CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000667
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1 
Protein Synonyms/Alias
 PAPS synthase 1; PAPSS 1; Sulfurylase kinase 1; SK 1; SK1; Sulfate adenylyltransferase; ATP-sulfurylase; Sulfate adenylate transferase; SAT; Adenylyl-sulfate kinase; 3'-phosphoadenosine-5'-phosphosulfate synthase; APS kinase; Adenosine-5'-phosphosulfate 3'-phosphotransferase; Adenylylsulfate 3'-phosphotransferase 
Gene Name
 PAPSS1 
Gene Synonyms/Alias
 ATPSK1; PAPSS 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
10IPGSLCKKVKLSNNAubiquitination[1]
12GSLCKKVKLSNNAQNubiquitination[2]
183KARAGEIKGFTGIDSubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
243ELYVPENKLHLAKTDubiquitination[1, 8]
404RLTPTELKQKFKDMNubiquitination[1, 8]
406TPTELKQKFKDMNADubiquitination[1]
619TVLTEYYKSLEKA**ubiquitination[1, 2, 4, 5, 6, 7, 8, 9]
623EYYKSLEKA******ubiquitination[2, 7, 9]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [9] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473
Functional Description
 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. 
Sequence Annotation
 NP_BIND 59 66 ATP (Potential).
 REGION 1 ?220 Adenylyl-sulfate kinase.
 REGION ?221 624 Sulfate adenylyltransferase.
 MOTIF 521 525 PP-motif.
 ACT_SITE 133 133 Phosphoserine intermediate (By  
Keyword
 3D-structure; ATP-binding; Complete proteome; Kinase; Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; Polymorphism; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 624 AA 
Protein Sequence
MEIPGSLCKK VKLSNNAQNW GMQRATNVTY QAHHVSRNKR GQVVGTRGGF RGCTVWLTGL 60
SGAGKTTVSM ALEEYLVCHG IPCYTLDGDN IRQGLNKNLG FSPEDREENV RRIAEVAKLF 120
ADAGLVCITS FISPYTQDRN NARQIHEGAS LPFFEVFVDA PLHVCEQRDV KGLYKKARAG 180
EIKGFTGIDS EYEKPEAPEL VLKTDSCDVN DCVQQVVELL QERDIVPVDA SYEVKELYVP 240
ENKLHLAKTD AETLPALKIN KVDMQWVQVL AEGWATPLNG FMREREYLQC LHFDCLLDGG 300
VINLSVPIVL TATHEDKERL DGCTAFALMY EGRRVAILRN PEFFEHRKEE RCARQWGTTC 360
KNHPYIKMVM EQGDWLIGGD LQVLDRVYWN DGLDQYRLTP TELKQKFKDM NADAVFAFQL 420
RNPVHNGHAL LMQDTHKQLL ERGYRRPVLL LHPLGGWTKD DDVPLMWRMK QHAAVLEEGV 480
LNPETTVVAI FPSPMMYAGP TEVQWHCRAR MVAGANFYIV GRDPAGMPHP ETGKDLYEPS 540
HGAKVLTMAP GLITLEIVPF RVAAYNKKKK RMDYYDSEHH EDFEFISGTR MRKLAREGQK 600
PPEGFMAPKA WTVLTEYYKS LEKA 624 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0004020; F:adenylylsulfate kinase activity; IEA:EC.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004781; F:sulfate adenylyltransferase (ATP) activity; ISS:UniProtKB.
 GO:0050428; P:3'-phosphoadenosine 5'-phosphosulfate biosynthetic process; TAS:Reactome.
 GO:0001501; P:skeletal system development; TAS:ProtInc.
 GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniPathway.
 GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. 
Interpro
 IPR002891; 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. 
Pfam
 PF01583; APS_kinase
 PF01747; ATP-sulfurylase
 PF14306; PUA_2 
SMART
  
PROSITE
  
PRINTS