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Human Metabolome Database Version 2.5

 

Showing metabocard for Adenosine phosphosulfate (HMDB01003)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-24 23:46:23
Accession Number HMDB01003
Secondary Accession Numbers Not Available
Common Name Adenosine phosphosulfate
Description Adenosine phosphosulfate (also known as APS) is the initial compound formed by the action of ATP sulfurylase (or PAPS synthetase) on sulfate ions after sulfate uptake. PAPS synthetase 1 is a bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway.
Synonyms
  1. Adenosine Phosphosulfate
  2. Adenosine phosphosulfic acid
  3. adenosine 5'-sulphatophosphate
  4. Adenosine 5'-phosphosulfate
  5. adenosine sulfatophosphate
  6. adenylic acid monoanhydride with sulfurate
  7. adenylic acid monoanhydride with sulfuric acid
  8. adenylyl sulfate
  9. adenylyl-sulfate
  10. AMPS
  11. phosphosulfate
  12. sulfatophosphate
  13. APS
Chemical IUPAC Name 6-amino-9-[3,4-dihydroxy-5-[(hydroxy-sulfooxy-phosphoryl)oxymethyl]oxolan-2-yl]-purine
Chemical Formula C10H14N5O10PS
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide monophosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • primary amine
  • primary aromatic amine
  • sulfuric acid
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Purine metabolism
  • Component of Sulfur metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 427.284
Monoisotopic Molecular Weight 427.019897
Isomeric SMILES NC1=NC=NC2=C1N=CN2[C@@H]1O[C@H](COP(O)(=O)OS(O)(=O)=O)[C@@H](O)[C@H]1O
Canonical SMILES NC1=NC=NC2=C1N=CN2C1OC(COP(O)(=O)OS(O)(=O)=O)C(O)C1O
KEGG Compound ID C00224 Link Image
BioCyc ID APS Link Image
BiGG ID 34307 Link Image
Wikipedia Link amps Link Image
NuGOwiki Link HMDB01003 Link Image
Metagene Link HMDB01003 Link Image
METLIN ID 5933 Link Image
PubChem Compound 228 Link Image
PubChem Substance 2148 Link Image
ChEBI ID 17709 Link Image
CAS Registry Number 485-84-7
InChI Identifier InChI=1/C10H14N5O10PS/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-26(18,19)25-27(20,21)22/h2-4,6-7,10,16-17H,1H2,(H,18,19)(H2,11,12,13)(H,20,21,22)/t4-,6-,7-,10-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 3.29 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.64 [Predicted by ALOGPS]; -4 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location Not Available
Tissue Location
Tissue References
Fibroblasts —
Pancreas —
Platelet —
Prostate —
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Sulfate/Sulfite Metabolism SMP00041 Link Image map00920 Link Image
General References
  1. Mateos-Trigos G, Evans RJ, Heath MF: Effects of P2Y(1) and P2Y(12) receptor antagonists on ADP-induced shape change of equine platelets: comparison with human platelets. Platelets. 2002 Aug-Sep;13(5-6):285-92. [PubMed Link Image]
  2. Chou HC, Lang NP, Kadlubar FF: Metabolic activation of N-hydroxy arylamines and N-hydroxy heterocyclic amines by human sulfotransferase(s). Cancer Res. 1995 Feb 1;55(3):525-9. [PubMed Link Image]
  3. Al-Buheissi SZ, Patel HR, Meinl W, Hewer A, Bryan RL, Glatt H, Miller RA, Phillips DH: N-Acetyltransferase and sulfotransferase activity in human prostate: potential for carcinogen activation. Pharmacogenet Genomics. 2006 Jun;16(6):391-9. [PubMed Link Image]
  4. Keogh JR, Wolf MF, Overend ME, Tang L, Eaton JW: Biocompatibility of sulphonated polyurethane surfaces. Biomaterials. 1996 Oct;17(20):1987-94. [PubMed Link Image]
  5. Eto Y, Tokoro T, Handa T, Herschkowitz NN, Rennert OM: Acid mucopolysaccharide (AMPS) abnormality in multiple sulfatase deficiency: chemical compositions of AMPS in urine and liver. Pediatr Res. 1982 May;16(5):395-9. [PubMed Link Image]
  6. Slomiany BL, Liau YH, Sarosiek J, Tsukada H, Mizuta K, Rosenthal W, Slomiany A: Sulfation of glycolipids by human gastric mucosa in disease. Digestion. 1987;36(4):246-52. [PubMed Link Image]
  7. Raju U, Kadner S, Levitz M, Kaganowicz A, Blaustein A: Glucosiduronidation and esterification of androsterone by human breast tumors in vitro. Steroids. 1981 Apr;37(4):399-407. [PubMed Link Image]
  8. Eklund E, Roden L, Malmstrom M, Malmstrom A: Dermatan is a better substrate for 4-O-sulfation than chondroitin: implications in the generation of 4-O-sulfated, L-iduronate-rich galactosaminoglycans. Arch Biochem Biophys. 2000 Nov 15;383(2):171-7. [PubMed Link Image]
  9. Wikipedia Link Image
Metabolic Enzymes
  1. Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1
  2. Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 2
  3. Adenosine 3'-phospho 5'-phosphosulfate transporter 1
  4. cDNA FLJ75757, highly similar to Homo sapiens PAP-inositol-1,4- phosphatase
  5. Adenosine 3'-phospho 5'-phosphosulfate transporter 2
Enzyme 1 [top]
Enzyme 1 ID 5581
Enzyme 1 Name Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1
Enzyme 1 Synonyms
  1. PAPS synthetase 1
  2. PAPSS 1
  3. Sulfurylase kinase 1
  4. SK1
  5. SK 1[Includes: Sulfate adenylyltransferase
  6. Sulfate adenylate transferase
  7. SAT
  8. ATP-sulfurylase
  9. Adenylyl-sulfate kinase
  10. Adenylylsulfate 3'-phosphotransferase
  11. APS kinase
  12. Adenosine-5'-phosphosulfate 3'-phosphotransferase
  13. 3'- phosphoadenosine-5'-phosphosulfate synthetase]
Enzyme 1 Gene Name PAPSS1
Enzyme 1 Protein Sequence >Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 
MEIPGSLCKKVKLSNNAQNWGMQRATNVTYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGL
SGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLF
ADAGLVCITSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDVKGLYKKARAG
EIKGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVPVDASYEVKELYVP
ENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGG
VINLSVPIVLTATHEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTC
KNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDGLDQYRLTPTELKQKFKDMNADAVFAFQL
RNPVHNGHALLMQDTHKQLLERGYRRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGV
LNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPS
HGAKVLTMAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHHEDFEFISGTRMRKLAREGQK
PPEGFMAPKAWTVLTEYYKSLEKA
Enzyme 1 Number of Residues 624
Enzyme 1 Molecular Weight 70834
Enzyme 1 Theoretical pI 6.85
Enzyme 1 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • nucleotidyltransferase activity
  • purine nucleotide binding
  • sulfate adenylyltransferase (ATP) activity
  • sulfate adenylyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • physiological process
  • sulfate assimilation
  • sulfur metabolism
  • sulfur utilization
Component
—
Enzyme 1 General Function Inorganic ion transport and metabolism
Enzyme 1 Specific Function Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS:activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate- activation pathway. Also involved in the biosynthesis of sulfated L-selectin ligands in endothelial cells
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + sulfate = diphosphate + adenylylsulfate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 2673862 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O43252 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PAPS1_HUMAN Link Image
Enzyme 1 PDB ID 1X6V Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1875 bp 
ATGGAGATCCCCGGGAGCTTGTGCAAGAAAGTCAAGCTGAGCAATAACGCGCAGAACTGG
GGAATGCAGAGAGCAACCAATGTCACCTACCAAGCCCATCATGTCAGCAGGAACAAGAGA
GGTCAGGTGGTGGGGACCAGAGGTGGCTTTCGTGGTTGCACAGTTTGGCTAACAGGCTTG
TCTGGAGCGGGAAAGACTACTGTGAGCATGGCCTTGGAGGAGTACCTGGTTTGTCATGGT
ATTCCATGCTACACTCTGGATGGTGACAATATTCGTCAAGGTCTCAATAAAAATCTTGGC
TTTAGTCCTGAAGACAGAGAAGAGAATGTTCGACGCATCGCAGAAGTTGCTAAACTGTTT
GCAGATGCTGGCTTAGTGTGCATCACAAGTTTCATATCACCTTACACTCAGGATCGCAAC
AATGCAAGGCAAATTCATGAAGGTGCAAGTTTACCGTTTTTTGAAGTATTTGTTGATGCT
CCTCTGCATGTTTGTGAACAGAGGGATGTCAAAGGACTCTACAAAAAAGCCCGGGCAGGA
GAAATTAAAGGTTTCACTGGGATCGATTCTGAATATGAAAAGCCAGAGGCCCCTGAGTTG
GTGCTGAAAACAGACTCCTGTGATGTAAATGACTGTGTCCAGCAAGTTGTGGAACTTCTA
CAGGAACGGGATATTGTACCTGTGGATGCATCTTATGAAGTAAAAGAACTATATGTGCCA
GAAAATAAACTTCATTTGGCAAAAACAGATGCGGAAACATTACCAGCACTGAAAATTAAT
AAAGTGGATATGCAGTGGGTGCAGGTTTTGGCAGAAGGTTGGGCAACCCCATTGAATGGC
TTTATGAGAGAGAGGGAGTACTTGCAGTGCCTTCATTTTGATTGTCTTCTGGATGGAGGT
GTCATTAACTTGTCAGTACCTATAGTTCTGACTGCGACTCATGAAGATAAAGAGAGGCTG
GACGGCTGTACAGCATTTGCTCTGATGTATGAGGGCCGCCGTGTGGCCATTCTTCGCAAT
CCAGAGTTTTTTGAGCACAGGAAAGAGGAGCGCTGTGCCAGACAGTGGGGAACGACATGC
AAGAACCACCCCTATATTAAGATGGTGATGGAACAAGGAGATTGGCTGATTGGAGGAGAT
CTTCAAGTCTTGGATCGAGTTTATTGGAATGATGGTCTTGATCAGTATCGTCTTACTCCT
ACTGAGCTAAAGCAGAAATTTAAAGATATGAATGCTGATGCTGTCTTTGCATTTCAACTA
CGCAACCCAGTGCACAATGGACATGCCCTGTTAATGCAGGATACCCATAAGCAACTTCTA
GAGAGGGGCTACCGGCGCCCTGTCCTCCTCCTCCACCCTCTGGGTGCTTGGACAAAGGAT
GACGATGTTCCTTTGATGTGGCGTATGAAGCAGCATGCTGCAGTGTTGGAGGAAGGAGTT
CTGAATCCTGAGACGACAGTGGTGGCCATCTTCCCATCTCCCATGATGTATGCTGGACCA
ACTGAGGTCCAGTGGCATTGCAGAGCACGGATGGTTGCAGGAGCCAACTTTTACATTGTT
GGACGAGACCCTGCTGGCATGCCTCATCCAGAAACAGGGAAGGATCTTTATGAGCCAAGT
CATGGTGCCAAAGTGCTGACGATGGCCCCTGGTTTAATCACTTTGGAAATAGTTCCCTTT
CGAGTTGCAGCTTACAACAAGAAAAAGAAGCGTATGGACTACTATGACTCTGAACACCAT
GAAGACTTTGAATTTATTTCAGGAACACGAATGCGCAAACTTGCTCGAGAAGGCCAGAAA
CCACCTGAAGGTTTCATGGCTCCCAAGGCTTGGACCGTGCTGACAGAATACTACAAATCC
TTGGAGAAAGCTTAG
Enzyme 1 GenBank Gene ID Y10387 Link Image
Enzyme 1 GeneCard ID PAPSS1 Link Image
Enzyme 1 GenAtlas ID PAPSS1 Link Image
Enzyme 1 HGNC ID HGNC:8603 Link Image
Enzyme 1 Chromosome Location 4
Enzyme 1 Locus 4q24
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Girard JP, Baekkevold ES, Amalric F: Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase. FASEB J. 1998 May;12(7):603-12. [PubMed Link Image]
  2. Venkatachalam KV, Akita H, Strott CA: Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains. J Biol Chem. 1998 Jul 24;273(30):19311-20. [PubMed Link Image]
  3. Yanagisawa K, Sakakibara Y, Suiko M, Takami Y, Nakayama T, Nakajima H, Takayanagi K, Natori Y, Liu MC: cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme. Biosci Biotechnol Biochem. 1998 May;62(5):1037-40. [PubMed Link Image]
  4. Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, Moon E, Kim UJ, Xu JP, Siciliano MJ, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization. Biochem Biophys Res Commun. 2000 Feb 16;268(2):437-44. [PubMed Link Image]
  5. Venkatachalam KV, Fuda H, Koonin EV, Strott CA: Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase. J Biol Chem. 1999 Jan 29;274(5):2601-4. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5589
Enzyme 2 Name Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 2
Enzyme 2 Synonyms
  1. PAPS synthetase 2
  2. PAPSS 2
  3. Sulfurylase kinase 2
  4. SK2
  5. SK 2[Includes: Sulfate adenylyltransferase
  6. Sulfate adenylate transferase
  7. SAT
  8. ATP-sulfurylase
  9. Adenylyl-sulfate kinase
  10. Adenylylsulfate 3'-phosphotransferase
  11. APS kinase
  12. Adenosine-5'-phosphosulfate 3'-phosphotransferase
  13. 3'- phosphoadenosine-5'-phosphosulfate synthetase]
Enzyme 2 Gene Name PAPSS2
Enzyme 2 Protein Sequence >Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 
MSGIKKQKTENQQKSTNVVYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTISF
ALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS
FISPFAKDRENARKIHESAGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDS
DYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVPYTIIKDIHELFVPENKLDHVRAE
AETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVINMSIPIVL
PVSAEDKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVM
ESGDWLVGGDLQVLEKIRWNDGLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHAL
LMQDTRRRLLERGYKHPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLDPKSTIVAI
FPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAP
GLTSVEIIPFRVAAYNKAKKAMDFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKA
WKVLTDYYRSLEKN
Enzyme 2 Number of Residues 614
Enzyme 2 Molecular Weight 69502
Enzyme 2 Theoretical pI 8.13
Enzyme 2 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • nucleotidyltransferase activity
  • purine nucleotide binding
  • sulfate adenylyltransferase (ATP) activity
  • sulfate adenylyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • physiological process
  • sulfate assimilation
  • sulfur metabolism
  • sulfur utilization
Component
—
Enzyme 2 General Function Inorganic ion transport and metabolism
Enzyme 2 Specific Function Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS:activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate- activation pathway. May have a important role in skeletogenesis during postnatal growth
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + sulfate = diphosphate + adenylylsulfate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 3769610 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O95340 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PAPS2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1845 bp 
ATGTCGGGGATCAAGAAGCAAAAGACGGAGAACCAGCAGAAATCCACCAATGTAGTCTAT
CAGGCCCACCATGTGAGCAGGAATAAGAGAGGGCAAGTGGTTGGAACAAGGGGTGGGTTC
CGAGGATGTACCGTGTGGCTAACAGGTCTCTCTGGTGCTGGAAAAACAACGATAAGTTTT
GCCCTGGAGGAGTACCTTGTCTCCCATGCCATCCCTTGTTACTCCCTGGATGGGGACAAT
GTCCGTCATGGCCTTAACAGAAATCTCGGATTCTCTCCTGGGGACAGAGAGGAAAATATC
CGCCGGATTGCTGAGGTGGCTAAGCTGTTTGCTGATGCTGGTCTGGTCTGCATTACCAGC
TTTATTTCTCCATTCGCAAAGGATCGTGAGAATGCCCGCAAAATACATGAATCAGCAGGG
CTGCCATTCTTTGAAATATTTGTAGATGCACCTCTAAATATTTGTGAAAGCAGAGACGTA
AAAGGCCTCTATAAAAGGGCCAGAGCTGGGGAGATTAAAGGATTTACAGGTATTGATTCT
GATTATGAGAAACCTGAAACTCCTGAGCGTGTGCTTAAAACCAATTTGTCCACAGTGAGT
GACTGTGTCCACCAGGTAGTGGAACTTCTGCAAGAGCAGAACATTGTACCCTATACTATA
ATCAAAGATATCCACGAACTCTTTGTGCCGGAAAACAAACTTGACCACGTCCGAGCTGAG
GCTGAAACTCTCCCTTCATTATCAATTACTAAGCTGGATCTCCAGTGGGTCCAGGTTTTG
AGCGAAGGCTGGGCCACTCCCCTCAAAGGTTTCATGCGGGAGAAGGAGTACTTACAGGTT
ATGCACTTTGACACCCTGCTAGATGATGGCGTGATCAACATGAGCATCCCCATTGTACTG
CCCGTCTCTGCAGAGGATAAGACACGGCTGGAAGGGTGCAGCAAGTTTGTCCTGGCACAT
GGTGGACGGAGGGTAGCTATCTTACGAGACGCTGAATTCTATGAACACAGAAAAGAGGAA
CGCTGTTCCCGTGTTTGGGGGACAACATGTACAAAACACCCCCATATCAAAATGGTGATG
GAAAGTGGGGACTGGCTGGTTGGTGGAGACCTTCAGGTGCTGGAGAAAATAAGATGGAAT
GATGGGCTGGACCAATACCGTCTGACACCTCTGGAGCTCAAACAGAAATGTAAAGAAATG
AATGCTGATGCGGTGTTTGCATTCCAGTTGCGCAATCCTGTCCACAATGGCCATGCCCTG
TTGATGCAGGACACCTGCCGCAGGCTCCTAGAGAGGGGCTACAAGCACCCGGTCCTCCTA
CTACACCCTCTGGGCGGCTGGACCAAGGATGACGATGTGCCTCTAGACTGGCGGATGAAG
CAGCACGCGGCTGTGCTCGAGGAAGGGGTCCTGGATCCCAAGTCAACCATTGTTGCCATC
TTTCCGTCTCCCATGTTATATGCTGGCCCCACAGAGGTCCAGTGGCACTGCAGGTCCCGG
ATGATTGCGGGTGCCAATTTCTACATTGTGGGGAGGGACCCTGCAGGAATGCCCCATCCT
GAAACCAAGAAGGATCTGTATGAACCCACTCATGGGGGCAAGGTCTTGAGCATGGCCCCT
GGCCTCACCTCTGTGGAAATCATTCCATTCCGAGTGGCTGCCTACAACAAAGCCAAAAAA
GCCATGGACTTCTATGATCCAGCAAGGCACAATGAGTTTGACTTCATCTCAGGAACTCGA
ATGAGGAAGCTCGCCCGGGAAGGAGAGAATCCCCCAGATGGCTTCATGGCCCCCAAAGCA
TGGAAGGTCCTGACAGATTATTACAGGTCCCTGGAGAAGAACTAA
Enzyme 2 GenBank Gene ID AF091242 Link Image
Enzyme 2 GeneCard ID PAPSS2 Link Image
Enzyme 2 GenAtlas ID PAPSS2 Link Image
Enzyme 2 HGNC ID HGNC:8604 Link Image
Enzyme 2 Chromosome Location 10
Enzyme 2 Locus 10q23-q24
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. ul Haque MF, King LM, Krakow D, Cantor RM, Rusiniak ME, Swank RT, Superti-Furga A, Haque S, Abbas H, Ahmad W, Ahmad M, Cohn DH: Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse. Nat Genet. 1998 Oct;20(2):157-62. [PubMed Link Image]
  2. Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, Moon E, Kim UJ, Xu JP, Siciliano MJ, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization. Biochem Biophys Res Commun. 2000 Feb 16;268(2):437-44. [PubMed Link Image]
  3. Kurima K, Singh B, Schwartz NB: Genomic organization of the mouse and human genes encoding the ATP sulfurylase/adenosine 5'-phosphosulfate kinase isoform SK2. J Biol Chem. 1999 Nov 19;274(47):33306-12. [PubMed Link Image]
  4. Ahmad M, Haque MF, Ahmad W, Abbas H, Haque S, Krakow D, Rimoin DL, Lachman RS, Cohn DH: Distinct, autosomal recessive form of spondyloepimetaphyseal dysplasia segregating in an inbred Pakistani kindred. Am J Med Genet. 1998 Aug 6;78(5):468-73. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 8826
Enzyme 3 Name Adenosine 3'-phospho 5'-phosphosulfate transporter 1
Enzyme 3 Synonyms
  1. PAPS transporter 1
  2. Solute carrier family 35 member B2
  3. Putative MAPK-activating protein PM15
  4. Putative NF-kappa-B-activating protein 48
Enzyme 3 Gene Name SLC35B2
Enzyme 3 Protein Sequence >Adenosine 3'-phospho 5'-phosphosulfate transporter 1 
MDARWWAVVVLAAFPSLGAGGETPEAPPESWTQLWFFRFVVNAAGYASFMVPGYLLVQYF
RRKNYLETGRGLCFPLVKACVFGNEPKASDEVPLAPRTEAAETTPMWQALKLLFCATGLQ
VSYLTWGVLQERVMTRSYGATATSPGERFTDSQFLVLMNRVLALIVAGLSCVLCKQPRHG
APMYRYSFASLSNVLSSWCQYEALKFVSFPTQVLAKASKVIPVMLMGKLVSRRSYEHWEY
LTATLISIGVSMFLLSSGPEPRSSPATTLSGLILLAGYIAFDSFTSNWQDALFAYKMSSV
QMMFGVNFFSCLFTVGSLLEQGALLEGTRFMGRHSEFAAHALLLSICSACGQLFIFYTIG
QFGAAVFTIIMTLRQAFAILLSCLLYGHTVTVVGGLGVAVVFAALLLRVYARGRLKQRGK
KAVPVESPVQKV
Enzyme 3 Number of Residues 432
Enzyme 3 Molecular Weight 47515
Enzyme 3 Theoretical pI 9.40
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Not Available
Enzyme 3 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 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-20
Enzyme 3 Transmembrane Regions
  • 5-25 40-60 109-129 154-174 238-258 265-285 299-319 353-373 387-407
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 32480471 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q8TB61 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name S35B2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 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 3 GenBank Gene ID AB106538 Link Image
Enzyme 3 GeneCard ID SLC35B2 Link Image
Enzyme 3 GenAtlas ID SLC35B2 Link Image
Enzyme 3 HGNC ID HGNC:16872 Link Image
Enzyme 3 Chromosome Location 6
Enzyme 3 Locus 6p12.1-p11.2
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 13112
Enzyme 4 Name cDNA FLJ75757, highly similar to Homo sapiens PAP-inositol-1,4- phosphatase
Enzyme 4 Synonyms
  1. PIP gene
  2. 3'(2', 5'-bisphosphate nucleotidase 1, isoform CRA_a
Enzyme 4 Gene Name BPNT1
Enzyme 4 Protein Sequence >cDNA FLJ75757, highly similar to Homo sapiens PAP-inositol-1,4- phosphatase 
MASSNTVLMRLVASAYSIAQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICS
SLARKFPKLTIIGEEDLPSEEVDQELIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLD
GTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVLGRTIWGVLGLGAFGF
QLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFAS
PGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLRNYDYYASRVPE
SIKNALVP
Enzyme 4 Number of Residues 308
Enzyme 4 Molecular Weight 33393
Enzyme 4 Theoretical pI 5.41
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Carbohydrate transport and metabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function Not Available
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 158257318 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID A8K7C8 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A8K7C8_HUMAN Link Image
Enzyme 4 PDB ID 1JP4 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AK291943 Link Image
Enzyme 4 GeneCard ID A8K7C8 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 17072
Enzyme 5 Name Adenosine 3'-phospho 5'-phosphosulfate transporter 2
Enzyme 5 Synonyms
  1. PAPS transporter 2
  2. Solute carrier family 35 member B3
  3. 3'-phosphoadenosine 5'-phosphosulfate transporter
Enzyme 5 Gene Name SLC35B3
Enzyme 5 Protein Sequence >Adenosine 3'-phospho 5'-phosphosulfate transporter 2 
MDLTQQAKDIQNITVQETNKNNSESIECSKITMDLKFNNSRKYISITVPSKTQTMSPHIK
SVDDVVVLGMNLSKFNKLTQFFICVAGVFVFYLIYGYLQELIFSVEGFKSCGWYLTLVQF
AFYSIFGLIELQLIQDKRRRIPGKTYMIIAFLTVGTMGLSNTSLGYLNYPTQVIFKCCKL
IPVMLGGVFIQGKRYNVADVSAAICMSLGLIWFTLADSTTAPNFNLTGVVLISLALCADA
VIGNVQEKAMKLHNASNSEMVLYSYSIGFVYILLGLTCTSGLGPAVTFCAKNPVRTYGYA
FLFSLTGYFGISFVLALIKIFGALIAVTVTTGRKAMTIVLSFIFFAKPFTFQYVWSGLLV
VLGIFLNVYSKNMDKIRLPSLYDLINKSVEARKSRTLAQTV
Enzyme 5 Number of Residues 401
Enzyme 5 Molecular Weight 44593
Enzyme 5 Theoretical pI 9.58
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Not Available
Enzyme 5 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 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 78-98 114-134 147-167 170-190 196-216 223-243 267-287 298-317 324-346 349-369
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID Q9H1N7 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name S35B3_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AB231931 Link Image
Enzyme 5 GeneCard ID Q9H1N7 Link Image
Enzyme 5 GenAtlas ID SLC35B3 Link Image
Enzyme 5 HGNC ID HGNC:21601 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 5 Metabolite References Not Available