|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5232 |
| Enzyme 1 Name |
Cytosolic 5'-nucleotidase 1B |
| Enzyme 1 Synonyms |
- Cytosolic 5'-nucleotidase IB
- cN1B
- cN-IB
- Autoimmune infertility-related protein
|
| Enzyme 1 Gene Name |
NT5C1B |
| Enzyme 1 Protein Sequence |
>Cytosolic 5'-nucleotidase 1B
MSQTSLKQKKNEPGMRSSKESLEAEKRKESDKTGVRLSNQMRRAVNPNHSLRCCPFQGHS
SCRRCLCAAEGTALGPCHTIRIYIHMCLLWEQGQQITMMRGSQESSLRKTDSRGYLVRSQ
WSRISRSPSTKAPSIDEPRSRNTSAKLPSSSTSSRTPSTSPSLHDSSPPPLSGQPSLQPP
ASPQLPRSLDSRPPTPPEPDPGSRRSTKMQENPEAWAQGIVREIRQTRDSQPLEYSRTSP
TEWKSSSQRRGIYPASTQLDRNSLSEQQQQQREDEDDYEAAYWASMRSFYEKNPSCSRPW
PPKPKNAITIALSSCALFNMVDGRKIYEQEGLEKYMEYQLTNENVILTPGPAFRFVKALQ
YVNARLRDLYPDEQDLFDIVLMTNNHAQVGVRLINSVNHYGLLIDRFCLTGGKDPIGYLK
AYLTNLYIAADSEKVQEAIQEGIASATMFDGAKDMAYCDTQLRVAFDGDAVLFSDESEHF
TKEHGLDKFFQYDTLCESKPLAQGPLKGFLEDLGRLQKKFYAKNERLLCPIRTYLVTARS
AASSGARVLKTLRRWGLEIDEALFLAGAPKSPILVKIRPHIFFDDHMFHIEGAQRLGSIA
AYGFNKKFSS
|
| Enzyme 1 Number of Residues |
610 |
| Enzyme 1 Molecular Weight |
68804 |
| Enzyme 1 Theoretical pI |
9.03 |
| Enzyme 1 GO Classification |
| Function |
- 5'-nucleotidase activity
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- magnesium ion binding
- metal ion binding
- nucleotidase activity
- nucleotide binding
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 1 General Function |
Not Available |
| Enzyme 1 Specific Function |
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Helps to regulate adenosine levels |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
13774961  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q96P26  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
5NT1B_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1699 bp
GGGCAAAAATGTGGATAACAACAAAAGAATTTCAACAGGTAAAAAAATGAGTCAAACATC
TCTCAAACAGAAAAAGAATGAGCCCGGAATGAGGTCCTCAAAAGAGAGTCTAGAAGCAGA
AAAAAGAAAGGAATCTGACAAAACAGGAGTTCGTCTGAGCAATCAGGGATCACAAGAATC
ATCACTGCGGAAGACAGACTCTCGAGGGTACCTTGTGCGCAGTCAATGGTCTAGAATATC
CCGGAGCCCATCCACCAAGGCTCCATCCATAGATGAGCCTAGAAGCAGGAACACCAGTGC
TAAGCTCCCCAGCAGCTCCACGAGCTCCCGGACTCCATCCACCTCCCCAAGCCTGCATGA
CTCCTCACCGCCGCCGCTGTCCGGGCAGCCCTCGCTCCAGCCACCCGCGTCGCCCCAGCT
GCCCCGGTCGCTGGACTCGCGGCCTCCCACGCCCCCAGAGCCCGATCCTGGCTCCCGGCG
CAGCACCAAAATGCAAGAAAATCCGGAGGCCTGGGCCCAAGGCATCGTGCGGGAAATCCG
CCAGACCCGGGACTCGCAGCCGCTGGAATATTCGCGCACGTCCCCCACCGAGTGGAAGTC
CTCCAGCCAGCGCAGGGGGATCTACCCCGCCTCCACCCAGCTGGACCGCAACTCTCTGTC
CGAGCAGCAGCAGCAGCAGCGGGAGGACGAAGACGACTACGAAGCTGCCTACTGGGCATC
CATGAAGTCGTTCTACGAAAAGAACCCGAGCTGCTGGCGCCCCTGGCCGCCCAAACCCAA
GAACGCCATCACCATTGCTCTCTCATCCTGCGCGCTCTTCAACATGGTGGACGGCAGGAA
AATCTACGAGCAAGAGGGTCTGGAAAAGTACATGGAGTATCAGCTCACCAATGAGAACGT
CATCCTGACCCCGGGCCCGGCGTTCCGTTTCGTCAAGGCACTACAGTATGTCAATGCTAG
ACTCCGTGATCTATATCCTGATGAACAGGACTTATTTGATATTGTACTGATGACTAATAA
CCATGCCCAAGTGGGAGTGCGGCTTATAAACAGCGTCAATCACTACGGCTTACTGATTGA
CCGCTTCTGTCTGACCGGGGGAAAAGACCCCATTGGCTATTTGAAGGCATATCTTACCAA
CTTGTATATTGCTGCAGATTCTGAAAAAGTGCAAGAGGCAATACAAGAAGGTATTGCCTC
TGCGACAATGTTTGATGGAGCCAAAGACATGGCTTACTGTGACACTCAGCTCCGTGTAGC
CTTTGATGGGGATGCTGTCCTCTTCTCTGATGAGTCTGAACATTTTACCAAGGAGCATGG
GCTGGACAAATTCTTCCAGTATGATACATTATGTGAAAGTAAGCCTCTTGCTCAGGGTCC
CCTAAAAGGCTTTCTGGAAGATTTAGGCAGACTGCAAAAGAAGTTCTATGCCAAAAATGA
ACGGTTACTTTGTCCTATCAGGACCTACCTGGTTACAGCTAGGAGTGCAGCCAGTTCAGG
CGCCCGTGTGCTGAAAACCTTCCGACGCTGGGGTCTAGAGATAGACGAAGCTCTTTTCCT
TGCTGGAGCCCCCAAAAGTCCCATCTTGGTGAAGATCCGGCCCCACATCTTCTTTGATGA
CCACATGTTCCACATTGAAGGGGCACAGAGGTTAGGTTCCATCGCAGCTTATGGCTTTAA
TAAAAAATTCAGTAGTTAG
|
| Enzyme 1 GenBank Gene ID |
AF356185  |
| Enzyme 1 GeneCard ID |
NT5C1B  |
| Enzyme 1 GenAtlas ID |
NT5C1B  |
| Enzyme 1 HGNC ID |
HGNC:17818  |
| Enzyme 1 Chromosome Location |
2 |
| Enzyme 1 Locus |
2p24.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Sala-Newby GB, Newby AC: Cloning of a mouse cytosolic 5'-nucleotidase-I identifies a new gene related to human autoimmune infertility-related protein. Biochim Biophys Acta. 2001 Oct 31;1521(1-3):12-8. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5233 |
| Enzyme 2 Name |
Cytosolic 5'-nucleotidase 1A |
| Enzyme 2 Synonyms |
- Cytosolic 5'-nucleotidase IA
- cN1A
- cN-IA
- cN-I
|
| Enzyme 2 Gene Name |
NT5C1A |
| Enzyme 2 Protein Sequence |
>Cytosolic 5'-nucleotidase 1A
MEPGQPREPQEPREPGPGAETAAAPVWEEAKIFYDNLAPKKKPKSPKPQNAVTIAVSSRA
LFRMDEEQQIYTEQGVEEYVRYQLEHENEPFSPGPAFPFVKALEAVNRRLRELYPDSEDV
FDIVLMTNNHAQVGVRLINSINHYDLFIERFCMTGGNSPICYLKAYHTNLYLSADAEKVR
EAIDEGIAAATIFSPSRDVVVSQSQLRVAFDGDAVLFSDESERIVKAHGLDRFFEHEKAH
ENKPLAQGPLKGFLEALGRLQKKFYSKGLRLECPIRTYLVTARSAASSGARALKTLRSWG
LETDEALFLAGAPKGPLLEKIRPHIFFDDQMFHVAGAQEMGTVAAHVPYGVAQTPRRTAP
AKQAPSAQ
|
| Enzyme 2 Number of Residues |
368 |
| Enzyme 2 Molecular Weight |
41021 |
| Enzyme 2 Theoretical pI |
6.52 |
| Enzyme 2 GO Classification |
| Function |
- 5'-nucleotidase activity
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- magnesium ion binding
- metal ion binding
- nucleotidase activity
- nucleotide binding
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides and has a broad substrate specificity. Helps to regulate adenosine levels in heart during ischemia and hypoxia |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
12659324  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q9BXI3  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
5NT1A_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1107 bp
ATGGAACCTGGGCAGCCCCGGGAGCCCCAGGAGCCCCGCGAGCCCGGGCCAGGAGCGGAG
ACCGCTGCGGCCCCGGTCTGGGAGGAAGCCAAGATTTTCTACGACAACCTCGCGCCCAAG
AAGAAACCCAAATCGCCCAAGCCTCAGAATGCAGTCACCATCGCTGTGTCCTCCCGAGCC
TTGTTTCGCATGGACGAGGAGCAGCAGATCTACACGGAGCAGGGCGTGGAGGAGTACGTG
CGCTACCAGCTGGAACATGAGAACGAACCCTTCAGTCCCGGGCCAGCCTTCCCTTTTGTG
AAGGCTCTGGAGGCCGTGAACAGGCGGCTGCGGGAGCTGTACCCTGATAGTGAGGACGTC
TTCGACATCGTCCTCATGACTAACAACCATGCTCAAGTGGGTGTCCGCCTCATCAACAGT
ATCAACCACTATGACCTGTTCATCGAGAGGTTCTGCATGACAGGTGGGAACAGCCCGATC
TGCTACCTCAAGGCCTATCACACCAACCTCTACTTGTCAGCCGATGCGGAAAAAGTGCGA
GAAGCCATTGATGAGGGGATCGCAGCTGCCACCATCTTCAGCCCCAGCAGGGATGTGGTT
GTGTCCCAGAGTCAGCTGCGCGTGGCCTTCGATGGGGACGCCGTGCTCTTCTCGGACGAG
TCGGAGCGCATCGTCAAGGCCCACGGGCTGGACCGATTCTTCGAGCATGAGAAGGCCCAC
GAGAACAAGCCTCTGGCTCAGGGCCCCTTAAAGGGCTTTCTGGAGGCACTGGGTAGGTTG
CAGAAGAAGTTCTACTCCAAAGGCCTGCGGCTGGAGTGCCCAATTCGTACCTACTTGGTG
ACAGCACGCAGTGCAGCCAGTTCCGGGGCCCGGGCTCTCAAGACCCTGCGCAGCTGGGGC
CTGGAGACAGATGAAGCCTTGTTCCTTGCTGGAGCGCCCAAGGGCCCTCTCCTTGAGAAG
ATCCGCCCACACATCTTCTTTGATGACCAGATGTTCCATGTGGCTGGGGCTCAGGAGATG
GGCACTGTGGCCGCCCATGTGCCTTATGGTGTGGCACAGACACCCCGGCGGACTGCACCT
GCAAAGCAGGCCCCATCTGCACAGTAG
|
| Enzyme 2 GenBank Gene ID |
AF331801  |
| Enzyme 2 GeneCard ID |
NT5C1A  |
| Enzyme 2 GenAtlas ID |
NT5C1A  |
| Enzyme 2 HGNC ID |
HGNC:17819  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1p34.3-p33 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Hunsucker SA, Spychala J, Mitchell BS: Human cytosolic 5'-nucleotidase I: characterization and role in nucleoside analog resistance. J Biol Chem. 2001 Mar 30;276(13):10498-504. Epub 2000 Dec 22. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5234 |
| Enzyme 3 Name |
5'(3')-deoxyribonucleotidase, cytosolic type |
| Enzyme 3 Synonyms |
- Cytosolic 5',3'-pyrimidine nucleotidase
- Deoxy-5'-nucleotidase 1
- dNT-1
|
| Enzyme 3 Gene Name |
NT5C |
| Enzyme 3 Protein Sequence |
>5'(3')-deoxyribonucleotidase, cytosolic type
MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADK
VASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHL
GPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFTCCHNRHLVLPPTRRRL
LSWSDNWREILDSKRGAAQRE
|
| Enzyme 3 Number of Residues |
201 |
| Enzyme 3 Molecular Weight |
23383 |
| Enzyme 3 Theoretical pI |
6.63 |
| Enzyme 3 GO Classification |
Not Available |
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 Specific Function |
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
7524492  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q8TCD5  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
NT5C_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>606 bp
ATGGCGCGGAGCGTGCGCGTGCTGGTGGACATGGACGGCGTCCTGGCCGACTTCGAGGCC
GGCCTCCTGCGGGGCTTCCGCCGCCGCTTCCCTGAGGAGCCGCACGTGCCGCTGGAGCAA
CGCCGCGGCTTCCTGGCCCGCGAGCAGTACCGCGCCCTGCGGCCCGACCTGGCGGATAAA
GTGGCCAGTGTGTACGAAGCCCCGGGCTTTTTCCTGGACCTGGAGCCCATCCCGGGAGCC
TTGGACGCTGTGCGGGAGATGAACGACCTACCGGACACGCAGGTCTTCATCTGCACCAGC
CCCCTGCTGAAGTACCACCACTGTGTGGGTGAGAAGTACCGCTGGGTGGAGCAGCACCTG
GGGCCCCAGTTCGTAGAACGAATTATCCTGACAAGGGACAAGACGGTGGTCTTGGGGGAC
CTGCTCATTGATGACAAGGACACAGTTCGAGGCCAGGAGGAGACCCCAAGCTGGGAGCAC
ATCTTGTTCACCTGCTGCCACAATCGGCACCTGGTCCTGCCCCCGACAAGGAGACGGCTG
CTCTCCTGGAGTGACAACTGGAGGGAGATCTTAGATAGCAAGCGCGGAGCTGCGCAGCGG
GAATGA
|
| Enzyme 3 GenBank Gene ID |
AF154829  |
| Enzyme 3 GeneCard ID |
NT5C  |
| Enzyme 3 GenAtlas ID |
NT5C  |
| Enzyme 3 HGNC ID |
HGNC:17144  |
| Enzyme 3 Chromosome Location |
17 |
| Enzyme 3 Locus |
17q25.1 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Rampazzo C, Johansson M, Gallinaro L, Ferraro P, Hellman U, Karlsson A, Reichard P, Bianchi V: Mammalian 5'(3')-deoxyribonucleotidase, cDNA cloning, and overexpression of the enzyme in Escherichia coli and mammalian cells. J Biol Chem. 2000 Feb 25;275(8):5409-15. [PubMed
]
- Rampazzo C, Kost-Alimova M, Ruzzenente B, Dumanski JP, Bianchi V: Mouse cytosolic and mitochondrial deoxyribonucleotidases: cDNA cloning of the mitochondrial enzyme, gene structures, chromosomal mapping and comparison with the human orthologs. Gene. 2002 Jul 10;294(1-2):109-17. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5235 |
| Enzyme 4 Name |
Deoxycytidine kinase |
| Enzyme 4 Synonyms |
- dCK
|
| Enzyme 4 Gene Name |
DCK |
| Enzyme 4 Protein Sequence |
>Deoxycytidine kinase
MATPPKRSCPSFSASSEGTRIKKISIEGNIAAGKSTFVNILKQLCEDWEVVPEPVARWCN
VQSTQDEFEELTMSQKNGGNVLQMMYEKPERWSFTFQTYACLSRIRAQLASLNGKLKDAE
KPVLFFERSVYSDRYIFASNLYESECMNETEWTIYQDWHDWMNNQFGQSLELDGIIYLQA
TPETCLHRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTNFDYLQEVPILTLDVNE
DFKDKYESLVEKVKEFLSTL
|
| Enzyme 4 Number of Residues |
260 |
| Enzyme 4 Molecular Weight |
30519 |
| Enzyme 4 Theoretical pI |
4.88 |
| Enzyme 4 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleotide binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Nucleotide transport and metabolism |
| Enzyme 4 Specific Function |
Required for the phosphorylation of several deoxyribonucleosides and certain nucleoside analogs widely employed as antiviral and chemotherapeutic agents |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- NTP + deoxycytidine = NDP + dCMP
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
181510  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P27707  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
DCK_HUMAN  |
| Enzyme 4 PDB ID |
1P62  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>783 bp
ATGGCCACCCCGCCCAAGAGAAGCTGCCCGTCTTTCTCAGCCAGCTCTGAGGGGACCCGC
ATCAAGAAAATCTCCATCGAAGGGAACATCGCTGCAGGGAAGTCAACATTTGTGAATATC
CTTAAACAATTGTGTGAAGATTGGGAAGTGGTTCCTGAACCTGTTGCCAGATGGTGCAAT
GTTCAAAGTACTCAAGATGAATTTGAGGAACTTACAATGTCTCAGAAAAATGGTGGGAAT
GTTCTTCAGATGATGTATGAGAAACCTGAACGATGGTCTTTTACCTTCCAAACATATGCC
TGTCTCAGTCGAATAAGAGCTCAGCTTGCCTCTCTGAATGGCAAGCTCAAAGATGCAGAG
AAACCTGTATTATTTTTTGAACGATCTGTGTATAGTGACAGGTATATTTTTGCATCTAAT
TTGTATGAATCTGAATGCATGAATGAGACAGAGTGGACAATTTATCAAGACTGGCATGAC
TGGATGAATAACCAATTTGGCCAAAGCCTTGAATTGGATGGAATCATTTATCTTCAAGCC
ACTCCAGAGACATGCTTACATAGAATATATTTACGGGGAAGAAATGAAGAGCAAGGCATT
CCTCTTGAATATTTAGAGAAGCTTCATTATAAACATGAAAGCTGGCTCCTGCATAGGACA
CTGAAAACCAACTTCGATTATCTTCAAGAGGTGCCTATCTTAACACTGGATGTTAATGAA
GACTTTAAAGACAAATATGAAAGTCTGGTTGAAAAGGTCAAAGAGTTTTTGAGTACTTTG
TGA
|
| Enzyme 4 GenBank Gene ID |
M60527  |
| Enzyme 4 GeneCard ID |
DCK  |
| Enzyme 4 GenAtlas ID |
DCK  |
| Enzyme 4 HGNC ID |
HGNC:2704  |
| Enzyme 4 Chromosome Location |
4 |
| Enzyme 4 Locus |
4q13.3-q21.1 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Chottiner EG, Shewach DS, Datta NS, Ashcraft E, Gribbin D, Ginsburg D, Fox IH, Mitchell BS: Cloning and expression of human deoxycytidine kinase cDNA. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1531-5. [PubMed
]
- Eriksson S, Cederlund E, Bergman T, Jornvall H, Bohman C: Characterization of human deoxycytidine kinase. Correlation with cDNA sequences. FEBS Lett. 1991 Mar 25;280(2):363-6. [PubMed
]
- Johansson M, Brismar S, Karlsson A: Human deoxycytidine kinase is located in the cell nucleus. Proc Natl Acad Sci U S A. 1997 Oct 28;94(22):11941-5. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5236 |
| Enzyme 5 Name |
5'(3')-deoxyribonucleotidase, mitochondrial precursor |
| Enzyme 5 Synonyms |
- 5',3'-nucleotidase, mitochondrial
- Deoxy-5'-nucleotidase 2
- dNT-2
|
| Enzyme 5 Gene Name |
NT5M |
| Enzyme 5 Protein Sequence |
>5'(3')-deoxyribonucleotidase, mitochondrial precursor
MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRAR
FPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMAS
LQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDI
TGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC
|
| Enzyme 5 Number of Residues |
228 |
| Enzyme 5 Molecular Weight |
25862 |
| Enzyme 5 Theoretical pI |
8.12 |
| Enzyme 5 GO Classification |
Not Available |
| Enzyme 5 General Function |
Not Available |
| Enzyme 5 Specific Function |
Dephosphorylates specifically the 5' and 2'(3')- phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
Not Available |
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
9408106  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9NPB1  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
NT5M_HUMAN  |
| Enzyme 5 PDB ID |
1Q92  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>687 bp
ATGATCCGGCTGGGCGGCTGGTGTGCGCGGCGGCTCTGCAGCGCGGCGGTTCCCGCGGGG
CGGCGCGGGGCGGCGGGCGGGCTGGGCCTGGCGGGAGGCCGCGCCCTACGGGTGCTGGTG
GACATGGACGGCGTGCTGGCTGACTTCGAGGGCGGATTCCTCAGGAAGTTCCGCGCGCGC
TTTCCCGACCAGCCCTTCATCGCGCTGGAGGACCGGCGCGGCTTCTGGGTGTCGGAGCAG
TACGGCCGCCTGCGGCCAGGGCTGAGCGAGAAGGCCATCAGCATTTGGGAGTCAAAGAAT
TTCTTTTTTGAACTTGAGCCTCTGCCAGGGGCCGTGGAAGCTGTCAAGGAGATGGCCAGC
CTACAAAACACTGACGTCTTCATCTGCACAAGCCCCATCAAGATGTTCAAGTACTGTCCC
TATGAGAAGTATGCCTGGGTGGAGAAGTACTTTGGCCCTGACTTTCTGGAGCAGATTGTG
CTGACCAGAGACAAGACCGTGGTCTCTGCTGACCTTCTCATAGACGACCGGCCGGACATC
ACAGGGGCCGAGCCAACCCCCAGCTGGGAGCATGTCCTCTTCACCGCCTGCCACAACCAG
CACCTGCAGCTGCAGCCCCCCCGCCGCAGGCTGCACTCGTGGGCGGACGACTGGAAGGCC
ATTCTGGACAGCAAGCGGCCCTGCTGA
|
| Enzyme 5 GenBank Gene ID |
AJ277557  |
| Enzyme 5 GeneCard ID |
NT5M  |
| Enzyme 5 GenAtlas ID |
NT5M  |
| Enzyme 5 HGNC ID |
HGNC:15769  |
| Enzyme 5 Chromosome Location |
17 |
| Enzyme 5 Locus |
17p11.2 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Rampazzo C, Gallinaro L, Milanesi E, Frigimelica E, Reichard P, Bianchi V: A deoxyribonucleotidase in mitochondria: involvement in regulation of dNTP pools and possible link to genetic disease. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8239-44. [PubMed
]
- Rinaldo-Matthis A, Rampazzo C, Reichard P, Bianchi V, Nordlund P: Crystal structure of a human mitochondrial deoxyribonucleotidase. Nat Struct Biol. 2002 Oct;9(10):779-87. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5237 |
| Enzyme 6 Name |
Cytosolic purine 5'-nucleotidase |
| Enzyme 6 Synonyms |
- 5'-nucleotidase cytosolic II
|
| Enzyme 6 Gene Name |
NT5C2 |
| Enzyme 6 Protein Sequence |
>Cytosolic purine 5'-nucleotidase
MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
PQEITHCHDEDDDEEEEEEEE
|
| Enzyme 6 Number of Residues |
561 |
| Enzyme 6 Molecular Weight |
64970 |
| Enzyme 6 Theoretical pI |
6.05 |
| Enzyme 6 GO Classification |
Not Available |
| Enzyme 6 General Function |
Not Available |
| Enzyme 6 Specific Function |
May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5-prime-monophosphate (IMP) and other purine nucleotides |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
633071  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P49902  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
5NTC_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1686 bp
ATGTCGACCTCCTGGAGTGATCGGTTACAGAATGCAGCAGATATGCCTGCTAACATGGAT
AAGCATGCCCTGAAAAAGTATCGTCGAGAAGCCTATCATCGGGTGTTTGTGAACCGAAGT
TTAGCAATGGAAAAGATAAAGTGTTTTGGTTTTGATATGGATTATACCCTTGCTGTGTAC
AAGTCCCCAGAGTATGAGTCCCTTGGTTTTGAGCTTACTGTGGAGAGATTAGTTTCTATT
GGCTATCCCCAGGAGTTGCTCAGCTTTGCTTATGATTCTACATTCCCTACCAGGGGACTT
GTCTTTGACACACTGTATGGAAATCTTTTGAAAGTCGATGCCTATGGAAACCTCTTGGTC
TGTGCACATGGATTTAACTTTATAAGGGGACCAGAAACTAGAGAACAGTATCCAAATAAA
TTTATCCAGCGAGATGATACTGAAAGATTTTACATTCTGAACACACTATTCAACCTACCA
GAGACCTACCTGTTGGCCTGCCTAGTAGATTTTTTTACTAATTGTCCCAGATATACCAGT
TGTGAAACAGGATTTAAAGATGGGGACCTCTTCATGTCCTACCGGAGTATGTTCCAGGAT
GTAAGAGATGCTGTTGACTGGGTTCATTACAAGGGCTCCCTTAAGGAAAAGACAGTTGAA
AATCTTGAGAAGTATGTAGTCAAAGATGGAAAACTGCCTTTGCTTCTGAGCCGGATGAAG
GAAGTAGGGAAAGTATTTCTTGCTACCAACAGTGACTATAAATATACAGATAAAATTATG
ACTTACCTGTTTGACTTCCCACATGGCCCCAAGCCTGGGAGCTCCCATCGACCATGGCAG
TCCTACTTTGACTTGATCTTGGTGGATGCACGGAAACCACTCTTTTTTGGAGAAGGCACA
GTACTGCGTCAGGTGGATACTAAAACTGGCAAGCTGAAAATTGGTACCTACACAGGGCCC
CTACAGCATGGTATCGTCTACTCAGGAGGTTCTTCTGATACGATCTGTGACCTGTTGGGA
GCCAAGGGAAAAGACATTTTGTATATTGGAGATCACATTTTTGGGGACATTTTAAAATCA
AAGAAACGGCAAGGGTGGCGAACTTTTTTGGTGATTCCTGAACTCGCACAGGAGCTACAT
GTCTGGACTGACAAGAGTTCACTTTTCGAAGAACTTCAGAGCTTGGATATTTTCTTGGCT
GAACTCTACAAGCATCTTGACAGCAGTAGCAATGAGCGTCCAGACATCAGTTCCATCCAG
AGACGTATTAAGAAAGTAACTCATGACATGGACATGTGCTATGGGATGATGGGAAGCCTG
TTTCGCAGTGGCTCCCGGCAGACCCTTTTTGCCAGTCAAGTGATGCGTTATGCTGACCTC
TATGCAGCATCTTTCATCAACCTGCTGTATTACCCTTTCAGCTACCTCTTCAGGGCTGCC
CATGTCTTGATGCCTCATGAATCAACGGTGGAGCACACACACGTAGATATCAATGAGATG
GAGTCTCCTCTTGCCACCCGGAACCGCACATCAGTGGATTTCAAAGACACTGACTACAAG
CGGCACCAGCTGACACGGTCAATTAGTGAGATTAAACCTCCCAACCTCTTCCCACTGGCC
CCCCAGGAAATTACACACTGCCATGACGAAGATGATGATGAAGAGGAGGAGGAGGAGGAA
GAATAA
|
| Enzyme 6 GenBank Gene ID |
D38524  |
| Enzyme 6 GeneCard ID |
NT5C2  |
| Enzyme 6 GenAtlas ID |
NT5C2  |
| Enzyme 6 HGNC ID |
HGNC:8022  |
| Enzyme 6 Chromosome Location |
10 |
| Enzyme 6 Locus |
10q24.32-q24.33 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Oka J, Matsumoto A, Hosokawa Y, Inoue S: Molecular cloning of human cytosolic purine 5'-nucleotidase. Biochem Biophys Res Commun. 1994 Nov 30;205(1):917-22. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5805 |
| Enzyme 7 Name |
Purine nucleoside phosphorylase |
| Enzyme 7 Synonyms |
- Inosine phosphorylase
- PNP
|
| Enzyme 7 Gene Name |
NP |
| Enzyme 7 Protein Sequence |
>Purine nucleoside phosphorylase
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST
VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL
NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ
MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
|
| Enzyme 7 Number of Residues |
289 |
| Enzyme 7 Molecular Weight |
32118 |
| Enzyme 7 Theoretical pI |
6.95 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- purine-nucleoside phosphorylase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring pentosyl groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Nucleotide transport and metabolism |
| Enzyme 7 Specific Function |
Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
35565  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P00491  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
PNPH_HUMAN  |
| Enzyme 7 PDB ID |
1RT9  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>870 bp
ATGGAGAACGGATACACCTATGAAGATTATAAGAACACTGCAGAATGGCTTCTGTCTCAT
ACTAAGCACCGACCTCAAGTTGCAATAATCTGTGGTTCTGGATTAGGAGGTCTGACTGAT
AAATTAACTCAGGCCCAGATCTTTGACTACAGTGAAATCCCCAACTTTCCTCGAAGTACA
GTGCCAGGTCATGCTGGCCGACTGGTGTTTGGGTTCCTGAATGGCAGGGCCTGTGTGATG
ATGCAGGGCAGGTTCCACATGTATGAAGGGTACCCACTCTGGAAGGTGACATTCCCAGTG
AGGGTTTTCCACCTTCTGGGTGTGGACACCCTGGTAGTCACCAATGCAGCAGGAGGGCTG
AACCCCAAGTTTGAGGTTGGAGATATCATGCTGATCCGTGACCATATCAACCTACCTGGT
TTCAGTGGTCAGAACCCTCTCAGAGGGCCCAATGATGAAAGGTTTGGAGATCGTTTCCCT
GCCATGTCTGATGCCTACGACCGGACTATGAGGCAGAGGGCTCTCAGTACCTGGAAACAA
ATGGGGGAGCAACGTGAGCTACAGGAAGGCACCTATGTGATGGTGGCAGGCCCCAGCTTT
GAGACTGTGGCAGAATGTCGTGTGCTGCAGAAGCTGGGAGCAGACGCTGTTGGCATGAGT
ACAGTACCAGAAGTTATCGTTGCACGGCACTGTGGACTTCGAGTCTTTGGCTTCTCACTC
ATCACTAACAAGGTCATCATGGATTATGAAAGCCTGGAGAAGGCCAACCATGAAGAAGTC
TTAGCAGCTGGCAAACAAGCTGCACAGAAATTGGAACAGTTTGTCTCCATTCTTATGGCC
AGCATTCCACTCCCTGACAAAGCCAGTTGA
|
| Enzyme 7 GenBank Gene ID |
X00737  |
| Enzyme 7 GeneCard ID |
NP  |
| Enzyme 7 GenAtlas ID |
NP  |
| Enzyme 7 HGNC ID |
HGNC:7892  |
| Enzyme 7 Chromosome Location |
14 |
| Enzyme 7 Locus |
14q13.1 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Williams SR, Goddard JM, Martin DW Jr: Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization. Nucleic Acids Res. 1984 Jul 25;12(14):5779-87. [PubMed
]
- Williams SR, Gekeler V, McIvor RS, Martin DW Jr: A human purine nucleoside phosphorylase deficiency caused by a single base change. J Biol Chem. 1987 Feb 15;262(5):2332-8. [PubMed
]
- Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. [PubMed
]
- Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE Jr, et al.: Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. J Biol Chem. 1990 Jan 25;265(3):1812-20. [PubMed
]
- Aust MR, Andrews LG, Barrett MJ, Norby-Slycord CJ, Markert ML: Molecular analysis of mutations in a patient with purine nucleoside phosphorylase deficiency. Am J Hum Genet. 1992 Oct;51(4):763-72. [PubMed
]
- Pannicke U, Tuchschmid P, Friedrich W, Bartram CR, Schwarz K: Two novel missense and frameshift mutations in exons 5 and 6 of the purine nucleoside phosphorylase (PNP) gene in a severe combined immunodeficiency (SCID) patient. Hum Genet. 1996 Dec;98(6):706-9. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5912 |
| Enzyme 8 Name |
Adenosine kinase |
| Enzyme 8 Synonyms |
- AK
- Adenosine 5'-phosphotransferase
|
| Enzyme 8 Gene Name |
ADK |
| Enzyme 8 Protein Sequence |
>Adenosine kinase
MAAAEEEPKPKKLKVEAPQALRENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAED
KHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFGCIGIDKFGEILKRKA
AEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEKHLDLEKNWMLVEKAR
VCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGN
ETEAATFAREQGFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFA
VLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTFPEKPD
FH
|
| Enzyme 8 Number of Residues |
362 |
| Enzyme 8 Molecular Weight |
40546 |
| Enzyme 8 Theoretical pI |
6.67 |
| Enzyme 8 GO Classification |
| Function |
- adenosine kinase activity
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- purine ribonucleoside salvage
- purine salvage
|
| Component |
| — |
|
| Enzyme 8 General Function |
Carbohydrate transport and metabolism |
| Enzyme 8 Specific Function |
ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- ATP + adenosine = ADP + AMP
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
1224125  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P55263  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
ADK_HUMAN  |
| Enzyme 8 PDB ID |
1BX4  |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1038 bp
ATGACGTCAGTCAGAGAAAATATTCTCTTTGGAATGGGAAATCCTCTGCTTGACATCTCT
GCTGTAGTGGACAAAGATTTCCTTGATAAGTATTCTCTGAAACCAAATGACCAAATCTTG
GCTGAAGACAAACACAAGGAACTGTTTGATGAACTTGTGAAAAAATTCAAAGTCGAATAT
CATGCTGGTGGCTCTACCCAGAATTCAATTAAAGTGGCTCAGTGGATGATTCAACAGCCA
CACAAAGCAGCAACATTTTTTGGATGCATTGGGATAGATAAATTTGGGGAGATCCTGAAG
AGAAAAGCTGCTGAAGCCCATGTGGATGCTCATTACTACGAGCAGAATGAGCAGCCAACA
GGAACTTGTGCTGCATGCATCACTGGTGACAACAGGTCCCTCATAGCTAATCTTGCTGCT
GCCAATTGTTATAAAAAGGAAAAACATCTTGATCTGGAGAAAAACTGGATGTTGGTAGAA
AAAGCAAGAGTTTGTTATATAGCAGGCTTTTTTCTTCACGTTTCCCCAGAGTCAGTATTA
AAGGTGGCTCACCATGCTTCTGAAAACAACAGGATTTTCACTTTGAATCTATCTGCACCG
TTTATTAGCCAGTTCTACAAGGAATCATTGATGAAAGTTATGCCTTATGTTGATATACTT
TTTGGAAATGAGACAGAAGCTGCCACTTTTGCTAGAGAGCAAGGCTTTGAGACTAAAGAC
ATTAAAGAGATAGCCAAAAAGACACAAGCCCTGCCAAAGATGAACTCAAAGAGGCAGCGA
ATCGTGATCTTCACCCAAGGGAGAGATGACACTATAATGGCTACAGAAAGTGAAGTCACT
GCTTTTGCTGTCTTGGATCAAGACCAGAAAGAAATTATTGATACCAATGGAGCTGGAGAT
GCATTTGTTGGAGGTTTTCTGTCTCAACTGGTCTCTGACAAGCCTCTGACTGAATGTATC
CGTGCTGGCCACTATGCAGCAAGCATCATAATTAGACGGACTGGCTGCACCTTTCCTGAG
AAGCCAGACTTCCACTGA
|
| Enzyme 8 GenBank Gene ID |
U50196  |
| Enzyme 8 GeneCard ID |
ADK  |
| Enzyme 8 GenAtlas ID |
ADK  |
| Enzyme 8 HGNC ID |
HGNC:257  |
| Enzyme 8 Chromosome Location |
10 |
| Enzyme 8 Locus |
10q22|10q11-q24 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Spychala J, Datta NS, Takabayashi K, Datta M, Fox IH, Gribbin T, Mitchell BS: Cloning of human adenosine kinase cDNA: sequence similarity to microbial ribokinases and fructokinases. Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1232-7. [PubMed
]
- Singh B, Hao W, Wu Z, Eigl B, Gupta RS: Cloning and characterization of cDNA for adenosine kinase from mammalian (Chinese hamster, mouse, human and rat) species. High frequency mutants of Chinese hamster ovary cells involve structural alterations in the gene. Eur J Biochem. 1996 Oct 15;241(2):564-71. [PubMed
]
- McNally T, Helfrich RJ, Cowart M, Dorwin SA, Meuth JL, Idler KB, Klute KA, Simmer RL, Kowaluk EA, Halbert DN: Cloning and expression of the adenosine kinase gene from rat and human tissues. Biochem Biophys Res Commun. 1997 Feb 24;231(3):645-50. [PubMed
]
- Mathews II, Erion MD, Ealick SE: Structure of human adenosine kinase at 1.5 A resolution. Biochemistry. 1998 Nov 10;37(45):15607-20. [PubMed
]
- Maguire PB, Wynne KJ, Harney DF, O'Donoghue NM, Stephens G, Fitzgerald DJ: Identification of the phosphotyrosine proteome from thrombin activated platelets. Proteomics. 2002 Jun;2(6):642-8. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5933 |
| Enzyme 9 Name |
Putative adenosylhomocysteinase 3 |
| Enzyme 9 Synonyms |
- S-adenosyl-L- homocysteine hydrolase 3
- AdoHcyase 3
|
| Enzyme 9 Gene Name |
KIAA0828 |
| Enzyme 9 Protein Sequence |
>Putative adenosylhomocysteinase 3
MSVQVVSAAAAAKVPEVELKDLSPSEAESQLGLSTAAVGAMAPPAGGGDPEAPAPAAERP
PVPGPGSGPAAALSPAAGKVPQASAMKRSDPHHQHQRHRDGGEALVSPDGTVTEAPRTVK
KQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNS
KGSSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTA
VLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVE
GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVN
DSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYV
TEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGH
SNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCSTVPTFVLSITA
TTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNK
NGPFKPNYYRY
|
| Enzyme 9 Number of Residues |
611 |
| Enzyme 9 Molecular Weight |
66722 |
| Enzyme 9 Theoretical pI |
7.39 |
| Enzyme 9 GO Classification |
| Function |
- adenosylhomocysteinase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ether bonds
- trialkylsulfonium hydrolase activity
|
| Process |
- cellular metabolism
- metabolism
- one-carbon compound metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 9 General Function |
Coenzyme transport and metabolism |
| Enzyme 9 Specific Function |
S-adenosyl-L-homocysteine + H(2)O = L- homocysteine + adenosine |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
4240145  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q96HN2  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
SAHH3_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1860 bp
GAGCCGGTGGTTGCAGCGGAGGCGGTGATGTCGGTGCAGGTTGTGTCAGCCGCGGCTGCC
GCCAAGGTGCCTGAGGTGGAGCTGAAGGACCTGAGCCCCTCCGAGGCGGAGTCGCAACTA
GGACTGAGCACGGCCGCCGTGGGCGCCATGGCCCCCCCGGCGGGCGGTGGAGACCCTGAG
GCTCCAGCTCCCGCCGCGGAGCGGCCCCCGGTCCCCGGCCCGGGCTCGGGGCCCGCCGCC
GCTCTCAGCCCCGCCGCCGGGAAGGTGCCTCAGGCGTCGGCCATGAAGCGGAGCGACCCA
CATCACCAGCACCAGCGGCACCGCGACGGCGGCGAGGCCCTGGTCAGCCCCGACGGCACC
GTCACCGAGGCGCCGCGCACAGTCAAGAAGATCCAGTTTGCTGACCAGAAGCAAGAATTC
AACAAACGTCCCACCAAAATTGGACGTCGCTCTTTGTCTCGTTCCATTTCTCAGTCATCT
ACTGACAGCTACAGCTCAGCGGCTTCATATACAGATAGCTCTGATGATGAGACATCGCCC
AGGGACAAGCAGCAAAAGAACTCTAAGGGAAGCAGTGACTTCTGTGTTAAGAACATCAAA
CAGGCAGAGTTTGGACGAAGAGAAATTGAAATTGCTGAACAAGAAATGCCTGCATTGATG
GCTTTGAGGAAGAGAGCTCAAGGAGAAAAGCCTTTGGCTGGAGCCAAAATCGTGGGTTGC
ACACACATCACTGCTCAGACTGCTGTGCTTATGGAAACTCTGGGTGCTCTGGGGGCCCAG
TGCCGATGGGCTGCCTGCAACATCTATTCCACTCTCAATGAAGTGGCTGCTGCTCTAGCA
GAAAGTGGATTTCCTGTTTTTGCCTGGAAGGGAGAGTCAGAAGATGACTTTTGGTGGTGT
ATCGATAGATGTGTGAATGTGGAGGGCTGGCAGCCAAACATGATCTTGGATGATGGAGGG
GATCTTACCCACTGGATTTATAAAAAGTATCCCAACATGTTTAAGAAAATCAAGGGCATA
GTAGAGGAGAGTGTTACTGGAGTTCACAGGCTGTACCAACTGTCCAAAGCTGGGAAGCTG
TGTGTTCCAGCCATGAATGTCAATGACTCAGTCACCAAACAGAAATTTGACAACCTCTAC
TGTTGCCGTGAATCAATTCTTGATGGACTTAAAAGGACAACAGACATGATGTTTGGTGGA
AAGCAAGTGGTAGTCTGTGGCTATGGAGAGGTGGGGAAAGGGTGCTGTGCTGCCCTGAAA
GCCATGGGCTCCATTGTGTATGTAACTGAAATTGACCCCATCTGTGCCCTGCAAGCCTGT
ATGGATGGATTTCGACTGGTGAAATTAAATGAGGTCATCCGACAAGTGGACATTGTTATT
ACCTGTACAGGTAACAAGAATGTGGTAACCAGAGAGCACTTGGACCGTATGAAGAATAGC
TGCATCGTTTGTAACATGGGACATTCCAACACAGAGATTGACGTGGCGAGTCTGCGGACA
CCAGAACTGACCTGGGAGCGAGTGAGATCTCAAGTTGACCATGTGATATGGCCTGATGGC
AAGAGGATAGTACTGCTGGCAGAGGGCCGCCTGCTGAACCTTAGCTGCTCCACAGTGCCT
ACATTTGTGCTCTCAATCACTGCTACTACTCAGGCTCTTGCCTTGATAGAGCTTTACAAT
GCTCCTGAGGGTCGCTATAAGCAGGATGTCTACCTGTTGCCCAAGAAGATGGATGAGTAT
GTGGCCAGCCTACACCTGCCTACCTTTGATGCCCACTTGACAGAGCTGACAGATGAACAG
GCCAAGTATCTGGGACTCAACAAGAATGGGCCCTTCAAGCCTAATTACTACAGGTATTAA
|
| Enzyme 9 GenBank Gene ID |
AB020635  |
| Enzyme 9 GeneCard ID |
Not Available |
| Enzyme 9 GenAtlas ID |
Not Available |
| Enzyme 9 HGNC ID |
Not Available |
| Enzyme 9 Chromosome Location |
7 |
| Enzyme 9 Locus |
7q32.1 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5935 |
| Enzyme 10 Name |
Putative adenosylhomocysteinase 2 |
| Enzyme 10 Synonyms |
- S-adenosyl-L- homocysteine hydrolase 2
- AdoHcyase 2
- S-adenosylhomocysteine hydrolase-like 1
- DC-expressed AHCY-like molecule
|
| Enzyme 10 Gene Name |
AHCYL1 |
| Enzyme 10 Protein Sequence |
>Putative adenosylhomocysteinase 2
MSMPDAMPLPGVGEELKQAKEIEDAEKYSFMATVTKAPKKQIQFADDMQEFTKFPTKTGR
RSLSRSISQSSTDSYSSAASYTDSSDDEVSPREKQQTNSKGSSNFCVKNIKQAEFGRREI
EIAEQDMSALISLRKRAQGEKPLAGAKIVGCTHITAQTAVLIETLCALGAQCRWSACNIY
STQNEVAAALAEAGVAVFAWKGESEDDFWWCIDRCVNMDGWQANMILDDGGDLTHWVYKK
YPNVFKKIRGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDG
LKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQACMDGFRVVKL
NEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVR
SQVDHVIWPDGKRVVLLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQD
VYLLPKKMDEYVASLHLPSFDAHLTELTDDQAKYLGLNKNGPFKPNYYRY
|
| Enzyme 10 Number of Residues |
530 |
| Enzyme 10 Molecular Weight |
58952 |
| Enzyme 10 Theoretical pI |
6.87 |
| Enzyme 10 GO Classification |
| Function |
- adenosylhomocysteinase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ether bonds
- trialkylsulfonium hydrolase activity
|
| Process |
- cellular metabolism
- metabolism
- one-carbon compound metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 10 General Function |
Coenzyme transport and metabolism |
| Enzyme 10 Specific Function |
S-adenosyl-L-homocysteine + H(2)O = L- homocysteine + adenosine |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
16588687  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
O43865  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
SAHH2_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1593 bp
ATGTCGATGCCTGACGCGATGCCGCTGCCCGGGGTCGGGGAGGAGCTGAAGCAGGCCAAG
GAGATCGAGGACGCCGAGAAGTACTCCTTCATGGCCACCGTCACCAAGGCGCCCAAGAAG
CAAATCCAGTTTGCTGATGACATGCAGGAGTTCACCAAATTCCCCACCAAAACTGGCCGA
AGATCTTTGTCTCGCTCGATCTCACAGTCCTCCACTGACAGCTACAGTTCAGCTGCATCC
TACACAGATAGCTCTGATGATGAGGTTTCTCCCCGAGAGAAGCAGCAAACCAACTCCAAG
GGCAGCAGCAATTTCTGTGTGAAGAACATCAAGCAGGCAGAATTTGGACGCCGGGAGATT
GAGATTGCAGAGCAAGACATGTCTGCTCTGATTTCACTCAGGAAACGTGCTCAGGGGGAG
AAGCCCTTGGCTGGTGCTAAAATAGTGGGCTGTACACACATCACAGCCCAGACAGCGGTG
TTGATTGAGACACTCTGTGCCCTGGGGGCTCAGTGCCGCTGGTCTGCTTGTAACATCTAC
TCAACTCAGAATGAAGTAGCTGCAGCACTGGCTGAGGCTGGAGTTGCAGTGTTCGCTTGG
AAGGGCGAGTCAGAAGATGACTTCTGGTGGTGTATTGACCGCTGTGTGAACATGGATGGG
TGGCAGGCCAACATGATCCTGGATGATGGGGGAGACTTAACCCACTGGGTTTATAAGAAG
TATCCAAACGTGTTTAAGAAGATCCGAGGCATTGTGGAAGAGAGCGTGACTGGTGTTCAC
AGGCTGTATCAGCTCTCCAAAGCTGGGAAGCTCTGTGTTCCGGCCATGAACGTCAATGAT
TCTGTTACCAAACAGAAGTTTGATAACTTGTACTGCTGCCGAGAATCCATTTTGGATGGC
CTGAAGAGGACCACAGATGTGATGTTTGGTGGGAAACAAGTGGTGGTGTGTGGCTATGGT
GAGGTAGGCAAGGGCTGCTGTGCTGCTCTCAAAGCTCTTGGAGCAATTGTCTACATTACC
GAAATCGACCCCATCTGTGCTCTGCAGGCCTGCATGGATGGGTTCAGGGTGGTAAAGCTA
AATGAAGTCATCCGGCAAGTCGATGTCGTAATAACTTGCACAGGAAATAAGAATGTAGTG
ACACGGGAGCACTTGGATCGCATGAAAAACAGTTGTATCGTATGCAATATGGGCCACTCC
AACACAGAAATCGATGTGACCAGCCTCCGCACTCCGGAGCTGACGTGGGAGCGAGTACGT
TCTCAGGTGGACCATGTCATCTGGCCAGATGGCAAACGAGTTGTCCTCCTGGCAGAGGGT
CGTCTACTCAATTTGAGCTGCTCCACAGTTCCCACCTTTGTTCTGTCCATCACAGCCACA
ACACAGGCTTTGGCACTGATAGAACTCTATAATGCACCCGAGGGGCGATACAAGCAGGAT
GTGTACTTGCTTCCTAAGAAAATGGATGAATACGTTGCCAGCTTGCATCTGCCATCATTT
GATGCCCACCTTACAGAGCTGACAGATGACCAAGCAAAATATCTGGGACTCAACAAAAAT
GGGCCATTCAAACCTAATTATTACAGATACTAA
|
| Enzyme 10 GenBank Gene ID |
AF315687  |
| Enzyme 10 GeneCard ID |
AHCYL1  |
| Enzyme 10 GenAtlas ID |
AHCYL1  |
| Enzyme 10 HGNC ID |
HGNC:344  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
1p13.2 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Dekker JW, Budhia S, Angel NZ, Cooper BJ, Clark GJ, Hart DN, Kato M: Identification of an S-adenosylhomocysteine hydrolase-like transcript induced during dendritic cell differentiation. Immunogenetics. 2002 Mar;53(12):993-1001. Epub 2002 Feb 13. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5937 |
| Enzyme 11 Name |
Adenosine deaminase |
| Enzyme 11 Synonyms |
- Adenosine aminohydrolase
|
| Enzyme 11 Gene Name |
ADA |
| Enzyme 11 Protein Sequence |
>Adenosine deaminase
MAQTPAFDKPKVELHVHLDGSIKPETILYYGRRRGIALPANTAEGLLNVIGMDKPLTLPD
FLAKFDYYMPAIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVEPIPWNQA
EGDLTPDEVVALVGQGLQEGERDFGVKARSILCCMRHQPNWSPKVVELCKKYQQQTVVAI
DLAGDETIPGSSLLPGHVQAYQEAVKSGIHRTVHAGEVGSAEVVKEAVDILKTERLGHGY
HTLEDQALYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRLKNDQANYSLNTDDPLIF
KSTLDTDYQMTKRDMGFTEEEFKRLNINAAKSSFLPEDEKRELLDLLYKAYGMPPSASAG
QNL
|
| Enzyme 11 Number of Residues |
363 |
| Enzyme 11 Molecular Weight |
40765 |
| Enzyme 11 Theoretical pI |
5.80 |
| Enzyme 11 GO Classification |
| Function |
- adenosine deaminase activity
- catalytic activity
- deaminase activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside monophosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside monophosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 11 General Function |
Replication, recombination and repair |
| Enzyme 11 Specific Function |
Adenosine + H(2)O = inosine + NH(3) |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- adenosine + H2O = inosine + ammonia
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
28380  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
P00813  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
ADA_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1092 bp
ATGGCCCAGACGCCCGCCTTCGACAAGCCCAAAGTAGAACTGCATGTCCACCTAGACGGA
TCCATCAAGCCTGAAACCATCTTATACTATGGCAGGAGGAGAGGGATCGCCCTCCCAGCT
AACACAGCAGAGGGGCTGCTGAACGTCATTGGCATGGACAAGCCGCTCACCCTTCCAGAC
TTCCTGGCCAAGTTTGACTACTACATGCCTGCTATCGCGGGCTGCCGGGAGGCTATCAAA
AGGATCGCCTATGAGTTTGTAGAGATGAAGGCCAAAGAGGGCGTGGTGTATGTGGAGGTG
CGGTACAGTCCGCACCTGCTGGCCAACTCCAAAGTGGAGCCAATCCCCTGGAACCAGGCT
GAAGGGGACCTCACCCCAGACGAGGTGGTGGCCCTAGTGGGCCAGGGCCTGCAGGAGGGG
GAGCGAGACTTCGGGGTCAAGGCCCGGTCCATCCTGTGCTGCATGCGCCACCAGCCCAAC
TGGTCCCCCAAGGTGGTGGAGCTGTGTAAGAAGTACCAGCAGCAGACCGTGGTGGCCATT
GACCTGGCTGGAGATGAGACCATCCCAGGAAGCAGCCTCTTGCCTGGACATGTCCAGGCC
TACCAGGAGGCTGTGAAGAGCGGCATTCACCGTACTGTCCACGCCGGGGAGGTGGGCTCG
GCCGAAGTAGTAAAAGAGGCTGTGGACATACTCAAGACAGAGCGGCTGGGACACGGCTAC
CACACCCTGGAAGACCAGGCCCTTTATAACAGGCTGCGGCAGGAAAACATGCACTTCGAG
ATCTGCCCCTGGTCCAGCTACCTCACTGGTGCCTGGAAGCCGGACACGGAGCATGCAGTC
ATTCGGCTCAAAAATGACCAGGCTAACTACTCGCTCAACACAGATGACCCGCTCATCTTC
AAGTCCACCCTGGACACTGATTACCAGATGACCAAACGGGACATGGGCTTTACTGAAGAG
GAGTTTAAAAGGCTGAACATCAATGCGGCCAAATCTAGTTTCCTCCCAGAAGATGAAAAG
AGGGAGCTTCTCGACCTGCTCTATAAAGCCTATGGGATGCCACCTTCAGCCTCTGCAGGG
CAGAACCTCTGA
|
| Enzyme 11 GenBank Gene ID |
X02994  |
| Enzyme 11 GeneCard ID |
ADA  |
| Enzyme 11 GenAtlas ID |
ADA  |
| Enzyme 11 HGNC ID |
HGNC:186  |
| Enzyme 11 Chromosome Location |
20 |
| Enzyme 11 Locus |
20q12-q13.11 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Daddona PE, Shewach DS, Kelley WN, Argos P, Markham AF, Orkin SH: Human adenosine deaminase. cDNA and complete primary amino acid sequence. J Biol Chem. 1984 Oct 10;259(19):12101-6. [PubMed
]
- Wiginton DA, Adrian GS, Hutton JJ: Sequence of human adenosine deaminase cDNA including the coding region and a small intron. Nucleic Acids Res. 1984 Mar 12;12(5):2439-46. [PubMed
]
- Valerio D, Duyvesteyn MG, Dekker BM, Weeda G, Berkvens TM, van der Voorn L, van Ormondt H, van der Eb AJ: Adenosine deaminase: characterization and expression of a gene with a remarkable promoter. EMBO J. 1985 Feb;4(2):437-43. [PubMed
]
- Wiginton DA, Kaplan DJ, States JC, Akeson AL, Perme CM, Bilyk IJ, Vaughn AJ, Lattier DL, Hutton JJ: Complete sequence and structure of the gene for human adenosine deaminase. Biochemistry. 1986 Dec 16;25(25):8234-44. [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
]
- Orkin SH, Daddona PE, Shewach DS, Markham AF, Bruns GA, Goff SC, Kelley WN: Molecular cloning of human adenosine deaminase gene sequences. J Biol Chem. 1983 Nov 10;258(21):12753-6. [PubMed
]
- Hirschhorn R, Yang DR, Israni A: An Asp8Asn substitution results in the adenosine deaminase (ADA) genetic polymorphism (ADA 2 allozyme): occurrence on different chromosomal backgrounds and apparent intragenic crossover. Ann Hum Genet. 1994 Jan;58(Pt 1):1-9. [PubMed
]
- Adrian GS, Wiginton DA, Hutton JJ: Structure of adenosine deaminase mRNAs from normal and adenosine deaminase-deficient human cell lines. Mol Cell Biol. 1984 Sep;4(9):1712-7. [PubMed
]
- Bonthron DT, Markham AF, Ginsburg D, Orkin SH: Identification of a point mutation in the adenosine deaminase gene responsible for immunodeficiency. J Clin Invest. 1985 Aug;76(2):894-7. [PubMed
]
- Akeson AL, Wiginton DA, Dusing MR, States JC, Hutton JJ: Mutant human adenosine deaminase alleles and their expression by transfection into fibroblasts. J Biol Chem. 1988 Nov 5;263(31):16291-6. [PubMed
]
- Hirschhorn R, Tzall S, Ellenbogen A, Orkin SH: Identification of a point mutation resulting in a heat-labile adenosine deaminase (ADA) in two unrelated children with partial ADA deficiency. J Clin Invest. 1989 Feb;83(2):497-501. [PubMed
]
- Hirschhorn R: Identification of two new missense mutations (R156C and S291L) in two ADA- SCID patients unusual for response to therapy with partial exchange transfusions. Hum Mutat. 1992;1(2):166-8. [PubMed
]
- Santisteban I, Arredondo-Vega FX, Kelly S, Mary A, Fischer A, Hummell DS, Lawton A, Sorensen RU, Stiehm ER, Uribe L, et al.: Novel splicing, missense, and deletion mutations in seven adenosine deaminase-deficient patients with late/delayed onset of combined immunodeficiency disease. Contribution of genotype to phenotype. J Clin Invest. 1993 Nov;92(5):2291-302. [PubMed
]
- Yang DR, Huie ML, Hirschhorn R: Homozygosity for a missense mutation (G20R) associated with neonatal onset adenosine deaminase-deficient severe combined immunodeficiency (ADA-SCID). Clin Immunol Immunopathol. 1994 Feb;70(2):171-5. [PubMed
]
- Santisteban I, Arredondo-Vega FX, Kelly S, Loubser M, Meydan N, Roifman C, Howell PL, Bowen T, Weinberg KI, Schroeder ML, et al.: Three new adenosine deaminase mutations that define a splicing enhancer and cause severe and partial phenotypes: implications for evolution of a CpG hotspot and expression of a transduced ADA cDNA. Hum Mol Genet. 1995 Nov;4(11):2081-7. [PubMed
]
- Santisteban I, Arredondo-Vega FX, Kelly S, Debre M, Fischer A, Perignon JL, Hilman B, elDahr J, Dreyfus DH, Gelfand EW, et al.: Four new adenosine deaminase mutations, altering a zinc-binding histidine, two conserved alanines, and a 5' splice site. Hum Mutat. 1995;5(3):243-50. [PubMed
]
- Hirschhorn R, Borkowsky W, Jiang CK, Yang DR, Jenkins T: Two newly identified mutations (Thr233Ile and Leu152Met) in partially adenosine deaminase-deficient (ADA-) individuals that result in differing biochemical and metabolic phenotypes. Hum Genet. 1997 Jul;100(1):22-9. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6980 |
| Enzyme 12 Name |
Adenosine A1 receptor |
| Enzyme 12 Synonyms |
Not Available |
| Enzyme 12 Gene Name |
ADORA1 |
| Enzyme 12 Protein Sequence |
>Adenosine A1 receptor
MPPSISAFQAAYIGIEVLIALVSVPGNVLVIWAVKVNQALRDATFCFIVSLAVADVAVGA
LVIPLAILINIGPQTYFHTCLMVACPVLILTQSSILALLAIAVDRYLRVKIPLRYKMVVT
PRRAAVAIAGCWILSFVVGLTPMFGWNNLSAVERAWAANGSMGEPVIKCEFEKVISMEYM
VYFNFFVWVLPPLLLMVLIYLEVFYLIRKQLNKKVSASSGDPQKYYGKELKIAKSLALIL
FLFALSWLPLHILNCITLFCPSCHKPSILTYIAIFLTHGNSAMNPIVYAFRIQKFRVTFL
KIWNDHFRCQPAPPIDEDLPEERPDD
|
| Enzyme 12 Number of Residues |
326 |
| Enzyme 12 Molecular Weight |
36512 |
| Enzyme 12 Theoretical pI |
8.75 |
| Enzyme 12 GO Classification |
| Function |
- A1 adenosine receptor activity, G-protein coupled
- G-protein coupled receptor activity
- adenosine receptor activity, G-protein coupled
- nucleotide receptor activity, G-protein coupled
- purinergic nucleotide receptor activity, G-protein coupled
- receptor activity
- rhodopsin-like receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 12 General Function |
Not Available |
| Enzyme 12 Specific Function |
Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
Not Available |
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
Not Available |
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
256155  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P30542  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
AA1R_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>981 bp
ATGCCGCCCTCCATCTCAGCTTTCCAGGCCGCCTACATCGGCATCGAGGTGCTCATCGCC
CTGGTCTCTGTGCCCGGGAACGTGCTGGTGATCTGGGCGGTGAAGGTGAACCAGGCGCTG
CGGGATGCCACCTTCTGCTTCATCGTGTCGCTGGCGGTGGCTGATGTGGCCGTGGGTGCC
CTGGTCATCCCCCTCGCCATCCTCATCAACATTGGGCCACAGACCTACTTCCACACCTGC
CTCATGGTTGCCTGTCCGGTCCTCATCCTCACCCAGAGCTCCATCCTGGCCCTGCTGGCA
ATTGCGGTGGACCGCTACCTCCGGGTCAAGATCCCTCTCCGGTACAAGATGGTGGTGACC
CCCCGGAGGGCGGCGGTGGCCATAGCCGGCTGCTGGATCCTCTCCTTCGTGGTGGGACTG
ACCCCTATGTTTGGCTGGAACAATCTGAGTGCGGTGGAGCGGGCCTGGGCAGCCAACGGC
AGCATGGGGGAGCCCGTGATCAAGTGCGAGTTCGAGAAGGTCATCAGCATGGAGTACATG
GTCTACTTCAACTTCTTTGTGTGGGTGCTCCCCCCGCTTCTCCTCATGGTCCTCATCTAC
CTGGAGGTCTTCTACCTAATCCGCAAGCAGCTCAACAAGAAGGTGTCGGCCTCCTCCGGC
GACCCGCAGAAGTACTATGGGAAGGAGCTGAAGATCGCCAAGTCGCTGGCCCTCATCCTC
TTCCTCTTTGCCCTCAGCTGGCTGCCTTTGCACATCCTCAACTGCATCACCCTCTTCTGC
CCGTCCTGCCACAAGCCCAGCATCCTTACCTACATTGCCATCTTCCTCACGCACGGCAAC
TCGGCCATGAACCCCATTGTCTATGCCTTCCGCATCCAGAAGTTCCGCGTCACCTTCCTT
AAGATTTGGAATGACCATTTCCGCTGCCAGCCTGCACCTCCCATTGACGAGGATCTCCCA
GAAGAGAGGCCTGATGACTAG
|
| Enzyme 12 GenBank Gene ID |
S45235  |
| Enzyme 12 GeneCard ID |
ADORA1  |
| Enzyme 12 GenAtlas ID |
ADORA1  |
| Enzyme 12 HGNC ID |
HGNC:262  |
| Enzyme 12 Chromosome Location |
1 |
| Enzyme 12 Locus |
1q32.1 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Libert F, Van Sande J, Lefort A, Czernilofsky A, Dumont JE, Vassart G, Ensinger HA, Mendla KD: Cloning and functional characterization of a human A1 adenosine receptor. Biochem Biophys Res Commun. 1992 Sep 16;187(2):919-26. [PubMed
]
- Townsend-Nicholson A, Shine J: Molecular cloning and characterisation of a human brain A1 adenosine receptor cDNA. Brain Res Mol Brain Res. 1992 Dec;16(3-4):365-70. [PubMed
]
- Ren H, Stiles GL: Characterization of the human A1 adenosine receptor gene. Evidence for alternative splicing. J Biol Chem. 1994 Jan 28;269(4):3104-10. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6982 |
| Enzyme 13 Name |
Adenosine A2a receptor |
| Enzyme 13 Synonyms |
Not Available |
| Enzyme 13 Gene Name |
ADORA2A |
| Enzyme 13 Protein Sequence |
>Adenosine A2a receptor
MPIMGSSVYITVELAIAVLAILGNVLVCWAVWLNSNLQNVTNYFVVSLAAADIAVGVLAI
PFAITISTGFCAACHGCLFIACFVLVLTQSSIFSLLAIAIDRYIAIRIPLRYNGLVTGTR
AKGIIAICWVLSFAIGLTPMLGWNNCGQPKEGKNHSQGCGEGQVACLFEDVVPMNYMVYF
NFFACVLVPLLLMLGVYLRIFLAARRQLKQMESQPLPGERARSTLQKEVHAAKSLAIIVG
LFALCWLPLHIINCFTFFCPDCSHAPLWLMYLAIVLSHTNSVVNPFIYAYRIREFRQTFR
KIIRSHVLRQQEPFKAAGTSARVLAAHGSDGEQVSLRLNGHPPGVWANGSAPHPERRPNG
YALGLVSGGSAQESQGNTGLPDVELLSHELKGVCPEPPGLDDPLAQDGAGVS
|
| Enzyme 13 Number of Residues |
412 |
| Enzyme 13 Molecular Weight |
44708 |
| Enzyme 13 Theoretical pI |
8.05 |
| Enzyme 13 GO Classification |
| Function |
- A2A adenosine receptor activity, G-protein coupled
- G-protein coupled receptor activity
- adenosine receptor activity, G-protein coupled
- nucleotide receptor activity, G-protein coupled
- purinergic nucleotide receptor activity, G-protein coupled
- receptor activity
- rhodopsin-like receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 13 General Function |
Not Available |
| Enzyme 13 Specific Function |
Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
Not Available |
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
Not Available |
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
177892  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
P29274  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
AA2AR_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1230 bp
ATGGGCTCCTCGGTGTACATCACGGTGGAGCTGGCCATTGCTGTGCTGGCCATCCTGGGC
AATGTGCTGGTGTGCTGGGCCGTGTGGCTCAACAGCAACCTGCAGAACGTCACCAACTAC
TTTGTGGTGTCACTGGCGGCGGCCGACATCGCAGTGGGTGTGCTCGCCATCCCCTTTGCC
ATCACCATCAGCACCGGGTTCTGCGCTGCCTGCCACGGCTGCCTCTTCATTGCCTGCTTC
GTCCTGGTCCTCACGCAGAGCTCCATCTTCAGTCTCCTGGCCATCGCCATTGACCGCTAC
ATTGCCATCCGCATCCCGCTCCGGTACAATGGCTTGGTGACCGGCACGAGGGCTAAGGGC
ATCATTGCCATCTGCTGGGTGCTGTCGTTTGCCATCGGCCTGACTCCCATGCTAGGTTGG
AACAACTGCGGTCAGCCAAAGGAGGGCAAGAACCACTCCCAGGGCTGCGGGGAGGGCCAA
GTGGCCTGTCTCTTTGAGGATGTGGTCCCCATGAACTACATGGTGTACTTCAACTTCTTT
GCCTGTGTGCTGGTGCCCCTGCTGCTCATGCTGGGTGTCTATTTGCGGATCTTCCTGGCG
GCGCGACGACAGCTGAAGCAGATGGAGAGCCAGCCTCTGCCGGGGGAGCGGGCACGGTCC
ACACTGCAGAAGGAGGTCCATGCTGCCAAGTCACTGGCCATCATTGTGGGGCTCTTTGCC
CTCTGCTGGCTGCCCCTACACATCATCAACTGCTTCACTTTCTTCTGCCCCGACTGCAGC
CACGCCCCTCTCTGGCTCATGTACCTGGCCATCGTCCTCTCCCACACCAATTCGGTTGTG
AATCCCTTCATCTACGCCTACCGTATCCGCGAGTTCCGCCAGACCTTCCGCAAGATCATT
CGCAGCCACGTCCTGAGGCAGCAAGAACCTTTCAAGGCAGCTGGCACCAGTGCCCGGGTC
TTGGCAGCTCATGGCAGTGACGGAGAGCAGGTCAGCCTCCGTCTCAACGGCCACCCGCCA
GGAGTGTGGGCCAACGGCAGTGCTCCCCACCCTGAGCGGAGGCCCAATGGCTATGCCCTG
GGGCTGGTGAGTGGAGGGAGTGCCCAAGAGTCCCAGGGGAACACGGGCCTCCCAGACGTG
GAGCTCCTTAGCCATGAGCTCAAGGGAGTGTGCCCAGAGCCCCCTGGCCTAGATGACCCC
CTGGCCCAGGATGGAGCAGGAGTGTCCTGA
|
| Enzyme 13 GenBank Gene ID |
M97370  |
| Enzyme 13 GeneCard ID |
ADORA2A  |
| Enzyme 13 GenAtlas ID |
ADORA2A  |
| Enzyme 13 HGNC ID |
HGNC:263  |
| Enzyme 13 Chromosome Location |
22 |
| Enzyme 13 Locus |
22q11.23 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Furlong TJ, Pierce KD, Selbie LA, Shine J: Molecular characterization of a human brain adenosine A2 receptor. Brain Res Mol Brain Res. 1992 Sep;15(1-2):62-6. [PubMed
]
- Le F, Townsend-Nicholson A, Baker E, Sutherland GR, Schofield PR: Characterization and chromosomal localization of the human A2a adenosine receptor gene: ADORA2A. Biochem Biophys Res Commun. 1996 Jun 14;223(2):461-7. [PubMed
]
- Kim J, Wess J, van Rhee AM, Schoneberg T, Jacobson KA: Site-directed mutagenesis identifies residues involved in ligand recognition in the human A2a adenosine receptor. J Biol Chem. 1995 Jun 9;270(23):13987-97. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
6985 |
| Enzyme 14 Name |
Adenosine A3 receptor |
| Enzyme 14 Synonyms |
Not Available |
| Enzyme 14 Gene Name |
ADORA3 |
| Enzyme 14 Protein Sequence |
>Adenosine A3 receptor
MPNNSTALSLANVTYITMEIFIGLCAIVGNVLVICVVKLNPSLQTTTFYFIVSLALADIA
VGVLVMPLAIVVSLGITIHFYSCLFMTCLLLIFTHASIMSLLAIAVDRYLRVKLTVRYKR
VTTHRRIWLALGLCWLVSFLVGLTPMFGWNMKLTSEYHRNVTFLSCQFVSVMRMDYMVYF
SFLTWIFIPLVVMCAIYLDIFYIIRNKLSLNLSNSKETGAFYGREFKTAKSLFLVLFLFA
LSWLPLSIINCIIYFNGEVPQLVLYMGILLSHANSMMNPIVYAYKIKKFKETYLLILKAC
VVCHPSDSLDTSIEKNSE
|
| Enzyme 14 Number of Residues |
318 |
| Enzyme 14 Molecular Weight |
36185 |
| Enzyme 14 Theoretical pI |
9.04 |
| Enzyme 14 GO Classification |
| Function |
- A3 adenosine receptor activity, G-protein coupled
- G-protein coupled receptor activity
- adenosine receptor activity, G-protein coupled
- nucleotide receptor activity, G-protein coupled
- purinergic nucleotide receptor activity, G-protein coupled
- receptor activity
- rhodopsin-like receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 14 General Function |
Not Available |
| Enzyme 14 Specific Function |
Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. Possible role in reproduction |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
Not Available |
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
- 15-37
49-72
85-106
127-148
178-198
232-255
262-284
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
349449  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P33765  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
AA3R_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>957 bp
ATGCCCAACAACAGCACTACTCTGTCATTGGCCAATGTTACCTACATCACCATGGAAATT
TTCATTGGACTCTGCGCCATAGTGGGCAACGTGCTGGTCATCTGCGTGGTCAAGCTGAAC
CCCAGCCTGCAGACCACCACCTTCTATTTCATTGTCTCTCTAGCCCTGGCTGACATTGCT
GTTGGGGTGCTGGTCATGCCTTTGGCCATTGTTGTCAGCCTGGGCATCACAATCCACTTC
TACAGCTGCCTTTTTATGACTTGCCTACTGCTTATCTTTACCCACGCCTCCATCATGTCC
TTGCTGGCCATCGCTGTGGACCGATACTTGCGGGTCAAGCTTACCGTCAGATACAAGAGG
GTCACCACTCACAGAAGAATATGGCTGGCCCTGGGCCTTTGCTGGCTGGTGTCATTCCTG
GTGGGATTGACCCCCATGTTTGGCTGGAACATGAAACTGACCTCAGAGTACCACAGAAAT
GTCACCTTCCTTTCATGCCAATTTGTTTCCGTCATGAGAATGGACTACATGGTATACTTC
AGCTTCCTCACCTGGATTTTCATCCCCCTGGTTGTCATGTGCGCCATCTATCTTGACATC
TTTTACATCATTCGGAACAAACTCAGTCTGAACTTATCTAACTCCAAAGAGACAGGTGCA
TTTTATGGACGGGAGTTCAAGACGGCTAAGTCCTTGTTTCTGGTTCTTTTCTTGTTTGCT
CTGTCATGGCTGCCTTTATCTATCATCAACTGCATCATCTACTTTAATGGTGAGGTACCA
CAGCTTGTGCTGTACATGGGCATCCTGCTGTCCCATGCCAACTCCATGATGAACCCTATC
GTCTATGCCTATAAAATAAAGAAGTTCAAGGAAACCTACCTTTTGATCCTCAAAGCCTGT
GTGGTCTGCCATCCCTCTGATTCTTTGGACACAAGCATTGAGAAGAATTCTGAGTAG
|
| Enzyme 14 GenBank Gene ID |
L20463  |
| Enzyme 14 GeneCard ID |
ADORA3  |
| Enzyme 14 GenAtlas ID |
ADORA3  |
| Enzyme 14 HGNC ID |
HGNC:268  |
| Enzyme 14 Chromosome Location |
1 |
| Enzyme 14 Locus |
1p13.2 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Sajjadi FG, Firestein GS: cDNA cloning and sequence analysis of the human A3 adenosine receptor. Biochim Biophys Acta. 1993 Oct 7;1179(1):105-7. [PubMed
]
- Salvatore CA, Jacobson MA, Taylor HE, Linden J, Johnson RG: Molecular cloning and characterization of the human A3 adenosine receptor. Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):10365-9. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Murphy WJ, Eizirik E, Johnson WE, Zhang YP, Ryder OA, O'Brien SJ: Molecular phylogenetics and the origins of placental mammals. Nature. 2001 Feb 1;409(6820):614-8. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
6986 |
| Enzyme 15 Name |
Adenosine A2b receptor |
| Enzyme 15 Synonyms |
Not Available |
| Enzyme 15 Gene Name |
ADORA2B |
| Enzyme 15 Protein Sequence |
>Adenosine A2b receptor
MLLETQDALYVALELVIAALSVAGNVLVCAAVGTANTLQTPTNYFLVSLAAADVAVGLFA
IPFAITISLGFCTDFYGCLFLACFVLVLTQSSIFSLLAVAVDRYLAICVPLRYKSLVTGT
RARGVIAVLWVLAFGIGLTPFLGWNSKDSATNNCTEPWDGTTNESCCLVKCLFENVVPMS
YMVYFNFFGCVLPPLLIMLVIYIKIFLVACRQLQRTELMDHSRTTLQREIHAAKSLAMIV
GIFALCWLPVHAVNCVTLFQPAQGKNKPKWAMNMAILLSHANSVVNPIVYAYRNRDFRYT
FHKIISRYLLCQADVKSGNGQAGVQPALGVGL
|
| Enzyme 15 Number of Residues |
332 |
| Enzyme 15 Molecular Weight |
36333 |
| Enzyme 15 Theoretical pI |
8.31 |
| Enzyme 15 GO Classification |
| Function |
- A2B adenosine receptor activity, G-protein coupled
- G-protein coupled receptor activity
- adenosine receptor activity, G-protein coupled
- nucleotide receptor activity, G-protein coupled
- purinergic nucleotide receptor activity, G-protein coupled
- receptor activity
- rhodopsin-like receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- G-protein coupled receptor protein signaling pathway
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- signal transduction
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 15 General Function |
Not Available |
| Enzyme 15 Specific Function |
Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
Not Available |
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
- 9-31
45-67
79-101
122-144
179-203
236-259
268-291
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
178150  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P29275  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
AA2BR_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>999 bp
ATGCTGCTGGAGACACAGGACGCGCTGTACGTGGCGCTGGAGCTGGTCATCGCCGCGCTT
TCGGTGGCGGGCAACGTGCTGGTGTGCGCCGCGGTGGGCACGGCGAACACTCTGCAGACG
CCCACCAACTACTTCCTGGTGTCCCTGGCTGCGGCCGACGTGGCCGTGGGGCTCTTCGCC
ATCCCCTTTGCCATCACCATCAGCCTGGGCTTCTGCACTGACTTCTACGGCTGCCTCTTC
CTCGCCTGCTTCGTGCTGGTGCTCACGCAGAGCTCCATCTTCAGCCTTCTGGCCGTGGCA
GTCGACAGATACCTGGCCATCTGTGTCCCGCTCAGGTATAAAAGTTTGGTCACGGGGACC
CGAGCAAGAGGGGTCATTGCTGTCCTCTGGGTCCTTGCCTTTGGCATCGGATTGACTCCA
TTCCTGGGGTGGAACAGTAAAGACAGTGCCACCAACAACTGCACAGAACCCTGGGATGGA
ACCACGAATGAAAGCTGCTGCCTTGTGAAGTGTCTCTTTGAGAATGTGGTCCCCATGAGC
TACATGGTATATTTCAATTTCTTTGGGTGTGTTCTGCCCCCACTGCTTATAATGCTGGTG
ATCTACATTAAGATCTTCCTGGTGGCCTGCAGGCAGCTTCAGCGCACTGAGCTGATGGAC
CACTCGAGGACCACCCTCCAGCGGGAGATCCATGCAGCCAAGTCACTGGCCATGATTGTG
GGGATTTTTGCCCTGTGCTGGTTACCTGTGCATGCTGTTAACTGTGTCACTCTTTTCCAG
CCAGCTCAGGGTAAAAATAAGCCCAAGTGGGCAATGAATATGGCCATTCTTCTGTCACAT
GCCAATTCAGTTGTCAATCCCATTGTCTATGCTTACCGGAACCGAGACTTCCGCTACACT
TTTCACAAAATTATCTCCAGGTATCTTCTCTGCCAAGCAGATGTCAAGAGTGGGAATGGT
CAGGCTGGGGTACAGCCTGCTCTCGGTGTGGGCCTATGA
|
| Enzyme 15 GenBank Gene ID |
M97759  |
| Enzyme 15 GeneCard ID |
ADORA2B  |
| Enzyme 15 GenAtlas ID |
ADORA2B  |
| Enzyme 15 HGNC ID |
HGNC:264  |
| Enzyme 15 Chromosome Location |
17 |
| Enzyme 15 Locus |
17p12-p11.2 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Pierce KD, Furlong TJ, Selbie LA, Shine J: Molecular cloning and expression of an adenosine A2b receptor from human brain. Biochem Biophys Res Commun. 1992 Aug 31;187(1):86-93. [PubMed
]
- Jacobson MA, Johnson RG, Luneau CJ, Salvatore CA: Cloning and chromosomal localization of the human A2b adenosine receptor gene (ADORA2B) and its pseudogene. Genomics. 1995 May 20;27(2):374-6. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
8749 |
| Enzyme 16 Name |
Cytosolic 5'-nucleotidase III |
| Enzyme 16 Synonyms |
- cN-III
- Pyrimidine 5'- nucleotidase 1
- P5'N-1
- P5N-1
- PN-I
- Uridine 5'-monophosphate hydrolase 1
- p36
|
| Enzyme 16 Gene Name |
NT5C3 |
| Enzyme 16 Protein Sequence |
>Cytosolic 5'-nucleotidase III
MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRKTGRKTKIIEMMPEFQKSSV
RIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDEC
RKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKLKEIVAESDVM
LKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLK
GFKGELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYL
NDRVDELLEKYMDSYDIVLVQDESLEVANSILQKIL
|
| Enzyme 16 Number of Residues |
336 |
| Enzyme 16 Molecular Weight |
37949 |
| Enzyme 16 Theoretical pI |
7.15 |
| Enzyme 16 GO Classification |
Not Available |
| Enzyme 16 General Function |
Not Available |
| Enzyme 16 Specific Function |
A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
11245474  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q9H0P0  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
5NT3_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>861 bp
ATGATGCCAGAATTCCAGAAAAGTTCAGTTCGAATCAAGAACCCTACAAGAGTAGAAGAA
ATTATCTGTGGTCTTATCAAAGGAGGAGCTGCCAAACTTCAGATAATAACGGACTTTGAT
ATGACACTCAGTAGATTTTCATATAAAGGGAAAAGATGCCCAACATGTCATAATATCATT
GACAACTGTAAGCTGGTTACAGATGAATGTAGAAAAAAGTTATTGCAACTAAAGGAAAAA
TACTACGCTATTGAAGTTGATCCTGTTCTTACTGTAGAAGAGAAGTACCCTTATATGGTG
GAATGGTATACTAAATCACATGGTTTGCTTGTTCAGCAAGCTTTACCAAAAGCTAAACTT
AAAGAAATTGTGGCAGAATCTGACGTTATGCTCAAAGAAGGATATGAGAATTTCTTTGAT
AAGCTCCAACAACATAGCATCCCCGTGTTCATATTTTCGGCTGGAATCGGCGATGTACTA
GAGGAAGTTATTCGTCAAGCTGGTGTTTATCATCCCAATGTCAAAGTTGTGTCCAATTTT
ATGGATTTTGATGAAACTGGGGTGCTCAAAGGATTTAAAGGAGAACTAATTCATGTATTT
AACAAACATGATGGTGCCTTGAGGAATACAGAATATTTCAATCAACTAAAAGACAATAGT
AACATAATTCTTCTGGGAGACTCCCAAGGAGACTTAAGAATGGCAGATGGAGTGGCCAAT
GTTGAGCACATTCTGAAAATTGGATATCTAAATGATAGAGTGGATGAGCTTTTAGAAAAG
TACATGGACTCTTATGATATTGTTTTAGTACAAGATGAATCATTAGAAGTAGCCAACTCT
ATTTTACAGAAGATTCTATAA
|
| Enzyme 16 GenBank Gene ID |
AF312735  |
| Enzyme 16 GeneCard ID |
NT5C3  |
| Enzyme 16 GenAtlas ID |
NT5C3  |
| Enzyme 16 HGNC ID |
HGNC:17820  |
| Enzyme 16 Chromosome Location |
7 |
| Enzyme 16 Locus |
7p14.3 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Amici A, Emanuelli M, Raffaelli N, Ruggieri S, Saccucci F, Magni G: Human erythrocyte pyrimidine 5-nucleotidase, PN-I, is identical to p36, a protein associated to lupus inclusion formation in response to alpha-interferon. Blood. 2000 Aug 15;96(4):1596-8. [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
]
- Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed
]
- Rich SA, Bose M, Tempst P, Rudofsky UH: Purification, microsequencing, and immunolocalization of p36, a new interferon-alpha-induced protein that is associated with human lupus inclusions. J Biol Chem. 1996 Jan 12;271(2):1118-26. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
8826 |
| Enzyme 17 Name |
Adenosine 3'-phospho 5'-phosphosulfate transporter 1 |
| Enzyme 17 Synonyms |
- PAPS transporter 1
- Solute carrier family 35 member B2
- Putative MAPK-activating protein PM15
- Putative NF-kappa-B-activating protein 48
|
| Enzyme 17 Gene Name |
SLC35B2 |
| Enzyme 17 Protein Sequence |
>Adenosine 3'-phospho 5'-phosphosulfate transporter 1
MDARWWAVVVLAAFPSLGAGGETPEAPPESWTQLWFFRFVVNAAGYASFMVPGYLLVQYF
RRKNYLETGRGLCFPLVKACVFGNEPKASDEVPLAPRTEAAETTPMWQALKLLFCATGLQ
VSYLTWGVLQERVMTRSYGATATSPGERFTDSQFLVLMNRVLALIVAGLSCVLCKQPRHG
APMYRYSFASLSNVLSSWCQYEALKFVSFPTQVLAKASKVIPVMLMGKLVSRRSYEHWEY
LTATLISIGVSMFLLSSGPEPRSSPATTLSGLILLAGYIAFDSFTSNWQDALFAYKMSSV
QMMFGVNFFSCLFTVGSLLEQGALLEGTRFMGRHSEFAAHALLLSICSACGQLFIFYTIG
QFGAAVFTIIMTLRQAFAILLSCLLYGHTVTVVGGLGVAVVFAALLLRVYARGRLKQRGK
KAVPVESPVQKV
|
| Enzyme 17 Number of Residues |
432 |
| Enzyme 17 Molecular Weight |
47515 |
| Enzyme 17 Theoretical pI |
9.40 |
| Enzyme 17 GO Classification |
Not Available |
| Enzyme 17 General Function |
Not Available |
| Enzyme 17 Specific Function |
Mediates the transport of adenosine 3'-phospho 5'- phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi. May indirectly participate in activation of the NF- kappa-B and MAPK pathways |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
Not Available |
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
- 5-25
40-60
109-129
154-174
238-258
265-285
299-319
353-373
387-407
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
32480471  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q8TB61  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
S35B2_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>1299 bp
ATGGACGCCAGATGGTGGGCAGTGGTGGTGCTGGCTGCGTTCCCCTCCCTAGGGGCAGGT
GGGGAGACTCCCGAAGCCCCTCCGGAGTCATGGACCCAGCTATGGTTCTTCCGATTTGTG
GTGAATGCTGCTGGCTATGCCAGCTTTATGGTACCTGGCTACCTCCTGGTGCAGTACTTC
AGGCGGAAGAACTACCTGGAGACCGGTAGGGGCCTCTGCTTTCCCCTGGTGAAAGCTTGT
GTGTTTGGCAATGAGCCCAAGGCCTCTGATGAGGTTCCCCTGGCGCCCCGAACAGAGGCG
GCAGAGACCACCCCGATGTGGCAGGCCCTGAAGCTGCTCTTCTGTGCCACAGGGCTCCAG
GTGTCTTATCTGACTTGGGGTGTGCTGCAGGAAAGAGTGATGACCCGCAGCTATGGGGCC
ACAGCCACATCACCGGGTGAGCGCTTTACGGACTCGCAGTTCCTGGTGCTAATGAACCGA
GTGCTGGCACTGATTGTGGCTGGCCTCTCCTGTGTTCTCTGCAAGCAGCCCCGGCATGGG
GCACCCATGTACCGGTACTCCTTTGCCAGCCTGTCCAATGTGCTTAGCAGCTGGTGCCAA
TACGAAGCTCTTAAGTTCGTCAGCTTCCCCACCCAGGTGCTGGCCAAGGCCTCTAAGGTG
ATCCCTGTCATGCTGATGGGAAAGCTTGTGTCTCGGCGCAGCTACGAACACTGGGAGTAC
CTGACAGCCACCCTCATCTCCATTGGGGTCAGCATGTTTCTGCTATCCAGCGGACCAGAG
CCCCGCAGCTCCCCAGCCACCACACTCTCAGGCCTCATCTTACTGGCAGGTTATATTGCT
TTTGACAGCTTCACCTCAAACTGGCAGGATGCCCTGTTTGCCTATAAGATGTCATCGGTG
CAGATGATGTTTGGGGTCAATTTCTTCTCCTGCCTCTTCACAGTGGGCTCACTGCTAGAA
CAGGGGGCCCTACTGGAGGGAACCCGCTTCATGGGGCGACACAGTGAGTTTGCTGCCCAT
GCCCTGCTACTCTCCATCTGCTCCGCATGTGGCCAGCTCTTCATCTTTTACACCATTGGG
CAGTTTGGGGCTGCCGTCTTCACCATCATCATGACCCTCCGCCAGGCCTTTGCCATCCTT
CTTTCCTGCCTTCTCTATGGCCACACTGTCACTGTGGTGGGAGGGCTGGGGGTGGCTGTG
GTCTTTGCTGCCCTCCTGCTCAGAGTCTACGCGCGGGGCCGTCTAAAGCAACGGGGAAAG
AAGGCTGTGCCTGTTGAGTCTCCTGTGCAGAAGGTTTGA
|
| Enzyme 17 GenBank Gene ID |
AB106538  |
| Enzyme 17 GeneCard ID |
SLC35B2  |
| Enzyme 17 GenAtlas ID |
SLC35B2  |
| Enzyme 17 HGNC ID |
HGNC:16872  |
| Enzyme 17 Chromosome Location |
6 |
| Enzyme 17 Locus |
6p12.1-p11.2 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Kamiyama S, Suda T, Ueda R, Suzuki M, Okubo R, Kikuchi N, Chiba Y, Goto S, Toyoda H, Saigo K, Watanabe M, Narimatsu H, Jigami Y, Nishihara S: Molecular cloning and identification of 3'-phosphoadenosine 5'-phosphosulfate transporter. J Biol Chem. 2003 Jul 11;278(28):25958-63. Epub 2003 Apr 25. [PubMed
]
- Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed
]
- 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 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
13068 |
| Enzyme 18 Name |
cDNA FLJ76252, highly similar to Homo sapiens S-adenosylhomocysteine hydrolase |
| Enzyme 18 Synonyms |
- AHCY, mRNA
- S-adenosylhomocysteine hydrolase, isoform CRA_a
|
| Enzyme 18 Gene Name |
AHCY |
| Enzyme 18 Protein Sequence |
>cDNA FLJ76252, highly similar to Homo sapiens S-adenosylhomocysteine hydrolase
MSDKLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVET
AVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYF
KDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINV
NDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVI
ITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIG
HFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSN
SFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMS
CDGPFKPDHYRY
|
| Enzyme 18 Number of Residues |
432 |
| Enzyme 18 Molecular Weight |
47717 |
| Enzyme 18 Theoretical pI |
6.29 |
| Enzyme 18 GO Classification |
Not Available |
| Enzyme 18 General Function |
Coenzyme transport and metabolism |
| Enzyme 18 Specific Function |
Not Available |
| Enzyme 18 Pathways |
Not Available |
| Enzyme 18 Reactions |
Not Available |
| Enzyme 18 Pfam Domain Function |
Not Available |
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
158261867  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
A8K307  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
A8K307_HUMAN  |
| Enzyme 18 PDB ID |
1LI4  |
| Enzyme 18 PDB File |
Show |
| Enzyme 18 3D Structure |
|
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
Not Available |
| Enzyme 18 GenBank Gene ID |
AK290422  |
| Enzyme 18 GeneCard ID |
A8K307  |
| Enzyme 18 GenAtlas ID |
Not Available |
| Enzyme 18 HGNC ID |
Not Available |
| Enzyme 18 Chromosome Location |
Not Available |
| Enzyme 18 Locus |
Not Available |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
Not Available |
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
15061 |
| Enzyme 19 Name |
cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA |
| Enzyme 19 Synonyms |
Not Available |
| Enzyme 19 Gene Name |
Not Available |
| Enzyme 19 Protein Sequence |
>cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
SQEITHCHDEDDDEEEEEEEE
|
| Enzyme 19 Number of Residues |
561 |
| Enzyme 19 Molecular Weight |
64960 |
| Enzyme 19 Theoretical pI |
6.05 |
| Enzyme 19 GO Classification |
Not Available |
| Enzyme 19 General Function |
Not Available |
| Enzyme 19 Specific Function |
Not Available |
| Enzyme 19 Pathways |
Not Available |
| Enzyme 19 Reactions |
Not Available |
| Enzyme 19 Pfam Domain Function |
Not Available |
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
158256766  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
A8K6K2  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
A8K6K2_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>1686 bp
ATGTCAACCTCCTGGAGTGATCGGTTACAGAATGCAGCAGATATGCCTGCTAACATGGAT
AAGCATGCCCTGAAAAAGTATCGTCGAGAAGCCTATCATCGGGTGTTTGTGAACCGAAGT
TTAGCAATGGAAAAGATAAAGTGTTTTGGTTTTGATATGGATTATACCCTTGCTGTGTAC
AAGTCCCCAGAGTATGAGTCCCTTGGTTTTGAGCTTACTGTGGAGAGATTAGTTTCTATT
GGCTATCCCCAGGAGTTGCTCAGCTTTGCTTATGATTCTACATTCCCTACCAGGGGACTT
GTCTTTGACACACTGTATGGAAATCTTTTGAAAGTCGATGCCTATGGAAACCTCTTGGTC
TGTGCACATGGATTTAACTTTATAAGGGGACCAGAAACTAGAGAACAGTATCCAAATAAA
TTTATCCAGCGAGATGATACTGAAAGATTTTACATTCTGAACACACTATTCAACCTACCA
GAGACCTACCTGTTGGCCTGCCTAGTAGATTTTTTTACTAATTGTCCCAGATATACCAGT
TGTGAAACAGGATTTAAAGATGGGGACCTCTTCATGTCCTACCGGAGTATGTTCCAGGAT
GTAAGAGATGCTGTTGACTGGGTTCATTACAAGGGCTCCCTTAAGGAAAAGACAGTTGAA
AATCTTGAGAAGTATGTAGTCAAAGATGGAAAACTGCCTTTGCTTCTGAGCCGGATGAAG
GAAGTAGGGAAAGTATTTCTTGCTACCAACAGTGACTATAAATATACAGATAAAATTATG
ACTTACCTGTTTGACTTCCCACATGGCCCCAAGCCTGGGAGCTCCCATCGACCATGGCAG
TCCTACTTTGACTTGATCTTGGTGGATGCACGGAAACCACTCTTTTTTGGAGAAGGCACA
GTACTGCGTCAGGTGGATACTAAAACTGGCAAGCTGAAAATTGGTACCTACACAGGGCCC
CTACAGCATGGTATCGTCTACTCAGGAGGTTCTTCTGATACGATCTGTGACCTGTTGGGA
GCCAAGGGAAAAGACATTTTGTATATTGGAGATCACATTTTTGGGGACATTTTAAAATCA
AAGAAACGGCAAGGGTGGCGAACTTTTTTGGTGATTCCTGAACTCGCACAGGAGCTACAT
GTCTGGACTGACAAGAGTTCACTTTTCGAAGAACTTCAGAGCTTGGATATTTTCTTGGCT
GAACTCTACAAGCATCTTGACAGCAGTAGCAATGAGCGTCCAGACATCAGTTCCATCCAG
AGACGTATTAAGAAAGTAACTCATGACATGGACATGTGCTATGGGATGATGGGAAGCCTG
TTTCGCAGTGGCTCCCGGCAGACCCTTTTTGCCAGTCAAGTGATGCGTTATGCTGACCTC
TATGCAGCATCTTTCATCAACCTGCTGTATTACCCTTTCAGCTACCTCTTCAGGGCTGCC
CATGTCTTGATGCCTCATGAATCAACGGTGGAGCACACACACGTAGATATCAATGAGATG
GAGTCTCCTCTTGCCACCCGGAACCGCACATCAGTGGATTTCAAAGACACTGACTACAAG
CGGCACCAGCTGACACGGTCAATTAGTGAGATTAAACCTCCCAACCTCTTCCCACTGGCC
TCCCAGGAAATTACACACTGCCATGATGAAGATGATGATGAAGAGGAGGAGGAGGAGGAA
GAATAA
|
| Enzyme 19 GenBank Gene ID |
AK291667  |
| Enzyme 19 GeneCard ID |
A8K6K2  |
| Enzyme 19 GenAtlas ID |
Not Available |
| Enzyme 19 HGNC ID |
Not Available |
| Enzyme 19 Chromosome Location |
Not Available |
| Enzyme 19 Locus |
Not Available |
| Enzyme 19 SNPs |
Not Available |
| Enzyme 19 General References |
Not Available |
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
16422 |
| Enzyme 20 Name |
cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA |
| Enzyme 20 Synonyms |
Not Available |
| Enzyme 20 Gene Name |
Not Available |
| Enzyme 20 Protein Sequence |
>cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
MCPRAARAPATLLLALGAVLWPAAGAWELTILHTNDVHSRLEQTSEDSSKCVNASRCMGG
VARLFTKVQQIRRAEPNVLLLDAGDQYQGTIWFTVYRGAEVAHFMNALRYDAMALGNHEF
DNGVEGLIEPLLKEAKFPILSANIKAKGPLASQISGLYLPYKVLPVGDEVVGIVGYTSKE
TPFLSNPGTNLVFEDEITALQPEVDKLKTLNVNKIIALGHSGFEMDKLIAQKVRGVDVVV
GGHSNTFLYTGNPPSKEVPAGKYPFIVTSDDGRKVPVVQAYAFGKYLGYLKIEFDERGNV
ISSHGNPILLNSSIPEDPSIKADINKWRIKLDNYSTQELGKTIVYLDGSSQSCRFRECNM
GNLICDAMINNNLRHTDEMFWNHVSMCILNGGGIRSPIDERNNGTITWENLAAVLPFGGT
FDLVQLKGSTLKKAFEHSVHRYGQSTGEFLQVGGIHVVYDLSRKPGDRVVKLDVLCTKCR
VPSYDPLKMDEVYKVILPNFLANGGDGFQMIKDELLRHDSGDQDINVVSTYISKMKVIYP
AVEGRIKFSTGSHCHGSFSLIFLSLWAVIFVLYQ
|
| Enzyme 20 Number of Residues |
574 |
| Enzyme 20 Molecular Weight |
63396 |
| Enzyme 20 Theoretical pI |
7.04 |
| Enzyme 20 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide catabolism
- nucleotide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 20 General Function |
Nucleotide transport and metabolism |
| Enzyme 20 Specific Function |
Not Available |
| Enzyme 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
Not Available |
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
Not Available |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
B2RBH2  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
B2RBH2_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
Not Available |
| Enzyme 20 GenBank Gene ID |
AK314661  |
| Enzyme 20 GeneCard ID |
B2RBH2  |
| Enzyme 20 GenAtlas ID |
Not Available |
| Enzyme 20 HGNC ID |
Not Available |
| Enzyme 20 Chromosome Location |
Not Available |
| Enzyme 20 Locus |
Not Available |
| Enzyme 20 SNPs |
Not Available |
| Enzyme 20 General References |
Not Available |
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
17072 |
| Enzyme 21 Name |
Adenosine 3'-phospho 5'-phosphosulfate transporter 2 |
| Enzyme 21 Synonyms |
- PAPS transporter 2
- Solute carrier family 35 member B3
- 3'-phosphoadenosine 5'-phosphosulfate transporter
|
| Enzyme 21 Gene Name |
SLC35B3 |
| Enzyme 21 Protein Sequence |
>Adenosine 3'-phospho 5'-phosphosulfate transporter 2
MDLTQQAKDIQNITVQETNKNNSESIECSKITMDLKFNNSRKYISITVPSKTQTMSPHIK
SVDDVVVLGMNLSKFNKLTQFFICVAGVFVFYLIYGYLQELIFSVEGFKSCGWYLTLVQF
AFYSIFGLIELQLIQDKRRRIPGKTYMIIAFLTVGTMGLSNTSLGYLNYPTQVIFKCCKL
IPVMLGGVFIQGKRYNVADVSAAICMSLGLIWFTLADSTTAPNFNLTGVVLISLALCADA
VIGNVQEKAMKLHNASNSEMVLYSYSIGFVYILLGLTCTSGLGPAVTFCAKNPVRTYGYA
FLFSLTGYFGISFVLALIKIFGALIAVTVTTGRKAMTIVLSFIFFAKPFTFQYVWSGLLV
VLGIFLNVYSKNMDKIRLPSLYDLINKSVEARKSRTLAQTV
|
| Enzyme 21 Number of Residues |
401 |
| Enzyme 21 Molecular Weight |
44593 |
| Enzyme 21 Theoretical pI |
9.58 |
| Enzyme 21 GO Classification |
Not Available |
| Enzyme 21 General Function |
Not Available |
| Enzyme 21 Specific Function |
Mediates the transport of adenosine 3'-phospho 5'- phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi. Compensates for the insufficient expression of SLC35B2/PAPST1 during the synthesis of sulfated glycoconjugates in the colon |
| Enzyme 21 Pathways |
Not Available |
| Enzyme 21 Reactions |
Not Available |
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
- 78-98
114-134
147-167
170-190
196-216
223-243
267-287
298-317
324-346
349-369
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
Not Available |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q9H1N7  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
S35B3_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
Not Available |
| Enzyme 21 GenBank Gene ID |
AB231931  |
| Enzyme 21 GeneCard ID |
Q9H1N7  |
| Enzyme 21 GenAtlas ID |
SLC35B3  |
| Enzyme 21 HGNC ID |
HGNC:21601  |
| Enzyme 21 Chromosome Location |
Not Available |
| Enzyme 21 Locus |
Not Available |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [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 21 Metabolite References |
Not Available |