CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037072
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Serine/threonine-protein phosphatase 
Protein Synonyms/Alias
  
Gene Name
 PPP1CB 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
112YGFYDECKRRFNIKLacetylation[1, 2]
112YGFYDECKRRFNIKLubiquitination[3, 4, 5, 6]
118CKRRFNIKLWKTFTDacetylation[2]
118CKRRFNIKLWKTFTDubiquitination[2, 3, 5, 6, 7]
121RFNIKLWKTFTDCFNubiquitination[4, 5, 6]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] 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]
 [3] 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]
 [4] 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]
 [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] 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]
 [7] 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; Hydrolase; Iron; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 169 AA 
Protein Sequence
MTEAEVRGLC IKSREIFLSQ PILLELEAPL KICGDIHGQY TDLLRLFEYG GFPPEANYLF 60
LGDYVDRGKQ SLETICLLLA YKIKYPENFF LLRGNHECAS INRIYGFYDE CKRRFNIKLW 120
KTFTDCFNCL PIAAIVDEKI FCCHGGLSPD LQSMEQIRRI MRPTDVPDT 169 
Gene Ontology
 GO:0042587; C:glycogen granule; IEA:Compara.
 GO:0000164; C:protein phosphatase type 1 complex; IEA:Compara.
 GO:0004722; F:protein serine/threonine phosphatase activity; IEA:Compara.
 GO:0006470; P:protein dephosphorylation; IEA:Compara.
 GO:0005979; P:regulation of glycogen biosynthetic process; IEA:Compara.
 GO:0005981; P:regulation of glycogen catabolic process; IEA:Compara. 
Interpro
 IPR004843; Metallo_PEstase_dom.
 IPR006186; Ser/Thr-sp_prot-phosphatase. 
Pfam
 PF00149; Metallophos 
SMART
 SM00156; PP2Ac 
PROSITE
 PS00125; SER_THR_PHOSPHATASE 
PRINTS
 PR00114; STPHPHTASE.