CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036983
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Sulfate adenylyltransferase 
Protein Synonyms/Alias
  
Gene Name
 PAPSS2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
177RARAGEIKGFTGIDSubiquitination[1, 2, 3, 4]
188GIDSDYEKPETPERVubiquitination[1]
538YEPTHGGKVLSMAPGubiquitination[3]
603PDGFMAPKAWKVLTDubiquitination[3, 5]
606FMAPKAWKVLTDYYRubiquitination[3, 5]
Reference
 [1] 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]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] 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]
 [4] 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]
 [5] 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
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 618 AA 
Protein Sequence
MIVLVTEWVD LSLENQQKST NVVYQAHHVS RNKRGQVVGT RGGFRGCTVW LTGLSGAGKT 60
TISFALEEYL VSHAIPCYSL DGDNVRHGLN RNLGFSPGDR EENIRRIAEV AKLFADAGLV 120
CITSFISPFA KDRENARKIH ESAGLPFFEI FVDAPLNICE SRDVKGLYKR ARAGEIKGFT 180
GIDSDYEKPE TPERVLKTNL STVSDCVHQV VELLQEQNIV PYTIIKDIHE LFVPENKLDH 240
VRAEAETLPS LSITKLDLQW VQVLSEGWAT PLKGFMREKE YLQVMHFDTL LDDGVINMSI 300
PIVLPVSAED KTRLEGCSKF VLAHGGRRVA ILRDAEFYEH RKEERCSRVW GTTCTKHPHI 360
KMVMESGDWL VGGDLQVLEK IRWNDGLDQY RLTPLELKQK CKEMNADAVF AFQLRNPVHN 420
GHALLMQDTR RRLLERGYKH PVLLLHPLGG WTKDDDVPLD WRMKQHAAVL EEGVLDPKST 480
IVAIFPSPML YAGPTEVQWH CRSRMIAGAN FYIVGRDPAG MPHPETKKDL YEPTHGGKVL 540
SMAPGLTSVE IIPFRVAAYN KAKKAMDFYD PARHNEFDFI SGTRMRKLAR EGENPPDGFM 600
APKAWKVLTD YYRSLEKN 618 
Gene Ontology
 GO:0004020; F:adenylylsulfate kinase activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:InterPro.
 GO:0000103; P:sulfate assimilation; IEA:InterPro. 
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