CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006673
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein phosphatase PP1-gamma catalytic subunit 
Protein Synonyms/Alias
 PP-1G; Protein phosphatase 1C catalytic subunit 
Gene Name
 PPP1CC 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MADLDKLNIDSIIubiquitination[1, 2, 3]
23LLEVRGSKPGKNVQLubiquitination[3]
26VRGSKPGKNVQLQENubiquitination[1, 2, 3, 4]
113LLLAYKIKYPENFFLubiquitination[1, 2]
141YGFYDECKRRYNIKLubiquitination[1, 2]
147CKRRYNIKLWKTFTDubiquitination[1, 2]
150RYNIKLWKTFTDCFNubiquitination[1]
238VVAKFLHKHDLDLICubiquitination[1, 2]
260DGYEFFAKRQLVTLFubiquitination[1, 2]
Reference
 [1] 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]
 [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] 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] 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] 
Functional Description
 Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density- associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. 
Sequence Annotation
 ACT_SITE 125 125 Proton donor.
 METAL 64 64 Iron.
 METAL 66 66 Iron.
 METAL 92 92 Iron.
 METAL 92 92 Manganese.
 METAL 124 124 Manganese.
 METAL 173 173 Manganese.
 METAL 248 248 Manganese.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 307 307 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Carbohydrate metabolism; Cell cycle; Cell division; Centromere; Chromosome; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Glycogen metabolism; Hydrolase; Iron; Kinetochore; Manganese; Metal-binding; Mitochondrion; Nucleus; Phosphoprotein; Polymorphism; Protein phosphatase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 323 AA 
Protein Sequence
MADLDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK 60
ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL 120
LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL 180
QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD 240
LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE 300
KKKPNATRPV TPPRVASGLN PSIQKASNYR NNTVLYE 337 
Gene Ontology
 GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
 GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
 GO:0005741; C:mitochondrial outer membrane; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:UniProtKB.
 GO:0070688; C:MLL5-L complex; IDA:UniProtKB.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0072357; C:PTW/PP1 phosphatase complex; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004722; F:protein serine/threonine phosphatase activity; IMP:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
 GO:0006470; P:protein dephosphorylation; IEA:Compara.
 GO:0046822; P:regulation of nucleocytoplasmic transport; IEA:Compara.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
 GO:0019433; P:triglyceride catabolic process; TAS:Reactome. 
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.