CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013931
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein phosphatase 1 regulatory subunit 15B 
Protein Synonyms/Alias
  
Gene Name
 PPP1R15B 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
35RSQAGSSKFPTPLGPubiquitination[1, 2]
572PYNPLNFKAPFQTSGubiquitination[2]
583QTSGENEKGCRDSKTubiquitination[2, 3, 4]
705RLQGTCFKGLNVLKQubiquitination[3]
711FKGLNVLKQC*****ubiquitination[3]
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] 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]
 [4] 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] 
Functional Description
 Maintains low levels of EIF2S1 phosphorylation in unstressed cells by promoting its dephosphorylation by PP1 (By similarity). 
Sequence Annotation
  
Keyword
 Complete proteome; Polymorphism; Reference proteome; Translation regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 713 AA 
Protein Sequence
MEPGTGGSRK RLGPRAGFRF WPPFFPRRSQ AGSSKFPTPL GPENSGNPTL LSSAQPETRV 60
SYWTKLLSQL LAPLPGLLQK VLIWSQLFGG MFPTRWLDFA GVYSALRALK GREKPAAPTA 120
QKSLSSLQLD SSDPSVTSPL DWLEEGIHWQ YSPPDLKLEL KAKGSALDPA AQAFLLEQQL 180
WGVELLPSSL QSRLYSNREL GSSPSGPLNI QRIDNFSVVS YLLNPSYLDC FPRLEVSYQN 240
SDGNSEVVGF QTLTPESSCL REDHCHPQPL SAELIPASWQ GCPPLSTEGL PEIHHLRMKR 300
LEFLQQANKG QDLPTPDQDN GYHSLEEEHS LLRMDPKHCR DNPTQFVPAA GDIPGNTQES 360
TEEKIELLTT EVPLALEEES PSEGCPSSEI PMEKEPGEGR ISVVDYSYLE GDLPISARPA 420
CSNKLIDYIL GGASSDLETS SDPEGEDWDE EAEDDGFDSD SSLSDSDLEQ DPEGLHLWNS 480
FCSVDPYNPQ NFTATIQTAA RIVPEEPSDS EKDLSGKSDL ENSSQSGSLP ETPEHSSGEE 540
DDWESSADEA ESLKLWNSFC NSDDPYNPLN FKAPFQTSGE NEKGCRDSKT PSESIVAISE 600
CHTLLSCKVQ LLGSQESECP DSVQRDVLSG GRHTHVKRKK VTFLEEVTEY YISGDEDRKG 660
PWEEFARDGC RFQKRIQETE DAIGYCLTFE HRERMFNRLQ GTCFKGLNVL KQC 713 
Gene Ontology
 GO:0000164; C:protein phosphatase type 1 complex; IEA:Compara.
 GO:0004722; F:protein serine/threonine phosphatase activity; IEA:Compara.
 GO:0006983; P:ER overload response; IEA:Compara.
 GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
 GO:0042542; P:response to hydrogen peroxide; IEA:Compara. 
Interpro
 IPR019523; Prot_Pase1_reg-su15A/B_C.
 IPR019512; Prot_Pase1_reg-su15B_N. 
Pfam
 PF10472; CReP_N
 PF10488; PP1c_bdg 
SMART
  
PROSITE
  
PRINTS