINAQQKLSGCFSSFLESKKSVDLQTFPSSRDDLHP
SVVCNSIGPGVSKINVQRPHNQSAMFTLKESTLIQKNIFDLSNHLSQVAQNTQISSGMSS
KIEDNANNIQRNYLSSIGKLSEYRNSLESKLDQAYTPNFLHCKDSQQQIVCIAEQSKHSE
TCSPGNTASEESQMPNNCFVTSLRSPIKQIAWEQKQRGFILDMSNFKPERVKPRSLSEAI
SQTKALSQCKNRNVSTPSAFGEGQSGLAVLKELLQKRQQKAQNANTTQDPLSNKHQPNKN
ISGSLEHNKANKRTRSVTSPRKPRTPRSTKQKEKIPKLLKVDSLNLQNSSQLDNSVSDDS
PIFFSDPGFESCYSLEDSLSPEHNYNFDINTIGQTGFCSFYSGSQFVPADQNLPQKFLSD
AVQDLFPGQAIEKNEFLSHDNQKCDEDKHHTTDSASWIRSGTLSPEIFEKSTIDSNENRR
HNQWKNSFHPLTTRSNSIMDSFCVQQAEDCLSEKSRLNRSSVSKEVFLSLPQPNNSDWIQ
GHTRKEMGQSLDSANTSFTAILSSPDGELVDVACEDLELYVSRNNDMLTPTPDSSPRSTS
SPSQSKNGSFTPRTANILKPLMSPPSREEIMATLLDHDLSETIYQEPFCSNPSDVPEKPR
EIGGRLLMVETRLANDLAEFEGDFSLEGLRLWKTAFSAMTQNPRPGSPLRSGQGVVNKGS
SNSPKMVEDKKIVIMPCKCAPSRQLVQVWLQAKEEYERSKKLPKTKPTGVVKSAENFSSS
VNPDDKPVVPPKMDVSPCILPTTAHTKEDVDNSQIALQAPTTGCSQTASESQMLPPVASA
SDPEKDEDDDDNYYISYSSPDSPVIPPWQQPISPDSKALNGDDRPSSPVEELPSLAFENF
LKPIKDGIQKSPCSEPQEPLVISPINTRARTGKCESLCFHSTPIIQRKLLERLPEAPGLS
PLSTEPKTQKLSNKKGSNTDTLRRVLLTQAKNQFAAVNTPQKETSQIDGPSLNNTYGFKV
SIQNLQEAKALHEIQNLTLISVELHARTRRDLEPDPEFDPICALFYCISSDTPLPDTEKT
ELTGVIVIDKDKTVFSQDIRYQTPLLIRSGITGLEVTYAADEKALFHEIANIIKRYDPDI
LLGYEIQMHSWGYLLQRAAALSIDLCRMISRVPDDKIENRFAAERDEYGSYTMSEINIVG
RITLNLWRIMRNEVALTNYTFENVSFHVLHQRFPLFTFRVLSDWFDNKTDLYRWKMVDHY
VSRVRGNLQMLEQLDLIGKTSEMARLFGIQFLHVLTRGSQYRVESMMLRIAKPMNYIPVT
PSVQQRSQMRAPQCVPLIMEPESRFYSNSVLVLDFQSLYPSIVIAYNYCFSTCLGHVENL
GKYDEFKFGCTSLRVPPDLLYQVRHDITVSPNGVAFVKPSVRKGVLPRMLEEILKTRFMV
KQSMKAYKQDRALSRMLDARQLGLKLIANVTFGYTSANFSGRMPCIEVGDSIVHKARETL
ERAIKLVNDTKKWGARVVYGDTDSMFVLLKGATKEQSFKIGQEIAEAVTATNPKPVKLKF
EKVYLPCVLQTKKRYVGYMYETLDQKDPVFDAKGIETVRRDSCPAVSKILERSLKLLFET
RDISLIKQYVQRQCMKLLEGKASIQDFIFAKEYRGSFSYKPGACVPALELTRKMLTYDRR
SEPQVGERVPYVIIYGTPGVPLIQLVRRPVEVLQDPTLRLNATYYITKQILPPLARIFSL
IGIDVFSWYHELPRIHKATSSSRSEPEGRKGTISQYFTTLHCPVCDDLTQHGICSKCRSQ
PQHVAVILNQEIRELERQQEQLVKICKNCTGCFDRHIPCVSLNCPVLFKLSRVNRELSKA
PYLRQLLDQF
|
| Enzyme 22 Number of Residues |
3130 |
| Enzyme 22 Molecular Weight |
352779 |
| Enzyme 22 Theoretical pI |
8.61 |
| Enzyme 22 GO Classification |
Not Available |
| Enzyme 22 General Function |
Replication, recombination and repair |
| Enzyme 22 Specific Function |
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1) |
| Enzyme 22 Pathways |
|
| Enzyme 22 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 22 Pfam Domain Function |
Not Available |
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
3063675  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
O60673  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
DPOLZ_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>9393 bp
ATGTTTTCAGTAAGGATAGTGACTGCAGACTACTACATGGCCAGCCCGCTGCAGGGGCTG
GATACCTGCCAATCCCCCCTCACCCAGGCCCCTGTCAAGAAGGTGCCGGTGGTGCGAGTC
TTCGGAGCGACCCCGGCAGGTCAGAAGACATGTCTTCATCTACATGGCATCTTTCCTTAC
CTCTATGTGCCATACGATGGTTATGGACAGCAGCCAGAAAGCTATCTTTCTCAGATGGCA
TTCAGTATCGACAGAGCACTTAATGTGGCTTTAGGCAATCCATCTTCCACTGCTCAGCAT
GTGTTCAAAGTGTCATTAGTATCAGGAATGCCTTTTTATGGTTATCATGAGAAGGAAAGA
CACTTTATGAAGATCTATCTTTACAATCCTACAATGGTGAAAAGGATATGTGAACTTTTG
CAAAGCGGAGCCATAATGAATAAATTTTACCAGCCTCATGAAGCGCATATTCCCTACCTC
CTACAGCTCTTCATTGACTACAATCTTTATGGCATGAATTTAATAAATCTGGCTGCTGTC
AAGTTCCGAAAAGCAAGAAGGAAAAGTAATACATTGCATGCAACTGGATCCTGCAAGAAT
CATTTATCAGGAAATTCTCTTGCTGATACTTTATTTCGGTGGGAACAAGATGAAATACCA
AGCTCTTTAATATTGGAAGGTGTTGAACCACAGAGTACATGTGAATTAGAAGTGGATGCT
GTAGCTGCTGATATCTTAAATCGTCTGGACATTGAAGCTCAAATTGGTGGAAACCCTGGT
CTACAGGCCATATGGGAAGATGAAAAGCAACGGCGAAGAAACAGAAATGAAACTTCTCAA
ATGAGCCAACCTGAGTCACAAGATCACAGGTTTGTGCCAGCAACAGAAAGTGAAAAAAAA
TTTCAGAAGAGACTTCAGGAAATTCTCAAACAGAATGATTTCTCTGTAACATTATCAGGA
TCTGTGGACTACAGCGATGGATCCCAGGAGTTCTCTGCTGAGTTAACATTGCACTCTGAG
GTTCTGTCTCCTGAAATGCTTCAGTGTACACCAGCCAATATGGTAGAAGTTCACAAAGAC
AAAGAGTCAAGCAAAGGTCACACTAGACACAAAGTGGAAGAAGCTCTTATTAATGAAGAA
GCAATTTTGAACCTTATGGAAAATAGTCAGACTTTTCAGCCTTTGACCCAAAGACTGAGT
GAGTCACCTGTTTTCATGGACAGTAGTCCTGATGAGGCTCTGGTACATCTTCTTGCTGGT
TTGGAAAGTGATGGATATCGGGGGGAAAGAAATAGGATGCCATCACCATGTCGCTCCTTT
GGAAATAATAAATATCCACAAAATAGTGATGATGAAGAAAATGAACCACAGATTGAAAAA
GAGGAAATGGAGCTTAGTTTGGTGATGTCCCAGAGATGGGACAGCAATATTGAAGAACAT
TGTGCCAAAAAGAGATCACTGTGCAGAAATACCCACAGAAGTTCAACTGAAGATGATGAC
TCATCTTCAGGAGAAGAAATGGAATGGAGTGATAACAGTTTGCTTCTAGCCAGTCTTTCT
ATACCTCAGTTAGATGGAACTGCAGATGAAAATAGTGACAATCCATTGAACAATGAAAAT
TCTAGAACCCACTCTTCTGTAATTGCAACAAGCAAGCTTTCAGTTAAACCCTCCATCTTT
CACAAAGATGCTGCTACATTAGAACCCTCATCTTCTGCTAAGATTACCTTTCAGTGTAAA
CACACAAGTGCCCTTTCTTCCCATGTTTTGAACAAGGAAGATTTAATTGAAGACCTTTCA
CAGACAAACAAAAATACAGAAAAAGGTCTAGATAACTCAGTCACTTCTTTTACAAACGAA
AGCACTTATTCTATGAAATACCCTGGATCTTTAAGCAGTACTGTTCATTCAGAAAATTCT
CATAAAGAGAATAGTAAGAAAGAGATCCTCCCAGTATCTTCCTGTGAAAGTAGTATTTTT
GATTATGAAGAAGATATTCCATCTGTTACAAGACAAGTACCAAGTAGAAAATATACAAAC
ATTAGAAAAATCGAAAAGGATTCCCCTTTTATACATATGCACCGTCACCCTAACGAGAAT
ACATTGGGCAAAAATTCTTTCAACTTTTCTGACTTAAATCATTCAAAAAATAAAGTATCC
TCTGAAGGAAATGAAAAAGGAAACAGCACAGCTCTGAGTAGTTTATTCCCTTCATCATTT
ACTGAAAATTGTGAATTACTGTCATGCTCAGGGGAGAATAGAACTATGGTGCATTCTCTT
AATAGCACTGCTGATGAAAGTGGACTAAATAAACTTAAAATTAGGTATGAAGAATTTCAA
GAACATAAAACAGAAAAGCCAAGCCTCAGCCAGCAAGCAGCACACTATATGTTTTTTCCC
AGTGTTGTTCTTTCTAACTGTCTTACTAGACCACAGAAACTATCTCCTGTCACATATAAA
TTACAACCTGGCAATAAACCATCCCGGTTAAAATTGAATAAAAGGAAACTTGCAGGTCAT
CAGGAGACTTCTACCAAAAGTAGTGAGACTGGATCCACAAAAGATAATTTTATACAAAAT
AATCCTTGTAATAGTAATCCTGAGAAGGATAATGCATTGGCTAGTGATTTAACTAAAACC
ACTCGTGGAGCTTTTGAAAATAAAACACCCACAGATGGTTTTATAGACTGTCACTTTGGA
GATGGGACGTTAGAAACTGAGCAGTCCTTTGGACTATATGGAAATAAATACACACTTAGA
GCCAAACGCAAGGTAAATTATGAGACTGAAGACAGTGAGTCAAGTTTTGTAACTCACAAC
TCAAAAATTAGTCTACCTCATCCCATGGAAATTGGTGAAAGTTTAGATGGAACTCTCAAA
TCCCGAAAACGAAGAAAAATGTCTAAAAAGCTGCCCCCTGTCATCATAAAGTATATTATT
ATTAATAGATTTAGAGGGAGAAAAAATATGCTTGTGAAGCTAGGAAAAATAGACTCTAAA
GAAAAACAAGTAATATTAACAGAAGAAAAAATGGAACTATATAAAAAGCTTGCACCTTTG
AAGGACTTTTGGCCAAAAGTTCCCGACTCCCCTGCAACCAAATATCCCATTTATCCACTA
ACACCAAAGAAAAGTCACAGAAGAAAGTCAAAACATAAATCTGCTAAGAAAAAAACTGGT
AAACAACAAAGGACAAATAATGAAAATATTAAAAGAACTTTGTCTTTCAGGAAAAAACGG
TCACATGCTATTCTTTCTCCTCCCTCACCATCTTACAATGCTGAAACCGAAGATTGTGAC
TTGAATTATAGTGATGTTATGTCTAAACTAGGTTTTCTTTCTGAGAGAAGCACAAGTCCC
ATAAATTCTTCTCCACCTCGCTGCTGGTCTCCCACAGATCCAAGAGCTGAAGAAATCATG
GCTGCTGCAGAAAAAGAGGCAATGCTTTTTAAGGGTCCTAATGTATATAAGAAGACTGTT
AATTCTCGTATAGGAAAAACTAGTCGCGCAAGAGCACAGATTAAGAAATCAAAAGCAAAG
CTTGCTAATCCCTCTATAGTTACTAAGAAAAGGAACAAACGAAATCAGACAAATAAACTA
GTAGATGATGGAAAAAAGAAACCAAGAGCAAAACAAAAAACAAATGAGAAAGGTACATCG
AGAAAGCATATAACACTTAAGGATGAAAAAATAAAATCTCAGTCTGGTGCTGAGGTTAAG
TTTGTACTGAAACACCAGAATGTGTCTGAATTTGCAAGTAGTTCTGGAGGCTCTCAACTA
CTTTTTAAACAGAAAGATATGCCACTAATGGGCTCTGCTGTAGATCATCCCCTTTCTGCT
TCCCTACCCACTGGAATTAATGCACAACAGAAGTTATCTGGCTGCTTTTCTTCTTTCTTA
GAAAGCAAGAAGTCTGTAGATTTGCAGACATTCCCCAGTTCACGAGATGATTTGCATCCA
TCAGTTGTTTGTAATTCTATAGGACCTGGAGTCTCAAAAATTAATGTTCAAAGGCCTCAT
AATCAAAGTGCTATGTTTACTCTAAAGGAATCAACGTTAATTCAAAAAAATATATTTGAC
CTTTCCAATCATTTATCTCAGGTAGCACAGAATACACAGATATCTTCTGGTATGTCCTCA
AAGATAGAAGATAATGCAAATAATATACAAAGAAACTATTTGTCATCAATCGGAAAGTTA
AGTGAATATCGCAATTCCCTAGAATCAAAGCTGGACCAAGCATATACCCCTAATTTTTTG
CATTGCAAAGACAGTCAGCAGCAGATTGTATGCATAGCGGAACAGTCAAAGCACAGTGAA
ACTTGTTCTCCGGGAAATACAGCTTCAGAGGAAAGCCAAATGCCTAATAATTGCTTTGTA
ACTTCCTTGAGAAGTCCAATCAAACAAATAGCATGGGAGCAAAAGCAAAGGGGCTTTATT
TTAGATATGTCAAATTTTAAACCTGAAAGAGTAAAACCGAGGTCATTATCAGAAGCAATT
TCACAAACCAAAGCACTTTCTCAGTGTAAAAATCGAAATGTGTCAACACCTTCAGCATTT
GGTGAAGGACAGTCTGGACTGGCAGTTCTAAAAGAATTGTTACAAAAAAGACAGCAGAAA
GCACAAAATGCAAATACTACACAAGACCCATTATCCAATAAACATCAACCAAATAAAAAT
ATTTCTGGTTCCCTTGAGCATAACAAAGCAAATAAACGGACACGATCGGTAACGTCCCCA
AGAAAACCTCGAACTCCCAGAAGTACAAAACAAAAAGAAAAAATCCCCAAACTTCTCAAA
GTAGACTCTTTAAATTTACAAAACTCTAGCCAGTTGGATAACTCTGTATCAGATGATAGT
CCCATCTTTTTTTCAGATCCAGGCTTTGAAAGTTGTTACTCACTTGAAGATAGTTTATCT
CCTGAACATAATTATAATTTTGATATTAACACAATAGGTCAGACTGGATTTTGTAGCTTT
TATTCTGGAAGTCAGTTTGTCCCAGCTGATCAGAATTTGCCTCAGAAGTTCCTAAGTGAT
GCTGTTCAGGATCTTTTTCCAGGACAAGCTATAGAAAAAAATGAGTTTTTAAGTCATGAC
AACCAGAAATGTGATGAAGACAAGCATCATACCACAGACTCAGCCTCATGGATTAGATCT
GGTACTTTAAGTCCTGAAATTTTTGAGAAGTCAACCATAGATAGCAATGAGAATCGTCGC
CACAACCAGTGGAAAAATAGCTTTCATCCTCTAACAACTCGGTCTAACTCAATAATGGAT
TCTTTCTGTGTTCAGCAGGCAGAAGACTGTCTAAGTGAAAAATCTAGATTGAATAGGAGT
TCAGTAAGCAAAGAAGTGTTTCTTAGCCTCCCACAGCCAAACAATTCAGACTGGATTCAA
GGTCACACCAGAAAAGAAATGGGACAGTCTCTTGACTCAGCCAATACCTCTTTTACTGCA
ATACTCTCCTCCCCTGATGGTGAACTTGTAGACGTGGCCTGTGAAGATTTAGAACTGTAT
GTTTCAAGAAACAATGATATGTTGACACCAACTCCTGATAGTTCACCAAGATCTACTAGC
TCTCCTTCACAATCTAAAAATGGCAGCTTCACCCCTCGAACTGCTAACATTCTGAAACCA
CTTATGTCCCCCCCAAGTAGGGAAGAAATTATGGCAACTTTGTTGGATCATGACCTGTCT
GAGACTATTTACCAGGAACCATTTTGCAGTAATCCTTCTGATGTACCAGAAAAGCCCAGG
GAGATTGGTGGACGGCTCCTCATGGTAGAAACTCGACTTGCAAATGATCTGGCTGAGTTT
GAGGGAGACTTTTCCTTGGAAGGACTTCGTCTTTGGAAAACAGCATTCTCAGCAATGACT
CAGAATCCAAGGCCAGGGTCACCCCTTCGCAGTGGCCAAGGAGTTGTCAATAAAGGGTCA
AGTAATAGCCCTAAGATGGTTGAAGATAAAAAAATTGTGATTATGCCTTGCAAATGTGCC
CCAAGTCGACAACTGGTTCAAGTGTGGCTTCAAGCCAAAGAAGAATACGAACGTTCCAAG
AAACTGCCTAAAACCAAGCCAACTGGAGTTGTAAAATCTGCTGAGAACTTTAGCTCTTCA
GTTAACCCAGATGACAAACCTGTAGTGCCTCCAAAAATGGATGTAAGTCCATGTATACTC
CCCACTACAGCACATACCAAGGAGGATGTTGATAATTCTCAGATTGCTTTACAAGCACCA
ACCACGGGATGTAGTCAAACTGCAAGTGAAAGTCAGATGCTGCCACCAGTTGCCTCTGCA
AGTGATCCCGAAAAAGATGAAGATGATGATGATAACTATTACATTAGTTATAGCTCCCCT
GATTCTCCAGTAATTCCCCCTTGGCAACAACCAATATCCCCAGATTCCAAAGCATTAAAT
GGAGATGATAGACCCTCATCACCAGTAGAGGAGCTGCCTTCATTGGCTTTTGAGAACTTC
TTAAAGCCAATAAAAGATGGTATACAAAAAAGCCCCTGCAGTGAGCCTCAAGAGCCTCTA
GTGATATCTCCAATTAATACTAGGGCAAGAACTGGGAAATGTGAATCACTTTGCTTTCAT
AGTACACCAATCATACAGAGAAAACTTCTGGAAAGGCTTCCTGAAGCACCTGGCCTTAGC
CCATTATCAACAGAACCAAAAACACAGAAGTTGAGTAATAAGAAAGGAAGTAATACTGAC
ACTCTTAGAAGAGTACTGTTAACACAAGCAAAGAATCAATTTGCAGCAGTAAATACCCCA
CAGAAAGAAACTTCTCAGATTGATGGACCATCTTTAAACAATACTTACGGTTTCAAAGTC
AGCATACAAAACTTACAGGAGGCAAAAGCTTTACATGAGATACAAAATCTTACCCTAATC
AGTGTGGAGTTGCATGCTCGAACTAGACGAGACTTAGAACCGGATCCTGAATTTGACCCA
ATCTGTGCTCTGTTCTACTGCATCTCATCTGACACTCCACTGCCAGATACAGAAAAAACA
GAACTCACAGGTGTAATAGTGATTGATAAAGACAAGACAGTTTTCAGTCAAGATATCAGA
TATCAGACTCCATTACTTATTAGATCTGGAATTACAGGACTCGAAGTCACCTATGCTGCT
GATGAGAAGGCACTTTTTCATGAAATTGCAAATATAATAAAGAGGTATGATCCTGATATT
CTGCTAGGATATGAGATTCAGATGCATTCCTGGGGTTACCTCTTACAAAGGGCTGCCGCT
TTAAGTATTGACTTATGTCGGATGATCTCTCGGGTGCCAGATGACAAAATTGAGAACAGA
TTTGCAGCTGAAAGAGATGAGTATGGATCATATACAATGAGTGAGATAAATATTGTTGGC
CGAATTACACTAAATCTTTGGAGAATCATGAGAAATGAGGTGGCTCTAACTAACTACACC
TTTGAAAATGTGAGCTTTCATGTTCTTCATCAGCGTTTTCCCCTCTTTACCTTTCGAGTC
TTGTCAGACTGGTTTGATAACAAGACAGATCTATACAGATGGAAAATGGTTGATCATTAT
GTTAGCCGTGTCCGTGGAAATCTCCAAATGTTAGAACAGCTGGACCTGATTGGGAAAACC
AGTGAGATGGCTAGACTTTTTGGCATTCAGTTTTTACATGTACTGACAAGGGGTTCACAG
TACCGTGTGGAATCAATGATGTTGCGTATTGCTAAACCAATGAACTATATTCCTGTGACA
CCTAGTGTTCAGCAAAGATCCCAGATGAGAGCCCCACAGTGTGTTCCTCTAATTATGGAG
CCTGAATCCCGCTTCTATAGCAACTCTGTTCTCGTTTTGGATTTCCAATCACTTTATCCT
TCTATTGTGATTGCATATAACTACTGCTTTTCCACCTGCCTTGGCCATGTGGAGAACTTG
GGAAAGTATGATGAGTTCAAATTTGGCTGTACCTCTCTGAGAGTACCTCCAGATTTACTT
TACCAAGTTAGGCATGATATCACAGTGTCCCCCAATGGAGTAGCTTTTGTCAAGCCTTCA
GTAAGAAAAGGTGTACTACCAAGAATGCTTGAAGAAATTTTGAAGACTAGATTTATGGTG
AAGCAGTCAATGAAGGCTTACAAGCAAGACAGAGCCCTGTCACGAATGCTTGATGCGCGT
CAGTTGGGACTTAAGCTGATAGCAAATGTCACATTTGGCTATACATCTGCTAATTTTTCT
GGGAGAATGCCATGCATTGAGGTTGGCGATAGTATTGTTCACAAAGCCAGAGAGACCTTG
GAACGAGCTATTAAACTGGTGAATGATACCAAGAAATGGGGGGCTAGGGTTGTATATGGC
GATACTGACAGTATGTTTGTGCTACTGAAAGGAGCCACTAAGGAGCAGTCTTTTAAGATT
GGTCAGGAAATTGCCGAAGCTGTAACTGCTACCAATCCTAAACCAGTGAAATTGAAGTTT
GAAAAGGTATATTTGCCCTGTGTTTTACAAACAAAAAAGAGGTATGTGGGTTACATGTAT
GAAACACTGGATCAGAAGGACCCAGTATTTGATGCAAAAGGAATAGAAACAGTCAGAAGA
GATTCCTGCCCTGCTGTTTCTAAGATACTTGAGCGTTCTCTAAAGCTGCTATTTGAAACG
AGAGATATAAGTCTAATTAAACAGTATGTTCAGCGACAATGTATGAAGCTTCTGGAAGGA
AAGGCCAGCATACAAGACTTTATCTTTGCCAAGGAATACAGAGGAAGTTTTTCTTATAAA
CCAGGAGCTTGTGTGCCAGCCCTTGAACTTACAAGGAAAATGCTGACTTATGACCGGCGC
TCTGAGCCTCAGGTTGGGGAGCGAGTGCCATACGTCATCATTTATGGGACCCCCGGAGTA
CCACTTATCCAGCTTGTAAGGCGCCCAGTGGAAGTCCTGCAGGACCCAACTCTGAGACTG
AATGCTACTTACTATATTACCAAGCAAATCCTTCCACCCTTGGCAAGAATCTTCTCACTT
ATTGGTATTGATGTCTTCAGCTGGTATCATGAATTACCAAGGATCCATAAAGCTACCAGC
TCCTCGCGAAGTGAACCTGAAGGGCGGAAAGGCACTATTTCACAATATTTTACTACCTTA
CACTGTCCTGTGTGTGATGACCTAACTCAGCATGGCATCTGTAGTAAATGTCGGAGCCAA
CCTCAGCATGTTGCAGTCATCCTCAACCAAGAAATCCGGGAGTTGGAACGTCAACAGGAG
CAACTTGTAAAGATATGCAAGAACTGTACAGGTTGCTTTGATCGACACATCCCATGTGTT
TCTCTGAACTGCCCAGTACTTTTCAAACTCTCCCGAGTAAATAGAGAATTGTCCAAGGCA
CCATATCTCCGGCAGTTATTAGACCAGTTTTAA
|
| Enzyme 22 GenBank Gene ID |
AF058701  |
| Enzyme 22 GeneCard ID |
REV3L  |
| Enzyme 22 GenAtlas ID |
REV3L  |
| Enzyme 22 HGNC ID |
HGNC:9968  |
| Enzyme 22 Chromosome Location |
6 |
| Enzyme 22 Locus |
6q21 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Gibbs PE, McGregor WG, Maher VM, Nisson P, Lawrence CW: A human homolog of the Saccharomyces cerevisiae REV3 gene, which encodes the catalytic subunit of DNA polymerase zeta. Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6876-80. [PubMed
]
- Lin W, Wu X, Wang Z: A full-length cDNA of hREV3 is predicted to encode DNA polymerase zeta for damage-induced mutagenesis in humans. Mutat Res. 1999 Mar 10;433(2):89-98. [PubMed
]
- Morelli C, Mungall AJ, Negrini M, Barbanti-Brodano G, Croce CM: Alternative splicing, genomic structure, and fine chromosome localization of REV3L. Cytogenet Cell Genet. 1998;83(1-2):18-20. [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
]
- Murakumo Y, Roth T, Ishii H, Rasio D, Numata S, Croce CM, Fishel R: A human REV7 homolog that interacts with the polymerase zeta catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2. J Biol Chem. 2000 Feb 11;275(6):4391-7. [PubMed
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
6249 |
| Enzyme 23 Name |
DNA polymerase epsilon, catalytic subunit A |
| Enzyme 23 Synonyms |
- DNA polymerase II subunit A
|
| Enzyme 23 Gene Name |
POLE |
| Enzyme 23 Protein Sequence |
>DNA polymerase epsilon, catalytic subunit A
MSLRSGGRRRADPGADGEASRDDGATSSVSALKRLERSQWTDKMDLRFGFERLKEPGEKT
GWLINMHPTEILDEDKRLGSAVDYYFIQDDGSRFKVALPYKPYFYIATRKGCEREVSSFL
SKKFQGKIAKVETVPKEDLDLPNHLVGLKRNYIRLSFHTVEDLVKVRKEISPAVKKNREQ
DHASDAYTALLSSVLQRGGVITDEEETSKKIADQLDNIVDMREYDVPYHIRLSIDLKIHV
AHWYNVRYRGNAFPVEITRRDDLVERPDPVVLAFDIETTKLPLKFPDAETDQIMMISYMI
DGQGYLITNREIVSEDIEDFEFTPKPEYEGPFCVFNEPDEAHLIQRWFEHVQETKPTIMV
TYNGDFFDWPFVEARAAVHGLSMQQEIGFQKDSQGEYKAPQCIHMDCLRWVKRDSYLPVG
SHNLKAAAKAKLGYDPVELDPEDMCRMATEQPQTLATYSVSDAVATYYLYMKYVHPFIFA
LCTIIPMEPDEVLRKGSGTLCEALLMVQAFHANIIFPNKQEQEFNKLTDDGHVLDSETYV
GGHVEALESGVFRSDIPCRFRMNPAAFDFLLQRVEKTLRHALEEEEKVPVEQVTNFEEVC
DEIKSKLASLKDVPSRIECPLIYHLDVGAMYPNIILTNRLQPSAMVDEATCAACDFNKPG
ANCQRKMAWQWRGEFMPASRSEYHRIQHQLESEKFPPLFPEGPARAFHELSREEQAKYEK
RRLADYCRKAYKKIHITKVEERLTTICQRENSFYVDTVRAFRDRRYEFKGLHKVWKKKLS
AAVEVGDAAEVKRCKNMEVLYDSLQLAHKCILNSFYGYVMRKGARWYSMEMAGIVCFTGA
NIITQARELIEQIGRPLELDTDGIWCVLPNSFPENFVFKTTNVKKPKVTISYPGAMLNIM
VKEGFTNDQYQELAEPSSLTYVTRSENSIFFEVDGPYLAMILPASKEEGKKLKKRYAVFN
EDGSLAELKGFEVKRRGELQLIKIFQSSVFEAFLKGSTLEEVYGSVAKVADYWLDVLYSK
AANMPDSELFELISENRSMSRKLEDYGEQKSTSISTAKRLAEFLGDQMVKDAGLSCRYII
SRKPEGSPVTERAIPLAIFQAEPTVRKHFLRKWLKSSSLQDFDIRAILDWDYYIERLGSA
IQKIITIPAALQQVKNPVPRVKHPDWLHKKLLEKNDVYKQKKISELFTLEGRRQVTMAEA
SEDSPRPSAPDMEDFGLVKLPHPAAPVTVKRKRVLWESQEESQDLTPTVPWQEILGQPPA
LGTSQEEWLVWLRFHKKKWQLQARQRLARRKRQRLESAEGVLRPGAIRDGPATGLGSFLR
RTARSILDLPWQIVQISETSQAGLFRLWALVGSDLHCIRLSIPRVFYVNQRVAKAEEGAS
YRKVNRVLPRSNMVYNLYEYSVPEDMYQEHINEINAELSAPDIEGVYETQVPLLFRALVH
LGCVCVVNKQLVRHLSGWEAETFALEHLEMRSLAQFSYLEPGSIRHIYLYHHAQAHKALF
GIFIPSQRRASVFVLDTVRSNQMPSLGALYSAEHGLLLEKVGPELLPPPKHTFEVRAETD
LKTICRAIQRFLLAYKEERRGPTLIAVQSSWELKRLASEIPVLEEFPLVPICVADKINYG
VLDWQRHGARRMIRHYLNLDTCLSQAFEMSRYFHIPIGNLPEDISTFGSDLFFARHLQRH
NHLLWLSPTARPDLGGKEADDNCLVMEFDDQATVEINSSGCYSTVCVELDLQNLAVNTIL
QSHHVNDMEGADSMGISFDVIQQASLEDMITGGQAASAPASYDETALCSNTFRILKSMVV
GWVKEITQYHNIYADNQVMHFYRWLRSPSSLLHDPALHRTLHNMMKKLFLQLIAEFKRLG
SSVIYANFNRIILCTKKRRVEDAIAYVEYITSSIHSKETFHSLTISFSRCWEFLLWMDPS
NYGGIKGKVSSRIHCGLQDSQKAGGAEDEQENEDDEEERDGEEEEEAEESNVEDLLENNW
NILQFLPQAASCQNYFLMIVSAYIVAVYHCMKDGLRRSAPGSTPVRRRGASQLSQEAEGA
VGALPGMITFSQDYVANELTQSFFTITQKIQKKVTGSRNSTELSEMFPVLPGSHLLLNNP
ALEFIKYVCKVLSLDTNITNQVNKLNRDLLRLVDVGEFSEEAQFRDPCRSYVLPEVICRS
CNFCRDLDLCKDSSFSEDGAVLPQWLCSNCQAPYDSSAIEMTLVEVLQKKLMAFTLQDLV
CLKCRGVKETSMPVYCSCAGDFALTIHTQVFMEQIGIFRNIAQHYGMSYLLETLEWLLQK
NPQLGH
|
| Enzyme 23 Number of Residues |
2286 |
| Enzyme 23 Molecular Weight |
261521 |
| Enzyme 23 Theoretical pI |
6.35 |
| Enzyme 23 GO Classification |
| Function |
- 3'-5' exonuclease activity
- DNA binding
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- exonuclease activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- nuclease activity
- nucleic acid binding
- nucleotide binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 23 General Function |
Replication, recombination and repair |
| Enzyme 23 Specific Function |
Participates in DNA repair and in chromosomal DNA replication |
| Enzyme 23 Pathways |
|
| Enzyme 23 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
303157  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q07864  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
DPOE1_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>6774 bp
ATGTCTCTGAGGAGCGGCGGGCGGCGGCGCGCGGACCCAGGCGCGGATGGCGAGGCCAGC
AGGGATGATGGCGCCACTTCCTCAGTTTCGGCACTCAAGCGCCTGGAACGGAGTCAGTGG
ACGGATAAGATGGATTTGCGGTTTGGTTTTGAGCGGCTGAAGGAGCCTGGTGAGAAGACA
GGCTGGCTCATTAACATGCATCCTGTGGCTTTGCCCTATAAACCGTATTTCTACATTGCG
ACCAGAAAGGGTTGTGAGCGAGAAGTTTCATCTTTTCTCTCCAAGAAGTTTCAGGGCAAA
ATTGCAAAAGTGGAGACTGTCCCCAAAGAGGATCTGGACTTGCCAAATCACTTGGTGGGT
TTGAAGCGAAATTACATCAGGCTGTCCTTCCACACTGTGGAGGATCTTGTCAAAGTGAGG
AAGGAGATCTCCCCTGCCGTGAAGAAGAACAGGGAGCAGGATCACGCCAGCGACGCGTAC
ACAGCTCTGCTTTCCAGTGTTCTGCAGAGGGGCGGTGTCATTACTGATGAAGAGGAAACC
TCTAAGAAGATAGCTGACCAGTTGGACAACATTGTGGACATGCGCGAGTACGATGTTCCC
TACCACATCCGCCTCTCCATTGACCTGAAGATCCACGTGGCTCATTGGTACAATGTCAGA
TACCGAGGAAATGCTTTTCCGGTAGAAATCACCCGCCGAGATGACCTTGTTGAACGACCT
GACCCTGTGGTTTTGGCATTTGACATTGAGACGACCAAACTGCCCCTCAAGTTTCCTGAT
GCTGAGACAGACCAGATTATGATGATTTCCTACATGATCGATGGCCAGGGCTACCTCATC
ACCAACAGGGAGATTGTTTCAGAAGATATTGAAGATTTTGAGTTCACCCCCAAGCCAGAA
TATGAAGGCCCCTTTTGTGTCTTCAATGAACCCGATGAGGCTCATCTGATCCAAAGGTGG
TTTGAACACGTCCAGGAGACCAAACCCACCATCATGGTCACCTACAACGGGGACTTTTTT
GACTGGCCATTTGTGGAGGCCCGGGCAGCAGTCCACGGTCTGAGCATGCAGCAGGAGATA
GGCTTCCAGAAGGACAGCCAGGGGGAGTACAAGGCGCCCCAGTGCATCCACATGGACTGC
CTCAGGTGGGTGAAGAGGGACAGTTACCTTCCTGTGGGCAGTCATAATCTCAAGGCGGCC
GCAAGCAAGCTAGGCTATGATCCCGTGGAGCTAGACCCGGAGACATGTGCCGGATCGACG
GAGCAGCCCCAGACTCTGGCCACGTATTCTGTGTCAGATGCTGTCGCCACTTACTACCTG
TACATGAAGTACGTCCACCCATTCATCTTTGCTCTGTGCACCATTATTCCCATGGAGCCC
GACGAGGTGCTGCGGAAGGGCTCTGGCACTCTGTGTGAGGCCTTGCTGATGGTGCAGGCC
TTCCACGCCAACATCATCTTCCCCAACAAGCAAGAGCAGGAGTTCAATAAGCTGACGGAC
GACGGACACGTGCTGGACTCTGAGACCTACGTCGGGGGCCACGTGGAGGCCCTCGAGTCT
GGGGTTTTCCGCAGCGATATCCCTTGCCGGTTTAGGATGAATCCTGCCGCCTTTGACTTC
CTGCTGCAGCGGGTTGAGAAGACCTTGCGCCACGCCCTTGAGGAAGAGGAGAAAGTGCCT
GTGGAGCAAGTCACCAACTTTGAAGAGGTGTGTGATGAGATTAAGAGCAAGCTTGCCTCC
CTGAAGGACGTTCCCAGCCGCATCGAGTGTCCACTCATCTACCACCTGGACGTGGGGGCC
ATGTACCCCAACATCATCCTGACCAACCGCCTGCAGCCCTCTGCCATGGTGGACGAAGCC
ACCTGTGCTGCCTGTGACTTCAATAAGCCTGGAGCAAACTGCCAGCGGAAGATGGCCTGG
CAGTGGAGGGGCGAGTTCATGCCAGCCAGTCGCAGCGAATACCATCGGATCCAGCACCAG
CTGGAGTCAGAGAAGTTCCCCCCCTTGTTCCCAGAGGGGCCAGCTCGGGCCTTTCATGAA
CTGTCCCGCGAGGAACAGGCGAAATACGAGAAGAGAAGGCTGGCGGATTACTGCCGGAAA
GCCTACAAGAAGATCCACATCACCAAGGTGGAAGAGCGTCTCACCACCATCTGCCAGCGG
GAAAACTCCTTCTACGTGGACACCGTGCGTGCCTTCCGGGACAGGCGTTACGAGTTCAAA
GGGCTCCACAAGGTGTGGAAAAAGAAGCTCTCGGCGGCCGTGGAGGTGGGCGACGCGGCT
GAGGTGAAGCGCTGCAAGAACATGGAGGTGCTGTATGACTCGCTGCAGCTGGCCCACAAG
TGCATCCTGAACTCCTTCTATGGCTATGTCATGCGCAAGGGGGCTCGCTGGTACTCCATG
GAGATGGCTGGCATCGTCTGCTTCACAGGGGCCAACATCATCACCCAGGCACGGGAGCTG
ATCGAGCAGATTGGGAGGCCCTTAGAGCTGGACACAGATGGTATATGGTGCGTCCTGCCC
AACAGCTTCCCAGAAAATTTTGTCTTCAAGACGACCAATGTGAAGAAGCCCAAAGTGACC
ATCTCCTACCCAGGCGCCATGTTGAACATCATGGTCAAGGAAGGCTTCACCAATGACCAG
TACCAGGAGCTGGCTGAGCCGTCCTCACTCACCTACGTCACCCGCTCAGAGAACAGCATC
TTTTTTGAGGTTGATGGGCCCTACCTTGCCATGATTCTTCCAGCCTCCAAGGAAGAAGGC
AAGAAATTGAAGAAGAGGTATGCTGTGTTCAATGAAGACGGTTCTCTGGCTGAGCTCAAG
GGCTTTGAGGTCAAACGCCGCGGGGAACTGCAGCTGATTAAGATCTTCCAATCCTCGGTG
TTTGAGGCCTTCCTCAAGGGCAGCACGCTGGAAGAGGTGTATGGCTCTGTAGCCAAGGTG
GCTGACTACTGGCTGGACGTGCTGTACAGCAAGGCAGCCAACATGCCTGACTCTGAGCTA
TTCGAGCTCATCTCTGAGAACCGTTCCATGTCTCGGAAGCTGGAAGATTACGGGGAGCAG
AAGTCTACGTCCATCAGCACAGCAAAGCGCCTGGCCGAGTTCCTGGGAGACCAGATGGTC
AAGGATGCAGGGCTGAGTTGCCGCTACATCATCTCCCGCAACGCCGAGGGCTCCCCTGTC
ACGGAGAGGGCCATCCCACTTGCCATTTTCCAAGCAGAGCCCACGGTGAGGAAGCACTTT
CTCCGGAAATGGCTCAAGAGCTCTTCCCTTCAAGACTTTGATATTCGAGCAATTCTGGAT
TGGGACTACTACATTGAGCGGCTGGGAAGCGCCATCCAGAAGATCATCACCATCCCTGCG
GCCCTGCAGCAGGTAAAGAACCCAGTGCCACGTGTCAAACACCCCGACTGGCTGCACAAA
AAACTGCTGGAGAAGAATGATGTCTACAAGCAGAAGAAGATCAGTGAGCTCTTCACCCTG
GAGGGCAGGAGACAGGTCACGATGGCCGAGGCCTCAGAAGACAGTCCGAGGCCAAGTGCT
CCTGACATGGAGGACTTCGGCCTCGTAAAGCTGCCTCACCCAGCAGCCCCTGTCACTGTG
AAGAGGAAGCGAGTTCTTTGGGAGAGCCAGGAGGAGTCCCAGGACCTCACGCCGACTGTG
CCCTGGCAGGAAATCTTGGGGCAGCCTCCCGCCCTGGGAACCAGCCAGGAGGAATGGCTT
GTCTGGCTCCGGTTCCACAAGAAGAAGTGGCAGCTGCAGGCCCGGCAGCGCCTCGCCCGC
AGGAAGAGGCAGCGTCTGGAGTCGGCAGAGGGTGTGCTCAGGCCCGGGGCCATCCGGGAT
GGTCCTGCCACGGGGCTGGGGAGCTTCTTGCGAAGAACTGCCCGCAGCATCCTGGACCTT
CCGTGGCAGATTGTGCAGATCAGCGAGACCAGCCAGGCCGGCCTGTTCAGGCTGTGGGCG
CTCGTTGGCAGTGACTTGCACTGCATCAGGCTGAGCATCCCCCGTGTGTTCTACGTGAAC
CAGCGAGTGCCTAAAGCGGAGGAGGGTGCTTCGTATCGCAAGGTAAATCGGGTCCTTCCT
CGCTCCAACATGGTCTACAATCTCTATGAGTATTCAGTGCCAGAGGACATGTACCAGGAA
CACATCAACGAGATCAACGCTGAGCTGTCAGCGCCAGACATCGAGGGCGTATATGAGACT
CAGGTTCCGTTACTGTTCCGGGCCCTGGTGCACCTGGGCTGTGTGTGTGTGGTCAATAAA
CAGCTGGTGAGGCACCTTTCAGGCTGGGAAGCAGAGACCTTTGCTCTTGAGCACCTGGAG
ATGCGCTCTCTGGCCCAGTTCAGCTACCTGGAACCAGGGAGTATCCGCCATATCTACCTG
TACCACCACGCACAGGCCCACAAAGCGCTCTTCGGGATCTTCATCCCCTCACAGCGCAGG
GCATCCGTCTTTGTGCTGGACACTGTGCGCACAGACCAGATGCCCAGCCTTGGCGCCCTG
TACTCAGCAGAGCACGGCCTCCTCCTGGAGAAGGTGGGCCCTGAGCTCCTGCCACCCCCC
AAACACACCTTCGAAGTTCGGGCAGAAACTGACCTGAAGACCATCTGCAGAGCCATCCAG
CGATTCCTGCTCGCCTACAAGGAGGAGCGCCGGGGGCCCACACTCATCGCTGTTCAGTCC
AGCTGGGAGCTGAAGAGGCTGGCCAGTGAAATTCCTGTCTTGGAGGAATTCCCACTGGTG
CCTATCTGTGTGGCTGACAAGATCAACTATGGGGTCCTGGACTGGCAGCGCCATGGAGCC
CGGCGCATGATCCGTCACTACCTCAACCTGGACACCTGCCTGTCGCAGGCCTTCGAGATG
AGCAGGTACTTTCACATTCCCATTGGGAACCTACCAGAGGACATCTCCACATTCGGCTCC
GACCTCTTCTTTGCCCGCCACCTCCAGCGCCACAACCACCTGCTCTGGCTGTCCCCTACA
GCCCGCCCTGACCTGGGTGGAAAGGAGGCTGATGACAACTGTCTTGTCATGGAGTTCGAT
GACCAAGCCACTGTTGAGATCAACAGTTCAGGCTGTTACTCCACAGTGTGTGTGGAGCTG
GACCTTCAGAACCTGGCCGTCAACACCATTCTCCAGTCTCACCATGTCAACGACATGGAG
GGGGCCGACAGCATGGGGATCAGCTTCGACGTGATCCAGCAGGCCTCCCTGGAGGACATG
ATCACGGGTGGTCAGGCTGCCAGTGCCCCGGCCAGCTACGATGAGACAGCCCTGTGCTCT
AACACCTTCAGGATCCTGAAGAGCATGGTCGTGGGCTGGGTGAAGGAGATCACCCAGTAC
CACAACATCTATGCAGACAACCAGGTGATGCACTTCTACCGCTGGCTTCGGTCGCCATCC
TCTCTGCTTCATGACCCTGCCCTGCACCGCACACTCCACAACATGATGAAGAAGCTCTTC
CTGCAGCTCATCGCTGAGTTCAAGCGCCTGGGGTCATCAGTCATCTACGCCAACTTCAAC
CGCATCATCCTCTGTACAAAGAAGCGCCGTGTGGAAGATGCCATCGCTTACGTGGAGTAC
ATCACCAGCAGCATCCATTCAAAGGAGACCTTCCATTCTCTGACAATTTCTTTCTCTCGA
TGCTGGGAATTTCTTCTCTGGATGGATCCATCTAACTATGGCGGAATCAAAGGAAAAGTT
TCATCTCGTATTCACTGTGGACTGCAAGACTCCCAGAAAGCAGGGGGAGCAGAGGATGAG
CAGGAAAATGAGGACGATGAGGAGGAAAGAGATGGGGAGGAGGAGGAAGAGGCGGAGGAA
TCCAACGTGGAGGATTTACTGGAAAACAACTGGAACATTTTGCAGTTTTTGCCACAGGCA
GCCTCCTGCCAGAACTACTTCCTCATGATTGTTTCAGCGTACATCGTGGCCGTGTACCAC
TGCATGAAGGACGGGCTGAGGCGCAGTGCTCCAGGGAGCACCCCCGTGAGGAGGAGGGGG
GCCAGCCAGCTCTCCCAGGAGGCCGAGGGGGCGGTCGGAGCCCTTCCCGGAATGATCACC
TTCTCTCAGGATTATGTCGCAAATGAGCTCACTCAGAGCTTCTTCACCATCACTCAGAAG
ATTCAGAAGAAAGTCACAGGCTCTCGGAACTCCACTGAGCTCTCAGAGATGTTTCCTGTC
CTCCCCGGTTCCCACTTGCTGCTCAATAACCCTGCCCTGGAGTTCATCAAATACGTGTGC
AAGGTGCTGTCCCTGGACACCAACATCACAAACCAGGTGAATAAGCTGAACCGAGACCTG
CTTCGCCTGGTGGATGTCGGCGAGTTCTCCGAGGAGGCCCAGTTCCGAGACCCCTGCCGC
TCCTACGTGCTTCCTGAGGTCATCTGCCGCAGCTGTAACTTCTGCCGCGACCTGGACCTG
TGTAAAGACTCTTCCTTCTCAGAGGATGGGGCGGTCCTGCCTCAGTGGCTCTGCTCCAAC
TGTCAGGCGCCCTACGACTCCTCTGCCATCGAGATGACGCTGGTGGAAGTTCTACAGAAG
AAGCTGATGGCCTTCACCCTGCAGGACCTGGTCTGCCTGAAGTGCCGCGGGGTGAAGGAG
ACCAGCATGCCTGTGTACTGCACGTGCGCGGGAGACTTCGCCCTCACCATCCACACCCAG
GTCTTCATGGAACAGATCGGAATATTCCGGAACATTGCCCAGCACTACGGCATGTCGTAC
CTCCTGGAGACCCTGGAGTGGCTGCTGCAGAAGAACCCACAGCTGGGCCATTAG
|
| Enzyme 23 GenBank Gene ID |
S60080  |
| Enzyme 23 GeneCard ID |
POLE  |
| Enzyme 23 GenAtlas ID |
POLE  |
| Enzyme 23 HGNC ID |
HGNC:9177  |
| Enzyme 23 Chromosome Location |
12 |
| Enzyme 23 Locus |
12q24.3 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Kesti T, Frantti H, Syvaoja JE: Molecular cloning of the cDNA for the catalytic subunit of human DNA polymerase epsilon. J Biol Chem. 1993 May 15;268(14):10238-45. [PubMed
]
- Post SM, Tomkinson AE, Lee EY: The human checkpoint Rad protein Rad17 is chromatin-associated throughout the cell cycle, localizes to DNA replication sites, and interacts with DNA polymerase epsilon. Nucleic Acids Res. 2003 Oct 1;31(19):5568-75. [PubMed
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
6252 |
| Enzyme 24 Name |
DNA polymerase mu |
| Enzyme 24 Synonyms |
- Pol Mu
|
| Enzyme 24 Gene Name |
POLM |
| Enzyme 24 Protein Sequence |
>DNA polymerase mu
MLPKRRRARVGSPSGDAASSTPPSTRFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLD
ACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWLTESLGAGQPVPVECR
HRLEVAGPRKGPLSPAWMPAYACQRPTPLTHHNTGLSEALEILAEAAGFEGSEGRLLTFC
RAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRSERYQTMKLF
TQIFGVGVKTADRWYREGLRTLDDLREQPQKLTQQQKAGLQHHQDLSTPVLRSDVDALQQ
VVEEAVGQALPGATVTLTGGFRRGKLQGHDVDFLITHPKEGQEAGLLPRVMCRLQDQGLI
LYHQHQHSCCESPTRLAQQSHMDAFERSFCIFRLPQPPGAAVGGSTRPCPSWKAVRVDLV
VAPVSQFPFALLGWTGSKLFQRELRRFSRKEKGLWLNSHGLFDPEQKTFFQAASEEDIFR
HLGLEYLPPEQRNA
|
| Enzyme 24 Number of Residues |
494 |
| Enzyme 24 Molecular Weight |
54816 |
| Enzyme 24 Theoretical pI |
8.50 |
| Enzyme 24 GO Classification |
| Function |
- DNA binding
- DNA nucleotidylexotransferase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
|
|
| Enzyme 24 General Function |
Replication, recombination and repair |
| Enzyme 24 Specific Function |
Seems to act as an Ig mutase which is responsible for immunoglobulin (Ig) gene hypermutation |
| Enzyme 24 Pathways |
|
| Enzyme 24 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 24 Pfam Domain Function |
Not Available |
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
6822168  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q9NP87  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
DPOLM_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>1485 bp
ATGCTCCCCAAACGGCGGCGAGCGCGGGTCGGGTCCCCTAGCGGCGATGCCGCTTCCTCC
ACGCCGCCCTCGACGCGCTTCCCGGGAGTCGCCATCTACCTGGTCGAGCCTCGCATGGGT
CGCAGCCGCCGGGCCTTCCTCACAGGCCTGGCGCGCTCCAAAGGCTTCCGCGTCCTTGAC
GCCTGCAGCTCCGAAGCGACACATGTTGTGATGGAAGAGACCTCAGCAGAGGAGGCCGTC
AGCTGGCAGGAGCGCAGGATGGCAGCTGCTCCCCCGGGTTGCACCCCCCCAGCTCTGCTG
GACATAAGCTGGTTAACAGAGAGCCTGGGAGCTGGGCAGCCTGTACCTGTGGAGTGCCGG
CACCGCCTGGAGGTGGCTGGGCCAAGGAAGGGGCCTCTGAGCCCAGCATGGATGCCTGCC
TATGCCTGCCAGCGCCCTACGCCCCTCACACACCACAACACTGGCCTCTCCGAGGCTCTG
GAGATACTGGCCGAGGCAGCAGGCTTTGAAGGCAGTGAGGGCCGCCTCCTCACCTTCTGC
AGAGCAGCCTCGGTGCTCAAGGCCCTTCCCAGCCCTGTCACAACCCTGAGCCAGCTGCAG
GGGCTTCCCCACTTTGGAGAACACTCCTCTAGGGTTGTCCAGGAGCTGCTGGAGCATGGA
GTGTGTGAGGAGGTGGAGAGAGTTCGGCGCTCAGAGAGGTACCAGACCATGAAGCTCTTC
ACCCAGATCTTCGGGGTCGGTGTGAAGACTGCTGACCGGTGGTACCGGGAAGGACTGCGA
ACCTTAGATGACCTCCGAGAGCAGCCCCAGAAACTAACCCAACAGCAGAAAGCGGGGCTC
CAGCACCACCAGGACCTGAGCACCCCAGTCCTGCGGTCCGATGTAGATGCCCTGCAGCAG
GTGGTGGAGGAAGCTGTGGGGCAGGCCCTGCCTGGGGCCACCGTCACGCTGACCGGCGGC
TTCCGCAGGGGGAAGTTGCAGGGCCATGACGTGGACTTCCTCATCACCCACCCCAAGGAG
GGTCAGGAGGCGGGGCTGCTGCCTAGAGTGATGTGCCGCCTGCAGGACCAGGGCCTCATC
CTGTACCACCAGCACCAGCACAGCTGCTGTGAGTCCCCTACCCGCCTGGCCCAACAGAGC
CACATGGACGCTTTTGAGAGAAGTTTCTGCATTTTCCGCCTACCACAACCTCCAGGGGCT
GCTGTGGGGGGATCCACGAGGCCCTGCCCATCCTGGAAGGCCGTGAGAGTGGACTTGGTA
GTTGCACCCGTCAGCCAGTTCCCTTTCGCCCTGCTCGGTTGGACTGGCTCCAAGCTTTTC
CAGCGGGAGCTGCGCCGCTTCAGCCGGAAGGAGAAGGGCCTGTGGCTGAACAGCCATGGG
CTGTTTGACCCGGAGCAGAAGACATTTTTCCAAGCGGCTTCAGAGGAAGACATCTTCAGA
CACCTGGGCCTTGAGTACCTTCCTCCAGAGCAGAGAAACGCCTGA
|
| Enzyme 24 GenBank Gene ID |
AJ131891  |
| Enzyme 24 GeneCard ID |
POLM  |
| Enzyme 24 GenAtlas ID |
POLM  |
| Enzyme 24 HGNC ID |
HGNC:9185  |
| Enzyme 24 Chromosome Location |
7 |
| Enzyme 24 Locus |
7p13 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Dominguez O, Ruiz JF, Lain de Lera T, Garcia-Diaz M, Gonzalez MA, Kirchhoff T, Martinez-A C, Bernad A, Blanco L: DNA polymerase mu (Pol mu), homologous to TdT, could act as a DNA mutator in eukaryotic cells. EMBO J. 2000 Apr 3;19(7):1731-42. [PubMed
]
- Aoufouchi S, Flatter E, Dahan A, Faili A, Bertocci B, Storck S, Delbos F, Cocea L, Gupta N, Weill JC, Reynaud CA: Two novel human and mouse DNA polymerases of the polX family. Nucleic Acids Res. 2000 Sep 15;28(18):3684-93. [PubMed
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
6254 |
| Enzyme 25 Name |
DNA polymerase epsilon subunit 3 |
| Enzyme 25 Synonyms |
- DNA polymerase II subunit 3
- DNA polymerase epsilon subunit p17
- Chromatin accessibility complex 17
- HuCHRAC17
- CHRAC-17
- Arsenic- transactivated protein
- AsTP
|
| Enzyme 25 Gene Name |
POLE3 |
| Enzyme 25 Protein Sequence |
>DNA polymerase epsilon subunit 3
MAERPEDLNLPNAVITRIIKEALPDGVNISKEARSAISRAASVFVLYATSCANNFAMKGK
RKTLNASDVLSAMEEMEFQRFVTPLKEALEAYRREQKGKKEASEQKKKDKDKKTDSEEQD
KSRDEDNDEDEERLEEEEQNEEEEVDN
|
| Enzyme 25 Number of Residues |
147 |
| Enzyme 25 Molecular Weight |
16860 |
| Enzyme 25 Theoretical pI |
4.38 |
| Enzyme 25 GO Classification |
| Function |
- DNA binding
- binding
- nucleic acid binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 25 General Function |
Chromatin structure and dynamics |
| Enzyme 25 Specific Function |
Forms a complex with DNA polymerase epsilon subunit CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodelling activity of ISWI/SNF2H and ACF1 |
| Enzyme 25 Pathways |
|
| Enzyme 25 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
8100806  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
Q9NRF9  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
DPOE3_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>444 bp
ATGGCGGAGAGGCCCGAGGACCTAAACCTGCCCAATGCCGTGATCACCAGGATCATCAAG
GAGGCGCTCCCGGACGGTGTCAACATCTCCAAGGAGGCCCGGAGCGCCATCTCCCGCGCC
GCCAGCGTCTTCGTGCTGTACGCCACATCCTGTGCTAACAACTTTGCAATGAAAGGAAAG
CGGAAGACGCTGAATGCCAGTGATGTGCTCTCAGCCATGGAAGAGATGGAGTTCCAGCGG
TTCGTTACCCCATTGAAAGAAGCTCTGGAAGCATATAGGCGGGAGCAGAAAGGCAAGAAG
GAGGCCTCAGAGCAAAAGAAGAAGGACAAAGACAAAAAAACAGACTCGGAAGAGCAAGAC
AAGAGCAGGGATGAGGACAATGATGAAGACGAAGAAAGGCTGGAAGAAGAAGAACAGAAT
GAAGAGGAAGAAGTAGACAACTGA
|
| Enzyme 25 GenBank Gene ID |
AF226077  |
| Enzyme 25 GeneCard ID |
POLE3  |
| Enzyme 25 GenAtlas ID |
POLE3  |
| Enzyme 25 HGNC ID |
HGNC:13546  |
| Enzyme 25 Chromosome Location |
9 |
| Enzyme 25 Locus |
9q33 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Poot RA, Dellaire G, Hulsmann BB, Grimaldi MA, Corona DF, Becker PB, Bickmore WA, Varga-Weisz PD: HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1 and two novel histone-fold proteins. EMBO J. 2000 Jul 3;19(13):3377-87. [PubMed
]
- Li Y, Pursell ZF, Linn S: Identification and cloning of two histone fold motif-containing subunits of HeLa DNA polymerase epsilon. J Biol Chem. 2000 Jul 28;275(30):23247-52. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
6256 |
| Enzyme 26 Name |
DNA polymerase subunit gamma 1 |
| Enzyme 26 Synonyms |
- Mitochondrial DNA polymerase catalytic subunit
- PolG-alpha
|
| Enzyme 26 Gene Name |
POLG |
| Enzyme 26 Protein Sequence |
>DNA polymerase subunit gamma 1
MSRLLWRKVAGATVGPGPVPAPGRWVSSSVPASDPSDGQRRRQQQQQQQQQQQQQPQQPQ
VLSSEGGQLRHNPLDIQMLSRGLHEQIFGQGGEMPGEAAVRRSVEHLQKHGLWGQPAVPL
PDVELRLPPLYGDNLDQHFRLLAQKQSLPYLEAANLLLQAQLPPKPPAWAWAEGWTRYGP
EGEAVPVAIPEERALVFDVEVCLAEGTCPTLAVAISPSAWYSWCSQRLVEERYSWTSQLS
PADLIPLEVPTGASSPTQRDWQEQLVVGHNVSFDRAHIREQYLIQGSRMRFLDTMSMHMA
ISGLSSFQRSLWIAAKQGKHKVQPPTKQGQKSQRKARRGPAISSWDWLDISSVNSLAEVH
RLYVGGPPLEKEPRELFVKGTMKDIRENFQDLMQYCAQDVWATHEVFQQQLPLFLERCPH
PVTLAGMLEMGVSYLPVNQNWERYLAEAQGTYEELQREMKKSLMDLANDACQLLSGERYK
EDPWLWDLEWDLQEFKQKKAKKVKKEPATASKLPIEGAGAPGDPMDQEDLGPCSEEEEFQ
QDVMARACLQKLKGTTELLPKRPQHLPGHPGWYRKLCPRLDDPAWTPGPSLLSLQMRVTP
KLMALTWDGFPLHYSERHGWGYLVPGRRDNLAKLPTGTTLESAGVVCPYRAIESLYRKHC
LEQGKQQLMPQEAGLAEEFLLTDNSAIWQTVEELDYLEVEAEAKMENLRAAVPGQPLALT
ARGGPKDTQPSYHHGNGPYNDVDIPGCWFFKLPHKDGNSCNVGSPFAKDFLPKMEDGTLQ
AGPGGASGPRALEINKMISFWRNAHKRISSQMVVWLPRSALPRAVIRHPDYDEEGLYGAI
LPQVVTAGTITRRAVEPTWLTASNARPDRVGSELKAMVQAPPGYTLVGADVDSQELWIAA
VLGDAHFAGMHGCTAFGWMTLQGRKSRGTDLHSKTATTVGISREHAKIFNYGRIYGAGQP
FAERLLMQFNHRLTQQEAAEKAQQMYAATKGLRWYRLSDEGEWLVRELNLPVDRTEGGWI
SLQDLRKVQRETARKSQWKKWEVVAERAWKGGTESEMFNKLESIATSDIPRTPVLGCCIS
RALEPSAVQEEFMTSRVNWVVQSSAVDYLHLMLVAMKWLFEEFAIDGRFCISIHDEVRYL
VREEDRYRAALALQITNLLTRCMFAYKLGLNDLPQSVAFFSAVDIDRCLRKEVTMDCKTP
SNPTGMERRYGIPQGEALDIYQIIELTKGSLEKRSQPGP
|
| Enzyme 26 Number of Residues |
1239 |
| Enzyme 26 Molecular Weight |
139564 |
| Enzyme 26 Theoretical pI |
6.89 |
| Enzyme 26 GO Classification |
| Function |
- DNA binding
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- gamma DNA-directed DNA polymerase activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
- gamma DNA polymerase complex
- protein complex
|
|
| Enzyme 26 General Function |
Replication, recombination and repair |
| Enzyme 26 Specific Function |
Involved in the replication of mitochondrial DNA |
| Enzyme 26 Pathways |
|
| Enzyme 26 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
1399956  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
P54098  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
DPOG1_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>3720 bp
ATGAGCCGCCTGCTCTGGAGGAAGGTGGCCGGCGCCACCGTCGGGCCAGGGCCGGTTCCA
GCTCCGGGGCGCTGGGTCTCCAGCTCCGTCCCCGCGTCCGACCCCAGCGACGGGCAGCGG
CGGCGGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAACAGCAGCCTCAGCAGCCGCAA
GTGCTATCCTCGGAGGGCGGGCAGCTGCGGCACAACCCATTGGACATCCAGATGCTCTCG
AGAGGGCTGCACGAGCAAATCTTCGGGCAAGGAGGGGAGATGCCTGGCGAGGCCGCGGTG
CGCCGCAGCGTCGAGCACCTGCAGAAGCACGGGCTCTGGGGGCAGCCAGCCGTGCCCTTG
CCCGACGTGGAGCTGCGCCTGCCGCCCCTCTACGGGGACAACCTGGACCAGCACTTCCGC
CTCCTGGCCCAGAAGCAGAGCCTGCCCTACCTGGAGGCGGCCAACTTGCTGTTGCAGGCC
CAGCTGCCCCCGAAGCCCCCGGCTTGGGCCTGGGCGGAGGGCTGGACCCGGTACGGCCCC
GAGGGGGAGGCCGTACCCGTGGCCATCCCCGAGGAGCGGGCCCTGGTGTTCGACGTGGAG
GTCTGCTTGGCAGAGGGAACTTGCCCCACATTGGCGGTGGCCATATCCCCCTCGGCCTGG
TATTCCTGGTGCAGCCAGCGGCTGGTGGAAGAGCGTTACTCTTGGACCAGCCAGCTGTCG
CCGGCTGACCTCATCCCCCTGGAGGTCCCTACTGGTGCCAGCAGCCCCACCCAGAGAGAC
TGGCAGGAGCAGTTAGTGGTGGGGCACAATGTTTCCTTTGACCGAGCTCATATCAGGGAG
CAGTACCTGATCCAGGGTTCCCGCATGCGTTTCCTGGACACCATGAGCATGCACATGGCC
ATCTCAGGGCTAAGCAGCTTCCAGCGCAGTCTGTGGATAGCAGCCAAGCAGGGCAAACAC
AAGGTCCAGCCCCCCACAAAGCAAGGCCAGAAGTCCCAGAGGAAAGCCAGAAGAGGCCCA
GCGATCTCATCCTGGGACTGGCTGGACATCAGCAGTGTCAACAGTCTGGCAGAGGTGCAC
AGACTTTATGTAGGGGGGCCTCCCTTAGAGAAGGAGCCTCGAGAACTGTTTGTGAAGGGC
ACCATGAAGGACATTCGTGAGAACTTCCAGGACCTGATGCAGTACTGTGCCCAGGACGTG
TGGGCCACCCATGAGGTTTTCCAGCAGCAGCTACCGCTCTTCTTGGAGAGGTGTCCCCAC
CCAGTGACTCTGGCCGGCATGCTGGAGATGGGTGTCTCCTACCTGCCTGTCAACCAGAAC
TGGGAGCGTTACCTGGCAGAGGCACAGGGCACTTATGAGGAGCTCCAGCGGGAGATGAAG
AAGTCGTTGATGGATCTGGCCAATGATGCCTGCCAGCTGCTCTCAGGAGAGAGGTACAAA
GAAGACCCCTGGCTCTGGGACCTGGAGTGGGACCTGCAAGAATTTAAGCAGAAGAAAGCT
AAGAAGGTGAAGAAGGAACCAGCCACAGCCAGCAAGTTGCCCATCGAGGGGGCTGGGGCC
CCTGGTGATCCCATGGATCAGGAAGACCTCGGCCCCTGCAGTGAGGAGGAGGAGTTTCAA
CAAGATGTCATGGCCCGCGCCTGCTTGCAGAAGCTGAAGGGGACCACAGAGCTCCTGCCC
AAGCGGCCCCAGCACCTTCCTGGACACCCTGGATGGTACCGGAAGCTCTGCCCCCGGCTA
GACGACCCTGCATGGACCCCGGGCCCCAGCCTCCTCAGCCTGCAGATGCGGGTCACACCT
AAACTCATGGCACTTACCTGGGATGGCTTCCCTCTGCACTACTCAGAGCGTCATGGCTGG
GGCTACTTGGTGCCTGGGCGGCGGGACAACCTGGCCAAGCTGCCGACAGGTACCACCCTG
GAGTCAGCTGGGGTGGTCTGCCCCTACAGAGCCATCGAGTCCCTGTACAGGAAGCACTGT
CTCGAACAGGGGAAGCAGCAGCTGATGCCCCAGGAGGCCGGCCTGGCGGAGGAGTTCCTG
CTCACTGACAATAGTGCCATATGGCAAACGGTAGAAGAACTGGATTACTTAGAAGTGGAG
GCTGAGGCCAAGATGGAGAACTTGCGAGCTGCAGTGCCAGGTCAACCCCTAGCTCTGACT
GCCCGTGGTGGCCCCAAGGACACCCAGCCCAGCTATCACCATGGCAATGGACCTTACAAC
GACGTGGACATCCCTGGCTGCTGGTTTTTCAAGCTGCCTCACAAGGATGGTAATAGCTGT
AATGTGGGAAGCCCCTTTGCCAAGGACTTCCTGCCCAAGATGGAGGATGGCACCCTGCAG
GCTGGCCCAGGAGGTGCCAGTGGGCCCCGTGCTCTGGAAATCAACAAAATGATTTCTTTC
TGGAGGAACGCCCATAAACGTATCAGCTCCCAGATGGTGGTGTGGCTGCCCAGGTCAGCT
CTGCCCCGTGCTGTGATCAGGCACCCCGACTATGATGAGGAAGGCCTCTATGGGGCCATC
CTGCCCCAAGTGGTGACTGCCGGCACCATCACTCGCCGGGCTGTGGAGCCCACATGGCTC
ACCGCCAGCAATGCCCGGCCTGACCGAGTAGGCAGTGAGTTGAAAGCCATGGTGCAGGCC
CCACCTGGCTACACCCTTGTGGGTGCTGATGTGGACTCCCAAGAGCTGTGGATTGCAGCT
GTGCTTGGAGACGCCCACTTTGCCGGCATGCATGGCTGCACAGCCTTTGGGTGGATGACA
CTGCAGGGCAGGAAGAGCAGGGGCACTGATCTACACAGTAAGACAGCCACTACTGTGGGC
ATCAGCCGTGAGCATGCCAAAATCTTCAACTACGGCCGCATCTATGGTGCTGGGCAGCCC
TTTGCTGAGCGCTTACTAATGCAGTTTAACCACCGGCTCACACAGCAGGAGGCAGCTGAG
AAGGCCCAGCAGATGTACGCTGCCACCAAGGGCCTCCGCTGGTATCGGCTGTCGGATGAG
GGCGAGTGGCTGGTGAGGGAGTTGAACCTCCCAGTGGACAGGACTGAGGGTGGCTGGATT
TCCCTGCAGGATCTGCGCAAGGTCCAGAGAGAAACTGCAAGGAAGTCACAGTGGAAGAAG
TGGGAGGTGGTTGCTGAACGGGCATGGAAGGGGGGCACAGAGTCAGAAATGTTCAATAAG
CTTGAGAGCATTGCTACGTCTGACATACCACGTACCCCGGTGCTGGGCTGCTGCATCAGC
CGAGCCCTGGAGCCCTCGGCTGTCCAGGAAGAGTTTATGACCAGCCGTGTGAATTGGGTG
GTACAGAGCTCTGCTGTTGACTACTTACACCTCATGCTTGTGGCCATGAAGTGGCTGTTT
GAAGAGTTTGCCATAGATGGGCGCTTCTGCATCAGCATCCATGACGAGGTTCGCTACCTG
GTGCGGGAGGAGGACCGCTACCGCGCTGCCCTGGCCTTGCAGATCACCAACCTCTTGACC
AGGTGCATGTTTGCCTACAAGCTGGGTCTGAATGACTTGCCCCAGTCAGTCGCCTTTTTC
AGTGCAGTCGATATTGACCGGTGCCTCAGGAAGGAAGTGACCATGGATTGTAAAACCCCT
TCCAACCCAACTGGGATGGAAAGGAGATACGGGATTCCCCAGGGTGAAGCGCTGGATATT
TACCAGATAATTGAACTCACCAAAGGCTCCTTGGAAAAACGAAGCCAGCCTGGACCATAG
|
| Enzyme 26 GenBank Gene ID |
U60325  |
| Enzyme 26 GeneCard ID |
POLG  |
| Enzyme 26 GenAtlas ID |
POLG  |
| Enzyme 26 HGNC ID |
HGNC:9179  |
| Enzyme 26 Chromosome Location |
15 |
| Enzyme 26 Locus |
15q25 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- Ropp PA, Copeland WC: Cloning and characterization of the human mitochondrial DNA polymerase, DNA polymerase gamma. Genomics. 1996 Sep 15;36(3):449-58. [PubMed
]
- Lecrenier N, Van Der Bruggen P, Foury F: Mitochondrial DNA polymerases from yeast to man: a new family of polymerases. Gene. 1997 Jan 31;185(1):147-52. [PubMed
]
- Van Goethem G, Dermaut B, Lofgren A, Martin JJ, Van Broeckhoven C: Mutation of POLG is associated with progressive external ophthalmoplegia characterized by mtDNA deletions. Nat Genet. 2001 Jul;28(3):211-2. [PubMed
]
- Van Goethem G, Martin JJ, Dermaut B, Lofgren A, Wibail A, Ververken D, Tack P, Dehaene I, Van Zandijcke M, Moonen M, Ceuterick C, De Jonghe P, Van Broeckhoven C: Recessive POLG mutations presenting with sensory and ataxic neuropathy in compound heterozygote patients with progressive external ophthalmoplegia. Neuromuscul Disord. 2003 Feb;13(2):133-42. [PubMed
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
6257 |
| Enzyme 27 Name |
DNA polymerase iota |
| Enzyme 27 Synonyms |
- RAD30 homolog B
- Eta2
|
| Enzyme 27 Gene Name |
POLI |
| Enzyme 27 Protein Sequence |
>DNA polymerase iota
MELADVGAAASSQGVHDQVLPTPNASSRVIVHVDLDCFYAQVEMISNPELKDKPLGVQQK
YLVVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGEDLTRYREMSYKVTELLEEFSPVV
ERLGFDENFVDLTEMVEKRLQQLQSDELSAVTVSGHVYNNQSINLLDVLHIRLLVGSQIA
AEMREAMYNQLGLTGCAGVASNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNHIKEIP
GIGYKTAKCLEALGINSVRDLQTFSPKILEKELGISVAQRIQKLSFGEDNSPVILSGPPQ
SFSEEDSFKKCSSEVEAKNKIEELLASLLNRVCQDGRKPHTVRLIIRRYSSEKHYGRESR
QCPIPSHVIQKLGTGNYDVMTPMVDILMKLFRNMVNVKMPFHLTLLSVCFCNLKALNTAK
KGLIDYYLMPSLSTTSRSGKHSFKMKDTHMEDFPKDKETNRDFLPSGRIESTRTRESPLD
TTNFSKEKDINEFPLCSLPEGVDQEVFKQLPVDIQEEILSGKSREKFQGKGSVSCPLHAS
RGVLSFFSKKQMQDIPINPRDHLSSSKQVSSVSPCEPGTSGFNSSSSSYMSSQKDYSYYL
DNRLKDERISQGPKEPQGFHFTNSNPAVSAFHSFPNLQSEQLFSRNHTTDSHKQTVATDS
HEGLTENREPDSVDEKITFPSDIDPQVFYELPEAVQKELLAEWKRTGSDFHIGHK
|
| Enzyme 27 Number of Residues |
715 |
| Enzyme 27 Molecular Weight |
80347 |
| Enzyme 27 Theoretical pI |
6.82 |
| Enzyme 27 GO Classification |
| Function |
- DNA binding
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- ion binding
- magnesium ion binding
- metal ion binding
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA repair
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 27 General Function |
Replication, recombination and repair |
| Enzyme 27 Specific Function |
Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunogobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity |
| Enzyme 27 Pathways |
|
| Enzyme 27 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
5739208  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
Q9UNA4  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
POLI_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>2148 bp
ATGGAACTGGCGGACGTGGGGGCGGCAGCCAGCTCGCAGGGAGTTCATGATCAAGTGTTG
CCCACACCAAATGCTTCATCCAGAGTCATAGTACATGTGGATCTGGATTGCTTTTATGCA
CAAGTAGAAATGATCTCAAATCCAGAGCTAAAAGACAAACCTTTAGGGGTTCAACAGAAA
TATTTGGTGGTTACCTGCAACTATGAAGCTAGGAAACTTGGAGTTAAGAAACTTATGAAT
GTCAGAGATGCAAAAGAAAAGTGTCCACAGTTGGTATTAGTTAATGGAGAAGACCTGACC
CGCTACAGAGAAATGTCTTATAAGGTTACAGAATTACTGGAAGAATTTAGTCCAGTTGTT
GAGAGACTTGGATTTGATGAAAATTTTGTGGATCTAACAGAAATGGTTGAGAAGAGACTA
CAGCAGCTGCAAAGTGATGAACTTTCTGCGGTGACTGTGTCGGGTCATGTATACAATAAT
CAGTCTATAAACCTGCTTGACGTCTTGCACATCAGACTACTTGTTGGATCTCAGATTGCA
GCAGAGATGCGGGAAGCCATGTATAATCAGTTGGGGCTCACTGGCTGTGCTGGAGTGGCT
TCTAATAAACTGTTGGCAAAATTAGTTTCTGGTGTCTTTAAACCAAATCAACAAACAGTC
TTATTACCTGAAAGTTGTCAACATCTTATTCATAGTTTGAATCACATAAAGGAAATACCT
GGTATTGGCTATAAAACTGCCAAATGTCTTGAAGCACTGGGTATCAATAGTGTGCGTGAT
CTCCAAACCTTTTCACCCAAAATTTTAGAAAAAGAATTAGGAATTTCAGTTGCTCAGCGT
ATCCAAAAGCTCAGTTTTGGAGAGGATAACTCCCCTGTGATACTCTCAGGACCACCTCAG
TCCTTTAGTGAAGAAGATTCATTTAAAAAATGTTCATCTGAAGTTGAAGCTAAAAATAAG
ATTGAAGAACTACTTGCTAGTCTTTTAAACAGAGTATGCCAAGATGGAAGGAAGCCTCAT
ACAGTGAGATTAATAATCCGTCGGTATTCCTCTGAGAAGCACTATGGTCGTGAGAGTCGT
CAGTGCCCTATTCCTTCACATGTAATTCAGAAATTAGGGACAGGAAATTATGATGTGATG
ACCCCAATGGTTGATATACTTATGAAACTTTTTCGAAATATGGTGAATGTGAAGATGCCA
TTTCACCTTACCCTTCTAAGTGTGTGCTTCTGCAACCTTAAAGCACTAAATACTGCTAAG
AAAGGGCTTATTGATTATTATTTAATGCCATCATTATCAACTACTTCACGCTCTGGCAAG
CACAGTTTTAAAATGAAAGACACTCATATGGAAGATTTTCCCAAAGACAAAGAAACAAAC
CGGGATTTCCTACCAAGTGGAAGAATTGAAAGTACAAGAACTAGGGAGTCTCCACTAGAT
ACCACAAATTTTTCTAAAGAAAAAGACATTAATGAATTCCCACTCTGTTCACTTCCTGAA
GGTGTTGACCAAGAAGTCTTCAAGCAGCTTCCAGTAGATATTCAAGAAGAAATCCTTTCT
GGAAAATCTAGGGAAAAATTTCAAGGGAAAGGAAGTGTGAGTTGTCCATTACATGCCTCT
AGAGGAGTATTATCTTTCTTTTCTAAAAAACAAATGCAAGATATTCCCATAAATCCTAGA
GATCATTTATCCAGTAGCAAACAGGTATCCTCTGTATCTCCTTGTGAACCGGGAACATCA
GGCTTTAATAGCAGTAGTTCTTCTTACATGTCTAGCCAAAAGGATTATTCATATTATTTA
GATAATAGATTAAAAGATGAACGAATAAGTCAAGGACCTAAAGAACCTCAAGGATTCCAC
TTTACAAATTCAAACCCTGCTGTGTCTGCTTTTCATTCATTTCCAAACTTGCAGAGTGAG
CAACTTTTCTCCAGAAACCACACTACAGATAGCCATAAGCAAACAGTAGCAACAGACTCT
CATGAAGGACTTACAGAAAATAGAGAGCCAGATTCTGTTGATGAGAAAATTACTTTCCCT
TCTGACATTGATCCTCAAGTTTTCTATGAACTACCAGAAGCAGTACAAAAGGAACTGCTG
GCAGAGTGGAAGAGAACAGGATCAGATTTCCACATTGGACATAAATAA
|
| Enzyme 27 GenBank Gene ID |
AF140501  |
| Enzyme 27 GeneCard ID |
POLI  |
| Enzyme 27 GenAtlas ID |
POLI  |
| Enzyme 27 HGNC ID |
HGNC:9182  |
| Enzyme 27 Chromosome Location |
18 |
| Enzyme 27 Locus |
18q21.1 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- McDonald JP, Rapic-Otrin V, Epstein JA, Broughton BC, Wang X, Lehmann AR, Wolgemuth DJ, Woodgate R: Novel human and mouse homologs of Saccharomyces cerevisiae DNA polymerase eta. Genomics. 1999 Aug 15;60(1):20-30. [PubMed
]
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed
]
- Tissier A, Frank EG, McDonald JP, Iwai S, Hanaoka F, Woodgate R: Misinsertion and bypass of thymine-thymine dimers by human DNA polymerase iota. EMBO J. 2000 Oct 2;19(19):5259-66. [PubMed
]
- Bebenek K, Tissier A, Frank EG, McDonald JP, Prasad R, Wilson SH, Woodgate R, Kunkel TA: 5'-Deoxyribose phosphate lyase activity of human DNA polymerase iota in vitro. Science. 2001 Mar 16;291(5511):2156-9. [PubMed
]
- Frank EG, Tissier A, McDonald JP, Rapic-Otrin V, Zeng X, Gearhart PJ, Woodgate R: Altered nucleotide misinsertion fidelity associated with poliota-dependent replication at the end of a DNA template. EMBO J. 2001 Jun 1;20(11):2914-22. [PubMed
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
6258 |
| Enzyme 28 Name |
DNA polymerase epsilon subunit 2 |
| Enzyme 28 Synonyms |
- DNA polymerase II subunit 2
- DNA polymerase epsilon subunit B
|
| Enzyme 28 Gene Name |
POLE2 |
| Enzyme 28 Protein Sequence |
>DNA polymerase epsilon subunit 2
MAPERLRSRALSAFKLRGLLLRGEAIKYLTEALQSISELELEDKLEKIINAVEKQPLSSN
MIERSVVEAAVQECSQSVDETIEHVFNIIGAFDIPRFVYNSERKKFLPLLMTNHPAPNLF
GTPRDKAEMFRERYTILHQRTHRHELFTPPVIGSHPDESGSKFQLKTIETLLGSTTKIGD
AIVLGMITQLKEGKFFLEDPTGTVQLDLSKAQFHSGLYTEACFVLAEGWFEDQVFHVNAF
GFPPTEPSSTTRAYYGNINFFGGPSNTSVKTSAKLKQLEEENKDAMFVFLSDVWLDQVEV
LEKLRIMFAGYSPAPPTCFILCGNFSSAPYGKNQVQALKDSLKTLADIICEYPDIHQSSR
FVFVPGPEDPGFGSILPRPPLAESITNEFRQRVPFSVFTTNPCRIQYCTQEITVFREDLV
NKMCRNCVRFPSSNLAIPNHFVKTILSQGHLTPLPLYVCPVYWAYDYALRVYPVPDLLVI
ADKYDPFTTTNTECLCINPGSFPRSGFSFKVFYPSNKTVEDSKLQGF
|
| Enzyme 28 Number of Residues |
527 |
| Enzyme 28 Molecular Weight |
59538 |
| Enzyme 28 Theoretical pI |
6.30 |
| Enzyme 28 GO Classification |
| Function |
- DNA binding
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 28 General Function |
Not Available |
| Enzyme 28 Specific Function |
Participates in DNA repair and in chromosomal DNA replication |
| Enzyme 28 Pathways |
|
| Enzyme 28 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
Not Available |
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
2697123  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
P56282  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
DPOE2_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>1581 bp
ATGGCGCCGGAGCGGCTGCGGAGCCGGGCGCCCTCCGCCTTCAAGTTGCGGGGCTTGCTG
CTCCGTGGTGAAGCTATTAAGTACCTCACAGAAGCTCTTCAGTCTATCAGTGAATTAGAG
CTTGAAGATAAACTGGAAAAGATAATTAATGCAGTTGAGAAGCAACCCTTGTCATCAAAC
ATGATTGAACGATCTGTGGTGGAAGCAGCAGTCCAGGAATGCAGTCAGTCTGTTGATGAA
ACTATAGAGCACGTTTTCAATATCATAGGAGCATTTGATATTCCACGCTTTGTGTACAAT
TCAGAAAGAAAAAAATTTCTTCCTCTGTTAATGACCAACCACCCTGCACCAAATTTATTT
GGAACACCAAGAGATAAAGCAGAGATGTTTCGTGAGCGATATACCATTTTGCACCAGAGG
ACCCACAGGCATGAATTATTTACTCCTCCGGTGATAGGTTCTCACCCTGATGAAAGCGGA
AGCAAATTCCAGCTTAAAACAATAGAAACCTTATTGGGTAGTACAACCAAAATCGGAGAT
GCGATTGTTCTTGGAATGATAACGCAGTTAAAAGAGGGAAAATTTTTTCTGGAAGATCCT
ACTGGAACAGTCCAACTAGACCTTAGTAAAGCTCAGTTCCATAGTGGTTTATACACAGAG
GCATGCTTTGTCTTAGCAGAAGGTTGGTTTGAAGATCAAGTGTTTCATGTCAATGCCTTT
GGATTTCCACCCACTGAGCCCTCTAGTACTACTAGGGCATACTATGGAAATATTAATTTT
TTTGGAGGTCCTTCTAATACATCTGTGAAGACTTCTGCAAAACTAAAACAGCTAGAAGAG
GAGAATAAAGATGCTATGTTTGTGTTTTTATCTGATGTTTGGTTGGACCAGGTGGAAGTA
TTGGAAAAACTTCGCATAATGTTTGCTGGTTATTCACCAGCACCTCCAACCTGCTTTATT
CTGTGTGGTAATTTTTCATCTGCACCATATGGAAAAAATCAAGTTCAAGCTTTGAAAGAT
TCCCTAAAAACTTTGGCAGATATAATATGTGAATACCCAGATATTCACCAAAGTCGTTTT
GTGTTTGTACCTGGTCCAGAGGATCCTGGATTTGGTTCCATCTTACCAAGGCCACCACTT
GCTGAAAGCATCACTAATGAATTCAGACAAAGGGTACCATTTTCAGTTTTTACTACTAAT
CCTTGCAGAATTCAGTACTGTACACAGGAAATTACTGTCTTCCGTGAAGACTTAGTAAAT
AAAATGTGCAGAAACTGCGTCCGTTTTCCTAGCAGCAATTTGGCTATTCCTAATCACTTT
GTAAAGACTATCTTATCCCAAGGACATCTGACTCCCCTACCTCTTTATGTCTGCCCAGTG
TATTGGGCATATGACTATGCTTTGAGAGTGTATCCTGTGCCCGATCTACTTGTCATTGCA
GACAAATATGATCCTTTCACTACGACAAATACCGAATGCCTCTGCATAAACCCTGGCTCT
TTTCCAAGAAGTGGATTTTCATTCAAAGTTTTTTATCCTTCTAATAAGACAGTAGAAGAT
AGCAAACTTCAAGGCTTTTGA
|
| Enzyme 28 GenBank Gene ID |
AF025840  |
| Enzyme 28 GeneCard ID |
POLE2  |
| Enzyme 28 GenAtlas ID |
POLE2  |
| Enzyme 28 HGNC ID |
HGNC:9178  |
| Enzyme 28 Chromosome Location |
14 |
| Enzyme 28 Locus |
14q21-q22 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- Li Y, Asahara H, Patel VS, Zhou S, Linn S: Purification, cDNA cloning, and gene mapping of the small subunit of human DNA polymerase epsilon. J Biol Chem. 1997 Dec 19;272(51):32337-44. [PubMed
]
- Jokela M, Makiniemi M, Lehtonen S, Szpirer C, Hellman U, Syvaoja JE: The small subunits of human and mouse DNA polymerase epsilon are homologous to the second largest subunit of the yeast Saccharomyces cerevisiae DNA polymerase epsilon. Nucleic Acids Res. 1998 Feb 1;26(3):730-4. [PubMed
]
- Huang D, Jokela M, Tuusa J, Skog S, Poikonen K, Syvaoja JE: E2F mediates induction of the Sp1-controlled promoter of the human DNA polymerase epsilon B-subunit gene POLE2. Nucleic Acids Res. 2001 Jul 1;29(13):2810-21. [PubMed
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
8075 |
| Enzyme 29 Name |
Uridine-cytidine kinase 2 |
| Enzyme 29 Synonyms |
- UCK 2
- Uridine monophosphokinase 2
- Cytidine monophosphokinase 2
|
| Enzyme 29 Gene Name |
UCK2 |
| Enzyme 29 Protein Sequence |
>Uridine-cytidine kinase 2
MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYRQKQVVILS
QDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELILKTLKEITEGKTVQIPVYDFVSHSRK
EETVTVYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ
ILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGPSKRQTNG
CLNGYTPSRKRQASESSSRPH
|
| Enzyme 29 Number of Residues |
261 |
| Enzyme 29 Molecular Weight |
29299 |
| Enzyme 29 Theoretical pI |
6.68 |
| Enzyme 29 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside kinase activity
- nucleotide binding
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- uridine kinase activity
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 29 General Function |
Nucleotide transport and metabolism |
| Enzyme 29 Specific Function |
Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, 4-N-acetylcytidine, 4-N- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and 4-N-anisoylcytidine |
| Enzyme 29 Pathways |
|
| Enzyme 29 Reactions |
- ATP + uridine = ADP + UMP
|
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
1655420  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
Q9BZX2  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
UCK2_HUMAN  |
| Enzyme 29 PDB ID |
1XRJ  |
| Enzyme 29 PDB File |
Show |
| Enzyme 29 3D Structure |
|
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>336 bp
ATGAAGCTTTTTGTGGATACAGATGCGGACACCCGGCTCTCACGCAGAGTATTAAGGGAC
ATCAGCGAGAGAGGCAGGGATCTTGAGCAGATTTTATCTCAGTACATTACGTTCGTCAAG
CCTGCCTTTGAGGAATTCTGCTTGCCAACAAAGCAGTATGCTGATGTGATCATCCCTAGA
GGTGCAGATAATCTGGTGGCCATCAACCTCATCGAGCAGCACATCCAGGACATCCTGAAT
GGAGGGCCCTCCAAACGGCAGACCAATGGCTGTCTCAACGGCTACACCCCTTCACGCAAG
AGGCAGGCATCGGAGTCCAGCAGCAGGCCGCATTGA
|
| Enzyme 29 GenBank Gene ID |
D78335  |
| Enzyme 29 GeneCard ID |
UCK2  |
| Enzyme 29 GenAtlas ID |
UCK2  |
| Enzyme 29 HGNC ID |
HGNC:12562  |
| Enzyme 29 Chromosome Location |
1 |
| Enzyme 29 Locus |
1q23 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- Ozaki K, Kuroki T, Hayashi S, Nakamura Y: Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a differential mRNA display method. Genomics. 1996 Sep 1;36(2):316-9. [PubMed
]
- Van Rompay AR, Norda A, Linden K, Johansson M, Karlsson A: Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases. Mol Pharmacol. 2001 May;59(5):1181-6. [PubMed
]
- Koizumi K, Shimamoto Y, Azuma A, Wataya Y, Matsuda A, Sasaki T, Fukushima M: Cloning and expression of uridine/cytidine kinase cDNA from human fibrosarcoma cells. Int J Mol Med. 2001 Sep;8(3):273-8. [PubMed
]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
13098 |
| Enzyme 30 Name |
Uridine/cytidine kinase-like 1 |
| Enzyme 30 Synonyms |
Not Available |
| Enzyme 30 Gene Name |
UCKL1 |
| Enzyme 30 Protein Sequence |
>Uridine/cytidine kinase-like 1
MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDRSNAESLDRLLPPVGTGRSPRKR
TTSQCKSEPPLLRTSKRTIYTAGRPPWYNEHGTQSKEAFAIGLGGGSASGKTTVARMIIE
ALDVPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV
PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRR
DISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQL
EERELSVRAALASAHQCHPLPRTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRL
LIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIG
TILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIF
LLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTDAVPDGSD
EEEVAYTG
|
| Enzyme 30 Number of Residues |
548 |
| Enzyme 30 Molecular Weight |
61142 |
| Enzyme 30 Theoretical pI |
7.40 |
| Enzyme 30 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside kinase activity
- nucleotide binding
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- uridine kinase activity
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 30 General Function |
Nucleotide transport and metabolism |
| Enzyme 30 Specific Function |
May contribute to UTP accumulation needed for blast transformation and proliferation |
| Enzyme 30 Pathways |
|
| Enzyme 30 Reactions |
- ATP + uridine = ADP + UMP [RN:R00964] ALL_REAC R00964
- (other) R00513 R00516 R00517 R00962 R00967 R00968 R00970 R01548 R01549 R01880 R02091 R02096 R02097 R02327 R02332 R02371 R02372
|
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
38228699  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
Q9NWZ5  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
UCKL1_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
Not Available |
| Enzyme 30 GenBank Gene ID |
AJ605558  |
| Enzyme 30 GeneCard ID |
Q9NWZ5  |
| Enzyme 30 GenAtlas ID |
UCKL1  |
| Enzyme 30 HGNC ID |
HGNC:15938  |
| Enzyme 30 Chromosome Location |
Not Available |
| Enzyme 30 Locus |
Not Available |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Kashuba E, Kashuba V, Sandalova T, Klein G, Szekely L: Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferase. BMC Cell Biol. 2002 Aug 29;3:23. Epub 2002 Aug 29. [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
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
13379 |
| Enzyme 31 Name |
Ectonucleoside triphosphate diphosphohydrolase 8 |
| Enzyme 31 Synonyms |
- NTPDase 8
- NTPDase8
- E-NTPDase 8
|
| Enzyme 31 Gene Name |
ENTPD8 |
| Enzyme 31 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 8
MGLSRKEQVFLALLGASGVSGLTALILLLVEATSVLLPTDIKFGIVFDAGSSHTSLFLYQ
WLANKENGTGVVSQALACQVEGPGISSYTSNAAQAGESLQGCLEEALVLIPEAQHRKTPT
FLGATAGMRLLSRKNSSQARDIFAAVTQVLGRSPVDFWGAELLAGQAEGAFGWITVNYGL
GTLVKYSFTGEWIQPPEEMLVGALDMGGASTQITFVPGGPILDKSTQADFRLYGSDYSVY
THSYLCFGRDQMLSRLLVGLVQSRPAALLRHPCYLSGYQTTLALGPLYESPCVHATPPLS
LPQNLTVEGTGNPGACVSAIRELFNFSSCQGQEDCAFDGVYQPPLRGQFYAFSNFYYTFH
FLNLTSRQPLSTVNATIWEFCQRPWKLVEASYPGQDRWLRDYCASGLYILTLLHEGYGFS
EETWPSLEFRKQAGGVDIGWTLGYMLNLTGMIPADAPAQWRAESYGVWVAKVVFMVLALV
AVVGAALVQLFWLQD
|
| Enzyme 31 Number of Residues |
495 |
| Enzyme 31 Molecular Weight |
53904 |
| Enzyme 31 Theoretical pI |
4.96 |
| Enzyme 31 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 31 General Function |
Not Available |
| Enzyme 31 Specific Function |
Canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside NTPDases catalyze the hydrolyzis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides. Has activity toward ATP, ADP, UTP and UDP, but not toward AMP |
| Enzyme 31 Pathways |
|
| Enzyme 31 Reactions |
- ATP + 2 H2O = AMP + 2 phosphate [RN:R00085] ALL_REAC R00085
- (other) R00086 R00122 R00155 R00159 R00328 R00335 R00514 R00569 R00719 R00961 R02092 R02095
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
59003409  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
Q5MY95  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
ENTP8_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>1488 bp
ATGGGGCTGTCCCGGAAGGAGCAGGTCTTCTTGGCCCTGCTGGGGGCCTCGGGGGTCTCA
GGCCTCACGGCACTCATTCTCCTCCTGGTGGAGGCCACCAGCGTGCTCCTGCCCACAGAC
ATCAAGTTTGGGATCGTGTTTGATGCGGGCTCCTCCCACACGTCCCTCTTCCTGTATCAG
TGGCCGGCGAACAAGGAGAATGGCACGGGTGTGGTCAGCCAGGCCCTGGCCTGCCAGGTG
GAAGGGCCTGGAATCTCCTCCTACACTTCTAATGCTGCACAGGCTGGTGAGAGCCTGCAG
GGCTGCTTGGAGGAGGCGCTGGTGCTGATCCCAGAGGCCCAGCATCGGAAAACACCCACG
TTCCTGGGGGCCACGGCTGGCATGAGGTTGCTCAGCCGGAAGAACAGCTCTCAGGCCAGG
GACATCTTTGCAGCAGTCACCCAGGTCCTGGGCCGGTCTCCCGTGGACTTTTGGGGTGCC
GAGCTCCTGGCCGGGCAGGCCGAAGGTGCCTTTGGTTGGATCACTGTCAACTACGGCTTG
GGGACGCTGGTCAAGTACTCCTTCACTGGAGAATGGATCCAGCCTCCGGAGGAGATGCTG
GTGGGTGCCCTGGACATGGGAGGGGCCTCCACCCAGATCACGTTCGTGCCTGGGGGCCCC
ATCTTGGACAAGAGCACCCAGGCCGATTTTCGCCTCTACGGCTCCGACTACAGCGTCTAC
ACTCACAGCTACCTGTGCTTTGGACGGGACCAGATGCTGAGCAGGCTCCTCGTGGGGCTG
GTGCAGAGCCGCCCGGCTGCCCTGCTCCGTCACCCGTGCTACCTCAGCGGCTACCAGACC
ACACTGGCCCTGGGCCCGCTGTATGAGTCACCCTGTGTCCACGCCACGCCCCCGCTGAGC
CTCCCCCAGAACCTCACAGTTGAAGGGACAGGCAACCCTGGAGCCTGCGTCTCAGCCATC
CGGGAACTTTTCAACTTCTCCAGCTGCCAGGGCCAGGAGGACTGCGCCTTTGACGGGGTC
TACCAGCCCCCGCTGCGGGGCCAGTTCTATGCCTTCTCCAACTTCTACTACACCTTCCAC
TTCCTGAACCTCACCTCCAGGCAGCCCCTGAGCACGGTCAACGCCACCATCTGGGAGTTT
TGCCAGAGGCCCTGGAAACTGGTGGAGGCCAGCTACCCTGGGCAGGACCGCTGGCTGCGG
GACTACTGTGCCTCAGGCCTGTACATCCTCACCCTCCTGCACGAGGGCTACGGGTTCAGC
GAGGAGACCTGGCCCAGCCTCGAGTTCCGAAAGCAGGCGGGCGGTGTGGACATTGGCTGG
ACACTGGGCTACATGCTGAACCTGACCGGGATGATCCCGGCCGATGCGCCGGCTCAGTGG
CGGGCAGAGAGCTACGGCGTCTGGGTGGCCAAAGTGGTGTTCATGGTGCTGGCCCTGGTG
GCGGTGGTGGGGGCTGCCTTGGTCCAGCTCTTCTGGTTGCAGGACTAG
|
| Enzyme 31 GenBank Gene ID |
AY903953  |
| Enzyme 31 GeneCard ID |
Q5MY95  |
| Enzyme 31 GenAtlas ID |
ENTPD8  |
| Enzyme 31 HGNC ID |
HGNC:24860  |
| Enzyme 31 Chromosome Location |
Not Available |
| Enzyme 31 Locus |
Not Available |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
|
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
14489 |
| Enzyme 32 Name |
Putative nucleoside diphosphate kinase |
| Enzyme 32 Synonyms |
- NDK
- NDP kinase
|
| Enzyme 32 Gene Name |
NME2P1 |
| Enzyme 32 Protein Sequence |
>Putative nucleoside diphosphate kinase
MQCGLVGKIIKRFEQKGFRLVAMKFLPASEEHLKQHYIDLKDRPFFPGLVKYMNSGPVVA
MVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVKSAEKEISLRFK
PEELVDYKSCAHDWVYE
|
| Enzyme 32 Number of Residues |
137 |
| Enzyme 32 Molecular Weight |
15529 |
| Enzyme 32 Theoretical pI |
8.83 |
| Enzyme 32 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- ion binding
- magnesium ion binding
- metal ion binding
- nucleoside diphosphate kinase activity
- nucleotide binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthesis
- GTP biosynthesis
- UTP biosynthesis
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside triphosphate biosynthesis
- nucleoside triphosphate metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside triphosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside triphosphate biosynthesis
- pyrimidine ribonucleoside triphosphate biosynthesis
- ribonucleoside triphosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 32 General Function |
Nucleotide transport and metabolism |
| Enzyme 32 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate |
| Enzyme 32 Pathways |
|
| Enzyme 32 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331] ALL_REAC R00331 > R00124 R00156 R00330 R00570 R00722 R01137 R01857 R02093 R02326 R02331 R03530
|
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
2935619  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
O60361  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
NDK8_HUMAN  |
| Enzyme 32 PDB ID |
1NSK  |
| Enzyme 32 PDB File |
Show |
| Enzyme 32 3D Structure |
|
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>414 bp
ATGCAGTGCGGCCTGGTGGGCAAGATCATCAAGCGCTTCGAGCAGAAGGGGTTCCGCCTC
GTGGCCATGAAGTTCCTCCCGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTG
AAGGACCGCCCATTCTTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTCGTGGCC
ATGGTCTGGGAGGGGCTGAACGTCGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAAT
CCAGCAGATTCTAAGCCAGGCACCATTCGTGGGGACTTTTGCATTCAGGTTGGCAGGAAC
ATCATTCATGGCAGTGATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTACGGTTTAAG
CCTGAAGAACTGGTTGACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
|
| Enzyme 32 GenBank Gene ID |
AC004263  |
| Enzyme 32 GeneCard ID |
O60361  |
| Enzyme 32 GenAtlas ID |
NME2P1  |
| Enzyme 32 HGNC ID |
HGNC:31358  |
| Enzyme 32 Chromosome Location |
12 |
| Enzyme 32 Locus |
12q24.31 |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
Not Available |
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
15191 |
| Enzyme 33 Name |
cDNA FLJ76131, highly similar to Homo sapiens non-metastatic cells 7, protein expressed in (nucleoside-diphosphate kinase) (NME7), transcript variant 1, mRNA (Non-metastatic cells 7, protein expressed in (Nucleoside-diphosphate kinase), isoform CRA_a) |
| Enzyme 33 Synonyms |
Not Available |
| Enzyme 33 Gene Name |
NME7 |
| Enzyme 33 Protein Sequence |
>cDNA FLJ76131, highly similar to Homo sapiens non-metastatic cells 7, protein expressed in (nucleoside-diphosphate kinase) (NME7), transcript variant 1, mRNA (Non-metastatic cells 7, protein expressed in (Nucleoside-diphosphate kinase), isoform CRA_a)
MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN
|
| Enzyme 33 Number of Residues |
376 |
| Enzyme 33 Molecular Weight |
42492 |
| Enzyme 33 Theoretical pI |
6.44 |
| Enzyme 33 GO Classification |
Not Available |
| Enzyme 33 General Function |
Nucleotide transport and metabolism |
| Enzyme 33 Specific Function |
Not Available |
| Enzyme 33 Pathways |
Not Available |
| Enzyme 33 Reactions |
Not Available |
| Enzyme 33 Pfam Domain Function |
Not Available |
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
158254838  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
A8K3T6  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
A8K3T6_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>1131 bp
ATGAATCATAGTGAAAGATTTGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
|
| Enzyme 33 GenBank Gene ID |
AK290701  |
| Enzyme 33 GeneCard ID |
A8K3T6  |
| Enzyme 33 GenAtlas ID |
Not Available |
| Enzyme 33 HGNC ID |
Not Available |
| Enzyme 33 Chromosome Location |
Not Available |
| Enzyme 33 Locus |
Not Available |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
Not Available |
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
15192 |
| Enzyme 34 Name |
DNA-directed RNA polymerase III subunit RPC1 |
| Enzyme 34 Synonyms |
- RNA polymerase III subunit C1
- DNA-directed RNA polymerase III subunit A
- DNA-directed RNA polymerase III largest subunit
- RPC155
- C160
|
| Enzyme 34 Gene Name |
POLR3A |
| Enzyme 34 Protein Sequence |
>DNA-directed RNA polymerase III subunit RPC1
MVKEQFRETDVAKKISHICFGMKSPEEMRQQAHIQVVSKNLYSQDNQHAPLLYGVLDHRM
GTSEKDRPCETCGKNLADCLGHYGYIDLELPCFHVGYFRAVIGILQMICKTCCHIMLSQE
EKKQFLDYLKRPGLTYLQKRGLKKKISDKCRKKNICHHCGAFNGTVKKCGLLKIIHEKYK
TNKKVVDPIVSNFLQSFETAIEHNKEVEPLLGRAQENLNPLVVLNLFKRIPAEDVPLLLM
NPEAGKPSDLILTRLLVPPLCIRPSVVSDLKSGTNEDDLTMKLTEIIFLNDVIKKHRISG
AKTQMIMEDWDFLQLQCALYINSELSGIPLNMAPKKWTRGFVQRLKGKQGRFRGNLSGKR
VDFSGRTVISPDPNLRIDEVAVPVHVAKILTFPEKVNKANINFLRKLVQNGPEVHPGANF
IQQRHTQMKRFLKYGNREKMAQELKYGDIVERHLIDGDVVLFNRQPSLHKLSIMAHLARV
KPHRTFRFNECVCTPYNADFDGDEMNLHLPQTEEAKAEALVLMGTKANLVTPRNGEPLIA
AIQDFLTGAYLLTLKDTFFDRAKACQIIASILVGKDEKIKVRLPPPTILKPVTLWTGKQI
FSVILRPSDDNPVRANLRTKGKQYCGKGEDLCANDSYVTIQNSELMSGSMDKGTLGSGSK
NNIFYILLRDWGQNEAADAMSRLARLAPVYLSNRGFSIGIGDVTPGQGLLKAKYELLNAG
YKKCDEYIEALNTGKLQQQPGCTAEETLEALILKELSVIRDHAGSACLRELDKSNSPLTM
ALCGSKGSFINISQMIACVGQQAISGSRVPDGFENRSLPHFEKHSKLPAAKGFVANSFYS
GLTPTEFFFHTMAGREGLVDTAVKTAETGYMQRRLVKSLEDLCSQYDLTVRSSTGDIIQF
IYGGDGLDPAAMEGKDEPLEFKRVLDNIKAVFPCPSEPALSKNELILTTESIMKKSEFLC
CQDSFLQEIKKFIKGVSEKIKKTRDKYGINDNGTTEPRVLYQLDRITPTQVEKFLETCRD
KYMRAQMEPGSAVGALCAQSIGEPGTQMTLKTFHFAGVASMNITLGVPRIKEIINASKAI
STPIITAQLDKDDDADYARLVKGRIEKTLLGEISEYIEEVFLPDDCFILVKLSLERIRLL
RLEVNAETVRYSICTSKLRVKPGDVAVHGEAVVCVTPRENSKSSMYYVLQFLKEDLPKVV
VQGIPEVSRAVIHIDEQSGKEKYKLLVEGDNLRAVMATHGVKGTRTTSNNTYEVEKTLGI
EAARTTIINEIQYTMVNHGMSIDRRHVMLLSDLMTYKGEVLGITRFGLAKMKESVLMLAS
FEKTADHLFDAAYFGQKDSVCGVSECIIMGIPMNIGTGLFKLLHKADRDPNPPKRPLIFD
TNEFHIPLVT
|
| Enzyme 34 Number of Residues |
1390 |
| Enzyme 34 Molecular Weight |
155644 |
| Enzyme 34 Theoretical pI |
8.62 |
| Enzyme 34 GO Classification |
| Function |
- DNA binding
- DNA-directed RNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- transcription
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 34 General Function |
Transcription |
| Enzyme 34 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition |
| Enzyme 34 Pathways |
Not Available |
| Enzyme 34 Reactions |
Not Available |
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
2460208  |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
O14802  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
RPC1_HUMAN  |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>4176 bp
ATGGTGAAGGAGCAGTTCCGGGAGACGGATGTGGCCAAGAAAACAAGCCACATCTGTTTT
GGAATGAAGTCACCTGAGGAGATGCGCCAGCAGGCGCACATCCAAGTTGTGAGTAAGAAC
CTGTACAGCCAGGACAACCAACATGCCCCCTTGCTATATGGGGTGCTCGACCATAGGATG
GGTACGAGTGAGAAGGATCGTCCATGTGAAACCTGTGGGAAAAACTTGGCTGACTGTCTA
GGCCACTATGGGTATATCGACCTGGAGTTGCCGTGTTTTCATGTAGGGTACTTCAGAGCA
GTCATAGGCATCTTACAGATGATCTGCAAAACCTGCTGCCACATCATGCTGTCCCAAGAG
GAGAAGAAGCAGTTTCTGGACTATCTAAAGAGGCCCGGCCTGACCTACCTTCAGAAGCGA
GGACTGAAAAAGAAAATCTCTGACAAGTGCCGGAAGAAAAACATCTGCCATCACTGTGGC
GCTTTTAATGGTACCGTAAAGAAGTGTGGACTGCTGAAAATAATTCATGAGAAATACAAG
ACCAACAAAAAAGTGGTGGATCCCATTGTATCAAATTTCCTTCAGTCTTTTGAAACAGCC
ATTGAACATAATAAAGAAGTGGAGCCTCTGCTGGGAAGGGCACAGGAAAACTTGAATCCC
TTAGTAGTTCTGAATTTATTTAAACGAATCCCAGCTGAAGATGTTCCTCTACTTCTGATG
AACCCAGAAGCCGGAAAGCCGTCTGATTTGATTCTCACACGACTTTTGGTGCCTCCTTTG
TGTTTCAGACCCTCCGTTGTGAGTGATTTGAAGTCTGGCACCAATGAAGATGATCTGACA
ATGAAACTGACAGAAATCATTTTCCTAAACGATGTTATTAAAAAGCATCGGATCTCAGGA
GCCAAGACCCAGATGATCATGGAGGACTGGGATTTCCTGCAGCTGCAGTGTGCCCTCTAC
ATTAACAGTGAGCTCTCGGGCATTCCCCTCAACATGGCACCCAAGAAGTGGACCAGAGGC
TTCGTCCAACGCCTGAAGGGAAAACAGGGTCGATTTAGAGGAAATCTCTCAGGAAAGAGA
GTGGATTTTTCTGGCAGAACAGTCATCTCGCCCGACCCCAACCTCCGGATTGATGAGGTA
GCTGTGCCAGTTCATGTGGCCAAAATTCTAACTTTTCCTGAGAAGGTAAACAAAGCAAAC
ATCAATTTCTTGAGGAAACTGGTTCAAAACGGCCCTGAGGTTCACCCAGGAGCAAACTTC
ATTCAGCAGAGACATACGCAGATGAAAAGGTTTTTGAAATACGGAAATCGAGAAAAGATG
GCTCAAGAGCTCAAGTATGGTGACATCGTAGAGAGACACCTCATCGATGGAGATGTGGTG
CTGTTCAATCGGCAGCCCTCGCTGCACAAATTGAGCATTATGGCTCATCTGGCCAGGGTC
AAGCCCCACCGGACCTTCAGATTTAATGAGTGTGTCTGTACACCCTATAATGCTGACTTT
GATGGTGATGAAATGAACCTTCATCTTCCTCAAACAGAAGAAGCTAAAGCAGAGGCCCTT
GTTCTGATGGGGACTAAAGCAAATCTTGTAACCCCGAGGAATGGGGAACCGCTGATTGCT
GCTATTCAGGATTTTCTAACAGGTGCCTATCTCCTCACTCTCAAGGACACTTTCTTTGAT
CGAGCCAAGGCTTGCCAAATCATTGCTTCAATACTGGTTGGCAAGGATGAGAAAATTAAA
GTTCGCCTCCCACCGCCTACAATCCTAAAGCCTGTCACCCTGTGGACGGGAAAGCAGATC
TTCAGTGTCATCCTCAGGCCTAGCGATGACAATCCAGTGAGGGCCAACCTGCGAACCAAG
GGCAAGCAGTACTGTGGCAAAGGGGAAGATCTCTGTGCCAATGATTCCTATGTTACAATC
CAGAACAGTGAGTTGATGAGTGGCAGCATGGACAAAGGAACCCTAGGGTCAGGATCCAAG
AACAATATTTTTTACATTTTGCTGCGAGACTGGGGACAGAATGAAGCTGCAGATGCCATG
TCACGGCTCGCCAGGCTGGCTCCTGTCTACCTGTCTAACCGTGGTTTCTCAATTGGGATC
GGTGATGTCACACCTGGCCAAGGACTGCTGAAGGCCAAGTATGAGTTGCTGAATGCCGGC
TACAAGAAATGTGATGAGTACATCGAAGCCCTGAACACGGGCAAGCTGCAGCAGCAGCCT
GGCTGCACTGCTGAGGAGACCCTGGAGGCACTGATCCTGAAGGAGCTGTCTGTGATCCGT
GACCACGCTGGCAGTGCCTGCCTCCGGGAGCTGGACAAGAGCAACAGCCCCCTCACCATG
GCTCTGTGCGGCTCCAAAGGTTCCTTCATTAACATATCACAGATGATTGCCTGTGTGGGA
CAGCAGGCCATCAGTGGCTCTCGAGTGCCAGACGGCTTTGAAAACAGGTCCTTGCCTCAT
TTTGAAAAACACTCAAAGCTCCCAGCTGCCAAAGGCTTTGTGGCTAATAGCTTTTATTCC
GGTTTGACACCAACTGAGTTTTTCTTCCACACAATGGCCGGCCGGGAAGGTCTAGTCGAC
ACGGCTGTAAAGACAGCTGAAACGGGATACATGCAGCGAAGGCTTGTCAAATCTCTTGAA
GATCTTTGCTCCCAGTATGATCTGACAGTCCGAAGCTCTACTGGCGATATTATCCAGTTC
ATTTATGGAGGAGATGGCTTAGATCCTGCAGCTATGGAGGGAAAAGATGAACCTTTGGAG
TTTAAAAGGGTTCTGGACAACATCAAAGCAGTCTTCCCGTGTCCCAGTGAGCCTGCTCTC
AGCAAAAACGAGCTGATCCTGACCACAGAGTCCATCATGAAGAAGAGTGAGTTCCTCTGC
TGCCAGGACAGCTTCCTGCAGGAAATAAAAAAATTCATTAAGGGGGTCTCTGAGAAGATC
AAGAAAACCAGAGATAAATATGGCATCAATGATAACGGCACAACAGAGCCCCGTGTGCTG
TACCAGCTGGACCGCATCACCCCCACCCAAGTAGAAAAGTTTCTGGAGACCTGTAGGGAC
AAGTACATGAGGGCACAGATGGAGCCAGGTTCTGCAGTGGGTGCTCTGTGTGCCCAGAGC
ATTGGTGAGCCAGGCACCCAGATGACCCTGAAGACTTTCCACTTTGGAGGTGTGGCCTCC
ATGAACATCACCCTGGGCGTGCCCCGGATTAAAGAGATCATCAACGCTTCCAAGGCCATC
AGCACTCCAATTATCACAGCACAGCTAGACAAGGATGACGACGCGGATTATGCTCGCCTC
GTGAAAGGGAGAATTGAGAAAACCCTCTTGGGAGAGATTTCCGAGTATATTGAAGAAGTG
TTTCTTCCTGATGACTGCTTTATTCTCGTCAAGCTCTCCCTGGAACGGATTAGGCTTCTG
AGACTGGAAGTGAACGCTGAGACAGTGAGATATTCCATCTGCACATCCAAGCTCCGTGTG
AAGCCCGGTGATGTGGCTGTTCATGGTGAGGCTGTGGTGTGTGTCACCCCCAGAGAGAAC
AGCAAGAGCTCCATGTACTACGTGCTGCAGTTCCTGAAAGAGGATCTCCCCAAGGTGGTG
GTGCAGGGCATTCCAGAGGTGTCCAGAGCTGTCATCCACATTGACGAGCAGAGTGGAAAG
GAGAAGTACAAGCTTCTGGTGGAAGGTGATAACCTGCGGGCAGTCATGGCCACACACGGT
GTGAAGGGCACCCGAACCACCTCCAATAACACCTATGAGGTGGAGAAAACTCTGGGCATC
GAGGCCGCCCGGACAACGATCATCAATGAAATCCAGTACACCATGGTGGTGAACCACGGC
ATGAGCATCGACAGGAGGCACGTGATGCTGCTCTCCGACCTCATGACCTACAAGGGTGAA
GTCCTGGGCATCACTAGGTTTGGCCTGGCCAAGATGAAGGAGAGTGTGCTGATGCTGGCC
TCCTTTGAGAAGACGGCTGACCATCTCTTTGACGCTGCCTACTTCGGGCAGAAGGACTCT
GTGTGTGGGGTGTCTGAGTGCATCATCATGGGAATCCCAATGAACATTGGAACCGGGCTC
TTCAAGCTGCTTCACAAGGCTGACAGGGACCCGAACCCTCCCAAGAGGCCCCTGATCTTC
GACACAAATGAATTCCACATCCCCCTTGTCACATAG
|
| Enzyme 34 GenBank Gene ID |
AF021351  |
| Enzyme 34 GeneCard ID |
O14802  |
| Enzyme 34 GenAtlas ID |
POLR3A  |
| Enzyme 34 HGNC ID |
HGNC:30074  |
| Enzyme 34 Chromosome Location |
10 |
| Enzyme 34 Locus |
10q22-q23 |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
- Sepehri S, Hernandez N: The largest subunit of human RNA polymerase III is closely related to the largest subunit of yeast and trypanosome RNA polymerase III. Genome Res. 1997 Oct;7(10):1006-19. [PubMed
]
- Kuwana M, Kimura K, Kawakami Y: Identification of an immunodominant epitope on RNA polymerase III recognized by systemic sclerosis sera: application to enzyme-linked immunosorbent assay. Arthritis Rheum. 2002 Oct;46(10):2742-7. [PubMed
]
- Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N: Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits. Mol Cell Biol. 2002 Nov;22(22):8044-55. [PubMed
]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
15193 |
| Enzyme 35 Name |
DNA-directed RNA polymerase I subunit RPA1 |
| Enzyme 35 Synonyms |
- RNA polymerase I subunit A1
- DNA-directed RNA polymerase I subunit A
- DNA-directed RNA polymerase I largest subunit
- RNA polymerase I 194 kDa subunit
- RPA194
- A190
|
| Enzyme 35 Gene Name |
POLR1A |
| Enzyme 35 Protein Sequence |
>DNA-directed RNA polymerase I subunit RPA1
MLISKNMPWRRLQGISFGMYSAEELKKLSVKSITNPRYLDSLGNPSANGLYDLALGPADS
KEVCSTCVQDFSNCSGHLGHIELPLTVYNPLLFDKLYLLLRGSCLNCHMLTCPRAVIHLL
LCQLRVLEVGALQAVYELERILNRFLEENPDPSASEIREELEQYTTEIVQNNLLGSQGAH
VKNVCESKSKLIALFWKAHMNAKRCPHCKTGRSVVRKEHNSKLTITFPAMVHRTAGQKDS
EPLGIEEAQIGKRGYLTPTSAREHLSALWKNEGFFLNYLFSGMDDDGMESRFNPSVFFLD
FLVVPPSRYRPVSRLGDQMFTNGQTVNLQAVMKDVVLIRKLLALMAQEQKLPEEVATPTT
DEEKDSLIAIDRSFLSTLPGQSLIDKLYNIWIRLQSHVNIVFDSEMDKLMMDKYPGIRQI
LEKKEGLFRKHMMGKRVDYAARSVICPDMYINTNEIGIPMVFATKLTYPQPVTPWNVQEL
RQAVINGPNVHPGASMVINEDGSRTALSAVDMTQREAVAKQLLTPATGAPKPQGTKIVCR
HVKNGDILLLNRQPTLHRPSIQAHRARILPEEKVLRLHYANCKAYNADFDGDEMNAHFPQ
SELGRAEAYVLACTDQQYLVPKDGQPLAGLIQDHMVSGASMTTRGCFFTREHYMELVYRG
LTDKVGRVKLLSPSILKPFPLWTGKQVVSTLLINIIPEDHIPLNLSGKAKITGKAWVKET
PRSVPGFNPDSMCESQVIIREGELLCGVLDKAHYGSSAYGLVHCCYEIYGGETSGKVLTC
LARLFTAYLQLYRGFTLGVEDILVKPKADVKRQRIIEESTHCGPQAVRAALNLPEAASYD
EVRGKWQDAHLGKDQRDFNMIDLKFKEEVNHYSNEINKACMPFGLHRQFPENSLQMMVQS
GAKGSTVNTMQISCLLGQIELEGRRPPLMASGKSLPCFEPYEFTPRAGGFVTGRFLTGIK
PPEFFFHCMAGREGLVDTAVKTSRSGYLQRCIIKHLEGLVVQYDLTVRDSDGSVVQFLYG
EDGLDIPKTQFLQPKQFPFLASNYEVIMKSQHLHEVLSRADPKKALHHFRAIKKWQSKHP
NTLLRRGAFLSYSQKIQEAVKALKLESENRNGRSPGTQEMLRMWYELDEESRRKYQKKAA
ACPDPSLSVWRPDIYFASVSETFETKVDDYSQEWAAQTEKSYEKSELSLDRLRTLLQLKW
QRSLCEPGEAVGLLAAQSIGEPSTQMTLNTFHFAGRGEMNVTLGIPRLREILMVASANIK
TPMMSVPVLNTKKALKRVKSLKKQLTRVCLGEVLQKIDVQESFCMEEKQNKFQVYQLRFQ
FLPHAYYQQEKCLRPEDILRFMETRFFKLLMESIKKKNNKASAFRNVNTRRATQRDLDNA
GELGRSRGEQEGDEEEEGHIVDAEAEEGDADASDAKRKEKQEEEVDYESEEEEEREGEEN
DDEDMQEERNPHREGARKTQEQDEEVGLGTEEDPSLPALLTQPRKPTHSQEPQGPEAMER
RVQAVREIHPFIDDYQYDTEESLWCQVTVKLPLMKINFDMSSLVVSLAHGAVIYATKGIT
RCLLNETTNNKNEKELVLNTEGINLPELFKYAEVLDLRRLYSNDIHAIANTYGIEAALRV
IEKEIKDVFAVYGIAVDPRHLSLVADYMCFEGVYKPLNRFGIRSNSSPLQQMTFETSFQF
LKQATMLGSHDELRSPSACLVVGKVVRGGTGLFELKQPLR
|
| Enzyme 35 Number of Residues |
1720 |
| Enzyme 35 Molecular Weight |
194814 |
| Enzyme 35 Theoretical pI |
7.03 |
| Enzyme 35 GO Classification |
| Function |
- DNA binding
- DNA-directed RNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- transcription
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 35 General Function |
Transcription |
| Enzyme 35 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition |
| Enzyme 35 Pathways |
Not Available |
| Enzyme 35 Reactions |
Not Available |
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
4096591  |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
O95602  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
RPA1_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>5154 bp
ATGTTGATCTCCAAGAACATGCCCTGGCGGCGGCTGCAGGGCATTTCCTTCGGGATGTAT
TCGGCTGAAGAGCTCAAGAAATTAAGTGTTAAATCCATTACGAACCCTCGATACCTGGAC
AGCCTGGGGAACCCATCGGCAAACGGCCTGTACGATTTAGCTTTGGGCCCTGCAGATTCC
AAAGAGGTGTGCTCCACCTGCGTGCAGGACTTCAGCAACTGTTCTGGGCACCTGGGCCAC
ATTGAGCTCCCACTCACAGTGTATAACCCTCTCCTCTTCGATAAGCTGTACCTGCTGCTT
CGGGGCTCTTGTTTAAACTGCCACATGCTGACTTGTCCCCGGGCCGTGATTCACCTCTTA
CTCTGCCAGCTGAGGGTTCTGGAAGTCGGGGCCCTACAAGCAGTCTACGAGCTTGAGAGA
ATTCTGAGCAGGTTTCTGGAAGAAAATGCCGATCCCTCTGCCTCTGAAATTCGGGAGGAA
TTAGAACAATACACAACTGAAATTGTGCAGAACAACCTCCTGGGGTCCCAGGGCGCACAT
GTAAAGAACGTGTGTGAGAGCAAGAGCAAGCTCATTGCTCTCTTCTGGAAGGCACATATG
AATGCTAAGCGCTGTCCCCACTGCAAGACCGGGCGATCCGTTGTCCGAAAGGAACACAAC
AGCAAGTTGACTATCACATTTCCAGCCATGGTGCACAGGACAGCTGGCCAGAAGGACTCT
GAGCCCCTGGGAATTGAGGAAGCTCAGATAGGAAAACGAGGATACTTAACACCCACCAGT
GCCCGCGAACACCTTTCTGCCCTGTGGAAGAATGAAGGATTCTTTCTGAACTACCTTTTT
TCGGGAATGGATGATGATGGTATGGAATCCAGATTCAATCCCAGTGTGTTCTTTCTAGAT
TTCTTGGTGGTGCCGCCCTCAAGGTCTCGCCCAGTCAGTCGCCTAGGAGACCAGATGTTT
ACTAATGGCCAGACGGTGAACTTGCAGGCTGTCATGAAGGATGTAGTTCTGATTCGAAAA
CTTCTGGCATTGATGGCCCAAGAACAGAAGTTGCCAGAGGAAGTGGCCACACCCACTACA
GATGAGGAAAAAGACTCTTTGATTGCTATTGACCGATCCTTTTTGAGTACACTTCCAGGC
CAGTCCCTCATAGACAAACTTTACAACATTTGGATTCGCCTTCAGAGCCACGTCAATATT
GTGTTTGATAGCGAGATGGACAAACTAATGAGGGACAAGTACCCAGGCATTAGGCAGATC
CTGGAGAAGAAAGAAGGCCTGTTCCGAAAACACATGATGGGAAAGCGAGTGGACTCGACT
GCGCGCTCAGTCATCTGCCCAGACATGTACATCAACACCAACGAAATTGGAATTCCCATG
GTGTTTGCCACAAAACTGACCTACCCACAGCCAGTTACCCCATGGAATGTTCAGGAACTT
AGGCAAGCGGTCATCAACGGCCCTAATGTGCACCCAGGAGCCTCCATGGTCATCAATGAG
GACGGCAGCCGCACAGCCCTGAGCGCTGTGGACATGACCCAGCGAGAGGCCGTGGCCAAG
CAGCTTCTGACCCCAGCCACGGGGGCACCTAAGCCCCAGGGGACAAAAATTGTGTGCCGG
CATGTGAAGAATGGGGACATTCTGCTACTGAACCGACAGCCCACACTGCACAGACCCTCC
ATCCAGGCCCACCGTGCCCGCATCCTGCCTGAAGAGAAAGTGCTGCGGCTCCACTATGCC
AACTGCAAGGCCTATAATGCCGACTTTGATGGAGACGAGATGAATGCCCATTTCCCCCAG
AGTGAGCTGGGCCGGGCCGAGGCCTACGTCCTGGCCTGCACTGATCAGCAGTACCTTGTT
CCCAAGGATGGCCAACCATTGGCGGGACTGATCCAGGATCACATGGTTTCAGGGGCAAGC
ATGACTACTCGGGGTTGCTTTTTCACCCGGGAGCACTATATGGAGCTGGTGTACCGAGGA
CTCACGGACAAAGTGGGGCGCGTGAAGCTCCTTTCTCCTTCCATCCTGAAGCCCTTTCCG
CTGTGGACAGGAAAACAGGTTGTGTCAACGCTGCTCATAAATATAATCCCAGAGGACCAC
ATCCCACTGAACTTATCTGGAAAGGCGAAAATCACTGGGAAAGCCTGGGTGAAGGAAACT
CCTCGATCCGTTCCTGGCTTTAACCCTGACTCGATGTGCGAGTCCCAGGTGATCATCAGG
GAAGGGGAGCTGCTCTGCGGAGTGCTGGACAAGGCGCACTATGGGAGCTCCGCCTACGGC
CTGGTCCACTGCTGCTATGAGATCTATGGAGGCGAGACCAGCGGCAAGGTTCTAACCTGC
CTGGCCCGCCTCTTCACCGCCTACCTGCAGCTCTACAGAGGCTTCACCTTGGGCGTGGAA
GACATTTTGGTGAAGCCAAAGCGAGATGTCAAGAGGCAACGTATCATTGAAGAATCCACC
CACTGCGGGCCCCAGGCTGTCAGGGCTGCATTAAACCTGCCAGAAGCCGCATCATATGAT
GAGGTCCGAGGAAAATGGCAGGATGCCCATCTGGGCAAGGACCAGAGGGATTTTAACATG
ATTGATCTGAAGTTCAAGGAGGAAGTGAACCATTACAGCAATGAGATTAACAAGGCATGC
ATGCCTTTTGGCCTACACAGACAGTTCCCAGAGAACACGCTGCAGCTGATGGTGCAGTCG
GGAGCCAAAGGTTCAACTGTGAACACGATGCAGATCTCGTGCCTGCTGGGCCAGATTGAA
CTGGAAGGTCGGAGCACCCCGCTGATGGCGTCTGGCAAGTCACTGCCCTGCTTTGAGCCT
TATGAGTTCACCCCCAGGGCTGGTGGCTTTGTCACTGGCAGGTTCCTCACCGGCATCAAA
CCTCCTGAGTTCTTCTTCCACTGCATGGCAGGACGAGAGGGCCTGGTGGACACTGCTGTG
AAAACCAGCCGCTCAGGCTATCTCCAAAGGTGCATCATCAAGCACCTAGAGGGGCTGGTC
GTGCAGTATGATCTCACGGTCCGTGACAGTGACGGCAGTGTGGTGCAGTTCCTGTATGGG
GAGGATGGCCTGGACATCCCCAAGACACAGTTCCTGCAGCCCAAGCAGTTCCCCTTCCTG
GCCAGCAACTACGAGGTGATAATGAAATCACAGCATCTCCATGAAGTTTTATCCAGAGCA
GATCCCAAAAAAGCTCTCCACCACTTCAGAGCTATCAAAAAATGGCAAAGCAAGCACCCC
AACACCCTGCTGAGAAGAGGCGCCTTCTTGAGTTATTCCCAGAAAATTCAGGAAGCTGTG
AAAGCCCTGAAACTTGAGAGTGAAAACCGCAATGGCCGCAGACCCTGGGACTCAGGGAGG
ATGCTGAGGATGTGGTATGAGTTGGATGAGGAAAGCCGAAGGAAATACCAGAAGAAGGCG
GCCGCTTGTCCTGACCCCAGTCTGTCTGTCTGGCGTCCTGACATCTACTTTGCATCAGTG
TCAGAAACATTTGAAACAAAGGTTGATGACTACAGTCAAGAGTGGGCAGCTCAAACAGAG
AAGAGTTATGAGAAATCAGAGCTTTCTCTCGACAGGTTGAGGACCTTGCTGCAGCTGAAG
TGGCAGCGCTCACTGTGTGAGCCGGGCGAGGCTGTGGGCCTGCTGGCTGCCCAGAGCATC
GGAGAGCCCTCCACCCAGATGACCCTCAACACCTTCCACTTTGCAGGCAGAGGCGAGATG
AACGTCACCCTGGGCATTCCAAGGTTGCGGGAGATTCTCATGGTGGCCAGCGCCAACATC
AAGACACCCATGATGAGCGTGCCCGTGCTCAACACCAAGAAAGCCCTGAAGAGAGTGAAA
AGCCTGAAGAAGCAACTCACCAGGGTGTGCTTGGGGGAGGTGTTGCAGAAAATTGACGTC
CAGGAGTCCTTCTGTATGGAAGAAAAACAGAACAAATTCCAGGTGTACCAGCTGCGGTTT
CAGTTCCTGCCACATGCATATTACCAGCAGGAGAAGTGCCTGAGACCCGAGGACATCCTG
CGCTTCATGGAAACAAGATTCTTTAAACTTCTGATGGAATCCATCAAAAAGAAGAATAAT
AAAGCATCAGCTTTCAGGAACGTAAACACTCGAAGAGCTACACAGCGGGATCTGGACAAC
GCTGGGGAGTTGGGGAGGAGTCGGGGAGAGCAGGAGGGTGATGAGGAAGAGGAGGGGCAC
ATTGTGGATGCTGAAGCTGAGGAGGGAGACGCCGATGCCTCTGATGCCAAACGCAAGGAG
AAGCAGGAGGAGGAGGTTGATTATGAGAGTGAGGAAGAGGAGGAGAGGGAGGGCGAGGAG
AACGACGATGAAGACATGCAGGAGGAACGAAATCCCCACAGGGAAGGTGCTCGAAAGACC
CAAGAGCAAGATGAAGAGGTGGGCTTAGGAGGACCCGTCCCTTCCCACCCTCCTGACGCA
GCCCCGGAAACCCACCCACAGCCAGGAGCCCCAGGGGCCGAGGCCATGGAGCGCCGGGTC
CAGGCTGTGCGTGAGATCCACCCGTTCATAGATGACTACCAGTACGACACCGAGGAGAGC
CTGTGGTGCCAGGTGACAGTGAAGCTCCCTCTGATGAAGATCAACTTTGACATGAGCTCC
CTGGTAGTATCTTTGGCCCATGGTGCCGTCATCTATGCGACCAAGGGCATCACTCGGTGC
CTCCTGAATGAAACAACCAACAATAAGAACGAGAAGGAGCTTGTGCTAAACACAGAAGGA
ATCAACCTCCCAGAGCTATTCAAGTATGCAGAGGTCCTGGATCTGCGCCGCCTCTACTCC
AACGACATCCACGCCATAGCCAACACGTATGGCATTGAGGCGCTGCGGGTGATCGAGAAG
GAGATCAAGGATGTGTTTGCCGTGTATGGCATCGCGGTCGACCCTCGCCATCTCTCCCTG
GTTGCTGATTATATGTGCTTCGAGGGTGTTTACAAGCCACTGAATCGCTTTGGGATCCGG
TCAAACTCTTCCCCGCTACAGCAGATGACATTTGAAACCAGCTTCCAGTTTCTGAAGCAA
GCCACCATGCTGGGATCCCACGATGAGCTGAGGTCTCCTTCTGCCTGCCTTGTGGTCGGG
AAAGTCGTCAGGGGCGGGACAGGCCTGTTCGAGCTCAAGCAGCCTCTGAGATAG
|
| Enzyme 35 GenBank Gene ID |
U33460  |
| Enzyme 35 GeneCard ID |
O95602  |
| Enzyme 35 GenAtlas ID |
POLR1A  |
| Enzyme 35 HGNC ID |
HGNC:17264  |
| Enzyme 35 Chromosome Location |
Not Available |
| Enzyme 35 Locus |
Not Available |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 General References |
Not Available |
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
15200 |
| Enzyme 36 Name |
Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e) |
| Enzyme 36 Synonyms |
Not Available |
| Enzyme 36 Gene Name |
UCK1 |
| Enzyme 36 Protein Sequence |
>Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRDKEVCRCDHPA
RSGQYGCHQPDRAAHPGHSEW
|
| Enzyme 36 Number of Residues |
201 |
| Enzyme 36 Molecular Weight |
22761 |
| Enzyme 36 Theoretical pI |
6.23 |
| Enzyme 36 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside kinase activity
- nucleotide binding
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- uridine kinase activity
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 36 General Function |
Nucleotide transport and metabolism |
| Enzyme 36 Specific Function |
Not Available |
| Enzyme 36 Pathways |
Not Available |
| Enzyme 36 Reactions |
Not Available |
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
57162360  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
Q5JT13  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
Q5JT13_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>807 bp
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGTCGACCGTGTGTGAGAAGATCATGGAGTTGCTGGGACAG
AACGAGGTGGAACAGCGGCAGCGGAAGGTGGTCATCCTGAGCCAGGACAGGTTCTACAAG
GTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTGAAAGGACAGTACAATTTTGACCATCCA
GATGCCTTTGATAATGATTTGATGCACAGGACTCTGAAGAACATCGTGGAGGGCAAAACG
GTGGAGGTGCCGACCTATGATTTTGTGACACACTCAAGGTTACCAGAGACCACGGTGGTC
TACCCTGCGGACGTGGTTCTGTTTGAGGGCATCTTGGTGTTCTACAGCCAGGAGATCCGG
GACATGTTCCACCTGCGCCTCTTCGTGGACACCGACTCCGACGTCAGGCTGTCTCGAAGA
GTTCTCCGGGACGTGCGCCGAGGGAGGGACCTGGAGCAGATTCTGACGCAGTACACCACC
TTCGTGAAGCCGGCCTTCGAGGAGTTCTGCCTGCCGACAAAGAAGTATGCCGATGTGATC
ATCCCGCGAGGAGTGGACAATATGGTTGCCATCAACCTGATCGTGCAGCACATCCAGGAC
ATTCTGAATGGTGACATCTGCAAATGGCACCGAGGAGGGTCCAATGGGCGGAGCTACAAG
CGGACCTTTTCTGAGCCAGGGGACCACCCTGGGATGCTGACCTCTGGCAAACGGTCACAT
TTGGAGTCCAGCAGCAGACCCCACTGA
|
| Enzyme 36 GenBank Gene ID |
AL358781  |
| Enzyme 36 GeneCard ID |
Q5JT13  |
| Enzyme 36 GenAtlas ID |
UCK1  |
| Enzyme 36 HGNC ID |
HGNC:14859  |
| Enzyme 36 Chromosome Location |
Not Available |
| Enzyme 36 Locus |
Not Available |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
Not Available |
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
15252 |
| Enzyme 37 Name |
Myb-binding protein 1A |
| Enzyme 37 Synonyms |
Not Available |
| Enzyme 37 Gene Name |
MYBBP1A |
| Enzyme 37 Protein Sequence |
>Myb-binding protein 1A
MESRDPAQPMSPGEATQSGARPADRYGLLKHSREFLDFFWDIAKPEQETRLAATEKLLEY
LRGRPKGSEMKYALKRLITGLGVGRETARPCYSLALAQLLQSFEDLPLCSILQQIQEKYD
LHQVKKAMLRPALFANLFGVLALFQSGRLVKDQEALMKSVKLLQALAQYQNHLQEQPRKA
LVDILSEVSKATLQEILPEVLKADLNIILSSPEQLELFLLAQQKVPSKLKKLVGSVNLFS
DENVPRLVNVLKMAASSVKKDRKLPAIALDLLRLALKEDKFPRFWKEVVEQGLLKMQFWP
ASYLCFRLLGAALPLLTKEQLHLVMQGDVIRHYGEHVCTAKLPKQFKFAPEMDDYVGTFL
EGCQDDPERQLAVLVAFSSVTNQGLPVTPTFWRVVRFLSPPALQGYVAWLRAMFLQPDLD
SLVDFSTNNQKKAQDSSLHMPERAVFRLRKWIIFRLVSIVDSLHLEMEEALTEQVARFCL
FHSFFVTKKPTSQIPETKHPFSFPLENQAREAVSSAFFSLLQTLSTQFKQAPGQTQGGQP
WTYHLVQFADLLLNHSHNVTTVTPFTAQQRQAWDRMLQTLKELEAHSAEARAAAFQHLLL
LVGIHLLKSPAESCDLLGDIQTCIRKSLGEKPRRSRTKTIDPQEPPWVEVLVEILLALLA
QPSHLMRQVARSVFGHICSHLTPRALQLILDVLNPETSEDENDRVVVTDDSDERRLKGAE
DKSEEGEDNRSSESEEESEGEESEEEERDGDVDQGFREQLMTVLQAGKALGGEDSENEEE
LGDEAMMALDQSLASLFAEQKLRIQARRDEKNKLQKEKALRRDFQIRVLDLVEVLVTKQP
ENALVLELLEPLLSIIRRSLRSSSSKQEQDLLHKTARIFTHHLCRARRYCHDLGERAGAL
HAQVERLVQQAGRQPDSPTALYHFNASLYLLRVLKGNTAEGCVHETQEKQKAGTDPSHMP
TGPQAASCLDLNLVTRVYSTALSSFLTKRNSPLTVPMFLSLFSRHPVLCQSLLPILVQHI
TGPVRPRHQACLLLQKTLSMREVRSCFEDPEWKQLMGQVLAKVTENLRVLGEAQTKAQHQ
QALSSLELLNVLFRTCKHEKLTLDLTVLLGVLQGQQQSLQQGAHSTGSSRLHDLYWQAMK
TLGVQRPKLEKKDAKEIPSATQSPISKKRKKKGFLPETKKRKKRKSEDGTPAEDGTPAAT
GGSQPPSMGRKKRNRTKAKVPAQANGTPTTKSPAPGAPTRSPSTPAKSPKLQKKNQKPSQ
VNGAPGSPTEPAGQKQHQKALPKKGVLGKSPLSALARKKARLSLVIRSPSLLQSGAKKKA
QVRKAGKP
|
| Enzyme 37 Number of Residues |
1328 |
| Enzyme 37 Molecular Weight |
148856 |
| Enzyme 37 Theoretical pI |
9.87 |
| Enzyme 37 GO Classification |
| Function |
- DNA binding
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- transcription
|
| Component |
| — |
|
| Enzyme 37 General Function |
Not Available |
| Enzyme 37 Specific Function |
May activate or repress transcription via interactions with sequence specific DNA-binding proteins. Repression may be mediated at least in part by histone deacetylase activity (HDAC activity) |
| Enzyme 37 Pathways |
Not Available |
| Enzyme 37 Reactions |
Not Available |
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
6959304  |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
Q9BQG0  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
MBB1A_HUMAN  |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
>3987 bp
ATGGAGAGCCGGGATCCCGCCCAGCCGATGTCGCCTGGAGAAGCGACGCAGAGTGGCGCC
CGGCCTGCCGACCGCTATGGCCTATTGAAGCACAGTCGCGAGTTCTTGGACTTCTTCTGG
GACATTGCGAAGCCTGAGCAGGAGACGCGACTTGCGGCCACGGAGAAGCTGCTGGAGTAT
CTGCGTGGCAGGCCGAAGGGGTCCGAGATGAAATATGCCCTGAAGCGTCTAATCACGGGA
CTCGGGGTCGGGCGAGAAACAGCCCGGCCCTGCTACAGTTTGGCCCTGGCACAGCTGTTA
CAGTCTTTTGAAGACCTCCCCTTGTGCAGCATCCTGCAGCAGATACAAGAAAAATATGAC
CTGCATCAGGTGAAGAAGGCAATGCTGAGACCTGCTCTCTTTGCAAACCTGTTTGGAGTG
CTCGCCCTCTTTCAGTCAGGTCGGCTGGTGAAGGACCAGGAGGCACTGATGAAGTCGGTG
AAGCTGCTGCAGGCCCTGGCCCAGTACCAAAACCACTTGCAGGAGCAGCCCCGGAAGGCC
CTGGTGGACATCCTCTCCGAGGTCTCGAAGGCCACATTGCAGGAGATCCTGCCGGAGGTC
CTCAAAGCCGACTTGAATATAATACTCAGCTCCCCTGAACAGCTAGAGCTCTTCCTCCTG
GCCCAGCAGAAGGTGCCCTCCAAGCTCAAGAAGCTGGTGGGATCCGTGAACCTATTCTCA
GATGAGAATGTCCCCAGGCTGGTGAATGTGCTGAAGATGGCCGCCTCCTCTGTGAAGAAG
GACCGCAAGCTGCCCGCCATTGCTCTGGACCTGCTCCGCCTGGCGCTCAAGGAAGACAAG
TTCCCACGGTTCTGGAAGGAGGTGGTGGAACAAGGGCTGCTGAAGATGCAGTTCTGGCCA
GCCAGCTACCTGTGTTTCCACCTGCTGGGCGCGGCCCTGCCCCTGCTGACCAAGGAGCAG
CTGCACCTGGTGATGCAGGGAGACGTGATCCGCCATTACGGGGAGCACGTGTGCACTGCT
AAGCTCCCAAAGCAGTTCAAGTTTGCCCCAGAGATGGACGATTACGTGGGCACCTTCCTA
GAGGGGTGCCAGGATGACCCTGAGCGGCAGCTGGCCGTGCTAGTGGCCTTCTCATCTGTC
ACCAACCAAGGCCTCCCTGTCACGCCTACTTTCTGGCGGGTCGTGCGGTTCCTGAGCCCT
CCGGCCCTGCAGGGCTATGTGGCCTGGCTGCGGGCCATGTTTCTCCAGCCAGACCTGGAC
TCCTTGGTTGACTTCAGCACCAACAACCAGAAGAAAGCCCAGGATTCATCGCTCCACATG
CCTGAGCGAGCTGTGTTCCGGCTGAGGAAATGGATCATCTTTCGATTGGTGAGCATTGTG
GACAGCCTGCACCTGGAGATGGAGGAGGCCTTGACTGAGCAGGTGGCCAGGTTTTGTTTG
TTCCACTCGTTCTTTGTCACAAAGAAGCCCACATCCCAGATCCCTGAGACAAAGCACCCG
TTCTCCTTCCCTTTGGAAAACCAGGCCCGAGAGGCTGTCAGCAGTGCCTTCTTCAGTCTG
TTGCAGACCCTCAGCACGCAGTTCAAGCAGGCACCGGGCCAGACCCAGGGTGGGCAGCCC
TGGACCTACCACCTGGTGCAATTCGCAGACCTCCTGTTGAATCACAGCCACAACGTGACC
ACCGTGACACCCTTCACTGCGCAGCAGCACCAGGCCTGGGACCGGATGCTGCAGACTCTG
AAGGAGCTGGAGGCCCACTCCGCAGAGGCCAGGGCTGCTGCCTTCCAGCACCTTCTGCTC
TTCGTGGGCATCCACCTCCTCAAGTCCCCTGCAGAGAGCTGTGACCTGCTGGGTGACATC
CAGACCTGCATCAGGAAAAGTCTGGGAGAGAAGCCCCGCCGGAGCCGCACCAAGACCATC
GACCCCCAGGAACCCCCGTGGGTAGAGGTGCTGGTGGAGATCTTGCTGGCCCTGTTGGCC
CAGCCCAGCCACCTCATGCGCCAGGTGGCCCGGAGCGTGTTTGGCCACATCTGCTCCCAC
CTGACCCCGCGTGCCCTGCAGCTAATTCTGGATGTGCTGAACCCCGAGACCAGTGAGGAT
GAGAATGACCGTGTGGTGGTGACGGACGATTCTGATGAGCGGCGGCTGAAGGGTGCAGAG
GACAAGAGCGAGGAAGGTGAGGACAACAGAAGCTCAGAGAGTGAAGAGGAGAGCGAGGGG
GAGGAGAGCGAGGAGGAGGAGCGCGACGGGGACGTGGATCAGGGCTTCCGGGAACAGCTG
ATGACCGTGCTGCAGGCTGGGAAGGCGCTGGGTGGAGAGGACAGTGAGAACGAGGAGGAG
CTGGGGGATGAGGCCATGATGGCCCTGGACCAGAGCCTCGCCAGCCTCTTTGCCGAGCAG
AAGCTGCGTATCCAGGCCCGGCGAGACGAGAAGAACAAGCTGCAGAAGGAGAAGGCTCTG
CGGCGCGACTTCCAGATCCGGGTGCTGGACCTGGTGGAGGTGCTAGTGACCAAGCAGCCC
GAGAATGCCCTGGTCCTGGAGCTGCTGGAGCCGCTGCTGAGCATCATCCGGCGCAGCCTG
CGCAGCAGCAGCTCCAAACAGGAGCAGGACCTTCTGCACAAGACGGCGCGCATCTTCACG
CATCACCTGTGCCGTGCCCGGCGCTACTGCCACGACTTGGGTGAGCGCGCAGGGGCCCTG
CACGCCCAGGTGGAGCGGTTGGTGCAGCAGGCTGGCCGCCAGCCCGACTCCCCCACCGCC
CTCTACCACTTCAACGCCTCTCTCTACCTGCTCCGGGTCTTGAAGGGCAACACTGCTGAG
GGCTGCGTGCATGAGACACAGGAGAAGCAGAAAGCTGGCACTGACCCCAGCCACATGCCC
ACGGGCCCGCAGGCTGCCAGCTGCTTGGACTTGAACCTGGTGACCCGGGTGTACTCGACA
GCACTGAGCTCCTTCCTGACCAAGCGCAACAGCCCCCTCACAGTTCCCATGTTCCTCAGC
CTCTTCTCCCGGCACCCGGTGCTCTGTCAGAGCCTGCTCCCCATCCTGGTCCAGCATATC
ACGGGCCCGGTGCGGCCCCGTCATCAGGCCTGCCTGCTGCTCCAGAAGACCCTGTCCATG
CGGGAGGTGAGGTCGTGCTTTGAGGACCCCGAGTGGAAGCAGCTGATGGGCCAGGTCCTA
GCAAAGGTCACCGAGAACTTGCGCGTGCTGGGGGAGGCGCAGACCAAGGCGCAGCATCAG
CAGGCACTGTCCTCCCTGGAGCTGCTCAACGTTCTCTTCAGGACCTGCAAACATGAGAAG
CTGACCTTGGACCTGACGGTGCTCCTGGGTGTGCTGCAGGGGCAACAGCAGAGCCTACAG
CAGGGGGCACACTCCACCGGCTCCAGCCGCCTGCACGACCTCTACTGGCAGGCCATGAAA
ACCCTGGGAGTCCAGCGCCCCAAGTTGGAGAAGAAGGATGCCAAGGAGATCCCCAGTGCC
ACCCAGAGCCCCATCAGTAAGAAGCGGAAGAAAAAGGGATTCTTGCCAGAGACGAAGAAG
CGCAAGAAACGCAAGTCAGAGGATGGCACGCCAGCGGAGGATGGCACACCTGCAGCCACC
GGCGGGAGCCAGCCCCCCAGCATGGGCAGGAAGAAGAGGAACAGGACAAAGGCTAAGGTC
CCAGCCCAGGCAAACGGGACGCCAACCACCAAGAGTCCAGCCCCTGGCGCCCCCACCCGG
AGCCCCAGCACCCCTGCCAAATCCCCAAAACTGCAGAAGAAAAACCAGAAGCCGTCCCAG
GTGAATGGAGCTCCCGGGTCCCCCACGGAACCTGCAGGCCAAAAGCAGCATCAGAAGGCT
CTTCCCAAAAAGGGGGTCTTGGGCAAATCACCACTGTCCGCGCTGGCACGGAAAAAGGCA
AGGCTGTCTTTGGTCATCAGGAGTCCCAGCCTGCTTCAGAGTGGGGCCAAGAAGAAAGCA
CAGGTGAGGAAGGCAGGGAAGCCCTGA
|
| Enzyme 37 GenBank Gene ID |
AF147709  |
| Enzyme 37 GeneCard ID |
Q9BQG0  |
| Enzyme 37 GenAtlas ID |
MYBBP1A  |
| Enzyme 37 HGNC ID |
HGNC:7546  |
| Enzyme 37 Chromosome Location |
17 |
| Enzyme 37 Locus |
17p13.3 |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
- Keough R, Woollatt E, Crawford J, Sutherland GR, Plummer S, Casey G, Gonda TJ: Molecular cloning and chromosomal mapping of the human homologue of MYB binding protein (P160) 1A (MYBBP1A) to 17p13.3. Genomics. 1999 Dec 15;62(3):483-9. [PubMed
]
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed
]
- Scherl A, Coute Y, Deon C, Calle A, Kindbeiter K, Sanchez JC, Greco A, Hochstrasser D, Diaz JJ: Functional proteomic analysis of human nucleolus. Mol Biol Cell. 2002 Nov;13(11):4100-9. [PubMed
]
|
| Enzyme 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
15253 |
| Enzyme 38 Name |
DNA polymerase theta |
| Enzyme 38 Synonyms |
Not Available |
| Enzyme 38 Gene Name |
POLQ |
| Enzyme 38 Protein Sequence |
>DNA polymerase theta
MNLLRRSGKRRRSESGSDSFSGSGGDSSASPQFLSGSVLSPPPGLGRCLKAAAAGECKPT
VPDYEIDKLLLANWGLPKAVLEKYHSFGVKKMFEWQAECLLLGQVLEGKNLVYSAPTSAG
KTLVAELLILKRVLEMRKKALFILPFVSVAKEKKYYLQSLFQEVGIKVDGYMGSTSPSRH
FSSLDIAVCTIERANGLINRLIEENKMDLLGMVVVDELHMLGDSHRGYLLELLLTKICYI
TRKSASCQADLASSLSNAVQIVGMSATLPNLELVASWLNAELYHTDFRPVPLLESVKVGN
SIYDSSMKLVREFEPMLQVKGDEDHVVSLCYETICDNHSVLLFCPSKKWCEKLADIIARE
FYNLHHQAEGLVKPSECPPVILEQKELLEVMDQLRRLPSGLDSVLQKTVPWGVAFHHAGL
TFEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIRTPIFGGRPLDILTYKQMVGR
AGRKGVDTVGESILICKNSEKSKGIALLQGSLKPVRSCLQRREGEEVTGSMIRAILEIIV
GGVASTSQDMHTYAACTFLAASMKEGKQGIQRNQESVQLGAIEACVMWLLENEFIQSTEA
SDGTEGKVYHPTHLGSATLSSSLSPADTLDIFADLQRAMKGFVLENDLHILYLVTPMFED
WTTIDWYRFFCLWEKLPTSMKRVAELVGVEEGFLARCVKGKVVARTERQHRQMAIHKRFF
TSLVLLDLISEVPLREINQKYGCNRGQIQSLQQSAAVYAGMITVFSNRLGWHNMELLLSQ
FQKRLTFGIQRELCDLVRVSLLNAQRARVLYASGFHTVADLARANIVEVEVILKNAVPFK
SARKAVDEEEEAVEERRNMRTIWVTGRKGLTEREAAALIVEEARMILQQDLVEMGVQWNP
CALLHSSTCSLTHSESEVKEHTFISQTKSSYKKLTSKNKSNTIFSDSYIKHSPNIVQDLN
KSREHTSSFNCNFQNGNQEHQRCSIFRARKRASLDINKEKPGASQNEGKTSDKKVVQTFS
QKTKKAPLNFNSEKMSRSFRSWKRRKHLKRSRDSSPLKDSGACRIHLQGQTLSNPSLCED
PFTLDEKKTEFRNSGPFAKNVSLSGKEKDNKTSFPLQIKQNCSWNITLTNDNFVEHIVTG
SQSKNVTCQATSVVSEKGRGVAVEAEKINEVLIQNGSKNQNVYMKHHDIHPINQYLRKQS
HEQTSTITKQKNIIERQMPCEAVSSYINRDSNVTINCERIKLNTEENKPSHFQALGDDIS
RTVIPSEVLPSAGAFSKSEGQHENFLNISRLQEKTGTYTTNKTKNNHVSDLGLVLCDFED
SFYLDTQSEKIIQQMATENAKLGAKDTNLAAGIMQKSLVQQNSMNSFQKECHIPFPAEQH
PLGATKIDHLDLKTVGTMKQSSDSHGVDILTPESPIFHSPILLEENGLFLKKNEVSVTDS
QLNSFLQGYQTQETVKPVILLIPQKRTPTGVEGECLPVPETSLNMSDSLLFDSFSDDYLV
KEQLPDMQMKEPLPSEVTSNHFSDSLCLQEDLIKKSNVNENQDTHQQLTCSNDESIIFSE
MDSVQMVEALDNVDIFPVQEKNHTVVSPRALELSDPVLDEHHQGDQDGGDQDERAEKSKL
TGTRQNHSFIWSGASFDLSPGLQRILDKVSSPLENEKLKSMTINFSSLNRKNTELNEEQE
VISNLETKQVQGISFSSNNEVKSKIEMLENNANHDETSSLLPRKESNIVDDNGLIPPTPI
PTSASKLTFPGILETPVNPWKTNNVLQPGESYLFGSPSDIKNHDLSPGSRNGFKDNSPIS
DTSFSLQLSQDGLQLTPASSSSESLSIIDVASDQNLFQTFIKEWRCKKRFSISLACEKIR
SLTSSKTATIGSRFKQASSPQEIPIRDDGFPIKGCDDTLVVGLAVCWGGRDAYYFSLQKE
QKHSEISASLVPPSLDPSLTLKDRMWYLQSCLRKESDKECSVVIYDFIQSYKILLLSCGI
SLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLEGMETSQGIQSLGLNAGSEH
SGRYRASVESILIFNSMNQLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECE
SQKHIMQAKLDAIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPNREMKNQGSKKTLGS
TRRGIDNGRKLRLGRQFSTSKDVLNKLKALHPLPGLILEWRRITNAITKVVFPLQREKCL
NPFLGMERIYPVSQSHTATGRITFTEPNIQNVPRDFEIKMPTLVGESPPSQAVGKGLLPM
GRGKYKKGFSVNPRCQAQMEERAADRGMPFSISMRHAFVPFPGGSILAADYSQLELRILA
HLSHDRRLIQVLNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGE
QMGIKENDAACYIDSFKSRYTGINQFMTETVKNCKRDGFVQTILGRRRYLPGIKDNNPYR
KAHAERQAINTIVQGSAADIVKIATVNIQKQLETFHSTFKSHGHREGMLQSDRTGLSRKR
KLQGMFCPIRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGA
SWGELKDFDV
|
| Enzyme 38 Number of Residues |
2590 |
| Enzyme 38 Molecular Weight |
289663 |
| Enzyme 38 Theoretical pI |
7.42 |
| Enzyme 38 GO Classification |
| Function |
- ATP binding
- DNA binding
- DNA-directed DNA polymerase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- helicase activity
- nucleic acid binding
- nucleotide binding
- nucleotidyltransferase activity
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 38 General Function |
Not Available |
| Enzyme 38 Specific Function |
Not Available |
| Enzyme 38 Pathways |
Not Available |
| Enzyme 38 Reactions |
Not Available |
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
76364226  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
Q6VMB5  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
Q6VMB5_HUMAN  |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>7773 bp
ATGAATCTTCTGCGTCGGAGTGGGAAACGGCGGCGTTCAGAATCAGGCTCAGATTCGTTC
TCGGGAAGCGGCGGTGACAGCAGTGCCAGCCCCCAGTTCCTCTCCGGGTCCGTGCTGAGC
CCGCCGCCCGGCCTTGGTCGCTGCCTGAAGGCCGCAGCTGCAGGAGAATGCAAGCCTACA
GTTCCTGACTACGAAATAGACAAGCTACTATTGGCAAACTGGGGACTTCCTAAAGCAGTT
CTGGAAAAATACCACAGTTTTGGTGTAAAAAAGATGTTTGAATGGCAGGCAGAGTGCCTT
TTGCTTGGACAAGTCCTGGAAGGAAAGAATTTAGTTTATTCAGCTCCTACAAGTGCTGGG
AAGACTCTTGTGGCAGAATTACTTATTTTGAAGCGGGTTTTGGAAATGCGGAAGAAAGCT
TTGTTTATTCTTCCCTTTGTTTCTGTGGCTAAAGAGAAGAAATACTACCTCCAGAGTCTG
TTTCAGGAAGTAGGAATAAAAGTAGACGGTTATATGGGCAGCACCTCTCCATCAAGGCAT
TTCTCTTCATTGGATATTGCAGTCTGCACAATTGAGAGAGCCAATGGTCTGATCAATCGC
CTCATAGAGGAAAATAAGATGGATCTGTTAGGAATGGTGGTTGTGGATGAATTACATATG
CTGGGAGACTCTCACCGAGGGTATCTGCTGGAACTTTTGCTGACCAAGATTTGCTATATT
ACTCGGAAATCAGCATCTTGTCAGGCAGATCTAGCCAGTTCTCTGTCTAATGCTGTGCAA
ATCGTTGGCATGAGTGCTACCCTTCCTAATTTGGAGCTTGTGGCTTCCTGGTTGAATGCT
GAACTCTACCATACCGACTTTCGCCCTGTACCGCTTTTGGAGTCAGTAAAAGTTGGAAAT
TCCATATATGACTCTTCAATGAAACTTGTGAGGGAATTTGAGCCCATGCTTCAAGTGAAG
GGAGATGAGGACCATGTTGTTAGCTTATGTTATGAGACGATTTGTGATAACCATTCAGTA
TTACTTTTTTGTCCATCAAAGAAATGGTGTGAGAAGCTGGCAGATATCATTGCTCGAGAG
TTTTATAATCTACATCATCAAGCTGAGGGTTTGGTGAAACCCTCTGAATGCCCACCAGTA
ATTCTGGAACAAAAAGAACTCCTGGAAGTGATGGATCAGTTAAGACGTTTGCCTTCAGGA
CTGGACTCTGTATTACAGAAAACTGTACCATGGGGAGTAGCATTTCATCATGCAGGTCTT
ACTTTTGAGGAGAGGGATATCATTGAAGGAGCCTTTCGTCAAGGTCTCATTCGGGTCTTG
GCGGCAACTTCTACTCTTTCTTCTGGGGTGAATTTACCTGCACGTCGTGTGATTATTCGA
ACCCCTATTTTTGGTGGTCGACCTCTAGATATTCTTACTTATAAGCAGATGGTTGGTCGT
GCTGGCAGGAAAGGAGTGGACACAGTAGGCGAGAGTATCTTAATTTGTAAGAACTCTGAG
AAATCAAAAGGCATAGCTCTCCTTCAGGGTTCTCTAAAGCCTGTTCGCAGCTGTCTGCAA
AGACGAGAAGGAGAAGAAGTAACTGGCAGCATGATACGAGCTATTCTGGAGATAATAGTT
GGTGGAGTGGCAAGTACATCACAAGATATGCATACTTATGCTGCCTGCACATTTTTGGCT
GCAAGTATGAAAGAAGGGAAGCAAGGAATTCAGAGAAATCAAGAGTCTGTTCAGCTTGGA
GCGATTGAGGCCTGTGTGATGTGGCTACTAGAAAATGAATTCATCCAGAGTACAGAAGCC
AGTGATGGAACAGAAGGAAAGGTGTATCATCCAACACATCTTGGTTCGGCCACTCTTTCT
TCTTCACTTTCTCCAGCTGATACTTTAGATATTTTTGCTGACCTGCAAAGAGCAATGAAG
GGCTTTGTTTTAGAGAATGATCTTCATATTCTCTATCTGGTTACACCTATGTTTGAGGAT
TGGACTACTATTGATTGGTATCGATTTTTCTGTTTATGGGAGAAGTTGCCAACTTCAATG
AAAAGGGTGGCAGAGCTAGTGGGAGTTGAAGAGGGGTTCTTGGCCCGTTGTGTGAAAGGA
AAAGTAGTAGCCAGAACTGAGAGACAGCATCGACAAATGGCCATCCATAAAAGGTTTTTC
ACCAGTCTTGTGCTATTAGATTTAATCAGTGAAGTTCCCTTAAGGGAAATAAATCAGAAA
TATGGATGCAATCGTGGGCAGATTCAATCTTTGCAACAGTCAGCTGCTGTTTATGCAGGG
ATGATTACAGTATTTTCCAACCGTCTGGGCTGGCACAACATGGAACTACTACTTTCCCAA
TTTCAGAAGCGTCTTACGTTTGGCATCCAGAGGGAGCTGTGTGACCTGGTTCGGGTATCC
TTACTAAATGCTCAGAGAGCCAGGGTTCTCTATGCTTCTGGCTTTCATACTGTGGCAGAC
CTTGCTAGAGCAAATATTGTGGAGGTGGAGGTGATTCTGAAAAATGCTGTGCCTTTCAAA
AGTGCCCGGAAGGCAGTGGATGAGGAAGAGGAAGCAGTTGAAGAACGTCGCAATATGCGA
ACTATCTGGGTGACTGGCAGAAAAGGTTTAACTGAAAGGGAAGCAGCAGCCCTTATAGTG
GAAGAAGCCAGAATGATTCTGCAGCAGGACTTAGTTGAAATGGGAGTGCAATGGAATCCA
TGTGCCCTGTTACATTCTAGTACATGCTCATTGACTCATAGTGAGTCCGAAGTAAAGGAA
CACACATTTATATCCCAAACTAAGAGTTCTTATAAAAAATTAACATCAAAGAACAAAAGT
AACACAATATTTAGTGATTCTTATATTAAGCATTCACCAAATATAGTGCAAGACTTAAAT
AAAAGTAGAGAGCATACAAGTTCCTTTAATTGTAATTTCCAGAATGGGAATCAAGAACAT
CAGAGATGTTCCATTTTCAGAGCAAGAAAACGGGCCTCTTTAGATATAAATAAAGAGAAG
CCAGGAGCCTCTCAGAATGAGGGGAAAACAAGTGATAAGAAAGTTGTTCAGACTTTTTCA
CAGAAAACAAAAAAGGCACCTTTGAATTTCAATTCAGAAAAGATGAGCAGAAGTTTTCGA
TCTTGGAAACGTAGAAAGCATCTAAAGCGATCTAGGGACAGCAGCCCCCTGAAAGACTCT
GGAGCGTGTAGAATCCATTTACAAGGACAGACTCTGTCTAATCCTAGTCTTTGTGAAGAC
CCGTTTACCTTAGATGAGAAGAAAACGGAATTTAGAAATTCAGGGCCATTTGCTAAAAAT
GTATCTTTGAGTGGTAAGGAAAAAGATAATAAAACATCATTCCCATTACAAATAAAGCAA
AATTGTTCATGGAACATAACACTAACTAATGATAATTTTGTGGAGCATATTGTCACAGGA
TCTCAGAGTAAAAATGTGACTTGTCAGGCCACTAGTGTGGTTAGTGAAAAGGGCAGAGGA
GTAGCTGTTGAGGCAGAAAAAATAAATGAAGTGCTGATACAAAATGGTTCAAAAAACCAG
AATGTTTATATGAAACACCATGACATCCATCCAATTAACCAGTACCTGCGAAAGCAATCT
CATGAACAGACAAGCACTATTACCAAACAGAAAAATATAATAGAGAGACAAATGCCCTGT
GAAGCAGTCAGTAGTTACATAAATAGAGACTCAAATGTTACTATCAATTGTGAAAGGATA
AAGCTTAATACAGAGGAAAATAAACCAAGTCATTTTCAGGCATTAGGAGATGATATAAGC
AGAACTGTGATACCCAGTGAAGTACTTCCATCAGCTGGAGCATTTAGCAAATCAGAAGGC
CAGCATGAGAATTTTCTAAATATTTCTAGACTACAAGAAAAAACAGGTACTTATACAACA
AACAAAACTAAAAATAATCATGTTTCTGACTTAGGTTTAGTCCTCTGTGATTTTGAAGAT
AGTTTCTATCTGGATACTCAGTCAGAGAAAATAATACAACAGATGGCAACTGAAAATGCC
AAACTAGGAGCAAAGGACACCAACCTGGCAGCAGGGATAATGCAGAAGAGCTTAGTCCAA
CAGAACTCAATGAACTCTTTTCAGAAGGAGTGTCACATTCCTTTTCCTGCTGAACAGCAC
CCTCTAGGAGCGACTAAGATAGATCATTTGGACCTTAAGACTGTAGGTACTATGAAACAA
AGCAGTGATTCACATGGGGTTGATATCCTGACTCCAGAAAGCCCGATTTTCCATTCTCCA
ATACTATTGGAGGAAAATGGTCTTTTTTTAAAAAAGAATGAAGTTTCTGTTACTGATTCA
CAATTAAATAGTTTTCTTCAAGGTTATCAAACACAAGAAACTGTGAAACCAGTTATACTT
CTGATTCCTCAAAAGAGAACTCCCACTGGTGTAGAAGGAGAATGTCTTCCAGTTCCTGAA
ACAAGTTTGAATATGAGTGATAGTTTACTATTTGATAGCTTCAGTGATGACTATCTAGTA
AAAGAACAATTACCTGATATGCAAATGAAAGAACCCCTTCCTTCAGAAGTAACATCAAAC
CATTTTAGTGATTCTCTGTGTCTACAAGAAGACCTAATTAAAAAATCAAATGTAAATGAG
AATCAAGATACCCACCAGCAGTTGACTTGTTCCAATGATGAATCTATTATATTTTCAGAA
ATGGATTCTGTTCAGATGGTTGAAGCTTTGGACAATGTGGATATATTTCCTGTCCAAGAG
AAGAATCATACTGTAGTATCTCCTAGAGCATTAGAACTAAGTGATCCAGTACTTGATGAG
CACCACCAAGGTGATCAAGATGGAGGAGATCAAGATGAAAGGGCTGAAAAATCAAAATTA
ACTGGGACCAGGCAAAATCATTCATTCATATGGTCAGGGGCATCATTTGATCTAAGTCCA
GGACTGCAAAGGATTTTAGATAAAGTATCCAGTCCTCTAGAAAATGAAAAGCTAAAATCA
ATGACTATAAACTTTTCCAGTTTGAATAGAAAAAATACAGAGTTAAATGAAGAACAAGAA
GTTATTTCAAACTTGGAGACAAAACAAGTGCAGGGAATTTCATTTTCTTCTAATAATGAA
GTAAAAAGCAAGATTGAGATGCTAGAAAACAATGCCAATCATGATGAAACCTCATCCCTC
TTACCTCGTAAAGAAAGTAATATAGTTGATGATAATGGTCTCATTCCTCCTACACCCATT
CCAACATCTGCTTCTAAGCTGACATTTCCAGGGATTCTTGAAACACCTGTAAACCCTTGG
AAAACTAATAATGTTTTACAACCTGGTGAAAGTTATTTATTTGGCTCACCTTCAGATATT
AAAAACCACGATTTAAGTCCAGGGAGTAGAAATGGGTTCAAAGACAACAGCCCTATTAGT
GACACAAGCTTTTCACTTCAGTTATCACAGGATGGATTACAGTTAACTCCAGCCTCAAGC
AGTTCAGAAAGTTTGTCCATAATTGATGTAGCAAGTGACCAAAATCTTTTCCAAACATTC
ATTAAGGAGTGGCGGTGCAAAAAGCGATTTTCCATCTCACTGGCTTGTGAAAAGATTAGA
AGTTTGACATCTTCTAAAACTGCTACTATTGGCAGTAGGTTTAAGCAAGCTAGCTCACCT
CAGGAAATTCCTATTAGAGATGATGGATTTCCCATTAAAGGTTGTGATGACACCTTGGTG
GTTGGACTGGCAGTATGCTGGGGTGGAAGGGATGCCTATTATTTTTCACTGCAGAAGGAA
CAAAAGCATTCTGAAATTAGTGCCAGTTTGGTTCCACCTTCTTTAGATCCAAGCCTGACT
TTGAAAGACAGGATGTGGTACCTTCAATCTTGCTTGCGAAAGGAATCTGATAAAGAATGT
TCTGTTGTCATCTATGACTTCATCCAGAGCTATAAAATTCTTCTTCTTTCTTGTGGCATC
TCCTTGGAGCAAAGTTATGAAGATCCTAAGGTGGCATGCTGGTTACTAGATCCAGATTCT
CAGGAGCCGACTCTTCATAGCATAGTTACCAGTTTTCTTCCTCATGAGCTTCCACTCCTA
GAAGGGATGGAGACCAGCCAAGGGATTCAAAGCCTGGGGCTAAATGCTGGCAGTGAGCAT
TCTGGGCGATACAGAGCATCTGTGGAGTCCATTCTCATCTTCAACTCTATGAATCAGCTC
AACTCTTTGTTGCAGAAGGAAAACCTTCAAGATGTTTTCCGTAAGGTGGAAATGCCCTCT
CAGTACTGCTTGGCCTTGCTAGAACTAAATGGAATTGGCTTTAGTACTGCAGAATGTGAA
AGTCAGAAACATATAATGCAAGCCAAGCTGGATGCAATTGAGACCCAGGCCTATCAACTA
GCTGGCCACAGTTTTTCTTTCACCAGTTCAGATGACATCGCTGAGGTTTTATTTTTGGAA
TTGAAGTTGCCCCCAAATAGAGAGATGAAAAACCAAGGCAGCAAGAAAACTCTGGGTTCT
ACCAGAAGAGGGATTGACAATGGACGCAAGCTAAGGCTGGGAAGACAGTTCAGCACTAGT
AAGGACGTTTTAAATAAATTAAAGGCATTACATCCTTTACCAGGCTTGATATTAGAATGG
AGAAGAATCACTAATGCTATTACCAAAGTGGTCTTTCCCCTTCAGCGGGAAAAGTGTCTT
AATCCTTTTCTTGGAATGGAAAGAATCTATCCTGTATCACAGTCGCACACTGCTACAGGA
CGAATAACCTTTACAGAACCAAATATTCAGAATGTGCCAAGAGATTTTGAAATCAAAATG
CCAACACTAGTAGGAGAAAGCCCACCTTCTCAAGCTGTAGGCAAAGGCCTACTTCCCATG
GGCAGAGGAAAATATAAGAAGGGTTTCAGCGTGAATCCTAGATGCCAGGCACAGATGGAG
GAGAGAGCTGCAGACAGAGGAATGCCATTTTCAATTAGCATGCGACATGCCTTTGTGCCT
TTCCCAGGTGGTTCAATACTGGCTGCTGACTACTCTCAGCTTGAACTGAGGATCTTGGCT
CATTTATCCCATGATCGTCGTCTCATTCAAGTGTTAAACACTGGAGCTGATGTTTTCAGG
AGCATTGCAGCAGAGTGGAAGATGATTGAGCCAGAGTCTGTTGGGGATGATCTGAGGCAG
CAGGCAAAACAGATTTGCTATGGGATCATTTATGGAATGGGAGCTAAATCTTTGGGAGAG
CAGATGGGCATTAAAGAAAATGATGCTGCATGCTATATTGACTCCTTCAAATCCAGATAC
ACAGGGATTAATCAATTCATGACAGAGACAGTGAAGAATTGTAAAAGAGACGGATTTGTT
CAGACCATTTTGGGAAGGCGTAGATATTTGCCAGGAATCAAAGACAACAACCCTTATCGT
AAAGCTCACGCTGAGCGTCAAGCTATCAACACAATAGTCCAAGGATCAGCAGCTGATATT
GTCAAAATAGCCACAGTTAACATTCAGAAGCAATTAGAGACCTTCCACTCAACCTTCAAA
TCCCATGGTCATCGAGAGGGTATGCTCCAAAGTGACCGAACAGGATTGTCACGAAAGAGA
AAACTGCAAGGGATGTTCTGCCCAATCAGAGGAGGCTTCTTCATCCTTCAACTCCATGAT
GAACTCCTATATGAAGTGGCAGAAGAAGATGTTGTTCAGGTAGCTCAGATTGTCAAGAAT
GAAATGGAAAGTGCTGTAAAACTGTCTGTGAAATTGAAAGTGAAAGTGAAAATAGGCGCC
AGCTGGGGAGAGCTAAAGGACTTTGATGTGTAA
|
| Enzyme 38 GenBank Gene ID |
AY338826  |
| Enzyme 38 GeneCard ID |
Q6VMB5  |
| Enzyme 38 GenAtlas ID |
POLQ  |
| Enzyme 38 HGNC ID |
HGNC:9186  |
| Enzyme 38 Chromosome Location |
Not Available |
| Enzyme 38 Locus |
Not Available |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 General References |
- Seki M, Marini F, Wood RD: POLQ (Pol theta), a DNA polymerase and DNA-dependent ATPase in human cells. Nucleic Acids Res. 2003 Nov 1;31(21):6117-26. [PubMed
]
|
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
15254 |
| Enzyme 39 Name |
cDNA FLJ76751, highly similar to Homo sapiens polymerase (DNA directed) sigma (POLS), mRNA (Polymerase (DNA directed) sigma) |
| Enzyme 39 Synonyms |
Not Available |
| Enzyme 39 Gene Name |
POLS |
| Enzyme 39 Protein Sequence |
>cDNA FLJ76751, highly similar to Homo sapiens polymerase (DNA directed) sigma (POLS), mRNA (Polymerase (DNA directed) sigma)
MSPCPEEAAMRREVVKRIETVVKDLWPTADVQIFGSFSTGLYLPTSDIDLVVFGKWERPP
LQLLEQALRKHNVAEPCSIKVLDKATVPIIKLTDQETEVKVDISFNMETGVRAAEFIKNY
MKKYSLLPYLILVLKQFLLQRDLNEVFTGGISSYSLILMAISFLQLHPRIDARRADENLG
MLLVEFFELYGRNFNYLKTGIRIKEGGAYIAKEEIMKAMTSGYRPSMLCIEDPLLPGNDV
GRSSYGAMQVKQVFDYAYIVLSHAVSPLARSYPNRDAESTLGRIIKVTQEVIDYRRWIKE
KWGSKAHPSPGMDSRIKIKERIATCNGEQTQNREPESPYGQRLTLSLSSPQLLSSGSSAS
SVSSLSGSDVDSDTPPCTTPSVYQFSLQAPAPLMAGLPTALPMPSGKPQPTTSRTLIMTT
NNQTRFTIPPPTLGVAPVPCRQAGVEGTASLKAVHHMSSPAIPSASPNPLSSPHLYHKQH
NGMKLSMKGSHGHTQGGGYSSVGSGGVRPPVGNRGHHQYNRTGWRRKKHTHTRDSLPVSL
SR
|
| Enzyme 39 Number of Residues |
542 |
| Enzyme 39 Molecular Weight |
59874 |
| Enzyme 39 Theoretical pI |
9.81 |
| Enzyme 39 GO Classification |
Not Available |
| Enzyme 39 General Function |
Not Available |
| Enzyme 39 Specific Function |
Not Available |
| Enzyme 39 Pathways |
Not Available |
| Enzyme 39 Reactions |
Not Available |
| Enzyme 39 Pfam Domain Function |
Not Available |
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
158260737  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
A8K1E2  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
A8K1E2_HUMAN  |
| Enzyme 39 PDB ID |
Not Available |
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>1629 bp
ATGTCCCCTTGTCCTGAAGAAGCAGCTATGAGAAGAGAGGTGGTGAAACGGATCGAAACT
GTGGTGAAAGACCTTTGGCCGACGGCTGATGTACAGATATTTGGCAGCTTTAGTACAGGT
CTTTATCTTCCAACTAGCGACATAGACCTGGTGGTCTTCGGGAAATGGGAGCGTCCTCCT
TTACAGCTGCTGGAGCAAGCCCTGCGGAAGCACAACGTGGCTGAGCCGTGTTCCATCAAA
GTCCTTGACAAGGCTACGGTACCAATAATAAAGCTCACAGATCAGGAGACTGAAGTGAAA
GTTGACATCAGCTTTAACATGGAGACGGGCGTCCGGGCAGCGGAGTTCATCAAGAATTAC
ATGAAGAAATATTCATTGCTGCCTTACTTGATTTTAGTATTGAAACAGTTCCTTCTGCAG
AGGGACCTGAATGAAGTTTTTACAGGTGGAATTAGCTCATACAGCCTAATTTTAATGGCC
ATTAGCTTTCTACAGTTGCATCCAAGAATTGATGCCCGGAGAGCTGATGAAAACCTTGGA
ATGCTTCTTGTAGAATTTTTTGAACTCTATGGGAGAAATTTTAATTACTTGAAAACCGGT
ATTAGAATCAAAGAAGGAGGTGCCTATATCGCCAAAGAGGAGATCATGAAAGCCATGACC
AGCGGGTACAGACCGTCGATGCTGTGCATTGAGGACCCCCTGCTGCCAGGGAATGACGTT
GGCCGGAGCTCCTATGGCGCCATGCAGGTGAAGCAGGTCTTCGATTATGCCTACATAGTG
CTCAGCCATGCTGTGTCACCGCTGGCCAGGTCCTATCCAAACAGAGACGCCGAAAGTACT
TTAGGAAGAATCATCAAAGTAACTCAGGAGGTGATTGACTACCGGAGGTGGATCAAAGAG
AAGTGGGGCAGCAAAGCCCACCCGTCGCCAGGCATGGACAGCAGGATCAAGATCAAAGAG
CGAATAGCCACATGCAATGGGGAGCAGACGCAGAACCGAGAGCCCGAGTCTCCCTATGGC
CAGCGCTTGACTTTGTCGCTGTCCAGCCCCCAGCTCCTGTCTTCAGGCTCCTCGGCCTCT
TCTGTGTCTTCACTTTCTGGGAGTGACGTTGATTCAGACACACCGCCCTGCACAACGCCC
AGTGTTTACCAGTTCAGTCTGCAAGCGCCAGCTCCTCTCATGGCCGGCTTACCCACCGCC
TTGCCAATGCCCAGTGGCAAACCTCAGCCCACCACTTCCAGAACACTGATCATGACAACC
AACAATCAGACCAGGTTTACTATACCTCCACCGACCCTAGGGGTTGCTCCTGTTCCTTGC
AGACAAGCTGGTGTAGAAGGAACTGCGTCTTTGAAAGCCGTCCACCACATGTCTTCCCCG
GCCATTCCCTCAGCGTCCCCCAACCCGCTCTCGAGCCCTCATCTGTATCATAAGCAGCAC
AACGGCATGAAACTGTCCATGAAGGGCTCTCACGGCCACACCCAAGGCGGCGGCTACAGC
TCTGTGGGTAGCGGAGGTGTGCGGCCCCCTGTGGGCAACAGGGGACACCACCAGTATAAC
CGCACCGGCTGGAGGAGGAAAAAACACACACACACACGGGACAGTCTGCCCGTGAGCCTC
AGCAGATAA
|
| Enzyme 39 GenBank Gene ID |
AK289857  |
| Enzyme 39 GeneCard ID |
A8K1E2  |
| Enzyme 39 GenAtlas ID |
Not Available |
| Enzyme 39 HGNC ID |
Not Available |
| Enzyme 39 Chromosome Location |
Not Available |
| Enzyme 39 Locus |
Not Available |
| Enzyme 39 SNPs |
SNPJam Report  |
| Enzyme 39 General References |
Not Available |
| Enzyme 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
16437 |
| Enzyme 40 Name |
cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b) |
| Enzyme 40 Synonyms |
Not Available |
| Enzyme 40 Gene Name |
ENTPD3 |
| Enzyme 40 Protein Sequence |
>cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
|
| Enzyme 40 Number of Residues |
529 |
| Enzyme 40 Molecular Weight |
59106 |
| Enzyme 40 Theoretical pI |
6.40 |
| Enzyme 40 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 40 General Function |
Not Available |
| Enzyme 40 Specific Function |
Not Available |
| 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 |
Not Available |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
B2R8D0  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
B2R8D0_HUMAN  |
| Enzyme 40 PDB ID |
Not Available |
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
Not Available |
| Enzyme 40 GenBank Gene ID |
AK313322  |
| Enzyme 40 GeneCard ID |
B2R8D0  |
| Enzyme 40 GenAtlas ID |
Not Available |
| Enzyme 40 HGNC ID |
Not Available |
| Enzyme 40 Chromosome Location |
Not Available |
| Enzyme 40 Locus |
Not Available |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 General References |
Not Available |
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
16536 |
| Enzyme 41 Name |
Polymerase (DNA directed) kappa, isoform CRA_b |
| Enzyme 41 Synonyms |
- SubName: cDNA, FLJ95449, Homo sapiens polymerase (DNA directed) kappa (POLK), mRNA
|
| Enzyme 41 Gene Name |
POLK |
| Enzyme 41 Protein Sequence |
>Polymerase (DNA directed) kappa, isoform CRA_b
MDSTKEKCDSYKDDLLLRMGLNDNKAGMEGLDKEKINKIIMEATKGSRFYGNELKKEKQV
NQRIENMMQQKAQITSQQLRKAQLQVDRFAMELEQSRNLSNTIVHIDMDAFYAAVEMRDN
PELKDKPIAVGSMSMLSTSNYHARRFGVRAAMPGFIAKRLCPQLIIVPPNFDKYRAVSKE
VKEILADYDPNFMAMSLDEAYLNITKHLEERQNWPEDKRRYFIKMGSSVENDNPGKEVNK
LSEHERSISPLLFEESPSDVQPPGDPFQVNFEEQNNPQILQNSVVFGTSAQEVVKEIRFR
IEQKTTLTASAGIAPNTMLAKVCSDKNKPNGQYQILPNRQAVMDFIKDLPIRKVSGIGKV
TEKMLKALGIITCTELYQQRALLSLLFSETSWHYFLHISLGLGSTHLTRDGERKSMSVER
TFSEINKAEEQYSLCQELCSELAQDLQKERLKGRTVTIKLKNVNFEVKTRASTVSSVVST
AEEIFAIAKELLKTEIDADFPHPLRLRLMGVRISSFPNEEDRKHQQRSIIGFLQAGNQAL
SATECTLEKTDKDKFVKPLEMSHKKSFFDKKRSERKWSHQDTFKCEAVNKQSFQTSQPFQ
VLKKKMNENLEISENSDDCQILTCPVCFRAQGCISLEALNKHVDECLDGPSISENFKMFS
CSHVSATKVNKKENVPASSLCEKQDYEAHPKIKEISSVDCIALVDTIDNSSKAESIDALS
NKHSKEECSSLPSKSFNIEHCHQNSSSTVSLENEDVGSFRQEYRQPYLCEVKTGQALVCP
VCNVEQKTSDLTLFNVHVDVCLNKSFIQELRKDKFNPVNQPKESSRSTGSSSGVQKAVTR
TKRPGLMTKYSTSKKIKPNNPKHTLDIFFK
|
| Enzyme 41 Number of Residues |
870 |
| Enzyme 41 Molecular Weight |
98810 |
| Enzyme 41 Theoretical pI |
8.22 |
| Enzyme 41 GO Classification |
| Function |
- DNA binding
- binding
- nucleic acid binding
|
| Process |
- DNA metabolism
- DNA repair
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 41 General Function |
Replication, recombination and repair |
| Enzyme 41 Specific Function |
Not Available |
| 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 |
Not Available |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
B2RBD2  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
B2RBD2_HUMAN  |
| Enzyme 41 PDB ID |
1T94  |
| Enzyme 41 PDB File |
Show |
| Enzyme 41 3D Structure |
|
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
Not Available |
| Enzyme 41 GenBank Gene ID |
AK314610  |
| Enzyme 41 GeneCard ID |
B2RBD2  |
| Enzyme 41 GenAtlas ID |
Not Available |
| Enzyme 41 HGNC ID |
Not Available |
| Enzyme 41 Chromosome Location |
Not Available |
| Enzyme 41 Locus |
Not Available |
| Enzyme 41 SNPs |
SNPJam Report  |
| Enzyme 41 General References |
Not Available |
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
17341 |
| Enzyme 42 Name |
RNA-directed RNA polymerase catalytic subunit |
| Enzyme 42 Synonyms |
- Polymerase basic protein 1
- PB1
- RNA-directed RNA polymerase subunit P1
|
| Enzyme 42 Gene Name |
PB1 |
| Enzyme 42 Protein Sequence |
>RNA-directed RNA polymerase catalytic subunit
MDVNPTLLFLKVPAQNAISTTFPYTGDPPYSHGTGTGYTMDTVNRTHQYSEKGKWTTNTE
TGAPQLNPIDGPLPEDNEPSGYAQTDCVLEAMAFLEESHPGIFENSCLETMEVIQQTRVD
KLTQGRQTYDWTLNRNQPAATALANTIEVFRSNGLTANESGRLIDFLKDVIESMDKEEME
ITTHFQRKRRVRDNMTKKMVTQRTIGKKKQRLNKRIYLIRALTLNTMTKDAERGKLKRRA
IATPGMQIRGFVYFVETLARSICENLEQSGLPVGGNEKKAKLANVVRKMMTNSQDTELSF
TITGDNTKWNENQNPRMFLAMITYITRNQPEWFRNVLSIAPIMFSNKMARLGKGYMFKSK
SMKLRTQIPAEMLTSIDLKYFNESTRKKIEKIRPLLIDGTVSLSPGMMMGMFNMLSTVLG
VSILNLGQKKYTKTTYWWDGLQSSDDFALIVNAPNHEGIQAGVDRFYRTCKLVGINMSKK
KSYTNRTGTFEFTSFFYRYGFVANFSMELPSFGVSGINESDDMSIGVTVIKNNMINNDLG
PATAQMALQLFIKDYRYTYRCHRGDTQIQTRRSFELKKLWEQTRSKAGLLISDGGPNLYN
IRNLHIPEVCLKWELMDEDYQGRLCNPLNPFVSHKEIESVNNAVVMPAHGPAKSMEYDAV
ATTHSWIPKRNRSILNTSQRGILEDQQMYQKCCNLFEKFFPSSSYRRPVGISSMVEAMVS
RARIDARIDFESGRIKKEEFAEIMKICSTIEELRRQK
|
| Enzyme 42 Number of Residues |
757 |
| Enzyme 42 Molecular Weight |
86507.6 |
| Enzyme 42 Theoretical pI |
9.68 |
| Enzyme 42 GO Classification |
| Function |
- RNA-directed RNA polymerase activity
- catalytic activity
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- transcription
- viral genome replication
- viral infectious cycle
- viral life cycle
|
| Component |
| — |
|
| Enzyme 42 General Function |
Involved in nucleotide binding |
| Enzyme 42 Specific Function |
RNA-dependent RNA polymerase which is responsible for replication and transcription of virus segments. Binds the promoter sequence of the encapsidated viral RNA. Displays an endonuclease activity involved in cap-stealing. Cleaves cellular pre-mRNA to generate primers for viral transcription |
| 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 |
324976  |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
P26120  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
RDRP_I57A2  |
| Enzyme 42 PDB ID |
Not Available |
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
>2274 bp
ATGGATGTCAATCCGACCTTACTTTTCTTGAAAGTTCCAGCGCAAAATGCCATAAGTACT
ACATTCCCTTATACTGGAGATCCTCCATACAGCCATGGAACAGGAACAGGATACACCATG
GACACAGTCAACAGAACACATCAATATTCAGAAAAGGGGAAGTGGACAACAAACACGGAA
ACTGGAGCGCCCCAACTTAACCCAATTGATGGACCACTACCTGAGGACAATGAACCAAGT
GGATATGCACAAACAGACTGCGTCCTGGAAGCAATGGCTTTCCTTGAAGAATCCCACCCA
GGAATCTTTGAAAACTCGTGTCTTGAAACGATGGAGGTTATTCAACAAACAAGAGTGGAC
AAACTGACCCAAGGTCGTCAGACCTATGATTGGACATTGAACAGAAATCAGCCGGCTGCA
ACTGCGCTAGCCAACACTATAGAGGTCTTCAGATCGAATGGTCTGACAGCTAATGAATCG
GGAAGGCTAATAGATTTCCTCAAGGATGTGATAGAATCAATGGATAAAGAGGAGATGGAA
ATAACAACACACTTCCAAAGAAAAAGAAGAGTAAGAGACAACATGACCAAGAAAATGGTC
ACACAACGAACAATAGGAAAGAAGAAGCAAAGATTGAACAAGAGAATCTATCTAATAAGA
GCACTGACATTGAACACAATGACTAAAGATGCAGAGAGAGGTAAATTAAAGAGAAGAGCA
ATTGCAACACCCGGTATGCAGATCAGAGGGTTCGTGTACTTTGTCGAAACACTAGCGAGA
AGTATTTGTGAGAATCTTGAACAGTCTGGGCTTCCGGTTGGAGGTAATGAAAAGAAGGCT
AAACTGGCAAATGTTGTGAGAAAAATGATGACTAATTCACAAGACACAGAGCTCTCTTTC
ACAATTACTGGAGACAATACCAAATGGAATGAGAATCAAAATCCTCGGATGTTCCTGGCG
ATGATAACATACATCACAAGAAATCAACCTGAATGGTTTAGAAACGTCCTGAGCATCGCA
CCTATAATGTTCTCAAATAAAATGGCAAGACTAGGGAAAGGATACATGTTCAAAAGCAAG
AGCATGAAGCTCCGAACACAAATACCAGCAGAAATGCTAACAAGTATTGACCTGAAATAC
TTTAATGAATCAACAAGAAAGAAAATCGAGAAAATAAGGCCTCTCCTAATAGATGGCACA
GTCTCATTGAGTCCTGGAATGATGATGGGCATGTTCAACATGCTAAGTACAGTCTTAGGA
GTCTCAATCCTGAATCTTGGACAAAAGAAGTACACCAAAACAACATACTGGTGGGACGGA
CTCCAATCCTCTGATGACTTCGCCCTCATAGTGAATGCACCAAATCATGAGGGAATACAA
GCAGGAGTGGATAGATTCTACAGAACCTGCAAGCTAGTCGGAATCAATATGAGCAAAAAG
AAGTCCTACACAAATAGGACAGGGACATTTGAATTCACAAGCTTTTTCTATCGCTATGGA
TTTGTAGCCAATTTTAGCATGGAGCTGCCCAGCTTTGGAGTGTCTGGAATTAATGAATCG
GATGATATGAGCATTGGGGTAACAGTGATAAAGAACAACATGATAAACAATGACCTTGGG
CCAGCAACAGCCCAAATGGCTCTTCAACTATTCATCAAAGACTACAGATATACGTACCGG
TGCCACAGAGGAGACACACAAATTCAGACAAGGAGATCATTCGAGCTAAAGAAGCTGTGG
GAGCAAACCCGCTCAAAGGCAGGACTTTTGATTTCTGATGGAGGACCAAACTTATACAAT
ATCCGGAATCTCCACATTCCAGAAGTCTGCTTGAAGTGGGAGCTAATGGATGAAGACTAT
CAGGGGAGGCTTTGTAATCCCCTGAATCCATTTGTCAGTCATAAGGAGATTGAGTCTGTA
AACAATGCTGTGGTAATGCCAGCTCACGGTCCAGCCAAGAGCATGGAATATGATGCTGTT
GCTACTACACACTCCTGGATCCCTAAGAGGAACCGCTCCATTCTCAACACAAGCCAAAGG
GGAATTCTTGAGGATCAACAGATGTATCAGAAGTGTTGCAATCTATTCGAGAAATTCTTC
CCTAGCAGTTCGTACAGGAGACCAGTTGGAATTTCCAGCATGGTGGAGGCCATGGTGTCT
AGGGCCCGGATTGATGCACGGATTGACTTCGAGTCTGGACGGATTAAGAAAGAGGAGTTC
GCTGAGATCATGAAGATCTGTTCCACCATTGAAGAGCTCAGACGGCAAAAATAG
|
| Enzyme 42 GenBank Gene ID |
M81580  |
| Enzyme 42 GeneCard ID |
PB1  |
| Enzyme 42 GenAtlas ID |
Not Available |
| Enzyme 42 HGNC ID |
Not Available |
| Enzyme 42 Chromosome Location |
Not Available |
| Enzyme 42 Locus |
Not Available |
| Enzyme 42 SNPs |
SNPJam Report  |
| Enzyme 42 General References |
- Klimov AI, Cox NJ, Yotov WV, Rocha E, Alexandrova GI, Kendal AP: Sequence changes in the live attenuated, cold-adapted variants of influenza A/Leningrad/134/57 (H2N2) virus. Virology. 1992 Feb;186(2):795-7. [PubMed
]
|
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
17342 |
| Enzyme 43 Name |
Genome polyprotein |
| Enzyme 43 Synonyms |
- Core protein p21
- Capsid protein C
- p21
- Core protein p19
- Envelope glycoprotein E1
- gp32
- gp35
- Envelope glycoprotein E2
- NS1
- gp68
- gp70
- p7
- Protease NS2-3
- p23
- Serine protease/NTPase/helicase NS3
- Hepacivirin
- NS3P
- p70
- Non-structural protein 4A
- NS4A
- p8
- Non-structural protein 4B
- NS4B
- p27
- Non-structural protein 5A
- NS5A
- p56
- RNA-directed RNA polymerase
- NS5B
- p68
|
| Enzyme 43 Gene Name |
Not Available |
| Enzyme 43 Protein Sequence |
>Genome polyprotein
MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRG
RRQPIPKARRPEGRTWAQPGYPWPLYGNEGCGWAGWLLSPRGSRPSWGPTDPRRRSRNLG
KVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLA
LLSCLTVPASAYQVRNSSGLYHVTNDCPNSSVVYEAADAILHTPGCVPCVREGNASRCWV
AVTPTVATRDGKLPTTQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRHHWT
TQDCNCSIYPGHITGHRMAWNMMMNWSPTAALVVAQLLRIPQAIMDMIAGAHWGVLAGIK
YFSMVGNWAKVLVVLLLFAGVDAETHVTGGNAGRTTAGLVGLLTPGAKQNIQLINTNGSW
HINSTALNCNESLNTGWLAGLFYQHKFNSSGCPERLASCRRLTDFAQGWGPISYANGSGL
DERPYCWHYPPRPCGIVPAKSVCGPVYCFTPSPVVVGTTDRSGAPTYSWGANDTDVFVLN
NTRPPLGNWFGCTWMNSTGFTKVCGAPPCVIGGVGNNTLLCPTDCFRKYPEATYSRCGSG
PRITPRCMVDYPYRLWHYPCTINYTIFKVRMYVGGVEHRLEAACNWTRGERCDLEDRDRS
ELSPLLLSTTQWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGVGSSIASWAIKWEYVV
LLFLLLADARVCSCLWMMLLISQAEAALENLVILNAASLAGTHGLVSFLVFFCFAWYLKG
RWVPGAVYALYGMWPLLLLLLALPQRAYALDTEVAASCGGVVLVGLMALTLSPYYKRYIS
WCMWWLQYFLTRVEAQLHVWVPPLNVRGGRDAVILLTCVVHPALVFDITKLLLAIFGPLW
ILQASLLKVPYFVRVQGLLRICALARKIAGGHYVQMAIIKLGALTGTCVYNHLAPLRDWA
HNGLRDLAVAVEPVVFSRMETKLITWGADTAACGDIINGLPVSARRGQEILLGPADGMVS
KGWRLLAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCINGVCWT
VYHGAGTRTIASPKGPVIQTYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVI
PVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPTGHAVGLFRAAVCTRGVAKAVDFIPVEN
LETTMRSPVFTDNSSPPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAKGYKVLVLNPSVAA
TLGFGAYMSKAHGVDPNIRTGVRTITTGSPITYSTYGKFLADAGCSGGAYDIIICDECHS
TDATSISGIGTVLDQAETAGARLVVLATATPPGSVTVSHPNIEEVALSTTGEIPFYGKAI
PLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVSTDAL
MTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTLPQDAVSRTQRRGRTGRGKPGIYR
FVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLGFWEG
VFTGLTHIDAHFLSQTKQSGENFPYLVAYQATVCARAQAPPPSWDQMRKCLIRLKPTLHG
PTPLLYRLGAVQNEVTLTHPITKYIMTCMSADLEVVTSTWVLVGGVLAALAAYCLSTGCV
VIVGRIVLSGKPAIIPDREVLYQEFDEMEECSQHLPYIEQGMMLAEQFKQKALGLLQTAS
RHAEVITPAVQTNWQKLEVFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTAAVTSP
LTTGQTLLFNILGGWVAAQLAAPGAATAFVGAGLAGAALDSVGLGKVLVDILAGYGAGVA
GALVAFKIMSGEVPSTEDLVNLLPAILSPGALAVGVVFASILRRRVGPGEGAVQWMNRLI
AFASRGNHVSPTHYVPESDAAARVTAILSSLTVTQLLRRLHQWISSECTTPCSGSWLRDI
WDWICEVLSDFKTWLKAKLMPQLPGIPFVSCQRGYRGVWRGDGIMHTRCHCGAEITGHVK
NGTMRIVGPRTCKNMWSGTFFINAYTTGPCTPLPAPNYKFALWRVSAEEYVEIRRVGDFH
YVSGMTTDNLKCPCQIPSPEFFTELDGVRLHRFAPPCKPLLREEVSFRVGLHEYPVGSQL
PCEPEPDVAVLTSMLTDPSHITAEAAGRRLARGSPPSMASSSASQLSAPSLKATCTANHD
SPDAELIEANLLWRQEMGGNITRVESENKVVILDSFDPLVAEEDEREVSVPAEILRKSRR
FAPALPVWARPDYNPLLVETWKKPDYEPPVVHGCPLPPPRSPPVPPPRKKRTVVLTESTL
PTALAELATKSFGSSSTSGITGDNTTTSSEPAPSGCPPDSDVESYSSMPPLEGEPGDPDL
SDGSWSTVSSGADTEDVVCCSMSYSWTGALVTPCAAEEQKLPINALSNSLLRHHNLVYST
TSRSACQRKKKVTFDRLQVLDSHYQDVLKEVKAAASKVKANLLSVEEACSLAPPHSAKSK
FGYGAKDVRCHARKAVAHINSVWKDLLEDSVTPIDTTIMAKNEVFCVQPEKGGRKPARLI
VFPDLGVRVCEKMALYDVVSKLPLAVMGSSYGFQYSPGQRVEFLVQAWKSKKTPMGLSYD
TRCFDSTVTESDIRTEEAIYQCCDLDPQARVAIKSLTERLYVGGPLTNSRGENCGYRRCR
ASRVLTTSCGNTLTRYIKARAACRAAGLQDCTMLVCGDDLVVICESAGVQEDAASLRAFT
EAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDGAGKRVYYLTRDPTTPLARAAWETA
RHTPVNSWLGNIIMFAPTLWARMILMTHFFSVLIARDQLEQALNCEIYGACYSIEPLDLP
PIIQRLHGLSAFSLHSYSPGEINRVAACLRKLGVPPLRAWRHRAWSVRARLLARGGKAAI
CGKYLFNWAVRTKLKLTPITAAGRLDLSGWFTAGYSGGDIYHSVSHARPRWFWFCLLLLA
AGVGIYLLPNR
|
| Enzyme 43 Number of Residues |
3011 |
| Enzyme 43 Molecular Weight |
327142.8 |
| Enzyme 43 Theoretical pI |
8.37 |
| Enzyme 43 GO Classification |
| Function |
- ATP binding
- RNA binding
- RNA-directed RNA polymerase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- helicase activity
- hydrolase activity
- nucleic acid binding
- nucleotide binding
- nucleotidyltransferase activity
- peptidase activity
- purine nucleotide binding
- serine-type peptidase activity
- structural molecule activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolism
- cellular protein metabolism
- interaction between organisms
- interaction with host
- interspecies interaction between organisms
- macromolecule metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- protein metabolism
- proteolysis
- symbiosis, encompassing mutualism through parasitism
- transcription
- transformation of host cell by virus
- viral genome replication
- viral infectious cycle
- viral life cycle
- virus-host interaction
|
| Component |
- viral capsid
- viral envelope
- virion
|
|
| Enzyme 43 General Function |
Involved in ATP binding |
| Enzyme 43 Specific Function |
NS5B is a RNA-dependent RNA polymerase that plays an essential role in the virus replication |
| Enzyme 43 Pathways |
Not Available |
| Enzyme 43 Reactions |
Not Available |
| Enzyme 43 Pfam Domain Function |
|
| Enzyme 43 Signals |
|
| Enzyme 43 Transmembrane Regions |
- 169-189
359-379
726-746
758-778
783-803
814-834
882-902
929-949
1658-1678
1806-1826
1829-1849
1851-1871
1882-1902
2991-3011
|
| Enzyme 43 Essentiality |
Not Available |
| Enzyme 43 GenBank ID Protein |
329738  |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
P27958  |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
POLG_HCVH  |
| Enzyme 43 PDB ID |
1CU1  |
| Enzyme 43 PDB File |
Show |
| Enzyme 43 3D Structure |
|
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
>9036 bp
ATGAGCACGAATCCTAAACCTCAAAGAAAAACCAAACGTAACACCAACCGTCGCCCACAG
GACGTCAAGTTCCCGGGTGGCGGTCAGATCGTTGGTGGAGTTTACTTGTTGCCGCGCAGG
GGCCCTAGATTGGGTGTGCGCGCGACGAGGAAGACTTCCGAGCGGTCGCAACCTCGAGGT
AGACGTCAGCCTATCCCCAAGGCACGTCGGCCCGAGGGCAGGACCTGGGCTCAGCCCGGG
TACCCTTGGCCCCTCTATGGCAATGAGGGTTGCGGGTGGGCGGGATGGCTCCTGTCTCCC
CGTGGCTCTCGGCCTAGCTGGGGCCCCACAGACCCCCGGCGTAGGTCGCGCAATTTGGGT
AAGGTCATCGATACCCTTACGTGCGGCTTCGCCGACCTCATGGGGTACATACCGCTCGTC
GGCGCCCCTCTTGGAGGCGCTGCCAGGGCCCTGGCGCATGGCGTCCGGGTTCTGGAAGAC
GGCGTGAACTATGCAACAGGGAACCTTCCTGGTTGCTCTTTCTCTATCTTCCTTCTGGCC
CTGCTCTCTTGCCTGACTGTGCCCGCTTCAGCCTACCAAGTGCGCAATTCCTCGGGGCTT
TACCATGTCACCAATGATTGCCCTAACTCGAGTGTTGTGTACGAGGCGGCCGATGCCATC
CTGCACACTCCGGGGTGTGTCCCTTGCGTTCGCGAGGGTAACGCCTCGAGGTGTTGGGTG
GCGGTGACCCCCACGGTGGCCACCAGGGACGGCAAACTCCCCACAACGCAGCTTCGACGT
CATATCGATCTGCTTGTCGGGAGCGCCACCCTCTGCTCGGCCCTCTACGTGGGGGACCTG
TGCGGGTCTGTCTTTCTTGTTGGTCAACTGTTTACCTTCTCTCCCAGGCACCACTGGACG
ACGCAAGACTGCAATTGTTCTATCTATCCCGGCCATATAACGGGTCATCGCATGGCATGG
AATATGATGATGAACTGGTCCCCTACGGCAGCGTTGGTGGTAGCTCAGCTGCTCCGAATC
CCACAAGCCATCATGGACATGATCGCTGGCGCCCACTGGGGAGTCCTGGCGGGCATAAAG
TATTTCTCCATGGTGGGGAACTGGGCGAAGGTCCTGGTAGTGCTGCTGCTATTTGCCGGC
GTCGACGCGGAAACCCACGTCACCGGGGGAAATGCCGGCCGCACCACGGCTGGGCTTGTT
GGTCTCCTTACACCAGGCGCCAAGCAGAACATCCAACTGATCAACACCAACGGCAGTTGG
CACATCAATAGCACGGCCTTGAACTGCAATGAAAGCCTTAACACCGGCTGGTTAGCAGGG
CTCTTCTATCAGCACAAATTCAACTCTTCAGGCTGTCCTGAGAGGTTGGCCAGCTGCCGA
CGCCTTACCGATTTTGCCCAGGGCTGGGGTCCTATCAGTTATGCCAACGGAAGCGGCCTC
GACGAACGCCCCTACTGCTGGCACTACCCTCCAAGACCTTGTGGCATTGTGCCCGCAAAG
AGCGTGTGTGGCCCGGTATATTGCTTCACTCCCAGCCCCGTGGTGGTGGGAACGACCGAC
AGGTCGGGCGCGCCTACCTACAGCTGGGGTGCAAATGATACGGATGTCTTCGTCCTTAAC
AACACCAGGCCACCGCTGGGCAATTGGTTCGGTTGTACCTGGATGAACTCAACTGGATTC
ACCAAAGTGTGCGGAGCGCCCCCTTGTGTCATCGGAGGGGTGGGCAACAACACCTTGCTC
TGCCCCACTGATTGCTTCCGCAAATATCCGGAAGCCACATACTCTCGGTGCGGCTCCGGT
CCCAGGATTACACCCAGGTGCATGGTCGACTACCCGTATAGGCTTTGGCACTATCCTTGT
ACCATCAATTACACCATATTCAAAGTCAGGATGTACGTGGGAGGGGTCGAGCACAGGCTG
GAAGCGGCCTGCAACTGGACGCGGGGCGAACGCTGTGATCTGGAAGACAGGGACAGGTCC
GAGCTCAGCCCGTTGCTGCTGTCCACCACACAGTGGCAGGTCCTTCCGTGTTCTTTCACG
ACCCTGCCAGCCTTGTCCACCGGCCTCATCCACCTCCACCAGAACATTGTGGACGTGCAG
TACTTGTACGGGGTAGGGTCAAGCATCGCGTCCTGGGCCATTAAGTGGGAGTACGTCGTT
CTCCTGTTCCTTCTGCTTGCAGACGCGCGCGTCTGTTCCTGCTTGTGGATGATGTTACTC
ATATCCCAAGCGGAGGCGGCTTTGGAGAACCTCGTAATACTCAATGCAGCATCCCTGGCC
GGGACGCATGGTCTTGTGTCCTTCCTCGTGTTCTTCTGCTTTGCGTGGTATCTGAAGGGT
AGGTGGGTGCCCGGAGCGGTCTACGCCCTCTACGGGATGTGGCCTCTCCTCCTGCTCCTG
CTGGCGTTGCCTCAGCGGGCATACGCACTGGACACGGAGGTGGCCGCGTCGTGTGGCGGC
GTTGTTCTTGTCGGGTTAATGGCGCTGACTCTGTCGCCATATTACAAGCGCTATATCAGC
TGGTGCATGTGGTGGCTTCAGTATTTTCTGACCAGAGTAGAAGCGCAACTGCACGTGTGG
GTTCCCCCCCTCAACGTCCGGGGGGGGCGCGATGCCGTCATCTTACTCACGTGTGTAGTA
CACCCGGCCCTGGTATTTGACATCACCAAACTACTCCTGGCCATCTTCGGACCCCTTTGG
ATTCTTCAAGCCAGTTTGCTTAAAGTCCCCTACTTCGTGCGCGTTCAAGGCCTTCTCCGG
ATCTGCGCGCTAGCGCGGAAGATAGCCGGAGGTCATTACGTGCAAATGGCCATCATCAAG
TTAGGGGCGCTTACTGGCACCTGTGTGTATAACCATCTCGCTCCTCTTCGAGACTGGGCG
CACAACGGCCTGCGAGATCTGGCCGTGGCTGTGGAACCAGTCGTCTTCTCCCGAATGGAG
ACCAAGCTCATCACGTGGGGGGCAGATACCGCCGCGTGCGGTGACATCATCAACGGCTTG
CCCGTCTCTGCCCGTAGGGGCCAGGAGATACTGCTTGGGCCAGCCGACGGAATGGTCTCC
AAGGGGTGGAGGTTGCTGGCGCCCATCACGGCGTACGCCCAGCAGACGAGAGGCCTCCTA
GGGTGTATAATCACCAGCCTGACTGGCCGGGACAAAAACCAAGTGGAGGGTGAGGTCCAG
ATCGTGTCAACTGCTACCCAGACCTTCCTGGCAACGTGCATCAATGGGGTATGCTGGACT
GTCTACCACGGGGCCGGAACGAGGACCATCGCATCACCCAAGGGTCCTGTCATCCAGACG
TATACCAATGTGGATCAAGACCTCGTGGGCTGGCCCGCTCCTCAAGGTTCCCGCTCATTG
ACACCCTGCACCTGCGGCTCCTCGGACCTTTACCTGGTCACGAGGCACGCCGATGTCATT
CCCGTGCGCCGGCGAGGTGATAGCAGGGGTAGCCTGCTTTCGCCCCGGCCCATTTCCTAC
TTGAAAGGCTCCTCGGGGGGTCCGCTGTTGTGCCCCACGGGACACGCCGTGGGCCTATTC
AGGGCCGCGGTGTGCACCCGTGGAGTGGCTAAGGCGGTGGACTTTATCCCTGTGGAGAAC
CTAGAGACAACCATGAGATCCCCGGTGTTCACGGACAACTCCTCTCCACCAGCAGTGCCC
CAGAGCTTCCAGGTGGCCCACCTGCATGCTCCCACCGGCAGCGGTAAGAGCACCAAGGTC
CCGGCTGCGTACGCAGCCAAGGGCTACAAGGTGTTGGTGCTCAACCCCTCTGTTGCTGCA
ACACTGGGCTTTGGTGCTTACATGTCCAAGGCCCATGGGGTTGATCCTAATATCAGGACC
GGGGTGAGAACAATTACCACTGGCAGCCCCATCACGTACTCCACCTACGGCAAGTTCCTT
GCCGACGCCGGGTGCTCAGGAGGTGCTTATGACATAATAATTTGTGACGAGTGCCACTCC
ACGGATGCCACATCCATCTCGGGCATCGGCACTGTCCTTGACCAAGCAGAGACTGCGGGG
GCGAGACTGGTTGTGCTCGCCACTGCTACCCCTCCGGGCTCCGTCACTGTGTCCCATCCT
AACATCGAGGAGGTTGCTCTGTCCACCACCGGAGAGATCCCCTTTTACGGCAAGGCTATC
CCCCTCGAGGTGATCAAGGGGGGAAGACATCTCATCTTCTGCCACTCAAAGAAGAAGTGC
GACGAGCTCGCCGCGAAGCTGGTCGCATTGGGCATCAATGCCGTGGCCTACTACCGCGGT
CTTGACGTGTCTGTCATCCCGACCAGCGGCGATGTTGTCGTCGTGTCGACCGATGCTCTC
ATGACTGGCTTTACCGGCGACTTCGACTCTGTGATAGACTGCAACACGTGTGTCACTCAG
ACAGTCGATTTTAGCCTTGACCCTACCTTTACCATTGAGACAACCACGCTCCCCCAGGAT
GCTGTCTCCAGGACTCAACGCCGGGGCAGGACTGGCAGGGGGAAGCCAGGCATCTATAGA
TTTGTGGCACCGGGGGAGCGCCCCTCCGGCATGTTCGACTCGTCCGTCCTCTGTGAGTGC
TATGACGCGGGCTGTGCTTGGTATGAGCTCACGCCCGCCGAGACTACAGTTAGGCTACGA
GCGTACATGAACACCCCGGGGCTTCCCGTGTGCCAGGACCATCTTGGATTTTGGGAGGGC
GTCTTTACGGGCCTCACTCATATAGATGCCCACTTTCTATCCCAGACAAAGCAGAGTGGG
GAGAACTTTCCTTACCTGGTAGCGTACCAAGCCACCGTGTGCGCTAGGGCTCAAGCCCCT
CCCCCATCGTGGGACCAGATGCGGAAGTGTTTGATCCGCCTTAAACCCACCCTCCATGGG
CCAACACCCCTGCTATACAGACTGGGCGCTGTTCAGAATGAAGTCACCCTGACGCACCCA
ATCACCAAATACATCATGACATGCATGTCGGCCGACCTGGAGGTCGTCACGAGCACCTGG
GTGCTCGTTGGCGGCGTCCTGGCTGCTCTGGCCGCGTATTGCCTGTCAACAGGCTGCGTG
GTCATAGTGGGCAGGATCGTCTTGTCCGGGAAGCCGGCAATTATACCTGACAGGGAGGTT
CTCTACCAGGAGTTCGATGAGATGGAAGAGTGCTCTCAGCACTTACCGTACATCGAGCAA
GGGATGATGCTCGCTGAGCAGTTCAAGCAGAAGGCCCTCGGCCTCCTGCAGACCGCGTCC
CGCCATGCAGAGGTTATCACCCCTGCTGTCCAGACCAACTGGCAGAAACTCGAGGTCTTT
TGGGCGAAGCACATGTGGAATTTCATCAGTGGGATACAATACTTGGCGGGCCTGTCAACG
CTGCCTGGTAACCCCGCCATTGCTTCATTGATGGCTTTTACAGCTGCCGTCACCAGCCCA
CTAACCACTGGCCAAACCCTCCTCTTCAACATATTGGGGGGGTGGGTGGCTGCCCAGCTC
GCCGCCCCCGGTGCCGCTACCGCCTTTGTGGGCGCTGGCTTAGCTGGCGCCGCACTCGAC
AGCGTTGGACTGGGGAAGGTCCTCGTGGACATTCTTGCAGGCTATGGCGCGGGCGTGGCG
GGAGCTCTTGTGGCATTCAAGATCATGAGCGGTGAGGTCCCCTCCACGGAGGACCTGGTC
AATCTGCTGCCCGCCATCCTCTCACCTGGAGCCCTTGCAGTCGGTGTGGTCTTTGCATCA
ATACTGCGCCGGCGTGTTGGCCCGGGCGAGGGGGCAGTGCAATGGATGAACCGGCTAATA
GCCTTCGCCTCCCGGGGGAACCATGTTTCCCCCACACACTACGTGCCGGAGAGCGATGCA
GCCGCCCGCGTCACTGCCATACTCAGCAGCCTCACTGTAACCCAGCTCCTGAGGCGACTG
CATCAGTGGATAAGCTCGGAGTGTACCACTCCATGCTCCGGTTCCTGGCTAAGGGACATC
TGGGACTGGATATGCGAGGTGCTGAGCGACTTTAAGACCTGGCTGAAAGCCAAGCTCATG
CCACAACTGCCTGGGATTCCCTTTGTGTCCTGCCAGCGCGGGTATAGGGGGGTCTGGCGA
GGAGACGGCATTATGCACACTCGCTGCCACTGTGGAGCTGAGATCACTGGACATGTCAAA
AACGGGACGATGAGGATCGTCGGTCCTAGGACCTGCAAGAACATGTGGAGTGGGACGTTC
TTCATTAATGCCTACACCACGGGCCCCTGTACTCCCCTTCCTGCGCCGAACTATAAGTTC
GCGCTGTGGAGGGTGTCTGCAGAGGAATACGTGGAGATAAGGCGGGTGGGGGACTTCCAC
TACGTATCGGGCATGACTACTGACAATCTCAAATGCCCGTGCCAGATCCCATCGCCCGAA
TTTTTCACAGAATTGGACGGGGTGCGCCTACATAGGTTTGCGCCCCCTTGCAAGCCCTTG
CTGCGGGAGGAGGTATCATTCAGAGTAGGACTCCACGAGTACCCGGTGGGGTCGCAATTA
CCTTGCGAGCCCGAACCGGACGTAGCCGTGTTGACGTCCATGCTCACTGATCCCTCCCAT
ATAACAGCAGAGGCGGCCGGGAGAAGGTTGGCGAGAGGGTCACCCCCTTCTATGGCCAGC
TCCTCGGCTAGCCAGCTGTCCGCTCCATCTCTCAAGGCAACTTGCACCGCCAACCATGAC
TCCCCTGACGCCGAGCTCATAGAGGCTAACCTCCTGTGGAGGCAGGAGATGGGCGGCAAC
ATCACCAGGGTTGAGTCAGAGAACAAAGTGGTGATTCTGGACTCCTTCGATCCGCTTGTG
GCAGAGGAGGATGAGCGGGAGGTCTCCGTACCCGCAGAAATTCTGCGGAAGTCTCGGAGA
TTCGCCCCAGCCCTGCCCGTCTGGGCGCGGCCGGACTACAACCCCCTGCTAGTAGAGACG
TGGAAAAAGCCTGACTACGAACCACCTGTGGTCCATGGCTGCCCGCTACCACCTCCACGG
TCCCCTCCTGTGCCTCCGCCTCGGAAAAAGCGTACGGTGGTCCTCACCGAATCAACCCTA
CCTACTGCCTTGGCCGAGCTTGCCACCAAAAGTTTTGGCAGCTCCTCAACTTCCGGCATT
ACGGGCGACAATACGACAACATCCTCTGAGCCCGCCCCTTCTGGCTGCCCCCCCGACTCC
GACGTTGAGTCCTATTCTTCCATGCCCCCCCTGGAGGGGGAGCCTGGGGATCCGGATCTC
AGCGACGGGTCATGGTCGACGGTCAGTAGTGGGGCCGACACGGAAGATGTCGTGTGCTGC
TCAATGTCTTATTCCTGGACAGGCGCACTCGTCACCCCGTGCGCTGCGGAGGAACAAAAA
CTGCCCATCAACGCACTGAGCAACTCGTTGCTACGCCATCACAATCTGGTGTATTCCACC
ACTTCACGCAGTGCTTGCCAAAGGAAGAAGAAAGTCACATTTGACAGACTGCAAGTTCTG
GACAGCCATTACCAGGACGTGCTCAAGGAGGTCAAAGCAGCGGCGTCAAAAGTGAAGGCT
AACTTGCTATCCGTAGAGGAAGCTTGCAGCCTGGCGCCCCCACATTCAGCCAAATCCAAG
TTTGGCTATGGGGCAAAAGACGTCCGTTGCCATGCCAGAAAGGCCGTAGCCCACATCAAC
TCCGTGTGGAAAGACCTTCTGGAAGACAGTGTAACACCAATAGACACTACCATCATGGCC
AAGAACGAGGTTTTCTGCGTTCAGCCTGAGAAGGGGGGTCGTAAGCCAGCTCGTCTCATC
GTGTTCCCCGACCTGGGCGTGCGCGTGTGCGAGAAGATGGCCCTGTACGACGTGGTTAGC
AAGCTCCCCTTGGCCGTGATGGGAAGCTCCTACGGATTCCAATACTCACCAGGACAGCGG
GTTGAATTCCTCGTGCAAGCGTGGAAGTCCAAGAAGACCCCGATGGGGCTCTCGTATGAT
ACCCGCTGTTTTGACTCCACAGTCACTGAGAGCGACATCCGTACGGAGGAGGCAATTTAC
CAATGTTGTGACCTGGACCCCCAAGCCCGCGTGGCCATCAAGTCCCTCACTGAGAGGCTT
TATGTTGGGGGCCCTCTTACTAATTCAAGGGGGGAAAACTGCGGCTACCGCAGGTGCCGC
GCGAGCAGAGTACTGACAACTAGCTGTGGTAACACCCTCACTCGCTACATCAAGGCCCGG
GCAGCCTGTCGAGCCGCAGGGCTCCAGGACTGCACCATGCTCGTGTGTGGCGACGACTTA
GTCGTTATCTGTGAAAGTGCGGGGGTCCAGGAGGACGCGGCGAGCCTGAGAGCCTTCACG
GAGGCTATGACCAGGTACTCCGCCCCCCCCGGGGACCCCCCACAACCAGAATACGACTTG
GAGCTTATAACATCATGCTCCTCCAACGTGTCAGTCGCCCACGACGGCGCTGGAAAGAGG
GTCTACTACCTTACCCGTGACCCTACAACCCCCCTCGCGAGAGCCGCGTGGGAGACAGCA
AGACACACTCCAGTCAATTCCTGGCTAGGCAACATAATCATGTTTGCCCCCACACTGTGG
GCGAGGATGATACTGATGACCCACTTCTTTAGCGTCCTCATAGCCAGGGATCAGCTTGAA
CAGGCTCTCAACTGCGAGATCTACGGAGCCTGCTACTCCATAGAACCACTGGATCTACCT
CCAATCATTCAAAGACTCCATGGCCTCAGCGCATTTTCACTCCACAGTTACTCTCCAGGT
GAAATTAATAGGGTGGCCGCATGCCTCAGAAAACTTGGGGTCCCGCCCTTGCGAGCTTGG
AGACACCGGGCCTGGAGCGTCCGCGCTAGGCTTCTGGCCAGAGGAGGCAAGGCTGCCATA
TGTGGCAAGTACCTCTTCAACTGGGCAGTAAGAACAAAGCTCAAACTCACTCCGATAACG
GCCGCTGGCCGGCTGGACTTGTCCGGCTGGTTCACGGCTGGCTACAGCGGGGGAGACATT
TATCACAGCGTGTCTCATGCCCGGCCCCGCTGGTTCTGGTTTTGCCTACTCCTGCTTGCT
GCAGGGGTAGGCATCTACCTCCTCCCCAACCGATGA
|
| Enzyme 43 GenBank Gene ID |
M67463  |
| Enzyme 43 GeneCard ID |
Not Available |
| Enzyme 43 GenAtlas ID |
Not Available |
| Enzyme 43 HGNC ID |
Not Available |
| Enzyme 43 Chromosome Location |
Not Available |
| Enzyme 43 Locus |
Not Available |
| Enzyme 43 SNPs |
Not Available |
| Enzyme 43 General References |
- Inchauspe G, Zebedee S, Lee DH, Sugitani M, Nasoff M, Prince AM: Genomic structure of the human prototype strain H of hepatitis C virus: comparison with American and Japanese isolates. Proc Natl Acad Sci U S A. 1991 Nov 15;88(22):10292-6. [PubMed
]
- Kolykhalov AA, Agapov EV, Blight KJ, Mihalik K, Feinstone SM, Rice CM: Transmission of hepatitis C by intrahepatic inoculation with transcribed RNA. Science. 1997 Jul 25;277(5325):570-4. [PubMed
]
- Yanagi M, Purcell RH, Emerson SU, Bukh J: Transcripts from a single full-length cDNA clone of hepatitis C virus are infectious when directly transfected into the liver of a chimpanzee. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8738-43. [PubMed
]
- Grakoui A, McCourt DW, Wychowski C, Feinstone SM, Rice CM: A second hepatitis C virus-encoded proteinase. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10583-7. [PubMed
]
- Grakoui A, Wychowski C, Lin C, Feinstone SM, Rice CM: Expression and identification of hepatitis C virus polyprotein cleavage products. J Virol. 1993 Mar;67(3):1385-95. [PubMed
]
- Ide Y, Zhang L, Chen M, Inchauspe G, Bahl C, Sasaguri Y, Padmanabhan R: Characterization of the nuclear localization signal and subcellular distribution of hepatitis C virus nonstructural protein NS5A. Gene. 1996 Dec 5;182(1-2):203-11. [PubMed
]
- Reed KE, Rice CM: Identification of the major phosphorylation site of the hepatitis C virus H strain NS5A protein as serine 2321. J Biol Chem. 1999 Sep 24;274(39):28011-8. [PubMed
]
- Ghosh AK, Majumder M, Steele R, Yaciuk P, Chrivia J, Ray R, Ray RB: Hepatitis C virus NS5A protein modulates transcription through a novel cellular transcription factor SRCAP. J Biol Chem. 2000 Mar 10;275(10):7184-8. [PubMed
]
- Cocquerel L, Wychowski C, Minner F, Penin F, Dubuisson J: Charged residues in the transmembrane domains of hepatitis C virus glycoproteins play a major role in the processing, subcellular localization, and assembly of these envelope proteins. J Virol. 2000 Apr;74(8):3623-33. [PubMed
]
- Kittlesen DJ, Chianese-Bullock KA, Yao ZQ, Braciale TJ, Hahn YS: Interaction between complement receptor gC1qR and hepatitis C virus core protein inhibits T-lymphocyte proliferation. J Clin Invest. 2000 Nov;106(10):1239-49. [PubMed
]
- Penin F, Combet C, Germanidis G, Frainais PO, Deleage G, Pawlotsky JM: Conservation of the conformation and positive charges of hepatitis C virus E2 envelope glycoprotein hypervariable region 1 points to a role in cell attachment. J Virol. 2001 Jun;75(12):5703-10. [PubMed
]
- Schmidt-Mende J, Bieck E, Hugle T, Penin F, Rice CM, Blum HE, Moradpour D: Determinants for membrane association of the hepatitis C virus RNA-dependent RNA polymerase. J Biol Chem. 2001 Nov 23;276(47):44052-63. [PubMed
]
- Cocquerel L, Op de Beeck A, Lambot M, Roussel J, Delgrange D, Pillez A, Wychowski C, Penin F, Dubuisson J: Topological changes in the transmembrane domains of hepatitis C virus envelope glycoproteins. EMBO J. 2002 Jun 17;21(12):2893-902. [PubMed
]
- Carrere-Kremer S, Montpellier-Pala C, Cocquerel L, Wychowski C, Penin F, Dubuisson J: Subcellular localization and topology of the p7 polypeptide of hepatitis C virus. J Virol. 2002 Apr;76(8):3720-30. [PubMed
]
- Brass V, Bieck E, Montserret R, Wolk B, Hellings JA, Blum HE, Penin F, Moradpour D: An amino-terminal amphipathic alpha-helix mediates membrane association of the hepatitis C virus nonstructural protein 5A. J Biol Chem. 2002 Mar 8;277(10):8130-9. Epub 2001 Dec 14. [PubMed
]
- Egger D, Wolk B, Gosert R, Bianchi L, Blum HE, Moradpour D, Bienz K: Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex. J Virol. 2002 Jun;76(12):5974-84. [PubMed
]
- Gosert R, Egger D, Lohmann V, Bartenschlager R, Blum HE, Bienz K, Moradpour D: Identification of the hepatitis C virus RNA replication complex in Huh-7 cells harboring subgenomic replicons. J Virol. 2003 May;77(9):5487-92. [PubMed
]
- Pavlovic D, Neville DC, Argaud O, Blumberg B, Dwek RA, Fischer WB, Zitzmann N: The hepatitis C virus p7 protein forms an ion channel that is inhibited by long-alkyl-chain iminosugar derivatives. Proc Natl Acad Sci U S A. 2003 May 13;100(10):6104-8. Epub 2003 Apr 28. [PubMed
]
- Sakai A, Claire MS, Faulk K, Govindarajan S, Emerson SU, Purcell RH, Bukh J: The p7 polypeptide of hepatitis C virus is critical for infectivity and contains functionally important genotype-specific sequences. Proc Natl Acad Sci U S A. 2003 Sep 30;100(20):11646-51. Epub 2003 Sep 22. [PubMed
]
- Dimitrova M, Imbert I, Kieny MP, Schuster C: Protein-protein interactions between hepatitis C virus nonstructural proteins. J Virol. 2003 May;77(9):5401-14. [PubMed
]
- Lundin M, Monne M, Widell A, Von Heijne G, Persson MA: Topology of the membrane-associated hepatitis C virus protein NS4B. J Virol. 2003 May;77(9):5428-38. [PubMed
]
- Cocquerel L, Kuo CC, Dubuisson J, Levy S: CD81-dependent binding of hepatitis C virus E1E2 heterodimers. J Virol. 2003 Oct;77(19):10677-83. [PubMed
]
- Bartosch B, Dubuisson J, Cosset FL: Infectious hepatitis C virus pseudo-particles containing functional E1-E2 envelope protein complexes. J Exp Med. 2003 Mar 3;197(5):633-42. [PubMed
]
- Bartosch B, Vitelli A, Granier C, Goujon C, Dubuisson J, Pascale S, Scarselli E, Cortese R, Nicosia A, Cosset FL: Cell entry of hepatitis C virus requires a set of co-receptors that include the CD81 tetraspanin and the SR-B1 scavenger receptor. J Biol Chem. 2003 Oct 24;278(43):41624-30. Epub 2003 Aug 11. [PubMed
]
- Op De Beeck A, Voisset C, Bartosch B, Ciczora Y, Cocquerel L, Keck Z, Foung S, Cosset FL, Dubuisson J: Characterization of functional hepatitis C virus envelope glycoproteins. J Virol. 2004 Mar;78(6):2994-3002. [PubMed
]
- Carrere-Kremer S, Montpellier C, Lorenzo L, Brulin B, Cocquerel L, Belouzard S, Penin F, Dubuisson J: Regulation of hepatitis C virus polyprotein processing by signal peptidase involves structural determinants at the p7 sequence junctions. J Biol Chem. 2004 Oct 1;279(40):41384-92. Epub 2004 Jul 7. [PubMed
]
- Cormier EG, Durso RJ, Tsamis F, Boussemart L, Manix C, Olson WC, Gardner JP, Dragic T: L-SIGN (CD209L) and DC-SIGN (CD209) mediate transinfection of liver cells by hepatitis C virus. Proc Natl Acad Sci U S A. 2004 Sep 28;101(39):14067-72. Epub 2004 Sep 15. [PubMed

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