CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008229
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Selenide, water dikinase 1 
Protein Synonyms/Alias
 Selenium donor protein 1; Selenophosphate synthase 1 
Gene Name
 SEPHS1 
Gene Synonyms/Alias
 SELD; SPS; SPS1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
16PESYELDKSFRLTRFubiquitination[1, 2, 3]
27LTRFTELKGTGCKVPacetylation[3]
27LTRFTELKGTGCKVPubiquitination[2]
139MTDRERDKVMPLIIQubiquitination[1, 2, 3, 4, 5]
341ARFCAEIKSPKYGEGacetylation[6]
341ARFCAEIKSPKYGEGubiquitination[2, 3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 Synthesizes selenophosphate from selenide and ATP. 
Sequence Annotation
 NP_BIND 67 69 ATP.
 NP_BIND 162 164 ATP; shared with dimeric partner.
 NP_BIND 267 273 ATP.
 ACT_SITE 31 31 Potential.
 BINDING 32 32 ATP.
 BINDING 87 87 ATP.
 BINDING 110 110 ATP.
 MOD_RES 2 2 N-acetylserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Membrane; Nucleotide-binding; Nucleus; Reference proteome; Selenium; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 392 AA 
Protein Sequence
MSTRESFNPE SYELDKSFRL TRFTELKGTG CKVPQDVLQK LLESLQENHF QEDEQFLGAV 60
MPRLGIGMDT CVIPLRHGGL SLVQTTDYIY PIVDDPYMMG RIACANVLSD LYAMGVTECD 120
NMLMLLGVSN KMTDRERDKV MPLIIQGFKD AAEEAGTSVT GGQTVLNPWI VLGGVATTVC 180
QPNEFIMPDN AVPGDVLVLT KPLGTQVAVA VHQWLDIPEK WNKIKLVVTQ EDVELAYQEA 240
MMNMARLNRT AAGLMHTFNA HAATDITGFG ILGHAQNLAK QQRNEVSFVI HNLPVLAKMA 300
AVSKACGNMF GLMHGTCPET SGGLLICLPR EQAARFCAEI KSPKYGEGHQ AWIIGIVEKG 360
NRTARIIDKP RIIEVAPQVA TQNVNPTPGA TS 392 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0031965; C:nuclear membrane; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0005524; F:ATP binding; TAS:ProtInc.
 GO:0005525; F:GTP binding; TAS:ProtInc.
 GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0004756; F:selenide, water dikinase activity; IEA:EC.
 GO:0006464; P:cellular protein modification process; TAS:ProtInc. 
Interpro
 IPR010918; AIR_synth_C_dom.
 IPR000728; AIR_synth_N_dom.
 IPR016188; PurM_N-like.
 IPR004536; SelD. 
Pfam
 PF00586; AIRS
 PF02769; AIRS_C 
SMART
  
PROSITE
  
PRINTS