CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000435
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein phosphatase 1G 
Protein Synonyms/Alias
 Protein phosphatase 1C; Protein phosphatase 2C isoform gamma; PP2C-gamma; Protein phosphatase magnesium-dependent 1 gamma 
Gene Name
 PPM1G 
Gene Synonyms/Alias
 PPM1C 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
80KYLPDIIKDQKAYKEubiquitination[1, 2]
92YKEGKLQKALEDAFLubiquitination[1, 3, 4]
128PTEDEDEKEKVADEDacetylation[5]
128PTEDEDEKEKVADEDubiquitination[6, 7]
172HKGPPHSKSGGGTGEubiquitination[1, 2, 6, 7, 8]
209QENGPTAKAYTGFSSacetylation[5]
209QENGPTAKAYTGFSSubiquitination[1, 2, 3, 4, 6, 7, 8]
247SCSSASDKLPRVAKSacetylation[2, 5]
247SCSSASDKLPRVAKSubiquitination[1, 2]
339VVALIRGKQLIVANAubiquitination[1, 2, 3, 4, 6, 7, 8, 9]
358CVVSEAGKALDMSYDubiquitination[1, 3, 4, 7, 8]
367LDMSYDHKPEDEVELubiquitination[1, 6]
383RIKNAGGKVTMDGRVacetylation[2, 5, 10, 11]
383RIKNAGGKVTMDGRVubiquitination[1, 6, 7]
406AIGDHFYKRNKNLPPubiquitination[1, 2]
409DHFYKRNKNLPPEEQubiquitination[1, 2, 6, 7, 8, 9]
519ELQPESGKRKLEEVLacetylation[2]
519ELQPESGKRKLEEVLubiquitination[1, 2, 6, 7]
539EENGNSDKKKKAKRDacetylation[5]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [11] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773] 
Functional Description
  
Sequence Annotation
 METAL 60 60 Manganese 1 (By similarity).
 METAL 60 60 Manganese 2 (By similarity).
 METAL 61 61 Manganese 1; via carbonyl oxygen (By
 METAL 441 441 Manganese 2 (By similarity).
 METAL 496 496 Manganese 2 (By similarity).
 MOD_RES 183 183 Phosphoserine.
 MOD_RES 383 383 N6-acetyllysine.
 MOD_RES 527 527 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding; Phosphoprotein; Protein phosphatase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 546 AA 
Protein Sequence
MGAYLSQPNT VKCSGDGVGA PRLPLPYGFS AMQGWRVSME DAHNCIPELD SETAMFSVYD 60
GHGGEEVALY CAKYLPDIIK DQKAYKEGKL QKALEDAFLA IDAKLTTEEV IKELAQIAGR 120
PTEDEDEKEK VADEDDVDNE EAALLHEEAT MTIEELLTRY GQNCHKGPPH SKSGGGTGEE 180
PGSQGLNGEA GPEDSTRETP SQENGPTAKA YTGFSSNSER GTEAGQVGEP GIPTGEAGPS 240
CSSASDKLPR VAKSKFFEDS EDESDEAEEE EEDSEECSEE EDGYSSEEAE NEEDEDDTEE 300
AEEDDEEEEE EMMVPGMEGK EEPGSDSGTT AVVALIRGKQ LIVANAGDSR CVVSEAGKAL 360
DMSYDHKPED EVELARIKNA GGKVTMDGRV NGGLNLSRAI GDHFYKRNKN LPPEEQMISA 420
LPDIKVLTLT DDHEFMVIAC DGIWNVMSSQ EVVDFIQSKI SQRDENGELR LLSSIVEELL 480
DQCLAPDTSG DGTGCDNMTC IIICFKPRNT AELQPESGKR KLEEVLSTEG AEENGNSDKK 540
KKAKRD 546 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
 GO:0007050; P:cell cycle arrest; TAS:ProtInc.
 GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:UniProtKB. 
Interpro
 IPR001932; PP2C-like.
 IPR000222; PP2C_Mn2_Asp60_BS.
 IPR015655; Protein_Pase_2C. 
Pfam
 PF00481; PP2C 
SMART
 SM00331; PP2C_SIG
 SM00332; PP2Cc 
PROSITE
 PS01032; PP2C 
PRINTS