CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008580
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein phosphatase 5 
Protein Synonyms/Alias
 PP5; Protein phosphatase T; PP-T; PPT 
Gene Name
 PPP5C 
Gene Synonyms/Alias
 PPP5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
26PPADGALKRAEELKTubiquitination[1]
32LKRAEELKTQANDYFubiquitination[1, 2]
40TQANDYFKAKDYENAacetylation[3]
40TQANDYFKAKDYENAubiquitination[1, 2]
42ANDYFKAKDYENAIKubiquitination[1]
49KDYENAIKFYSQAIEubiquitination[1, 2]
94RAIELDKKYIKGYYRubiquitination[1]
97ELDKKYIKGYYRRAAubiquitination[1]
111ASNMALGKFRAALRDubiquitination[1]
141MKYQECNKIVKQKAFubiquitination[1]
185GPKLEDGKVTISFMKubiquitination[1, 2]
199KELMQWYKDQKKLHRubiquitination[1]
320YGFEGEVKAKYTAQMubiquitination[1, 2]
412QFGPDVTKAFLEENNubiquitination[1, 4]
430IIRSHEVKAEGYEVAubiquitination[1]
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] 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]
 [3] 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]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
 May play a role in the regulation of RNA biogenesis and/or mitosis. In vitro, dephosphorylates serine residues of skeletal muscle phosphorylase and histone H1. 
Sequence Annotation
 REPEAT 28 61 TPR 1.
 REPEAT 62 95 TPR 2.
 REPEAT 96 129 TPR 3.
 REGION 184 499 Catalytic.
 ACT_SITE 304 304 Proton donor (By similarity).
 METAL 242 242 Iron (By similarity).
 METAL 244 244 Iron (By similarity).
 METAL 271 271 Iron (By similarity).
 METAL 271 271 Manganese (By similarity).
 METAL 303 303 Manganese (By similarity).
 METAL 352 352 Manganese (By similarity).
 METAL 427 427 Manganese (By similarity).
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Hydrolase; Iron; Manganese; Metal-binding; Nucleus; Protein phosphatase; Reference proteome; Repeat; TPR repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 499 AA 
Protein Sequence
MAMAEGERTE CAEPPRDEPP ADGALKRAEE LKTQANDYFK AKDYENAIKF YSQAIELNPS 60
NAIYYGNRSL AYLRTECYGY ALGDATRAIE LDKKYIKGYY RRAASNMALG KFRAALRDYE 120
TVVKVKPHDK DAKMKYQECN KIVKQKAFER AIAGDEHKRS VVDSLDIESM TIEDEYSGPK 180
LEDGKVTISF MKELMQWYKD QKKLHRKCAY QILVQVKEVL SKLSTLVETT LKETEKITVC 240
GDTHGQFYDL LNIFELNGLP SETNPYIFNG DFVDRGSFSV EVILTLFGFK LLYPDHFHLL 300
RGNHETDNMN QIYGFEGEVK AKYTAQMYEL FSEVFEWLPL AQCINGKVLI MHGGLFSEDG 360
VTLDDIRKIE RNRQPPDSGP MCDLLWSDPQ PQNGRSISKR GVSCQFGPDV TKAFLEENNL 420
DYIIRSHEVK AEGYEVAHGG RCVTVFSAPN YCDQMGNKAS YIHLQGSDLR PQFHQFTAVP 480
HPNVKPMAYA NTLLQLGMM 499 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0043005; C:neuron projection; IEA:Compara.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0005634; C:nucleus; TAS:ProtInc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004722; F:protein serine/threonine phosphatase activity; TAS:ProtInc.
 GO:0004871; F:signal transducer activity; IMP:UniProtKB.
 GO:0007067; P:mitosis; TAS:ProtInc.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
 GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
 GO:0051291; P:protein heterooligomerization; IEA:Compara.
 GO:0043278; P:response to morphine; IEA:Compara.
 GO:0006351; P:transcription, DNA-dependent; TAS:ProtInc. 
Interpro
 IPR004843; Metallo_PEstase_dom.
 IPR013235; PPP_dom.
 IPR006186; Ser/Thr-sp_prot-phosphatase.
 IPR011236; Ser/Thr_PPase_5.
 IPR001440; TPR-1.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR019734; TPR_repeat. 
Pfam
 PF00149; Metallophos
 PF08321; PPP5
 PF00515; TPR_1 
SMART
 SM00156; PP2Ac
 SM00028; TPR 
PROSITE
 PS00125; SER_THR_PHOSPHATASE
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS
 PR00114; STPHPHTASE.