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Protein

Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1

Gene

PAPSS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 (PubMed:9576487, PubMed:9668121, PubMed:9648242, PubMed:14747722). Required for normal biosynthesis of sulfated L-selectin ligands in endothelial cells (PubMed:9576487).4 Publications

Catalytic activityi

ATP + sulfate = diphosphate + adenylyl sulfate.4 Publications
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate.6 Publications

Activity regulationi

Inhibited by chlorate (PubMed:9576487). The kinase activity is subject to inhibition by the substrate adenylyl sulfate (PubMed:17540769).2 Publications

Pathwayi: sulfate assimilation

This protein is involved in the pathway sulfate assimilation, which is part of Sulfur metabolism.4 Publications
View all proteins of this organism that are known to be involved in the pathway sulfate assimilation and in Sulfur metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei101Adenylyl sulfateCombined sources1 Publication1
Binding sitei171Adenylyl sulfateCombined sources1 Publication1
Binding sitei207ATP 1; via carbonyl oxygenCombined sources3 Publications1
Binding sitei212ATP 1Combined sources1 Publication1
Binding sitei563ATP 2; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi62 – 67ATP 1Combined sources3 Publications6
Nucleotide bindingi419 – 422ATP 2Combined sources1 Publication4
Nucleotide bindingi521 – 525ATP 2Combined sources1 Publication5

GO - Molecular functioni

  • adenylylsulfate kinase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • nucleotidyltransferase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • sulfate adenylyltransferase (ATP) activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionKinase, Multifunctional enzyme, Nucleotidyltransferase, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS06566-MONOMER
BRENDAi2.7.1.25 2681
2.7.7.4 2681
ReactomeiR-HSA-174362 Transport and synthesis of PAPS
R-HSA-2408550 Metabolism of ingested H2SeO4 and H2SeO3 into H2Se
R-HSA-6802952 Signaling by BRAF and RAF fusions
SABIO-RKiO43252
UniPathwayi
UPA00097

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
Short name:
PAPS synthase 1
Short name:
PAPSS 1
Alternative name(s):
Sulfurylase kinase 1
Short name:
SK 1
Short name:
SK1
Including the following 2 domains:
Sulfate adenylyltransferase (EC:2.7.7.44 Publications)
Alternative name(s):
ATP-sulfurylase
Sulfate adenylate transferase
Short name:
SAT
Adenylyl-sulfate kinase (EC:2.7.1.256 Publications)
Alternative name(s):
3'-phosphoadenosine-5'-phosphosulfate synthase
APS kinase
Adenosine-5'-phosphosulfate 3'-phosphotransferase
Adenylylsulfate 3'-phosphotransferase
Gene namesi
Name:PAPSS1
Synonyms:ATPSK1, PAPSS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000138801.8
HGNCiHGNC:8603 PAPSS1
MIMi603262 gene
neXtProtiNX_O43252

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi37R → A: Abolishes inhibition by the substrate adenylyl sulfate. 1 Publication1
Mutagenesisi40R → A: Abolishes inhibition by the substrate adenylyl sulfate. 1 Publication1
Mutagenesisi425H → A: Loss of activity. 1 Publication1
Mutagenesisi426N → K: Increased activity. 1 Publication1
Mutagenesisi427 – 428GH → AA: Loss of activity. 2
Mutagenesisi427G → A: 30% decrease in activity. 1 Publication1
Mutagenesisi428H → A: Loss of activity. 1 Publication1

Organism-specific databases

DisGeNETi9061
OpenTargetsiENSG00000138801
PharmGKBiPA384

Chemistry databases

DrugBankiDB03708 Adenosine-5'-Phosphosulfate
DB04077 Glycerol

Polymorphism and mutation databases

BioMutaiPAPSS1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001059591 – 624Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1Add BLAST624

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei12N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO43252
PaxDbiO43252
PeptideAtlasiO43252
PRIDEiO43252
ProteomicsDBi48837

PTM databases

iPTMnetiO43252
PhosphoSitePlusiO43252

Expressioni

Tissue specificityi

Expressed in testis, pancreas, kidney, thymus, prostate, ovary, small intestine, colon, leukocytes and liver. Also expressed in high endothelial venules (HEV) cells and in cartilage.1 Publication

Gene expression databases

BgeeiENSG00000138801 Expressed in 240 organ(s), highest expression level in endometrium
CleanExiHS_PAPSS1
GenevisibleiO43252 HS

Organism-specific databases

HPAiHPA049781

Interactioni

Subunit structurei

Homodimer.3 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi114522, 48 interactors
IntActiO43252, 13 interactors
STRINGi9606.ENSP00000265174

Structurei

Secondary structure

1624
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliO43252
SMRiO43252
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43252

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 225Adenylyl-sulfate kinase3 PublicationsAdd BLAST225
Regioni89 – 92Adenylyl sulfate bindingCombined sources1 Publication4
Regioni106 – 109Adenylyl sulfate bindingCombined sources2 Publications4
Regioni132 – 133Adenylyl sulfate bindingCombined sources2 Publications2
Regioni184 – 185Adenylyl sulfate bindingCombined sources2 Publications2
Regioni234 – 624Sulfate adenylyltransferase1 PublicationAdd BLAST391

Domaini

The N-terminal first 50 residues are required for inhibition by the substrate adenylyl sulfate.1 Publication

Sequence similaritiesi

In the N-terminal section; belongs to the APS kinase family.Curated
In the C-terminal section; belongs to the sulfate adenylyltransferase family.Curated

Phylogenomic databases

eggNOGiKOG0635 Eukaryota
KOG4238 Eukaryota
COG0529 LUCA
COG2046 LUCA
GeneTreeiENSGT00390000009613
HOVERGENiHBG053503
KOiK13811
OMAiCKEHPYI
OrthoDBiEOG091G07ZR
PhylomeDBiO43252
TreeFamiTF313143

Family and domain databases

CDDicd02027 APSK, 1 hit
cd00517 ATPS, 1 hit
Gene3Di3.40.50.620, 1 hit
HAMAPiMF_00065 Adenylyl_sulf_kinase, 1 hit
InterProiView protein in InterPro
IPR002891 APS_kinase
IPR025980 ATP-Sase_PUA-like_dom
IPR027417 P-loop_NTPase
IPR015947 PUA-like_sf
IPR014729 Rossmann-like_a/b/a_fold
IPR024951 Sulfurylase_cat_dom
IPR002650 Sulphate_adenylyltransferase
PfamiView protein in Pfam
PF01747 ATP-sulfurylase, 1 hit
PF14306 PUA_2, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
SSF88697 SSF88697, 1 hit
TIGRFAMsiTIGR00455 apsK, 1 hit
TIGR00339 sopT, 1 hit

Sequencei

Sequence statusi: Complete.

O43252-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEIPGSLCKK VKLSNNAQNW GMQRATNVTY QAHHVSRNKR GQVVGTRGGF
60 70 80 90 100
RGCTVWLTGL SGAGKTTVSM ALEEYLVCHG IPCYTLDGDN IRQGLNKNLG
110 120 130 140 150
FSPEDREENV RRIAEVAKLF ADAGLVCITS FISPYTQDRN NARQIHEGAS
160 170 180 190 200
LPFFEVFVDA PLHVCEQRDV KGLYKKARAG EIKGFTGIDS EYEKPEAPEL
210 220 230 240 250
VLKTDSCDVN DCVQQVVELL QERDIVPVDA SYEVKELYVP ENKLHLAKTD
260 270 280 290 300
AETLPALKIN KVDMQWVQVL AEGWATPLNG FMREREYLQC LHFDCLLDGG
310 320 330 340 350
VINLSVPIVL TATHEDKERL DGCTAFALMY EGRRVAILRN PEFFEHRKEE
360 370 380 390 400
RCARQWGTTC KNHPYIKMVM EQGDWLIGGD LQVLDRVYWN DGLDQYRLTP
410 420 430 440 450
TELKQKFKDM NADAVFAFQL RNPVHNGHAL LMQDTHKQLL ERGYRRPVLL
460 470 480 490 500
LHPLGGWTKD DDVPLMWRMK QHAAVLEEGV LNPETTVVAI FPSPMMYAGP
510 520 530 540 550
TEVQWHCRAR MVAGANFYIV GRDPAGMPHP ETGKDLYEPS HGAKVLTMAP
560 570 580 590 600
GLITLEIVPF RVAAYNKKKK RMDYYDSEHH EDFEFISGTR MRKLAREGQK
610 620
PPEGFMAPKA WTVLTEYYKS LEKA
Length:624
Mass (Da):70,833
Last modified:October 10, 2002 - v2
Checksum:iA3DC9B943E68CDD6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti456G → A in CAA71413 (PubMed:9576487).Curated1
Sequence conflicti456Missing in AAC39894 (PubMed:9668121).Curated1
Sequence conflicti519 – 520IV → MC in AAD09325 (Ref. 4) Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_014065270L → F1 PublicationCorresponds to variant dbSNP:rs1127008Ensembl.1
Natural variantiVAR_014064587S → L3 PublicationsCorresponds to variant dbSNP:rs1127014Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10387 mRNA Translation: CAA71413.1
U53447 Genomic DNA Translation: AAC39894.1
AF033026 mRNA Translation: AAC28429.1
AF016496 mRNA Translation: AAD09325.1
AF105227 mRNA Translation: AAF40236.1
AF097721
, AF097710, AF097711, AF097712, AF097713, AF097714, AF097715, AF097716, AF097717, AF097718, AF097719, AF097720 Genomic DNA Translation: AAF40235.1
AK292774 mRNA Translation: BAF85463.1
CR457028 mRNA Translation: CAG33309.1
CH471057 Genomic DNA Translation: EAX06210.1
BC011392 mRNA Translation: AAH11392.1
BC050627 mRNA Translation: AAH50627.1
CCDSiCCDS3676.1
PIRiJW0087
RefSeqiNP_005434.4, NM_005443.4
XP_011530702.1, XM_011532400.1
XP_011530703.1, XM_011532401.1
UniGeneiHs.368610

Genome annotation databases

EnsembliENST00000265174; ENSP00000265174; ENSG00000138801
GeneIDi9061
KEGGihsa:9061
UCSCiuc003hyk.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10387 mRNA Translation: CAA71413.1
U53447 Genomic DNA Translation: AAC39894.1
AF033026 mRNA Translation: AAC28429.1
AF016496 mRNA Translation: AAD09325.1
AF105227 mRNA Translation: AAF40236.1
AF097721
, AF097710, AF097711, AF097712, AF097713, AF097714, AF097715, AF097716, AF097717, AF097718, AF097719, AF097720 Genomic DNA Translation: AAF40235.1
AK292774 mRNA Translation: BAF85463.1
CR457028 mRNA Translation: CAG33309.1
CH471057 Genomic DNA Translation: EAX06210.1
BC011392 mRNA Translation: AAH11392.1
BC050627 mRNA Translation: AAH50627.1
CCDSiCCDS3676.1
PIRiJW0087
RefSeqiNP_005434.4, NM_005443.4
XP_011530702.1, XM_011532400.1
XP_011530703.1, XM_011532401.1
UniGeneiHs.368610

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X6VX-ray1.75A/B1-624[»]
1XJQX-ray2.06A/B1-624[»]
1XNJX-ray1.98A/B1-624[»]
2OFWX-ray2.05A/B/C/D/E/F/G/H24-225[»]
2OFXX-ray1.90A/B25-227[»]
2PEYX-ray1.88A/B51-226[»]
2PEZX-ray1.40A/B51-226[»]
2QJFX-ray2.20A/B220-624[»]
ProteinModelPortaliO43252
SMRiO43252
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114522, 48 interactors
IntActiO43252, 13 interactors
STRINGi9606.ENSP00000265174

Chemistry databases

DrugBankiDB03708 Adenosine-5'-Phosphosulfate
DB04077 Glycerol

PTM databases

iPTMnetiO43252
PhosphoSitePlusiO43252

Polymorphism and mutation databases

BioMutaiPAPSS1

Proteomic databases

EPDiO43252
PaxDbiO43252
PeptideAtlasiO43252
PRIDEiO43252
ProteomicsDBi48837

Protocols and materials databases

DNASUi9061
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265174; ENSP00000265174; ENSG00000138801
GeneIDi9061
KEGGihsa:9061
UCSCiuc003hyk.4 human

Organism-specific databases

CTDi9061
DisGeNETi9061
EuPathDBiHostDB:ENSG00000138801.8
GeneCardsiPAPSS1
HGNCiHGNC:8603 PAPSS1
HPAiHPA049781
MIMi603262 gene
neXtProtiNX_O43252
OpenTargetsiENSG00000138801
PharmGKBiPA384
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0635 Eukaryota
KOG4238 Eukaryota
COG0529 LUCA
COG2046 LUCA
GeneTreeiENSGT00390000009613
HOVERGENiHBG053503
KOiK13811
OMAiCKEHPYI
OrthoDBiEOG091G07ZR
PhylomeDBiO43252
TreeFamiTF313143

Enzyme and pathway databases

UniPathwayi
UPA00097

BioCyciMetaCyc:HS06566-MONOMER
BRENDAi2.7.1.25 2681
2.7.7.4 2681
ReactomeiR-HSA-174362 Transport and synthesis of PAPS
R-HSA-2408550 Metabolism of ingested H2SeO4 and H2SeO3 into H2Se
R-HSA-6802952 Signaling by BRAF and RAF fusions
SABIO-RKiO43252

Miscellaneous databases

ChiTaRSiPAPSS1 human
EvolutionaryTraceiO43252
GeneWikiiPAPSS1
GenomeRNAii9061
PROiPR:O43252
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000138801 Expressed in 240 organ(s), highest expression level in endometrium
CleanExiHS_PAPSS1
GenevisibleiO43252 HS

Family and domain databases

CDDicd02027 APSK, 1 hit
cd00517 ATPS, 1 hit
Gene3Di3.40.50.620, 1 hit
HAMAPiMF_00065 Adenylyl_sulf_kinase, 1 hit
InterProiView protein in InterPro
IPR002891 APS_kinase
IPR025980 ATP-Sase_PUA-like_dom
IPR027417 P-loop_NTPase
IPR015947 PUA-like_sf
IPR014729 Rossmann-like_a/b/a_fold
IPR024951 Sulfurylase_cat_dom
IPR002650 Sulphate_adenylyltransferase
PfamiView protein in Pfam
PF01747 ATP-sulfurylase, 1 hit
PF14306 PUA_2, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
SSF88697 SSF88697, 1 hit
TIGRFAMsiTIGR00455 apsK, 1 hit
TIGR00339 sopT, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPAPS1_HUMAN
AccessioniPrimary (citable) accession number: O43252
Secondary accession number(s): O43841
, O75332, Q6IAX6, Q96FB1, Q96TF4, Q9P1P9, Q9UE98
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: October 10, 2002
Last modified: September 12, 2018
This is version 188 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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