CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022562
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial 
Protein Synonyms/Alias
 PDP 2; Pyruvate dehydrogenase phosphatase catalytic subunit 2; PDPC 2 
Gene Name
 PDP2 
Gene Synonyms/Alias
 KIAA1348 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
94RAGETTHKILDLESRubiquitination[1]
357DVQLKWSKELQRSILubiquitination[1]
438LAEADWHKTDLAQRPubiquitination[2, 3]
459QSLLLQRKASGLHEAubiquitination[1, 4]
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] 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]
 [3] 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]
 [4] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266
Functional Description
 Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex (By similarity). 
Sequence Annotation
 METAL 141 141 Manganese 1 (By similarity).
 METAL 141 141 Manganese 2 (By similarity).
 METAL 142 142 Manganese 1; via carbonyl oxygen (By
 METAL 412 412 Manganese 2 (By similarity).  
Keyword
 Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion; Protein phosphatase; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 529 AA 
Protein Sequence
MSSTVSYWIL NSTRNSIATL QGGRRLYSRY VSNRNKLKWR LFSRVPPTLN SSPCGGFTLC 60
KAYRHTSTEE DDFHLQLSPE QINEVLRAGE TTHKILDLES RVPNSVLRFE SNQLAANSPV 120
EDRRGVASCL QTNGLMFGIF DGHGGHACAQ AVSERLFYYV AVSLMSHQTL EHMEGAMESM 180
KPLLPILHWL KHPGDSIYKD VTSVHLDHLR VYWQELLDLH MEMGLSIEEA LMYSFQRLDS 240
DISLEIQAPL EDEVTRNLSL QVAFSGATAC MAHVDGIHLH VANAGDCRAI LGVQEDNGMW 300
SCLPLTRDHN AWNQAELSRL KREHPESEDR TIIMEDRLLG VLIPCRAFGD VQLKWSKELQ 360
RSILERGFNT EALNIYQFTP PHYYTPPYLT AEPEVTYHRL RPQDKFLVLA SDGLWDMLSN 420
EDVVRLVVGH LAEADWHKTD LAQRPANLGL MQSLLLQRKA SGLHEADQNA ATRLIRHAIG 480
NNEYGEMEAE RLAAMLTLPE DLARMYRDDI TVTVVYFNSE SIGAYYKGG 529 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0004741; F:[pyruvate dehydrogenase (lipoamide)] phosphatase activity; IEA:EC.
 GO:0004724; F:magnesium-dependent protein serine/threonine phosphatase activity; IEA:Compara.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0035970; P:peptidyl-threonine dephosphorylation; IEA:Compara.
 GO:0006090; P:pyruvate metabolic process; TAS:Reactome.
 GO:0010510; P:regulation of acetyl-CoA biosynthetic process from pyruvate; TAS:Reactome. 
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