|
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 |
5636 |
| Enzyme 9 Name |
N-acylneuraminate cytidylyltransferase |
| Enzyme 9 Synonyms |
- CMP-N- acetylneuraminic acid synthetase
- CMP-NeuNAc synthetase
|
| Enzyme 9 Gene Name |
CMAS |
| Enzyme 9 Protein Sequence |
>N-acylneuraminate cytidylyltransferase
MDSVEKGAATSVSNPRGRPSRGRPPKLQRNSRGGQGRGVEKPPHLAALILARGGSKGIPL
KNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVHRRSSEVSKDSS
TSLDAIIEFLNYHNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRW
SEIQKGVREVTEPLNLNPAKRPRRQDWDGELYENGSFYFAKRHLIEMGYLQGGKMAYYEM
RAEHSVDIDVDIDWPIAEQRVLRYGYFGKEKLKEIKLLVCNIDGCLTNGHIYVSGDQKEI
ISYDVKDAIGISLLKKSGIEVRLISERACSKQTLSSLKLDCKMEVSVSDKLAVVDEWRKE
MGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAEH
ICLLMEKVNNSCQK
|
| Enzyme 9 Number of Residues |
434 |
| Enzyme 9 Molecular Weight |
48380 |
| Enzyme 9 Theoretical pI |
8.02 |
| Enzyme 9 GO Classification |
| Function |
| — |
| Process |
- carbohydrate biosynthesis
- lipopolysaccharide biosynthesis
- macromolecule biosynthesis
- macromolecule metabolism
- metabolism
- physiological process
- polysaccharide biosynthesis
|
| Component |
| — |
|
| Enzyme 9 General Function |
Not Available |
| Enzyme 9 Specific Function |
Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN) |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
22085790  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q8NFW8  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
NEUA_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1305 bp
ATGGACTCGGTGGAGAAGGGGGCCGCCACCTCCGTCTCCAACCCGCGGGGGCGACCGTCC
CGGGGCCGGCCGCCGAAGCTGCAGCGCAACTCTCGCGGCGGCCAGGGCCGAGGTGTGGAG
AAGCCCCCGCACCTGGCAGCCCTAATTCTGGCCCGGGGAGGCAGCAAAGGCATCCCCCTG
AAGAACATTAAGCACCTGGCGGGGGTCCCGCTCATTGGCTGGGTCCTGCGTGCGGCCCTG
GATTCAGGGGCCTTCCAGAGTGTATGGGTTTCGACAGACCATGATGAAATTGAGAATGTG
GCCAAACAATTTGGTGCACAAGTTCATCGAAGAAGTTCTGAAGTTTCAAAAGACAGCTCT
ACCTCACTAGATGCCATCATAGAATTTCTTAATTATYATAATGAGGKTGACATTGTAGGA
AATATTCAAGCTACTTCTYCATGTTTACATCCTACTGATCTTCAAAAAGTTGCAGAAATG
ATTCGAGAAGAAGGATATGATTCTGKTTTCTCTGTTGTGAGACGCCATCAGTTTCGATGG
AGTGAAATTCAGAAAGGAGTTCGTGAAGTGACCGAACCTCTGAATTTAAATCCAGCTAAA
CGGCCTCGTCGACAAGACTGGGATGGAGAATTATATGAAAATGGCTCATTTTATTTTGCT
AAAAGACATTTGATAGAGATGGGTTACTTGCAGGGTGGAAAAATGGCATACTACGAAATG
CGAGCTGAACATAGTGTGGATATAGATGTGGATATTGATTGGCCTATTGCAGAGCAAAGA
GTATTAAGATATGGCTATTTTGGCAAAGAGAAGCTTAAGGAAATAAAACTTTTGGTTTGC
AATATTGATGGATGTCTCACCAATGGCCACATTTATGTATCAGGAGACCAAAAAGAAATA
ATATCTTATGATGTAAAAGATGCTATTGGGATAAGTTTATTAAAGAAAAGTGGTATTGAG
GTGAGGCTAATCTCAGAAAGGGCCTGTTCAAAGCAGACGCTGTCTTCTTTAAAACTGGAT
TGCAAAATGGAAGTCAGTGTATCAGACAAGCTAGCAGTTGTAGATGAATGGAGAAAAGAA
ATGGGCCTGTGCTGGAAAGAAGTGGCATATCTTGGAAATGAAGTGTCTGATGAAGAGTGC
TTGAAGAGAGTGGGCCTAAGTGGCGCTCCTGCTGATGCCTGTTCCTACGCCCAGAAGGCT
GTTGGATACATTTGCAAATGTAATGGTGGCCGTGGTGCCATCCGAGAATTTGCAGAGCAC
ATTTGCCTACTAATGGAAAAAGTTAATAATTCATGCCAAAAATAG
|
| Enzyme 9 GenBank Gene ID |
AF397212  |
| Enzyme 9 GeneCard ID |
CMAS  |
| Enzyme 9 GenAtlas ID |
CMAS  |
| Enzyme 9 HGNC ID |
HGNC:18290  |
| Enzyme 9 Chromosome Location |
Not Available |
| Enzyme 9 Locus |
Not Available |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
Not Available |
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5668 |
| Enzyme 10 Name |
Inosine triphosphate pyrophosphatase |
| Enzyme 10 Synonyms |
- ITPase
- Inosine triphosphatase
- Putative oncogene protein hlc14-06-p
|
| Enzyme 10 Gene Name |
ITPA |
| Enzyme 10 Protein Sequence |
>Inosine triphosphate pyrophosphatase
MAASLVGKKIVFVTGNAKKLEEVVQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEA
VRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLLAGFEDKSAYALCTFAL
STGDPSQPVRLFRGRTSGRIVAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFR
ALLELQEYFGSLAA
|
| Enzyme 10 Number of Residues |
194 |
| Enzyme 10 Molecular Weight |
21446 |
| Enzyme 10 Theoretical pI |
5.34 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 10 General Function |
Nucleotide transport and metabolism |
| Enzyme 10 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 10 Pathways |
|
| Enzyme 10 Reactions |
- A nucleoside triphosphate + H2O = a nucleotide + diphosphate
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
13398328  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q9BY32  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
ITPA_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>585 bp
ATGGCGGCCTCATTGGTGGGGAAGAAGATCGTGTTTGTAACGGGGAACGCCAAGAAGCTG
GAGGAGGTCGTTCAGATTCTAGGAGATAAGTTTCCACGCACTTTGGTGGCACAGAAAATT
GACCTGCCGGAGTACCAGGGGGAGCCGGATGAGATTTCCATACAGAAATGTCAGGAGGCA
GTTCGCCAGGTACAGGGGCCCGTGCTGGTTGAGGACACTTGTCTGTGCTTCAATGCCCTT
GGAGGGCTCCCCGGCCCCTACATAAAGTGGTTTCTGGAGAAGTTAAAGCCTGAAGGTCTC
CACCAGCTCCTGGCCGGGTTCGAGGACAAGTCAGCCTATGCGCTCTGCACGTTTGCACTC
AGCACCGGGGACCCAAGCCAGCCCGTGCGCCTGTTCAGGGGCCGGACCTCGGGCCGGATC
GTGGCACCCAGAGGCTGCCAGGACTTTGGCTGGGACCCCTGCTTTCAGCCTGATGGATAT
GAGCAGACGTACGCAGAGATGCCTAAGGCGGAGAAGAACGCTGTCTCCCATCGCTTCCGG
GCCCTGCTGGAGCTGCAGGAGTACTTTGGCAGTTTGGCAGCTTGA
|
| Enzyme 10 GenBank Gene ID |
AF219116  |
| Enzyme 10 GeneCard ID |
ITPA  |
| Enzyme 10 GenAtlas ID |
ITPA  |
| Enzyme 10 HGNC ID |
HGNC:6176  |
| Enzyme 10 Chromosome Location |
20 |
| Enzyme 10 Locus |
20p |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 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 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5949 |
| Enzyme 11 Name |
CTP synthase 1 |
| Enzyme 11 Synonyms |
- UTP--ammonia ligase 1
- CTP synthetase 1
|
| Enzyme 11 Gene Name |
CTPS |
| Enzyme 11 Protein Sequence |
>CTP synthase 1
MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFV
LDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDA
IQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHV
SLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ
VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCS
IALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQK
LCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDAN
STEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRH
RFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPY
FGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD
|
| Enzyme 11 Number of Residues |
591 |
| Enzyme 11 Molecular Weight |
66691 |
| Enzyme 11 Theoretical pI |
6.42 |
| Enzyme 11 GO Classification |
| Function |
- CTP synthase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
- pyrimidine nucleotide biosynthesis
- pyrimidine nucleotide metabolism
|
| Component |
| — |
|
| Enzyme 11 General Function |
Nucleotide transport and metabolism |
| Enzyme 11 Specific Function |
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- ATP + UTP + NH3 = ADP + phosphate + CTP
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
30293  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
P17812  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
PYRG1_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1776 bp
ATGAAGTACATTCTGGTTACTGGTGGTGTTATATCAGGAATTGGAAAAGGAATCATTGCC
AGCAGTGTGGGCACAATACTCAAGTCATGTGGTTTACATGTAACTTCAATCAAAATTGAC
CCCTACATTAACATTGATGCAGGAACATTCTCTCCTTATGAGCATGGTGAGGTTTTTGTG
CTGGATGATGGTGGGGAAGTAGACCTTGACCTGGGTAACTATGAGCGGTTCCTTGACATC
CGCCTCACCAAGGACAATAATCTGACCACTGGAAAGATATACCAGTATGTCATTAACAAG
GAACGGAAAGGAGATTACTTGGGGAAAACTGTCCAAGTTGTCCCTCATATCACAGATGCA
ATCCAGGAGTGGGTGATGAGACAGGCGTTAATACCTGTAGATGAAGATGGCCTGGAACCT
CAAGTGTGTGTTATTGAGCTTGGTGGAACCGTGGGGGACATAGAAAGCATGCCCTTTATT
GAGGCCTTCCGTCAGTTCCAATTCAAGGTCAAAAGAGAGAACTTTTGTAACATCCACGTC
AGTCTAGTTCCCCAGCCAAGTTCAACAGGGGAACAGAAGACTAAACCTACCCAGAATAGT
GTTCGGGAACTTAGAGGACTTGGGCTTTCCCCAGATCTGGTTGTATGCAGGTGCTCAAAT
CCACTTGACACATCAGTGAAGGAGAAAATATCAATGTTCTGCCATGTTGAGCCTGAACAA
GTGATCTGTGTCCACGATGTCTCATCCATCTACCGAGTCCCCTTGTTGTTAGAGGAGCAA
GGGGTTGTAGATTATTTTCTTCGAAGACTTGACCTTCCTATTGAGAGGCAGCCAAGAAAA
ATGCTGATGAAATGGAAAGAGATGGCTGACAGATATGATCGCTTGCTGGAGACCTGCTCT
ATTGCCCTTGTGGCGAAATACACCGAGTTCTCAGACTCCTATGCCTCTGTCATTAAGGCT
CTGGAGCATTCTGCACTGGCCATCAACCACAAATTGGAAATCAAGTACATAGATTCTGCG
GACTTGGAGCCCATCACCTCGCAAGAAGAGCCCGTGCGCTACCACGAAGCTTGGCAGAAG
CTCTGTAGTGCTCATGGAGTGCTGGTTCCAGGAGGATTTGGTGTTCGAGGAACAGAAGGA
AAAATCCAAGCAATTGCCTGGGCTCGGAATCAGAAAAAGCCTTTTTTGGGCGTGTGCTTA
GGGATGCAGTTGGCAGTGGTTGAATTCTCAAGAAACGTGCTGGGATGGCAAGATGCCAAT
TCTACAGAGTTTGACCCTACGACCAGTCATCCCGTGGTCGTAGACATGCCAGAACACAAC
CCAGGGCAGATGGGCGGAACCATGAGGCTGGGCAAGAGGAGAACCCTGTTCCAGACCAAG
AACTCAGTCATGAGGAAACTCTATGGAGACGCAGACTACTTGGAAGAGAGGCACCGCCAC
CGATTTGAGGTGAATCCAGTCTGGAAAAAGTGTTTGGAAGAACAAGGCTTGAAGTTTGTT
GGCCAAGATGTTGAAGGAGAGAGAATGGAAATTGTGGAGTTAGAAGATCATCCCTTTTTT
GTTGGGGTTCAGTACCACCCTGAGTTCCTGTCCAGGCCTATCAAGCCCTCCCCACCATAC
TTTGGCCTCCTCCTGGCCTCTGTGGGGCGGCTCTCACATTACCTCCAGAAAGGCTGCAGG
CTCTCACCCAGGGACACCTATAGTGACAGGAGTGGAAGCAGCTCCCCTGACTCTGAAATC
ACCGAACTGAAGTTTCCATCAATAAATCATGACTGA
|
| Enzyme 11 GenBank Gene ID |
X52142  |
| Enzyme 11 GeneCard ID |
CTPS  |
| Enzyme 11 GenAtlas ID |
CTPS  |
| Enzyme 11 HGNC ID |
HGNC:2519  |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
1p34.1 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Yamauchi M, Yamauchi N, Meuth M: Molecular cloning of the human CTP synthetase gene by functional complementation with purified human metaphase chromosomes. EMBO J. 1990 Jul;9(7):2095-9. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6007 |
| Enzyme 12 Name |
Choline-phosphate cytidylyltransferase B |
| Enzyme 12 Synonyms |
- Phosphorylcholine transferase B
- CTP:phosphocholine cytidylyltransferase B
- CT B
- CCT B
- CCT-beta
|
| Enzyme 12 Gene Name |
PCYT1B |
| Enzyme 12 Protein Sequence |
>Choline-phosphate cytidylyltransferase B
MPVVTTDAESETGIPKSLSNEPPSETMEEIEHTCPQPRLTLTAPAPFADETNCQCQAPHE
KLTIAQARLGTPADRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHK
FKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLEKHKIDFVAHDDIPYSSAGSDD
VYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKRY
RFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLELFGPDGAWK
QMFQERSSRMLQALSPKQSPVSSPTRSRSPSRSPSPTFSWLPLKTSPPSSPKAASASISS
MSEGDEDEK
|
| Enzyme 12 Number of Residues |
369 |
| Enzyme 12 Molecular Weight |
41940 |
| Enzyme 12 Theoretical pI |
6.36 |
| Enzyme 12 GO Classification |
| Function |
- catalytic activity
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 12 Specific Function |
Controls phosphatidylcholine synthesis |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- CTP + choline phosphate = diphosphate + CDP-choline
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
3153239  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q9Y5K3  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
PCY1B_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>993 bp
ATGCCAGTAGTTACCACTGATGCTGAGTCAGAAACAGGTATCCCAAAATCCCTTTCCAAT
GAGCCTCCCTCAGAAACCATGGAGGAAATAGAGCACACATGCCCACAGCCTCGACTGACC
CTGACTGCACCTGCCCCATTTGCTGATGAAACCAACTGCCAGTGTCAAGCACCCCATGAA
AAACTGACCATTGCTCAGGCCCGCTTAGGAACACCAGCTGACAGGCCTGTCAGAGTATAC
GCCGATGGAATATTTGACCTCTTCCACTCAGGTCATGCAAGAGCCCTTATGCAAGCAAAA
ACACTGTTTCCCAACAGCTACTTGTTGGTAGGAGTTTGCAGTGATGATCTCACCCACAAA
TTCAAAGGTTTCACCGTGATGAATGAAGCCGAGAGATACGAAGCTCTCAGACACTGTCGC
TACGTAGACGAAGTTATCAGAGATGCTCCCTGGACACTCACGCCAGAGTTTCTGGAAAAA
CACAAGATTGACTTTGTGGCTCATGATGACATTCCGTATTCCTCTGCTGGCTCTGATGAT
GTTTACAAGCACATAAAGGAAGCAGGGATGTTCGTTCCAACGCAGAGAACAGAAGGCATC
TCAACATCGGACATCATTACCAGAATTGTTCGTGACTATGATGTTTATGCCCGACGTAAC
CTCCAGAGAGGGTATACAGCCAAGGAACTGAATGTCAGCTTTATAAATGAGAAGAGGTAC
CGTTTCCAGAACCAAGTGGACAAAATGAAGGAAAAAGTCAAGAATGTGGAGGAAAGATCA
AAGGAATTTGTGAACAGAGTGGAAGAAAAGAGCCATGATCTAATTCAAAAGTGGGAAGAG
AAGTCAAGGGAATTCATTGGCAACTTCCTAGAACTGTTTGGACCTGATGGAGCATGGAAG
CAGATGTTCCAGGAGAGGAGCAGCCGGATGCTGCAGGCCTTATCCCCGAAGCAGAGCCCT
CTGAAGAGTTGGGCGAGGTGCAGAGACTTCTAG
|
| Enzyme 12 GenBank Gene ID |
AF052510  |
| Enzyme 12 GeneCard ID |
PCYT1B  |
| Enzyme 12 GenAtlas ID |
PCYT1B  |
| Enzyme 12 HGNC ID |
HGNC:8755  |
| Enzyme 12 Chromosome Location |
X |
| Enzyme 12 Locus |
Xp22.11 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Lykidis A, Murti KG, Jackowski S: Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase. J Biol Chem. 1998 May 29;273(22):14022-9. [PubMed
]
- Lykidis A, Baburina I, Jackowski S: Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTbeta splice variant. J Biol Chem. 1999 Sep 17;274(38):26992-7001. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6009 |
| Enzyme 13 Name |
6-phosphofructokinase type C |
| Enzyme 13 Synonyms |
- Phosphofructokinase 1
- Phosphohexokinase
- Phosphofructo-1-kinase isozyme C
- PFK-C
- 6- phosphofructokinase, platelet type
|
| Enzyme 13 Gene Name |
PFKP |
| Enzyme 13 Protein Sequence |
>6-phosphofructokinase type C
MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFI
YEGYQGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTREGRLKAACNLLQRGIT
NLCVIGGDGSLTGANLFRKEWSGLLEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCG
TDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLP
ESPPEEGWEEQMCVKLSENRARKKRLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDT
RVTILGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACVVSLNGNHAVRLPLMEC
VQMTQDVQKAMDERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGA
PAAGMNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWTDVGGWTGQGGSILGTK
RVLPGKYLEEIATQMRTHSINALLIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVS
NNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGA
DAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKG
VFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEARGRGKKFTTDDSICVL
GISKRNVIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAKYKASYDVSDSGQLEHVQ
PWSV
|
| Enzyme 13 Number of Residues |
784 |
| Enzyme 13 Molecular Weight |
85597 |
| Enzyme 13 Theoretical pI |
7.60 |
| Enzyme 13 GO Classification |
| Function |
- 6-phosphofructokinase activity
- catalytic activity
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
- 6-phosphofructokinase complex
- cell
- cytoplasm
- intracellular
- protein complex
|
|
| Enzyme 13 General Function |
Carbohydrate transport and metabolism |
| Enzyme 13 Specific Function |
ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
560105  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q01813  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
K6PP_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>2355 bp
ATGGACGCGGACGACTCCCGGGCCCCCAAGGGCTCCTTGCGGAAGTTCCTGGAGCACCTC
TCCGGGGCCGGCAAGGCCATCGGCGTGCTGACCAGCGGCGGGGATGCTCAAGGTATGAAC
GCTGCCGTCCGTGCCGTGGTGCGCATGGGTATCTACGTGGGGGCCAAGGTGTACTTCATC
TACGAGGGCTACCAGGGCATGGTGGACGGAGGCTCAAACATCGCAGAGGCCGACTGGGAG
AGTGTCTCCAGCATCCTGCAAGTGGGCGGGACGATCATTGGCAGTGCGCGGTGCCAGGCC
TTCCGCACGCGGGAAGGCCGCCTGAAGGCTGCTTGCAACCTGCTGCAGCGCGGCATCACC
AACCTGTGTGTGATCGGCGGGGACGGGAGCCTCACCGGGGCCAACCTCTTCCGGAAGGAG
TGGAGTGGGCTGCTGGAGGAGCTGGCCAGGAACGGCCAGATCGATAAGGAGGCCGTGCAG
AAGTACGCCTACCTCAACGTGGTGGGCATGGTGGGCTCCATCGACAATGATTTCTGCGGC
ACCGACATGACCATCGGCACGGACTCCGCCCTGCACAGGATCATCGAGGTCGTCGACGCC
ATCATGACCACGGCCCAGAGCCACCAGAGGACCTTCGTTCTGGAGGTGATGGGACGACAC
TGTGGGTACCTGGCCCTGGTGAGTGCCTTGGCCTGCGGTGCGGACTGGGTGTTCCTTCCA
GAATCTCCACCAGAGGAAGGCTGGGAGGAGCAGATGTGTGTCAAACTCTCGGAGAACCGT
GCCCGGAAAAAAAGGCTGAATATTATTATTGTGGCTGAAGGAGCAATTGATACCCAAAAT
AAACCCATCACCTCTGAGAAAATCAAAGAGCTTGTCGTCACGCAGCTGGGCTATGACACA
CGTGTGACCATCCTCGGGCACGTGCAGAGAGGAGGGACCCCTTCGGCATTCGACAGGATC
TTGGCCAGCCGCATGGGAGTGGAGGCAGTCATCGCCTTGCTAGAGGCCACCCCGGACACC
CCAGCTTGCGTCGTGTCACTGAACGGGAACCACGCCGTGCGCCTGCCGCTGATGGAGTGC
GTGCAGATGACTCAGGATGTGCAGAAGGCGATGGACGAGAGGAGATTTCAAGATGCGGTT
CGACTCCGAGGGAGGAGCTTTGCGGGCAACCTGAACACCTACAAGCGACTTGCCATCAAG
CTGCCGGATGATCAGATCCCAAAGACCAATTGCAACGTAGCTGTCATCAACGTGGGGGCA
CCCGCGGCTGGGATGAACGCGGCCGTACGCTCAGCTGTGCGCGTGGGCATTGCCGACGGC
CACAGGATGCTCGCCATCTATGATGGCTTTGACGGCTTCGCCAAGGGCCAGATCAAAGAA
ATCGGCTGGACAGATGTCGGGGGCTGGACCGGCCAAGGAGGCTCCATTCTTGGGACAAAA
CGCGTTCTCCCGGGGAAGTACTTGGAAGAGATCGCCACACAGATGCGCACGCACAGCATC
AACGCGCTGCTGATCATCGGTGGATTCGAGGCCTACCTGGGACTCCTGGAGCTGTCAGCC
GCCCGGGAGAAGCACGAGGAGTTCTGTGTCCCCATGGTCATGGTTCCCGCTACTGTGTCC
AACAATGTGCCGGGTTCCGATTTCAGCATCGGGGCAGACACCGCCCTGAACACTATCACC
GACACCTGCGACCGCATCAAGCAGTCCGCCAGCGGAACCAAGCGGCGCGTGTTCATCATC
GAGACCATGGGCGGCTACTGTGGCTACCTGGCCAACATGGGGGGGCTCGCGGCCGGAGCT
GATGCCGCATACATTTTCGAAGAGCCCTTCGACATCAGGGATCTGCAGTCCAACGTGGAG
CACCTGACGGAGAAAATGAAGACCACCATCCAGAGAGGCCTTGTGCTCAGAAATGAGAGC
TGCAGTGAAAACTACACCACCGACTTCATTTACCAGCTGTATTCAGAAGAGGGCAAAGGC
GTGTTTGACTGCAGGAAGAACGTGCTGGGTCACATGCAGCAGGGTGGGGCACCCTCTCCA
TTTGATAGAAACTTTGGAACCAAAATCTCTGCCAGAGCTATGGAGTGGATCACTGCAAAA
CTCAAGGAGGCCCGGGGCAGAGGAAAAAAATTTACCACCGATGATTCCATTTGTGTGCTG
GGAATAAGCAAAAGAAACGTTATTTTTCAACCTGTGGCAGAGCTGAAGAAGCAAACGGAT
TTTGAGCACAGGATTCCCAAAGAACAGTGGTGGCTCAAGCTACGGCCCCTCATGAAAATC
CTGGCCAAGTACAAGGCCAGCTATGACGTGTCGGACTCAGGCCAGCTGGAACATGTGCAG
CCCTGGAGTGTCTGA
|
| Enzyme 13 GenBank Gene ID |
D25328  |
| Enzyme 13 GeneCard ID |
PFKP  |
| Enzyme 13 GenAtlas ID |
PFKP  |
| Enzyme 13 HGNC ID |
HGNC:8878  |
| Enzyme 13 Chromosome Location |
10 |
| Enzyme 13 Locus |
10p15.3-p15.2 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Eto K, Sakura H, Yasuda K, Hayakawa T, Kawasaki E, Moriuchi R, Nagataki S, Yazaki Y, Kadowaki T: Cloning of a complete protein-coding sequence of human platelet-type phosphofructokinase isozyme from pancreatic islet. Biochem Biophys Res Commun. 1994 Feb 15;198(3):990-8. [PubMed
]
- Simpson CJ, Fothergill-Gilmore LA: Isolation and sequence of a cDNA encoding human platelet phosphofructokinase. Biochem Biophys Res Commun. 1991 Oct 15;180(1):197-203. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
6011 |
| Enzyme 14 Name |
DNA-directed RNA polymerase III subunit D |
| Enzyme 14 Synonyms |
- DNA-directed RNA polymerase III 47 kDa polypeptide
- RNA polymerase C subunit 4
- RPC4
- RPC53
- Protein BN51
|
| Enzyme 14 Gene Name |
POLR3D |
| Enzyme 14 Protein Sequence |
>DNA-directed RNA polymerase III subunit D
MSEGNAAGEPSTPGGPRPLLTGARGLIGRRPAPPLTPGRLPSIRSRDLTLGGVKKKTFTP
NIISRKIKEEPKEEVTVKKEKRERDRDRQREGHGRGRGRPEVIQSHSIFEQGPAEMMKKK
GNWDKTVDVSDMGPSHIINIKKEKRETDEETKQILRMLEKDDFLDDPGLRNDTRNMPVQL
PLAHSGWLFKEENDEPDVKPWLAGPKEEDMEVDIPAVKVKEEPRDEEEEAKMKAPPKAAR
KTPGLPKDVSVAELLRELSLTKEEELLFLQLPDTLPGQPPTQDIKPIKTEVQGEDGQVVL
IKQEKDREAKLAENACTLADLTEGQVGKLLIRKSGRVQLLLGKVTLDVTMGTACSFLQEL
VSVGLGDSRTGEMTVLGHVKHKLVCSPDFESLLDHKHR
|
| Enzyme 14 Number of Residues |
398 |
| Enzyme 14 Molecular Weight |
44396 |
| Enzyme 14 Theoretical pI |
6.97 |
| 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 |
- RNA metabolism
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- tRNA metabolism
- transcription
|
| Component |
| — |
|
| Enzyme 14 General Function |
Not Available |
| 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 |
179513  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P05423  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
RPO3D_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>1188 bp
ATGTCGGAAGGAAACGCCGCCGGACGCCCAGCACGGCAGGGCCCGGACCTTCTCCTGACT
GGGGCCCGGGGGTCATCGGGCGGCGGCGGCCTCCCCTCACCCCCGGCCGTTCCCTCCATC
CGTTCCAGGGACCTAACCCTCGGGGGAGTCAAGAAGAAAACCTTCACCCCAAATATCATC
AGTCGGAAGATCAAGGAAGAGCCCAAGGAAGAAGTAACTGTCAAGAAGGAGAAGCGTGAA
AGGGACAGAGACCGACAACGAGAGGGGCATGGACGAGGGCGACGCCGTCCAGAAGTGATC
CAGTCTCACTCCATCTTTGAGCAGGGCCCAGCTGAAATGATGAAGAAAAAAGGGAACTGG
GATAAGACAGTGGATGTGTCAGACATGGGACCTTCTCATATCATCAACATCAAAAAAGAG
AAGAGAGAGACAGACGAAGAAACTAAACAGATCTTGCGTATGCTGGAGAAGGACGATTTC
CTCGATGACCCCGGCCTGAGGAACGACACTCGAAATATGCCTGTGCAGCTGCCGCTGGCT
CACTCAGGATGGCTTTTTAAGGAAGAAAATGACGAACCAGATGTTAAACCTTGGCTGGCT
GGCCCCAAGGAAGAGGACATGGAGGTGGACATACCTGCTGTGAAAGTGAAAGAGGAGCCA
CGAGATGAGGAGGAAGAGGCCAAGATGAAGGCTCCTCCCAAAGCAGCCAGGAAGACTCCA
GGCCTCCCGAAGGATGTATCTGTGGCAGAGCTGCTGAGGGAGCTGAGCCTCACCAAGGAA
GAGGAACTGCTGTTTCTGCAGCTGCCAGACACCCTCCCTGGCCAGCCACCCACCCAGGAC
ATCAAGCCTATCAAGACAGAGGTGCAGGGCGAGGACGGACAGGTGGTGCTCATCAAGCAG
GAGAAAGACCGAGAAGCCAAATTGGCAGAGAATGCTTGTACCCTGGCTGACCTGACAGAG
GGTCAGGTTGGCAAGCTACTCATCCGCAAGTCTGGAAGGGTGCAACTCCTCTTGGGCAAG
GTGACTCTGGACGTGACCATGGGAACTGCCTGCTCCTTCCTGCAGGAGCTGGTGTCCGTG
GGCCTTGGAGACAGTAGGACAGGGGAGATGACAGTCCTGGGACACGTGAAGCACAAACTT
GTATGTTCCCCTGATTTTGAATCCCTCTTGGATCACAAACACCGGTAA
|
| Enzyme 14 GenBank Gene ID |
M17754  |
| Enzyme 14 GeneCard ID |
POLR3D  |
| Enzyme 14 GenAtlas ID |
POLR3D  |
| Enzyme 14 HGNC ID |
HGNC:1080  |
| Enzyme 14 Chromosome Location |
8 |
| Enzyme 14 Locus |
8q21 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Ittmann M, Greco A, Basilico C: Isolation of the human gene that complements a temperature-sensitive cell cycle mutation in BHK cells. Mol Cell Biol. 1987 Oct;7(10):3386-93. [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
]
- Chong SS, Hu P, Hernandez N: Reconstitution of transcription from the human U6 small nuclear RNA promoter with eight recombinant polypeptides and a partially purified RNA polymerase III complex. J Biol Chem. 2001 Jun 8;276(23):20727-34. Epub 2001 Feb 27. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
6012 |
| Enzyme 15 Name |
DNA-directed RNA polymerase II 140 kDa polypeptide |
| Enzyme 15 Synonyms |
- RNA polymerase II subunit 2
- RPB2
|
| Enzyme 15 Gene Name |
POLR2B |
| Enzyme 15 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 15 Number of Residues |
1174 |
| Enzyme 15 Molecular Weight |
133898 |
| Enzyme 15 Theoretical pI |
6.87 |
| Enzyme 15 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 15 General Function |
Transcription |
| Enzyme 15 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
36122  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P30876  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
RPB2_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 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 15 GenBank Gene ID |
X63563  |
| Enzyme 15 GeneCard ID |
POLR2B  |
| Enzyme 15 GenAtlas ID |
POLR2B  |
| Enzyme 15 HGNC ID |
HGNC:9188  |
| Enzyme 15 Chromosome Location |
4 |
| Enzyme 15 Locus |
4q12 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 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 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
6014 |
| Enzyme 16 Name |
DNA-directed RNA polymerase II largest subunit |
| Enzyme 16 Synonyms |
- RPB1
|
| Enzyme 16 Gene Name |
POLR2A |
| Enzyme 16 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 16 Number of Residues |
1970 |
| Enzyme 16 Molecular Weight |
217208 |
| Enzyme 16 Theoretical pI |
7.38 |
| Enzyme 16 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 16 General Function |
Transcription |
| Enzyme 16 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
36124  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P24928  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
RPB1_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 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 16 GenBank Gene ID |
X63564  |
| Enzyme 16 GeneCard ID |
POLR2A  |
| Enzyme 16 GenAtlas ID |
POLR2A  |
| Enzyme 16 HGNC ID |
HGNC:9187  |
| Enzyme 16 Chromosome Location |
17 |
| Enzyme 16 Locus |
17p13.1 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 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 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
6017 |
| Enzyme 17 Name |
DNA-directed RNA polymerase, mitochondrial precursor |
| Enzyme 17 Synonyms |
- MtRPOL
|
| Enzyme 17 Gene Name |
POLRMT |
| Enzyme 17 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 17 Number of Residues |
1230 |
| Enzyme 17 Molecular Weight |
138622 |
| Enzyme 17 Theoretical pI |
9.25 |
| Enzyme 17 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 17 General Function |
Not Available |
| Enzyme 17 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
2114396  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
O00411  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
RPOM_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 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 17 GenBank Gene ID |
U75370  |
| Enzyme 17 GeneCard ID |
POLRMT  |
| Enzyme 17 GenAtlas ID |
POLRMT  |
| Enzyme 17 HGNC ID |
HGNC:9200  |
| Enzyme 17 Chromosome Location |
19 |
| Enzyme 17 Locus |
19p13.3 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 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 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
6018 |
| Enzyme 18 Name |
DNA-directed RNA polymerase I 135 kDa polypeptide |
| Enzyme 18 Synonyms |
- RNA polymerase I subunit 2
- RPA135
|
| Enzyme 18 Gene Name |
POLR1B |
| Enzyme 18 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 18 Number of Residues |
1135 |
| Enzyme 18 Molecular Weight |
128231 |
| Enzyme 18 Theoretical pI |
7.88 |
| Enzyme 18 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 18 General Function |
Transcription |
| Enzyme 18 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 18 Pathways |
|
| Enzyme 18 Reactions |
- nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
10433976  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q9H9Y6  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
RPA2_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 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 18 GenBank Gene ID |
AK022533  |
| Enzyme 18 GeneCard ID |
POLR1B  |
| Enzyme 18 GenAtlas ID |
POLR1B  |
| Enzyme 18 HGNC ID |
HGNC:20454  |
| Enzyme 18 Chromosome Location |
2 |
| Enzyme 18 Locus |
2q13 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
Not Available |
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
6027 |
| Enzyme 19 Name |
DNA-directed RNA polymerase III subunit 127.6 kDa polypeptide |
| Enzyme 19 Synonyms |
- RNA polymerase III subunit 2
- RPC2
|
| Enzyme 19 Gene Name |
POLR3B |
| Enzyme 19 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 19 Number of Residues |
1133 |
| Enzyme 19 Molecular Weight |
127787 |
| Enzyme 19 Theoretical pI |
8.64 |
| Enzyme 19 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 19 General Function |
Transcription |
| Enzyme 19 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
24429617  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9NW08  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
RPC2_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 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 19 GenBank Gene ID |
AY092084  |
| Enzyme 19 GeneCard ID |
POLR3B  |
| Enzyme 19 GenAtlas ID |
POLR3B  |
| Enzyme 19 HGNC ID |
HGNC:30348  |
| Enzyme 19 Chromosome Location |
12 |
| Enzyme 19 Locus |
12q23.3 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 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 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
6030 |
| Enzyme 20 Name |
Choline-phosphate cytidylyltransferase A |
| Enzyme 20 Synonyms |
- Phosphorylcholine transferase A
- CTP:phosphocholine cytidylyltransferase A
- CT A
- CCT A
- CCT-alpha
|
| Enzyme 20 Gene Name |
PCYT1A |
| Enzyme 20 Protein Sequence |
>Choline-phosphate cytidylyltransferase A
MDAQCSAKVNARKRRKEAPGPNGATEEDGVPSKVQRCAVGLRQPAPFSDEIEVDFSKPYV
RVTMEEASRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHN
FKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDD
VYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKY
HLQERVDKVKEKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGPEGALK
HMLKEGKGRMLQAISPKQSPSSSPTRERSPSPSFRWPFSGKTSPPCSPANLSRHKAAAYD
ISEDEED
|
| Enzyme 20 Number of Residues |
367 |
| Enzyme 20 Molecular Weight |
41732 |
| Enzyme 20 Theoretical pI |
6.85 |
| Enzyme 20 GO Classification |
| Function |
- catalytic activity
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 20 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 20 Specific Function |
Controls phosphatidylcholine synthesis |
| Enzyme 20 Pathways |
|
| Enzyme 20 Reactions |
- CTP + choline phosphate = diphosphate + CDP-choline
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
575486  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
P49585  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
PCY1A_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>1104 bp
ATGGATGCACAGTGTTCAGCCAAGGTCAATGCAAGGAAGAGGAGAAAAGAGGCGCCCGGA
CCCAACGGGGCAACAGAAGAAGATGGGGTTCCTTCCAAAGTGCAGCGCTGTGCAGTGGGC
TTACGGCAACCAGCTCCTTTTTCTGATGAAATTGAAGTTGACTTTAGTAAGCCCTATGTC
AGGGTAACTATGGAAGAAGCCAGCAGAGGAACTCCTTGTGAGCGACCTGTGAGAGTTTAT
GCCGATGGAATATTTGACTTATTTCACTCTGGTCACGCCCGAGCTCTGATGCAAGCGAAG
AACCTTTTCCCTAATACGTACCTCATTGTGGGAGTTTGCAGTGATGAGCTCACACACAAC
TTCAAAGGCTTCACGGTGATGAACGAGAATGAGCGCTATGACGCAGTCCAGCACTGCCGC
TACGTGGATGAGGTGGTGAGGAATGCGCCCTGGACGCTGACACCCGAGTTCCTGGCCGAA
CACCGGATTGATTTTGTAGCCCATGATGATATTCCTTATTCATCTGCTGGCAGTGATGAT
GTTTATAAGCACATCAAGGAGGCAGGCATGTTTGCTCCAACACAGAGGACAGAAGGTATC
TCCACATCAGACATCATCACCCGAATTGTGCGGGATTATGATGTGTATGCGAGGCGGAAC
CTGCAGAGGGGCTACACAGCAAAGGAGCTCAATGTCAGCTTTATCAACGAGAAGAAATAC
CACTTGCAGGAGAGGGTTGACAAAGTAAAGGAGAAAGTGAAAGATGTGGAGGAAAAGTCA
AAAGAATTTGTTCAGAAGGTGGAGGAAAAAAGCATTGACCTCATTCAGAAGTGGGAGGAG
AAGTCCCGAGAATTCATTGGAAGTTTTCTGGAAATGTTTGGTCCGGAAGGAGCACTGAAA
CATATGCTGAAAGAGGGGAAGGGCCGGATGCTGCAGGCCATCAGCCCGAAGCAGAGCCCC
AGCAGCAGCCCTACTCGCGAGCGCTCCCCCTCCCCCTCTTTCCGATGGCCCTTCTCCGGC
AAGACTTCCCCACCTTGCTCCCCAGCAAATCTCTCCAGGCACAAGGCTGCAGCCTATGAT
ATCAGTGAGGATGAAGAAGACTAA
|
| Enzyme 20 GenBank Gene ID |
L28957  |
| Enzyme 20 GeneCard ID |
PCYT1A  |
| Enzyme 20 GenAtlas ID |
PCYT1A  |
| Enzyme 20 HGNC ID |
HGNC:8754  |
| Enzyme 20 Chromosome Location |
3 |
| Enzyme 20 Locus |
3q29 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Kalmar GB, Kay RJ, LaChance AC, Cornell RB: Primary structure and expression of a human CTP:phosphocholine cytidylyltransferase. Biochim Biophys Acta. 1994 Oct 18;1219(2):328-34. [PubMed
]
- Dunne SJ, Cornell RB, Johnson JE, Glover NR, Tracey AS: Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase. Biochemistry. 1996 Sep 17;35(37):11975-84. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
6031 |
| Enzyme 21 Name |
DNA-directed RNA polymerase I-associated factor 53 kDa subunit |
| Enzyme 21 Synonyms |
- RNA polymerase I polypeptide E
- RNA polymerase I- associated factor 1
|
| Enzyme 21 Gene Name |
POLR1E |
| Enzyme 21 Protein Sequence |
>DNA-directed RNA polymerase I-associated factor 53 kDa subunit
MYQASAVSLLPRDIPSCHSPSPGFSHLPTSSSQLAPDLLQFPLGQDPSFLAIPILTLPPS
DSLVPPYIVWYIVWPSALISFLGCTLTVQFSNGKLQSPGNMRFTLYENKDSTNPRKRNQR
ILAAETDRLSYVGNNFGTGALKCNTLCRHFVGILNKTSGQMEVYDAELFNMQPLFSDVSV
ESELALESQTKTYREKMDSCIEAFGTTKQKRALNTRRMNRVGNESLNRAVAKAAETIIDT
KGVTALVSDAIHNDLQDDSLYLPPCYDDAAKPEDVYKFEDLLSPAEYEALQSPSEAFRNV
TSEEILKMIEENSHCTFVIEALKSLPSDVESRDRQARCIWFLDTLIKFRAHRVVKRKSAL
GPGVPHIINTKLLKHFTCLTYNNGRLRNLISDSMKAKITAYVIILALHIHDFQIDLTVLQ
RDLKLSEKRMMEIAKAMRLKISKRRVSVAAGSEEDHKLGTLSLPLPPAQTSDRLAKRRKI
T
|
| Enzyme 21 Number of Residues |
481 |
| Enzyme 21 Molecular Weight |
53963 |
| Enzyme 21 Theoretical pI |
8.74 |
| Enzyme 21 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 21 General Function |
Not Available |
| Enzyme 21 Specific Function |
Required for the initiation of transcription by the DNA- dependent RNA polymerase I holoenzyme. This complex catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
10435392  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q9GZS1  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
RPF53_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>1260 bp
ATGGCGGCGGAGGTGTTGCCGAGTGCGAGGTGGCAGTATTGTGGGGCGCCCGACGGGAGC
CAGAGAGCTGTACTGGTCCAGTTCTCCAACGGGAAGCTACAGAGTCCAGGCAACATGCGC
TTTACCTTGTATGAGAACAAAGATTCCACCAACCCCAGGAAGAGGAATCAACGGATCCTG
GCAGCTGAAACAGATAGGCTCTCCTATGTGGGAAACAATTTTGGGACTGGAGCCCTCAAA
TGCAACACTTTGTGCAGGCACTTTGTGGGAATTTTGAACAAGACCTCTGGCCAAATGGAA
GTATATGATGCTGAATTGTTCAACATGCAGCCACTATTTTCAGATGTATCAGTTGAGAGT
GAACTGGCGCTAGAGAGTCAGACCAAAACTTACAGAGAAAAGATGGATTCTTGTATTGAA
GCCTTTGGTACCACCAAACAGAAGCGAGCTCTGAACACCAGGAGAATGAACAGAGTTGGC
AATGAATCTTTGAATCGTGCAGTGGCTAAAGCTGCAGAGACTATCATTGATACGAAGGGT
GTGACTGCTCTGGTCAGCGATGCTATCCACAATGACTTGCAAGATGACTCCCTCTACCTT
CCTCCCTGCTATGATGATGCAGCCAAGCCTGAAGACGTGTATAAATTTGAAGATCTTCTT
TCCCCTGCGGAGTATGAAGCTCTTCAGAGCCCATCTGAAGCTTTCAGGAACGTCACGTCA
GAAGAAATACTGAAGATGATTGAGGAGAACAGCCATTGCACCTTTGTCATAGAAGCGTTG
AAGTCTTTGCCATCAGATGTGGAGAGCCGAGACCGCCAGGCCCGATGCATATGGTTTCTG
GATACCCTCATCAAATTTCGAGCTCATAGGGTAGTTAAGCGGAAAAGTGCTCTGGGACCT
GGAGTTCCCCACATCATCAACACCAAACTGCTGAAGCACTTTACTTGCTTGACCTACAAC
AATGGCAGATTACGGAACTTAATTTCGGATTCTATGAAGGCGAAGATTACTGCATATGTG
ATCATACTTGCCTTGCACATACATGACTTCCAAATTGACCTGACAGTGTTACAGAGGGAC
TTGAAGCTCAGTGAGAAAAGGATGATGGAGATAGCCAAAGCCATGAGGCTGAAGATCTCC
AAAAGAAGGGTGTCTGTGGCCGCCGGCAGTGAAGAAGATCACAAACTGGGCACCCTGTCC
CTCCCGCTGCCTCCAGCCCAGACCTCAGACCGCCTGGCAAAGCGGAGGAAGATTACCTAG
|
| Enzyme 21 GenBank Gene ID |
AK023452  |
| Enzyme 21 GeneCard ID |
POLR1E  |
| Enzyme 21 GenAtlas ID |
POLR1E  |
| Enzyme 21 HGNC ID |
HGNC:17631  |
| Enzyme 21 Chromosome Location |
9 |
| Enzyme 21 Locus |
9p13.2 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- 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 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
6033 |
| Enzyme 22 Name |
6-phosphofructokinase, liver type |
| Enzyme 22 Synonyms |
- Phosphofructokinase 1
- Phosphohexokinase
- Phosphofructo-1-kinase isozyme B
- PFK-B
|
| Enzyme 22 Gene Name |
PFKL |
| Enzyme 22 Protein Sequence |
>6-phosphofructokinase, liver type
MAAVDLEKLRASGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVE
GGENIKQANWLSVSNIIQLGGTIIGSARCKAFTTREGRRAAAYNLVQHGITNLCVIGGDG
SLTGANIFRSEWGSLLEELVAEGKISETTARTYSHLNIAGLVGSIDNDFCGTDMTIGTDS
ALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWE
NFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQ
RGGTPSAFDRILSSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQK
AMDDKRFDEATQLRGGSFENNWNIYKLLAHQKPPKEKSNFSLAILNVGAPAAGMNAAVRS
AVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKGQLESI
VENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLG
SDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFN
IHDLKVNVEHMTEKMKTDIQRGLVLRNEKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGH
LQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFANAPDSACVIGLKKKAVAFS
PVTELKKDTDFEHRMPREQWWLSLRLMLKMLAQYRISMAAYVSGELEHVTRRTLSMDKGF
|
| Enzyme 22 Number of Residues |
780 |
| Enzyme 22 Molecular Weight |
85020 |
| Enzyme 22 Theoretical pI |
7.54 |
| Enzyme 22 GO Classification |
| Function |
- 6-phosphofructokinase activity
- catalytic activity
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
- 6-phosphofructokinase complex
- cell
- cytoplasm
- intracellular
- protein complex
|
|
| Enzyme 22 General Function |
Carbohydrate transport and metabolism |
| Enzyme 22 Specific Function |
ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate |
| Enzyme 22 Pathways |
|
| Enzyme 22 Reactions |
- ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
35431  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
P17858  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
K6PL_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>2343 bp
ATGGCCGCGGTGGACCTGGAGAAGCTGCGGGCGTCGGGCGCGGGCAAGGCCATCGGCGTC
CTGACCAGCGGCGGCGACCGGCAAGGCATGAACGCTGCTGTCCGGGCTGTGACGCGCATG
GGCATTTATGTGGGTGCCAAAGTCTTCCTCATCTACGAGGGCTATGAGGGCCTCGTGGAG
GGAGGTGAGAACATCAAGCAGGCCAACTGGCTGAGCGTCTCCAACATCATCCAGCTGGGC
GGCACTATCATTGGCAGCGCTCGCTCGAAGGCCTTTACCACCAGGGAGGGGCGCCGGGCA
GCGGCCTACAACCTGGTCCAGCACGGCATCACCAACCTGTGCGTCATCGGCGGGGATGGC
AGCCTCACAGGTGCCAACATCTTCCGCAGCGAGTGGGGCAGCCTGCTGGAGGAGCTGGTG
GCGGAAGGTAAGATCTCAGAGACTACAGCCTGGACCTACTCGCACCTGAACATCGCGGGC
CTAGTGGGCTCCATCGATAACGACTTCTGCGGCACCGACATGACCATCGGCACGGACTCG
GCCCTCCACCGCATCATGGAGGTCATCGATGCCATCACCACCACTGCCCAGAGCCACCAG
AGGACCTTCGTGCTGGAAGTGATGGGCCGGCACTGCGGGTACCTGGCGCTGGTATCTGCA
CTGGCCTCAGGGGCCGACTGGCTGTTCATCCCCGAGGCTCCACCCGAGGACGGCTGGGAG
AACTTCATGTGTGAGAGGCTGGGTGAGACTCGGAGCCGTGGGTCCCGACTGAACATCATC
ATCATCGCTGAGGGTGCCATTGACCGCAACGGGAAGCCCATCTCGTCCAGCTACGTGAAG
GACCTGGTGGTTCAGAGGCTGGGCTTCGACACCCGTGTAACTGTGCTGGGCCACGTGCAG
CGGGGAGGGACGCCCTCTGCCTTCGACCGGATCCTGAGCAGCAAGATGGGCATGGAGGCG
GTGATGGCGCTGCTGGAAGCCACGCCTGACACGCCGGCCTGCGTGGTCACCCTCTCGGGG
AACCAGTCAGTGCGGCTGCCCCTCATGGAGTGCGTGCAGATGACCAAGGAAGTGCAGAAA
GCCATGGATGACAAGAGGTTTGACGAGGCCACCCAGCTCCGTGGTGGGAGCTTCGAGAAC
AACTGGAACATTTACAAGCTCCTCACCCACCAGAAGCCCCCCAAGGAGAAGTCTAACTTC
TCCCTGGCCATCCTGAATGTGGGGGCCCCGGCGGCTGGCATGAATGCGGCCGTGCGCTCG
GCGGTGCGGACCGGCATCTCCCATGGACACACAGTATACGTGGTGCACGATGGCTTCGAA
GGCCTAGCCAAGGGTCAGGTGCAAGAAGTAGGCTGGCACGACGTGGCCGGCTGGTTGGGG
CGTGGTGGCTCCATGCTGGGGACCAAGAGGACCCTGCCCAAGGGCCAGCTGGAGTCCATT
GTGGAGAACATCCGCATCTATGGTATTCACGCCCTGCTGGTGGTCGGTGGGTTTGAGGCC
TATGAAGGGGTGCTGCAGCTGGTGGAGGCTCGCGGGCGCTACGAGGAGCTCTGCATCGTC
ATGTGTGTCATCCCAGCCACCATCAGCAACAACGTCCCTGGCACCGACTTCAGCCTGGGC
TCCGACACTGCTGTAAATGCCGCCATGGAGAGCTGTGACCGCATCAAACAGTCTGCCTCG
GGGACCAAGCGCCGTGTGTTCATCGTGGAGACCATGGGGGGTTACTGTGGCTACCTGGCC
ACCGTGACTGGCATTGCTGTGGGGGCCGACGCCGCCTACGTCTTCGAGGACCCTTTCAAC
ATCCACGACTTAAAGGTCAACGTGGAGCACATGACGGAGAAGATGAAGACAGACATTCAG
AGGGGCCTGGTGCTGCGGAACGAGAAGTGCCATGACTACTACACCACGGAGTTCCTGTAC
AACCTGTACTCATCAGAGGGCAAGGGCGTCTTCGACTGCAGGACCAATGTCCTGGGCCAC
CTGCAGCAGGGTGGCGCTCCAACCCCCTTTGACCGGAACTATGGGACCAAGCTGGGGGTG
AAGGCCATGCTGTGGTTGTCGGAGAAGCTGCGCGAGGTTTACCGCAAGGGACGGGTGTTC
GCCAATGCCCCAGACTCGGCCTGCGTGATCGGCCTGAAGAAGAAGGCGGTGGCCTTCAGC
CCCGTCACTGAGCTCAAGAAAGACACTGATTTCGAGCACCGCATGCCACGGGAGCAGTGG
TGGCTGAGCCTGCGGCTCATGCTGAAGATGCTGGCACAATACCGCATCAGTATGGCCGCC
TACGTGTCAGGGGAGCTGGAGCACGTGACCCGCCGCACCCTGAGCATGGACAAGGGCTTC
TGA
|
| Enzyme 22 GenBank Gene ID |
X15573  |
| Enzyme 22 GeneCard ID |
PFKL  |
| Enzyme 22 GenAtlas ID |
PFKL  |
| Enzyme 22 HGNC ID |
HGNC:8876  |
| Enzyme 22 Chromosome Location |
Not Available |
| Enzyme 22 Locus |
Not Available |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Levanon D, Danciger E, Dafni N, Bernstein Y, Elson A, Moens W, Brandeis M, Groner Y: The primary structure of human liver type phosphofructokinase and its comparison with other types of PFK. DNA. 1989 Dec;8(10):733-43. [PubMed
]
- Elson A, Levanon D, Brandeis M, Dafni N, Bernstein Y, Danciger E, Groner Y: The structure of the human liver-type phosphofructokinase gene. Genomics. 1990 May;7(1):47-56. [PubMed
]
- Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
6035 |
| Enzyme 23 Name |
DNA-directed RNA polymerase III subunit 22.9 kDa polypeptide |
| Enzyme 23 Synonyms |
- RPC8
|
| Enzyme 23 Gene Name |
POLR3H |
| Enzyme 23 Protein Sequence |
>DNA-directed RNA polymerase III subunit 22.9 kDa polypeptide
MFVLVEMVDTVRIPPWQFERKLNDSIAEELNKKLANKVVYNVGLCICLFDITKLEDAYVF
PGDGASHTKVHFRCVVFHPFLDEILIGKIKGCSPEGVHVSLGFFDDILIPPESLQQPAKF
DEAEQVWVWEYETEEGAHDLYMDTGEEIRFRVVDESFVDTSPTGPSSADATTSSEELPKK
EAPYTLVGSISEPGLGLLSWWTSN
|
| Enzyme 23 Number of Residues |
204 |
| Enzyme 23 Molecular Weight |
22918 |
| Enzyme 23 Theoretical pI |
4.21 |
| Enzyme 23 GO Classification |
| Function |
- DNA-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
|
| Component |
| — |
|
| Enzyme 23 General Function |
Transcription |
| Enzyme 23 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates |
| Enzyme 23 Pathways |
|
| Enzyme 23 Reactions |
- nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
24429623  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q9Y535  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
RPC8_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>615 bp
ATGTTCGTCCTGGTGGAAATGGTGGACACCGTCCGGATCCCCCCTTGGCAGTTTGAGAGG
AAGCTCAACGACTCCATTGCCGAGGAGCTGAACAAGAAGTTGGCCAACAAGGTCGTGTAC
AACGTGGGACTCTGCATTTGTCTGTTTGATATCACCAAACTGGAGGATGCCTATGTATTC
CCTGGGGATGGCGCATCACACACCAAAGTCCATTTTCGCTGCGTGGTGTTTCATCCATTC
CTAGATGAGATTCTCATTGGGAAGATCAAAGGCTGCAGCCCAGAAGGAGTGCACGTCTCT
CTAGGCTTCTTCGATGACATTCTCATCCCCCCAGAGTCACTGCAGCAGCCAGCCAAGTTC
GACGAAGCGGAGCAGGTGTGGGTGTGGGAGTACGAGACGGAGGAAGGAGCACACGACCTC
TACATGGACACCGGCGAGGAGATCCGCTTCCGGGTGGTGGACGAGAGCTTTGTTGACACG
TCCCCCACAGGGCCCAGCTCAGCAGATGCCACCACTTCCAGTGAGGAGCTGCCAAAGAAG
GAGGCTCCGTACACGCTTGTGGGATCCATCAGTGAGCCAGGCCTGGGCCTTCTCTCCTGG
TGGACCAGCAACTAG
|
| Enzyme 23 GenBank Gene ID |
AY092087  |
| Enzyme 23 GeneCard ID |
POLR3H  |
| Enzyme 23 GenAtlas ID |
POLR3H  |
| Enzyme 23 HGNC ID |
HGNC:30349  |
| Enzyme 23 Chromosome Location |
22 |
| Enzyme 23 Locus |
22q13.2 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 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
]
- Hirosawa M, Nagase T, Murahashi Y, Kikuno R, Ohara O: Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping. DNA Res. 2001 Feb 28;8(1):1-9. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
6036 |
| Enzyme 24 Name |
DNA-directed RNA polymerases III 12.5 kDa polypeptide |
| Enzyme 24 Synonyms |
- RNA polymerase III subunit K
- RNA polymerase III C11 subunit
- HsC11p
- hRPC11
|
| Enzyme 24 Gene Name |
POLR3K |
| Enzyme 24 Protein Sequence |
>DNA-directed RNA polymerases III 12.5 kDa polypeptide
MLLFCPGCGNGLIVEEGQRCHRFSCNTCPYVHNITRKVTNRKYPKLKEVDDVLGGAAAWE
NVDSTAESCPKCEHPRAYFMQLQTRSADEPMTTFYKCCNAQCGHRWRD
|
| Enzyme 24 Number of Residues |
108 |
| Enzyme 24 Molecular Weight |
12336 |
| Enzyme 24 Theoretical pI |
7.89 |
| Enzyme 24 GO Classification |
| Function |
- DNA binding
- DNA-directed RNA polymerase activity
- binding
- catalytic activity
- cation binding
- ion binding
- nucleic acid binding
- nucleotidyltransferase activity
- transcription factor activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- RNA elongation
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- regulation of biological process
- regulation of cellular metabolism
- regulation of metabolism
- regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- regulation of physiological process
- regulation of transcription
- regulation of transcription, DNA-dependent
- transcription
- transcription, DNA-dependent
|
| Component |
| — |
|
| Enzyme 24 General Function |
Transcription |
| Enzyme 24 Specific Function |
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1) |
| Enzyme 24 Pathways |
|
| Enzyme 24 Reactions |
- nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
4877775  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q9Y2Y1  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
RPC11_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>327 bp
ATGCTGCTGTTCTGCCCCGGCTGCGGGAACGGGCTGATCGTGGAGGAGGGACAACGCTGC
CACCGCTTCGCCTGCAACACGTGCCCCTACGTGCACAACATCACCCGCAAGGTAACAAAT
CGGAAGTACCCAAAACTGAAAGAAGTGGATGATGTGCTTGGTGGAGCAGCTGCCTGGGAG
AATGTTGACTCTACTGCAGAGTCGTGTCCCAAATGCGAACATCCTCGTGCTTACTTCATG
CAGCTTCAGACCCGCTCTGCAGATGAGCCGATGACCACCTTCTACAAGTGCTGCAATGCT
CAGTGTGGACACCGCTGGAGGGATTAG
|
| Enzyme 24 GenBank Gene ID |
AF126531  |
| Enzyme 24 GeneCard ID |
POLR3K  |
| Enzyme 24 GenAtlas ID |
POLR3K  |
| Enzyme 24 HGNC ID |
HGNC:14121  |
| Enzyme 24 Chromosome Location |
16 |
| Enzyme 24 Locus |
16p13.3 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Chedin S, Riva M, Schultz P, Sentenac A, Carles C: The RNA cleavage activity of RNA polymerase III is mediated by an essential TFIIS-like subunit and is important for transcription termination. Genes Dev. 1998 Dec 15;12(24):3857-71. [PubMed
]
- Spakovskii GV, Lebedenko EN: [Molecular identification and characteristics of hRPC11, the smallest specific subunit of human RNA polymerase III] Bioorg Khim. 1998 Nov;24(11):877-80. [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 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
6037 |
| Enzyme 25 Name |
6-phosphofructokinase, muscle type |
| Enzyme 25 Synonyms |
- Phosphofructokinase 1
- Phosphohexokinase
- Phosphofructo-1-kinase isozyme A
- PFK-A
- Phosphofructokinase-M
|
| Enzyme 25 Gene Name |
PFKM |
| Enzyme 25 Protein Sequence |
>6-phosphofructokinase, muscle type
MTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVD
GGDHIKEATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAYNLVKRGITNLCVIGGDG
SLTGADTFRSEWSDLLSDLQKAGKITDEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDS
ALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWE
EHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQ
RGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTK
AMDEKKFDEALKLRGRSFMNNWEVYKLLAHVRPPVSKSGSHTVAVMNVGAPAAGMNAAVR
STVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQ
ISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSV
GADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPF
TIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLG
HMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVF
QPVAELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHITRKRSGEAAV
|
| Enzyme 25 Number of Residues |
780 |
| Enzyme 25 Molecular Weight |
85184 |
| Enzyme 25 Theoretical pI |
8.07 |
| Enzyme 25 GO Classification |
| Function |
- 6-phosphofructokinase activity
- catalytic activity
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
- 6-phosphofructokinase complex
- cell
- cytoplasm
- intracellular
- protein complex
|
|
| Enzyme 25 General Function |
Carbohydrate transport and metabolism |
| Enzyme 25 Specific Function |
ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate |
| Enzyme 25 Pathways |
|
| Enzyme 25 Reactions |
- ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
1101758  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
P08237  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
K6PF_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>2343 bp
ATGACCCATGAAGAGCACCATGCAGCCAAAACCCTGGGGATTGGCAAAGCCATTGCTGTC
TTAACCTCTGGTGGAGATGCCCAAGGTATGAATGCTGCTGTCAGGGCTGTGGTTCGAGTT
GGTATCTTCACCGGTGCCCGTGTCTTCTTTGTCCATGAGGGTTATCAAGGCCTGGTGGAT
GGTGGAGATCACATCAAGGAAGCCACCTGGGAGAGCGTTTCGATGATGCTTCAGCTGGGA
GGCACGGTGATTGGAAGTGCCCGGTGCAAGGACTTTCGGGAACGAGAAGGACGACTCCGA
GCTGCCTACAACCTGGTGAAGCGTGGGATCACCAATCTCTGTGTCATTGGGGGTGATGGC
AGCCTCACTGGGGCTGACACCTTCCGTTCTGAGTGGAGTGACTTGTTGAGTGACCTCCAG
AAAGCAGGTAAGATCACAGATGAGGAGGCTACGAAGTCCAGCTACCTGAACATTGTGGGC
CTGGTTGGGTCAATTGACAATGACTTCTGTGGCACTGATATGACCATTGGCACTGACTCT
GCCCTGCATCGGATCATGGAAATTGTAGATGCCATCACTACCACTGCCCAGAGCCACCAG
AGGACATTTGTGTTAGAAGTAATGGGCCGCCACTGTGGATACCTGGCCCTTGTCACCTCT
CTGTCCTGTGGGGCCGACTGGGTTTTTATTCCTGAATGTCCACCAGATGACGACTGGGAG
GAACACCTTTGTCGCCGACTCAGCGAGACAAGGACCCGTGGTTCTCGTCTCAACATCATC
ATTGTGGCTGAGGGTGCAATTGACAAGAATGGAAAACCAATCACCTCAGAAGACATCAAG
AATCTGGTGGTTAAGCGTCTGGGATATGACACCCGGGTTACTGTCTTGGGGCATGTGCAG
AGGGGTGGGACGCCATCAGCCTTTGACAGAATTCTGGGCAGCAGGATGGGTGTGGAAGCA
GTGATGGCACTTTTGGAGGGGACCCCAGATACCCCAGCCTGTGTAGTGAGCCTCTCTGGT
AACCAGGCTGTGCGCCTGCCCCTCATGGAATGTGTCCAGGTGACCAAAGATGTGACCAAG
GCCATGGATGAGAAGAAATTTGACGAAGCCCTGAAGCTGAGAGGCCGGAGCTTCATGAAC
AACTGGGAGGTGTACAAGCTTCTAGCTCATGTCAGACCCCCGGTATCTAAGAGTGGTTCG
CACACAGTGGCTGTGATGAACGTGGGGGCTCCGGCTGCAGGCATGAATGCTGCTGTTCGC
TCCACTGTGAGGATTGGCCTTATCCAGGGCAACCGAGTGCTCGTTGTCCATGATGGTTTC
GAGGGCCTGGCCAAGGGGCAGATAGAGGAAGCTGGCTGGAGCTATGTTGGGGGCTGGACT
GGCCAAGGTGGCTCTAAACTTGGGACTAAAAGGACTCTACCCAAGAAGAGCTTTGAACAG
ATCAGTGCCAATATAACTAAGTTTAACATTCAGGGCCTTGTCATCATTGGGGGCTTTGAG
GCTTACACAGGGGGCCTGGAACTGATGGAGGGCAGGAAGCAGTTTGATGAGCTCTGCATC
CCATTTGTGGTCATTCCTGCTACAGTCTCCAACAATGTCCCTGGCTCAGACTTCAGCGTT
GGGGCTGACACAGCACTCAATACTATCTGCACAACCTGTGACCGCATCAAGCAGTCAGCA
GCTGGCACCAAGCGTCGGGTGTTTATCATTGAGACTATGGGTGGCTACTGTGGCTACCTG
GCTACCATGGCTGGACTGGCAGCTGGGGCCGATGCTGCCTACATTTTTGAGGAGCCCTTC
ACCATTCGAGACCTGCAGGCAAATGTTGAACATCTGGTGCAAAAGATGAAAACAACTGTG
AAAAGGGGCTTGGTGTTAAGGAATGAAAAGTGCAATGAGAACTATACCACTGACTTCATT
TTCAACCTGTACTCTGAGGAGGGGAAGGGCATCTTCGACAGCAGGAAGAATGTGCTTGGT
CACATGCAGCAGGGTGGGAGCCCAACCCCATTTGATAGGAATTTTGCCACTAAGATGGGC
GCCAAGGCTATGAACTGGATGTCTGGGAAAATCAAAGAGAGTTACCGTAATGGGCGGATC
TTTGCCAATACTCCAGATTCGGGCTGTGTTCTGGGGATGCGTAAGAGGGCTCTGGTCTTC
CAACCAGTGGCTGAGCTGAAGGACCAGACAGATTTTGAGCATCGAATCCCCAAGGAACAG
TGGTGGCTGAAACTGAGGCCCATCCTCAAAATCCTAGCCAAGTACGAGATTGACTTGGAC
ACTTCAGACCATGCCCACCTGGAGCACATCACCCGGAAGCGGTCCGGGGAAGCTGCCGTC
TAA
|
| Enzyme 25 GenBank Gene ID |
M59741  |
| Enzyme 25 GeneCard ID |
PFKM  |
| Enzyme 25 GenAtlas ID |
PFKM  |
| Enzyme 25 HGNC ID |
HGNC:8877  |
| Enzyme 25 Chromosome Location |
12 |
| Enzyme 25 Locus |
12q13.3 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Yamasaki T, Nakajima H, Kono N, Hotta K, Yamada K, Imai E, Kuwajima M, Noguchi T, Tanaka T, Tarui S: Structure of the entire human muscle phosphofructokinase-encoding gene: a two-promoter system. Gene. 1991 Aug 15;104(2):277-82. [PubMed
]
- Sharma PM, Reddy GR, Vora S, Babior BM, McLachlan A: Cloning and expression of a human muscle phosphofructokinase cDNA. Gene. 1989 Apr 15;77(1):177-83. [PubMed
]
- Nakajima H, Noguchi T, Yamasaki T, Kono N, Tanaka T, Tarui S: Cloning of human muscle phosphofructokinase cDNA. FEBS Lett. 1987 Oct 19;223(1):113-6. [PubMed
]
- Sharma PM, Reddy GR, Babior BM, McLachlan A: Alternative splicing of the transcript encoding the human muscle isoenzyme of phosphofructokinase. J Biol Chem. 1990 Jun 5;265(16):9006-10. [PubMed
]
- Valdez BC, Chen Z, Sosa MG, Younathan ES, Chang SH: Human 6-phosphofructo-1-kinase gene has an additional intron upstream of start codon. Gene. 1989 Mar 15;76(1):167-9. [PubMed
]
- Raben N, Sherman JB: Mutations in muscle phosphofructokinase gene. Hum Mutat. 1995;6(1):1-6. [PubMed
]
- Tsujino S, Servidei S, Tonin P, Shanske S, Azan G, DiMauro S: Identification of three novel mutations in non-Ashkenazi Italian patients with muscle phosphofructokinase deficiency. Am J Hum Genet. 1994 May;54(5):812-9. [PubMed
]
- Raben N, Exelbert R, Spiegel R, Sherman JB, Nakajima H, Plotz P, Heinisch J: Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency. Am J Hum Genet. 1995 Jan;56(1):131-41. [PubMed
]
- Hamaguchi T, Nakajima H, Noguchi T, Nakagawa C, Kuwajima M, Kono N, Tarui S, Matsuzawa Y: Novel missense mutation (W686C) of the phosphofructokinase-M gene in a Japanese patient with a mild form of glycogenosis VII. Hum Mutat. 1996;8(3):273-5. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
6041 |
| Enzyme 26 Name |
Pyruvate kinase isozymes R/L |
| Enzyme 26 Synonyms |
- R-type/L-type pyruvate kinase
- Red cell/liver pyruvate kinase
- Pyruvate kinase 1
|
| Enzyme 26 Gene Name |
PKLR |
| Enzyme 26 Protein Sequence |
>Pyruvate kinase isozymes R/L
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQ
LPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFS
HGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKG
SQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQV
ENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKM
QHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS
AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
|
| Enzyme 26 Number of Residues |
574 |
| Enzyme 26 Molecular Weight |
61831 |
| Enzyme 26 Theoretical pI |
7.83 |
| Enzyme 26 GO Classification |
| Function |
- catalytic activity
- kinase activity
- pyruvate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 26 General Function |
Carbohydrate transport and metabolism |
| Enzyme 26 Specific Function |
ATP + pyruvate = ADP + phosphoenolpyruvate |
| Enzyme 26 Pathways |
|
| Enzyme 26 Reactions |
- ATP + pyruvate = ADP + phosphoenolpyruvate
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
3327365  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
P30613  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
KPYR_HUMAN  |
| Enzyme 26 PDB ID |
1LIU  |
| Enzyme 26 PDB File |
Show |
| Enzyme 26 3D Structure |
|
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>1725 bp
ATGTCGATCCAGGAGAACATATCATCCCTGCAGCTTCGGTCATGGGTCTCTAAGTCCCAA
AGAGACTTAGCAAAGTCCATCCTGATTGGGGCTCCAGGAGGGCCAGCGGGGTATCTGCGG
CGGGCCAGTGTGGCCCAACTGACCCAGGAGCTGGGCACTGCCTTCTTCCAGCAGCAGCAG
CTGCCAGCTGCTATGGCAGACACCTTCCTGGAACACCTCTGCCTACTGGACATTGACTCC
GAGCCCGTGGCTGCTCGCAGTACCAGCATCATTGCCACCATCGGGCCAGCATCTCGCTCC
GTGGAGCGCCTCAAGGAGATGATCAAGGCCGGGATGAACATTGCGCGACTCAACTTCTCC
CACGGCTCCCACGAGTACCATGCTGAGTCCATCGCCAACGTCCGGGAGGCGGTGGAGAGC
TTTGCAGGTTCCCCACTCAGCTACCGGCCCGTGGCCATCGCCCTGGACACCAAGGGACCG
GAGATCCGCACTGGGATCCTGCAGGGGGGTCCAGAGTCGGAAGTGGAGCTGGTGAAGGGC
TCCCAGGTGCTGGTGACTGTGGACCCCGCGTTCCGGACGCGGGGGAACGCGAACACCGTG
TGGGTGGACTACCCCAATATTGTCCGGGTCGTGCCGGTGGGGGGCCGCATCTACATTGAC
GACGGGCTCATCTCCCTAGTGGTCCAGAAAATCGGCCCAGAGGGACTGGTGACCCAAGTG
GAGAACGGCGGCGTCCTGGGCAGCCGGAAGGGCGTGAACTTGCCAGGGGCCCAGGTGGAC
TTGCCCGGGCTGTCCGAGCAGGACGTCCGAGACCTGCGCTTCGGGGTGGAGCATGGGGTG
GACATCGTCTTTGCCTCCTTTGTGCGGAAAGCCAGCGACGTGGCTGCCGTCAGGGCTGCT
CTGGGTCCGGAAGGACACGGCATCAAGATCATCAGCAAAATTGAGAACCACGAAGGCGTG
AAGAGGTTTGATGAAATCCTGGAGGTGAGCGACGGCATCATGGTGGCACGGGGGGACCTA
GGCATCGAGATCCCAGCAGAGAAGGTTTTCCTGGCTCAGAAGATGATGATTGGGCGCTGC
AACTTGGCGGGCAAGCCTGTTGTCTGTGCCACACAGATGCTGGAGAGCATGATTACCAAG
CCCCGGCCAACGAGGGCAGAGACAAGCGATGTCGCCAATGCTGTGCTGGATGGGGCTGAC
TGCATCATGCTGTCAGGGGAGACTGCCAAGGGCAACTTCCCTGTGGAAGCGGTGAAGATG
CAGCATGCGATTGCCCGGGAGGCAGAGGCCGCAGTGTACCACCGGCAGCTGTTTGAGGAG
CTACGTCGGGCAGCGCCACTAAGCCGTGATCCCACTGAGGTCACCGCCATTGGTGCTGTG
GAGGCTGCCTTCAAGTGCTGTGCTGCTGCCATCATTGTGCTGACCACAACTGGCCGCTCA
GCCCAGCTTCTGTCTCGGTACCGACCTCGGGCAGCAGTCATTGCTGTCACCCGCTCTGCC
CAGGCTGCCCGCCAGGTCCACTTATGCCGAGGAGTCTTCCCCTTGCTTTACCGTGAACCT
CCAGAAGCCATCTGGGCAGATGATGTAGATCGCCGGGTGCAATTTGGCATTGAAAGTGGA
AAGCTCCGTGGCTTCCTCCGTGTTGGAGACCTGGTGATTGTGGTGACAGGCTGGCGACCT
GGCTCCGGCTACACCAACATCATGAGGGTGCTAAGCATATCCTGA
|
| Enzyme 26 GenBank Gene ID |
AB015983  |
| Enzyme 26 GeneCard ID |
PKLR  |
| Enzyme 26 GenAtlas ID |
PKLR  |
| Enzyme 26 HGNC ID |
HGNC:9020  |
| Enzyme 26 Chromosome Location |
1 |
| Enzyme 26 Locus |
1q21 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- Kanno H, Fujii H, Hirono A, Miwa S: cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8218-21. [PubMed
]
- Tani K, Fujii H, Nagata S, Miwa S: Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells. Proc Natl Acad Sci U S A. 1988 Mar;85(6):1792-5. [PubMed
]
- Tani K, Fujii H, Tsutsumi H, Sukegawa J, Toyoshima K, Yoshida MC, Noguchi T, Tanaka T, Miwa S: Human liver type pyruvate kinase: cDNA cloning and chromosomal assignment. Biochem Biophys Res Commun. 1987 Mar 13;143(2):431-8. [PubMed
]
- Kanno H, Fujii H, Tsujino G, Miwa S: Molecular basis of impaired pyruvate kinase isozyme conversion in erythroid cells: a single amino acid substitution near the active site and decreased mRNA content of the R-type PK. Biochem Biophys Res Commun. 1993 Apr 15;192(1):46-52. [PubMed
]
- Beutler E, Baronciani L: Mutations in pyruvate kinase. Hum Mutat. 1996;7(1):1-6. [PubMed
]
- Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase. Blood Cells Mol Dis. 1996;22(1):85-9. [PubMed
]
- Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (1st update). Blood Cells Mol Dis. 1996;22(3):259-64. [PubMed
]
- Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (2nd update). Blood Cells Mol Dis. 1998 Sep;24(3):273-9. [PubMed
]
- Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (Third update). Blood Cells Mol Dis. 2000 Feb;26(1):47-53. [PubMed
]
- Neubauer B, Lakomek M, Winkler H, Parke M, Hofferbert S, Schroter W: Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency. Blood. 1991 May 1;77(9):1871-5. [PubMed
]
- Kanno H, Fujii H, Hirono A, Omine M, Miwa S: Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia. Blood. 1992 Mar 1;79(5):1347-50. [PubMed
]
- Kanno H, Fujii H, Miwa S: Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused by a single amino acid substitution (426 Arg-->Gln) associated with hereditary hemolytic anemia. Blood. 1993 May 1;81(9):2439-41. [PubMed
]
- Baronciani L, Beutler E: Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia. Proc Natl Acad Sci U S A. 1993 May 1;90(9):4324-7. [PubMed
]
- Kanno H, Ballas SK, Miwa S, Fujii H, Bowman HS: Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish. Blood. 1994 Apr 15;83(8):2311-6. [PubMed
]
- Lenzner C, Nurnberg P, Thiele BJ, Reis A, Brabec V, Sakalova A, Jacobasch G: Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia. Blood. 1994 May 15;83(10):2817-22. [PubMed
]
- Baronciani L, Beutler E: Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia. J Clin Invest. 1995 Apr;95(4):1702-9. [PubMed
]
- Beutler E, Westwood B, van Zwieten R, Roos D: G-->T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase) gene is the molecular basis of a case of hereditary increase of red blood cell ATP. Hum Mutat. 1997;9(3):282-5. [PubMed
]
- Zarza R, Alvarez R, Pujades A, Nomdedeu B, Carrera A, Estella J, Remacha A, Sanchez JM, Morey M, Cortes T, Perez Lungmus G, Bureo E, Vives Corrons JL: Molecular characterization of the PK-LR gene in pyruvate kinase deficient Spanish patients. Red Cell Pathology Group of the Spanish Society of Haematology (AEHH). Br J Haematol. 1998 Nov;103(2):377-82. [PubMed
]
- Cohen-Solal M, Prehu C, Wajcman H, Poyart C, Bardakdjian-Michau J, Kister J, Prome D, Valentin C, Bachir D, Galacteros F: A new sickle cell disease phenotype associating Hb S trait, severe pyruvate kinase deficiency (PK Conakry), and an alpha2 globin gene variant (Hb Conakry). Br J Haematol. 1998 Dec;103(4):950-6. [PubMed
]
- Pastore L, Della Morte R, Frisso G, Alfinito F, Vitale D, Calise RM, Ferraro F, Zagari A, Rotoli B, Salvatore F: Novel mutations and structural implications in R-type pyruvate kinase-deficient patients from Southern Italy. Hum Mutat. 1998;11(2):127-34. [PubMed
]
- Zanella A, Bianchi P, Fermo E, Iurlo A, Zappa M, Vercellati C, Boschetti C, Baronciani L, Cotton F: Molecular characterization of the PK-LR gene in sixteen pyruvate kinase-deficient patients. Br J Haematol. 2001 Apr;113(1):43-8. [PubMed
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
8529 |
| Enzyme 27 Name |
Novel protein |
| Enzyme 27 Synonyms |
Not Available |
| Enzyme 27 Gene Name |
RP11-163G10.1 |
| Enzyme 27 Protein Sequence |
>Novel protein
MFYLAAAVSDFYVPVSEMPEHKIQSSGGPLQITMKMVPKLLSPLVKDWAPKAFIISFKLE
TDPAIVINRARKALEIYQHQVVVANILESRQSFVFIVTKDSETKLLLSEEEIEKGVEIEE
KIVDNLQSRHTAFIGDRN
|
| Enzyme 27 Number of Residues |
138 |
| Enzyme 27 Molecular Weight |
15645 |
| Enzyme 27 Theoretical pI |
5.71 |
| Enzyme 27 GO Classification |
Not Available |
| Enzyme 27 General Function |
Coenzyme transport and metabolism |
| Enzyme 27 Specific Function |
Not Available |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
Not Available |
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
Not Available |
| Enzyme 27 Transmembrane Regions |
Not Available |
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
55665116  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
Q5VVM0  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
Q5VVM0_HUMAN  |
| Enzyme 27 PDB ID |
1P9O  |
| Enzyme 27 PDB File |
Show |
| Enzyme 27 3D Structure |
|
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>936 bp
ATGGCGGAAATGGATCCGGTAGCCGAGTTCCCCCAGCCTCCCGGTGCTGCGCGCTGGGCT
GAGGTTATGGCTCGCTTCGCGGCCAGGCTGGGCGCGCAGGGCCGGCGGGTGGTGTTGGTT
ACGTCAGGCGGCACCAAGGTCCCACTGGAAGCGCGGCCGGTGCGCTTCCTGGACAACTTC
AGCAGCGGGCGGCGCGGTGCAACCTCGGCCGAGGCCTTCCTAGCCGCCGGCTACGGGGTC
CTGTTCTTGTATCGCGCTCGCTCTGCCTTCCCCTATGCCCACCGCTTCCCACCCCAGACT
TGGCTGTCCGCTCTGCGGCCTTCGGGCCCAGCCCTTTCGGGCTTGCTGAGCCTGGAGGCC
GAGGAGAATGCACTTCCGGGTTTTGCTGAGGCTCTGAGGAGCTACCAGGAGGCTGCGGCT
GCAGGCACCTTCCTGGCAGTAGAGTTCACCACTTTGGCGGACTATTTGCATCTGTTGCAG
GCTGCGGCCCAGGCACTCAATCCGCTAGGCCCTTCTGCGATGTTTTACCTGGCTGCGGCT
GTGTCAGATTTCTATGTTCCTGTCTCTGAAATGCCTGAACACAAGATCCAGTCATCTGGG
GGCCCACTGCAGATAACAATGAAGATGGTGCCAAAACTGCTTTCTCCTTTGGTTAAAGAT
TGGGCTCCCAAAGCATTTATAATTTCCTTTAAGTTGGAGACTGACCCCGCCATTGTAATT
AATCGAGCTCGGAAGGCTTTGGAAATTTATCAGCATCAAGTGGTGGTGGCTAATATCCTT
GAGTCACGACAGTCCTTTGTGTTTATTGTAACCAAAGACTCGGAAACCAAGTTATTGCTA
TCAGAGGAAGAAATAGAAAAAGGCGTAGAGATAGAAGAGAAGATAGTGGATAATCTTCAG
TCTCGACACACAGCTTTTATAGGTGACAGAAACTGA
|
| Enzyme 27 GenBank Gene ID |
AL445669  |
| Enzyme 27 GeneCard ID |
RP11-163G10.1  |
| Enzyme 27 GenAtlas ID |
RP11-163G10.1  |
| Enzyme 27 HGNC ID |
HGNC:25686  |
| Enzyme 27 Chromosome Location |
Not Available |
| Enzyme 27 Locus |
Not Available |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
Not Available |
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
8876 |
| Enzyme 28 Name |
CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase |
| Enzyme 28 Synonyms |
Not Available |
| Enzyme 28 Gene Name |
CAD |
| Enzyme 28 Protein Sequence |
>CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase
MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNY
GIPPDEMDEFGLCKWFESSGIHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVD
TRELTKKLREQGSLLGKLVQNGTEPSSLPFLDPNARPLVPEVSIKTPRVFNTGGAPRILA
LDCGLKYNQIRCLCQRGAEVTVVPWDHALDSQEYEGLFLSNGPGDPASYPSVVSTLSRVL
SEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVE
TDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEA
TAGNPGGQTVRERLTERLCPPGIPTPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAI
KALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGGQT
ALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQ
AQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHTSQVLVDKSLKGWKEI
EYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRQTAIKVTQHLG
IVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRN
SVTGGTAAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKAL
RMVDENCVGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRM
KRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAV
KQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQ
QLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLP
NNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQT
VGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAV
ASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFN
LQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVG
VKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIG
SYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSI
LEQLAEKNFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEAL
GQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMV
CAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYLN
ETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEE
ILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEVRPELGSRQDVEALWENMAVI
DCFASDHAPHTLEEKCGSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIF
HLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVL
VPPGYGQDVRKWPQGAVPQLPPSAPATSEMTTTPERPRRGIPGLPDGRFHLPPRIHRASD
PGLPAEEPKEKSSRKVAEPELMGTPDGTCYPPPPVPRQASPQNLGTPGLLHPQTSPLLHS
LVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSF
AAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRR
PVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVS
LRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEA
CFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLAT
VLGRF
|
| Enzyme 28 Number of Residues |
2225 |
| Enzyme 28 Molecular Weight |
242987 |
| Enzyme 28 Theoretical pI |
6.42 |
| Enzyme 28 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- amine binding
- amino acid binding
- aspartate carbamoyltransferase activity
- binding
- carbamoyl-phosphate synthase activity
- carboxyl- and carbamoyltransferase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleotide binding
- purine nucleotide binding
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- 'de novo' pyrimidine base biosynthesis
- amino acid and derivative metabolism
- amino acid metabolism
- arginine biosynthesis
- arginine metabolism
- biosynthesis
- cellular metabolism
- glutamine family amino acid metabolism
- glutamine metabolism
- metabolism
- nitrogen compound metabolism
- nucleobase metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- pyrimidine base biosynthesis
- pyrimidine base metabolism
- urea cycle intermediate metabolism
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 28 General Function |
Amino acid transport and metabolism |
| Enzyme 28 Specific Function |
This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase) |
| Enzyme 28 Pathways |
|
| Enzyme 28 Reactions |
- 2 ATP + L-glutamine + CO2 + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate
|
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
Not Available |
| Enzyme 28 Transmembrane Regions |
Not Available |
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
1228049  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
P27708  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
PYR1_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>6678 bp
ATGGCGGCCCTAGTGTTGGAGGACGGGTCGGTCCTGCGGGGCCAGCCCTTTGGGGCCGCC
GTGTCGACTGCCGGGGAAGTGGTGTTTCAAACCGGCATGGTCGGCTACCCCGAGGCCCTC
ACTGATCCCTCCTACAAGGCACAGATCTTAGTGCTCACCTATCCTCTGATCGGCAACTAT
GGCATCCCCCCAGATGAAATGGATGAGTTCGGTCTCTGCAAGTGGTTTGAATCCTCGGGC
ATCCACGTAGCAGCACTGGTAGTGGGAGAGTGCTGTCCTACTCCCAGCCACTGGAGTGCC
ACCCGCACCCTGCATGAGTGGCTGCAGCAGCATGGCATCCCTGGCTTGCAAGGAGTAGAC
ACTCGGGAGCTGACCAAGAAGTTGCGGGAACAGGGGTCTCTGCTGGGGAAGCTGGTCCAG
AATGGAACAGAACCTTCATCCCTGCCATTCTTGGACCCCAATGCCCGCCCCCTGGTACCA
GAGGTCTCCATTAAGACTCCACGGGTATTCAATACAGGGGGTGCCCCTCGGATCCTTGCT
TTGGACTGTGGCCTCAAGTATAATCAGATCCGATGCCTCTGCCAGCGTGGGGCTGAGGTC
ACTGTGGTACCCTGGGACCATGCACTAGACAGCCAAGAGTATGAGGGTCTCTTCTTAAGT
AATGGGCCTGGTGACCCTGCCTCCTATCCCAGTGTCGTATCCACACTGAGCCGTGTTTTA
TCTGAGCCTAATCCCCGACCTGTCTTTGGGATCTGCCTGGGACACCAGCTATTGGCCTTA
GCCATTGGGGCCAAGACTTACAAGATGAGATATGGGAACCGAGGCCATAACCAGCCCTGC
TTGTTGGTGGGCTCTGGGCGCTGCTTTCTGACATCCCAGAACCATGGGTTTGCTGTGGAG
ACAGACTCACTGCCAGCAGACTGGGCTCCTCTCTTCACCAACGCCAATGATGGTTCCAAT
GAAGGCATTGTGCACAACAGCTTGCCTTTCTTCAGTGTCCAGTTTCACCCAGAGCACCAA
GCTGGCCCTTCAGATATGGAACTGCTTTTCGATATCTTTCTGGAAACTGTGAAAGAGGCC
ACAGCTGGGAACCCTGGGGGCCAGACAGTTAGAGAGCGGCTGACTGAGCGCCTCTGTCCC
CCTGGGATTCCCACTCCCGGCTCTGGACTTCCACCACCACGAAAGGTTCTGATCCTGGGC
TCAGGGGGCCTCTCCATTGGCCAAGCTGGAGAATTTGACTACTCGGGCTCTCAGGCAATT
AAGGCCCTGAAGGAGGAAAACATCCAGACGTTGCTGATCAACCCCAATATTGCCACAGTG
CAGACCTCCCAGGGGCTGGCCGACAAGGTCTATTTTCTTCCCATAACACCTCATTATGTA
ACCCAGGTGATACGTAATGAACGCCCCGATGGTGTGTTACTGACTTTTGGGGGCCAGACT
GCTCTGAACTGTGGTGTGGAGCTGACCAAGGCCGGGGTGCTGGCTCGGTATGGGGTCCGG
GTCCTGGGCACAACAGTGGAGACCATTGAGCTGACCGAGGATCGACGGGCCTTTGCTGCC
AGAATGGCAGAGATCGGAGAGCATGTGGCCCCGAGCGAGGCAGGAAATTCTCTTGAACAG
GCCCAGGCAGCCGCTGAACGGCTGGGGTACCCTGTGCTAGTGCGTGCAGCCTTTGCCGTG
GGTGGCCTGGGCTCTGGCTTTGCCTCTAACAGGGAGGAGCTCTCTGCTCTCGTGGCCCCA
GCTTTTGCCCATACCAGCCAAGTGCTAGTAGACAAGTCTCTGAAGGGATGGAAGGAGATT
GAGTACGAGGTGGTGAGAGACGCCTATGGCAACTGTGTCACGGTGTGTAACATGGAGAAC
TTGGACCCACTGGGCATCCACACTGGTGAGTCCATAGTGGTGGCCCCTAGCCAGACACTG
AATGACAGGGAGTATCAGCTCCTGAGGCAGACAGCTATCAAGGTGACCCAGCACCTGGGA
ATTGTTGGGGAGTGCAATGTGCAGTATGCCTTGAACCCTGAGTCTGAGCAGTATTACATC
ATTGAAGTGAATGCCAGGCTCTCTCGCAGCTCTGCCCTGGCCAGTAAGGCCACAGGTTAT
CCACTGGCTTATGTGGCAGCCAAGCTAGCATTGGGCATCCCTTTGCCTGAGCTCAGGAAC
TCTGTGACAGGGGGTACAGCAGCCTTTGAACCCAGCGTGGATTATTGTGTGGTGAAGATT
CCTCGATGGGACCTTAGCAAGTTCCTGCGAGTCAGCACAAAGATTGGGAGCTGCATGAAG
AGCGTTGGTGAAGTCATGGGCATTGGGCGTTCATTTGAGGAGGCCTTCCAGAAGGCCCTG
CGCATGGTGGATGAGAACTGTGTGGGCTTTGATCACACAGTGAAACCAGTCAGCGATATG
GAGTTGGAGACTCCAACAGATAAGCGGATTTTTGTGGTGGCAGCTGCTTTGTGGGCTGGT
TATTCAGTGGACCGCCTGTATGAGCTCACACGCATCGACCGCTGGTTCCTGCACCGAATG
AAGCGTATCATCGCACATGCCCAGCTGCTAGAACAACACCGTGGACAGCCTTTGCCGCCA
GACCTGCTGCAACAGGCCAAGTGTCTTGGCTTCTCAGACAAACAGATTGCCCTTGCAGTT
CTGAGCACAGAGCTGGCTGTTCGCAAGCTGCGTCAGGAACTGGGGATCTGTCCAGCAGTG
AAACAGATTGACACAGTTGCAGCTGAGTGGCCAGCCCAGACAAATTACCTATACCTAACG
TATTGGGGCACCACCCATGACCTCACCTTTCGAACACCTCATGTCCTAGTCCTTGGCTCT
GGCGTCTACCGTATTGGCTCCAGTGTTGAGTTTGACTGGTGTGCTGTAGGCTGCATCCAG
CAGCTCCGAAAGATGGGATATAAGACCATCATGGTGAACTATAACCCAGAGACAGTCAGC
ACCGACTATGACATGTGTGATCGACTCTACTTTGATGAGATCTCTTTTGAGGTGGTGATG
GACATCTATGAGCTCGAGAACCCTGAAGGTGTGATCCTATCCATGGGTGGACAGCTGCCC
AACAACATGGCCATGGCGTTGCATCGGCAGCAGTGCCGGGTGCTGGGCACCTCCCCTGAA
GCCATTGACTCGGCTGAGAACCGTTTCAAGTTTTCCCGGCTCCTTGACACCATTGGTATC
AGCCAGCCTCAGTGGAGGGAGCTCAGTGACCTCGAGTCTGCTCGCCAATTCTGCCAGACC
GTGGGGTACCCCTGTGTGGTGCGCCCCTCCTATGTGCTGAGCGGTGCTGCTATGAATGTG
GCCTACGCGGATGGAGACCTGGAGCGCTTCCTGAGCAGCGCAGCAGCCGTCTCCAAAGAG
CATCCCGTGGTCATCTCCAAGTTCATCCAGGAGGCTAAGGAGATTGACGTGGATGCCGTG
GCCTCTGATGGTGTGGTGGCAGCCATCGCCATCTCTGAGCATGTGGAGAATGCAGGTGTG
CATTCAGGTGATGCGACGCTGGTGACCCCCCCACAAGATATCACTGCCAAAACCCTGGAG
CGGATCAAAGCCATTGTGCATGCTGTGGGCCAGGAGCTACAGGTCACAGGACCCTTCAAT
CTGCAGCTCATTGCCAAGGATGACCAGCTGAAAGTTATTGAATGCAACGTACGTGTCTCT
CGCTCCTTCCCCTTCGTTTCCAAGACACTGGGTGTGGACCTAGTAGCCTTGGCCACGCGG
GTCATCATGGGGGAAGAAGTGGAACCTGTGGGGCTAATGACTGGTTCTGGAGTCGTGGGA
GTAAAGGTGCCTCAGTTCTCCTTCTCCCGCTTGGCGGGTGCTGACGTGGTGTTGGGTGTG
GAAATGACCAGTACTGGGGAGGTGGCCGGCTTTGGGGAGAGCCGCTGTGAGGCATACCTC
AAGGCCATGCTAAGCACTGGCTTTAAGATCCCCAAGAAGAATATCCTGCTGACCATTGGC
AGCTATAAGAACAAAAGCGAGCTGCTCCCAACTGTGCGGCTACTGGAGAGCCTGGGCTAC
AGCCTCTATGCCAGTCTCGGCACAGCTGACTTCTACACTGAGCATGGCGTCAAGGTAACA
GCTGTGGACTGGCACTTTGAGGAGGCTGTGGATGGTGAGTGCCCACCACAGCGGAGCATC
CTGGAGCAGCTAGCTGAGAAAAACTTTGAGCTGGTGATTAACCTGTCAATGCGTGGAGCT
GGGGGCCGGCGTCTCTCCTCCTTTGTCACCAAGGGCTACCGCACCCGACGCTTGGCCGCT
GACTTCTCCGTGCCCCTAATCATCGATATCAAGTGCACCAAACTCTTTGTGGAGGCCCTA
GGCCAGATCGGGCCAGCCCCTCCTTTGAAGGTGCATGTTGACTGTATGACCTCCCAAAAG
CTTGTGCGACTGCCGGGATTGATTGATGTCCATGTGCACCTGCGGGAACCAGGTGGGACA
CATAAGGAGGACTTTGCTTCAGGCACAGCCGCTGCCCTGGCTGGGGGTATCACCATGGTG
TGTGCCATGCCTAATACCCGGCCCCCCATCATTGACGGCCCTGCTCTGGCCCTGGCCCAG
AAGCTGGCAGAGGCTGGCGCCCGGTGCGACTTTGCGCTATTCCTTGGGGCCTCGTCTGAA
AATGCAGGAACCTTGGGCACCGTGGCCGGGTCTGCAGCCGGGCTGAAGCTTTACCTCAAT
GAGACCTTCTCTGAGCTGCGGCTGGACAGCGTGGTCCAGTGGATGGAGCATTTCGAGACA
TGGCCCTCCCACCTCCCCATTGTGGCTCACGCAGAGCAGCAAACCGTGGCTGCTGTCCTC
ATGGTGGCTCAGCTCACTCAGCGCTCAGTGCACATATGTCACGTGGCACGGAAGGAGGAG
ATCCTGCTAATTAAAGCTGCAAAGGCACGGGGCTTGCCAGTGACCTGCGAGGTGGCTCCC
CACCACCTGTTCCTAAGCCATGATGACCTGGAGCGCCTGGGGCCTGGGAAGGGGGAGGTC
CGGCCTGAGCTTGGCTCCCGCCAGGATGTGGAAGCCCTGTGGGAGGACATGGCTGTCATC
GACTGCTTTGCCTCAGACCATGCTCCCCATACCTTGGAGGAGAAGTGTGGGTCCAGGCCC
CCACCTGGGTTCCCAGGGTTAGAGACCATGCTGCCACTACTCCTGACGGCTGTAAGCGAG
GGCCGGCTCAGCCTGGACGACCTGCTGCAGCGATTGCACCACAATCCTCGGCGCATCTTT
CACCTGCCCCCGCAGGAGGACACCTATGTGGAGGTGGATCTGGAGCATGAGTGGACAATT
CCCAGCCACATGCCCTTCTCCAAGGCCCACTGGACACCTTTTGAAGGGCAGAAAGTGAAG
GGCACCGTCCGCCGTGTGGTCCTGCGAGGGGAGGTTGCCTATATCGATGGGCAGGTTCTG
GTACCCCCGGGCTATGGACAGGATGTACGGAAGTGGCCACAGGGGGCTGTTCCTCAGCTC
CCACCCTCAGCCCCTGCCACTAGTGAGATGACCACGACACCTGAAAGACCCCGCCGTGGC
ATCCCAGGGCTTCCTGATGGCCGCTTCCATCTGCCGCCCCGAATCCATCGAGCCTCCGAC
CCAGGTTTGCCAGCTGAGGAGCCAAAGGAGAAGTCCTCTCGGAAGGTAGCCGAGCCAGAG
CTGATGGGAACCCCTGATGGCACCTGCTACCCTCCACCACCAGTACCGAGACAGGCATCT
CCCCAGAACCTGGGGACCCCTGGCTTGCTGCACCCCCAGACCTCACCCCTGCTGCACTCA
TTAGTGGGCCAACATATCCTGTCCGTCCAGCAGTTCACCAAGGATCAGATGTCTCACCTG
TTCAATGTGGCACACACACTGCGTATGATGGTGCAGAAGGAGCGGAGCCTCGACATCCTG
AAGGGGAAGGTCATGGCCTCCATGTTCTATGAAGTGAGCACACGGACCAGCAGCTCCTTT
GCAGCAGCCATGGCCCGGCTGGGAGGTGCTGTGCTCAGCTTCTCGGAAGCCACATCGTCC
GTCCAGAAGGGCGAATCCCTGGCTGACTCCGTGCAGACCATGAGCTGCTATGCCGACGTC
GTCGTGCTCCGGCACCCCCAGCCTGGAGCAGTGGAGCTGGCCGCCAAGCACTGCCGGAGG
CCAGTGATCAATGCTGGGGATGGGGTCGGAGAGCACCCCACCCAGGCCCTGCTGGACATC
TTCACCATCCGTGAGGAGCTGGGAACTGTCAATGGCATGACGATCACGATGGTGGGTGAC
CTGAAGCACGGACGCACAGTACATTCCCTGGCCTGCCTGCTCACCCAGTATCGTGTCAGC
CTGCGCTACGTGGCACCTCCCAGCCTGCGCATGCCACCCACTGTGCGGGCCTTCGTGGCC
TCCCGCGGCACCAAGCAGGAGGAATTCGAGAGCATTGAGGAGGCGCTGCCTGACACTGAT
GTGCTCTACATGACTCGAATCCAGAAGGAACGATTTGGCTCTACCCAGGAGTACGAAGCT
TGCTTTGGTCAGTTCATCCTCACTCCCCACATCATGACCCGGGCCAAGAAGAAGATGGTG
GTGATGCACCCGATGCCCCGTGTCAACGAGATAAGCGTGGAAGTGGACTCGGATCCCCGC
GCAGCCTACTTCCGCCAGGCTGAGAACGGCATGTACATCCGCATGGCTCTGTTAGCCACC
GTGCTGGGCCGTTTCTAG
|
| Enzyme 28 GenBank Gene ID |
D78586  |
| Enzyme 28 GeneCard ID |
CAD  |
| Enzyme 28 GenAtlas ID |
CAD  |
| Enzyme 28 HGNC ID |
HGNC:1424  |
| Enzyme 28 Chromosome Location |
2 |
| Enzyme 28 Locus |
2p22-p21 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- Iwahana H, Fujimura M, Ii S, Kondo M, Moritani M, Takahashi Y, Yamaoka T, Yoshimoto K, Itakura M: Molecular cloning of a human cDNA encoding a trifunctional enzyme of carbamoyl-phosphate synthetase-aspartate transcarbamoylase-dihydroorotase in de Novo pyrimidine synthesis. Biochem Biophys Res Commun. 1996 Feb 6;219(1):249-55. [PubMed
]
- Davidson JN, Rao GN, Niswander L, Andreano C, Tamer C, Chen KC: Organization and nucleotide sequence of the 3' end of the human CAD gene. DNA Cell Biol. 1990 Nov;9(9):667-76. [PubMed
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
13093 |
| Enzyme 29 Name |
Uncharacterized protein POLR3G |
| Enzyme 29 Synonyms |
- Polymerase
- RNAIII
- DNA directedpolypeptide G
- 32kD, isoform CRA_a
|
| Enzyme 29 Gene Name |
POLR3G |
| Enzyme 29 Protein Sequence |
>Uncharacterized protein POLR3G
MAGNKGRGRAAYTFNIEAVGFSKGEKLPDVVLKPPPLFPDTDYKPVPLKTGEGEEYMLAL
KQELRETMKRMPYFIETPEERQDIERYSKRYMKVYKEEWIPDWRRLPREMMPRNKCKKAG
PKPKKAKDAGKGTPLTNTEDVLKKMEELEKRGDGEKSDEENEEKEGSKEKSKEGDDDDDD
DAAEQEEYDEEEQEEENDYINSYFEDGDDFGADSDDNMDEATY
|
| Enzyme 29 Number of Residues |
223 |
| Enzyme 29 Molecular Weight |
25915 |
| Enzyme 29 Theoretical pI |
4.26 |
| Enzyme 29 GO Classification |
Not Available |
| Enzyme 29 General Function |
Not Available |
| Enzyme 29 Specific Function |
Not Available |
| Enzyme 29 Pathways |
Not Available |
| Enzyme 29 Reactions |
Not Available |
| Enzyme 29 Pfam Domain Function |
Not Available |
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
Not Available |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
A8MTH0  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
A8MTH0_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
Not Available |
| Enzyme 29 GenBank Gene ID |
AC027323  |
| Enzyme 29 GeneCard ID |
A8MTH0  |
| Enzyme 29 GenAtlas ID |
POLR3G  |
| Enzyme 29 HGNC ID |
HGNC:30075  |
| Enzyme 29 Chromosome Location |
Not Available |
| Enzyme 29 Locus |
Not Available |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
Not Available |
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
13379 |
| Enzyme 30 Name |
Ectonucleoside triphosphate diphosphohydrolase 8 |
| Enzyme 30 Synonyms |
- NTPDase 8
- NTPDase8
- E-NTPDase 8
|
| Enzyme 30 Gene Name |
ENTPD8 |
| Enzyme 30 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 8
MGLSRKEQVFLALLGASGVSGLTALILLLVEATSVLLPTDIKFGIVFDAGSSHTSLFLYQ
WLANKENGTGVVSQALACQVEGPGISSYTSNAAQAGESLQGCLEEALVLIPEAQHRKTPT
FLGATAGMRLLSRKNSSQARDIFAAVTQVLGRSPVDFWGAELLAGQAEGAFGWITVNYGL
GTLVKYSFTGEWIQPPEEMLVGALDMGGASTQITFVPGGPILDKSTQADFRLYGSDYSVY
THSYLCFGRDQMLSRLLVGLVQSRPAALLRHPCYLSGYQTTLALGPLYESPCVHATPPLS
LPQNLTVEGTGNPGACVSAIRELFNFSSCQGQEDCAFDGVYQPPLRGQFYAFSNFYYTFH
FLNLTSRQPLSTVNATIWEFCQRPWKLVEASYPGQDRWLRDYCASGLYILTLLHEGYGFS
EETWPSLEFRKQAGGVDIGWTLGYMLNLTGMIPADAPAQWRAESYGVWVAKVVFMVLALV
AVVGAALVQLFWLQD
|
| Enzyme 30 Number of Residues |
495 |
| Enzyme 30 Molecular Weight |
53904 |
| Enzyme 30 Theoretical pI |
4.96 |
| Enzyme 30 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 30 General Function |
Not Available |
| Enzyme 30 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 30 Pathways |
|
| Enzyme 30 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 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
59003409  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
Q5MY95  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
ENTP8_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 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 30 GenBank Gene ID |
AY903953  |
| Enzyme 30 GeneCard ID |
Q5MY95  |
| Enzyme 30 GenAtlas ID |
ENTPD8  |
| Enzyme 30 HGNC ID |
HGNC:24860  |
| Enzyme 30 Chromosome Location |
Not Available |
| Enzyme 30 Locus |
Not Available |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 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 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
14489 |
| Enzyme 31 Name |
Putative nucleoside diphosphate kinase |
| Enzyme 31 Synonyms |
- NDK
- NDP kinase
|
| Enzyme 31 Gene Name |
NME2P1 |
| Enzyme 31 Protein Sequence |
>Putative nucleoside diphosphate kinase
MQCGLVGKIIKRFEQKGFRLVAMKFLPASEEHLKQHYIDLKDRPFFPGLVKYMNSGPVVA
MVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVKSAEKEISLRFK
PEELVDYKSCAHDWVYE
|
| Enzyme 31 Number of Residues |
137 |
| Enzyme 31 Molecular Weight |
15529 |
| Enzyme 31 Theoretical pI |
8.83 |
| Enzyme 31 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 31 General Function |
Nucleotide transport and metabolism |
| Enzyme 31 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 31 Pathways |
|
| Enzyme 31 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331] ALL_REAC R00331 > R00124 R00156 R00330 R00570 R00722 R01137 R01857 R02093 R02326 R02331 R03530
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
2935619  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
O60361  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
NDK8_HUMAN  |
| Enzyme 31 PDB ID |
1NSK  |
| Enzyme 31 PDB File |
Show |
| Enzyme 31 3D Structure |
|
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>414 bp
ATGCAGTGCGGCCTGGTGGGCAAGATCATCAAGCGCTTCGAGCAGAAGGGGTTCCGCCTC
GTGGCCATGAAGTTCCTCCCGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTG
AAGGACCGCCCATTCTTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTCGTGGCC
ATGGTCTGGGAGGGGCTGAACGTCGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAAT
CCAGCAGATTCTAAGCCAGGCACCATTCGTGGGGACTTTTGCATTCAGGTTGGCAGGAAC
ATCATTCATGGCAGTGATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTACGGTTTAAG
CCTGAAGAACTGGTTGACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
|
| Enzyme 31 GenBank Gene ID |
AC004263  |
| Enzyme 31 GeneCard ID |
O60361  |
| Enzyme 31 GenAtlas ID |
NME2P1  |
| Enzyme 31 HGNC ID |
HGNC:31358  |
| Enzyme 31 Chromosome Location |
12 |
| Enzyme 31 Locus |
12q24.31 |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
Not Available |
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
15191 |
| Enzyme 32 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 32 Synonyms |
Not Available |
| Enzyme 32 Gene Name |
NME7 |
| Enzyme 32 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 32 Number of Residues |
376 |
| Enzyme 32 Molecular Weight |
42492 |
| Enzyme 32 Theoretical pI |
6.44 |
| Enzyme 32 GO Classification |
Not Available |
| Enzyme 32 General Function |
Nucleotide transport and metabolism |
| Enzyme 32 Specific Function |
Not Available |
| Enzyme 32 Pathways |
Not Available |
| Enzyme 32 Reactions |
Not Available |
| Enzyme 32 Pfam Domain Function |
Not Available |
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
158254838  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
A8K3T6  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
A8K3T6_HUMAN  |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>1131 bp
ATGAATCATAGTGAAAGATTTGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
|
| Enzyme 32 GenBank Gene ID |
AK290701  |
| Enzyme 32 GeneCard ID |
A8K3T6  |
| Enzyme 32 GenAtlas ID |
Not Available |
| Enzyme 32 HGNC ID |
Not Available |
| Enzyme 32 Chromosome Location |
Not Available |
| Enzyme 32 Locus |
Not Available |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
Not Available |
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
15192 |
| Enzyme 33 Name |
DNA-directed RNA polymerase III subunit RPC1 |
| Enzyme 33 Synonyms |
- RNA polymerase III subunit C1
- DNA-directed RNA polymerase III subunit A
- DNA-directed RNA polymerase III largest subunit
- RPC155
- C160
|
| Enzyme 33 Gene Name |
POLR3A |
| Enzyme 33 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 33 Number of Residues |
1390 |
| Enzyme 33 Molecular Weight |
155644 |
| Enzyme 33 Theoretical pI |
8.62 |
| Enzyme 33 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 33 General Function |
Transcription |
| Enzyme 33 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 33 Pathways |
Not Available |
| Enzyme 33 Reactions |
Not Available |
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
2460208  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
O14802  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
RPC1_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 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 33 GenBank Gene ID |
AF021351  |
| Enzyme 33 GeneCard ID |
O14802  |
| Enzyme 33 GenAtlas ID |
POLR3A  |
| Enzyme 33 HGNC ID |
HGNC:30074  |
| Enzyme 33 Chromosome Location |
10 |
| Enzyme 33 Locus |
10q22-q23 |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 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 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
15193 |
| Enzyme 34 Name |
DNA-directed RNA polymerase I subunit RPA1 |
| Enzyme 34 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 34 Gene Name |
POLR1A |
| Enzyme 34 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 34 Number of Residues |
1720 |
| Enzyme 34 Molecular Weight |
194814 |
| Enzyme 34 Theoretical pI |
7.03 |
| 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 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 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 |
4096591  |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
O95602  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
RPA1_HUMAN  |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 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 34 GenBank Gene ID |
U33460  |
| Enzyme 34 GeneCard ID |
O95602  |
| Enzyme 34 GenAtlas ID |
POLR1A  |
| Enzyme 34 HGNC ID |
HGNC:17264  |
| Enzyme 34 Chromosome Location |
Not Available |
| Enzyme 34 Locus |
Not Available |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
Not Available |
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
15194 |
| Enzyme 35 Name |
DNA-directed RNA polymerase subunit |
| Enzyme 35 Synonyms |
Not Available |
| Enzyme 35 Gene Name |
ZNRD1 |
| Enzyme 35 Protein Sequence |
>DNA-directed RNA polymerase subunit
MSVMDLANTCSSFQSDLDFCSDCGSVLPLPGAQDTVTCIRCGFNINVRDFEGKVVKTSVV
FHQLGTAMPMSVEEGPECQGPVVDRRCPRCGHEGMAYHTRQMRSADEGQTVFYTCTNCKF
QEKEDS
|
| Enzyme 35 Number of Residues |
126 |
| Enzyme 35 Molecular Weight |
13904 |
| Enzyme 35 Theoretical pI |
4.68 |
| Enzyme 35 GO Classification |
| Function |
- DNA binding
- DNA-directed RNA polymerase activity
- binding
- catalytic activity
- cation binding
- ion binding
- nucleic acid binding
- nucleotidyltransferase activity
- transcription factor activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- RNA elongation
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- regulation of biological process
- regulation of cellular metabolism
- regulation of metabolism
- regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- regulation of physiological process
- regulation of transcription
- regulation of transcription, DNA-dependent
- transcription
- transcription, DNA-dependent
|
| Component |
| — |
|
| Enzyme 35 General Function |
Transcription |
| Enzyme 35 Specific Function |
Not Available |
| 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 |
86197925  |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
Q2L6J2  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
Q2L6J2_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>381 bp
ATGTCTGTCATGGACCTCGCCAATACTTGCTCCAGCTTTCAGTCGGACCTGGATTTCTGT
TCAGATTGCGGCTCGGTCCTGCCTCTGCCCGGGGCTCAGGATACGGTCACCTGTATTCGC
TGTGGCTTCAACATCAACGTTCGGGACTTTGAGGGGAAGGTTGTGAAGACTTCGGTTGTG
TTCCACCAACTGGGGACAGCCATGCCTATGTCGGTGGAGGAAGGGCCTGAGTGCCAGGGA
CCTGTGGTTGACAGGCGCTGCCCTCGATGTGGTCATGAAGGAATGGCATACCACACCAGA
CAGATGCGTTCAGCCGATGAAGGGCAAACTGTCTTCTACACCTGTACCAACTGCAAGTTC
CAGGAGAAGGAAGACTCTTGA
|
| Enzyme 35 GenBank Gene ID |
AB202082  |
| Enzyme 35 GeneCard ID |
Q2L6J2  |
| Enzyme 35 GenAtlas ID |
ZNRD1  |
| Enzyme 35 HGNC ID |
HGNC:13182  |
| 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 |
15195 |
| Enzyme 36 Name |
DNA-directed RNA polymerases I and III subunit RPAC2 |
| Enzyme 36 Synonyms |
- RNA polymerases I and III subunit AC2
- DNA-directed RNA polymerase I subunit D
- DNA-directed RNA polymerase I 16 kDa polypeptide
- RPA16
- RPC16
- hRPA19
- AC19
|
| Enzyme 36 Gene Name |
POLR1D |
| Enzyme 36 Protein Sequence |
>DNA-directed RNA polymerases I and III subunit RPAC2
MEEDQELERKISGLKTSMAEGERKTALEMVQAAGTDRHCVTFVLHEEDHTLGNSLRYMIM
KNPEVEFCGYTTTHPSESKINLRIQTRGTLPAVEPFQRGLNELMNVCQHVLDKFEASIKD
YKDQKASRNESTF
|
| Enzyme 36 Number of Residues |
133 |
| Enzyme 36 Molecular Weight |
15237 |
| Enzyme 36 Theoretical pI |
5.62 |
| Enzyme 36 GO Classification |
| Function |
- DNA binding
- DNA-directed RNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- protein binding
- protein dimerization 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 36 General Function |
Transcription |
| Enzyme 36 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common core component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively |
| 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 |
4689136  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
Q9Y2S0  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
RPAC2_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>402 bp
ATGGAAGAGGATCAGGAGCTGGAGAGAAAAATATCTGGATTGAAGACCTCAATGGCTGAA
GGCGAGAGGAAGACAGCCCTGGAAATGGTCCAGGCAGCTGGAACAGATAGACACTGTGTG
ACATTTGTATTGCACGAGGAAGACCATACCCTAGGAAATTCTCTACGTTACATGATCATG
AAGAACCCGGAAGTGGAATTTTGTGGTTACACTACGACCCATCCTTCAGAGAGCAAAATT
AATTTACGCATTCAGACTCGAGGTACCCTTCCAGCTGTTGAGCCATTTCAGAGAGGCCTG
AATGAGCTCATGAATGTCTGCCAACATGTGCTTGACAAGTTTGAGGCCAGCATAAAGGAC
TATAAGGATCAAAAAGCAAGCAGAAATGAATCCACATTCTAG
|
| Enzyme 36 GenBank Gene ID |
AF077044  |
| Enzyme 36 GeneCard ID |
Q9Y2S0  |
| Enzyme 36 GenAtlas ID |
POLR1D  |
| Enzyme 36 HGNC ID |
HGNC:20422  |
| Enzyme 36 Chromosome Location |
13 |
| Enzyme 36 Locus |
13q12.2 |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 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 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
15196 |
| Enzyme 37 Name |
cDNA FLJ75210, highly similar to H.sapiens RNA polymerase II 140 kDa subunit (Polymerase (RNA) II (DNA directed) polypeptide B, 140kDa) |
| Enzyme 37 Synonyms |
Not Available |
| Enzyme 37 Gene Name |
POLR2B |
| Enzyme 37 Protein Sequence |
>cDNA FLJ75210, highly similar to H.sapiens RNA polymerase II 140 kDa subunit (Polymerase (RNA) II (DNA directed) polypeptide B, 140kDa)
MYDADEDMQYDEDDDEITPDLWQEACWIVISSYFDEKGLVRQQLDSFDEFIQMSVQRIVE
DAPPIDLQAEAQHASGEVEEPPRYLLKFEQIYLSKPTHWERDGAPSPMMPNEARLRNLTY
SAPLYVDITKTVIKEGEEQLQTQHQKTFIGKIPIMLRSTYCLLNGLTDRDLCELNECPLD
PGGYFIINGSEKVLIAQEKMATNTVYVFAKKDSKYAYTGECRSCLENSSRPTSTIWVSML
ARGGQGAKKSAIGQRIVATLPYIKQEVPIIIVFRALGFVSDRDILEHIIYDFEDPEMMEM
VKPSLDEAFVIQEQNVALNFIGSRGAKPGVTKEKRIKYAKEVLQKEMLPHVGVSDFCETK
KAYFLGYMVHRLLLAALGRRELDDRDHYGNKRLDLAGPLLAFLFRGMFKNLLKEVRIYAQ
KFIDRGKDFNLELAIKTRIISDGLKYSLATGNWGDQKKAHQARAGVSQVLNRLTFASTLS
HLRRLNSPIGRDGKLAKPRQLHNTLWGMVCPAETPEGHAVGLVKNLALMAYISVGSQPSP
ILEFLEEWSMENLEEISPAAIADATKIFVNGCWVGIHKDPEQLMNTLRKLRRQMDIIVSE
VSMIRDIREREIRIYTDAGRICRPLLIVEKQKLLLKKRHIDQLKEREYNNYSWQDLVASG
VVEYIDTLEEETVMLAMTPDDLQEKEVAYCSTYTHCEIHPSMILGVCASIIPFPDHNQSP
RNTYQSAMGKQAMGVYITNFHVRMDTLAHVLYYPQKPLVTTRSMEYLRFRELPAGINSIV
AIASYTGYNQEDSVIMNRSAVDRGFFRSVFYRSYKEQESKKGFDQEEVFEKPTRETCQGM
RHAIYDKLDDDGLIAPGVRVSGDDVIIGKTVTLPENEDELESTNRRYTKRDCSTFLRTSE
TGIVDQVMVTLNQEGYKFCKIRVRSVRIPQIGDKFASRHGQKGTCGIQYRQEDMPFTCEG
ITPDIIINPHAIPSRMTIGHLIECLQGKVSANKGEIGDATPFNDAVNVQKISNLLSDYGY
HLRGNEVLYNGFTGRKITSQIFIGPTYYQRLKHMVDDKIHSRARGPIQILNRQPMEGRSR
DGGLRFGEMERDCQIAHGAAQFLRERLFEASDPYQVHVCNLCGIMAIANTRTHTYECRGC
RNKTQISLVRMPYACKLLFQELMSMSIAPRMMSV
|
| Enzyme 37 Number of Residues |
1174 |
| Enzyme 37 Molecular Weight |
133898 |
| Enzyme 37 Theoretical pI |
6.87 |
| Enzyme 37 GO Classification |
Not Available |
| Enzyme 37 General Function |
Transcription |
| Enzyme 37 Specific Function |
Not Available |
| Enzyme 37 Pathways |
Not Available |
| Enzyme 37 Reactions |
Not Available |
| Enzyme 37 Pfam Domain Function |
Not Available |
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
158260669  |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
A8K1A8  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
A8K1A8_HUMAN  |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
>3525 bp
ATGTACGACGCGGATGAGGATATGCAATATGATGAGGATGATGATGAAATCACCCCGGAT
TTGTGGCAAGAAGCATGCTGGATTGTAATCAGTTCCTATTTTGACGAGAAAGGCTTGGTT
AGACAACAGCTGGATTCTTTTGATGAGTTTATTCAGATGTCTGTTCAAAGAATTGTGGAA
GACGCTCCTCCTATAGACCTACAGGCTGAAGCTCAGCATGCTAGTGGAGAAGTTGAAGAA
CCGCCACGATATTTGCTGAAGTTTGAACAAATTTATCTTTCCAAGCCTACCCATTGGGAA
AGAGATGGTGCTCCTTCACCAATGATGCCCAATGAAGCTAGATTAAGGAATCTCACGTAT
TCTGCTCCGCTTTATGTTGATATAACAAAAACAGTCATTAAAGAAGGTGAAGAACAACTT
CAGACTCAGCATCAGAAAACTTTTATAGGAAAAATTCCAATTATGTTGCGGTCAACTTAC
TGCCTTTTGAATGGCTTGACAGATCGTGATCTTTGTGAGTTAAATGAATGCCCTTTGGAT
CCTGGTGGCTATTTCATTATTAATGGATCAGAAAAGGTTCTGATTGCCCAAGAGAAAATG
GCAACAAACACAGTTTATGTGTTTGCCAAAAAGGATTCTAAATATGCCTACACAGGAGAG
TGTAGATCATGTCTTGAGAATTCTTCCCGACCCACCAGTACTATATGGGTTAGCATGCTG
GCAAGAGGAGGACAGGGTGCCAAGAAGAGTGCTATTGGTCAGCGCATTGTGGCAACTCTA
CCATATATCAAGCAAGAAGTTCCCATCATTATTGTGTTCAGAGCATTAGGTTTTGTGTCC
GACAGAGATATTTTAGAACATATTATTTATGATTTTGAAGATCCAGAGATGATGGAAATG
GTTAAACCTTCTCTCGATGAAGCTTTTGTCATCCAAGAACAGAATGTTGCACTAAATTTC
ATTGGTTCAAGAGGAGCAAAGCCTGGTGTTACTAAAGAGAAAAGAATTAAATATGCAAAG
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 37 GenBank Gene ID |
AK289823  |
| Enzyme 37 GeneCard ID |
A8K1A8  |
| Enzyme 37 GenAtlas ID |
Not Available |
| Enzyme 37 HGNC ID |
Not Available |
| Enzyme 37 Chromosome Location |
Not Available |
| Enzyme 37 Locus |
Not Available |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
Not Available |
| Enzyme 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
15197 |
| Enzyme 38 Name |
DNA-directed RNA polymerase (EC 2.7.7.6) |
| Enzyme 38 Synonyms |
Not Available |
| Enzyme 38 Gene Name |
DKFZp686D10173 |
| Enzyme 38 Protein Sequence |
>DNA-directed RNA polymerase (EC 2.7.7.6)
MDVLAEEFGNLTPEQLAAPIPTVEEKWRLLPAFLKVKGLVKQHIDSFNYFINVEIKKIMK
ANEKVTSDADPMWYLKYLNIYVGLPDVEESFNVTRPVSPHECRLRDMTYSAPITVDIEYT
RGSQRIIRNALPIGRMPIMLRSSNCVLTGKTPAEFAKLNECPLDPGGYFIVKGVEKVILI
QEQLSKNRIIVEADRKGAVGASVTSSTHEKKSRTNMAVKQGRFYLRHNTLSEDIPIVIIF
KAMGVESDQEIVQMIGTEEHVMAAFGPSLEECQKAQIFTQMQALKYIGNKVRRQRMWGGG
PKKTKIEEARELLASTILTHVPVKEFNFRAKCIYTAVMVRRVILAQGDNKVDDRDYYGNK
RLELAGQLLSLLFEDLFKKFNSEMKKIADQVIPKQRAAQFDVVKHMRQDQITNGMVNAIS
TGNWSLKRFKMDRQGVTQVLSRLSYISALGMMTRISSQFEKTRKVSGPRSLQPSQWGMLC
PSDTPEGEACGLVKNLALMTHITTDMEDGPIVKLASNLGVEDVNLLCGEELSYPNVFLVF
LNGNILGVIRDHKKLVNTFRLMRRAGYINEFVSISTNLTDRCVYISSDGGRLCRPYIIVK
KQKPAVTNKHMEELAQGYRNFEDFLHESLVEYLDVNEENDCNIALYEHTINKDTTHLEIE
PFTLLGVCAGLIPYPHHNQSPRNTYQCAMGKQAMGTIGYNQRNRIDTLMYLLAYPQKPMV
KTKTIELIEFEKLPAGQNATVAVMSYSGYDIEDALVLNKASLDRGFGRCLVYKNAKCTLK
RYTNQTFDKVMGPMLDAATRKPIWRHEILDADGICSPGEKVENKQVLVNKSMPTVTQIPL
EGSNVPQQPQYKDVPITYKGATDSYIEKVMISSNAEDAFLIKMLLRQTRRPEIGDKFSSR
HGQKGVCGLIVPQEDMPFCDSGICPDIIMNPHGFPSRMTVGKLIELLAGKAGVLDGRFHY
GTAFGGSKVKDVCEDLVRHGYNYLGKDYVTSGITGEPFEAYIYFGPVYYQKLKHMVLDKM
HARARGPRAVLTRQPTEGRSRDGGLRLGEMERDCLIGYGASMLLLERLMISSDAFEVDVC
GQCGLLGYSGWCHYCKSSCHVSSLRIPYACKLLFQELQSMNIIPRLKLSKYNE
|
| Enzyme 38 Number of Residues |
1133 |
| Enzyme 38 Molecular Weight |
127821 |
| Enzyme 38 Theoretical pI |
8.64 |
| Enzyme 38 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 38 General Function |
Transcription |
| Enzyme 38 Specific Function |
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1) |
| Enzyme 38 Pathways |
Not Available |
| Enzyme 38 Reactions |
- nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444] ALL_REAC R00444 > R00435 R00441 R00442 R00443
|
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
31873396  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
Q7Z3R8  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
Q7Z3R8_HUMAN  |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>3402 bp
ATGGACGTGCTAGCGGAGGAGTTTGGGAACCTGACTCCGGAGCAGCTGGCGGCGCCGATC
CCGACTGTAGAGGAAAAATGGAGGCTGCTTCCAGCATTTTTAAAGGTGAAAGGCCTTGTG
AAACAGCATATAGATTCATTTAACTATTTCATTAATGTAGAGATAAAGAAGATAATGAAA
GCCAATGAAAAGGTTACAAGTGACGCTGACCCTATGTGGTACTTAAAATATCTTAATATC
TATGTTGGGCTTCCTGATGTTGAAGAAAGCTTCAATGTAACTAGACCAGTGTCCCCTCAT
GAGTGCCGTTTGAGAGACATGACATACTCTGCCCCTATTACAGTGGATATTGAATATACC
CGAGGCAGCCAGAGGATCATCCGCAATGCCTTACCTATCGGCAGAATGCCCATAATGCTA
CGTAGTTCAAACTGTGTTCTTACAGGAAAAACGCCAGCAGAATTTGCCAAACTGAACGAA
TGTCCCTTAGATCCAGGTGGCTACTTCATTGTTAAAGGAGTAGAAAAAGTTATTCTTATC
CAAGAGCAGCTGTCTAAGAACAGGATCATCGTGGAGGCTGATAGAAAAGGGGCTGTTGGA
GCTTCAGTTACCAGCTCTACCCATGAGAAAAAAAGCAGAACCAATATGGCTGTGAAACAA
GGACGATTTTATTTGAGGCATAATACTTTGTCAGAAGATATACCCATTGTCATCATATTT
AAGGCCATGGGTGTTGAGAGTGACCAGGAAATTGTGCAGATGATTGGAACAGAGGAGCAC
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
TATAACTACTTGGGGAAAGACTATGTTACATCCGGCATCACAGGTGAGCCCTTCGAAGCA
TACATCTATTTTGGCCCCGTGTACTATCAGAAGCTGAAACACATGGTGCTAGATAAAATG
CATGCCCGGGCCCGGGGCCCACGAGCCGTCCTTACCAGGCAACCCACTGAAGGACGGTCT
CGTGATGGTGGCTTGCGTCTCGGGGAAATGGAACGTGACTGTTTAATCGGTTATGGAGCC
AGTATGCTTTTGCTAGAGAGACTAATGATTTCAAGTGATGCCTTTGAGGTTGATGTCTGT
GGGCAGTGTGGACTTCTGGGGTATTCTGGCTGGTGCCATTACTGCAAGTCATCCTGCCAC
GTGTCTTCCCTCCGTATTCCGTATGCCTGCAAGCTGCTCTTCCAGGAACTACAGTCTATG
AACATCATCCCCAGGTTAAAACTGTCCAAGTACAATGAATGA
|
| Enzyme 38 GenBank Gene ID |
BX537447  |
| Enzyme 38 GeneCard ID |
Q7Z3R8  |
| Enzyme 38 GenAtlas ID |
DKFZp686D10173  |
| Enzyme 38 HGNC ID |
HGNC:30348  |
| Enzyme 38 Chromosome Location |
Not Available |
| Enzyme 38 Locus |
Not Available |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 General References |
Not Available |
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
15198 |
| Enzyme 39 Name |
DNA-directed RNA polymerase III subunit RPC7-like |
| Enzyme 39 Synonyms |
- RNA polymerase III subunit C7-like
- DNA-directed RNA polymerase III subunit G-like
|
| Enzyme 39 Gene Name |
POLR3GL |
| Enzyme 39 Protein Sequence |
>DNA-directed RNA polymerase III subunit RPC7-like
MASRGGGRGRGRGQLTFNVEAVGIGKGDALPPPTLQPSPLFPPLEFRPVPLPSGEEGEYV
LALKQELRGAMRQLPYFIRPAVPKRDVERYSDKYQMSGPIDNAIDWNPDWRRLPRELKIR
VRKLQKERITILLPKRPPKTTEDKEETIQKLETLEKKEEEVTSEEDEEKEEEEEKEEEEE
EEYDEEEHEEETDYIMSYFDNGEDFGGDSDDNMDEAIY
|
| Enzyme 39 Number of Residues |
218 |
| Enzyme 39 Molecular Weight |
25334 |
| Enzyme 39 Theoretical pI |
4.19 |
| Enzyme 39 GO Classification |
Not Available |
| Enzyme 39 General Function |
Transcription |
| 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 |
16552536  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
Q9BT43  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
RPC7L_HUMAN  |
| Enzyme 39 PDB ID |
Not Available |
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>657 bp
ATGGCCAGCCGGGGTGGGGGCCGGGGTCGTGGCCGGGGCCAGTTGACCTTCAACGTGGAG
GCCGTGGGCATTGGGAAAGGGGATGCTTTGCCCCCACCCACCCTGCAGCCTTCTCCACTC
TTCCCTCCCTTGGAGTTCCGCCCAGTACCTTTGCCCTCAGGCGAGGAAGGGGAATATGTC
CTGGCACTGAAGCAAGAGCTACGAGGAGCCATGAGGCAGCTCCCCTACTTCATCCGGCCA
GCTGTCCCCAAGAGAGATGTGGAGCGTTATTCAGACAAATATCAGATGTCAGGTCCGATT
GACAATGCCATCGATTGGAACCCTGATTGGCGGCGTCTACCCCGGGAGCTAAAGATCCGA
GTGCGGAAGCTACAGAAGGAACGGATTACAATTCTGCTCCCCAAGAGGCCCCCTAAGACC
ACAGAAGATAAGGAGGAAACAATACAGAAACTAGAGACCCTGGAGAAGAAGGAAGAAGAA
GTAACTTCAGAGGAGGATGAGGAGAAAGAAGAAGAAGAAGAGAAGGAAGAGGAGGAAGAA
GAAGAGTATGATGAAGAAGAACATGAAGAGGAAACTGATTACATCATGTCATATTTTGAC
AATGGAGAGGACTTTGGTGGTGACAGTGATGACAATATGGACGAGGCTATATACTGA
|
| Enzyme 39 GenBank Gene ID |
AK056984  |
| Enzyme 39 GeneCard ID |
Q9BT43  |
| Enzyme 39 GenAtlas ID |
POLR3GL  |
| Enzyme 39 HGNC ID |
HGNC:28466  |
| 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 |
15199 |
| Enzyme 40 Name |
POLR1C protein (Fragment) |
| Enzyme 40 Synonyms |
Not Available |
| Enzyme 40 Gene Name |
POLR1C |
| Enzyme 40 Protein Sequence |
>POLR1C protein (Fragment)
EMRSRVVLGEFGVRNVHTTDFPGNYSGYDDAWDQDRFEKNFRVDVVHMDENSLEFDMVGI
DAAIANAFRRILLAEVPTMAVEKVLVYNNTSIVQDEILAHRLGLIPIHADPRLFEYRNQG
DEEGTEIDTLQFRLQVRCTRNPHAAKDSSDPNELYVNHKVYTRHMTWIPLGNQADLFPEG
TIRPVHDDILIAQLRPGQEIDLLMHCVKGIGKDHAKFSPVATASYRLLPDITLLEPVEGE
AAEELSRCFSPGVIEVQEVQGKKVARVANPRLDTFSREIFRNEKLKKVVRLARVRDHYIF
SVESTGVLPPDVLVSEAIKVLMGKCRRFLDELDAVQMD
|
| Enzyme 40 Number of Residues |
338 |
| Enzyme 40 Molecular Weight |
38462 |
| Enzyme 40 Theoretical pI |
5.30 |
| Enzyme 40 GO Classification |
| Function |
- DNA binding
- DNA-directed RNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- protein binding
- protein dimerization 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 40 General Function |
Transcription |
| 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 |
14198113  |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
Q96HT3  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
Q96HT3_HUMAN  |
| Enzyme 40 PDB ID |
Not Available |
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
>1018 bp
GGAAATGCGGAGCCGCGTGGTTCTGGGGGAGTTTGGGGTTCGCAATGTCCATACTACTGA
CTTTCCCGGTAACTATTCCGGTTATGATGATGCCTGGGACCAGGACCGCTTCGAGAAGAA
TTTCCGTGTGGATGTAGTACACATGGATGAAAACTCACTGGAGTTTGACATGGTGGGAAT
TGACGCAGCCATTGCCAATGCTTTTCGACGAATTCTGCTAGCTGAGGTGCCAACTATGGC
TGTGGAGAAGGTCCTGGTGTACAATAATACATCCATTGTTCAGGATGAGATTCTTGCTCA
CCGTCTGGGGCTCATTCCCATTCATGCTGATCCCCGTCTTTTTGAGTATCGGAACCAAGG
AGATGAAGAAGGCACAGAGATAGATACTCTACAGTTTCGTCTCCAGGTCAGATGCACTCG
GAACCCCCATGCTGCTAAAGATTCCTCTGACCCCAACGAACTGTACGTGAACCACAAAGT
GTATACCAGGCATATGACATGGATCCCCCTGGGGAACCAGGCTGATCTCTTTCCAGAGGG
CACTATCCGACCAGTGCATGATGATATCCTCATCGCTCAGCTGCGGCCTGGCCAAGAAAT
TGACCTGCTCATGCACTGTGTCAAGGGCATTGGCAAAGATCATGCCAAGTTTTCACCAGT
GGCAACAGCCAGTTACAGGCTCCTGCCAGACATCACCCTGCTTGAGCCCGTGGAAGGGGA
GGCAGCTGAGGAGTTGAGCAGGTGCTTCTCACCTGGTGTTATTGAGGTGCAGGAAGTCCA
AGGTAAAAAGGTGGCCAGAGTTGCCAACCCCCGGCTGGATACCTTCAGCAGAGAAATCTT
CCGGAATGAGAAGCTAAAGAAGGTTGTGAGGCTTGCCCGGGTTCGAGATCATTATATCTT
CTCTGTTGAGTCAACGGGGGTGTTGCCACCAGATGTGCTGGTGAGTGAAGCCATCAAAGT
ACTGATGGGGAAGTGCCGGCGCTTCTTGGATGAACTAGATGCGGTTCAGATGGACTGA
|
| Enzyme 40 GenBank Gene ID |
BC008118  |
| Enzyme 40 GeneCard ID |
Q96HT3  |
| Enzyme 40 GenAtlas ID |
POLR1C  |
| Enzyme 40 HGNC ID |
HGNC:20194  |
| Enzyme 40 Chromosome Location |
Not Available |
| Enzyme 40 Locus |
Not Available |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
16437 |
| Enzyme 41 Name |
cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b) |
| Enzyme 41 Synonyms |
Not Available |
| Enzyme 41 Gene Name |
ENTPD3 |
| Enzyme 41 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 41 Number of Residues |
529 |
| Enzyme 41 Molecular Weight |
59106 |
| Enzyme 41 Theoretical pI |
6.40 |
| Enzyme 41 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 41 General Function |
Not Available |
| 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 |
B2R8D0  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
B2R8D0_HUMAN  |
| Enzyme 41 PDB ID |
Not Available |
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
Not Available |
| Enzyme 41 GenBank Gene ID |
AK313322  |
| Enzyme 41 GeneCard ID |
B2R8D0  |
| 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 |
16463 |
| Enzyme 42 Name |
cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2) |
| Enzyme 42 Synonyms |
- SubName: cDNA FLJ43358 fis, clone NT2RP7014005, highly similar to CTP synthase 2 (EC 6.3.4.2)
- SubName: CTP synthase II, isoform CRA_a
|
| Enzyme 42 Gene Name |
CTPS2 |
| Enzyme 42 Protein Sequence |
>cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFV
LNDGGEVDLDLGNYERFLDINLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDA
VQEWVMNQAKVPVDGNKEEPQICVIELGGTIGDIEGMPFVEAFRQFQFKAKRENFCNIHV
SLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ
VICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSASNLLFKWRNMADRYERLQKICS
IALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEKITETEDPVKFHEAWQK
LCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCLGMQLAVIEFARNCLNLKDAD
STEFRPNAPVPLVIDMPEHNPGNLGGTMRLGIRRTVFKTENSILRKLYGDVPFIEERHRH
RFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPY
LGLLLAATGNLNAYLQQGCKLSSSDRYSDASDDSFSEPRIAELEIS
|
| Enzyme 42 Number of Residues |
586 |
| Enzyme 42 Molecular Weight |
65678 |
| Enzyme 42 Theoretical pI |
6.91 |
| Enzyme 42 GO Classification |
| Function |
- CTP synthase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
- pyrimidine nucleotide biosynthesis
- pyrimidine nucleotide metabolism
|
| Component |
| — |
|
| Enzyme 42 General Function |
Nucleotide transport and metabolism |
| Enzyme 42 Specific Function |
Not Available |
| Enzyme 42 Pathways |
Not Available |
| Enzyme 42 Reactions |
- ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571] ALL_REAC R00571
- (other) R00573
|
| Enzyme 42 Pfam Domain Function |
|
| Enzyme 42 Signals |
|
| Enzyme 42 Transmembrane Regions |
|
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
Not Available |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
B3KWM2  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
B3KWM2_HUMAN  |
| Enzyme 42 PDB ID |
Not Available |
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
Not Available |
| Enzyme 42 GenBank Gene ID |
AK125332  |
| Enzyme 42 GeneCard ID |
B3KWM2  |
| 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 |
Not Available |
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
16476 |
| Enzyme 43 Name |
cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e) |
| Enzyme 43 Synonyms |
Not Available |
| Enzyme 43 Gene Name |
PKM2 |
| Enzyme 43 Protein Sequence |
>cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVET
LKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIR
TGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGL
ISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMV
FASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIE
IPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIM
LSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEAS
FKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQE
AWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
|
| Enzyme 43 Number of Residues |
531 |
| Enzyme 43 Molecular Weight |
57938 |
| Enzyme 43 Theoretical pI |
7.94 |
| Enzyme 43 GO Classification |
| Function |
- catalytic activity
- kinase activity
- pyruvate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 43 General Function |
Carbohydrate transport and metabolism |
| Enzyme 43 Specific Function |
Not Available |
| Enzyme 43 Pathways |
Not Available |
| Enzyme 43 Reactions |
Not Available |
| Enzyme 43 Pfam Domain Function |
|
| Enzyme 43 Signals |
|
| Enzyme 43 Transmembrane Regions |
|
| Enzyme 43 Essentiality |
Not Available |
| Enzyme 43 GenBank ID Protein |
Not Available |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
B2R5N8  |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
B2R5N8_HUMAN  |
| Enzyme 43 PDB ID |
1F3X  |
| Enzyme 43 PDB File |
Show |
| Enzyme 43 3D Structure |
|
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
Not Available |
| Enzyme 43 GenBank Gene ID |
AK312253  |
| Enzyme 43 GeneCard ID |
B2R5N8  |
| Enzyme 43 GenAtlas ID |
Not Available |
| Enzyme 43 HGNC ID |
Not Available |
| Enzyme 43 Chromosome Location |
15 |
| Enzyme 43 Locus |
15q22 |
| Enzyme 43 SNPs |
SNPJam Report  |
| Enzyme 43 General References |
Not Available |
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
16477 |
| Enzyme 44 Name |
cDNA, FLJ94990, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 1 (CDS1), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 1, isoform CRA_a) |
| Enzyme 44 Synonyms |
Not Available |
| Enzyme 44 Gene Name |
CDS1 |
| Enzyme 44 Protein Sequence |
>cDNA, FLJ94990, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 1 (CDS1), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 1, isoform CRA_a)
MLELRHRGSCPGPREAVSPPHREGEAAGGDHETESTSDKETDIDDRYGDLDSRTDSDIPE
IPPSSDRTPEILKKALSGLSSRWKNWWIRGILTLTMISLFFLIIYMGSFMLMLLVLGIQV
KCFHEIITIGYRVYHSYDLPWFRTLSWYFLLCVNYFFYGETVADYFATFVQREEQLQFLI
RYHRFISFALYLAGFCMFVLSLVKKHYRLQFYMFAWTHVTLLITVTQSHLVIQNLFEGMI
WFLVPISSVICNDITAYLFGFFFGRTPLIKLSPKKTWEGFIGGFFSTVVFGFIAAYVLSK
YQYFVCPVEYRSDVNSFVTECEPSELFQLQTYSLPPFLKAVLRQERVSLYPFQIHSIALS
TFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVHVYITSFIRG
PNPSKVLQQLLVLQPEQQLNIYKTLKTHLIEKGILQPTLKV
|
| Enzyme 44 Number of Residues |
461 |
| Enzyme 44 Molecular Weight |
53305 |
| Enzyme 44 Theoretical pI |
8.19 |
| Enzyme 44 GO Classification |
| Function |
- catalytic activity
- nucleotidyltransferase activity
- phosphatidate cytidylyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular lipid metabolism
- lipid metabolism
- membrane lipid metabolism
- metabolism
- phospholipid biosynthesis
- phospholipid metabolism
- physiological process
- primary metabolism
|
| Component |
|
|
| Enzyme 44 General Function |
Lipid transport and metabolism |
| Enzyme 44 Specific Function |
Not Available |
| Enzyme 44 Pathways |
Not Available |
| Enzyme 44 Reactions |
Not Available |
| Enzyme 44 Pfam Domain Function |
|
| Enzyme 44 Signals |
|
| Enzyme 44 Transmembrane Regions |
|
| Enzyme 44 Essentiality |
Not Available |
| Enzyme 44 GenBank ID Protein |
Not Available |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
B2RAL5  |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
B2RAL5_HUMAN  |
| Enzyme 44 PDB ID |
Not Available |
| Enzyme 44 Cellular Location |
Not Available |
| Enzyme 44 Gene Sequence |
Not Available |
| Enzyme 44 GenBank Gene ID |
AK314245  |
| Enzyme 44 GeneCard ID |
B2RAL5  |
| Enzyme 44 GenAtlas ID |
Not Available |
| Enzyme 44 HGNC ID |
Not Available |
| Enzyme 44 Chromosome Location |
Not Available |
| Enzyme 44 Locus |
Not Available |
| Enzyme 44 SNPs |
SNPJam Report  |
| Enzyme 44 General References |
Not Available |
| Enzyme 44 Metabolite References |
Not Available |
|
Enzyme 45
[top]
|
| Enzyme 45 ID |
16478 |
| Enzyme 45 Name |
cDNA, FLJ96552, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 2 (CDS2), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 2, isoform CRA_a) |
| Enzyme 45 Synonyms |
Not Available |
| Enzyme 45 Gene Name |
CDS2 |
| Enzyme 45 Protein Sequence |
>cDNA, FLJ96552, Homo sapiens CDP-diacylglycerol synthase (phosphatidatecytidylyltransferase) 2 (CDS2), mRNA (CDP-diacylglycerol synthase (Phosphatidate cytidylyltransferase) 2, isoform CRA_a)
MTELRQRVAHEPVAPPEDKESESEAKVDGETASDSESRAESAPLPVSADDTPEVLNRALS
NLSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMIIVMCVQIKCFHEIITIGYNVYHSY
DLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFTLYLIGFCM
FVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAY
MFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSF
TVDCEPSDLFRLQEYNIPGVIQSVIGWKTVRMYPFQIHSIALSTFASLIGPFGGFFASGF
KRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLIQQFLTLRPDQ
QLHIFNTLRSHLIDKGMLTSTTEDE
|
| Enzyme 45 Number of Residues |
445 |
| Enzyme 45 Molecular Weight |
51419 |
| Enzyme 45 Theoretical pI |
7.10 |
| Enzyme 45 GO Classification |
| Function |
- catalytic activity
- nucleotidyltransferase activity
- phosphatidate cytidylyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular lipid metabolism
- lipid metabolism
- membrane lipid metabolism
- metabolism
- phospholipid biosynthesis
- phospholipid metabolism
- physiological process
- primary metabolism
|
| Component |
|
|
| Enzyme 45 General Function |
Lipid transport and metabolism |
| Enzyme 45 Specific Function |
Not Available |
| Enzyme 45 Pathways |
Not Available |
| Enzyme 45 Reactions |
Not Available |
| Enzyme 45 Pfam Domain Function |
|
| Enzyme 45 Signals |
|
| Enzyme 45 Transmembrane Regions |
|
| Enzyme 45 Essentiality |
Not Available |
| Enzyme 45 GenBank ID Protein |
Not Available |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
B2RDC6  |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
B2RDC6_HUMAN  |
| Enzyme 45 PDB ID |
Not Available |
| Enzyme 45 Cellular Location |
Not Available |
| Enzyme 45 Gene Sequence |
Not Available |
| Enzyme 45 GenBank Gene ID |
AK315489  |
| Enzyme 45 GeneCard ID |
B2RDC6  |
| Enzyme 45 GenAtlas ID |
Not Available |
| Enzyme 45 HGNC ID |
Not Available |
| Enzyme 45 Chromosome Location |
20 |
| Enzyme 45 Locus |
20p13 |
| Enzyme 45 SNPs |
SNPJam Report  |
| Enzyme 45 General References |
Not Available |
| Enzyme 45 Metabolite References |
Not Available |
|
Enzyme 46
[top]
|
| Enzyme 46 ID |
17341 |
| Enzyme 46 Name |
RNA-directed RNA polymerase catalytic subunit |
| Enzyme 46 Synonyms |
- Polymerase basic protein 1
- PB1
- RNA-directed RNA polymerase subunit P1
|
| Enzyme 46 Gene Name |
PB1 |
| Enzyme 46 Protein Sequence |
>RNA-directed RNA polymerase catalytic subunit
MDVNPTLLFLKVPAQNAISTTFPYTGDPPYSHGTGTGYTMDTVNRTHQYSEKGKWTTNTE
TGAPQLNPIDGPLPEDNEPSGYAQTDCVLEAMAFLEESHPGIFENSCLETMEVIQQTRVD
KLTQGRQTYDWTLNRNQPAATALANTIEVFRSNGLTANESGRLIDFLKDVIESMDKEEME
ITTHFQRKRRVRDNMTKKMVTQRTIGKKKQRLNKRIYLIRALTLNTMTKDAERGKLKRRA
IATPGMQIRGFVYFVETLARSICENLEQSGLPVGGNEKKAKLANVVRKMMTNSQDTELSF
TITGDNTKWNENQNPRMFLAMITYITRNQPEWFRNVLSIAPIMFSNKMARLGKGYMFKSK
SMKLRTQIPAEMLTSIDLKYFNESTRKKIEKIRPLLIDGTVSLSPGMMMGMFNMLSTVLG
VSILNLGQKKYTKTTYWWDGLQSSDDFALIVNAPNHEGIQAGVDRFYRTCKLVGINMSKK
KSYTNRTGTFEFTSFFYRYGFVANFSMELPSFGVSGINESDDMSIGVTVIKNNMINNDLG
PATAQMALQLFIKDYRYTYRCHRGDTQIQTRRSFELKKLWEQTRSKAGLLISDGGPNLYN
IRNLHIPEVCLKWELMDEDYQGRLCNPLNPFVSHKEIESVNNAVVMPAHGPAKSMEYDAV
ATTHSWIPKRNRSILNTSQRGILEDQQMYQKCCNLFEKFFPSSSYRRPVGISSMVEAMVS
RARIDARIDFESGRIKKEEFAEIMKICSTIEELRRQK
|
| Enzyme 46 Number of Residues |
757 |
| Enzyme 46 Molecular Weight |
86507.6 |
| Enzyme 46 Theoretical pI |
9.68 |
| Enzyme 46 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 46 General Function |
Involved in nucleotide binding |
| Enzyme 46 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 46 Pathways |
Not Available |
| Enzyme 46 Reactions |
Not Available |
| Enzyme 46 Pfam Domain Function |
|
| Enzyme 46 Signals |
|
| Enzyme 46 Transmembrane Regions |
|
| Enzyme 46 Essentiality |
Not Available |
| Enzyme 46 GenBank ID Protein |
324976  |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
P26120  |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
RDRP_I57A2  |
| Enzyme 46 PDB ID |
Not Available |
| Enzyme 46 Cellular Location |
Not Available |
| Enzyme 46 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 46 GenBank Gene ID |
M81580  |
| Enzyme 46 GeneCard ID |
PB1  |
| Enzyme 46 GenAtlas ID |
Not Available |
| Enzyme 46 HGNC ID |
Not Available |
| Enzyme 46 Chromosome Location |
Not Available |
| Enzyme 46 Locus |
Not Available |
| Enzyme 46 SNPs |
SNPJam Report  |
| Enzyme 46 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 46 Metabolite References |
Not Available |
|
Enzyme 47
[top]
|
| Enzyme 47 ID |
17342 |
| Enzyme 47 Name |
Genome polyprotein |
| Enzyme 47 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 47 Gene Name |
Not Available |
| Enzyme 47 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 47 Number of Residues |
3011 |
| Enzyme 47 Molecular Weight |
327142.8 |
| Enzyme 47 Theoretical pI |
8.37 |
| Enzyme 47 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 47 General Function |
Involved in ATP binding |
| Enzyme 47 Specific Function |
NS5B is a RNA-dependent RNA polymerase that plays an essential role in the virus replication |
| Enzyme 47 Pathways |
Not Available |
| Enzyme 47 Reactions |
Not Available |
| Enzyme 47 Pfam Domain Function |
|
| Enzyme 47 Signals |
|
| Enzyme 47 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 47 Essentiality |
Not Available |
| Enzyme 47 GenBank ID Protein |
329738  |
| Enzyme 47 UniProtKB/Swiss-Prot ID |
P27958  |
| Enzyme 47 UniProtKB/Swiss-Prot Entry Name |
POLG_HCVH  |
| Enzyme 47 PDB ID |
1CU1  |
| Enzyme 47 PDB File |
Show |
| Enzyme 47 3D Structure |
|
| Enzyme 47 Cellular Location |
Not Available |
| Enzyme 47 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 47 GenBank Gene ID |
M67463  |
| Enzyme 47 GeneCard ID |
Not Available |
| Enzyme 47 GenAtlas ID |
Not Available |
| Enzyme 47 HGNC ID |
Not Available |
| Enzyme 47 Chromosome Location |
Not Available |
| Enzyme 47 Locus |
Not Available |
| Enzyme 47 SNPs |
Not Available |
| Enzyme 47 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
]
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