CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030497
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform 
Protein Synonyms/Alias
 cDNA FLJ33169 fis, clone ADRGL2000384, highly similar to Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform 
Gene Name
 PPP2R1A 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9VRRAAASKLGEFAKVacetylation[1]
9VRRAAASKLGEFAKVubiquitination[1, 2, 3, 4, 5, 6, 7]
15SKLGEFAKVLELDNVubiquitination[1, 2, 3, 6, 7]
23VLELDNVKSEIIPMFubiquitination[3, 4, 7]
76LRQAAEDKSWRVRYMubiquitination[1, 3, 6, 8]
87VRYMVADKFTELQKAubiquitination[1, 2, 3, 4, 5, 6, 7]
93DKFTELQKAVGPEITacetylation[9]
93DKFTELQKAVGPEITubiquitination[1, 2, 3, 7]
101AVGPEITKTDLVPAFacetylation[1, 10]
101AVGPEITKTDLVPAFubiquitination[2, 3, 6, 7]
113PAFQNLMKDCEAEVRubiquitination[1]
126VRAAASHKVKEFCENubiquitination[3]
128AAASHKVKEFCENLSubiquitination[1, 2, 4, 6, 8]
237VELAEDAKWRVRLAIubiquitination[2, 6, 7]
288EAATSNLKKLVEKFGubiquitination[3]
293NLKKLVEKFGKEWAHubiquitination[2]
296KLVEKFGKEWAHATIubiquitination[1, 2, 3, 7]
306AHATIIPKVLAMSGDubiquitination[2]
363NVRFNVAKSLQKIGPubiquitination[1, 2, 3, 4, 5, 6, 7]
367NVAKSLQKIGPILDNubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
382STLQSEVKPILEKLTubiquitination[1, 2, 3, 6, 7]
387EVKPILEKLTQDQDVubiquitination[4, 7]
Reference
 [1] 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]
 [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] 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] 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] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] 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]
 [10] 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
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 410 AA 
Protein Sequence
MVRRAAASKL GEFAKVLELD NVKSEIIPMF SNLASDEQDS VRLLAVEACV NIAQLLPQED 60
LEALVMPTLR QAAEDKSWRV RYMVADKFTE LQKAVGPEIT KTDLVPAFQN LMKDCEAEVR 120
AAASHKVKEF CENLSADCRE NVIMSQILPC IKELVSDANQ HVKSALASVI MGLSPILGKD 180
NTIEHLLPLF LAQLKDECPE VRLNIISNLD CVNEVIGIRQ LSQSLLPAIV ELAEDAKWRV 240
RLAIIEYMPL LAGQLGVEFF DEKLNSLCMA WLVDHVYAIR EAATSNLKKL VEKFGKEWAH 300
ATIIPKVLAM SGDPNYLHRM TTLFCINVLS EVCGQDITTK HMLPTVLRMA GDPVANVRFN 360
VAKSLQKIGP ILDNSTLQSE VKPILEKLTQ DQDVDVKYFA QEALTVLSLA 410 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0000159; C:protein phosphatase type 2A complex; IEA:Compara.
 GO:0004722; F:protein serine/threonine phosphatase activity; IEA:Compara.
 GO:0070262; P:peptidyl-serine dephosphorylation; IEA:Compara.
 GO:0042981; P:regulation of apoptotic process; IEA:Compara. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR000357; HEAT.
 IPR021133; HEAT_type_2. 
Pfam
 PF02985; HEAT 
SMART
  
PROSITE
 PS50077; HEAT_REPEAT 
PRINTS