|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5338 |
| Enzyme 1 Name |
Nucleoside diphosphate kinase, mitochondrial precursor |
| Enzyme 1 Synonyms |
- NDP kinase, mitochondrial
- NDK
- nm23-H4
- Nucleoside diphosphate kinase D
- NDPKD
|
| Enzyme 1 Gene Name |
NME4 |
| Enzyme 1 Protein Sequence |
>Nucleoside diphosphate kinase, mitochondrial precursor
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
|
| Enzyme 1 Number of Residues |
187 |
| Enzyme 1 Molecular Weight |
20659 |
| Enzyme 1 Theoretical pI |
10.75 |
| Enzyme 1 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 1 General Function |
Nucleotide transport and metabolism |
| Enzyme 1 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
Not Available |
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
1945762  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
O00746  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
NDKM_HUMAN  |
| Enzyme 1 PDB ID |
1EHW  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCA
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
|
| Enzyme 1 GenBank Gene ID |
Y07604  |
| Enzyme 1 GeneCard ID |
NME4  |
| Enzyme 1 GenAtlas ID |
NME4  |
| Enzyme 1 HGNC ID |
HGNC:7852  |
| Enzyme 1 Chromosome Location |
16 |
| Enzyme 1 Locus |
16p13.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 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 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5341 |
| Enzyme 2 Name |
Nucleoside diphosphate kinase A |
| Enzyme 2 Synonyms |
- NDK A
- NDP kinase A
- Tumor metastatic process-associated protein
- Metastasis inhibition factor nm23
- nm23-H1
- Granzyme A-activated DNase
- GAAD
|
| Enzyme 2 Gene Name |
NME1 |
| Enzyme 2 Protein Sequence |
>Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
|
| Enzyme 2 Number of Residues |
152 |
| Enzyme 2 Molecular Weight |
17149 |
| Enzyme 2 Theoretical pI |
6.11 |
| Enzyme 2 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 2 General Function |
Nucleotide transport and metabolism |
| Enzyme 2 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
35068  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P15531  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
NDKA_HUMAN  |
| Enzyme 2 PDB ID |
1JXV  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>543 bp
TGCTGCGAACCACGTGGGTCCCGGGCGCGTTTCGGGTGCTGGCGGCTGCAGCCGGAGTTC
AAACCTAAGCAGCTGGAAGGAACCATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAA
CCAGATGGGGTCCAGCGGGGTCTTGTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGA
TTCCGCCTTGTTGGTCTGAAATTCATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTAC
GTTGACCTGAAGGACCGTCCATTCTTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCG
GTAGTTGCCATGGTCTGGGAGGGGCTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGG
GAGACCAACCCTGCAGACTCCAAGCCTGGGACCATCCGTGGAGACTTCTGCATACAAGTT
GGCAGGAACATTATACATGGCAGTGATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTG
TGGTTTCACCCTGAGGAACTGGTAGATTACACGAGCTGTGCTCAGAACTGGATCTATGAA
TGA
|
| Enzyme 2 GenBank Gene ID |
X17620  |
| Enzyme 2 GeneCard ID |
NME1  |
| Enzyme 2 GenAtlas ID |
NME1  |
| Enzyme 2 HGNC ID |
HGNC:7849  |
| Enzyme 2 Chromosome Location |
17 |
| Enzyme 2 Locus |
17q21.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 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 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5344 |
| Enzyme 3 Name |
Nucleoside diphosphate kinase B |
| Enzyme 3 Synonyms |
- NDK B
- NDP kinase B
- nm23-H2
- C-myc purine-binding transcription factor PUF
|
| Enzyme 3 Gene Name |
NME2 |
| Enzyme 3 Protein Sequence |
>Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
|
| Enzyme 3 Number of Residues |
152 |
| Enzyme 3 Molecular Weight |
17298 |
| Enzyme 3 Theoretical pI |
8.69 |
| 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 |
Acts as a transcriptional activator of the c-Myc gene; binds DNA nonspecifically (Ref.3) |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
4467843  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P22392  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
NDKB_HUMAN  |
| Enzyme 3 PDB ID |
1NSK  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
|
| Enzyme 3 GenBank Gene ID |
X58965  |
| Enzyme 3 GeneCard ID |
NME2  |
| Enzyme 3 GenAtlas ID |
NME2  |
| Enzyme 3 HGNC ID |
HGNC:7850  |
| Enzyme 3 Chromosome Location |
17 |
| Enzyme 3 Locus |
17q21.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 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 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5346 |
| Enzyme 4 Name |
Nucleoside diphosphate kinase 6 |
| Enzyme 4 Synonyms |
- NDK 6
- NDP kinase 6
- nm23-H6
- Inhibitor of p53-induced apoptosis-alpha
- IPIA-alpha
|
| Enzyme 4 Gene Name |
NME6 |
| Enzyme 4 Protein Sequence |
>Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
|
| Enzyme 4 Number of Residues |
186 |
| Enzyme 4 Molecular Weight |
21142 |
| Enzyme 4 Theoretical pI |
8.49 |
| 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. 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 4 Pathways |
|
| Enzyme 4 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
Not Available |
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
3228530  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
O75414  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
NDK6_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
|
| Enzyme 4 GenBank Gene ID |
AF051941  |
| Enzyme 4 GeneCard ID |
NME6  |
| Enzyme 4 GenAtlas ID |
NME6  |
| Enzyme 4 HGNC ID |
HGNC:20567  |
| Enzyme 4 Chromosome Location |
3 |
| Enzyme 4 Locus |
3p21 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 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 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5442 |
| Enzyme 5 Name |
Glucokinase |
| Enzyme 5 Synonyms |
- Hexokinase-4
- Hexokinase type IV
- HK IV
- HK4
- Hexokinase-D
|
| Enzyme 5 Gene Name |
GCK |
| Enzyme 5 Protein Sequence |
>Glucokinase
MLDDRARMEAAKKEKVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPT
YVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQMYSIPEDAMTGTAE
MLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNN
VVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQN
VELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGE
LVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLRPS
TTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFK
ERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKACMLGQ
|
| Enzyme 5 Number of Residues |
465 |
| Enzyme 5 Molecular Weight |
52192 |
| Enzyme 5 Theoretical pI |
4.85 |
| Enzyme 5 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleotide binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleotide binding
- 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 5 General Function |
Not Available |
| Enzyme 5 Specific Function |
Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- ATP + D-glucose = ADP + D-glucose 6-phosphate
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
179427  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P35557  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
HXK4_HUMAN  |
| Enzyme 5 PDB ID |
1V4T  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1398 bp
ATGCTGGACGACAGAGCCAGGATGGAGGCCGCCAAGAAGGAGAAGGTAGAGCAGATCCTG
GCAGAGTTCCAGCTGCAGGAGGAGGACCTGAAGAAGGTGATGAGACGGATGCAGAAGGAG
ATGGACCGCGGCCTGAGGCTGGAGACCCATGAAGAGGCCAGTGTGAAGATGCTGCCCACC
TACGTGCGCTCCACCCCAGAAGGCTCAGAAGTCGGGGACTTCCTCTCCCTGGACCTGGGT
GGCACTAACTTCAGGGTGATGCTGGTGAAGGTGGGAGAAGGTGAGGAGGGGCAGTGGAGC
GTGAAGACCAAACACCAGATGTACTCCATCCCCGAGGACGCCATGACCGGCACTGCTGAG
ATGCTCTTCGACTACATCTCTGAGTGCATCTCCGACTTCCTGGACAAGCATCAGATGAAA
CACAAGAAGCTGCCCCTGGGCTTCACCTTCTCCTTTCCTGTGAGGCACGAAGACATCGAT
AAGGGCATCCTTCTCAACTGGACCAAGGGCTTCAAGGCCTCAGGAGCAGAAGGGAACAAT
GTCGTGGGGCTTCTGCGAGACGCTATCAAACGGAGAGGGGACTTTGAAATGGATGTGGTG
GCAATGGTGAATGACACGGTGGCCACGATGATCTCCTGCTACTACGAAGACCATCAGTGC
GAGGTCGGCATGATCGTGGGCACGGGCTGCAATGCCTGCTACATGGAGGAGATGCAGAAT
GTGGAGCTGGTGGAGGGGGACGAGGGCCGCATGTGCGTCAATACCGAGTGGGGCGCCTTC
GGGGACTCCGGCGAGCTGGACGAGTTCCTGCTGGAGTATGACCGCCTGGTGGACGAGAGC
TCTGCAAACCCCGGTCAGCAGCTGTATGAGAAGCTCATAGGTGGCAAGTACATGGGCGAG
CTGGTGCGGCTTGTGCTGCTCAGGCTCGTGGACGAAAACCTGCTCTTCCACGGGGAGGCC
TCCGAGCAGCTGCGCACACGCGGAGCCTTCGAGACGCGCTTCGTGTCGCAGGTGGAGAGC
GACACGGGCGACCGCAAGCAGATCTACAACATCCTGAGCACGCTGGGGCTGCGACCCTCG
ACCACCGACTGCGACATCGTGCGCCGCGCCTGCGAGAGCGTGTCTACGCGCGCTGCGCAC
ATGTGCTCGGCGGGGCTGGCGGGCGTCATCAACCGCATGCGCGAGAGCCGCAGCGAGGAC
GTAATGCGCATCACTGTGGGCGTGGATGGCTCCGTGTACAAGCTGCACCCCAGCTTCAAG
GAGCGGTTCCATGCCAGCGTGCGCAGGCTGACGCCCAGCTGCGAGATCACCTTCATCGAG
TCGGAGGAGGGCAGTGGCCGGGGCGCGGCCCTGGTCTCGGCGGTGGCCTGTAAGAAGGCC
TGTATGCTGGGCCAGTGA
|
| Enzyme 5 GenBank Gene ID |
M88011  |
| Enzyme 5 GeneCard ID |
GCK  |
| Enzyme 5 GenAtlas ID |
GCK  |
| Enzyme 5 HGNC ID |
HGNC:4195  |
| Enzyme 5 Chromosome Location |
7 |
| Enzyme 5 Locus |
7p15.3-p15.1 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Tanizawa Y, Matsutani A, Chiu KC, Permutt MA: Human glucokinase gene: isolation, structural characterization, and identification of a microsatellite repeat polymorphism. Mol Endocrinol. 1992 Jul;6(7):1070-81. [PubMed
]
- Tanizawa Y, Koranyi LI, Welling CM, Permutt MA: Human liver glucokinase gene: cloning and sequence determination of two alternatively spliced cDNAs. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7294-7. [PubMed
]
- Nishi S, Stoffel M, Xiang K, Shows TB, Bell GI, Takeda J: Human pancreatic beta-cell glucokinase: cDNA sequence and localization of the polymorphic gene to chromosome 7, band p 13. Diabetologia. 1992 Aug;35(8):743-7. [PubMed
]
- Koranyi LI, Tanizawa Y, Welling CM, Rabin DU, Permutt MA: Human islet glucokinase gene. Isolation and sequence analysis of full-length cDNA. Diabetes. 1992 Jul;41(7):807-11. [PubMed
]
- Stoffel M, Froguel P, Takeda J, Zouali H, Vionnet N, Nishi S, Weber IT, Harrison RW, Pilkis SJ, Lesage S, et al.: Human glucokinase gene: isolation, characterization, and identification of two missense mutations linked to early-onset non-insulin-dependent (type 2) diabetes mellitus. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7698-702. [PubMed
]
- Sakura H, Eto K, Kadowaki H, Simokawa K, Ueno H, Koda N, Fukushima Y, Akanuma Y, Yazaki Y, Kadowaki T: Structure of the human glucokinase gene and identification of a missense mutation in a Japanese patient with early-onset non-insulin-dependent diabetes mellitus. J Clin Endocrinol Metab. 1992 Dec;75(6):1571-3. [PubMed
]
- St Charles R, Harrison RW, Bell GI, Pilkis SJ, Weber IT: Molecular model of human beta-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B. Diabetes. 1994 Jun;43(6):784-91. [PubMed
]
- Stoffel M, Patel P, Lo YM, Hattersley AT, Lucassen AM, Page R, Bell JI, Bell GI, Turner RC, Wainscoat JS: Missense glucokinase mutation in maturity-onset diabetes of the young and mutation screening in late-onset diabetes. Nat Genet. 1992 Oct;2(2):153-6. [PubMed
]
- Chiu KC, Tanizawa Y, Permutt MA: Glucokinase gene variants in the common form of NIDDM. Diabetes. 1993 Apr;42(4):579-82. [PubMed
]
- Stoffel M, Bell KL, Blackburn CL, Powell KL, Seo TS, Takeda J, Vionnet N, Xiang KS, Gidh-Jain M, Pilkis SJ, et al.: Identification of glucokinase mutations in subjects with gestational diabetes mellitus. Diabetes. 1993 Jun;42(6):937-40. [PubMed
]
- Takeda J, Gidh-Jain M, Xu LZ, Froguel P, Velho G, Vaxillaire M, Cohen D, Shimada F, Makino H, Nishi S, et al.: Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants. J Biol Chem. 1993 Jul 15;268(20):15200-4. [PubMed
]
- Gidh-Jain M, Takeda J, Xu LZ, Lange AJ, Vionnet N, Stoffel M, Froguel P, Velho G, Sun F, Cohen D, et al.: Glucokinase mutations associated with non-insulin-dependent (type 2) diabetes mellitus have decreased enzymatic activity: implications for structure/function relationships. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1932-6. [PubMed
]
- Hager J, Blanche H, Sun F, Vaxillaire NV, Poller W, Cohen D, Czernichow P, Velho G, Robert JJ, Cohen N, et al.: Six mutations in the glucokinase gene identified in MODY by using a nonradioactive sensitive screening technique. Diabetes. 1994 May;43(5):730-3. [PubMed
]
- Velho G, Blanche H, Vaxillaire M, Bellanne-Chantelot C, Pardini VC, Timsit J, Passa P, Deschamps I, Robert JJ, Weber IT, Marotta D, Pilkis SJ, Lipkind GM, Bell GI, Froguel P: Identification of 14 new glucokinase mutations and description of the clinical profile of 42 MODY-2 families. Diabetologia. 1997 Feb;40(2):217-24. [PubMed
]
- Hattersley AT, Beards F, Ballantyne E, Appleton M, Harvey R, Ellard S: Mutations in the glucokinase gene of the fetus result in reduced birth weight. Nat Genet. 1998 Jul;19(3):268-70. [PubMed
]
- Glaser B, Kesavan P, Heyman M, Davis E, Cuesta A, Buchs A, Stanley CA, Thornton PS, Permutt MA, Matschinsky FM, Herold KC: Familial hyperinsulinism caused by an activating glucokinase mutation. N Engl J Med. 1998 Jan 22;338(4):226-30. [PubMed
]
- Ng MC, Cockburn BN, Lindner TH, Yeung VT, Chow CC, So WY, Li JK, Lo YM, Lee ZS, Cockram CS, Critchley JA, Bell GI, Chan JC: Molecular genetics of diabetes mellitus in Chinese subjects: identification of mutations in glucokinase and hepatocyte nuclear factor-1alpha genes in patients with early-onset type 2 diabetes mellitus/MODY. Diabet Med. 1999 Nov;16(11):956-63. [PubMed
]
- Nam JH, Lee HC, Kim YH, Cha BS, Song YD, Lim SK, Kim KR, Huh KB: Identification of glucokinase mutation in subjects with post-renal transplantation diabetes mellitus. Diabetes Res Clin Pract. 2000 Dec;50(3):169-76. [PubMed
]
- Njolstad PR, Sovik O, Cuesta-Munoz A, Bjorkhaug L, Massa O, Barbetti F, Undlien DE, Shiota C, Magnuson MA, Molven A, Matschinsky FM, Bell GI: Neonatal diabetes mellitus due to complete glucokinase deficiency. N Engl J Med. 2001 May 24;344(21):1588-92. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5444 |
| Enzyme 6 Name |
Hexokinase-3 |
| Enzyme 6 Synonyms |
- Hexokinase type III
- HK III
|
| Enzyme 6 Gene Name |
HK3 |
| Enzyme 6 Protein Sequence |
>Hexokinase-3
MDSIGSSGLRQGEETLSCSEEGLPGPSDSSELVQECLQQFKVTRAQLQQIQASLLGSMEQ
ALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP
RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRST
LISWTKGFRCSGVEGQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVG
LVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSLSDDGALGPVLTTFDHTLDHESLN
PGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST
GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQ
VAVATGGRVCERHPRFCSVLQGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARLAAHR
RLLEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLA
LDLGGTNFRVLLVRVTTGVQITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQ
SLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREAITRRQAVELNVVAI
VNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGD
DGSLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQ
RLQTRDIFKTKFLSEIESDSLALRQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLC
GAGVAAVVEKIRGNRGLEELAVSVGVDGTLYKLHPRFSSLVAATVRELAPRCVVTFLQSE
DGSGKGAALVTAVACRLAQLTRV
|
| Enzyme 6 Number of Residues |
923 |
| Enzyme 6 Molecular Weight |
98921 |
| Enzyme 6 Theoretical pI |
5.11 |
| Enzyme 6 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleotide binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleotide binding
- 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 6 General Function |
Not Available |
| Enzyme 6 Specific Function |
ATP + D-hexose = ADP + D-hexose 6-phosphate |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- ATP + D-hexose = ADP + D-hexose 6-phosphate
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
1255788  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P52790  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
HXK3_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>2772 bp
ATGGACTCCATTGGGTCTTCAGGGTTGCGGCAGGGGGAAGAAACCCTGAGTTGCTCTGAG
GAGGGCTTGCCCGGGCCCTCAGACAGCTCAGAGCTGGTGCAGGAGTGCCTGCAGCAGTTC
AAGGTGACAAGGGCACAGCTACAGCAGATCCAAGCCAGCCTCTTGGGTTCCATGGAGCAG
GCGCTGAGGGGACAGGCCAGCCCTGCCCCTGCGGTCCGGATGCTGCCTACATACGTGGGG
TCCACCCCACATGGCACTGAGCAAGGAGACTTCGTGGTGCTGGAGCTGGGGGCCACAGGG
GCCTCACTGCGTGTTTTGTGGGTGACTCTAACTGGCATTGAGGGGCATAGGGTGGAGCCC
AGAAGCCAGGAGTTTGTGATCCCCCAAGAGGTGATGCTGGGTGCTGGCCAGCAGCTCTTT
GACTTTGCTGCCCACTGCCTGTCTGAGTTCCTGGATGCGCAGCCTGTGAACAAACAGGGT
CTGCAGCTTGGCTTCAGCTTCTCTTTCCCTTGTCACCAGACGGGCTTGGACAGGAGCACC
CTCATTTCCTGGACCAAAGGTTTTAGGTGCAGTGGTGTGGAAGGCCAGGATGTGGTCCAG
CTGCTGAGAGATGCCATTCGGAGGCAGGGGGCCTACAACATCGACGTGGTTGCTGTGGTG
AACGACACAGTGGGCACCATGATGGGCTGTGAGCCGGGGGTCAGGCCGTGTGAGGTTGGG
CTAGTTGTAGACACGGGCACCAACGCGTGTTACATGGAGGAGGCACGGCATGTGGCAGTG
CTGGACGAAGACCGGGGCCGCGTCTGCGTCAGCGTCGAGTGGGGCTCCTTAAGCGATGAT
GGGGCGCTGGGACCAGTGCTGACCACCTTCGACCATACCCTGGACCATGAGTCCCTGAAT
CCTGGTGCTCAGAGGTTTGAGAAGATGATCGGAGGCCTGTACCTGGGTGAGCTGGTGCGG
CTGGTGCTGGCTCACTTGGCCCGGTGTGGGGTCCTCTTTGGTGGCTGCACCTCCCCTGCC
CTGCTGAGCCAAGGCAGCATCCTCCTGGAACACGTGGCTGAGATGGAGGACCCCTCTACT
GGGGCAGCCCGTGTCCATGCTATCCTGCAGGACTTGGGCCTGAGCCCTGGGGCTTCGGAT
GTTGAGCTTGTGCAGCACGTCTGTGCGGCCGTGTGCACGCGGGCTGCCCAGCTCTGTGCT
GCCGCCCTGGCCGCTGTTCTCTCCTGCCTCCAGCACAGCCGGGAGCAACAAACACTCCAG
GTTGCTGTGGCCACCGGAGGCCGAGTGTGTGAGCGGCACCCCAGGTTCTGCAGCGTCCTG
CAGGGGACAGTGATGCTCCTGGCCCCGGAATGCGATGTCTCCTTAATCCCCTCTGTGGAT
GGTGGTGGCCGGGGAGTGGCGATGGTGACTGCTGTGGCTGCCCGTCTGGCTGCCCACCGG
CGCCTGCTGGAGGAGACCCTGGCCCCATTCCGGTTGAACCATGATCAACTGGCTGCGGTT
CAGGCACAGATGCGGAAGGCCATGGCCAAGGGGCTCCGAGGGGAGGCCTCCTCCCTTCGC
ATGCTGCCCACTTTCGTCCGGGCCACCCCTGACGGCAGCGAGCGAGGGGATTTCCTGGCC
CTGGACCTCGGGGGCACGAACTTCCGTGTCCTCCTGGTACGTGTGACCACAGGCGTGCAG
ATCACCAGCGAGATCTACTCCATTCCCGAGACTGTGGCCCAGGGTTCTGGGCAGCAGCTC
TTTGACCACATCGTGGACTGCATCGTGGACTTCCAGCAGAAGCAGGGCCTGAGCGGGCAG
AGCCTCCCACTGGGTTTTACCTTCTCCTTCCCATGTAGGCAGCTTGGCCTAGACCAGGGC
ATCCTCCTGAACTGGACCAAGGGTTTCAAGGCATCAGACTGCGAGGGCCAAGATGTCGTG
AGTCTGTTGCGGGAAGCCATCACTCGCAGACAGGCAGTGGAGCTGAATGTGGTTGCCATT
GTCAATGACACGGTGGGGACCATGATGTCCTGTGGCTATGAGGACCCCCGTTGCGAGATA
GGCCTCATTGTCGGAACCGGCACCAATGCCTGCTACATGGAGGAGCTCCGGAATGTGGCG
GGCGTGCCTGGGGACTCAGGCCGCATGTGCATCAACATGGAGTGGGGCGCCTTTGGGGAC
GATGGCTCTCTGGCCATGCTCAGCACCCGCTTTGATGCAAGTGTGGACCAGGCGTCCATC
AACCCCGGCAAGCAGAGGTTTGAAAAGATGATCAGCGGCATGTACCTGGGGGAGATCGTC
CGCCACATCCTTTTACATTTAACCAGCCTTGGCGTTCTCTTCCGGGGCCAGCAGATCCAG
CGCCTTCAGACCAGGGACATCTTCAAGACCAAGTTCCTCTCTGAGATCGAAAGTGACAGC
CTGGCCCTGCGGCAGGTCCGAGCCATCCTAGAGGATCTGGGGCTACCCCTGACCTCAGAT
GACGCCCTGATGGTGCTAGAGGTGTGCCAGGCTGTGTCCCAGAGGGCTGCCCAGCTCTGT
GGGGCGGGTGTAGCTGCCGTGGTGGAGAAGATCCGGGGGAACCGGGGCCTGGAAGAGCTG
GCAGTGTCTGTGGGGGTGGATGGAACGCTCTACAAGCTGCACCCGCGCTTCTCCAGCCTG
GTGGCGGCCACAGTGCGGGAGCTGGCCCCTCGCTGTGTGGTCACGTTCCTGCAGTCAGAG
GATGGGTCCGGCAAAGGTGCGGCCCTGGTCACCGCTGTTGCCTGCCGCCTTGCGCAGTTG
ACTCGTGTCTGA
|
| Enzyme 6 GenBank Gene ID |
U51333  |
| Enzyme 6 GeneCard ID |
HK3  |
| Enzyme 6 GenAtlas ID |
HK3  |
| Enzyme 6 HGNC ID |
HGNC:4925  |
| Enzyme 6 Chromosome Location |
5 |
| Enzyme 6 Locus |
5q35.2 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Furuta H, Nishi S, Le Beau MM, Fernald AA, Yano H, Bell GI: Sequence of human hexokinase III cDNA and assignment of the human hexokinase III gene (HK3) to chromosome band 5q35.2 by fluorescence in situ hybridization. Genomics. 1996 Aug 15;36(1):206-9. [PubMed
]
- Palma F, Agostini D, Mason P, Dacha M, Piccoli G, Biagiarelli B, Fiorani M, Stocchi V: Purification and characterization of the carboxyl-domain of human hexokinase type III expressed as fusion protein. Mol Cell Biochem. 1996 Feb 9;155(1):23-9. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5445 |
| Enzyme 7 Name |
Hexokinase-2 |
| Enzyme 7 Synonyms |
- Hexokinase type II
- HK II
- Muscle form hexokinase
|
| Enzyme 7 Gene Name |
HK2 |
| Enzyme 7 Protein Sequence |
>Hexokinase-2
MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAA
VKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMR
GSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGV
EGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYME
EMRHIDMVEGDEGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGM
YMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLG
LDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKH
PHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLEHLQLS
HDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRV
LLVRVRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGF
TFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVG
TMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDD
FRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRG
IFETKFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAA
VVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKG
AALITAVACRIREAGQR
|
| Enzyme 7 Number of Residues |
917 |
| Enzyme 7 Molecular Weight |
102381 |
| Enzyme 7 Theoretical pI |
5.93 |
| Enzyme 7 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleotide binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleotide binding
- 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 7 General Function |
Not Available |
| Enzyme 7 Specific Function |
ATP + D-hexose = ADP + D-hexose 6-phosphate |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- ATP + D-hexose = ADP + D-hexose 6-phosphate
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
587202  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P52789  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
HXK2_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>2754 bp
ATGATTGCCTCGCATCTGCTTGCCTACTTCTTCACGGAGCTCAACCATGACCAAGTGCAG
AAGGTTGACCAGTATCTCTACCACATGCGCCTCTCTGATGAGACCCTCTTGGAGATCTCT
AAGCGGTTCCGCAAGGAGATGGAGAAAGGGCTTGGAGCCACCACTCACCCTACTGCAGCA
GTGAAGATGCTGCCCACCTTTGTGAGGTCCACTCCAGATGGGACAGAACACGGAGAGTTC
CTGGCTCTGGATCTTGGAGGGACCAACTTCCGTGTGCTTTGGGTGAAAGTAACGGACAAT
GGGCTCCAGAAGGTGGAGATGGAGAATCAGATCTATGCCATCCCTGAGGACATCATGCGA
GGCAGTGGCACCCAGCTGTTTGACCACATTGCCGAATGCCTGGCTAACTTCATGGATAAG
CTACAAATCAAAGACAAGAAGCTCCCACTGGGTTTTACCTTCTCGTTCCCCTGCCACCAG
ACTAAACTAGACGAGAGTTTCCTGGTCTCATGGACCAAGGGATTCAAGTCCAGTGGAGTG
GAAGGCAGAGACGTTGTGGCTCTGATCCGGAAGGCCATCCAGAGGAGAGGGGACTTTGAT
ATCGACATTGTGGCTGTGGTGAATGACACAGTTGGGACCATGATGACCTGTGGTTATGAT
GACCACAACTGTGAGATTGGTCTCATTGTGGGCACGGGCAGCAACGCCTGCTACATGGAA
GAGATGCGCCACATCGACATGGTGGAAGGCGATGAGGGGCGGATGTGTATCAATATGGAG
TGGGGGGCCTTCGGGGACGATGGCTCGCTCAACGACATTCGCACTGAGTTTGACCAGGAG
ATTGACATGGGCTCACTGAACCCGGGAAAGCAACTGTTTGAGAAGATGATCAGTGGGATG
TACATGGGGGAGCTGGTGAGGCTTATCCTGGTGAAGATGGCCAAGGAGGAGCTGCTCTTT
GGGGGGAAGCTCAGCCCAGAGCTTCTCAACACCGGTCGCTTTGAGACCAAAGACATCTCA
GACATTGAAGGGGAGAAGGATGGCATCCGGAAGGCCCGTGAGGTCCTGATGCGGTTGGGC
CTGGACCCGACTCAGGAGGACTGCGTGGCCACTCACCGGATCTGCCAGATCGTGTCCACA
CGCTCCGCCAGCCTGTGCGCAGCCACCCTGGCCGCCGTGCTGCAGCGCATCAAGGAGAAC
AAAGGCGAGGAGCGGCTGCGCTCTACTATTGGGGTCGACGGTTCCGTCTACAAGAAACAC
CCCCATTTTGCCAAGCGTCTACATAAGACCGTGCGGCGGCTGGTGCCCGGCTGCGATGTC
CGCTTCCTCCGCTCCGAGGATGGCAGTGGCAAAGGTGCAGCCATGGTGACAGCAGTGGCT
TACCGGCTGGCCGATCAACACCGTGCCCGCCAGAAGACATTAGAGCATCTGCAGCTGAGC
CATGACCAGCTGCTGGAGGTCAAGAGGAGGATGAAGGTAGAAATGGAGCGAGGTCTGAGC
AAGGAGACTCATGCCAGTGCCCCCGTCAAGATGCTGCCCACCTACGTGTGTGCTACCCCG
GACGGCACAGAGAAAGGGGACTTCTTGGCCTTGGACCTTGGAGGAACAAATTTCCGGGTC
CTGCTGGTCCGTGTTCGGAATGGGAAGTGGGGTGGAGTGGAGATGCACAACAAGATCTAC
GCCATCCCGCAGGAGGTCATGCACGGCACCGGGGACGAGCTCTTTGACCACATTGTCCAG
TGCATCGCGGACTTCCTCGAGTACATGGGCATGAAGGGCGTGTCCCTGCCTCTGGGTTTT
ACCTTCTCCTTCCCCTGCCAGCAGAACAGCCTGGACGAGAGCATCCTCCTCAAGTGGACA
AAAGGCTTCAAGGCATCTGGCTGCGAGGGCGAGGACGTGGTGACCCTGCTGAAGGAAGCG
ATCCACCGGCGAGAGGAGTTTGACCTGGATGTGGTTGCTGTGGTGAACGACACAGTCGGA
ACTATGATGACCTGTGGCTTTGAAGACCCTCACTGTGAAGTTGGCCTCATTGTTGGCACG
GGCAGCAATGCCTGCTACATGGAGGAGATGCGCAACGTGGAACTGGTGGAAGGAGAAGAG
GGGCGGATGTGTGTGAACATGGAATGGGGGGCCTTCGGGGACAATGGATGCCTAGATGAC
TTCCGCACAGAATTTGATGTGGCTGTGGATGAGCTTTCACTCAACCCCGGCAAGCAGAGG
TTCGAGAAAATGATCAGTGGAATGTACCTGGGTGAGATTGTCCGTAACATTCTCATCGAT
TTCACCAAGCGTGGACTACTCTTCCGAGGCCGCATCTCAGAGCGGCTCAAGACAAGGGGC
ATCTTTGAAACCAAGTTCTTGTCTCAGATTGAGAGTGACTGCCTGGCCCTGCTGCAAGTC
CGAGCCACCCTGCAACACTTAGGGCTTGAGAGCACCTGTGACGACAGCATCATTGTTAAG
GAGGTGTGCACTGTGGTGGCCCGGCGGGCAGCCCAGCTCTGTGGCGCAGGCATGGCCGCT
GTGGTGGACAGGATACGAGAAAACCGTGGGCTGGACGCTCTCAAAGTGACAGTGGGTGTG
GATGGGACCCTCTACAAGCTACATCCTCACTTTGCCAAAGTCATGCATGAGACAGTGAAG
GACCTGGCTCCGAAATGTGATGTGTCTTTCCTGCAGTCAGAGGATGGCAGCGGGAAGGGG
GCGGCGCTCATCACTGCTGTGGCCTGCCGCATCCGTGAGGCTGGACAGCGATAG
|
| Enzyme 7 GenBank Gene ID |
Z46376  |
| Enzyme 7 GeneCard ID |
HK2  |
| Enzyme 7 GenAtlas ID |
HK2  |
| Enzyme 7 HGNC ID |
HGNC:4923  |
| Enzyme 7 Chromosome Location |
2 |
| Enzyme 7 Locus |
2p13 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Lehto M, Huang X, Davis EM, Le Beau MM, Laurila E, Eriksson KF, Bell GI, Groop L: Human hexokinase II gene: exon-intron organization, mutation screening in NIDDM, and its relationship to muscle hexokinase activity. Diabetologia. 1995 Dec;38(12):1466-74. [PubMed
]
- Deeb SS, Malkki M, Laakso M: Human hexokinase II: sequence and homology to other hexokinases. Biochem Biophys Res Commun. 1993 Nov 30;197(1):68-74. [PubMed
]
- Shinohara Y, Yamamoto K, Kogure K, Ichihara J, Terada H: Steady state transcript levels of the type II hexokinase and type 1 glucose transporter in human tumor cell lines. Cancer Lett. 1994 Jul 15;82(1):27-32. [PubMed
]
- Laakso M, Malkki M, Deeb SS: Amino acid substitutions in hexokinase II among patients with NIDDM. Diabetes. 1995 Mar;44(3):330-4. [PubMed
]
- Vidal-Puig A, Printz RL, Stratton IM, Granner DK, Moller DE: Analysis of the hexokinase II gene in subjects with insulin resistance and NIDDM and detection of a Gln142-->His substitution. Diabetes. 1995 Mar;44(3):340-6. [PubMed
]
- Echwald SM, Bjorbaek C, Hansen T, Clausen JO, Vestergaard H, Zierath JR, Printz RL, Granner DK, Pedersen O: Identification of four amino acid substitutions in hexokinase II and studies of relationships to NIDDM, glucose effectiveness, and insulin sensitivity. Diabetes. 1995 Mar;44(3):347-53. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6041 |
| Enzyme 8 Name |
Pyruvate kinase isozymes R/L |
| Enzyme 8 Synonyms |
- R-type/L-type pyruvate kinase
- Red cell/liver pyruvate kinase
- Pyruvate kinase 1
|
| Enzyme 8 Gene Name |
PKLR |
| Enzyme 8 Protein Sequence |
>Pyruvate kinase isozymes R/L
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQ
LPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFS
HGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKG
SQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQV
ENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKM
QHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS
AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
|
| Enzyme 8 Number of Residues |
574 |
| Enzyme 8 Molecular Weight |
61831 |
| Enzyme 8 Theoretical pI |
7.83 |
| Enzyme 8 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 8 General Function |
Carbohydrate transport and metabolism |
| Enzyme 8 Specific Function |
ATP + pyruvate = ADP + phosphoenolpyruvate |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- ATP + pyruvate = ADP + phosphoenolpyruvate
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
3327365  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P30613  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
KPYR_HUMAN  |
| Enzyme 8 PDB ID |
1LIU  |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 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 8 GenBank Gene ID |
AB015983  |
| Enzyme 8 GeneCard ID |
PKLR  |
| Enzyme 8 GenAtlas ID |
PKLR  |
| Enzyme 8 HGNC ID |
HGNC:9020  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
1q21 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 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 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
6238 |
| Enzyme 9 Name |
DNA polymerase beta |
| Enzyme 9 Synonyms |
Not Available |
| Enzyme 9 Gene Name |
POLB |
| Enzyme 9 Protein Sequence |
>DNA polymerase beta
MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAK
KLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIK
TLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGS
FRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQ
LPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRP
LGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE
|
| Enzyme 9 Number of Residues |
335 |
| Enzyme 9 Molecular Weight |
38178 |
| Enzyme 9 Theoretical pI |
9.41 |
| Enzyme 9 GO Classification |
| Function |
- DNA binding
- DNA-directed DNA polymerase activity
- beta DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA repair
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
|
|
| Enzyme 9 General Function |
Replication, recombination and repair |
| Enzyme 9 Specific Function |
Repair polymerase. Conducts "gap-filling" DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. Has a 5'-deoxyribose-5- phosphate lyase (dRP lyase) activity |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 9 Pfam Domain Function |
Not Available |
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
292397  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P06746  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
DPOLB_HUMAN  |
| Enzyme 9 PDB ID |
8ICK  |
| Enzyme 9 PDB File |
Show |
| Enzyme 9 3D Structure |
|
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1008 bp
ATGAGCAAACGGAAGGCGCCGCAGGAGACTCTCAACGGGGGAATCACCGACATGCTCACA
GAACTCGCAAACTTTGAGAAGAACGTGAGCCAAGCTATCCACAAGTACAATGCTTACAGA
AAAGCAGCATCTGTTATAGCAAAATACCCACACAAAATAAAGAGTGGAGCTGAAGCTAAG
AAATTGCCTGGAGTAGGAACAAAAATTGCTGAAAAGATTGATGAGTTTTTAGCAACTGGA
AAATTACGTAAACTGGAAAAGATTCGGCAGGATGATACGAGTTCATCCATCAATTTCCTG
ACTCGAGTTAGTGGCATTGGTCCATCTGCTGCAAGGAAGTTTGTAGATGAAGGAATTAAA
ACACTAGAAGATCTCAGAAAAAATGAAGATAAATTGAACCATCATCAGCGAATTGGGCTG
AAATATTTTGGGGACTTTGAAAAAAGAATTCCTCGTGAAGAGATGTTACAAATGCAAGAT
ATTGTACTAAATGAAGTTAAAAAAGTGGATTCTGAATACATTGCTACAGTCTGTGGCAGT
TTCAGAAGAGGTGCAGAGTCCAGTGGTGACATGGATGTTCTCCTGACCCATCCCAGCTTC
ACTTCAGAATCAACCAAACAGCCAAAACTGTTACATCAGGTTGTGGAGCAGTTACAAAAG
GTTCATTTTATCACAGATACCCTGTCAAAGGGTGAGACAAAGTTCATGGGTGTTTGCCAG
CTTCCCAGTAAAAATGATGAAAAAGAATATCCACACAGAAGAATTGATATCAGGTTGATA
CCCAAAGATCAGTATTACTGTGGTGTTCTCTATTTCACTGGGAGTGATATTTTCAATAAG
AATATGAGGGCTCATGCCCTAGAAAAGGGTTTCACAATCAATGAGTACACCATCCGTCCC
TTGGGAGTCACTGGAGTTGCAGGAGAACCCCTGCCAGTGGATAGTGAAAAAGACATCTTT
GATTACATCCAGTGGAAATACCGGGAACCCAAGGACCGGAGCGAATGA
|
| Enzyme 9 GenBank Gene ID |
L11607  |
| Enzyme 9 GeneCard ID |
POLB  |
| Enzyme 9 GenAtlas ID |
POLB  |
| Enzyme 9 HGNC ID |
HGNC:9174  |
| Enzyme 9 Chromosome Location |
8 |
| Enzyme 9 Locus |
8p11.2 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Chyan YJ, Ackerman S, Shepherd NS, McBride OW, Widen SG, Wilson SH, Wood TG: The human DNA polymerase beta gene structure. Evidence of alternative splicing in gene expression. Nucleic Acids Res. 1994 Jul 25;22(14):2719-25. [PubMed
]
- SenGupta DN, Zmudzka BZ, Kumar P, Cobianchi F, Skowronski J, Wilson SH: Sequence of human DNA polymerase beta mRNA obtained through cDNA cloning. Biochem Biophys Res Commun. 1986 Apr 14;136(1):341-7. [PubMed
]
- Abbotts J, SenGupta DN, Zmudzka B, Widen SG, Notario V, Wilson SH: Expression of human DNA polymerase beta in Escherichia coli and characterization of the recombinant enzyme. Biochemistry. 1988 Feb 9;27(3):901-9. [PubMed
]
- Widen SG, Kedar P, Wilson SH: Human beta-polymerase gene. Structure of the 5'-flanking region and active promoter. J Biol Chem. 1988 Nov 15;263(32):16992-8. [PubMed
]
- Matsumoto Y, Kim K, Katz DS, Feng JA: Catalytic center of DNA polymerase beta for excision of deoxyribose phosphate groups. Biochemistry. 1998 May 5;37(18):6456-64. [PubMed
]
- DeMott MS, Beyret E, Wong D, Bales BC, Hwang JT, Greenberg MM, Demple B: Covalent trapping of human DNA polymerase beta by the oxidative DNA lesion 2-deoxyribonolactone. J Biol Chem. 2002 Mar 8;277(10):7637-40. Epub 2002 Jan 22. [PubMed
]
- Pelletier H, Sawaya MR, Wolfle W, Wilson SH, Kraut J: A structural basis for metal ion mutagenicity and nucleotide selectivity in human DNA polymerase beta. Biochemistry. 1996 Oct 1;35(39):12762-77. [PubMed
]
- Pelletier H, Sawaya MR: Characterization of the metal ion binding helix-hairpin-helix motifs in human DNA polymerase beta by X-ray structural analysis. Biochemistry. 1996 Oct 1;35(39):12778-87. [PubMed
]
- Sawaya MR, Prasad R, Wilson SH, Kraut J, Pelletier H: Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: evidence for an induced fit mechanism. Biochemistry. 1997 Sep 16;36(37):11205-15. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6239 |
| Enzyme 10 Name |
DNA polymerase alpha catalytic subunit |
| Enzyme 10 Synonyms |
Not Available |
| Enzyme 10 Gene Name |
POLA1 |
| Enzyme 10 Protein Sequence |
>DNA polymerase alpha catalytic subunit
MAPVHGDDSLSDSGSFVSSRARREKKSKKGRQEALERLKKAKAGEKYKYEVEDFTGVYEE
VDEEQYSKLVQARQDDDWIVDDDGIGYVEDGREIFDDDLEDDALDADEKGKDGKARNKDK
RNVKKLAVTKPNNIKSMFIACAGKKTADKAVDLSKDGLLGDILQDLNTETPQITPPPVMI
LKKKRSIGASPNPFSVHTATAVPSGKIASPVSRKEPPLTPVPLKRAEFAGDDVQVESTEE
EQESGAMEFEDGDFDEPMEVEEVDLEPMAAKAWDKESEPAEEVKQEADSGKGTVSYLGSF
LPDVSCWDIDQEGDSSFSVQEVQVDSSHLPLVKGADEEQVFHFYWLDAYEDQYNQPGVVF
LFGKVWIESAETHVSCCVMVKNIERTLYFLPREMKIDLNTGKETGTPISMKDVYEEFDEK
IATKYKIMKFKSKPVEKNYAFEIPDVPEKSEYLEVKYSAEMPQLPQDLKGETFSHVFGTN
TSSLELFLMNRKIKGPCWLEVKSPQLLNQPVSWCKVEAMALKPDLVNVIKDVSPPPLVVM
AFSMKTMQNAKNHQNEIIAMAALVHHSFALDKAAPKPPFQSHFCVVSKPKDCIFPYAFKE
VIEKKNVKVEVAATERTLLGFFLAKVHKIDPDIIVGHNIYGFELEVLLQRINVCKAPHWS
KIGRLKRSNMPKLGGRSGFGERNATCGRMICDVEISAKELIRCKSYHLSELVQQILKTER
VVIPMENIQNMYSESSQLLYLLEHTWKDAKFILQIMCELNVLPLALQITNIAGNIMSRTL
MGGRSERNEFLLLHAFYENNYIVPDKQIFRKPQQKLGDEDEEIDGDTNKYKKGRKKAAYA
GGLVLDPKVGFYDKFILLLDFNSLYPSIIQEFNICFTTVQRVASEAQKVTEDGEQEQIPE
LPDPSLEMGILPREIRKLVERRKQVKQLMKQQDLNPDLILQYDIRQKALKLTANSMYGCL
GFSYSRFYAKPLAALVTYKGREILMHTKEMVQKMNLEVIYGDTDSIMINTNSTNLEEVFK
LGNKVKSEVNKLYKLLEIDIDGVFKSLLLLKKKKYAALVVEPTSDGNYVTKQELKGLDIV
RRDWCDLAKDTGNFVIGQILSDQSRDTIVENIQKRLIEIGENVLNGSVPVSQFEINKALT
KDPQDYPDKKSLPHVHVALWINSQGGRKVKAGDTVSYVICQDGSNLTASQRAYAPEQLQK
QDNLTIDTQYYLAQQIHPVVARICEPIDGIDAVLIATWLGLDPTQFRVHHYHKDEENDAL
LGGPAQLTDEEKYRDCERFKCPCPTCGTENIYDNVFDGSGTDMEPSLYRCSNIDCKASPL
TFTVQLSNKLIMDIRRFIKKYYDGWLICEEPTCRNRTRHLPLQFSRTGPLCPACMKATLQ
PEYSDKSLYTQLCFYRYIFDAECALEKLTTDHEKDKLKKQFFTPKVLQDYRKLKNTAEQF
LSRSGYSEVNLSKLFAGCAVKS
|
| Enzyme 10 Number of Residues |
1462 |
| Enzyme 10 Molecular Weight |
165914 |
| Enzyme 10 Theoretical pI |
5.59 |
| Enzyme 10 GO Classification |
| Function |
- 3'-5' exonuclease activity
- DNA binding
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- exonuclease activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- nuclease activity
- nucleic acid binding
- nucleotide binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 10 General Function |
Replication, recombination and repair |
| Enzyme 10 Specific Function |
Polymerase alpha in a complex with DNA primase is a replicative polymerase |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
35568  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P09884  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
DPOLA_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>4389 bp
ATGGCACCTGTGCACGGCGACGACTCTCTGTCAGATTCAGGGAGTTTTGTATCTTCTCGA
GCCCGGCGAGAAAAAAAATCAAAGAAGGGGCGCCAAGAAGCCCTAGAAAGACTGAAAAAG
GCTAAAGCTGGTGAGAAGTATAAATATGAAGTCGAGGACTTCACAGGTGTTTATGAAGAA
GTTGATGAAGAACAGTATTCGAAGCTGGTTCAGGCACGCCAGGATGATGACTGGATTGTG
GATGATGATGGTATTGGCTATGTGGAAGATGGCCGAGAGATTTTTGATGATGACCTTGAA
GATGATGCCCTTGATGCTGATGAGAAAGGAAAAGATGGTAAAGCACGCAATAAAGACAAG
AGGAATGTAAAGAAGCTCGCAGTGACAAAACCGAACAACATTAAGTCAATGTTCATTGCT
TGTGCTGGAAAGAAAACTGCAGATAAAGCTGTAGACTTGTCCAAGGATGGTCTGCTAGGT
GACATTCTACAGGATCTTAACACTGAGACACCTCAAATAACTCCACCACCTGTAATGATA
CTGAAGAAGAAAAGATCCATTGGAGCTTCACCGAATCCTTTCTCTGTGCACACCGCCACG
GCAGTTCCTTCAGGAAAAATTGCTTCCCCTGTCTCCAGAAAGGAGCCTCCATTAACTCCT
GTTCCTCTTAAACGTGCTGAATTTGCTGGCGATGATGTACAGGTCGAGAGTACAGAAGAA
GAGCAGGAGTCAGGGGCAATGGAGTTTGAAGATGGTGACTTTGATGAGCCCATGGAAGTT
GAAGAGGTGGACCTGGAGCCTATGGCTGCCAAGGCTTGGGACAAAGAGAGTGAGCCAGCA
GAGGAAGTGAAACAAGAGGCGGATTCTGGGAAAGGGACCGTGTCCTACTTAGGAAGTTTT
CTCCCGGATGTCTCTTGTTGGGACATTGATCAAGAAGGTGATAGCAGTTTCTCAGTGCAA
GAAGTTCAAGTGGATTCCAGTCACCTCCCATTGGTAAAAGGGGCAGATGAGGAACAAGTA
TTCCACTTTTATTGGTTGGATGCTTATGAGGATCAGTACAACCAACCAGGTGTGGTATTT
CTGTTTGGGAAAGTTTGGATTGAATCAGCCGAGACCCATGTGAGCTGTTGTGTCATGGTG
AAAAATATCGAGCGAACGCTTTACTTCCTTCCCCGTGAAATGAAAATTGATCTAAATACG
GGGAAAGAAACAGGAACTCCAATTTCAATGAAGGATGTTTATGAGGAATTTGATGAGAAA
ATAGCAACAAAATATAAAATTATGAAGTTCAAGTCTAAGCCAGTGGAAAAGAACTATGCT
TTTGAGATACCTGATGTTCCAGAAAAATCTGAGTACTTGGAAGTTAAATACTCGGCTGAA
ATGCCACAGCTTCCTCAAGATTTGAAAGGAGAAACTTTTTCTCATGTATTTGGGACCAAC
ACATCTAGCCTGGAACTGTTCTTGATGAACAGAAAGATCAAAGGACCTTGTTGGCTTGAA
GTAAAAAAGTCCACAGCTCTTAATCAGCCAGTCAGTTGGTGTAAAGTTGAGGCAATGGCT
TTGAAACCAGACCTGGTGAATGTAATTAAGGATGTCAGTCCACCACCGCTTGTCGTGATG
GCTTTCAGCATGAAGACAATGCAGAATGCAAAGAACCATCAAAATGAGATTATTGCTATG
GCAGCTTTGGTCCATCACAGTTTTGCATTGGATAAAGCAGCCCCAAAGCCTCCCTTTCAG
TCACACTTCTGTGTTGTGTCTAAACCAAAGGACTGTATTTTTCCATATGCTTTCAAAGAA
GTCATTGAGAAAAAGAATGTGAAGGTTGAGGTTGCTGCAACAGAAAGAACACTGCTAGGT
TTTTTCCTTGCAAAAGTTCACAAAATTGATCCTGATATCATTGTGGGTCATAATATTTAT
GGGTTTGAACTGGAAGTACTACTGCAGAGAATTAATGTGTGCAAAGCTCCTCACTGGTCC
AAGATAGGTCGACTGAAGCGATCCAACATGCCAAAGCTTGGGGGCCGGAGTGGATTTGGT
GAAAGAAATGCTACCTGTGGTCGAATGATCTGTGATGTGGAAATTTCAGCAAAGGAATTG
ATTCGTTGTAAAAGCTACCATCTGTCTGAACTTGTTCAGCAGATTCTAAAAACTGAAAGG
GTTGTAATCCCAATGGAAAATATACAAAATATGTACAGTGAATCTTCTCAACTGTTATAC
CTGTTGGAACACACCTGGAAAGATGCCAAGTTCATTTTGCAGATCATGTGTGAGCTAAAT
GTTCTTCCATTAGCATTGCAGATCACTAACATCGCTGGGAACATTATGTCCAGGACGCTG
ATGGGTGGACGATCCGAGCGTAACGAGTTCTTGTTGCTTCATGCATTTTACGAAAACAAC
TATATTGTGCCTGACAAGCAGATTTTCAGAAAGCCTCAGCAAAAACTGGGAGATGAAGAT
GAAGAAATTGATGGAGATACCAATAAATACAAGAAAGGACGTAAGAAAGGAGCTTATGCT
GGAGGCTTGGTTTTGGACCCCAAAGTTGGTTTTTATGATAAGTTCATTTTGCTTCTGGAC
TTCAACAGTCTATATCCTTCCATCATTCAGGAATTTAACATTTGTTTTACAACAGTACAA
AGAGTTGCTTCAGAGGCACAGAAAGTTACAGAGGATGGAGAACAAGAACAGATCCCTGAG
TTGCCAGATCCAAGCTTAGAAATGGGCATTTTGCCCAGAGAGATCCGGAAACTGGTAGAA
CGGAGAAAACAAGTCAAACAGCTAATGAAACAGCAAGACTTAAATCCAGACCTTATTCTT
CAGTATGACATTCGACAGAAGGCTTTGAAGCTCACAGCGAACAGTATGTATGGTTGCCTG
GGATTTTCCTATAGCAGATTTTACGCCAAACCACTGGCTGCCTTGGTGACATACAAAGGA
AGGGAGATTTTGATGCATACGAAAGAGATGGTACAAAAGATGAATCTTGAAGTTATTTAT
GGAGATACAGATTCAATTATGATAAACACCAATAGCACCAATCTGGAAGAAGTATTTAAG
TTGGGAAACAAGGTAAAAAGTGAAGTGAATAAGTTGTACAAACTGCTTGAAATAGACATT
GATGGGGTTTTCAAGTCTCTGCTACTGCTGAAAAAAAAGAAGTACGCTGCTCTGGTTGTT
GAGCCAACGTCGGATGGGAATTATGTCACCAAACAGGAGCTCAAAGGATTAGATATAGTT
AGAAGAGATTGGTGTGATCTTGCTAAAGACACTGGAAACTTTGTGATTGGCCAGATTCTT
TCTGATCAAAGCCGGGACACTATAGTGGAAAACATTCAGAAGAGGCTGATAGAAATTGGA
GAAAATGTGCTAAATGGCAGTGTCCCAGTGAGCCAGTTTGAAATTAACAAGGCATTGACA
AAGGATCCCCAGGATTACCCTGATAAAAAAAGCCTACCTCATGTACATGTTGCCCTCTGG
ATAAATTCTCAAGGAGGCAGAAAGGTGAAAGCTGGAGATACTGTGTCATATGTCATCTGT
CAGGATGGATCAAACCTCACTGCAAGTCAGAGGGCCTATGCGCCTGAGCAGCTGCAGAAA
CAGGATAATCTAACCATTGACACCCAGTACTACCTGGCCCAGCAGATCCACCCAGTCGTG
GCTCGGATCTGTGAACCAATAGACGGAATTGATGCTGTCCTCATTGCAACGTGGTTGGGA
CTTGACCCCACCCAATTTAGAGTTCATCATTATCATAAAGATGAAGAGAATGATGCTCTA
CTTGGTGGCCCAGCACAGCTCACTGATGAAGAGAAATACAGGGACTGTGAAAGATTCAAA
TGTCCATGCCCTACATGTGGAACTGAGAATATTTATGATAATGTCTTTGATGGTTCGGGA
ACAGATATGGAGCCCAGCTTGTATCGTTGCAGTAACATCGATTGTAAGGCTTCACCTCTG
ACCTTTACAGTACAACTGAGCAACAAATTGATCATGGACATTAGACGTTTCATTAAAAAG
TACTATGATGGCTGGTTGATATGTGAAGAGCCAACCTGTCGCAATCGAACTCGTCACCTT
CCCCTTCAATTCTCCCGAACTGGGCCTCTTTGCCCAGCCTGCATGAAAGCTACACTTCAA
CCAGAGTATTCTGACAAGTCCCTGTACACCCAGCTGTGCTTTTACCGGTACATTTTTGAT
GCGGAGTGTGCACTGGAGAAACTTACTACCGATCATGAGAAAGATAAATTGAAGAAGCAA
TTTTTTACCCCCAAAGTTCTGCAGGACTACAGAAAACTCAAGAACACAGCAGAGCAATTC
TTGTCCCGAAGTGGCTACTCCGAAGTGAATCTGAGCAAACTCTTCGCTGGTTGTGCCGTG
AAATCCTAA
|
| Enzyme 10 GenBank Gene ID |
X06745  |
| Enzyme 10 GeneCard ID |
POLA1  |
| Enzyme 10 GenAtlas ID |
POLA1  |
| Enzyme 10 HGNC ID |
HGNC:9173  |
| Enzyme 10 Chromosome Location |
X |
| Enzyme 10 Locus |
Xp22.1-p21.3 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Wong SW, Wahl AF, Yuan PM, Arai N, Pearson BE, Arai K, Korn D, Hunkapiller MW, Wang TS: Human DNA polymerase alpha gene expression is cell proliferation dependent and its primary structure is similar to both prokaryotic and eukaryotic replicative DNA polymerases. EMBO J. 1988 Jan;7(1):37-47. [PubMed
]
- Pearson BE, Nasheuer HP, Wang TS: Human DNA polymerase alpha gene: sequences controlling expression in cycling and serum-stimulated cells. Mol Cell Biol. 1991 Apr;11(4):2081-95. [PubMed
]
- Hsi KL, Copeland WC, Wang TS: Human DNA polymerase alpha catalytic polypeptide binds ConA and RCA and contains a specific labile site in the N-terminus. Nucleic Acids Res. 1990 Nov 11;18(21):6231-7. [PubMed
]
- Evanics F, Maurmann L, Yang WW, Bose RN: Nuclear magnetic resonance structures of the zinc finger domain of human DNA polymerase-alpha. Biochim Biophys Acta. 2003 Sep 23;1651(1-2):163-71. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6240 |
| Enzyme 11 Name |
DNA polymerase subunit delta 3 |
| Enzyme 11 Synonyms |
- DNA polymerase subunit delta p66
|
| Enzyme 11 Gene Name |
POLD3 |
| Enzyme 11 Protein Sequence |
>DNA polymerase subunit delta 3
MADQLYLENIDEFVTDQNKIVTYKWLSYTLGVHVNQAKQMLYDYVERKRKENSGAQLHVT
YLVSGSLIQNGHSCHKVAVVREDKLEAVKSKLAVTASIHVYSIQKAMLKDSGPLFNTDYD
ILKSNLQNCSKFSAIQCAAAVPRAPAESSSSSKKFEQSHLHMSSETQANNELTTNGHGPP
ASKQVSQQPKGIMGMFASKAAAKTQETNKETKTEAKEVTNASAAGNKAPGKGNMMSNFFG
KAAMNKFKVNLDSEQAVKEEKIVEQPTVSVTEPKLATPAGLKKSSKKAEPVKVLQKEKKR
GKRVALSDDETKETENMRKKRRRIKLPESDSSEDEVFPDSPGAYEAESPSPPPPPSPPLE
PVPKTEPEPPSVKSSSGENKRKRKRVLKSKTYLDGEGCIVTEKVYESESCTDSEEELNMK
TSSVHRPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK
|
| Enzyme 11 Number of Residues |
466 |
| Enzyme 11 Molecular Weight |
51401 |
| Enzyme 11 Theoretical pI |
9.96 |
| Enzyme 11 GO Classification |
Not Available |
| Enzyme 11 General Function |
Not Available |
| Enzyme 11 Specific Function |
The function of subunit 3 is not clear |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
Not Available |
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
436222  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q15054  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
DPOD3_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1476 bp
AGACGTTTCCCGCCGGCGGGAGCTGTGGCTGTGATTGAGAGAGGGGTTAGAGGCGGGTCC
CAGCGCTGCCGCACCATGGCGGACCAGCTTTATCTGGAAAATATAGACGAGTTCGTCACG
GACCAAAACAAGATCGTGACATACAAATGGCTGAGCTATACACTAGGGGTTCATGTTAAC
CAGGCCAAACAGATGCTGTATGATTATGTTGAAAGGAAACGAAAAGAAAATTCAGGAGCC
CAACTGCATGTTACCTACTTGGTGTCTGGCAGTCTCATTCAGAATGGACATTCCTGCCAC
AAGGTTGCAGTAGTGAGAGAAGATAAATTGGAAGCAGTGAAGTCCAAGCTAGCTGTGACT
GCCAGCATCCATGTGTACAGCATCCAGAAAGCCATGCTAAAGGACAGTGGGCCTCTGTTC
AATACTGACTATGACATCCTTAAAAGCAACTTGCAGAACTGCAGCAAATTTAGTGCTATA
CAATGTGCAGCTGCCGTCCCTAGAGCTCCTGCTGAATCCTCTTCGTCTTCCAAAAAGTTT
GAGCAGTCACATCTTCACATGTCAAGTGAGACACAAGCCAACAATGAGCTGACCACCAAT
GGTCATGGCCCACCTGCATCCAAGCAGGTTTCCCAGCAGCCCAAAGGAATTATGGGAATG
TTTGCCTCCAAAGCTGCTGCTAAAACCCAAGAAACCAACAAGGAAACGAAAACAGAGGCT
AAAGAAGTAACAAATGCATCTGCAGCAGGCAACAAGGCACCAGGGAAAGGGAATATGATG
AGCAACTTTTTTGGAAAAGCTGCTATGAATAAATTTAAAGTCAATTTGGACTCAGAACAA
GCAGTGAAAGAAGAAAAAATAGTGGAGCAGCCTACAGTGTCTGTCACGGAACCAAAGCTG
GCAACTCCTGCAGGCCTGAAAAAATCCAGCAAAAAAGCAGAGCCTGTTAAGGTGCTGCAG
AAGGAAAAAAAAAGGGGGAAGCGAGTAGCATTATCTGATGATGAGACAAAGGAAACTGAA
AACATGAGGAAAAAGAGGAGAAGAATCAAACTTCCTGAATCTGATAGCAGTGAAGATGAA
GTCTTTCCAGACTCTCCTGGGGCTTATGAAGCTGAGTCACCATCCCCACCTCCTCCTCCG
TCTCCACCTCTTGAACCAGTGCCAAAGACTGAGCCTGAACCTCCTTCTGTCAAGAGCTCA
AGTGGAGAAAACAAAAGAAAACGAAAACGCGTACTAAAATCTAAAACTTACCTGGATGGG
GAAGGCTGCATAGTGACTGAAAAAGTCTACGAGAGTGAATCCTGCACAGATAGTGAAGAG
GAGCTTAACATGAAGACATCCTCAGTACACAGACCCCCTGCCATGACTGTGAAAAAAGAA
CCCAGAGAGGAACGAAAGGGCCCCAAGAAAGGGACTGCTGCTCTGGGCAAAGCCAACAGA
CAGGTGTCCATTACTGGCTTCTTCCAGAGGAAATAA
|
| Enzyme 11 GenBank Gene ID |
D26018  |
| Enzyme 11 GeneCard ID |
POLD3  |
| Enzyme 11 GenAtlas ID |
POLD3  |
| Enzyme 11 HGNC ID |
HGNC:20932  |
| Enzyme 11 Chromosome Location |
11 |
| Enzyme 11 Locus |
11q14 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed
]
- Hughes P, Tratner I, Ducoux M, Piard K, Baldacci G: Isolation and identification of the third subunit of mammalian DNA polymerase delta by PCNA-affinity chromatography of mouse FM3A cell extracts. Nucleic Acids Res. 1999 May 15;27(10):2108-14. [PubMed
]
- Mo J, Liu L, Leon A, Mazloum N, Lee MY: Evidence that DNA polymerase delta isolated by immunoaffinity chromatography exhibits high-molecular weight characteristics and is associated with the KIAA0039 protein and RPA. Biochemistry. 2000 Jun 20;39(24):7245-54. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6243 |
| Enzyme 12 Name |
DNA polymerase lambda |
| Enzyme 12 Synonyms |
- Pol Lambda
- DNA polymerase kappa
- DNA polymerase beta-2
- Pol beta2
|
| Enzyme 12 Gene Name |
POLL |
| Enzyme 12 Protein Sequence |
>DNA polymerase lambda
MDPRGILKAFPKRQKIHADASSKVLAKIPRREEGEEAEEWLSSLRAHVVRTGIGRARAEL
FEKQIVQHGGQLCPAQGPGVTHIVVDEGMDYERALRLLRLPQLPPGAQLVKSAWLSLCLQ
ERRLVDVAGFSIFIPSRYLDHPQPSKAEQDASIPPGTHEALLQTALSPPPPPTRPVSPPQ
KAKEAPNTQAQPISDDEASDGEETQVSAADLEALISGHYPTSLEGDCEPSPAPAVLDKWV
CAQPSSQKATNHNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSFHKPVTSYQEAC
SIPGIGKRMAEKIIEILESGHLRKLDHISESVPVLELFSNIWGAGTKTAQMWYQQGFRSL
EDIRSQASLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGLLCVACGSYRR
GKATCGDVDVLITHPDGRSHRGIFSRLLDSLRQEGFLTDDLVSQEENGQQQKYLGVCRLP
GPGRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTAVVRNT
HGCKVGPGRVLPTPTEKDVFRLLGLPYREPAERDW
|
| Enzyme 12 Number of Residues |
575 |
| Enzyme 12 Molecular Weight |
63483 |
| Enzyme 12 Theoretical pI |
7.94 |
| Enzyme 12 GO Classification |
| Function |
- DNA binding
- DNA-directed DNA polymerase activity
- beta DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA repair
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
|
|
| Enzyme 12 General Function |
Replication, recombination and repair |
| Enzyme 12 Specific Function |
Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 12 Pfam Domain Function |
Not Available |
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
6687796  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q9UGP5  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
DPOLL_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1728 bp
ATGGATCCCAGGGGTATCTTGAAGGCATTTCCCAAGCGGCAGAAAATTCATGCTGATGCA
TCATCAAAAGTACTTGCAAAGATTCCTAGGAGGGAAGAGGGAGAAGAAGCAGAAGAGTGG
CTGAGCTCCCTTCGGGCCCATGTTGTGCGCACTGGCATTGGACGAGCCCGGGCAGAACTC
TTTGAGAAGCAGATTGTTCAGCATGGCGGCCAGCTATGCCCTGCCCAGGGCCCAGGTGTC
ACTCACATTGTGGTGGATGAAGGCATGGACTATGAGCGAGCCCTCCGCCTTCTCAGACTA
CCCCAGCTGCCCCCGGGTGCTCAGCTGGTGAAGTCAGCCTGGCTGAGCTTGTGCCTTCAG
GAGAGGAGGCTGGTGGATGTAGCTGGATTCAGCATCTTCATCCCCAGTAGGTACTTGGAC
CATCCACAGCCCAGCAAGGCAGAGCAGGATGCTTCTATTCCTCCTGGCACCCATGAGGCC
CTGCTTCAGACAGCCCTTTCTCCTCCTCCTCCTCCCACCAGGCCTGTGTCTCCTCCCCAA
AAGGCAAAAGAGGCACCAAACACCCAAGCCCAGCCCATCTCTGATGATGAAGCCAGTGAT
GGGGAAGAAACCCAGGTTAGTGCAGCTGATCTGGAAGCCCTCATCAGTGGCCACTACCCC
ACCTCCCTTGAGGGAGATTGTGAGCCTAGCCCAGCCCCTGCTGTCCTGGATAAGTGGGTC
TGTGCACAGCCCTCAAGCCAGAAGGCGACCAATCACAACCTCCATATCACAGAGAAGCTG
GAAGTTCTGGCCAAAGCCTACAGTGTTCAGGGAGACAAGTGGAGGGCCCTGGGCTATGCC
AAGGCCATCAATGCCCTCAAGAGCTTCCATAAGCCTGTCACCTCGTACCAGGAGGCCTGC
AGTATCCCTGGGATTGGGAAGCGGATGGCTGAGAAAATCATAGAGATCCTGGAGAGCGGG
CATTTGCGGAAGCTGGACCATATCAGTGAGAGCGTGCCTGTCTTGGAGCTCTTCTCCAAC
ATCTGGGGAGCTGGGACCAAGACTGCCCAGATGTGGTACCAACAGGGCTTCCGAAGTCTG
GAAGACATCCGCAGCCAGGCCTCCCTGACAACCCAGCAGGCCATCGGCCTGAAGCATTAC
AGTGACTTCCTGGAACGTATGCCCAGGGAGGAGGCTACAGAGATTGAGCAGACAGTCCAG
AAAGCAGCCCAGGCCTTTAACTCTGGGCTGCTGTGTGTGGCATGTGGTTCATACCGACGG
GGAAAGGCGACCTGTGGTGATGTCGACGTGCTCATCACTCACCCAGATGGCCGGTCCCAC
CGGGGTATCTTCAGCCGCCTCCTTGACAGTCTTCGGCAGGAAGGGTTCCTCACAGATGAC
TTGGTGAGCCAAGAGGAGAATGGTCAGCAACAGAAGTACTTGGGGGTGTGCCGGCTCCCA
GGGCCAGGGCGGCGGCACCGGCGCCTGGACATCATCGTGGTGCCCTATAGCGAGTTTGCC
TGTGCCCTGCTCTACTTCACCGGCTCTGCACACTTCAACCGCTCCATGCGAGCCCTGGCC
AAAACCAAGGGCATGAGTCTGTCAGAACATGCCCTCAGCACTGCTGTGGTCCGGAACACC
CATGGCTGCAAGGTGGGGCCTGGCCGAGTGCTGCCCACTCCCACTGAGAAGGATGTCTTC
AGGCTCTTAGGCCTCCCCTACCGAGAACCTGCTGAGCGGGACTGGTGA
|
| Enzyme 12 GenBank Gene ID |
AJ131890  |
| Enzyme 12 GeneCard ID |
POLL  |
| Enzyme 12 GenAtlas ID |
POLL  |
| Enzyme 12 HGNC ID |
HGNC:9184  |
| Enzyme 12 Chromosome Location |
10 |
| Enzyme 12 Locus |
10q23 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Aoufouchi S, Flatter E, Dahan A, Faili A, Bertocci B, Storck S, Delbos F, Cocea L, Gupta N, Weill JC, Reynaud CA: Two novel human and mouse DNA polymerases of the polX family. Nucleic Acids Res. 2000 Sep 15;28(18):3684-93. [PubMed
]
- Nagasawa K, Kitamura K, Yasui A, Nimura Y, Ikeda K, Hirai M, Matsukage A, Nakanishi M: Identification and characterization of human DNA polymerase beta 2, a DNA polymerase beta -related enzyme. J Biol Chem. 2000 Oct 6;275(40):31233-8. [PubMed
]
- Garcia-Diaz M, Bebenek K, Kunkel TA, Blanco L: Identification of an intrinsic 5'-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair. J Biol Chem. 2001 Sep 14;276(37):34659-63. Epub 2001 Jul 16. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6244 |
| Enzyme 13 Name |
DNA polymerase epsilon subunit 4 |
| Enzyme 13 Synonyms |
- DNA polymerase II subunit 4
- DNA polymerase epsilon subunit p12
|
| Enzyme 13 Gene Name |
POLE4 |
| Enzyme 13 Protein Sequence |
>DNA polymerase epsilon subunit 4
MAAAAAAGSGTPREEEGPAGEAAASQPQAPTSVPGARLSRLPLARVKALVKADPDVTLAG
QEAIFILARAAELFVETIAKDAYCCAQQGKRKTLQRRDLDNAIEAVDEFAFLEGTLD
|
| Enzyme 13 Number of Residues |
117 |
| Enzyme 13 Molecular Weight |
12209 |
| Enzyme 13 Theoretical pI |
4.55 |
| Enzyme 13 GO Classification |
| Function |
- DNA binding
- binding
- nucleic acid binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 13 General Function |
Not Available |
| Enzyme 13 Specific Function |
May play a role in allowing polymerase epsilon to carry out its replication and/or repair function |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
9623361  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q9NR33  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
DPOE4_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>354 bp
ATGGCGGCGGCGGCGGCGGCAGGAAGCGGGACGCCCCGAGAGGAGGAGGTACCTGCTGGG
GAGGCAGCGGCCTCGCAGCCCCAGGCCCCAACGAGTGTGCCTGGGGCTCGTCTCTCGAGG
TTGCCTCTGGCGCGAGTGAAGGCCTTGGTGAAGGCAGATCCCGACGTGACGCTAGCGGGA
CAGGAAGCCATCTTCATTCTGGCACGAGCCGCGGAACTGTTTGTGGAGACCATTGCAAAA
GATGCCTACTGTTGCGCTCAGCAGGGAAAAAGGAAAACCCTTCAGAGGAGAGACTTGGAT
AATGCAATAGAAGCTGTGGATGAATTTGCTTTTCTGGAAGGTACTTTAGATTGA
|
| Enzyme 13 GenBank Gene ID |
AF261688  |
| Enzyme 13 GeneCard ID |
POLE4  |
| Enzyme 13 GenAtlas ID |
POLE4  |
| Enzyme 13 HGNC ID |
HGNC:18755  |
| Enzyme 13 Chromosome Location |
2 |
| Enzyme 13 Locus |
2p12 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Li Y, Pursell ZF, Linn S: Identification and cloning of two histone fold motif-containing subunits of HeLa DNA polymerase epsilon. J Biol Chem. 2000 Jul 28;275(30):23247-52. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
6245 |
| Enzyme 14 Name |
DNA polymerase eta |
| Enzyme 14 Synonyms |
- RAD30 homolog A
- Xeroderma pigmentosum variant type protein
|
| Enzyme 14 Gene Name |
POLH |
| Enzyme 14 Protein Sequence |
>DNA polymerase eta
MATGQDRVVALVDMDCFFVQVEQRQNPHLRNKPCAVVQYKSWKGGGIIAVSYEARAFGVT
RSMWADDAKKLCPDLLLAQVRESRGKANLTKYREASVEVMEIMSRFAVIERASIDEAYVD
LTSAVQERLQKLQGQPISADLLPSTYIEGLPQGPTTAEETVQKEGMRKQGLFQWLDSLQI
DNLTSPDLQLTVGAVIVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSH
GSVPQLFSQMPIRKIRSLGGKLGASVIEILGIEYMGELTQFTESQLQSHFGEKNGSWLYA
MCRGIEHDPVKPRQLPKTIGCSKNFPGKTALATREQVQWWLLQLAQELEERLTKDRNDND
RVATQLVVSIRVQGDKRLSSLRRCCALTRYDAHKMSHDAFTVIKNCNTSGIQTEWSPPLT
MLFLCATKFSASAPSSSTDITSFLSSDPSSLPKVPVTSSEAKTQGSGPAVTATKKATTSL
ESFFQKAAERQKVKEASLSSLTAPTQAPMSNSPSKPSLPFQTSQSTGTEPFFKQKSLLLK
QKQLNNSSVSSPQQNPWSNCKALPNSLPTEYPGCVPVCEGVSKLEESSKATPAEMDLAHN
SQSMHASSASKSVLEVTQKATPNPSLLAAEDQVPCEKCGSLVPVWDMPEHMDYHFALELQ
KSFLQPHSSNPQVVSAVSHQGKRNPKSPLACTNKRPRPEGMQTLESFFKPLTH
|
| Enzyme 14 Number of Residues |
713 |
| Enzyme 14 Molecular Weight |
78414 |
| Enzyme 14 Theoretical pI |
8.56 |
| Enzyme 14 GO Classification |
| Function |
| — |
| Process |
- DNA metabolism
- DNA repair
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Replication, recombination and repair |
| Enzyme 14 Specific Function |
DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Targets POLI to replication foci |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
5138988  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q9Y253  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
POLH_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>2142 bp
ATGGCTACTGGACAGGATCGAGTGGTTGCTCTCGTGGACATGGACTGTTTTTTTGTTCAA
GTGGAGCAGCGGCAAAATCCTCATTTGAGGAATAAACCTTGTGCAGTTGTACAGTACAAA
TCATGGAAGGGTGGTGGAATAATTGCAGTGAGTTATGAAGCTCGTGCATTTGGAGTCACT
AGAAGTATGTGGGCAGATGATGCTAAGAAGTTATGTCCAGATCTTCTACTGGCACAAGTT
CGTGAGTCCCGTGGGAAAGCTAACCTCACCAAGTACCGGGAAGCCAGTGTTGAAGTGATG
GAGATAATGTCTCGTTTTGCTGTGATTGAACGTGCCAGCATTGATGAGGCTTACGTAGAT
CTGACCAGTGCTGTACAAGAGAGACTACAAAAGCTACAAGGTCAGCCTATCTCGGCAGAC
TTGTTGCCAAGCACTTACATTGAAGGGTTGCCCCAAGGCCCTACAACGGCAGAAGAGACT
GTTCAGAAAGAGGGGATGCGAAAACAAGGCTTATTTCAATGGCTCGATTCTCTTCAGATT
GATAACCTCACCTCTCCAGACCTGCAGCTCACCGTGGGAGCAGTGATTGTGGAGGAAATG
AGAGCAGCCATAGAGAGGGAGACTGGTTTTCAGTGTTCAGCTGGAATTTCACACAATAAG
GTCCTGGCAAAACTGGCCTGTGGACTAAACAAGCCCAACCGCCAAACCCTGGTTTCACAT
GGGTCAGTCCCACAGCTCTTCAGCCAAATGCCCATTCGCAAAATCCGTAGTCTTGGAGGA
AAGCTAGGGGCCTCTGTCATTGAGATCCTAGGGATAGAATACATGGGTGAACTGACCCAG
TTCACTGAATCCCAGCTCCAGAGTCATTTTGGGGAGAAGAATGGGTCTTGGCTATATGCC
ATGTGCCGAGGGATTGAACATGATCCAGTTAAACCCAGGCAACTACCCAAAACCATTGGC
TGTAGTAAGAACTTCCCAGGAAAAACAGCTCTTGCTACTCGGGAACAGGTACAATGGTGG
CTGTTGCAATTAGCCCAGGAACTAGAGGAGAGACTGACTAAAGACCGAAATGATAATGAC
AGGGTAGCCACCCAGCTGGTTGTGAGCATTCGTGTACAAGGAGACAAACGCCTCAGCAGC
CTGCGCCGCTGCTGTGCCCTTACCCGCTATGATGCTCACAAGATGAGCCATGATGCATTT
ACTGTCATCAAGAACTGTAATACTTCTGGAATCCAGACAGAATGGTCTCCTCCTCTCACA
ATGCTTTTCCTCTGTGCTACAAAATTTTCTGCCTCTGCCCCTTCATCTTCTACAGACATC
ACCAGCTTCTTGAGCAGTGACCCAAGTTCTCTGCCAAAGGTGCCAGTTACCAGCTCAGAA
GCTAAGACCCAGGGAAGTGGCCCAGCGGTGACAGCCACTAAGAAAGCAACCACGTCTCTG
GAATCATTCTTCCAAAAAGCTGCAGAAAGGCAGAAAGTTAAAGAAGCTTCGCTTTCATCT
CTTACTGCTCCCACTCAGGCTCCCATGAGCAATTCACCATCCAAGCCCTCATTACCTTTT
CAAACCAGTCAAAGTACAGGAACTGAGCCCTTCTTTAAGCAGAAAAGTCTGCTTCTAAAG
CAGAAACAGCTTAATAATTCTTCAGTTTCTTCCCCCCAACAAAACCCATGGTCCAACTGT
AAAGCATTACCAAACTCTTTACCAACAGAGTATCCAGGGTGTGTCCCTGTTTGTGAAGGG
GTGTCGAAGCTAGAAGAATCCTCTAAAGCAACTCCTGCAGAGATGGATTTGGCCCACAAC
AGCCAAAGCATGCACGCCTCTTCAGCTTCCAAATCTGTGCTGGAGGTGACTCAGAAAGCA
ACCCCAAATCCAAGTCTTCTAGCTGCTGAGGACCAAGTGCCCTGTGAGAAGTGTGGCTCC
CTGGTACCGGTATGGGATATGCCAGAACACATGGACTATCATTTTGCATTGGAGTTGCAG
AAATCCTTTTTGCAGCCCCACTCTTCAAACCCCCAGGTTGTTTCTGCCGTATCTCATCAA
GGCAAAAGAAATCCCAAGAGCCCTTTGGCCTGCACTAATAAACGCCCCAGGCCTGAGGGC
ATGCAAACATTGGAATCATTTTTTAAGCCATTAACACATTAG
|
| Enzyme 14 GenBank Gene ID |
AB024313  |
| Enzyme 14 GeneCard ID |
POLH  |
| Enzyme 14 GenAtlas ID |
POLH  |
| Enzyme 14 HGNC ID |
HGNC:9181  |
| Enzyme 14 Chromosome Location |
6 |
| Enzyme 14 Locus |
6p21.1 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Masutani C, Kusumoto R, Yamada A, Dohmae N, Yokoi M, Yuasa M, Araki M, Iwai S, Takio K, Hanaoka F: The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase eta. Nature. 1999 Jun 17;399(6737):700-4. [PubMed
]
- Johnson RE, Kondratick CM, Prakash S, Prakash L: hRAD30 mutations in the variant form of xeroderma pigmentosum. Science. 1999 Jul 9;285(5425):263-5. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
6246 |
| Enzyme 15 Name |
DNA polymerase delta catalytic subunit |
| Enzyme 15 Synonyms |
- DNA polymerase subunit delta p125
|
| Enzyme 15 Gene Name |
POLD1 |
| Enzyme 15 Protein Sequence |
>DNA polymerase delta catalytic subunit
MDGKRRPGPGPGVPPKRARGGLWDDDDAPRPSQFEEDLALMEEMEAEHRLQEQEEEELQS
VLEGVADGQVPPSAIDPRWLRPTPPALDPQTEPLIFQQLEIDHYVGPAQPVPGGPPPSRG
SVPVLRAFGVTDEGFSVCCHIHGFAPYFYTPAPPGFGPEHMGDLQRELNLAISRDSRGGR
ELTGPAVLAVELCSRESMFGYHGHGPSPFLRITVALPRLVAPARRLLEQGIRVAGLGTPS
FAPYEANVDFEIRFMVDTDIVGCNWLELPAGKYALRLKEKATQCQLEADVLWSDVVSHPP
EGPWQRIAPLRVLSFDIECAGRKGIFPEPERDPVIQICSLGLRWGEPEPFLRLALTLRPC
APILGAKVQSYEKEEDLLQAWSTFIRIMDPDVITGYNIQNFDLPYLISRAQTLKVQTFPF
LGRVAGLCSNIRDSSFQSKQTGRRDTKVVSMVGRVQMDMLQVLLREYKLRSYTLNAVSFH
FLGEQKEDVQHSIITDLQNGNDQTRRRLAVYCLKDAYLPLRLLERLMVLVNAVEMARVTG
VPLSYLLSRGQQVKVVSQLLRQAMHEGLLMPVVKSEGGEDYTGATVIEPLKGYYDVPIAT
LDFSSLYPSIMMAHNLCYTTLLRPGTAQKLGLTEDQFIRTPTGDEFVKTSVRKGLLPQIL
ENLLSARKRAKAELAKETDPLRRQVLDGRQLALKVSANSVYGFTGAQVGKLPCLEISQSV
TGFGRQMIEKTKQLVESKYTVENGYSTSAKVVYGDTDSVMCRFGVSSVAEAMALGREAAD
WVSGHFPSPIRLEFEKVYFPYLLISKKRYAGLLFSSRPDAHDRMDCKGLEAVRRDNCPLV
ANLVTASLRRLLIDRDPEGAVAHAQDVISDLLCNRIDISQLVITKELTRAASDYAGKQAH
VELAERMRKRDPGSAPSLGDRVPYVIISAAKGVAAYMKSEDPLFVLEHSLPIDTQYYLEQ
QLAKPLLRIFEPILGEGRAEAVLLRGDHTRCKTVLTGKVGGLLAFAKRRNCCIGCRTVLS
HQGAVCEFCQPRESELYQKEVSHLNALEERFSRLWTQCQRCQGSLHEDVICTSRDCPIFY
MRKKVRKDLEDQEQLLRRFGPPGPEAW
|
| Enzyme 15 Number of Residues |
1107 |
| Enzyme 15 Molecular Weight |
123633 |
| Enzyme 15 Theoretical pI |
7.03 |
| Enzyme 15 GO Classification |
| Function |
- 3'-5' exonuclease activity
- DNA binding
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- exonuclease activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- nuclease activity
- nucleic acid binding
- nucleotide binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 15 General Function |
Replication, recombination and repair |
| Enzyme 15 Specific Function |
Possesses two enzymatic activities:DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction. Required with its accessory proteins (proliferating cell nuclear antigen (PCNA) and replication factor C (RFC) or activator 1) for leading strand synthesis. Also involved in completing Okazaki fragments initiated by the DNA polymerase alpha/primase complex |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
181620  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P28340  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
DPOD1_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>3324 bp
ATGGATGGCAAGCGGCGGCCAGGCCCAGGGCCCGGGGTGCCCCCAAAGCGGGCCCGTGGG
GGCCTCTGGGATGATGATGATGCACCTTGGCCATCCCAATTCGAGGAGGACCTGGCACTG
ATGGAGGAGATGGAGGCAGAACACAGGCTGCAGGAGCAGGAGGAGGAGGAGCTGCAGTCA
GTCCTGGAGGGGGTTGCAGACGGGCAGGTCCCACCATCAGCCATAGATCCTCGCTGGCTT
CGGCCCACACCACCAGCGCTGGACCCCCAGACAGAGCCCCTCATCTTCCAACAGTTGGAG
ATTGACCATTATGTGGGCCCAGCGCAGCCTGTGCCTGGGGGGCCCCCACCATCCCGCGGC
TCCGTGCCTGTGCTCCGCGCCTTCGGGGTCACCGATGAGGGGTTCTCTGTCTGCTGCCAC
ATCCACGGCTTCGCTCCCTACTTCTACACCCCAGCGCCCCCTGGTTTCGGGCCCGAGCAC
ATGGGTGACCTGCAACGGGAGCTGAACTTGGCCATCAGCCGGGACAGTCGCGGGGGGAGG
GAGCTGACTGGGCCGGCCGTGCTGGCTGTGGAACTGTGCTCCCGAGAGAGCATGTTTGGG
TACCACGGGCACGGCCCCTCCCCGTTCCTGCGCATCACCGTGGCGCTGCCGCGCCTCGTG
GCCCCGGCCCGCCGTCTCCTGGAACAGGGCATCCGTGTGGCAGGCCTGGGCACGCCCAGC
TTCGCGCCCTACGAGGCCAACGTCGACTTTGAGATCCGGTTCATGGTGGACACGGACATC
GTCGGCTGCAACTGGCTGGAGCTCCCAGCTGGGAAATACGCCCTGAGGCTGAAGGAGAAG
GCTACGCAGTGCCAGCTGGAGGCGGACGTGCTGTGGTCTGACGTGGTCAGTCACCCACCG
GAAGGGCCATGGCAGCGCATTGCGCCCTTGCGCGTGCTCAGCTTCGATATCGAGTGCGCC
GGCCGCAAAGGCATCTTCCCTGAGCCTGAGCGGGACCCTGTCATCCAGATCTGCTCGCTG
GGCCTGCGCTGGGGGGAGCCGGAGCCCTTCCTACGCCTGGCGCTCACCCTGCGGCCCTGT
GCCCCCATCCTGGGTGCCAAGGTGCAGAGCTACGAGAAGGAGGAGGACCTGCTGCAGGCC
TGGTCCACCTTCATCCGTATCATGGACCCCGACGTGATCACCGGTTACAACATCCAGAAC
TTCGACCTTCCGTACCTCATCTCTCGGGCCCAGACCCTCAAGGTACAAACATTCCCTTTC
CTGGGCCGTGTGGCCGGCCTTTGCTCCAACATCCGGGACTCTTCATTCCAGTCCAAGCAG
ACGGGCCGGCGGGACACCAAGGTTGTCAGCATGGTGGGCCGCGTGCAGATGGACATGCTG
CAGGTGCTGCTGCGGGAGTACAAGCTCCGCTCCCACACGCTCAATGCCGTGAGCTTCCAC
TTCCTGGGCGAGCAGAAGGAGGACGTGCAGCACAGCATCATCACCGACCTGCAGAATGGG
AACGACCAGACCCGCCGCCGCCTGGCTGTGTACTGCCTGAAGGATGCCTACCTGCCACTG
CGGCTGCTGGAGCGGCTCATGGTGCTGGTGAACGCCGTGGAGATGGCGAGGGTCACTGGC
GTGCCCCTCAGCTACCTGCTCAGTCGTGGCCAGCAGGTCAAAGTCGTATCCCAGCTGTTG
CGGCAGGCCATGCACGAGGGGCTGCTGATGCCCGTGGTGAAGTCAGAGGGCGGCGAGGAC
TACACGGGAGCCACTGTCATCGAGCCCCTCAAAGGGTACTACGACGTCCCCATCGCCACC
CTGGACTTCTCCTCGCTGTACCCGTCCATCATGATGGCCCACAACCTGTGTTACACCACG
CTCCTTCGGCCCGGGACTGCACAGAAACTGGGCCTGACTGAGGATCAGTTCATCAGGACC
CCCACCGGGGACGAGTTTGTGAAGACCTCAGTGCGGAAGGGGCTGCTGCCCCAGATCCTG
GAGAACCTGCTCAGTGCCCGGAAGAGGGCCAAGGCCGAGCTGGCCAAGGAGACAGACCCC
CTCCGGCGCCAGGTCCTGGATGGACGGCAGCTGGCGCTGAAGGTGAGCGCCAACTCCGTA
TACGGCTTCACTGGCGCCCAGGTGGGCAAGTTGCCGTGCCTGGAGATCTCACAGAGCGTC
ACGGGGTTCGGACGTCAGATGATCGAGAAAACCAAGCAGCTGGTGGAGTCTAAGTACACA
GTGGAGAATGGCTACAGCACCAGTGCCAAGGTGGTGTATGGTGACACTGACTCCGTCATG
TGCCGATTCGGCGTGTCCTCGGTGGCTGAGGCGATGGCCCTGGGGCGGGAGGCCGCGGAC
TGGGTGTCAGGTCACTTCCCGTCGCCCATCCGGCTGGAGTTTGAGAAGGTCTACTTCCCA
TACCTGCTTATCAGCAAGAAGCGCTACGCGGGCCTGCTCTTCTCCTCCCGGCCCGACGCC
CACGACCGCATGGACTGCAAGGGCCTGGAGGCCGTGCGCAGGGACAACTGCCCCCTCGTG
GCCAACCTGGTCACTGCCTCACTGCGCCGCCTGCTCATCGACCGAGACCCTGAGGGCGCG
GTGGCTCACGCACAGGACGTCATCTCGGACCTGCTGTGCAACCGCATCGATATCTCCCAG
CTGGTCATCACCAAGGAGCTGACCCGCGCGGCCTCCGACTATGCCGGCAAGCAGGCCCAC
GTGGAGCTGGCCGAGAGGATGAGGAAGCGGGACCCCGGGAGTGCGCCCAGCCTGGGCGAC
CGCGTCCCCTACGTGATCATCAGTGCCGCCAAGGGTGTGGCCGCCTACATGAAGTCGGAG
GACCCGCTGTTCGTGCTGGAGCACAGCCTGCCCATTGACACGCAGTACTACCTGGAGCAG
CAGCTGGCCAAGCCCCTCCTGCGCATCTTCGAGCCCATCCTGGGCGAGGGCCGTGCCGAG
GCTGTGCTACTGCGGGGGGACCACACGCGCTGCAAGACGGTGCTCACGGGCAAGGTGGGC
GGCCTCCTGGCCTTCGCCAAACGCCGCAACTGCTGCATTGGCTGCCGCACAGTGCTCAGC
CACCAGGGAGCCGTGTGTGAGTTCTGCCAGCCCCGGGAGTCTGAGCTGTATCAGAAGGAG
GTATCCCATCTGAATGCCCTGGAGGAGCGCTTCTCGCGCCTCTGGACGCAGTGCCAGCGC
TGCCAGGGCAGCCTGCACGAGGACGTCATCTGCACCAGCCGGGACTGCCCCATCTTCTAC
ATGCGCAAGAAGGTGCGGAAGGACCTGGAAGACCAGGAGCAGCTCCTGCGGCGCTTCGGA
CCCCCTGGACCTGAGGCCTGGTGA
|
| Enzyme 15 GenBank Gene ID |
M80397  |
| Enzyme 15 GeneCard ID |
POLD1  |
| Enzyme 15 GenAtlas ID |
POLD1  |
| Enzyme 15 HGNC ID |
HGNC:9175  |
| Enzyme 15 Chromosome Location |
19 |
| Enzyme 15 Locus |
19q13.3 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Chung DW, Zhang JA, Tan CK, Davie EW, So AG, Downey KM: Primary structure of the catalytic subunit of human DNA polymerase delta and chromosomal location of the gene. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11197-201. [PubMed
]
- Yang CL, Chang LS, Zhang P, Hao H, Zhu L, Toomey NL, Lee MY: Molecular cloning of the cDNA for the catalytic subunit of human DNA polymerase delta. Nucleic Acids Res. 1992 Feb 25;20(4):735-45. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
6247 |
| Enzyme 16 Name |
DNA polymerase zeta catalytic subunit |
| Enzyme 16 Synonyms |
- hREV3
|
| Enzyme 16 Gene Name |
REV3L |
| Enzyme 16 Protein Sequence |
>DNA polymerase zeta catalytic subunit
MFSVRIVTADYYMASPLQGLDTCQSPLTQAPVKKVPVVRVFGATPAGQKTCLHLHGIFPY
LYVPYDGYGQQPESYLSQMAFSIDRALNVALGNPSSTAQHVFKVSLVSGMPFYGYHEKER
HFMKIYLYNPTMVKRICELLQSGAIMNKFYQPHEAHIPYLLQLFIDYNLYGMNLINLAAV
KFRKARRKSNTLHATGSCKNHLSGNSLADTLFRWEQDEIPSSLILEGVEPQSTCELEVDA
VAADILNRLDIEAQIGGNPGLQAIWEDEKQRRRNRNETSQMSQPESQDHRFVPATESEKK
FQKRLQEILKQNDFSVTLSGSVDYSDGSQEFSAELTLHSEVLSPEMLQCTPANMVEVHKD
KESSKGHTRHKVEEALINEEAILNLMENSQTFQPLTQRLSESPVFMDSSPDEALVHLLAG
LESDGYRGERNRMPSPCRSFGNNKYPQNSDDEENEPQIEKEEMELSLVMSQRWDSNIEEH
CAKKRSLCRNTHRSSTEDDDSSSGEEMEWSDNSLLLASLSIPQLDGTADENSDNPLNNEN
SRTHSSVIATSKLSVKPSIFHKDAATLEPSSSAKITFQCKHTSALSSHVLNKEDLIEDLS
QTNKNTEKGLDNSVTSFTNESTYSMKYPGSLSSTVHSENSHKENSKKEILPVSSCESSIF
DYEEDIPSVTRQVPSRKYTNIRKIEKDSPFIHMHRHPNENTLGKNSFNFSDLNHSKNKVS
SEGNEKGNSTALSSLFPSSFTENCELLSCSGENRTMVHSLNSTADESGLNKLKIRYEEFQ
EHKTEKPSLSQQAAHYMFFPSVVLSNCLTRPQKLSPVTYKLQPGNKPSRLKLNKRKLAGH
QETSTKSSETGSTKDNFIQNNPCNSNPEKDNALASDLTKTTRGAFENKTPTDGFIDCHFG
DGTLETEQSFGLYGNKYTLRAKRKVNYETEDSESSFVTHNSKISLPHPMEIGESLDGTLK
SRKRRKMSKKLPPVIIKYIIINRFRGRKNMLVKLGKIDSKEKQVILTEEKMELYKKLAPL
KDFWPKVPDSPATKYPIYPLTPKKSHRRKSKHKSAKKKTGKQQRTNNENIKRTLSFRKKR
SHAILSPPSPSYNAETEDCDLNYSDVMSKLGFLSERSTSPINSSPPRCWSPTDPRAEEIM
AAAEKEAMLFKGPNVYKKTVNSRIGKTSRARAQIKKSKAKLANPSIVTKKRNKRNQTNKL
VDDGKKKPRAKQKTNEKGTSRKHTTLKDEKIKSQSGAEVKFVLKHQNVSEFASSSGGSQL
LFKQKDMPLMGSAVDHPLSASLPTGINAQQKLSGCFSSFLESKKSVDLQTFPSSRDDLHP
SVVCNSIGPGVSKINVQRPHNQSAMFTLKESTLIQKNIFDLSNHLSQVAQNTQISSGMSS
KIEDNANNIQRNYLSSIGKLSEYRNSLESKLDQAYTPNFLHCKDSQQQIVCIAEQSKHSE
TCSPGNTASEESQMPNNCFVTSLRSPIKQIAWEQKQRGFILDMSNFKPERVKPRSLSEAI
SQTKALSQCKNRNVSTPSAFGEGQSGLAVLKELLQKRQQKAQNANTTQDPLSNKHQPNKN
ISGSLEHNKANKRTRSVTSPRKPRTPRSTKQKEKIPKLLKVDSLNLQNSSQLDNSVSDDS
PIFFSDPGFESCYSLEDSLSPEHNYNFDINTIGQTGFCSFYSGSQFVPADQNLPQKFLSD
AVQDLFPGQAIEKNEFLSHDNQKCDEDKHHTTDSASWIRSGTLSPEIFEKSTIDSNENRR
HNQWKNSFHPLTTRSNSIMDSFCVQQAEDCLSEKSRLNRSSVSKEVFLSLPQPNNSDWIQ
GHTRKEMGQSLDSANTSFTAILSSPDGELVDVACEDLELYVSRNNDMLTPTPDSSPRSTS
SPSQSKNGSFTPRTANILKPLMSPPSREEIMATLLDHDLSETIYQEPFCSNPSDVPEKPR
EIGGRLLMVETRLANDLAEFEGDFSLEGLRLWKTAFSAMTQNPRPGSPLRSGQGVVNKGS
SNSPKMVEDKKIVIMPCKCAPSRQLVQVWLQAKEEYERSKKLPKTKPTGVVKSAENFSSS
VNPDDKPVVPPKMDVSPCILPTTAHTKEDVDNSQIALQAPTTGCSQTASESQMLPPVASA
SDPEKDEDDDDNYYISYSSPDSPVIPPWQQPISPDSKALNGDDRPSSPVEELPSLAFENF
LKPIKDGIQKSPCSEPQEPLVISPINTRARTGKCESLCFHSTPIIQRKLLERLPEAPGLS
PLSTEPKTQKLSNKKGSNTDTLRRVLLTQAKNQFAAVNTPQKETSQIDGPSLNNTYGFKV
SIQNLQEAKALHEIQNLTLISVELHARTRRDLEPDPEFDPICALFYCISSDTPLPDTEKT
ELTGVIVIDKDKTVFSQDIRYQTPLLIRSGITGLEVTYAADEKALFHEIANIIKRYDPDI
LLGYEIQMHSWGYLLQRAAALSIDLCRMISRVPDDKIENRFAAERDEYGSYTMSEINIVG
RITLNLWRIMRNEVALTNYTFENVSFHVLHQRFPLFTFRVLSDWFDNKTDLYRWKMVDHY
VSRVRGNLQMLEQLDLIGKTSEMARLFGIQFLHVLTRGSQYRVESMMLRIAKPMNYIPVT
PSVQQRSQMRAPQCVPLIMEPESRFYSNSVLVLDFQSLYPSIVIAYNYCFSTCLGHVENL
GKYDEFKFGCTSLRVPPDLLYQVRHDITVSPNGVAFVKPSVRKGVLPRMLEEILKTRFMV
KQSMKAYKQDRALSRMLDARQLGLKLIANVTFGYTSANFSGRMPCIEVGDSIVHKARETL
ERAIKLVNDTKKWGARVVYGDTDSMFVLLKGATKEQSFKIGQEIAEAVTATNPKPVKLKF
EKVYLPCVLQTKKRYVGYMYETLDQKDPVFDAKGIETVRRDSCPAVSKILERSLKLLFET
RDISLIKQYVQRQCMKLLEGKASIQDFIFAKEYRGSFSYKPGACVPALELTRKMLTYDRR
SEPQVGERVPYVIIYGTPGVPLIQLVRRPVEVLQDPTLRLNATYYITKQILPPLARIFSL
IGIDVFSWYHELPRIHKATSSSRSEPEGRKGTISQYFTTLHCPVCDDLTQHGICSKCRSQ
PQHVAVILNQEIRELERQQEQLVKICKNCTGCFDRHIPCVSLNCPVLFKLSRVNRELSKA
PYLRQLLDQF
|
| Enzyme 16 Number of Residues |
3130 |
| Enzyme 16 Molecular Weight |
352779 |
| Enzyme 16 Theoretical pI |
8.61 |
| Enzyme 16 GO Classification |
Not Available |
| Enzyme 16 General Function |
Replication, recombination and repair |
| Enzyme 16 Specific Function |
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1) |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 16 Pfam Domain Function |
Not Available |
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
3063675  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
O60673  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
DPOLZ_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>9393 bp
ATGTTTTCAGTAAGGATAGTGACTGCAGACTACTACATGGCCAGCCCGCTGCAGGGGCTG
GATACCTGCCAATCCCCCCTCACCCAGGCCCCTGTCAAGAAGGTGCCGGTGGTGCGAGTC
TTCGGAGCGACCCCGGCAGGTCAGAAGACATGTCTTCATCTACATGGCATCTTTCCTTAC
CTCTATGTGCCATACGATGGTTATGGACAGCAGCCAGAAAGCTATCTTTCTCAGATGGCA
TTCAGTATCGACAGAGCACTTAATGTGGCTTTAGGCAATCCATCTTCCACTGCTCAGCAT
GTGTTCAAAGTGTCATTAGTATCAGGAATGCCTTTTTATGGTTATCATGAGAAGGAAAGA
CACTTTATGAAGATCTATCTTTACAATCCTACAATGGTGAAAAGGATATGTGAACTTTTG
CAAAGCGGAGCCATAATGAATAAATTTTACCAGCCTCATGAAGCGCATATTCCCTACCTC
CTACAGCTCTTCATTGACTACAATCTTTATGGCATGAATTTAATAAATCTGGCTGCTGTC
AAGTTCCGAAAAGCAAGAAGGAAAAGTAATACATTGCATGCAACTGGATCCTGCAAGAAT
CATTTATCAGGAAATTCTCTTGCTGATACTTTATTTCGGTGGGAACAAGATGAAATACCA
AGCTCTTTAATATTGGAAGGTGTTGAACCACAGAGTACATGTGAATTAGAAGTGGATGCT
GTAGCTGCTGATATCTTAAATCGTCTGGACATTGAAGCTCAAATTGGTGGAAACCCTGGT
CTACAGGCCATATGGGAAGATGAAAAGCAACGGCGAAGAAACAGAAATGAAACTTCTCAA
ATGAGCCAACCTGAGTCACAAGATCACAGGTTTGTGCCAGCAACAGAAAGTGAAAAAAAA
TTTCAGAAGAGACTTCAGGAAATTCTCAAACAGAATGATTTCTCTGTAACATTATCAGGA
TCTGTGGACTACAGCGATGGATCCCAGGAGTTCTCTGCTGAGTTAACATTGCACTCTGAG
GTTCTGTCTCCTGAAATGCTTCAGTGTACACCAGCCAATATGGTAGAAGTTCACAAAGAC
AAAGAGTCAAGCAAAGGTCACACTAGACACAAAGTGGAAGAAGCTCTTATTAATGAAGAA
GCAATTTTGAACCTTATGGAAAATAGTCAGACTTTTCAGCCTTTGACCCAAAGACTGAGT
GAGTCACCTGTTTTCATGGACAGTAGTCCTGATGAGGCTCTGGTACATCTTCTTGCTGGT
TTGGAAAGTGATGGATATCGGGGGGAAAGAAATAGGATGCCATCACCATGTCGCTCCTTT
GGAAATAATAAATATCCACAAAATAGTGATGATGAAGAAAATGAACCACAGATTGAAAAA
GAGGAAATGGAGCTTAGTTTGGTGATGTCCCAGAGATGGGACAGCAATATTGAAGAACAT
TGTGCCAAAAAGAGATCACTGTGCAGAAATACCCACAGAAGTTCAACTGAAGATGATGAC
TCATCTTCAGGAGAAGAAATGGAATGGAGTGATAACAGTTTGCTTCTAGCCAGTCTTTCT
ATACCTCAGTTAGATGGAACTGCAGATGAAAATAGTGACAATCCATTGAACAATGAAAAT
TCTAGAACCCACTCTTCTGTAATTGCAACAAGCAAGCTTTCAGTTAAACCCTCCATCTTT
CACAAAGATGCTGCTACATTAGAACCCTCATCTTCTGCTAAGATTACCTTTCAGTGTAAA
CACACAAGTGCCCTTTCTTCCCATGTTTTGAACAAGGAAGATTTAATTGAAGACCTTTCA
CAGACAAACAAAAATACAGAAAAAGGTCTAGATAACTCAGTCACTTCTTTTACAAACGAA
AGCACTTATTCTATGAAATACCCTGGATCTTTAAGCAGTACTGTTCATTCAGAAAATTCT
CATAAAGAGAATAGTAAGAAAGAGATCCTCCCAGTATCTTCCTGTGAAAGTAGTATTTTT
GATTATGAAGAAGATATTCCATCTGTTACAAGACAAGTACCAAGTAGAAAATATACAAAC
ATTAGAAAAATCGAAAAGGATTCCCCTTTTATACATATGCACCGTCACCCTAACGAGAAT
ACATTGGGCAAAAATTCTTTCAACTTTTCTGACTTAAATCATTCAAAAAATAAAGTATCC
TCTGAAGGAAATGAAAAAGGAAACAGCACAGCTCTGAGTAGTTTATTCCCTTCATCATTT
ACTGAAAATTGTGAATTACTGTCATGCTCAGGGGAGAATAGAACTATGGTGCATTCTCTT
AATAGCACTGCTGATGAAAGTGGACTAAATAAACTTAAAATTAGGTATGAAGAATTTCAA
GAACATAAAACAGAAAAGCCAAGCCTCAGCCAGCAAGCAGCACACTATATGTTTTTTCCC
AGTGTTGTTCTTTCTAACTGTCTTACTAGACCACAGAAACTATCTCCTGTCACATATAAA
TTACAACCTGGCAATAAACCATCCCGGTTAAAATTGAATAAAAGGAAACTTGCAGGTCAT
CAGGAGACTTCTACCAAAAGTAGTGAGACTGGATCCACAAAAGATAATTTTATACAAAAT
AATCCTTGTAATAGTAATCCTGAGAAGGATAATGCATTGGCTAGTGATTTAACTAAAACC
ACTCGTGGAGCTTTTGAAAATAAAACACCCACAGATGGTTTTATAGACTGTCACTTTGGA
GATGGGACGTTAGAAACTGAGCAGTCCTTTGGACTATATGGAAATAAATACACACTTAGA
GCCAAACGCAAGGTAAATTATGAGACTGAAGACAGTGAGTCAAGTTTTGTAACTCACAAC
TCAAAAATTAGTCTACCTCATCCCATGGAAATTGGTGAAAGTTTAGATGGAACTCTCAAA
TCCCGAAAACGAAGAAAAATGTCTAAAAAGCTGCCCCCTGTCATCATAAAGTATATTATT
ATTAATAGATTTAGAGGGAGAAAAAATATGCTTGTGAAGCTAGGAAAAATAGACTCTAAA
GAAAAACAAGTAATATTAACAGAAGAAAAAATGGAACTATATAAAAAGCTTGCACCTTTG
AAGGACTTTTGGCCAAAAGTTCCCGACTCCCCTGCAACCAAATATCCCATTTATCCACTA
ACACCAAAGAAAAGTCACAGAAGAAAGTCAAAACATAAATCTGCTAAGAAAAAAACTGGT
AAACAACAAAGGACAAATAATGAAAATATTAAAAGAACTTTGTCTTTCAGGAAAAAACGG
TCACATGCTATTCTTTCTCCTCCCTCACCATCTTACAATGCTGAAACCGAAGATTGTGAC
TTGAATTATAGTGATGTTATGTCTAAACTAGGTTTTCTTTCTGAGAGAAGCACAAGTCCC
ATAAATTCTTCTCCACCTCGCTGCTGGTCTCCCACAGATCCAAGAGCTGAAGAAATCATG
GCTGCTGCAGAAAAAGAGGCAATGCTTTTTAAGGGTCCTAATGTATATAAGAAGACTGTT
AATTCTCGTATAGGAAAAACTAGTCGCGCAAGAGCACAGATTAAGAAATCAAAAGCAAAG
CTTGCTAATCCCTCTATAGTTACTAAGAAAAGGAACAAACGAAATCAGACAAATAAACTA
GTAGATGATGGAAAAAAGAAACCAAGAGCAAAACAAAAAACAAATGAGAAAGGTACATCG
AGAAAGCATATAACACTTAAGGATGAAAAAATAAAATCTCAGTCTGGTGCTGAGGTTAAG
TTTGTACTGAAACACCAGAATGTGTCTGAATTTGCAAGTAGTTCTGGAGGCTCTCAACTA
CTTTTTAAACAGAAAGATATGCCACTAATGGGCTCTGCTGTAGATCATCCCCTTTCTGCT
TCCCTACCCACTGGAATTAATGCACAACAGAAGTTATCTGGCTGCTTTTCTTCTTTCTTA
GAAAGCAAGAAGTCTGTAGATTTGCAGACATTCCCCAGTTCACGAGATGATTTGCATCCA
TCAGTTGTTTGTAATTCTATAGGACCTGGAGTCTCAAAAATTAATGTTCAAAGGCCTCAT
AATCAAAGTGCTATGTTTACTCTAAAGGAATCAACGTTAATTCAAAAAAATATATTTGAC
CTTTCCAATCATTTATCTCAGGTAGCACAGAATACACAGATATCTTCTGGTATGTCCTCA
AAGATAGAAGATAATGCAAATAATATACAAAGAAACTATTTGTCATCAATCGGAAAGTTA
AGTGAATATCGCAATTCCCTAGAATCAAAGCTGGACCAAGCATATACCCCTAATTTTTTG
CATTGCAAAGACAGTCAGCAGCAGATTGTATGCATAGCGGAACAGTCAAAGCACAGTGAA
ACTTGTTCTCCGGGAAATACAGCTTCAGAGGAAAGCCAAATGCCTAATAATTGCTTTGTA
ACTTCCTTGAGAAGTCCAATCAAACAAATAGCATGGGAGCAAAAGCAAAGGGGCTTTATT
TTAGATATGTCAAATTTTAAACCTGAAAGAGTAAAACCGAGGTCATTATCAGAAGCAATT
TCACAAACCAAAGCACTTTCTCAGTGTAAAAATCGAAATGTGTCAACACCTTCAGCATTT
GGTGAAGGACAGTCTGGACTGGCAGTTCTAAAAGAATTGTTACAAAAAAGACAGCAGAAA
GCACAAAATGCAAATACTACACAAGACCCATTATCCAATAAACATCAACCAAATAAAAAT
ATTTCTGGTTCCCTTGAGCATAACAAAGCAAATAAACGGACACGATCGGTAACGTCCCCA
AGAAAACCTCGAACTCCCAGAAGTACAAAACAAAAAGAAAAAATCCCCAAACTTCTCAAA
GTAGACTCTTTAAATTTACAAAACTCTAGCCAGTTGGATAACTCTGTATCAGATGATAGT
CCCATCTTTTTTTCAGATCCAGGCTTTGAAAGTTGTTACTCACTTGAAGATAGTTTATCT
CCTGAACATAATTATAATTTTGATATTAACACAATAGGTCAGACTGGATTTTGTAGCTTT
TATTCTGGAAGTCAGTTTGTCCCAGCTGATCAGAATTTGCCTCAGAAGTTCCTAAGTGAT
GCTGTTCAGGATCTTTTTCCAGGACAAGCTATAGAAAAAAATGAGTTTTTAAGTCATGAC
AACCAGAAATGTGATGAAGACAAGCATCATACCACAGACTCAGCCTCATGGATTAGATCT
GGTACTTTAAGTCCTGAAATTTTTGAGAAGTCAACCATAGATAGCAATGAGAATCGTCGC
CACAACCAGTGGAAAAATAGCTTTCATCCTCTAACAACTCGGTCTAACTCAATAATGGAT
TCTTTCTGTGTTCAGCAGGCAGAAGACTGTCTAAGTGAAAAATCTAGATTGAATAGGAGT
TCAGTAAGCAAAGAAGTGTTTCTTAGCCTCCCACAGCCAAACAATTCAGACTGGATTCAA
GGTCACACCAGAAAAGAAATGGGACAGTCTCTTGACTCAGCCAATACCTCTTTTACTGCA
ATACTCTCCTCCCCTGATGGTGAACTTGTAGACGTGGCCTGTGAAGATTTAGAACTGTAT
GTTTCAAGAAACAATGATATGTTGACACCAACTCCTGATAGTTCACCAAGATCTACTAGC
TCTCCTTCACAATCTAAAAATGGCAGCTTCACCCCTCGAACTGCTAACATTCTGAAACCA
CTTATGTCCCCCCCAAGTAGGGAAGAAATTATGGCAACTTTGTTGGATCATGACCTGTCT
GAGACTATTTACCAGGAACCATTTTGCAGTAATCCTTCTGATGTACCAGAAAAGCCCAGG
GAGATTGGTGGACGGCTCCTCATGGTAGAAACTCGACTTGCAAATGATCTGGCTGAGTTT
GAGGGAGACTTTTCCTTGGAAGGACTTCGTCTTTGGAAAACAGCATTCTCAGCAATGACT
CAGAATCCAAGGCCAGGGTCACCCCTTCGCAGTGGCCAAGGAGTTGTCAATAAAGGGTCA
AGTAATAGCCCTAAGATGGTTGAAGATAAAAAAATTGTGATTATGCCTTGCAAATGTGCC
CCAAGTCGACAACTGGTTCAAGTGTGGCTTCAAGCCAAAGAAGAATACGAACGTTCCAAG
AAACTGCCTAAAACCAAGCCAACTGGAGTTGTAAAATCTGCTGAGAACTTTAGCTCTTCA
GTTAACCCAGATGACAAACCTGTAGTGCCTCCAAAAATGGATGTAAGTCCATGTATACTC
CCCACTACAGCACATACCAAGGAGGATGTTGATAATTCTCAGATTGCTTTACAAGCACCA
ACCACGGGATGTAGTCAAACTGCAAGTGAAAGTCAGATGCTGCCACCAGTTGCCTCTGCA
AGTGATCCCGAAAAAGATGAAGATGATGATGATAACTATTACATTAGTTATAGCTCCCCT
GATTCTCCAGTAATTCCCCCTTGGCAACAACCAATATCCCCAGATTCCAAAGCATTAAAT
GGAGATGATAGACCCTCATCACCAGTAGAGGAGCTGCCTTCATTGGCTTTTGAGAACTTC
TTAAAGCCAATAAAAGATGGTATACAAAAAAGCCCCTGCAGTGAGCCTCAAGAGCCTCTA
GTGATATCTCCAATTAATACTAGGGCAAGAACTGGGAAATGTGAATCACTTTGCTTTCAT
AGTACACCAATCATACAGAGAAAACTTCTGGAAAGGCTTCCTGAAGCACCTGGCCTTAGC
CCATTATCAACAGAACCAAAAACACAGAAGTTGAGTAATAAGAAAGGAAGTAATACTGAC
ACTCTTAGAAGAGTACTGTTAACACAAGCAAAGAATCAATTTGCAGCAGTAAATACCCCA
CAGAAAGAAACTTCTCAGATTGATGGACCATCTTTAAACAATACTTACGGTTTCAAAGTC
AGCATACAAAACTTACAGGAGGCAAAAGCTTTACATGAGATACAAAATCTTACCCTAATC
AGTGTGGAGTTGCATGCTCGAACTAGACGAGACTTAGAACCGGATCCTGAATTTGACCCA
ATCTGTGCTCTGTTCTACTGCATCTCATCTGACACTCCACTGCCAGATACAGAAAAAACA
GAACTCACAGGTGTAATAGTGATTGATAAAGACAAGACAGTTTTCAGTCAAGATATCAGA
TATCAGACTCCATTACTTATTAGATCTGGAATTACAGGACTCGAAGTCACCTATGCTGCT
GATGAGAAGGCACTTTTTCATGAAATTGCAAATATAATAAAGAGGTATGATCCTGATATT
CTGCTAGGATATGAGATTCAGATGCATTCCTGGGGTTACCTCTTACAAAGGGCTGCCGCT
TTAAGTATTGACTTATGTCGGATGATCTCTCGGGTGCCAGATGACAAAATTGAGAACAGA
TTTGCAGCTGAAAGAGATGAGTATGGATCATATACAATGAGTGAGATAAATATTGTTGGC
CGAATTACACTAAATCTTTGGAGAATCATGAGAAATGAGGTGGCTCTAACTAACTACACC
TTTGAAAATGTGAGCTTTCATGTTCTTCATCAGCGTTTTCCCCTCTTTACCTTTCGAGTC
TTGTCAGACTGGTTTGATAACAAGACAGATCTATACAGATGGAAAATGGTTGATCATTAT
GTTAGCCGTGTCCGTGGAAATCTCCAAATGTTAGAACAGCTGGACCTGATTGGGAAAACC
AGTGAGATGGCTAGACTTTTTGGCATTCAGTTTTTACATGTACTGACAAGGGGTTCACAG
TACCGTGTGGAATCAATGATGTTGCGTATTGCTAAACCAATGAACTATATTCCTGTGACA
CCTAGTGTTCAGCAAAGATCCCAGATGAGAGCCCCACAGTGTGTTCCTCTAATTATGGAG
CCTGAATCCCGCTTCTATAGCAACTCTGTTCTCGTTTTGGATTTCCAATCACTTTATCCT
TCTATTGTGATTGCATATAACTACTGCTTTTCCACCTGCCTTGGCCATGTGGAGAACTTG
GGAAAGTATGATGAGTTCAAATTTGGCTGTACCTCTCTGAGAGTACCTCCAGATTTACTT
TACCAAGTTAGGCATGATATCACAGTGTCCCCCAATGGAGTAGCTTTTGTCAAGCCTTCA
GTAAGAAAAGGTGTACTACCAAGAATGCTTGAAGAAATTTTGAAGACTAGATTTATGGTG
AAGCAGTCAATGAAGGCTTACAAGCAAGACAGAGCCCTGTCACGAATGCTTGATGCGCGT
CAGTTGGGACTTAAGCTGATAGCAAATGTCACATTTGGCTATACATCTGCTAATTTTTCT
GGGAGAATGCCATGCATTGAGGTTGGCGATAGTATTGTTCACAAAGCCAGAGAGACCTTG
GAACGAGCTATTAAACTGGTGAATGATACCAAGAAATGGGGGGCTAGGGTTGTATATGGC
GATACTGACAGTATGTTTGTGCTACTGAAAGGAGCCACTAAGGAGCAGTCTTTTAAGATT
GGTCAGGAAATTGCCGAAGCTGTAACTGCTACCAATCCTAAACCAGTGAAATTGAAGTTT
GAAAAGGTATATTTGCCCTGTGTTTTACAAACAAAAAAGAGGTATGTGGGTTACATGTAT
GAAACACTGGATCAGAAGGACCCAGTATTTGATGCAAAAGGAATAGAAACAGTCAGAAGA
GATTCCTGCCCTGCTGTTTCTAAGATACTTGAGCGTTCTCTAAAGCTGCTATTTGAAACG
AGAGATATAAGTCTAATTAAACAGTATGTTCAGCGACAATGTATGAAGCTTCTGGAAGGA
AAGGCCAGCATACAAGACTTTATCTTTGCCAAGGAATACAGAGGAAGTTTTTCTTATAAA
CCAGGAGCTTGTGTGCCAGCCCTTGAACTTACAAGGAAAATGCTGACTTATGACCGGCGC
TCTGAGCCTCAGGTTGGGGAGCGAGTGCCATACGTCATCATTTATGGGACCCCCGGAGTA
CCACTTATCCAGCTTGTAAGGCGCCCAGTGGAAGTCCTGCAGGACCCAACTCTGAGACTG
AATGCTACTTACTATATTACCAAGCAAATCCTTCCACCCTTGGCAAGAATCTTCTCACTT
ATTGGTATTGATGTCTTCAGCTGGTATCATGAATTACCAAGGATCCATAAAGCTACCAGC
TCCTCGCGAAGTGAACCTGAAGGGCGGAAAGGCACTATTTCACAATATTTTACTACCTTA
CACTGTCCTGTGTGTGATGACCTAACTCAGCATGGCATCTGTAGTAAATGTCGGAGCCAA
CCTCAGCATGTTGCAGTCATCCTCAACCAAGAAATCCGGGAGTTGGAACGTCAACAGGAG
CAACTTGTAAAGATATGCAAGAACTGTACAGGTTGCTTTGATCGACACATCCCATGTGTT
TCTCTGAACTGCCCAGTACTTTTCAAACTCTCCCGAGTAAATAGAGAATTGTCCAAGGCA
CCATATCTCCGGCAGTTATTAGACCAGTTTTAA
|
| Enzyme 16 GenBank Gene ID |
AF058701  |
| Enzyme 16 GeneCard ID |
REV3L  |
| Enzyme 16 GenAtlas ID |
REV3L  |
| Enzyme 16 HGNC ID |
HGNC:9968  |
| Enzyme 16 Chromosome Location |
6 |
| Enzyme 16 Locus |
6q21 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Gibbs PE, McGregor WG, Maher VM, Nisson P, Lawrence CW: A human homolog of the Saccharomyces cerevisiae REV3 gene, which encodes the catalytic subunit of DNA polymerase zeta. Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6876-80. [PubMed
]
- Lin W, Wu X, Wang Z: A full-length cDNA of hREV3 is predicted to encode DNA polymerase zeta for damage-induced mutagenesis in humans. Mutat Res. 1999 Mar 10;433(2):89-98. [PubMed
]
- Morelli C, Mungall AJ, Negrini M, Barbanti-Brodano G, Croce CM: Alternative splicing, genomic structure, and fine chromosome localization of REV3L. Cytogenet Cell Genet. 1998;83(1-2):18-20. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Murakumo Y, Roth T, Ishii H, Rasio D, Numata S, Croce CM, Fishel R: A human REV7 homolog that interacts with the polymerase zeta catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2. J Biol Chem. 2000 Feb 11;275(6):4391-7. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
6249 |
| Enzyme 17 Name |
DNA polymerase epsilon, catalytic subunit A |
| Enzyme 17 Synonyms |
- DNA polymerase II subunit A
|
| Enzyme 17 Gene Name |
POLE |
| Enzyme 17 Protein Sequence |
>DNA polymerase epsilon, catalytic subunit A
MSLRSGGRRRADPGADGEASRDDGATSSVSALKRLERSQWTDKMDLRFGFERLKEPGEKT
GWLINMHPTEILDEDKRLGSAVDYYFIQDDGSRFKVALPYKPYFYIATRKGCEREVSSFL
SKKFQGKIAKVETVPKEDLDLPNHLVGLKRNYIRLSFHTVEDLVKVRKEISPAVKKNREQ
DHASDAYTALLSSVLQRGGVITDEEETSKKIADQLDNIVDMREYDVPYHIRLSIDLKIHV
AHWYNVRYRGNAFPVEITRRDDLVERPDPVVLAFDIETTKLPLKFPDAETDQIMMISYMI
DGQGYLITNREIVSEDIEDFEFTPKPEYEGPFCVFNEPDEAHLIQRWFEHVQETKPTIMV
TYNGDFFDWPFVEARAAVHGLSMQQEIGFQKDSQGEYKAPQCIHMDCLRWVKRDSYLPVG
SHNLKAAAKAKLGYDPVELDPEDMCRMATEQPQTLATYSVSDAVATYYLYMKYVHPFIFA
LCTIIPMEPDEVLRKGSGTLCEALLMVQAFHANIIFPNKQEQEFNKLTDDGHVLDSETYV
GGHVEALESGVFRSDIPCRFRMNPAAFDFLLQRVEKTLRHALEEEEKVPVEQVTNFEEVC
DEIKSKLASLKDVPSRIECPLIYHLDVGAMYPNIILTNRLQPSAMVDEATCAACDFNKPG
ANCQRKMAWQWRGEFMPASRSEYHRIQHQLESEKFPPLFPEGPARAFHELSREEQAKYEK
RRLADYCRKAYKKIHITKVEERLTTICQRENSFYVDTVRAFRDRRYEFKGLHKVWKKKLS
AAVEVGDAAEVKRCKNMEVLYDSLQLAHKCILNSFYGYVMRKGARWYSMEMAGIVCFTGA
NIITQARELIEQIGRPLELDTDGIWCVLPNSFPENFVFKTTNVKKPKVTISYPGAMLNIM
VKEGFTNDQYQELAEPSSLTYVTRSENSIFFEVDGPYLAMILPASKEEGKKLKKRYAVFN
EDGSLAELKGFEVKRRGELQLIKIFQSSVFEAFLKGSTLEEVYGSVAKVADYWLDVLYSK
AANMPDSELFELISENRSMSRKLEDYGEQKSTSISTAKRLAEFLGDQMVKDAGLSCRYII
SRKPEGSPVTERAIPLAIFQAEPTVRKHFLRKWLKSSSLQDFDIRAILDWDYYIERLGSA
IQKIITIPAALQQVKNPVPRVKHPDWLHKKLLEKNDVYKQKKISELFTLEGRRQVTMAEA
SEDSPRPSAPDMEDFGLVKLPHPAAPVTVKRKRVLWESQEESQDLTPTVPWQEILGQPPA
LGTSQEEWLVWLRFHKKKWQLQARQRLARRKRQRLESAEGVLRPGAIRDGPATGLGSFLR
RTARSILDLPWQIVQISETSQAGLFRLWALVGSDLHCIRLSIPRVFYVNQRVAKAEEGAS
YRKVNRVLPRSNMVYNLYEYSVPEDMYQEHINEINAELSAPDIEGVYETQVPLLFRALVH
LGCVCVVNKQLVRHLSGWEAETFALEHLEMRSLAQFSYLEPGSIRHIYLYHHAQAHKALF
GIFIPSQRRASVFVLDTVRSNQMPSLGALYSAEHGLLLEKVGPELLPPPKHTFEVRAETD
LKTICRAIQRFLLAYKEERRGPTLIAVQSSWELKRLASEIPVLEEFPLVPICVADKINYG
VLDWQRHGARRMIRHYLNLDTCLSQAFEMSRYFHIPIGNLPEDISTFGSDLFFARHLQRH
NHLLWLSPTARPDLGGKEADDNCLVMEFDDQATVEINSSGCYSTVCVELDLQNLAVNTIL
QSHHVNDMEGADSMGISFDVIQQASLEDMITGGQAASAPASYDETALCSNTFRILKSMVV
GWVKEITQYHNIYADNQVMHFYRWLRSPSSLLHDPALHRTLHNMMKKLFLQLIAEFKRLG
SSVIYANFNRIILCTKKRRVEDAIAYVEYITSSIHSKETFHSLTISFSRCWEFLLWMDPS
NYGGIKGKVSSRIHCGLQDSQKAGGAEDEQENEDDEEERDGEEEEEAEESNVEDLLENNW
NILQFLPQAASCQNYFLMIVSAYIVAVYHCMKDGLRRSAPGSTPVRRRGASQLSQEAEGA
VGALPGMITFSQDYVANELTQSFFTITQKIQKKVTGSRNSTELSEMFPVLPGSHLLLNNP
ALEFIKYVCKVLSLDTNITNQVNKLNRDLLRLVDVGEFSEEAQFRDPCRSYVLPEVICRS
CNFCRDLDLCKDSSFSEDGAVLPQWLCSNCQAPYDSSAIEMTLVEVLQKKLMAFTLQDLV
CLKCRGVKETSMPVYCSCAGDFALTIHTQVFMEQIGIFRNIAQHYGMSYLLETLEWLLQK
NPQLGH
|
| Enzyme 17 Number of Residues |
2286 |
| Enzyme 17 Molecular Weight |
261521 |
| Enzyme 17 Theoretical pI |
6.35 |
| Enzyme 17 GO Classification |
| Function |
- 3'-5' exonuclease activity
- DNA binding
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- exonuclease activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- nuclease activity
- nucleic acid binding
- nucleotide binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 17 General Function |
Replication, recombination and repair |
| Enzyme 17 Specific Function |
Participates in DNA repair and in chromosomal DNA replication |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
303157  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q07864  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
DPOE1_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>6774 bp
ATGTCTCTGAGGAGCGGCGGGCGGCGGCGCGCGGACCCAGGCGCGGATGGCGAGGCCAGC
AGGGATGATGGCGCCACTTCCTCAGTTTCGGCACTCAAGCGCCTGGAACGGAGTCAGTGG
ACGGATAAGATGGATTTGCGGTTTGGTTTTGAGCGGCTGAAGGAGCCTGGTGAGAAGACA
GGCTGGCTCATTAACATGCATCCTGTGGCTTTGCCCTATAAACCGTATTTCTACATTGCG
ACCAGAAAGGGTTGTGAGCGAGAAGTTTCATCTTTTCTCTCCAAGAAGTTTCAGGGCAAA
ATTGCAAAAGTGGAGACTGTCCCCAAAGAGGATCTGGACTTGCCAAATCACTTGGTGGGT
TTGAAGCGAAATTACATCAGGCTGTCCTTCCACACTGTGGAGGATCTTGTCAAAGTGAGG
AAGGAGATCTCCCCTGCCGTGAAGAAGAACAGGGAGCAGGATCACGCCAGCGACGCGTAC
ACAGCTCTGCTTTCCAGTGTTCTGCAGAGGGGCGGTGTCATTACTGATGAAGAGGAAACC
TCTAAGAAGATAGCTGACCAGTTGGACAACATTGTGGACATGCGCGAGTACGATGTTCCC
TACCACATCCGCCTCTCCATTGACCTGAAGATCCACGTGGCTCATTGGTACAATGTCAGA
TACCGAGGAAATGCTTTTCCGGTAGAAATCACCCGCCGAGATGACCTTGTTGAACGACCT
GACCCTGTGGTTTTGGCATTTGACATTGAGACGACCAAACTGCCCCTCAAGTTTCCTGAT
GCTGAGACAGACCAGATTATGATGATTTCCTACATGATCGATGGCCAGGGCTACCTCATC
ACCAACAGGGAGATTGTTTCAGAAGATATTGAAGATTTTGAGTTCACCCCCAAGCCAGAA
TATGAAGGCCCCTTTTGTGTCTTCAATGAACCCGATGAGGCTCATCTGATCCAAAGGTGG
TTTGAACACGTCCAGGAGACCAAACCCACCATCATGGTCACCTACAACGGGGACTTTTTT
GACTGGCCATTTGTGGAGGCCCGGGCAGCAGTCCACGGTCTGAGCATGCAGCAGGAGATA
GGCTTCCAGAAGGACAGCCAGGGGGAGTACAAGGCGCCCCAGTGCATCCACATGGACTGC
CTCAGGTGGGTGAAGAGGGACAGTTACCTTCCTGTGGGCAGTCATAATCTCAAGGCGGCC
GCAAGCAAGCTAGGCTATGATCCCGTGGAGCTAGACCCGGAGACATGTGCCGGATCGACG
GAGCAGCCCCAGACTCTGGCCACGTATTCTGTGTCAGATGCTGTCGCCACTTACTACCTG
TACATGAAGTACGTCCACCCATTCATCTTTGCTCTGTGCACCATTATTCCCATGGAGCCC
GACGAGGTGCTGCGGAAGGGCTCTGGCACTCTGTGTGAGGCCTTGCTGATGGTGCAGGCC
TTCCACGCCAACATCATCTTCCCCAACAAGCAAGAGCAGGAGTTCAATAAGCTGACGGAC
GACGGACACGTGCTGGACTCTGAGACCTACGTCGGGGGCCACGTGGAGGCCCTCGAGTCT
GGGGTTTTCCGCAGCGATATCCCTTGCCGGTTTAGGATGAATCCTGCCGCCTTTGACTTC
CTGCTGCAGCGGGTTGAGAAGACCTTGCGCCACGCCCTTGAGGAAGAGGAGAAAGTGCCT
GTGGAGCAAGTCACCAACTTTGAAGAGGTGTGTGATGAGATTAAGAGCAAGCTTGCCTCC
CTGAAGGACGTTCCCAGCCGCATCGAGTGTCCACTCATCTACCACCTGGACGTGGGGGCC
ATGTACCCCAACATCATCCTGACCAACCGCCTGCAGCCCTCTGCCATGGTGGACGAAGCC
ACCTGTGCTGCCTGTGACTTCAATAAGCCTGGAGCAAACTGCCAGCGGAAGATGGCCTGG
CAGTGGAGGGGCGAGTTCATGCCAGCCAGTCGCAGCGAATACCATCGGATCCAGCACCAG
CTGGAGTCAGAGAAGTTCCCCCCCTTGTTCCCAGAGGGGCCAGCTCGGGCCTTTCATGAA
CTGTCCCGCGAGGAACAGGCGAAATACGAGAAGAGAAGGCTGGCGGATTACTGCCGGAAA
GCCTACAAGAAGATCCACATCACCAAGGTGGAAGAGCGTCTCACCACCATCTGCCAGCGG
GAAAACTCCTTCTACGTGGACACCGTGCGTGCCTTCCGGGACAGGCGTTACGAGTTCAAA
GGGCTCCACAAGGTGTGGAAAAAGAAGCTCTCGGCGGCCGTGGAGGTGGGCGACGCGGCT
GAGGTGAAGCGCTGCAAGAACATGGAGGTGCTGTATGACTCGCTGCAGCTGGCCCACAAG
TGCATCCTGAACTCCTTCTATGGCTATGTCATGCGCAAGGGGGCTCGCTGGTACTCCATG
GAGATGGCTGGCATCGTCTGCTTCACAGGGGCCAACATCATCACCCAGGCACGGGAGCTG
ATCGAGCAGATTGGGAGGCCCTTAGAGCTGGACACAGATGGTATATGGTGCGTCCTGCCC
AACAGCTTCCCAGAAAATTTTGTCTTCAAGACGACCAATGTGAAGAAGCCCAAAGTGACC
ATCTCCTACCCAGGCGCCATGTTGAACATCATGGTCAAGGAAGGCTTCACCAATGACCAG
TACCAGGAGCTGGCTGAGCCGTCCTCACTCACCTACGTCACCCGCTCAGAGAACAGCATC
TTTTTTGAGGTTGATGGGCCCTACCTTGCCATGATTCTTCCAGCCTCCAAGGAAGAAGGC
AAGAAATTGAAGAAGAGGTATGCTGTGTTCAATGAAGACGGTTCTCTGGCTGAGCTCAAG
GGCTTTGAGGTCAAACGCCGCGGGGAACTGCAGCTGATTAAGATCTTCCAATCCTCGGTG
TTTGAGGCCTTCCTCAAGGGCAGCACGCTGGAAGAGGTGTATGGCTCTGTAGCCAAGGTG
GCTGACTACTGGCTGGACGTGCTGTACAGCAAGGCAGCCAACATGCCTGACTCTGAGCTA
TTCGAGCTCATCTCTGAGAACCGTTCCATGTCTCGGAAGCTGGAAGATTACGGGGAGCAG
AAGTCTACGTCCATCAGCACAGCAAAGCGCCTGGCCGAGTTCCTGGGAGACCAGATGGTC
AAGGATGCAGGGCTGAGTTGCCGCTACATCATCTCCCGCAACGCCGAGGGCTCCCCTGTC
ACGGAGAGGGCCATCCCACTTGCCATTTTCCAAGCAGAGCCCACGGTGAGGAAGCACTTT
CTCCGGAAATGGCTCAAGAGCTCTTCCCTTCAAGACTTTGATATTCGAGCAATTCTGGAT
TGGGACTACTACATTGAGCGGCTGGGAAGCGCCATCCAGAAGATCATCACCATCCCTGCG
GCCCTGCAGCAGGTAAAGAACCCAGTGCCACGTGTCAAACACCCCGACTGGCTGCACAAA
AAACTGCTGGAGAAGAATGATGTCTACAAGCAGAAGAAGATCAGTGAGCTCTTCACCCTG
GAGGGCAGGAGACAGGTCACGATGGCCGAGGCCTCAGAAGACAGTCCGAGGCCAAGTGCT
CCTGACATGGAGGACTTCGGCCTCGTAAAGCTGCCTCACCCAGCAGCCCCTGTCACTGTG
AAGAGGAAGCGAGTTCTTTGGGAGAGCCAGGAGGAGTCCCAGGACCTCACGCCGACTGTG
CCCTGGCAGGAAATCTTGGGGCAGCCTCCCGCCCTGGGAACCAGCCAGGAGGAATGGCTT
GTCTGGCTCCGGTTCCACAAGAAGAAGTGGCAGCTGCAGGCCCGGCAGCGCCTCGCCCGC
AGGAAGAGGCAGCGTCTGGAGTCGGCAGAGGGTGTGCTCAGGCCCGGGGCCATCCGGGAT
GGTCCTGCCACGGGGCTGGGGAGCTTCTTGCGAAGAACTGCCCGCAGCATCCTGGACCTT
CCGTGGCAGATTGTGCAGATCAGCGAGACCAGCCAGGCCGGCCTGTTCAGGCTGTGGGCG
CTCGTTGGCAGTGACTTGCACTGCATCAGGCTGAGCATCCCCCGTGTGTTCTACGTGAAC
CAGCGAGTGCCTAAAGCGGAGGAGGGTGCTTCGTATCGCAAGGTAAATCGGGTCCTTCCT
CGCTCCAACATGGTCTACAATCTCTATGAGTATTCAGTGCCAGAGGACATGTACCAGGAA
CACATCAACGAGATCAACGCTGAGCTGTCAGCGCCAGACATCGAGGGCGTATATGAGACT
CAGGTTCCGTTACTGTTCCGGGCCCTGGTGCACCTGGGCTGTGTGTGTGTGGTCAATAAA
CAGCTGGTGAGGCACCTTTCAGGCTGGGAAGCAGAGACCTTTGCTCTTGAGCACCTGGAG
ATGCGCTCTCTGGCCCAGTTCAGCTACCTGGAACCAGGGAGTATCCGCCATATCTACCTG
TACCACCACGCACAGGCCCACAAAGCGCTCTTCGGGATCTTCATCCCCTCACAGCGCAGG
GCATCCGTCTTTGTGCTGGACACTGTGCGCACAGACCAGATGCCCAGCCTTGGCGCCCTG
TACTCAGCAGAGCACGGCCTCCTCCTGGAGAAGGTGGGCCCTGAGCTCCTGCCACCCCCC
AAACACACCTTCGAAGTTCGGGCAGAAACTGACCTGAAGACCATCTGCAGAGCCATCCAG
CGATTCCTGCTCGCCTACAAGGAGGAGCGCCGGGGGCCCACACTCATCGCTGTTCAGTCC
AGCTGGGAGCTGAAGAGGCTGGCCAGTGAAATTCCTGTCTTGGAGGAATTCCCACTGGTG
CCTATCTGTGTGGCTGACAAGATCAACTATGGGGTCCTGGACTGGCAGCGCCATGGAGCC
CGGCGCATGATCCGTCACTACCTCAACCTGGACACCTGCCTGTCGCAGGCCTTCGAGATG
AGCAGGTACTTTCACATTCCCATTGGGAACCTACCAGAGGACATCTCCACATTCGGCTCC
GACCTCTTCTTTGCCCGCCACCTCCAGCGCCACAACCACCTGCTCTGGCTGTCCCCTACA
GCCCGCCCTGACCTGGGTGGAAAGGAGGCTGATGACAACTGTCTTGTCATGGAGTTCGAT
GACCAAGCCACTGTTGAGATCAACAGTTCAGGCTGTTACTCCACAGTGTGTGTGGAGCTG
GACCTTCAGAACCTGGCCGTCAACACCATTCTCCAGTCTCACCATGTCAACGACATGGAG
GGGGCCGACAGCATGGGGATCAGCTTCGACGTGATCCAGCAGGCCTCCCTGGAGGACATG
ATCACGGGTGGTCAGGCTGCCAGTGCCCCGGCCAGCTACGATGAGACAGCCCTGTGCTCT
AACACCTTCAGGATCCTGAAGAGCATGGTCGTGGGCTGGGTGAAGGAGATCACCCAGTAC
CACAACATCTATGCAGACAACCAGGTGATGCACTTCTACCGCTGGCTTCGGTCGCCATCC
TCTCTGCTTCATGACCCTGCCCTGCACCGCACACTCCACAACATGATGAAGAAGCTCTTC
CTGCAGCTCATCGCTGAGTTCAAGCGCCTGGGGTCATCAGTCATCTACGCCAACTTCAAC
CGCATCATCCTCTGTACAAAGAAGCGCCGTGTGGAAGATGCCATCGCTTACGTGGAGTAC
ATCACCAGCAGCATCCATTCAAAGGAGACCTTCCATTCTCTGACAATTTCTTTCTCTCGA
TGCTGGGAATTTCTTCTCTGGATGGATCCATCTAACTATGGCGGAATCAAAGGAAAAGTT
TCATCTCGTATTCACTGTGGACTGCAAGACTCCCAGAAAGCAGGGGGAGCAGAGGATGAG
CAGGAAAATGAGGACGATGAGGAGGAAAGAGATGGGGAGGAGGAGGAAGAGGCGGAGGAA
TCCAACGTGGAGGATTTACTGGAAAACAACTGGAACATTTTGCAGTTTTTGCCACAGGCA
GCCTCCTGCCAGAACTACTTCCTCATGATTGTTTCAGCGTACATCGTGGCCGTGTACCAC
TGCATGAAGGACGGGCTGAGGCGCAGTGCTCCAGGGAGCACCCCCGTGAGGAGGAGGGGG
GCCAGCCAGCTCTCCCAGGAGGCCGAGGGGGCGGTCGGAGCCCTTCCCGGAATGATCACC
TTCTCTCAGGATTATGTCGCAAATGAGCTCACTCAGAGCTTCTTCACCATCACTCAGAAG
ATTCAGAAGAAAGTCACAGGCTCTCGGAACTCCACTGAGCTCTCAGAGATGTTTCCTGTC
CTCCCCGGTTCCCACTTGCTGCTCAATAACCCTGCCCTGGAGTTCATCAAATACGTGTGC
AAGGTGCTGTCCCTGGACACCAACATCACAAACCAGGTGAATAAGCTGAACCGAGACCTG
CTTCGCCTGGTGGATGTCGGCGAGTTCTCCGAGGAGGCCCAGTTCCGAGACCCCTGCCGC
TCCTACGTGCTTCCTGAGGTCATCTGCCGCAGCTGTAACTTCTGCCGCGACCTGGACCTG
TGTAAAGACTCTTCCTTCTCAGAGGATGGGGCGGTCCTGCCTCAGTGGCTCTGCTCCAAC
TGTCAGGCGCCCTACGACTCCTCTGCCATCGAGATGACGCTGGTGGAAGTTCTACAGAAG
AAGCTGATGGCCTTCACCCTGCAGGACCTGGTCTGCCTGAAGTGCCGCGGGGTGAAGGAG
ACCAGCATGCCTGTGTACTGCACGTGCGCGGGAGACTTCGCCCTCACCATCCACACCCAG
GTCTTCATGGAACAGATCGGAATATTCCGGAACATTGCCCAGCACTACGGCATGTCGTAC
CTCCTGGAGACCCTGGAGTGGCTGCTGCAGAAGAACCCACAGCTGGGCCATTAG
|
| Enzyme 17 GenBank Gene ID |
S60080  |
| Enzyme 17 GeneCard ID |
POLE  |
| Enzyme 17 GenAtlas ID |
POLE  |
| Enzyme 17 HGNC ID |
HGNC:9177  |
| Enzyme 17 Chromosome Location |
12 |
| Enzyme 17 Locus |
12q24.3 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Kesti T, Frantti H, Syvaoja JE: Molecular cloning of the cDNA for the catalytic subunit of human DNA polymerase epsilon. J Biol Chem. 1993 May 15;268(14):10238-45. [PubMed
]
- Post SM, Tomkinson AE, Lee EY: The human checkpoint Rad protein Rad17 is chromatin-associated throughout the cell cycle, localizes to DNA replication sites, and interacts with DNA polymerase epsilon. Nucleic Acids Res. 2003 Oct 1;31(19):5568-75. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
6252 |
| Enzyme 18 Name |
DNA polymerase mu |
| Enzyme 18 Synonyms |
- Pol Mu
|
| Enzyme 18 Gene Name |
POLM |
| Enzyme 18 Protein Sequence |
>DNA polymerase mu
MLPKRRRARVGSPSGDAASSTPPSTRFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLD
ACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWLTESLGAGQPVPVECR
HRLEVAGPRKGPLSPAWMPAYACQRPTPLTHHNTGLSEALEILAEAAGFEGSEGRLLTFC
RAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRSERYQTMKLF
TQIFGVGVKTADRWYREGLRTLDDLREQPQKLTQQQKAGLQHHQDLSTPVLRSDVDALQQ
VVEEAVGQALPGATVTLTGGFRRGKLQGHDVDFLITHPKEGQEAGLLPRVMCRLQDQGLI
LYHQHQHSCCESPTRLAQQSHMDAFERSFCIFRLPQPPGAAVGGSTRPCPSWKAVRVDLV
VAPVSQFPFALLGWTGSKLFQRELRRFSRKEKGLWLNSHGLFDPEQKTFFQAASEEDIFR
HLGLEYLPPEQRNA
|
| Enzyme 18 Number of Residues |
494 |
| Enzyme 18 Molecular Weight |
54816 |
| Enzyme 18 Theoretical pI |
8.50 |
| Enzyme 18 GO Classification |
| Function |
- DNA binding
- DNA nucleotidylexotransferase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
|
|
| Enzyme 18 General Function |
Replication, recombination and repair |
| Enzyme 18 Specific Function |
Seems to act as an Ig mutase which is responsible for immunoglobulin (Ig) gene hypermutation |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 18 Pfam Domain Function |
Not Available |
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
6822168  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q9NP87  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
DPOLM_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>1485 bp
ATGCTCCCCAAACGGCGGCGAGCGCGGGTCGGGTCCCCTAGCGGCGATGCCGCTTCCTCC
ACGCCGCCCTCGACGCGCTTCCCGGGAGTCGCCATCTACCTGGTCGAGCCTCGCATGGGT
CGCAGCCGCCGGGCCTTCCTCACAGGCCTGGCGCGCTCCAAAGGCTTCCGCGTCCTTGAC
GCCTGCAGCTCCGAAGCGACACATGTTGTGATGGAAGAGACCTCAGCAGAGGAGGCCGTC
AGCTGGCAGGAGCGCAGGATGGCAGCTGCTCCCCCGGGTTGCACCCCCCCAGCTCTGCTG
GACATAAGCTGGTTAACAGAGAGCCTGGGAGCTGGGCAGCCTGTACCTGTGGAGTGCCGG
CACCGCCTGGAGGTGGCTGGGCCAAGGAAGGGGCCTCTGAGCCCAGCATGGATGCCTGCC
TATGCCTGCCAGCGCCCTACGCCCCTCACACACCACAACACTGGCCTCTCCGAGGCTCTG
GAGATACTGGCCGAGGCAGCAGGCTTTGAAGGCAGTGAGGGCCGCCTCCTCACCTTCTGC
AGAGCAGCCTCGGTGCTCAAGGCCCTTCCCAGCCCTGTCACAACCCTGAGCCAGCTGCAG
GGGCTTCCCCACTTTGGAGAACACTCCTCTAGGGTTGTCCAGGAGCTGCTGGAGCATGGA
GTGTGTGAGGAGGTGGAGAGAGTTCGGCGCTCAGAGAGGTACCAGACCATGAAGCTCTTC
ACCCAGATCTTCGGGGTCGGTGTGAAGACTGCTGACCGGTGGTACCGGGAAGGACTGCGA
ACCTTAGATGACCTCCGAGAGCAGCCCCAGAAACTAACCCAACAGCAGAAAGCGGGGCTC
CAGCACCACCAGGACCTGAGCACCCCAGTCCTGCGGTCCGATGTAGATGCCCTGCAGCAG
GTGGTGGAGGAAGCTGTGGGGCAGGCCCTGCCTGGGGCCACCGTCACGCTGACCGGCGGC
TTCCGCAGGGGGAAGTTGCAGGGCCATGACGTGGACTTCCTCATCACCCACCCCAAGGAG
GGTCAGGAGGCGGGGCTGCTGCCTAGAGTGATGTGCCGCCTGCAGGACCAGGGCCTCATC
CTGTACCACCAGCACCAGCACAGCTGCTGTGAGTCCCCTACCCGCCTGGCCCAACAGAGC
CACATGGACGCTTTTGAGAGAAGTTTCTGCATTTTCCGCCTACCACAACCTCCAGGGGCT
GCTGTGGGGGGATCCACGAGGCCCTGCCCATCCTGGAAGGCCGTGAGAGTGGACTTGGTA
GTTGCACCCGTCAGCCAGTTCCCTTTCGCCCTGCTCGGTTGGACTGGCTCCAAGCTTTTC
CAGCGGGAGCTGCGCCGCTTCAGCCGGAAGGAGAAGGGCCTGTGGCTGAACAGCCATGGG
CTGTTTGACCCGGAGCAGAAGACATTTTTCCAAGCGGCTTCAGAGGAAGACATCTTCAGA
CACCTGGGCCTTGAGTACCTTCCTCCAGAGCAGAGAAACGCCTGA
|
| Enzyme 18 GenBank Gene ID |
AJ131891  |
| Enzyme 18 GeneCard ID |
POLM  |
| Enzyme 18 GenAtlas ID |
POLM  |
| Enzyme 18 HGNC ID |
HGNC:9185  |
| Enzyme 18 Chromosome Location |
7 |
| Enzyme 18 Locus |
7p13 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Dominguez O, Ruiz JF, Lain de Lera T, Garcia-Diaz M, Gonzalez MA, Kirchhoff T, Martinez-A C, Bernad A, Blanco L: DNA polymerase mu (Pol mu), homologous to TdT, could act as a DNA mutator in eukaryotic cells. EMBO J. 2000 Apr 3;19(7):1731-42. [PubMed
]
- Aoufouchi S, Flatter E, Dahan A, Faili A, Bertocci B, Storck S, Delbos F, Cocea L, Gupta N, Weill JC, Reynaud CA: Two novel human and mouse DNA polymerases of the polX family. Nucleic Acids Res. 2000 Sep 15;28(18):3684-93. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
6254 |
| Enzyme 19 Name |
DNA polymerase epsilon subunit 3 |
| Enzyme 19 Synonyms |
- DNA polymerase II subunit 3
- DNA polymerase epsilon subunit p17
- Chromatin accessibility complex 17
- HuCHRAC17
- CHRAC-17
- Arsenic- transactivated protein
- AsTP
|
| Enzyme 19 Gene Name |
POLE3 |
| Enzyme 19 Protein Sequence |
>DNA polymerase epsilon subunit 3
MAERPEDLNLPNAVITRIIKEALPDGVNISKEARSAISRAASVFVLYATSCANNFAMKGK
RKTLNASDVLSAMEEMEFQRFVTPLKEALEAYRREQKGKKEASEQKKKDKDKKTDSEEQD
KSRDEDNDEDEERLEEEEQNEEEEVDN
|
| Enzyme 19 Number of Residues |
147 |
| Enzyme 19 Molecular Weight |
16860 |
| Enzyme 19 Theoretical pI |
4.38 |
| Enzyme 19 GO Classification |
| Function |
- DNA binding
- binding
- nucleic acid binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 19 General Function |
Chromatin structure and dynamics |
| Enzyme 19 Specific Function |
Forms a complex with DNA polymerase epsilon subunit CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodelling activity of ISWI/SNF2H and ACF1 |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
8100806  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9NRF9  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
DPOE3_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>444 bp
ATGGCGGAGAGGCCCGAGGACCTAAACCTGCCCAATGCCGTGATCACCAGGATCATCAAG
GAGGCGCTCCCGGACGGTGTCAACATCTCCAAGGAGGCCCGGAGCGCCATCTCCCGCGCC
GCCAGCGTCTTCGTGCTGTACGCCACATCCTGTGCTAACAACTTTGCAATGAAAGGAAAG
CGGAAGACGCTGAATGCCAGTGATGTGCTCTCAGCCATGGAAGAGATGGAGTTCCAGCGG
TTCGTTACCCCATTGAAAGAAGCTCTGGAAGCATATAGGCGGGAGCAGAAAGGCAAGAAG
GAGGCCTCAGAGCAAAAGAAGAAGGACAAAGACAAAAAAACAGACTCGGAAGAGCAAGAC
AAGAGCAGGGATGAGGACAATGATGAAGACGAAGAAAGGCTGGAAGAAGAAGAACAGAAT
GAAGAGGAAGAAGTAGACAACTGA
|
| Enzyme 19 GenBank Gene ID |
AF226077  |
| Enzyme 19 GeneCard ID |
POLE3  |
| Enzyme 19 GenAtlas ID |
POLE3  |
| Enzyme 19 HGNC ID |
HGNC:13546  |
| Enzyme 19 Chromosome Location |
9 |
| Enzyme 19 Locus |
9q33 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Poot RA, Dellaire G, Hulsmann BB, Grimaldi MA, Corona DF, Becker PB, Bickmore WA, Varga-Weisz PD: HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1 and two novel histone-fold proteins. EMBO J. 2000 Jul 3;19(13):3377-87. [PubMed
]
- Li Y, Pursell ZF, Linn S: Identification and cloning of two histone fold motif-containing subunits of HeLa DNA polymerase epsilon. J Biol Chem. 2000 Jul 28;275(30):23247-52. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
6256 |
| Enzyme 20 Name |
DNA polymerase subunit gamma 1 |
| Enzyme 20 Synonyms |
- Mitochondrial DNA polymerase catalytic subunit
- PolG-alpha
|
| Enzyme 20 Gene Name |
POLG |
| Enzyme 20 Protein Sequence |
>DNA polymerase subunit gamma 1
MSRLLWRKVAGATVGPGPVPAPGRWVSSSVPASDPSDGQRRRQQQQQQQQQQQQQPQQPQ
VLSSEGGQLRHNPLDIQMLSRGLHEQIFGQGGEMPGEAAVRRSVEHLQKHGLWGQPAVPL
PDVELRLPPLYGDNLDQHFRLLAQKQSLPYLEAANLLLQAQLPPKPPAWAWAEGWTRYGP
EGEAVPVAIPEERALVFDVEVCLAEGTCPTLAVAISPSAWYSWCSQRLVEERYSWTSQLS
PADLIPLEVPTGASSPTQRDWQEQLVVGHNVSFDRAHIREQYLIQGSRMRFLDTMSMHMA
ISGLSSFQRSLWIAAKQGKHKVQPPTKQGQKSQRKARRGPAISSWDWLDISSVNSLAEVH
RLYVGGPPLEKEPRELFVKGTMKDIRENFQDLMQYCAQDVWATHEVFQQQLPLFLERCPH
PVTLAGMLEMGVSYLPVNQNWERYLAEAQGTYEELQREMKKSLMDLANDACQLLSGERYK
EDPWLWDLEWDLQEFKQKKAKKVKKEPATASKLPIEGAGAPGDPMDQEDLGPCSEEEEFQ
QDVMARACLQKLKGTTELLPKRPQHLPGHPGWYRKLCPRLDDPAWTPGPSLLSLQMRVTP
KLMALTWDGFPLHYSERHGWGYLVPGRRDNLAKLPTGTTLESAGVVCPYRAIESLYRKHC
LEQGKQQLMPQEAGLAEEFLLTDNSAIWQTVEELDYLEVEAEAKMENLRAAVPGQPLALT
ARGGPKDTQPSYHHGNGPYNDVDIPGCWFFKLPHKDGNSCNVGSPFAKDFLPKMEDGTLQ
AGPGGASGPRALEINKMISFWRNAHKRISSQMVVWLPRSALPRAVIRHPDYDEEGLYGAI
LPQVVTAGTITRRAVEPTWLTASNARPDRVGSELKAMVQAPPGYTLVGADVDSQELWIAA
VLGDAHFAGMHGCTAFGWMTLQGRKSRGTDLHSKTATTVGISREHAKIFNYGRIYGAGQP
FAERLLMQFNHRLTQQEAAEKAQQMYAATKGLRWYRLSDEGEWLVRELNLPVDRTEGGWI
SLQDLRKVQRETARKSQWKKWEVVAERAWKGGTESEMFNKLESIATSDIPRTPVLGCCIS
RALEPSAVQEEFMTSRVNWVVQSSAVDYLHLMLVAMKWLFEEFAIDGRFCISIHDEVRYL
VREEDRYRAALALQITNLLTRCMFAYKLGLNDLPQSVAFFSAVDIDRCLRKEVTMDCKTP
SNPTGMERRYGIPQGEALDIYQIIELTKGSLEKRSQPGP
|
| Enzyme 20 Number of Residues |
1239 |
| Enzyme 20 Molecular Weight |
139564 |
| Enzyme 20 Theoretical pI |
6.89 |
| Enzyme 20 GO Classification |
| Function |
- DNA binding
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- gamma DNA-directed DNA polymerase activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
- gamma DNA polymerase complex
- protein complex
|
|
| Enzyme 20 General Function |
Replication, recombination and repair |
| Enzyme 20 Specific Function |
Involved in the replication of mitochondrial DNA |
| Enzyme 20 Pathways |
|
| Enzyme 20 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
1399956  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
P54098  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
DPOG1_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>3720 bp
ATGAGCCGCCTGCTCTGGAGGAAGGTGGCCGGCGCCACCGTCGGGCCAGGGCCGGTTCCA
GCTCCGGGGCGCTGGGTCTCCAGCTCCGTCCCCGCGTCCGACCCCAGCGACGGGCAGCGG
CGGCGGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAACAGCAGCCTCAGCAGCCGCAA
GTGCTATCCTCGGAGGGCGGGCAGCTGCGGCACAACCCATTGGACATCCAGATGCTCTCG
AGAGGGCTGCACGAGCAAATCTTCGGGCAAGGAGGGGAGATGCCTGGCGAGGCCGCGGTG
CGCCGCAGCGTCGAGCACCTGCAGAAGCACGGGCTCTGGGGGCAGCCAGCCGTGCCCTTG
CCCGACGTGGAGCTGCGCCTGCCGCCCCTCTACGGGGACAACCTGGACCAGCACTTCCGC
CTCCTGGCCCAGAAGCAGAGCCTGCCCTACCTGGAGGCGGCCAACTTGCTGTTGCAGGCC
CAGCTGCCCCCGAAGCCCCCGGCTTGGGCCTGGGCGGAGGGCTGGACCCGGTACGGCCCC
GAGGGGGAGGCCGTACCCGTGGCCATCCCCGAGGAGCGGGCCCTGGTGTTCGACGTGGAG
GTCTGCTTGGCAGAGGGAACTTGCCCCACATTGGCGGTGGCCATATCCCCCTCGGCCTGG
TATTCCTGGTGCAGCCAGCGGCTGGTGGAAGAGCGTTACTCTTGGACCAGCCAGCTGTCG
CCGGCTGACCTCATCCCCCTGGAGGTCCCTACTGGTGCCAGCAGCCCCACCCAGAGAGAC
TGGCAGGAGCAGTTAGTGGTGGGGCACAATGTTTCCTTTGACCGAGCTCATATCAGGGAG
CAGTACCTGATCCAGGGTTCCCGCATGCGTTTCCTGGACACCATGAGCATGCACATGGCC
ATCTCAGGGCTAAGCAGCTTCCAGCGCAGTCTGTGGATAGCAGCCAAGCAGGGCAAACAC
AAGGTCCAGCCCCCCACAAAGCAAGGCCAGAAGTCCCAGAGGAAAGCCAGAAGAGGCCCA
GCGATCTCATCCTGGGACTGGCTGGACATCAGCAGTGTCAACAGTCTGGCAGAGGTGCAC
AGACTTTATGTAGGGGGGCCTCCCTTAGAGAAGGAGCCTCGAGAACTGTTTGTGAAGGGC
ACCATGAAGGACATTCGTGAGAACTTCCAGGACCTGATGCAGTACTGTGCCCAGGACGTG
TGGGCCACCCATGAGGTTTTCCAGCAGCAGCTACCGCTCTTCTTGGAGAGGTGTCCCCAC
CCAGTGACTCTGGCCGGCATGCTGGAGATGGGTGTCTCCTACCTGCCTGTCAACCAGAAC
TGGGAGCGTTACCTGGCAGAGGCACAGGGCACTTATGAGGAGCTCCAGCGGGAGATGAAG
AAGTCGTTGATGGATCTGGCCAATGATGCCTGCCAGCTGCTCTCAGGAGAGAGGTACAAA
GAAGACCCCTGGCTCTGGGACCTGGAGTGGGACCTGCAAGAATTTAAGCAGAAGAAAGCT
AAGAAGGTGAAGAAGGAACCAGCCACAGCCAGCAAGTTGCCCATCGAGGGGGCTGGGGCC
CCTGGTGATCCCATGGATCAGGAAGACCTCGGCCCCTGCAGTGAGGAGGAGGAGTTTCAA
CAAGATGTCATGGCCCGCGCCTGCTTGCAGAAGCTGAAGGGGACCACAGAGCTCCTGCCC
AAGCGGCCCCAGCACCTTCCTGGACACCCTGGATGGTACCGGAAGCTCTGCCCCCGGCTA
GACGACCCTGCATGGACCCCGGGCCCCAGCCTCCTCAGCCTGCAGATGCGGGTCACACCT
AAACTCATGGCACTTACCTGGGATGGCTTCCCTCTGCACTACTCAGAGCGTCATGGCTGG
GGCTACTTGGTGCCTGGGCGGCGGGACAACCTGGCCAAGCTGCCGACAGGTACCACCCTG
GAGTCAGCTGGGGTGGTCTGCCCCTACAGAGCCATCGAGTCCCTGTACAGGAAGCACTGT
CTCGAACAGGGGAAGCAGCAGCTGATGCCCCAGGAGGCCGGCCTGGCGGAGGAGTTCCTG
CTCACTGACAATAGTGCCATATGGCAAACGGTAGAAGAACTGGATTACTTAGAAGTGGAG
GCTGAGGCCAAGATGGAGAACTTGCGAGCTGCAGTGCCAGGTCAACCCCTAGCTCTGACT
GCCCGTGGTGGCCCCAAGGACACCCAGCCCAGCTATCACCATGGCAATGGACCTTACAAC
GACGTGGACATCCCTGGCTGCTGGTTTTTCAAGCTGCCTCACAAGGATGGTAATAGCTGT
AATGTGGGAAGCCCCTTTGCCAAGGACTTCCTGCCCAAGATGGAGGATGGCACCCTGCAG
GCTGGCCCAGGAGGTGCCAGTGGGCCCCGTGCTCTGGAAATCAACAAAATGATTTCTTTC
TGGAGGAACGCCCATAAACGTATCAGCTCCCAGATGGTGGTGTGGCTGCCCAGGTCAGCT
CTGCCCCGTGCTGTGATCAGGCACCCCGACTATGATGAGGAAGGCCTCTATGGGGCCATC
CTGCCCCAAGTGGTGACTGCCGGCACCATCACTCGCCGGGCTGTGGAGCCCACATGGCTC
ACCGCCAGCAATGCCCGGCCTGACCGAGTAGGCAGTGAGTTGAAAGCCATGGTGCAGGCC
CCACCTGGCTACACCCTTGTGGGTGCTGATGTGGACTCCCAAGAGCTGTGGATTGCAGCT
GTGCTTGGAGACGCCCACTTTGCCGGCATGCATGGCTGCACAGCCTTTGGGTGGATGACA
CTGCAGGGCAGGAAGAGCAGGGGCACTGATCTACACAGTAAGACAGCCACTACTGTGGGC
ATCAGCCGTGAGCATGCCAAAATCTTCAACTACGGCCGCATCTATGGTGCTGGGCAGCCC
TTTGCTGAGCGCTTACTAATGCAGTTTAACCACCGGCTCACACAGCAGGAGGCAGCTGAG
AAGGCCCAGCAGATGTACGCTGCCACCAAGGGCCTCCGCTGGTATCGGCTGTCGGATGAG
GGCGAGTGGCTGGTGAGGGAGTTGAACCTCCCAGTGGACAGGACTGAGGGTGGCTGGATT
TCCCTGCAGGATCTGCGCAAGGTCCAGAGAGAAACTGCAAGGAAGTCACAGTGGAAGAAG
TGGGAGGTGGTTGCTGAACGGGCATGGAAGGGGGGCACAGAGTCAGAAATGTTCAATAAG
CTTGAGAGCATTGCTACGTCTGACATACCACGTACCCCGGTGCTGGGCTGCTGCATCAGC
CGAGCCCTGGAGCCCTCGGCTGTCCAGGAAGAGTTTATGACCAGCCGTGTGAATTGGGTG
GTACAGAGCTCTGCTGTTGACTACTTACACCTCATGCTTGTGGCCATGAAGTGGCTGTTT
GAAGAGTTTGCCATAGATGGGCGCTTCTGCATCAGCATCCATGACGAGGTTCGCTACCTG
GTGCGGGAGGAGGACCGCTACCGCGCTGCCCTGGCCTTGCAGATCACCAACCTCTTGACC
AGGTGCATGTTTGCCTACAAGCTGGGTCTGAATGACTTGCCCCAGTCAGTCGCCTTTTTC
AGTGCAGTCGATATTGACCGGTGCCTCAGGAAGGAAGTGACCATGGATTGTAAAACCCCT
TCCAACCCAACTGGGATGGAAAGGAGATACGGGATTCCCCAGGGTGAAGCGCTGGATATT
TACCAGATAATTGAACTCACCAAAGGCTCCTTGGAAAAACGAAGCCAGCCTGGACCATAG
|
| Enzyme 20 GenBank Gene ID |
U60325  |
| Enzyme 20 GeneCard ID |
POLG  |
| Enzyme 20 GenAtlas ID |
POLG  |
| Enzyme 20 HGNC ID |
HGNC:9179  |
| Enzyme 20 Chromosome Location |
15 |
| Enzyme 20 Locus |
15q25 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Ropp PA, Copeland WC: Cloning and characterization of the human mitochondrial DNA polymerase, DNA polymerase gamma. Genomics. 1996 Sep 15;36(3):449-58. [PubMed
]
- Lecrenier N, Van Der Bruggen P, Foury F: Mitochondrial DNA polymerases from yeast to man: a new family of polymerases. Gene. 1997 Jan 31;185(1):147-52. [PubMed
]
- Van Goethem G, Dermaut B, Lofgren A, Martin JJ, Van Broeckhoven C: Mutation of POLG is associated with progressive external ophthalmoplegia characterized by mtDNA deletions. Nat Genet. 2001 Jul;28(3):211-2. [PubMed
]
- Van Goethem G, Martin JJ, Dermaut B, Lofgren A, Wibail A, Ververken D, Tack P, Dehaene I, Van Zandijcke M, Moonen M, Ceuterick C, De Jonghe P, Van Broeckhoven C: Recessive POLG mutations presenting with sensory and ataxic neuropathy in compound heterozygote patients with progressive external ophthalmoplegia. Neuromuscul Disord. 2003 Feb;13(2):133-42. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
6257 |
| Enzyme 21 Name |
DNA polymerase iota |
| Enzyme 21 Synonyms |
- RAD30 homolog B
- Eta2
|
| Enzyme 21 Gene Name |
POLI |
| Enzyme 21 Protein Sequence |
>DNA polymerase iota
MELADVGAAASSQGVHDQVLPTPNASSRVIVHVDLDCFYAQVEMISNPELKDKPLGVQQK
YLVVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGEDLTRYREMSYKVTELLEEFSPVV
ERLGFDENFVDLTEMVEKRLQQLQSDELSAVTVSGHVYNNQSINLLDVLHIRLLVGSQIA
AEMREAMYNQLGLTGCAGVASNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNHIKEIP
GIGYKTAKCLEALGINSVRDLQTFSPKILEKELGISVAQRIQKLSFGEDNSPVILSGPPQ
SFSEEDSFKKCSSEVEAKNKIEELLASLLNRVCQDGRKPHTVRLIIRRYSSEKHYGRESR
QCPIPSHVIQKLGTGNYDVMTPMVDILMKLFRNMVNVKMPFHLTLLSVCFCNLKALNTAK
KGLIDYYLMPSLSTTSRSGKHSFKMKDTHMEDFPKDKETNRDFLPSGRIESTRTRESPLD
TTNFSKEKDINEFPLCSLPEGVDQEVFKQLPVDIQEEILSGKSREKFQGKGSVSCPLHAS
RGVLSFFSKKQMQDIPINPRDHLSSSKQVSSVSPCEPGTSGFNSSSSSYMSSQKDYSYYL
DNRLKDERISQGPKEPQGFHFTNSNPAVSAFHSFPNLQSEQLFSRNHTTDSHKQTVATDS
HEGLTENREPDSVDEKITFPSDIDPQVFYELPEAVQKELLAEWKRTGSDFHIGHK
|
| Enzyme 21 Number of Residues |
715 |
| Enzyme 21 Molecular Weight |
80347 |
| Enzyme 21 Theoretical pI |
6.82 |
| Enzyme 21 GO Classification |
| Function |
- DNA binding
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- ion binding
- magnesium ion binding
- metal ion binding
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA repair
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 21 General Function |
Replication, recombination and repair |
| Enzyme 21 Specific Function |
Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunogobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
5739208  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q9UNA4  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
POLI_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>2148 bp
ATGGAACTGGCGGACGTGGGGGCGGCAGCCAGCTCGCAGGGAGTTCATGATCAAGTGTTG
CCCACACCAAATGCTTCATCCAGAGTCATAGTACATGTGGATCTGGATTGCTTTTATGCA
CAAGTAGAAATGATCTCAAATCCAGAGCTAAAAGACAAACCTTTAGGGGTTCAACAGAAA
TATTTGGTGGTTACCTGCAACTATGAAGCTAGGAAACTTGGAGTTAAGAAACTTATGAAT
GTCAGAGATGCAAAAGAAAAGTGTCCACAGTTGGTATTAGTTAATGGAGAAGACCTGACC
CGCTACAGAGAAATGTCTTATAAGGTTACAGAATTACTGGAAGAATTTAGTCCAGTTGTT
GAGAGACTTGGATTTGATGAAAATTTTGTGGATCTAACAGAAATGGTTGAGAAGAGACTA
CAGCAGCTGCAAAGTGATGAACTTTCTGCGGTGACTGTGTCGGGTCATGTATACAATAAT
CAGTCTATAAACCTGCTTGACGTCTTGCACATCAGACTACTTGTTGGATCTCAGATTGCA
GCAGAGATGCGGGAAGCCATGTATAATCAGTTGGGGCTCACTGGCTGTGCTGGAGTGGCT
TCTAATAAACTGTTGGCAAAATTAGTTTCTGGTGTCTTTAAACCAAATCAACAAACAGTC
TTATTACCTGAAAGTTGTCAACATCTTATTCATAGTTTGAATCACATAAAGGAAATACCT
GGTATTGGCTATAAAACTGCCAAATGTCTTGAAGCACTGGGTATCAATAGTGTGCGTGAT
CTCCAAACCTTTTCACCCAAAATTTTAGAAAAAGAATTAGGAATTTCAGTTGCTCAGCGT
ATCCAAAAGCTCAGTTTTGGAGAGGATAACTCCCCTGTGATACTCTCAGGACCACCTCAG
TCCTTTAGTGAAGAAGATTCATTTAAAAAATGTTCATCTGAAGTTGAAGCTAAAAATAAG
ATTGAAGAACTACTTGCTAGTCTTTTAAACAGAGTATGCCAAGATGGAAGGAAGCCTCAT
ACAGTGAGATTAATAATCCGTCGGTATTCCTCTGAGAAGCACTATGGTCGTGAGAGTCGT
CAGTGCCCTATTCCTTCACATGTAATTCAGAAATTAGGGACAGGAAATTATGATGTGATG
ACCCCAATGGTTGATATACTTATGAAACTTTTTCGAAATATGGTGAATGTGAAGATGCCA
TTTCACCTTACCCTTCTAAGTGTGTGCTTCTGCAACCTTAAAGCACTAAATACTGCTAAG
AAAGGGCTTATTGATTATTATTTAATGCCATCATTATCAACTACTTCACGCTCTGGCAAG
CACAGTTTTAAAATGAAAGACACTCATATGGAAGATTTTCCCAAAGACAAAGAAACAAAC
CGGGATTTCCTACCAAGTGGAAGAATTGAAAGTACAAGAACTAGGGAGTCTCCACTAGAT
ACCACAAATTTTTCTAAAGAAAAAGACATTAATGAATTCCCACTCTGTTCACTTCCTGAA
GGTGTTGACCAAGAAGTCTTCAAGCAGCTTCCAGTAGATATTCAAGAAGAAATCCTTTCT
GGAAAATCTAGGGAAAAATTTCAAGGGAAAGGAAGTGTGAGTTGTCCATTACATGCCTCT
AGAGGAGTATTATCTTTCTTTTCTAAAAAACAAATGCAAGATATTCCCATAAATCCTAGA
GATCATTTATCCAGTAGCAAACAGGTATCCTCTGTATCTCCTTGTGAACCGGGAACATCA
GGCTTTAATAGCAGTAGTTCTTCTTACATGTCTAGCCAAAAGGATTATTCATATTATTTA
GATAATAGATTAAAAGATGAACGAATAAGTCAAGGACCTAAAGAACCTCAAGGATTCCAC
TTTACAAATTCAAACCCTGCTGTGTCTGCTTTTCATTCATTTCCAAACTTGCAGAGTGAG
CAACTTTTCTCCAGAAACCACACTACAGATAGCCATAAGCAAACAGTAGCAACAGACTCT
CATGAAGGACTTACAGAAAATAGAGAGCCAGATTCTGTTGATGAGAAAATTACTTTCCCT
TCTGACATTGATCCTCAAGTTTTCTATGAACTACCAGAAGCAGTACAAAAGGAACTGCTG
GCAGAGTGGAAGAGAACAGGATCAGATTTCCACATTGGACATAAATAA
|
| Enzyme 21 GenBank Gene ID |
AF140501  |
| Enzyme 21 GeneCard ID |
POLI  |
| Enzyme 21 GenAtlas ID |
POLI  |
| Enzyme 21 HGNC ID |
HGNC:9182  |
| Enzyme 21 Chromosome Location |
18 |
| Enzyme 21 Locus |
18q21.1 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- McDonald JP, Rapic-Otrin V, Epstein JA, Broughton BC, Wang X, Lehmann AR, Wolgemuth DJ, Woodgate R: Novel human and mouse homologs of Saccharomyces cerevisiae DNA polymerase eta. Genomics. 1999 Aug 15;60(1):20-30. [PubMed
]
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed
]
- Tissier A, Frank EG, McDonald JP, Iwai S, Hanaoka F, Woodgate R: Misinsertion and bypass of thymine-thymine dimers by human DNA polymerase iota. EMBO J. 2000 Oct 2;19(19):5259-66. [PubMed
]
- Bebenek K, Tissier A, Frank EG, McDonald JP, Prasad R, Wilson SH, Woodgate R, Kunkel TA: 5'-Deoxyribose phosphate lyase activity of human DNA polymerase iota in vitro. Science. 2001 Mar 16;291(5511):2156-9. [PubMed
]
- Frank EG, Tissier A, McDonald JP, Rapic-Otrin V, Zeng X, Gearhart PJ, Woodgate R: Altered nucleotide misinsertion fidelity associated with poliota-dependent replication at the end of a DNA template. EMBO J. 2001 Jun 1;20(11):2914-22. [PubMed
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
6258 |
| Enzyme 22 Name |
DNA polymerase epsilon subunit 2 |
| Enzyme 22 Synonyms |
- DNA polymerase II subunit 2
- DNA polymerase epsilon subunit B
|
| Enzyme 22 Gene Name |
POLE2 |
| Enzyme 22 Protein Sequence |
>DNA polymerase epsilon subunit 2
MAPERLRSRALSAFKLRGLLLRGEAIKYLTEALQSISELELEDKLEKIINAVEKQPLSSN
MIERSVVEAAVQECSQSVDETIEHVFNIIGAFDIPRFVYNSERKKFLPLLMTNHPAPNLF
GTPRDKAEMFRERYTILHQRTHRHELFTPPVIGSHPDESGSKFQLKTIETLLGSTTKIGD
AIVLGMITQLKEGKFFLEDPTGTVQLDLSKAQFHSGLYTEACFVLAEGWFEDQVFHVNAF
GFPPTEPSSTTRAYYGNINFFGGPSNTSVKTSAKLKQLEEENKDAMFVFLSDVWLDQVEV
LEKLRIMFAGYSPAPPTCFILCGNFSSAPYGKNQVQALKDSLKTLADIICEYPDIHQSSR
FVFVPGPEDPGFGSILPRPPLAESITNEFRQRVPFSVFTTNPCRIQYCTQEITVFREDLV
NKMCRNCVRFPSSNLAIPNHFVKTILSQGHLTPLPLYVCPVYWAYDYALRVYPVPDLLVI
ADKYDPFTTTNTECLCINPGSFPRSGFSFKVFYPSNKTVEDSKLQGF
|
| Enzyme 22 Number of Residues |
527 |
| Enzyme 22 Molecular Weight |
59538 |
| Enzyme 22 Theoretical pI |
6.30 |
| Enzyme 22 GO Classification |
| Function |
- DNA binding
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 22 General Function |
Not Available |
| Enzyme 22 Specific Function |
Participates in DNA repair and in chromosomal DNA replication |
| Enzyme 22 Pathways |
|
| Enzyme 22 Reactions |
- deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
Not Available |
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
2697123  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
P56282  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
DPOE2_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>1581 bp
ATGGCGCCGGAGCGGCTGCGGAGCCGGGCGCCCTCCGCCTTCAAGTTGCGGGGCTTGCTG
CTCCGTGGTGAAGCTATTAAGTACCTCACAGAAGCTCTTCAGTCTATCAGTGAATTAGAG
CTTGAAGATAAACTGGAAAAGATAATTAATGCAGTTGAGAAGCAACCCTTGTCATCAAAC
ATGATTGAACGATCTGTGGTGGAAGCAGCAGTCCAGGAATGCAGTCAGTCTGTTGATGAA
ACTATAGAGCACGTTTTCAATATCATAGGAGCATTTGATATTCCACGCTTTGTGTACAAT
TCAGAAAGAAAAAAATTTCTTCCTCTGTTAATGACCAACCACCCTGCACCAAATTTATTT
GGAACACCAAGAGATAAAGCAGAGATGTTTCGTGAGCGATATACCATTTTGCACCAGAGG
ACCCACAGGCATGAATTATTTACTCCTCCGGTGATAGGTTCTCACCCTGATGAAAGCGGA
AGCAAATTCCAGCTTAAAACAATAGAAACCTTATTGGGTAGTACAACCAAAATCGGAGAT
GCGATTGTTCTTGGAATGATAACGCAGTTAAAAGAGGGAAAATTTTTTCTGGAAGATCCT
ACTGGAACAGTCCAACTAGACCTTAGTAAAGCTCAGTTCCATAGTGGTTTATACACAGAG
GCATGCTTTGTCTTAGCAGAAGGTTGGTTTGAAGATCAAGTGTTTCATGTCAATGCCTTT
GGATTTCCACCCACTGAGCCCTCTAGTACTACTAGGGCATACTATGGAAATATTAATTTT
TTTGGAGGTCCTTCTAATACATCTGTGAAGACTTCTGCAAAACTAAAACAGCTAGAAGAG
GAGAATAAAGATGCTATGTTTGTGTTTTTATCTGATGTTTGGTTGGACCAGGTGGAAGTA
TTGGAAAAACTTCGCATAATGTTTGCTGGTTATTCACCAGCACCTCCAACCTGCTTTATT
CTGTGTGGTAATTTTTCATCTGCACCATATGGAAAAAATCAAGTTCAAGCTTTGAAAGAT
TCCCTAAAAACTTTGGCAGATATAATATGTGAATACCCAGATATTCACCAAAGTCGTTTT
GTGTTTGTACCTGGTCCAGAGGATCCTGGATTTGGTTCCATCTTACCAAGGCCACCACTT
GCTGAAAGCATCACTAATGAATTCAGACAAAGGGTACCATTTTCAGTTTTTACTACTAAT
CCTTGCAGAATTCAGTACTGTACACAGGAAATTACTGTCTTCCGTGAAGACTTAGTAAAT
AAAATGTGCAGAAACTGCGTCCGTTTTCCTAGCAGCAATTTGGCTATTCCTAATCACTTT
GTAAAGACTATCTTATCCCAAGGACATCTGACTCCCCTACCTCTTTATGTCTGCCCAGTG
TATTGGGCATATGACTATGCTTTGAGAGTGTATCCTGTGCCCGATCTACTTGTCATTGCA
GACAAATATGATCCTTTCACTACGACAAATACCGAATGCCTCTGCATAAACCCTGGCTCT
TTTCCAAGAAGTGGATTTTCATTCAAAGTTTTTTATCCTTCTAATAAGACAGTAGAAGAT
AGCAAACTTCAAGGCTTTTGA
|
| Enzyme 22 GenBank Gene ID |
AF025840  |
| Enzyme 22 GeneCard ID |
POLE2  |
| Enzyme 22 GenAtlas ID |
POLE2  |
| Enzyme 22 HGNC ID |
HGNC:9178  |
| Enzyme 22 Chromosome Location |
14 |
| Enzyme 22 Locus |
14q21-q22 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Li Y, Asahara H, Patel VS, Zhou S, Linn S: Purification, cDNA cloning, and gene mapping of the small subunit of human DNA polymerase epsilon. J Biol Chem. 1997 Dec 19;272(51):32337-44. [PubMed
]
- Jokela M, Makiniemi M, Lehtonen S, Szpirer C, Hellman U, Syvaoja JE: The small subunits of human and mouse DNA polymerase epsilon are homologous to the second largest subunit of the yeast Saccharomyces cerevisiae DNA polymerase epsilon. Nucleic Acids Res. 1998 Feb 1;26(3):730-4. [PubMed
]
- Huang D, Jokela M, Tuusa J, Skog S, Poikonen K, Syvaoja JE: E2F mediates induction of the Sp1-controlled promoter of the human DNA polymerase epsilon B-subunit gene POLE2. Nucleic Acids Res. 2001 Jul 1;29(13):2810-21. [PubMed
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
7769 |
| Enzyme 23 Name |
Apoptotic protease-activating factor 1 |
| Enzyme 23 Synonyms |
- Apaf-1
|
| Enzyme 23 Gene Name |
APAF1 |
| Enzyme 23 Protein Sequence |
>Apoptotic protease-activating factor 1
MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMI
LKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSSSSGKDSVSGITSYVRTVLCEGGVP
QRPVVFVTRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPG
GVHWVSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAKDRLRILMLRKHPRSLL
ILDDVWDSWVLKAFDSQCQILLTTRDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVN
MKKADLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQLQNKQFKRIRKSSSYD
YEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVN
KSLLFCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQFQRYHQPHTLSPDQEDC
MYWYNFLAYHMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAV
SENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQEVDNGMLYLEWINK
KNITNLSRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEV
LCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNCCHFTNSSHHLLLATGS
SDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWDATSANERKS
INVKQFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLFDIHTSGLLGEIHTGHH
STIQYCDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTS
SDDQTIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIRRLQLINGRTGQIDYLT
EAQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLIS
SSDDAEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFDGTVKVWNIITGNKEKD
FVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDST
LLATGDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLCFSPDGKMLISAGGYIK
WWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVTVDNLGILYILQTLE
|
| Enzyme 23 Number of Residues |
1248 |
| Enzyme 23 Molecular Weight |
141841 |
| Enzyme 23 Theoretical pI |
6.37 |
| Enzyme 23 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- nucleotide binding
- protein binding
- purine nucleotide binding
|
| Process |
- apoptosis
- cell death
- death
- physiological process
- programmed cell death
- regulation of apoptosis
- regulation of biological process
- regulation of cellular physiological process
- regulation of physiological process
- regulation of programmed cell death
|
| Component |
|
|
| Enzyme 23 General Function |
Not Available |
| Enzyme 23 Specific Function |
Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP. Isoform 6 is less effective in inducing apoptosis |
| Enzyme 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
Not Available |
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
2330015  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
O14727  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
APAF_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>3585 bp
ATGGATGCAAAAGCTCGAAATTGTTTGCTTCAACATAGAGAAGCTCTGGAAAAGGACATC
AAGACATCCTACATCATGGATCACATGATTAGTGATGGATTTTTAACAATATCAGAAGAG
GAAAAAGTAAGAAATGAGCCCACTCAACAGCAAAGAGCAGCTATGCTGATTAAAATGATA
CTTAAAAAAGATAATGATTCCTACGTATCATTCTACAATGCTCTACTACATGAAGGATAT
AAAGATCTTGCTGCCCTTCTCCATGATGGCATTCCTGTTGTCTCTTCTTCCAGTGTAAGG
ACAGTCCTGTGTGAAGGTGGAGTACCACAGAGGCCAGTTGTTTTTGTCACAAGGAAGAAG
CTGGTGAATGCAATTCAGCAGAAGCTCTCCAAATTGAAAGGTGAACCAGGATGGGTCACC
ATACATGGAATGGCAGGCTGTGGGAAGTCTGTATTAGCTGCAGAAGCTGTTAGAGATCAT
TCCCTTTTAGAAGGTTGTTTCCCAGGGGGAGTGCATTGGGTTTCAGTTGGGAAACAAGAC
AAATCTGGGCTTCTGATGAAACTGCAGAATCTTTGCACACGGTTGGATCAGGATGAGAGT
TTTTCCCAGAGGCTTCCACTTAATATTGAAGAGGCTAAAGACCGTCTCCGCATTCTGATG
CTTCGCAAACACCCAAGGTCTCTCTTGATCTTGGATGATGTTTGGGACTCTTGGGTGTTG
AAAGCTTTTGACAGTCAGTGTCAGATTCTTCTTACAACCAGAGACAAGAGTGTTACAGAT
TCAGTAATGGGTCCTAAATATGTAGTCCCTGTGGAGAGTTCCTTAGGAAAGGAAAAAGGA
CTTGAAATTTTATCCCTTTTTGTTAATATGAAGAAGGCAGATTTGCCAGAACAAGCTCAT
AGTATTATAAAAGAATGTAAAGGCTCTCCCCTTGTAGTATCTTTAATTGGTGCACTTTTA
CGTGATTTTCCCAATCGCTGGGAGTACTACCTCAAACAGCTTCAGAATAAGCAGTTTAAG
AGAATAAGGAAATCTTCGTCTTATGATTATGAGGCTCTAGATGAAGCCATGTCTATAAGT
GTTGAAATGCTCAGAGAAGACATCAAAGATTATTACACAGATCTTTCCATCCTTCAGAAG
GACGTTAAGGTGCCTACAAAGGTGTTATGTATTCTCTGGGACATGGAAACTGAAGAAGTT
GAAGACATACTGCAGGAGTTTGTAAATAAGTCTCTTTTATTCTGTGATCGGAATGGAAAG
TCGTTTCGTTATTATTTACATGATCTTCAAGTAGATTTTCTTACAGAGAAGAATTGCAGC
CAGCTTCAGGATCTACATAAGAAGATAATCACTCAGTTTCAGAGATATCACCAGCCGCAT
ACTCTTTCACCAGATCAGGAAGACTGTATGTATTGGTACAACTTTCTGGCCTATCACATG
GCCAGTGCCAAGATGCACAAGGAACTTTGTGCTTTAATGTTTTCCCTGGATTGGATTAAA
GCAAAAACAGAACTTGTAGGCCCTGCTCATCTGATTCATGAATTTGTGGAATACAGACAT
ATACTAGATGAAAAGGATTGTGCAGTCAGTGAGAATTTTCAGGAGTTTTTATCTTTAAAT
GGACACCTTCTTGGACGACAGCCATTTCCTAATATTGTACAACTGGGTCTCTGTGAGCCG
GAAACTTCAGAAGTTTATCAGCAAGCTAAGCTGCAGGCCAAGCAGGAGGTCGATAATGGA
ATGCTTTACCTGGAATGGATAAACAAAAAAAACATCACGAATCTTTCCCGCTTAGTTGTC
CGCCCCCACACAGATGCTGTTTACCATGCCTGCTTTTCTGAGGATGGTCAGAGAATAGCT
TCTTGTGGAGCTGATAAAACCTTACAGGTGTTCAAAGCTGAAACAGGAGAGAAACTTCTA
GAAATCAAGGCTCATGAGGATGAAGTGCTTTGTTGTGCATTCTCTACAGATGACAGATTT
ATAGCAACCTGCTCAGTGGATAAAAAAGTGAAGATTTGGAATTCTATGACTGGGGAACTA
GTACACACCTATGATGAGCACTCAGAGCAAGTCAATTGCTGCCATTTCACCAACAGTAGT
CATCATCTTCTCTTAGCCACTGGGTCAAGTGACTGCTTCCTCAAACTTTGGGATTTGAAT
CAAAAAGAATGTCGAAATACCATGTTTGGTCATACAAATTCAGTCAATCACTGCAGATTT
TCACCAGATGATAAGCTTTTGGCTAGTTGTTCAGCTGATGGAACCTTAAAGCTTTGGGAT
GCGACATCAGCAAATGAGAGGAAAAGCATTAATGTGAAACAGTTCTTCCTAAATTTGGAG
GACCCTCAAGAGGATATGGAAGTGATAGTGAAGTGTTGTTCGTGGTCTGCTGATGGTGCA
AGGATAATGGTGGCAGCAAAAAATAAAATCTTTTTGTGGAATACAGACTCACGTTCAAAG
GTGGCTGATTGCAGAGGACATTTAAGTTGGGTTCATGGTGTGATGTTTTCTCCTGATGGA
TCATCATTTTTGACATCTTCTGATGACCAGACAATCAGGCTCTGGGAGACAAAGAAAGTA
TGTAAGAACTCTGCTGTAATGTTAAAGCAAGAAGTAGATGTTGTGTTTCAAGAAAATGAA
GTGATGGTCCTTGCAGTTGACCATATAAGACGTCTGCAACTCATTAATGGAAGAACAGGT
CAGATTGATTATCTGACTGAAGCTCAAGTTAGCTGCTGTTGCTTAAGTCCACATCTTCAG
TACATTGCATTTGGAGATGAAAATGGAGCCATTGAGATTTTAGAACTTGTAAACAATAGA
ATCTTCCAGTCCAGGTTTCAGCACAAGAAAACTGTATGGCACATCCAGTTCACAGCCGAT
GAGAAGACTCTTATTTCAAGTTCTGATGATGCTGAAATTCAGGTATGGAATTGGCAATTG
GACAAATGTATCTTTCTACGAGGCCATCAGGAAACAGTGAAAGACTTTAGACTCTTGAAA
AATTCAAGACTGCTTTCTTGGTCATTTGATGGAACAGTGAAGGTATGGAATATTATTACT
GGAAATAAAGAAAAAGACTTTGTCTGTCACCAGGGTACAGTACTTTCTTGTGACATTTCT
CACGATGCTACCAAGTTTTCATCTACCTCTGCTGACAAGACTGCAAAGATCTGGAGTTTT
GATCTCCTTTTGCCACTTCATGAATTGAGGGGCCACAACGGCTGTGTGCGCTGCTCTGCC
TTCTCTGTGGACAGTACCCTGCTGGCAACGGGAGATGACAATGGAGAAATCAGGATATGG
AATGTCTCAAACGGTGAGCTTCTTCATTTGTGTGCTCCGCTTTCAGAAGAAGGAGCTGCT
ACCCATGGAGGCTGGGTGACTGACCTTTGCTTTTCTCCAGATGGCAAAATGCTTATCTCT
GCTGGAGGATATATTAAGTGGTGGAACGTTGTCACTGGGGAATCCTCACAGACCTTCTAC
ACAAATGGAACCAATCTTAAGAAAATACACGTGTCCCCTGACTTCAAAACATATGTGACT
GTGGATAATCTTGGTATTTTATATATTTTACAGACTTTAGAATAA
|
| Enzyme 23 GenBank Gene ID |
AF013263  |
| Enzyme 23 GeneCard ID |
APAF1  |
| Enzyme 23 GenAtlas ID |
APAF1  |
| Enzyme 23 HGNC ID |
HGNC:576  |
| Enzyme 23 Chromosome Location |
12 |
| Enzyme 23 Locus |
12q23 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Zou H, Henzel WJ, Liu X, Lutschg A, Wang X: Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell. 1997 Aug 8;90(3):405-13. [PubMed
]
- Hahn C, Hirsch B, Jahnke D, Durkop H, Stein H: Three new types of Apaf-1 in mammalian cells. Biochem Biophys Res Commun. 1999 Aug 11;261(3):746-9. [PubMed
]
- Saleh A, Srinivasula SM, Acharya S, Fishel R, Alnemri ES: Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation. J Biol Chem. 1999 Jun 18;274(25):17941-5. [PubMed
]
- Hu Y, Benedict MA, Ding L, Nunez G: Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis. EMBO J. 1999 Jul 1;18(13):3586-95. [PubMed
]
- Ogawa T, Shiga K, Hashimoto S, Kobayashi T, Horii A, Furukawa T: APAF-1-ALT, a novel alternative splicing form of APAF-1, potentially causes impeded ability of undergoing DNA damage-induced apoptosis in the LNCaP human prostate cancer cell line. Biochem Biophys Res Commun. 2003 Jun 27;306(2):537-43. [PubMed
]
- Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1997 Oct 31;4(5):307-13. [PubMed
]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed
]
- Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Alnemri ES: Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization. Mol Cell. 1998 Jun;1(7):949-57. [PubMed
]
- Moroni MC, Hickman ES, Lazzerini Denchi E, Caprara G, Colli E, Cecconi F, Muller H, Helin K: Apaf-1 is a transcriptional target for E2F and p53. Nat Cell Biol. 2001 Jun;3(6):552-8. [PubMed
]
- Vaughn DE, Rodriguez J, Lazebnik Y, Joshua-Tor L: Crystal structure of Apaf-1 caspase recruitment domain: an alpha-helical Greek key fold for apoptotic signaling. J Mol Biol. 1999 Oct 29;293(3):439-47. [PubMed
]
- Day CL, Dupont C, Lackmann M, Vaux DL, Hinds MG: Solution structure and mutagenesis of the caspase recruitment domain (CARD) from Apaf-1. Cell Death Differ. 1999 Nov;6(11):1125-32. [PubMed
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
8075 |
| Enzyme 24 Name |
Uridine-cytidine kinase 2 |
| Enzyme 24 Synonyms |
- UCK 2
- Uridine monophosphokinase 2
- Cytidine monophosphokinase 2
|
| Enzyme 24 Gene Name |
UCK2 |
| Enzyme 24 Protein Sequence |
>Uridine-cytidine kinase 2
MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYRQKQVVILS
QDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELILKTLKEITEGKTVQIPVYDFVSHSRK
EETVTVYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ
ILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGPSKRQTNG
CLNGYTPSRKRQASESSSRPH
|
| Enzyme 24 Number of Residues |
261 |
| Enzyme 24 Molecular Weight |
29299 |
| Enzyme 24 Theoretical pI |
6.68 |
| Enzyme 24 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside kinase activity
- nucleotide binding
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- uridine kinase activity
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 24 General Function |
Nucleotide transport and metabolism |
| Enzyme 24 Specific Function |
Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, 4-N-acetylcytidine, 4-N- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and 4-N-anisoylcytidine |
| Enzyme 24 Pathways |
|
| Enzyme 24 Reactions |
- ATP + uridine = ADP + UMP
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
1655420  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q9BZX2  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
UCK2_HUMAN  |
| Enzyme 24 PDB ID |
1XRJ  |
| Enzyme 24 PDB File |
Show |
| Enzyme 24 3D Structure |
|
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>336 bp
ATGAAGCTTTTTGTGGATACAGATGCGGACACCCGGCTCTCACGCAGAGTATTAAGGGAC
ATCAGCGAGAGAGGCAGGGATCTTGAGCAGATTTTATCTCAGTACATTACGTTCGTCAAG
CCTGCCTTTGAGGAATTCTGCTTGCCAACAAAGCAGTATGCTGATGTGATCATCCCTAGA
GGTGCAGATAATCTGGTGGCCATCAACCTCATCGAGCAGCACATCCAGGACATCCTGAAT
GGAGGGCCCTCCAAACGGCAGACCAATGGCTGTCTCAACGGCTACACCCCTTCACGCAAG
AGGCAGGCATCGGAGTCCAGCAGCAGGCCGCATTGA
|
| Enzyme 24 GenBank Gene ID |
D78335  |
| Enzyme 24 GeneCard ID |
UCK2  |
| Enzyme 24 GenAtlas ID |
UCK2  |
| Enzyme 24 HGNC ID |
HGNC:12562  |
| Enzyme 24 Chromosome Location |
1 |
| Enzyme 24 Locus |
1q23 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Ozaki K, Kuroki T, Hayashi S, Nakamura Y: Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a differential mRNA display method. Genomics. 1996 Sep 1;36(2):316-9. [PubMed
]
- Van Rompay AR, Norda A, Linden K, Johansson M, Karlsson A: Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases. Mol Pharmacol. 2001 May;59(5):1181-6. [PubMed
]
- Koizumi K, Shimamoto Y, Azuma A, Wataya Y, Matsuda A, Sasaki T, Fukushima M: Cloning and expression of uridine/cytidine kinase cDNA from human fibrosarcoma cells. Int J Mol Med. 2001 Sep;8(3):273-8. [PubMed
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
13098 |
| Enzyme 25 Name |
Uridine/cytidine kinase-like 1 |
| Enzyme 25 Synonyms |
Not Available |
| Enzyme 25 Gene Name |
UCKL1 |
| Enzyme 25 Protein Sequence |
>Uridine/cytidine kinase-like 1
MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDRSNAESLDRLLPPVGTGRSPRKR
TTSQCKSEPPLLRTSKRTIYTAGRPPWYNEHGTQSKEAFAIGLGGGSASGKTTVARMIIE
ALDVPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV
PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRR
DISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQL
EERELSVRAALASAHQCHPLPRTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRL
LIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIG
TILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIF
LLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTDAVPDGSD
EEEVAYTG
|
| Enzyme 25 Number of Residues |
548 |
| Enzyme 25 Molecular Weight |
61142 |
| Enzyme 25 Theoretical pI |
7.40 |
| Enzyme 25 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside kinase activity
- nucleotide binding
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- uridine kinase activity
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 25 General Function |
Nucleotide transport and metabolism |
| Enzyme 25 Specific Function |
May contribute to UTP accumulation needed for blast transformation and proliferation |
| Enzyme 25 Pathways |
|
| Enzyme 25 Reactions |
- ATP + uridine = ADP + UMP [RN:R00964] ALL_REAC R00964
- (other) R00513 R00516 R00517 R00962 R00967 R00968 R00970 R01548 R01549 R01880 R02091 R02096 R02097 R02327 R02332 R02371 R02372
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
38228699  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
Q9NWZ5  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
UCKL1_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
Not Available |
| Enzyme 25 GenBank Gene ID |
AJ605558  |
| Enzyme 25 GeneCard ID |
Q9NWZ5  |
| Enzyme 25 GenAtlas ID |
UCKL1  |
| Enzyme 25 HGNC ID |
HGNC:15938  |
| Enzyme 25 Chromosome Location |
Not Available |
| Enzyme 25 Locus |
Not Available |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Kashuba E, Kashuba V, Sandalova T, Klein G, Szekely L: Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferase. BMC Cell Biol. 2002 Aug 29;3:23. Epub 2002 Aug 29. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
15191 |
| Enzyme 26 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 26 Synonyms |
Not Available |
| Enzyme 26 Gene Name |
NME7 |
| Enzyme 26 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 26 Number of Residues |
376 |
| Enzyme 26 Molecular Weight |
42492 |
| Enzyme 26 Theoretical pI |
6.44 |
| Enzyme 26 GO Classification |
Not Available |
| Enzyme 26 General Function |
Nucleotide transport and metabolism |
| Enzyme 26 Specific Function |
Not Available |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
Not Available |
| Enzyme 26 Pfam Domain Function |
Not Available |
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
158254838  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
A8K3T6  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
A8K3T6_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>1131 bp
ATGAATCATAGTGAAAGATTTGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
|
| Enzyme 26 GenBank Gene ID |
AK290701  |
| Enzyme 26 GeneCard ID |
A8K3T6  |
| Enzyme 26 GenAtlas ID |
Not Available |
| Enzyme 26 HGNC ID |
Not Available |
| Enzyme 26 Chromosome Location |
Not Available |
| Enzyme 26 Locus |
Not Available |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
Not Available |
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
15200 |
| Enzyme 27 Name |
Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e) |
| Enzyme 27 Synonyms |
Not Available |
| Enzyme 27 Gene Name |
UCK1 |
| Enzyme 27 Protein Sequence |
>Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRDKEVCRCDHPA
RSGQYGCHQPDRAAHPGHSEW
|
| Enzyme 27 Number of Residues |
201 |
| Enzyme 27 Molecular Weight |
22761 |
| Enzyme 27 Theoretical pI |
6.23 |
| Enzyme 27 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside kinase activity
- nucleotide binding
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- uridine kinase activity
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 27 General Function |
Nucleotide 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 |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
57162360  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
Q5JT13  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
Q5JT13_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>807 bp
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGTCGACCGTGTGTGAGAAGATCATGGAGTTGCTGGGACAG
AACGAGGTGGAACAGCGGCAGCGGAAGGTGGTCATCCTGAGCCAGGACAGGTTCTACAAG
GTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTGAAAGGACAGTACAATTTTGACCATCCA
GATGCCTTTGATAATGATTTGATGCACAGGACTCTGAAGAACATCGTGGAGGGCAAAACG
GTGGAGGTGCCGACCTATGATTTTGTGACACACTCAAGGTTACCAGAGACCACGGTGGTC
TACCCTGCGGACGTGGTTCTGTTTGAGGGCATCTTGGTGTTCTACAGCCAGGAGATCCGG
GACATGTTCCACCTGCGCCTCTTCGTGGACACCGACTCCGACGTCAGGCTGTCTCGAAGA
GTTCTCCGGGACGTGCGCCGAGGGAGGGACCTGGAGCAGATTCTGACGCAGTACACCACC
TTCGTGAAGCCGGCCTTCGAGGAGTTCTGCCTGCCGACAAAGAAGTATGCCGATGTGATC
ATCCCGCGAGGAGTGGACAATATGGTTGCCATCAACCTGATCGTGCAGCACATCCAGGAC
ATTCTGAATGGTGACATCTGCAAATGGCACCGAGGAGGGTCCAATGGGCGGAGCTACAAG
CGGACCTTTTCTGAGCCAGGGGACCACCCTGGGATGCTGACCTCTGGCAAACGGTCACAT
TTGGAGTCCAGCAGCAGACCCCACTGA
|
| Enzyme 27 GenBank Gene ID |
AL358781  |
| Enzyme 27 GeneCard ID |
Q5JT13  |
| Enzyme 27 GenAtlas ID |
UCK1  |
| Enzyme 27 HGNC ID |
HGNC:14859  |
| 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 |
15209 |
| Enzyme 28 Name |
cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA |
| Enzyme 28 Synonyms |
Not Available |
| Enzyme 28 Gene Name |
Not Available |
| Enzyme 28 Protein Sequence |
>cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTAT
VKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVH
GSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGV
EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYME
ELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGM
YLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLG
VEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTH
PQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFHLT
KDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRV
LLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGF
TFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVG
TMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDD
IRTHYDRLVDEYSLNAGKQGYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRG
IFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAA
VVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKG
AALITAVGVRLRTEASS
|
| Enzyme 28 Number of Residues |
917 |
| Enzyme 28 Molecular Weight |
102388 |
| Enzyme 28 Theoretical pI |
6.70 |
| Enzyme 28 GO Classification |
Not Available |
| Enzyme 28 General Function |
Not Available |
| Enzyme 28 Specific Function |
Not Available |
| Enzyme 28 Pathways |
Not Available |
| Enzyme 28 Reactions |
Not Available |
| Enzyme 28 Pfam Domain Function |
Not Available |
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
158257456  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
A8K7J7  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
A8K7J7_HUMAN  |
| Enzyme 28 PDB ID |
1HKB  |
| Enzyme 28 PDB File |
Show |
| Enzyme 28 3D Structure |
|
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>2754 bp
ATGATCGCCGCGCAGCTCCTGGCCTATTACTTCACGGAGCTGAAGGATGACCAGGTCAAA
AAGATTGACAAGTATCTGTATGCCATGCGGCTCTCCGATGAAACTCTCATAGATATCATG
ACTCGCTTCAGGAAGGAGATGAAGAATGGCCTCTCCCGGGATTTTAATCCAACAGCCACA
GTCAAGATGTTGCCAACATTCGTAAGGTCCATTCCTGATGGCTCTGAAAAGGGAGATTTC
ATTGCCCTGGATCTTGGTGGGTCTTCCTTTCGAATTCTGCGGGTGCAAGTGAATCATGAG
AAAAACCAGAATGTTCACATGGAGTCCGAGGTTTATGACACCCCAGAGAACATCGTGCAC
GGCAGTGGAAGCCAGCTTTTTGATCATGTTGCTGAGTGCCTGGGAGATTTCATGGAGAAA
AGGAAGATCAAGGACAAGAAGTTACCTGTGGGATTCACGTTTTCTTTTCCTTGCCAACAA
TCCAAAATAGATGAGGCCATCCTGATCACCTGGACAAAGCGATTTAAAGCGAGCGGAGTG
GAAGGAGCAGATGTGGTCAAACTGCTTAACAAAGCCATCAAAAAGCGAGGGGACTATGAT
GCCAACATCGTAGCTGTGGTGAATGACACAGTGGGCACCATGATGACCTGTGGCTATGAC
GACCAGCACTGTGAAGTCGGCCTGATCATCGGCACTGGCACCAATGCTTGCTACATGGAG
GAACTGAGGCACATTGATCTGGTGGAAGGAGACGAGGGGAGGATGTGTATCAATACAGAA
TGGGGAGCCTTTGGAGACGATGGATCATTAGAAGACATCCGGACAGAGTTTGACAGGGAG
ATAGACCGGGGATCCCTCAACCCTGGAAAACAGCTGTTTGAGAAGATGGTCAGTGGCATG
TACTTGGGAGAGCTGGTTCGACTGATCCTAGTCAAGATGGCCAAGGAGGGCCTCTTATTT
GAAGGGCGGATCACCCCGGAGCTGCTCACCCGAGGGAAGTTTAACACCAGTGATGTGTCA
GCCATCGAAAAGAATAAGGAAGGCCTCCACAATGCCAAAGAAATCCTGACCCGCCTGGGA
GTGGAGCCGTCCGATGATGACTGTGTCTCAGTCCAGCACGTTTGCACCATTGTCTCATTT
CGCTCAGCCAACTTGGTGGCTGCCACACTGGGCGCCATCTTGAACCGCCTGCGTGATAAC
AAGGGCACACCCAGGCTGCGGACCACGGTTGGTGTCGACGGATCTCTTTACAAGACGCAC
CCACAGTATTCCCGGCGTTTCCACAAGACTCTAAGGCGCTTGGTGCCAGACTCCGATGTG
CGCTTCCTCCTCTCGGAGAGTGGCAGCGGCAAGGGGGCTGCCATGGTGACGGCGGTGGCC
TACCGCTTGGCCGAGCAGCACCGGCAGATAGAGGAGACCCTGGCTCATTTCCACCTCACC
AAAGACATGCTGCTGGAGGTGAAGAAGAGGATGCGGGCCGAGATGGAGCTGGGGCTGAGG
AAGCAGACGCACAACAATGCCGTGGTTAAGATGCTGCCCTCCTTCGTCCGGAGAACTCCC
GACGGGACCGAGAATGGTGACTTCTTGGCCCTGGATCTTGGAGGAACCAATTTCCGTGTG
CTGCTGGTGAAAATCCGTAGTGGGAAAAAGAGAACGGTGGAAATGCACAACAAGATCTAC
GCCATTCCTATTGAAATCATGCAGGGCACTGGGGAAGAGCTGTTTGATCACATTGTCTCC
TGCATCTCTGACTTCTTGGACTACATGGGGATCAAAGGCCCCAGGATGCCTCTGGGCTTC
ACGTTCTCATTTCCCTGCCAGCAGACGAGTCTGGACGCGGGAATCTTGATCACGTGGACA
AAGGGTTTTAAGGCAACAGACTGCGTGGGCCACGATGTAGTCACCTTACTAAGGGATGCG
ATAAAAAGGAGAGAGGAATTTGACCTGGACGTGGTGGCTGTGGTCAACGACACAGTGGGC
ACCATGATGACCTGTGCTTATGAGGAGCCCACCTGTGAGGTTGGACTCATTGTTGGGACC
GGCAGCAATGCCTGCTACATGGAGGAGATGAAGAACGTGGAGATGGTGGAGGGGGACCAG
GGGCAGATGTGCATCAACATGGAGTGGGGGGCCTTTGGGGACAACGGGTGTCTGGATGAT
ATCAGGACACACTACGACAGACTGGTGGACGAATATTCCCTAAATGCTGGGAAACAAGGG
TATGAGAAGATGATCAGTGGTATGTACCTGGGTGAAATCGTCCGCAACATCTTAATCGAC
TTCACCAAGAAGGGATTCCTCTTCCGAGGGCAGATCTCTGAGACGCTGAAGACCCGGGGC
ATCTTTGAGACCAAGTTTCTCTCTCAGATCGAGAGTGACCGATTAGCACTGCTCCAGGTC
CGGGCTATCCTCCAGCAGCTAGGTCTGAATAGCACCTGCGATGACAGTATCCTCGTCAAG
ACAGTGTGCGGGGTGGTGTCCAGGAGGGCCGCACAGCTGTGTGGCGCAGGCATGGCTGCG
GTTGTGGATAAGATCCGCGAGAACAGAGGACTGGACCGTCTGAATGTGACTGTGGGAGTG
GACGGGACACTCTACAAGCTTCATCCACACTTCTCCAGAATCATGCACCAGACGGTGAAG
GAACTGTCACCAAAATGTAACGTGTCCTTCCTCCTGTCTGAGGATGGCAGCGGCAAGGGG
GCCGCCCTCATCACGGCCGTGGGCGTGCGGTTACGCACAGAGGCAAGCAGCTAA
|
| Enzyme 28 GenBank Gene ID |
AK292012  |
| Enzyme 28 GeneCard ID |
A8K7J7  |
| Enzyme 28 GenAtlas ID |
Not Available |
| Enzyme 28 HGNC ID |
Not Available |
| Enzyme 28 Chromosome Location |
Not Available |
| Enzyme 28 Locus |
Not Available |
| Enzyme 28 SNPs |
Not Available |
| Enzyme 28 General References |
Not Available |
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
15252 |
| Enzyme 29 Name |
Myb-binding protein 1A |
| Enzyme 29 Synonyms |
Not Available |
| Enzyme 29 Gene Name |
MYBBP1A |
| Enzyme 29 Protein Sequence |
>Myb-binding protein 1A
MESRDPAQPMSPGEATQSGARPADRYGLLKHSREFLDFFWDIAKPEQETRLAATEKLLEY
LRGRPKGSEMKYALKRLITGLGVGRETARPCYSLALAQLLQSFEDLPLCSILQQIQEKYD
LHQVKKAMLRPALFANLFGVLALFQSGRLVKDQEALMKSVKLLQALAQYQNHLQEQPRKA
LVDILSEVSKATLQEILPEVLKADLNIILSSPEQLELFLLAQQKVPSKLKKLVGSVNLFS
DENVPRLVNVLKMAASSVKKDRKLPAIALDLLRLALKEDKFPRFWKEVVEQGLLKMQFWP
ASYLCFRLLGAALPLLTKEQLHLVMQGDVIRHYGEHVCTAKLPKQFKFAPEMDDYVGTFL
EGCQDDPERQLAVLVAFSSVTNQGLPVTPTFWRVVRFLSPPALQGYVAWLRAMFLQPDLD
SLVDFSTNNQKKAQDSSLHMPERAVFRLRKWIIFRLVSIVDSLHLEMEEALTEQVARFCL
FHSFFVTKKPTSQIPETKHPFSFPLENQAREAVSSAFFSLLQTLSTQFKQAPGQTQGGQP
WTYHLVQFADLLLNHSHNVTTVTPFTAQQRQAWDRMLQTLKELEAHSAEARAAAFQHLLL
LVGIHLLKSPAESCDLLGDIQTCIRKSLGEKPRRSRTKTIDPQEPPWVEVLVEILLALLA
QPSHLMRQVARSVFGHICSHLTPRALQLILDVLNPETSEDENDRVVVTDDSDERRLKGAE
DKSEEGEDNRSSESEEESEGEESEEEERDGDVDQGFREQLMTVLQAGKALGGEDSENEEE
LGDEAMMALDQSLASLFAEQKLRIQARRDEKNKLQKEKALRRDFQIRVLDLVEVLVTKQP
ENALVLELLEPLLSIIRRSLRSSSSKQEQDLLHKTARIFTHHLCRARRYCHDLGERAGAL
HAQVERLVQQAGRQPDSPTALYHFNASLYLLRVLKGNTAEGCVHETQEKQKAGTDPSHMP
TGPQAASCLDLNLVTRVYSTALSSFLTKRNSPLTVPMFLSLFSRHPVLCQSLLPILVQHI
TGPVRPRHQACLLLQKTLSMREVRSCFEDPEWKQLMGQVLAKVTENLRVLGEAQTKAQHQ
QALSSLELLNVLFRTCKHEKLTLDLTVLLGVLQGQQQSLQQGAHSTGSSRLHDLYWQAMK
TLGVQRPKLEKKDAKEIPSATQSPISKKRKKKGFLPETKKRKKRKSEDGTPAEDGTPAAT
GGSQPPSMGRKKRNRTKAKVPAQANGTPTTKSPAPGAPTRSPSTPAKSPKLQKKNQKPSQ
VNGAPGSPTEPAGQKQHQKALPKKGVLGKSPLSALARKKARLSLVIRSPSLLQSGAKKKA
QVRKAGKP
|
| Enzyme 29 Number of Residues |
1328 |
| Enzyme 29 Molecular Weight |
148856 |
| Enzyme 29 Theoretical pI |
9.87 |
| Enzyme 29 GO Classification |
| Function |
- DNA binding
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- transcription
|
| Component |
| — |
|
| Enzyme 29 General Function |
Not Available |
| Enzyme 29 Specific Function |
May activate or repress transcription via interactions with sequence specific DNA-binding proteins. Repression may be mediated at least in part by histone deacetylase activity (HDAC activity) |
| Enzyme 29 Pathways |
Not Available |
| Enzyme 29 Reactions |
Not Available |
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
6959304  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
Q9BQG0  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
MBB1A_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>3987 bp
ATGGAGAGCCGGGATCCCGCCCAGCCGATGTCGCCTGGAGAAGCGACGCAGAGTGGCGCC
CGGCCTGCCGACCGCTATGGCCTATTGAAGCACAGTCGCGAGTTCTTGGACTTCTTCTGG
GACATTGCGAAGCCTGAGCAGGAGACGCGACTTGCGGCCACGGAGAAGCTGCTGGAGTAT
CTGCGTGGCAGGCCGAAGGGGTCCGAGATGAAATATGCCCTGAAGCGTCTAATCACGGGA
CTCGGGGTCGGGCGAGAAACAGCCCGGCCCTGCTACAGTTTGGCCCTGGCACAGCTGTTA
CAGTCTTTTGAAGACCTCCCCTTGTGCAGCATCCTGCAGCAGATACAAGAAAAATATGAC
CTGCATCAGGTGAAGAAGGCAATGCTGAGACCTGCTCTCTTTGCAAACCTGTTTGGAGTG
CTCGCCCTCTTTCAGTCAGGTCGGCTGGTGAAGGACCAGGAGGCACTGATGAAGTCGGTG
AAGCTGCTGCAGGCCCTGGCCCAGTACCAAAACCACTTGCAGGAGCAGCCCCGGAAGGCC
CTGGTGGACATCCTCTCCGAGGTCTCGAAGGCCACATTGCAGGAGATCCTGCCGGAGGTC
CTCAAAGCCGACTTGAATATAATACTCAGCTCCCCTGAACAGCTAGAGCTCTTCCTCCTG
GCCCAGCAGAAGGTGCCCTCCAAGCTCAAGAAGCTGGTGGGATCCGTGAACCTATTCTCA
GATGAGAATGTCCCCAGGCTGGTGAATGTGCTGAAGATGGCCGCCTCCTCTGTGAAGAAG
GACCGCAAGCTGCCCGCCATTGCTCTGGACCTGCTCCGCCTGGCGCTCAAGGAAGACAAG
TTCCCACGGTTCTGGAAGGAGGTGGTGGAACAAGGGCTGCTGAAGATGCAGTTCTGGCCA
GCCAGCTACCTGTGTTTCCACCTGCTGGGCGCGGCCCTGCCCCTGCTGACCAAGGAGCAG
CTGCACCTGGTGATGCAGGGAGACGTGATCCGCCATTACGGGGAGCACGTGTGCACTGCT
AAGCTCCCAAAGCAGTTCAAGTTTGCCCCAGAGATGGACGATTACGTGGGCACCTTCCTA
GAGGGGTGCCAGGATGACCCTGAGCGGCAGCTGGCCGTGCTAGTGGCCTTCTCATCTGTC
ACCAACCAAGGCCTCCCTGTCACGCCTACTTTCTGGCGGGTCGTGCGGTTCCTGAGCCCT
CCGGCCCTGCAGGGCTATGTGGCCTGGCTGCGGGCCATGTTTCTCCAGCCAGACCTGGAC
TCCTTGGTTGACTTCAGCACCAACAACCAGAAGAAAGCCCAGGATTCATCGCTCCACATG
CCTGAGCGAGCTGTGTTCCGGCTGAGGAAATGGATCATCTTTCGATTGGTGAGCATTGTG
GACAGCCTGCACCTGGAGATGGAGGAGGCCTTGACTGAGCAGGTGGCCAGGTTTTGTTTG
TTCCACTCGTTCTTTGTCACAAAGAAGCCCACATCCCAGATCCCTGAGACAAAGCACCCG
TTCTCCTTCCCTTTGGAAAACCAGGCCCGAGAGGCTGTCAGCAGTGCCTTCTTCAGTCTG
TTGCAGACCCTCAGCACGCAGTTCAAGCAGGCACCGGGCCAGACCCAGGGTGGGCAGCCC
TGGACCTACCACCTGGTGCAATTCGCAGACCTCCTGTTGAATCACAGCCACAACGTGACC
ACCGTGACACCCTTCACTGCGCAGCAGCACCAGGCCTGGGACCGGATGCTGCAGACTCTG
AAGGAGCTGGAGGCCCACTCCGCAGAGGCCAGGGCTGCTGCCTTCCAGCACCTTCTGCTC
TTCGTGGGCATCCACCTCCTCAAGTCCCCTGCAGAGAGCTGTGACCTGCTGGGTGACATC
CAGACCTGCATCAGGAAAAGTCTGGGAGAGAAGCCCCGCCGGAGCCGCACCAAGACCATC
GACCCCCAGGAACCCCCGTGGGTAGAGGTGCTGGTGGAGATCTTGCTGGCCCTGTTGGCC
CAGCCCAGCCACCTCATGCGCCAGGTGGCCCGGAGCGTGTTTGGCCACATCTGCTCCCAC
CTGACCCCGCGTGCCCTGCAGCTAATTCTGGATGTGCTGAACCCCGAGACCAGTGAGGAT
GAGAATGACCGTGTGGTGGTGACGGACGATTCTGATGAGCGGCGGCTGAAGGGTGCAGAG
GACAAGAGCGAGGAAGGTGAGGACAACAGAAGCTCAGAGAGTGAAGAGGAGAGCGAGGGG
GAGGAGAGCGAGGAGGAGGAGCGCGACGGGGACGTGGATCAGGGCTTCCGGGAACAGCTG
ATGACCGTGCTGCAGGCTGGGAAGGCGCTGGGTGGAGAGGACAGTGAGAACGAGGAGGAG
CTGGGGGATGAGGCCATGATGGCCCTGGACCAGAGCCTCGCCAGCCTCTTTGCCGAGCAG
AAGCTGCGTATCCAGGCCCGGCGAGACGAGAAGAACAAGCTGCAGAAGGAGAAGGCTCTG
CGGCGCGACTTCCAGATCCGGGTGCTGGACCTGGTGGAGGTGCTAGTGACCAAGCAGCCC
GAGAATGCCCTGGTCCTGGAGCTGCTGGAGCCGCTGCTGAGCATCATCCGGCGCAGCCTG
CGCAGCAGCAGCTCCAAACAGGAGCAGGACCTTCTGCACAAGACGGCGCGCATCTTCACG
CATCACCTGTGCCGTGCCCGGCGCTACTGCCACGACTTGGGTGAGCGCGCAGGGGCCCTG
CACGCCCAGGTGGAGCGGTTGGTGCAGCAGGCTGGCCGCCAGCCCGACTCCCCCACCGCC
CTCTACCACTTCAACGCCTCTCTCTACCTGCTCCGGGTCTTGAAGGGCAACACTGCTGAG
GGCTGCGTGCATGAGACACAGGAGAAGCAGAAAGCTGGCACTGACCCCAGCCACATGCCC
ACGGGCCCGCAGGCTGCCAGCTGCTTGGACTTGAACCTGGTGACCCGGGTGTACTCGACA
GCACTGAGCTCCTTCCTGACCAAGCGCAACAGCCCCCTCACAGTTCCCATGTTCCTCAGC
CTCTTCTCCCGGCACCCGGTGCTCTGTCAGAGCCTGCTCCCCATCCTGGTCCAGCATATC
ACGGGCCCGGTGCGGCCCCGTCATCAGGCCTGCCTGCTGCTCCAGAAGACCCTGTCCATG
CGGGAGGTGAGGTCGTGCTTTGAGGACCCCGAGTGGAAGCAGCTGATGGGCCAGGTCCTA
GCAAAGGTCACCGAGAACTTGCGCGTGCTGGGGGAGGCGCAGACCAAGGCGCAGCATCAG
CAGGCACTGTCCTCCCTGGAGCTGCTCAACGTTCTCTTCAGGACCTGCAAACATGAGAAG
CTGACCTTGGACCTGACGGTGCTCCTGGGTGTGCTGCAGGGGCAACAGCAGAGCCTACAG
CAGGGGGCACACTCCACCGGCTCCAGCCGCCTGCACGACCTCTACTGGCAGGCCATGAAA
ACCCTGGGAGTCCAGCGCCCCAAGTTGGAGAAGAAGGATGCCAAGGAGATCCCCAGTGCC
ACCCAGAGCCCCATCAGTAAGAAGCGGAAGAAAAAGGGATTCTTGCCAGAGACGAAGAAG
CGCAAGAAACGCAAGTCAGAGGATGGCACGCCAGCGGAGGATGGCACACCTGCAGCCACC
GGCGGGAGCCAGCCCCCCAGCATGGGCAGGAAGAAGAGGAACAGGACAAAGGCTAAGGTC
CCAGCCCAGGCAAACGGGACGCCAACCACCAAGAGTCCAGCCCCTGGCGCCCCCACCCGG
AGCCCCAGCACCCCTGCCAAATCCCCAAAACTGCAGAAGAAAAACCAGAAGCCGTCCCAG
GTGAATGGAGCTCCCGGGTCCCCCACGGAACCTGCAGGCCAAAAGCAGCATCAGAAGGCT
CTTCCCAAAAAGGGGGTCTTGGGCAAATCACCACTGTCCGCGCTGGCACGGAAAAAGGCA
AGGCTGTCTTTGGTCATCAGGAGTCCCAGCCTGCTTCAGAGTGGGGCCAAGAAGAAAGCA
CAGGTGAGGAAGGCAGGGAAGCCCTGA
|
| Enzyme 29 GenBank Gene ID |
AF147709  |
| Enzyme 29 GeneCard ID |
Q9BQG0  |
| Enzyme 29 GenAtlas ID |
MYBBP1A  |
| Enzyme 29 HGNC ID |
HGNC:7546  |
| Enzyme 29 Chromosome Location |
17 |
| Enzyme 29 Locus |
17p13.3 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- Keough R, Woollatt E, Crawford J, Sutherland GR, Plummer S, Casey G, Gonda TJ: Molecular cloning and chromosomal mapping of the human homologue of MYB binding protein (P160) 1A (MYBBP1A) to 17p13.3. Genomics. 1999 Dec 15;62(3):483-9. [PubMed
]
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed
]
- Scherl A, Coute Y, Deon C, Calle A, Kindbeiter K, Sanchez JC, Greco A, Hochstrasser D, Diaz JJ: Functional proteomic analysis of human nucleolus. Mol Biol Cell. 2002 Nov;13(11):4100-9. [PubMed
]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
15253 |
| Enzyme 30 Name |
DNA polymerase theta |
| Enzyme 30 Synonyms |
Not Available |
| Enzyme 30 Gene Name |
POLQ |
| Enzyme 30 Protein Sequence |
>DNA polymerase theta
MNLLRRSGKRRRSESGSDSFSGSGGDSSASPQFLSGSVLSPPPGLGRCLKAAAAGECKPT
VPDYEIDKLLLANWGLPKAVLEKYHSFGVKKMFEWQAECLLLGQVLEGKNLVYSAPTSAG
KTLVAELLILKRVLEMRKKALFILPFVSVAKEKKYYLQSLFQEVGIKVDGYMGSTSPSRH
FSSLDIAVCTIERANGLINRLIEENKMDLLGMVVVDELHMLGDSHRGYLLELLLTKICYI
TRKSASCQADLASSLSNAVQIVGMSATLPNLELVASWLNAELYHTDFRPVPLLESVKVGN
SIYDSSMKLVREFEPMLQVKGDEDHVVSLCYETICDNHSVLLFCPSKKWCEKLADIIARE
FYNLHHQAEGLVKPSECPPVILEQKELLEVMDQLRRLPSGLDSVLQKTVPWGVAFHHAGL
TFEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIRTPIFGGRPLDILTYKQMVGR
AGRKGVDTVGESILICKNSEKSKGIALLQGSLKPVRSCLQRREGEEVTGSMIRAILEIIV
GGVASTSQDMHTYAACTFLAASMKEGKQGIQRNQESVQLGAIEACVMWLLENEFIQSTEA
SDGTEGKVYHPTHLGSATLSSSLSPADTLDIFADLQRAMKGFVLENDLHILYLVTPMFED
WTTIDWYRFFCLWEKLPTSMKRVAELVGVEEGFLARCVKGKVVARTERQHRQMAIHKRFF
TSLVLLDLISEVPLREINQKYGCNRGQIQSLQQSAAVYAGMITVFSNRLGWHNMELLLSQ
FQKRLTFGIQRELCDLVRVSLLNAQRARVLYASGFHTVADLARANIVEVEVILKNAVPFK
SARKAVDEEEEAVEERRNMRTIWVTGRKGLTEREAAALIVEEARMILQQDLVEMGVQWNP
CALLHSSTCSLTHSESEVKEHTFISQTKSSYKKLTSKNKSNTIFSDSYIKHSPNIVQDLN
KSREHTSSFNCNFQNGNQEHQRCSIFRARKRASLDINKEKPGASQNEGKTSDKKVVQTFS
QKTKKAPLNFNSEKMSRSFRSWKRRKHLKRSRDSSPLKDSGACRIHLQGQTLSNPSLCED
PFTLDEKKTEFRNSGPFAKNVSLSGKEKDNKTSFPLQIKQNCSWNITLTNDNFVEHIVTG
SQSKNVTCQATSVVSEKGRGVAVEAEKINEVLIQNGSKNQNVYMKHHDIHPINQYLRKQS
HEQTSTITKQKNIIERQMPCEAVSSYINRDSNVTINCERIKLNTEENKPSHFQALGDDIS
RTVIPSEVLPSAGAFSKSEGQHENFLNISRLQEKTGTYTTNKTKNNHVSDLGLVLCDFED
SFYLDTQSEKIIQQMATENAKLGAKDTNLAAGIMQKSLVQQNSMNSFQKECHIPFPAEQH
PLGATKIDHLDLKTVGTMKQSSDSHGVDILTPESPIFHSPILLEENGLFLKKNEVSVTDS
QLNSFLQGYQTQETVKPVILLIPQKRTPTGVEGECLPVPETSLNMSDSLLFDSFSDDYLV
KEQLPDMQMKEPLPSEVTSNHFSDSLCLQEDLIKKSNVNENQDTHQQLTCSNDESIIFSE
MDSVQMVEALDNVDIFPVQEKNHTVVSPRALELSDPVLDEHHQGDQDGGDQDERAEKSKL
TGTRQNHSFIWSGASFDLSPGLQRILDKVSSPLENEKLKSMTINFSSLNRKNTELNEEQE
VISNLETKQVQGISFSSNNEVKSKIEMLENNANHDETSSLLPRKESNIVDDNGLIPPTPI
PTSASKLTFPGILETPVNPWKTNNVLQPGESYLFGSPSDIKNHDLSPGSRNGFKDNSPIS
DTSFSLQLSQDGLQLTPASSSSESLSIIDVASDQNLFQTFIKEWRCKKRFSISLACEKIR
SLTSSKTATIGSRFKQASSPQEIPIRDDGFPIKGCDDTLVVGLAVCWGGRDAYYFSLQKE
QKHSEISASLVPPSLDPSLTLKDRMWYLQSCLRKESDKECSVVIYDFIQSYKILLLSCGI
SLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLEGMETSQGIQSLGLNAGSEH
SGRYRASVESILIFNSMNQLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECE
SQKHIMQAKLDAIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPNREMKNQGSKKTLGS
TRRGIDNGRKLRLGRQFSTSKDVLNKLKALHPLPGLILEWRRITNAITKVVFPLQREKCL
NPFLGMERIYPVSQSHTATGRITFTEPNIQNVPRDFEIKMPTLVGESPPSQAVGKGLLPM
GRGKYKKGFSVNPRCQAQMEERAADRGMPFSISMRHAFVPFPGGSILAADYSQLELRILA
HLSHDRRLIQVLNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGE
QMGIKENDAACYIDSFKSRYTGINQFMTETVKNCKRDGFVQTILGRRRYLPGIKDNNPYR
KAHAERQAINTIVQGSAADIVKIATVNIQKQLETFHSTFKSHGHREGMLQSDRTGLSRKR
KLQGMFCPIRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGA
SWGELKDFDV
|
| Enzyme 30 Number of Residues |
2590 |
| Enzyme 30 Molecular Weight |
289663 |
| Enzyme 30 Theoretical pI |
7.42 |
| Enzyme 30 GO Classification |
| Function |
- ATP binding
- DNA binding
- DNA-directed DNA polymerase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- helicase activity
- nucleic acid binding
- nucleotide binding
- nucleotidyltransferase activity
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolism
- DNA replication
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 30 General Function |
Not Available |
| Enzyme 30 Specific Function |
Not Available |
| Enzyme 30 Pathways |
Not Available |
| Enzyme 30 Reactions |
Not Available |
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
76364226  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
Q6VMB5  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
Q6VMB5_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>7773 bp
ATGAATCTTCTGCGTCGGAGTGGGAAACGGCGGCGTTCAGAATCAGGCTCAGATTCGTTC
TCGGGAAGCGGCGGTGACAGCAGTGCCAGCCCCCAGTTCCTCTCCGGGTCCGTGCTGAGC
CCGCCGCCCGGCCTTGGTCGCTGCCTGAAGGCCGCAGCTGCAGGAGAATGCAAGCCTACA
GTTCCTGACTACGAAATAGACAAGCTACTATTGGCAAACTGGGGACTTCCTAAAGCAGTT
CTGGAAAAATACCACAGTTTTGGTGTAAAAAAGATGTTTGAATGGCAGGCAGAGTGCCTT
TTGCTTGGACAAGTCCTGGAAGGAAAGAATTTAGTTTATTCAGCTCCTACAAGTGCTGGG
AAGACTCTTGTGGCAGAATTACTTATTTTGAAGCGGGTTTTGGAAATGCGGAAGAAAGCT
TTGTTTATTCTTCCCTTTGTTTCTGTGGCTAAAGAGAAGAAATACTACCTCCAGAGTCTG
TTTCAGGAAGTAGGAATAAAAGTAGACGGTTATATGGGCAGCACCTCTCCATCAAGGCAT
TTCTCTTCATTGGATATTGCAGTCTGCACAATTGAGAGAGCCAATGGTCTGATCAATCGC
CTCATAGAGGAAAATAAGATGGATCTGTTAGGAATGGTGGTTGTGGATGAATTACATATG
CTGGGAGACTCTCACCGAGGGTATCTGCTGGAACTTTTGCTGACCAAGATTTGCTATATT
ACTCGGAAATCAGCATCTTGTCAGGCAGATCTAGCCAGTTCTCTGTCTAATGCTGTGCAA
ATCGTTGGCATGAGTGCTACCCTTCCTAATTTGGAGCTTGTGGCTTCCTGGTTGAATGCT
GAACTCTACCATACCGACTTTCGCCCTGTACCGCTTTTGGAGTCAGTAAAAGTTGGAAAT
TCCATATATGACTCTTCAATGAAACTTGTGAGGGAATTTGAGCCCATGCTTCAAGTGAAG
GGAGATGAGGACCATGTTGTTAGCTTATGTTATGAGACGATTTGTGATAACCATTCAGTA
TTACTTTTTTGTCCATCAAAGAAATGGTGTGAGAAGCTGGCAGATATCATTGCTCGAGAG
TTTTATAATCTACATCATCAAGCTGAGGGTTTGGTGAAACCCTCTGAATGCCCACCAGTA
ATTCTGGAACAAAAAGAACTCCTGGAAGTGATGGATCAGTTAAGACGTTTGCCTTCAGGA
CTGGACTCTGTATTACAGAAAACTGTACCATGGGGAGTAGCATTTCATCATGCAGGTCTT
ACTTTTGAGGAGAGGGATATCATTGAAGGAGCCTTTCGTCAAGGTCTCATTCGGGTCTTG
GCGGCAACTTCTACTCTTTCTTCTGGGGTGAATTTACCTGCACGTCGTGTGATTATTCGA
ACCCCTATTTTTGGTGGTCGACCTCTAGATATTCTTACTTATAAGCAGATGGTTGGTCGT
GCTGGCAGGAAAGGAGTGGACACAGTAGGCGAGAGTATCTTAATTTGTAAGAACTCTGAG
AAATCAAAAGGCATAGCTCTCCTTCAGGGTTCTCTAAAGCCTGTTCGCAGCTGTCTGCAA
AGACGAGAAGGAGAAGAAGTAACTGGCAGCATGATACGAGCTATTCTGGAGATAATAGTT
GGTGGAGTGGCAAGTACATCACAAGATATGCATACTTATGCTGCCTGCACATTTTTGGCT
GCAAGTATGAAAGAAGGGAAGCAAGGAATTCAGAGAAATCAAGAGTCTGTTCAGCTTGGA
GCGATTGAGGCCTGTGTGATGTGGCTACTAGAAAATGAATTCATCCAGAGTACAGAAGCC
AGTGATGGAACAGAAGGAAAGGTGTATCATCCAACACATCTTGGTTCGGCCACTCTTTCT
TCTTCACTTTCTCCAGCTGATACTTTAGATATTTTTGCTGACCTGCAAAGAGCAATGAAG
GGCTTTGTTTTAGAGAATGATCTTCATATTCTCTATCTGGTTACACCTATGTTTGAGGAT
TGGACTACTATTGATTGGTATCGATTTTTCTGTTTATGGGAGAAGTTGCCAACTTCAATG
AAAAGGGTGGCAGAGCTAGTGGGAGTTGAAGAGGGGTTCTTGGCCCGTTGTGTGAAAGGA
AAAGTAGTAGCCAGAACTGAGAGACAGCATCGACAAATGGCCATCCATAAAAGGTTTTTC
ACCAGTCTTGTGCTATTAGATTTAATCAGTGAAGTTCCCTTAAGGGAAATAAATCAGAAA
TATGGATGCAATCGTGGGCAGATTCAATCTTTGCAACAGTCAGCTGCTGTTTATGCAGGG
ATGATTACAGTATTTTCCAACCGTCTGGGCTGGCACAACATGGAACTACTACTTTCCCAA
TTTCAGAAGCGTCTTACGTTTGGCATCCAGAGGGAGCTGTGTGACCTGGTTCGGGTATCC
TTACTAAATGCTCAGAGAGCCAGGGTTCTCTATGCTTCTGGCTTTCATACTGTGGCAGAC
CTTGCTAGAGCAAATATTGTGGAGGTGGAGGTGATTCTGAAAAATGCTGTGCCTTTCAAA
AGTGCCCGGAAGGCAGTGGATGAGGAAGAGGAAGCAGTTGAAGAACGTCGCAATATGCGA
ACTATCTGGGTGACTGGCAGAAAAGGTTTAACTGAAAGGGAAGCAGCAGCCCTTATAGTG
GAAGAAGCCAGAATGATTCTGCAGCAGGACTTAGTTGAAATGGGAGTGCAATGGAATCCA
TGTGCCCTGTTACATTCTAGTACATGCTCATTGACTCATAGTGAGTCCGAAGTAAAGGAA
CACACATTTATATCCCAAACTAAGAGTTCTTATAAAAAATTAACATCAAAGAACAAAAGT
AACACAATATTTAGTGATTCTTATATTAAGCATTCACCAAATATAGTGCAAGACTTAAAT
AAAAGTAGAGAGCATACAAGTTCCTTTAATTGTAATTTCCAGAATGGGAATCAAGAACAT
CAGAGATGTTCCATTTTCAGAGCAAGAAAACGGGCCTCTTTAGATATAAATAAAGAGAAG
CCAGGAGCCTCTCAGAATGAGGGGAAAACAAGTGATAAGAAAGTTGTTCAGACTTTTTCA
CAGAAAACAAAAAAGGCACCTTTGAATTTCAATTCAGAAAAGATGAGCAGAAGTTTTCGA
TCTTGGAAACGTAGAAAGCATCTAAAGCGATCTAGGGACAGCAGCCCCCTGAAAGACTCT
GGAGCGTGTAGAATCCATTTACAAGGACAGACTCTGTCTAATCCTAGTCTTTGTGAAGAC
CCGTTTACCTTAGATGAGAAGAAAACGGAATTTAGAAATTCAGGGCCATTTGCTAAAAAT
GTATCTTTGAGTGGTAAGGAAAAAGATAATAAAACATCATTCCCATTACAAATAAAGCAA
AATTGTTCATGGAACATAACACTAACTAATGATAATTTTGTGGAGCATATTGTCACAGGA
TCTCAGAGTAAAAATGTGACTTGTCAGGCCACTAGTGTGGTTAGTGAAAAGGGCAGAGGA
GTAGCTGTTGAGGCAGAAAAAATAAATGAAGTGCTGATACAAAATGGTTCAAAAAACCAG
AATGTTTATATGAAACACCATGACATCCATCCAATTAACCAGTACCTGCGAAAGCAATCT
CATGAACAGACAAGCACTATTACCAAACAGAAAAATATAATAGAGAGACAAATGCCCTGT
GAAGCAGTCAGTAGTTACATAAATAGAGACTCAAATGTTACTATCAATTGTGAAAGGATA
AAGCTTAATACAGAGGAAAATAAACCAAGTCATTTTCAGGCATTAGGAGATGATATAAGC
AGAACTGTGATACCCAGTGAAGTACTTCCATCAGCTGGAGCATTTAGCAAATCAGAAGGC
CAGCATGAGAATTTTCTAAATATTTCTAGACTACAAGAAAAAACAGGTACTTATACAACA
AACAAAACTAAAAATAATCATGTTTCTGACTTAGGTTTAGTCCTCTGTGATTTTGAAGAT
AGTTTCTATCTGGATACTCAGTCAGAGAAAATAATACAACAGATGGCAACTGAAAATGCC
AAACTAGGAGCAAAGGACACCAACCTGGCAGCAGGGATAATGCAGAAGAGCTTAGTCCAA
CAGAACTCAATGAACTCTTTTCAGAAGGAGTGTCACATTCCTTTTCCTGCTGAACAGCAC
CCTCTAGGAGCGACTAAGATAGATCATTTGGACCTTAAGACTGTAGGTACTATGAAACAA
AGCAGTGATTCACATGGGGTTGATATCCTGACTCCAGAAAGCCCGATTTTCCATTCTCCA
ATACTATTGGAGGAAAATGGTCTTTTTTTAAAAAAGAATGAAGTTTCTGTTACTGATTCA
CAATTAAATAGTTTTCTTCAAGGTTATCAAACACAAGAAACTGTGAAACCAGTTATACTT
CTGATTCCTCAAAAGAGAACTCCCACTGGTGTAGAAGGAGAATGTCTTCCAGTTCCTGAA
ACAAGTTTGAATATGAGTGATAGTTTACTATTTGATAGCTTCAGTGATGACTATCTAGTA
AAAGAACAATTACCTGATATGCAAATGAAAGAACCCCTTCCTTCAGAAGTAACATCAAAC
CATTTTAGTGATTCTCTGTGTCTACAAGAAGACCTAATTAAAAAATCAAATGTAAATGAG
AATCAAGATACCCACCAGCAGTTGACTTGTTCCAATGATGAATCTATTATATTTTCAGAA
ATGGATTCTGTTCAGATGGTTGAAGCTTTGGACAATGTGGATATATTTCCTGTCCAAGAG
AAGAATCATACTGTAGTATCTCCTAGAGCATTAGAACTAAGTGATCCAGTACTTGATGAG
CACCACCAAGGTGATCAAGATGGAGGAGATCAAGATGAAAGGGCTGAAAAATCAAAATTA
ACTGGGACCAGGCAAAATCATTCATTCATATGGTCAGGGGCATCATTTGATCTAAGTCCA
GGACTGCAAAGGATTTTAGATAAAGTATCCAGTCCTCTAGAAAATGAAAAGCTAAAATCA
ATGACTATAAACTTTTCCAGTTTGAATAGAAAAAATACAGAGTTAAATGAAGAACAAGAA
GTTATTTCAAACTTGGAGACAAAACAAGTGCAGGGAATTTCATTTTCTTCTAATAATGAA
GTAAAAAGCAAGATTGAGATGCTAGAAAACAATGCCAATCATGATGAAACCTCATCCCTC
TTACCTCGTAAAGAAAGTAATATAGTTGATGATAATGGTCTCATTCCTCCTACACCCATT
CCAACATCTGCTTCTAAGCTGACATTTCCAGGGATTCTTGAAACACCTGTAAACCCTTGG
AAAACTAATAATGTTTTACAACCTGGTGAAAGTTATTTATTTGGCTCACCTTCAGATATT
AAAAACCACGATTTAAGTCCAGGGAGTAGAAATGGGTTCAAAGACAACAGCCCTATTAGT
GACACAAGCTTTTCACTTCAGTTATCACAGGATGGATTACAGTTAACTCCAGCCTCAAGC
AGTTCAGAAAGTTTGTCCATAATTGATGTAGCAAGTGACCAAAATCTTTTCCAAACATTC
ATTAAGGAGTGGCGGTGCAAAAAGCGATTTTCCATCTCACTGGCTTGTGAAAAGATTAGA
AGTTTGACATCTTCTAAAACTGCTACTATTGGCAGTAGGTTTAAGCAAGCTAGCTCACCT
CAGGAAATTCCTATTAGAGATGATGGATTTCCCATTAAAGGTTGTGATGACACCTTGGTG
GTTGGACTGGCAGTATGCTGGGGTGGAAGGGATGCCTATTATTTTTCACTGCAGAAGGAA
CAAAAGCATTCTGAAATTAGTGCCAGTTTGGTTCCACCTTCTTTAGATCCAAGCCTGACT
TTGAAAGACAGGATGTGGTACCTTCAATCTTGCTTGCGAAAGGAATCTGATAAAGAATGT
TCTGTTGTCATCTATGACTTCATCCAGAGCTATAAAATTCTTCTTCTTTCTTGTGGCATC
TCCTTGGAGCAAAGTTATGAAGATCCTAAGGTGGCATGCTGGTTACTAGATCCAGATTCT
CAGGAGCCGACTCTTCATAGCATAGTTACCAGTTTTCTTCCTCATGAGCTTCCACTCCTA
GAAGGGATGGAGACCAGCCAAGGGATTCAAAGCCTGGGGCTAAATGCTGGCAGTGAGCAT
TCTGGGCGATACAGAGCATCTGTGGAGTCCATTCTCATCTTCAACTCTATGAATCAGCTC
AACTCTTTGTTGCAGAAGGAAAACCTTCAAGATGTTTTCCGTAAGGTGGAAATGCCCTCT
CAGTACTGCTTGGCCTTGCTAGAACTAAATGGAATTGGCTTTAGTACTGCAGAATGTGAA
AGTCAGAAACATATAATGCAAGCCAAGCTGGATGCAATTGAGACCCAGGCCTATCAACTA
GCTGGCCACAGTTTTTCTTTCACCAGTTCAGATGACATCGCTGAGGTTTTATTTTTGGAA
TTGAAGTTGCCCCCAAATAGAGAGATGAAAAACCAAGGCAGCAAGAAAACTCTGGGTTCT
ACCAGAAGAGGGATTGACAATGGACGCAAGCTAAGGCTGGGAAGACAGTTCAGCACTAGT
AAGGACGTTTTAAATAAATTAAAGGCATTACATCCTTTACCAGGCTTGATATTAGAATGG
AGAAGAATCACTAATGCTATTACCAAAGTGGTCTTTCCCCTTCAGCGGGAAAAGTGTCTT
AATCCTTTTCTTGGAATGGAAAGAATCTATCCTGTATCACAGTCGCACACTGCTACAGGA
CGAATAACCTTTACAGAACCAAATATTCAGAATGTGCCAAGAGATTTTGAAATCAAAATG
CCAACACTAGTAGGAGAAAGCCCACCTTCTCAAGCTGTAGGCAAAGGCCTACTTCCCATG
GGCAGAGGAAAATATAAGAAGGGTTTCAGCGTGAATCCTAGATGCCAGGCACAGATGGAG
GAGAGAGCTGCAGACAGAGGAATGCCATTTTCAATTAGCATGCGACATGCCTTTGTGCCT
TTCCCAGGTGGTTCAATACTGGCTGCTGACTACTCTCAGCTTGAACTGAGGATCTTGGCT
CATTTATCCCATGATCGTCGTCTCATTCAAGTGTTAAACACTGGAGCTGATGTTTTCAGG
AGCATTGCAGCAGAGTGGAAGATGATTGAGCCAGAGTCTGTTGGGGATGATCTGAGGCAG
CAGGCAAAACAGATTTGCTATGGGATCATTTATGGAATGGGAGCTAAATCTTTGGGAGAG
CAGATGGGCATTAAAGAAAATGATGCTGCATGCTATATTGACTCCTTCAAATCCAGATAC
ACAGGGATTAATCAATTCATGACAGAGACAGTGAAGAATTGTAAAAGAGACGGATTTGTT
CAGACCATTTTGGGAAGGCGTAGATATTTGCCAGGAATCAAAGACAACAACCCTTATCGT
AAAGCTCACGCTGAGCGTCAAGCTATCAACACAATAGTCCAAGGATCAGCAGCTGATATT
GTCAAAATAGCCACAGTTAACATTCAGAAGCAATTAGAGACCTTCCACTCAACCTTCAAA
TCCCATGGTCATCGAGAGGGTATGCTCCAAAGTGACCGAACAGGATTGTCACGAAAGAGA
AAACTGCAAGGGATGTTCTGCCCAATCAGAGGAGGCTTCTTCATCCTTCAACTCCATGAT
GAACTCCTATATGAAGTGGCAGAAGAAGATGTTGTTCAGGTAGCTCAGATTGTCAAGAAT
GAAATGGAAAGTGCTGTAAAACTGTCTGTGAAATTGAAAGTGAAAGTGAAAATAGGCGCC
AGCTGGGGAGAGCTAAAGGACTTTGATGTGTAA
|
| Enzyme 30 GenBank Gene ID |
AY338826  |
| Enzyme 30 GeneCard ID |
Q6VMB5  |
| Enzyme 30 GenAtlas ID |
POLQ  |
| Enzyme 30 HGNC ID |
HGNC:9186  |
| Enzyme 30 Chromosome Location |
Not Available |
| Enzyme 30 Locus |
Not Available |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Seki M, Marini F, Wood RD: POLQ (Pol theta), a DNA polymerase and DNA-dependent ATPase in human cells. Nucleic Acids Res. 2003 Nov 1;31(21):6117-26. [PubMed
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
15254 |
| Enzyme 31 Name |
cDNA FLJ76751, highly similar to Homo sapiens polymerase (DNA directed) sigma (POLS), mRNA (Polymerase (DNA directed) sigma) |
| Enzyme 31 Synonyms |
Not Available |
| Enzyme 31 Gene Name |
POLS |
| Enzyme 31 Protein Sequence |
>cDNA FLJ76751, highly similar to Homo sapiens polymerase (DNA directed) sigma (POLS), mRNA (Polymerase (DNA directed) sigma)
MSPCPEEAAMRREVVKRIETVVKDLWPTADVQIFGSFSTGLYLPTSDIDLVVFGKWERPP
LQLLEQALRKHNVAEPCSIKVLDKATVPIIKLTDQETEVKVDISFNMETGVRAAEFIKNY
MKKYSLLPYLILVLKQFLLQRDLNEVFTGGISSYSLILMAISFLQLHPRIDARRADENLG
MLLVEFFELYGRNFNYLKTGIRIKEGGAYIAKEEIMKAMTSGYRPSMLCIEDPLLPGNDV
GRSSYGAMQVKQVFDYAYIVLSHAVSPLARSYPNRDAESTLGRIIKVTQEVIDYRRWIKE
KWGSKAHPSPGMDSRIKIKERIATCNGEQTQNREPESPYGQRLTLSLSSPQLLSSGSSAS
SVSSLSGSDVDSDTPPCTTPSVYQFSLQAPAPLMAGLPTALPMPSGKPQPTTSRTLIMTT
NNQTRFTIPPPTLGVAPVPCRQAGVEGTASLKAVHHMSSPAIPSASPNPLSSPHLYHKQH
NGMKLSMKGSHGHTQGGGYSSVGSGGVRPPVGNRGHHQYNRTGWRRKKHTHTRDSLPVSL
SR
|
| Enzyme 31 Number of Residues |
542 |
| Enzyme 31 Molecular Weight |
59874 |
| Enzyme 31 Theoretical pI |
9.81 |
| Enzyme 31 GO Classification |
Not Available |
| Enzyme 31 General Function |
Not Available |
| Enzyme 31 Specific Function |
Not Available |
| Enzyme 31 Pathways |
Not Available |
| Enzyme 31 Reactions |
Not Available |
| Enzyme 31 Pfam Domain Function |
Not Available |
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
158260737  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
A8K1E2  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
A8K1E2_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>1629 bp
ATGTCCCCTTGTCCTGAAGAAGCAGCTATGAGAAGAGAGGTGGTGAAACGGATCGAAACT
GTGGTGAAAGACCTTTGGCCGACGGCTGATGTACAGATATTTGGCAGCTTTAGTACAGGT
CTTTATCTTCCAACTAGCGACATAGACCTGGTGGTCTTCGGGAAATGGGAGCGTCCTCCT
TTACAGCTGCTGGAGCAAGCCCTGCGGAAGCACAACGTGGCTGAGCCGTGTTCCATCAAA
GTCCTTGACAAGGCTACGGTACCAATAATAAAGCTCACAGATCAGGAGACTGAAGTGAAA
GTTGACATCAGCTTTAACATGGAGACGGGCGTCCGGGCAGCGGAGTTCATCAAGAATTAC
ATGAAGAAATATTCATTGCTGCCTTACTTGATTTTAGTATTGAAACAGTTCCTTCTGCAG
AGGGACCTGAATGAAGTTTTTACAGGTGGAATTAGCTCATACAGCCTAATTTTAATGGCC
ATTAGCTTTCTACAGTTGCATCCAAGAATTGATGCCCGGAGAGCTGATGAAAACCTTGGA
ATGCTTCTTGTAGAATTTTTTGAACTCTATGGGAGAAATTTTAATTACTTGAAAACCGGT
ATTAGAATCAAAGAAGGAGGTGCCTATATCGCCAAAGAGGAGATCATGAAAGCCATGACC
AGCGGGTACAGACCGTCGATGCTGTGCATTGAGGACCCCCTGCTGCCAGGGAATGACGTT
GGCCGGAGCTCCTATGGCGCCATGCAGGTGAAGCAGGTCTTCGATTATGCCTACATAGTG
CTCAGCCATGCTGTGTCACCGCTGGCCAGGTCCTATCCAAACAGAGACGCCGAAAGTACT
TTAGGAAGAATCATCAAAGTAACTCAGGAGGTGATTGACTACCGGAGGTGGATCAAAGAG
AAGTGGGGCAGCAAAGCCCACCCGTCGCCAGGCATGGACAGCAGGATCAAGATCAAAGAG
CGAATAGCCACATGCAATGGGGAGCAGACGCAGAACCGAGAGCCCGAGTCTCCCTATGGC
CAGCGCTTGACTTTGTCGCTGTCCAGCCCCCAGCTCCTGTCTTCAGGCTCCTCGGCCTCT
TCTGTGTCTTCACTTTCTGGGAGTGACGTTGATTCAGACACACCGCCCTGCACAACGCCC
AGTGTTTACCAGTTCAGTCTGCAAGCGCCAGCTCCTCTCATGGCCGGCTTACCCACCGCC
TTGCCAATGCCCAGTGGCAAACCTCAGCCCACCACTTCCAGAACACTGATCATGACAACC
AACAATCAGACCAGGTTTACTATACCTCCACCGACCCTAGGGGTTGCTCCTGTTCCTTGC
AGACAAGCTGGTGTAGAAGGAACTGCGTCTTTGAAAGCCGTCCACCACATGTCTTCCCCG
GCCATTCCCTCAGCGTCCCCCAACCCGCTCTCGAGCCCTCATCTGTATCATAAGCAGCAC
AACGGCATGAAACTGTCCATGAAGGGCTCTCACGGCCACACCCAAGGCGGCGGCTACAGC
TCTGTGGGTAGCGGAGGTGTGCGGCCCCCTGTGGGCAACAGGGGACACCACCAGTATAAC
CGCACCGGCTGGAGGAGGAAAAAACACACACACACACGGGACAGTCTGCCCGTGAGCCTC
AGCAGATAA
|
| Enzyme 31 GenBank Gene ID |
AK289857  |
| Enzyme 31 GeneCard ID |
A8K1E2  |
| Enzyme 31 GenAtlas ID |
Not Available |
| Enzyme 31 HGNC ID |
Not Available |
| Enzyme 31 Chromosome Location |
Not Available |
| Enzyme 31 Locus |
Not Available |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
Not Available |
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
16476 |
| Enzyme 32 Name |
cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e) |
| Enzyme 32 Synonyms |
Not Available |
| Enzyme 32 Gene Name |
PKM2 |
| Enzyme 32 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 32 Number of Residues |
531 |
| Enzyme 32 Molecular Weight |
57938 |
| Enzyme 32 Theoretical pI |
7.94 |
| Enzyme 32 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 32 General Function |
Carbohydrate transport and metabolism |
| Enzyme 32 Specific Function |
Not Available |
| Enzyme 32 Pathways |
Not Available |
| Enzyme 32 Reactions |
Not Available |
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
Not Available |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
B2R5N8  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
B2R5N8_HUMAN  |
| Enzyme 32 PDB ID |
1F3X  |
| Enzyme 32 PDB File |
Show |
| Enzyme 32 3D Structure |
|
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
Not Available |
| Enzyme 32 GenBank Gene ID |
AK312253  |
| Enzyme 32 GeneCard ID |
B2R5N8  |
| Enzyme 32 GenAtlas ID |
Not Available |
| Enzyme 32 HGNC ID |
Not Available |
| Enzyme 32 Chromosome Location |
15 |
| Enzyme 32 Locus |
15q22 |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
Not Available |
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
16536 |
| Enzyme 33 Name |
Polymerase (DNA directed) kappa, isoform CRA_b |
| Enzyme 33 Synonyms |
- SubName: cDNA, FLJ95449, Homo sapiens polymerase (DNA directed) kappa (POLK), mRNA
|
| Enzyme 33 Gene Name |
POLK |
| Enzyme 33 Protein Sequence |
>Polymerase (DNA directed) kappa, isoform CRA_b
MDSTKEKCDSYKDDLLLRMGLNDNKAGMEGLDKEKINKIIMEATKGSRFYGNELKKEKQV
NQRIENMMQQKAQITSQQLRKAQLQVDRFAMELEQSRNLSNTIVHIDMDAFYAAVEMRDN
PELKDKPIAVGSMSMLSTSNYHARRFGVRAAMPGFIAKRLCPQLIIVPPNFDKYRAVSKE
VKEILADYDPNFMAMSLDEAYLNITKHLEERQNWPEDKRRYFIKMGSSVENDNPGKEVNK
LSEHERSISPLLFEESPSDVQPPGDPFQVNFEEQNNPQILQNSVVFGTSAQEVVKEIRFR
IEQKTTLTASAGIAPNTMLAKVCSDKNKPNGQYQILPNRQAVMDFIKDLPIRKVSGIGKV
TEKMLKALGIITCTELYQQRALLSLLFSETSWHYFLHISLGLGSTHLTRDGERKSMSVER
TFSEINKAEEQYSLCQELCSELAQDLQKERLKGRTVTIKLKNVNFEVKTRASTVSSVVST
AEEIFAIAKELLKTEIDADFPHPLRLRLMGVRISSFPNEEDRKHQQRSIIGFLQAGNQAL
SATECTLEKTDKDKFVKPLEMSHKKSFFDKKRSERKWSHQDTFKCEAVNKQSFQTSQPFQ
VLKKKMNENLEISENSDDCQILTCPVCFRAQGCISLEALNKHVDECLDGPSISENFKMFS
CSHVSATKVNKKENVPASSLCEKQDYEAHPKIKEISSVDCIALVDTIDNSSKAESIDALS
NKHSKEECSSLPSKSFNIEHCHQNSSSTVSLENEDVGSFRQEYRQPYLCEVKTGQALVCP
VCNVEQKTSDLTLFNVHVDVCLNKSFIQELRKDKFNPVNQPKESSRSTGSSSGVQKAVTR
TKRPGLMTKYSTSKKIKPNNPKHTLDIFFK
|
| Enzyme 33 Number of Residues |
870 |
| Enzyme 33 Molecular Weight |
98810 |
| Enzyme 33 Theoretical pI |
8.22 |
| Enzyme 33 GO Classification |
| Function |
- DNA binding
- binding
- nucleic acid binding
|
| Process |
- DNA metabolism
- DNA repair
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 33 General Function |
Replication, recombination and repair |
| Enzyme 33 Specific Function |
Not Available |
| 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 |
Not Available |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
B2RBD2  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
B2RBD2_HUMAN  |
| Enzyme 33 PDB ID |
1T94  |
| Enzyme 33 PDB File |
Show |
| Enzyme 33 3D Structure |
|
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
Not Available |
| Enzyme 33 GenBank Gene ID |
AK314610  |
| Enzyme 33 GeneCard ID |
B2RBD2  |
| Enzyme 33 GenAtlas ID |
Not Available |
| Enzyme 33 HGNC ID |
Not Available |
| Enzyme 33 Chromosome Location |
Not Available |
| Enzyme 33 Locus |
Not Available |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
Not Available |
| Enzyme 33 Metabolite References |
Not Available |