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Q60967 (PAPS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Sulfate adenylyltransferase
    EC=2.7.7.4
    Alternative name(s):
    ATP-sulfurylase
    Sulfate adenylate transferase
    Short name=SAT
  2. Adenylyl-sulfate kinase
    EC=2.7.1.25
    Alternative name(s):
    3'-phosphoadenosine-5'-phosphosulfate synthase
    APS kinase
    Adenosine-5'-phosphosulfate 3'-phosphotransferase
    Adenylylsulfate 3'-phosphotransferase
Gene names
Name:Papss1
Synonyms:Asapk, Atpsk1, Papss
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length624 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. HAMAP-Rule MF_00065

Catalytic activity

ATP + sulfate = diphosphate + adenylyl sulfate. HAMAP-Rule MF_00065

ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate. HAMAP-Rule MF_00065

Pathway

Sulfur metabolism; sulfate assimilation. HAMAP-Rule MF_00065

Tissue specificity

Expressed in the neonatal brain and in cartilage.

Sequence similarities

In the N-terminal section; belongs to the APS kinase family.

In the C-terminal section; belongs to the sulfate adenylyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 624624Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1 HAMAP-Rule MF_00065
PRO_0000105960

Regions

Nucleotide binding59 – 668ATP Potential
Region1 – ?220220Adenylyl-sulfate kinase HAMAP-Rule MF_00065
Region?221 – 624404Sulfate adenylyltransferase HAMAP-Rule MF_00065
Motif521 – 5255PP-motif HAMAP-Rule MF_00065

Sites

Active site1331Phosphoserine intermediate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue121N6-acetyllysine Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q60967 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B487EFAF9B78BE3E

FASTA62470,794
        10         20         30         40         50         60 
MEIPGSLCKK VKLSNNAQNW GMQRATNVTY QAHHVSRNKR GQVVGTRGGF RGCTVWLTGL 

        70         80         90        100        110        120 
SGAGKTTVSM ALEEYLVCHG IPCYTLDGDN IRQGLNKNLG FSPEDREENV RRIAEVAKLF 

       130        140        150        160        170        180 
ADAGLVCITS FISPYTQDRN NARQIHEGAS LPFFEVFVDA PLHVCEQRDV KGLYKKARAG 

       190        200        210        220        230        240 
EIKGFTGIDS EYEKPEAPEL VLKTDSCDVN DCVQQVVELL QERDIVPVDA SYEVKELYVP 

       250        260        270        280        290        300 
ENKLHLAKTD AEALPALKIN KVDMQWVQVL AEGWATPLNG FMREREYLQC LHFDCLLDGG 

       310        320        330        340        350        360 
VINLSVPIVL TATHEDKERL DGCTAFALVY EGRRVAILRN PEFFEHRKEE RCARQWGTTC 

       370        380        390        400        410        420 
KNHPYIKMVL EQGDWLIGGD LQVLDRIYWN DGLDQYRLTP TELKQKFKDM NADAVFAFQL 

       430        440        450        460        470        480 
RNPVHNGHAL LMQDTHKQLL ERGYRRPVLL LHPLGGWTKD DDVPLMWRMK QHAAVLEEGI 

       490        500        510        520        530        540 
LDPETTVVAI FPSPMMYAGP TEVQWHCRAR MVAGANFYIV GRDPAGMPHP ETGKDLYEPT 

       550        560        570        580        590        600 
HGAKVLTMAP GLITLEIVPF RVAAYNKKKK RMDYYDSEHH EDFEFISGTR MRKLAREGQK 

       610        620 
PPEGFMAPKA WTVLVEYYKS LEKA 

« Hide

References

« Hide 'large scale' references
[1]"The isolation and characterization of cDNA encoding the mouse bifunctional ATP sulfurylase-adenosine 5'-phosphosulfate kinase."
Li H., Deyrup A., Mensch J.R. Jr., Domowicz M., Konstantinidis A.K., Schwartz N.B.
J. Biol. Chem. 270:29453-29459(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U34883 mRNA. Translation: AAC52328.1.
RefSeqNP_035993.1. NM_011863.2.
UniGeneMm.244912.

3D structure databases

ProteinModelPortalQ60967.
SMRQ60967. Positions 25-623.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204832. 2 interactions.
IntActQ60967. 3 interactions.
MINTMINT-4106569.

PTM databases

PhosphoSiteQ60967.

Proteomic databases

PaxDbQ60967.
PRIDEQ60967.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029666; ENSMUSP00000029666; ENSMUSG00000028032.
GeneID23971.
KEGGmmu:23971.
UCSCuc008rjr.2. mouse.

Organism-specific databases

CTD9061.
MGIMGI:1330587. Papss1.

Phylogenomic databases

eggNOGCOG0529.
GeneTreeENSGT00390000009613.
HOGENOMHOG000069045.
HOVERGENHBG053503.
InParanoidQ60967.
KOK13811.
OMANLYDATH.
OrthoDBEOG74TWZ4.
PhylomeDBQ60967.
TreeFamTF313143.

Enzyme and pathway databases

UniPathwayUPA00097.

Gene expression databases

ArrayExpressQ60967.
BgeeQ60967.
CleanExMM_PAPSS1.
GenevestigatorQ60967.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00065. Adenylyl_sulf_kinase.
InterProIPR002891. APS_kinase.
IPR025980. ATP-Sase_PUA-like_dom.
IPR027417. P-loop_NTPase.
IPR015947. PUA-like_domain.
IPR014729. Rossmann-like_a/b/a_fold.
IPR024951. Sulfurylase_cat_dom.
IPR002650. Sulphate_adenylyltransferase.
[Graphical view]
PfamPF01583. APS_kinase. 1 hit.
PF01747. ATP-sulfurylase. 1 hit.
PF14306. PUA_2. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsTIGR00455. apsK. 1 hit.
TIGR00339. sopT. 1 hit.
ProtoNetSearch...

Other

NextBio303857.
PROQ60967.
SOURCESearch...

Entry information

Entry namePAPS1_MOUSE
AccessionPrimary (citable) accession number: Q60967
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot