CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005846
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
 Medium tumor antigen-associated 61 kDa protein; PP2A subunit A isoform PR65-alpha; PP2A subunit A isoform R1-alpha 
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
34LRLNSIKKLSTIALAubiquitination[1, 2]
107EETVVRDKAVESLRAubiquitination[2, 3, 4]
133AHFVPLVKRLAGGDWubiquitination[1, 2, 3, 4]
163PRVSSAVKAELRQYFubiquitination[1, 2, 3, 4, 5, 6]
188VRRAAASKLGEFAKVubiquitination[1, 2, 3, 4]
194SKLGEFAKVLELDNVubiquitination[1, 2, 3, 4, 5]
202VLELDNVKSEIIPMFubiquitination[3, 4]
255LRQAAEDKSWRVRYMubiquitination[2, 3]
266VRYMVADKFTELQKAubiquitination[1, 2, 3, 4, 5, 6]
272DKFTELQKAVGPEITubiquitination[1, 3, 4]
280AVGPEITKTDLVPAFacetylation[7]
280AVGPEITKTDLVPAFubiquitination[1, 2, 3, 4]
305VRAAASHKVKEFCENubiquitination[3]
307AAASHKVKEFCENLSubiquitination[1, 2]
374PLFLAQLKDECPEVRubiquitination[8]
416VELAEDAKWRVRLAIubiquitination[1, 2, 4]
467EAATSNLKKLVEKFGubiquitination[3]
472NLKKLVEKFGKEWAHubiquitination[1]
475KLVEKFGKEWAHATIubiquitination[1, 3, 4]
485AHATIIPKVLAMSGDubiquitination[1]
542NVRFNVAKSLQKIGPubiquitination[1, 2, 3, 4]
546NVAKSLQKIGPILDNubiquitination[1, 2, 3, 4, 5, 6, 8]
561STLQSEVKPILEKLTacetylation[9]
561STLQSEVKPILEKLTubiquitination[1, 2, 3, 4]
566EVKPILEKLTQDQDVubiquitination[4]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [9] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Required for proper chromosome segregation and for centromeric localization of SGOL1 in mitosis. 
Sequence Annotation
 REPEAT 8 46 HEAT 1.
 REPEAT 47 84 HEAT 2.
 REPEAT 85 123 HEAT 3.
 REPEAT 124 161 HEAT 4.
 REPEAT 162 200 HEAT 5.
 REPEAT 201 239 HEAT 6.
 REPEAT 240 278 HEAT 7.
 REPEAT 279 321 HEAT 8.
 REPEAT 322 360 HEAT 9.
 REPEAT 361 399 HEAT 10.
 REPEAT 400 438 HEAT 11.
 REPEAT 439 477 HEAT 12.
 REPEAT 478 516 HEAT 13.
 REPEAT 517 555 HEAT 14.
 REPEAT 556 589 HEAT 15.
 REGION 8 399 PP2A subunit B binding.
 REGION 47 321 Polyoma small and medium T antigens
 REGION 85 239 SV40 small T antigen binding.
 REGION 400 589 PP2A subunit C binding.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 280 280 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Centromere; Chromosome; Chromosome partition; Complete proteome; Cytoplasm; Direct protein sequencing; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 589 AA 
Protein Sequence
MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE LLPFLTDTIY 60
DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE ETVVRDKAVE SLRAISHEHS 120
PSDLEAHFVP LVKRLAGGDW FTSRTSACGL FSVCYPRVSS AVKAELRQYF RNLCSDDTPM 180
VRRAAASKLG EFAKVLELDN VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL 240
EALVMPTLRQ AAEDKSWRVR YMVADKFTEL QKAVGPEITK TDLVPAFQNL MKDCEAEVRA 300
AASHKVKEFC ENLSADCREN VIMSQILPCI KELVSDANQH VKSALASVIM GLSPILGKDN 360
TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL SQSLLPAIVE LAEDAKWRVR 420
LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW LVDHVYAIRE AATSNLKKLV EKFGKEWAHA 480
TIIPKVLAMS GDPNYLHRMT TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV 540
AKSLQKIGPI LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA 589 
Gene Ontology
 GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:UniProtKB.
 GO:0016020; C:membrane; NAS:UniProtKB.
 GO:0015630; C:microtubule cytoskeleton; NAS:UniProtKB.
 GO:0005739; C:mitochondrion; NAS:UniProtKB.
 GO:0005634; C:nucleus; NAS:UniProtKB.
 GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
 GO:0003823; F:antigen binding; IPI:UniProtKB.
 GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:UniProtKB.
 GO:0004722; F:protein serine/threonine phosphatase activity; IEA:Compara.
 GO:0006672; P:ceramide metabolic process; NAS:UniProtKB.
 GO:0007059; P:chromosome segregation; IDA:UniProtKB.
 GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0000188; P:inactivation of MAPK activity; NAS:UniProtKB.
 GO:0006917; P:induction of apoptosis; TAS:UniProtKB.
 GO:0007084; P:mitotic nuclear envelope reassembly; TAS:Reactome.
 GO:0030308; P:negative regulation of cell growth; NAS:UniProtKB.
 GO:0042518; P:negative regulation of tyrosine phosphorylation of Stat3 protein; NAS:UniProtKB.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
 GO:0070262; P:peptidyl-serine dephosphorylation; IEA:Compara.
 GO:0006461; P:protein complex assembly; TAS:UniProtKB.
 GO:0006470; P:protein dephosphorylation; TAS:UniProtKB.
 GO:0030155; P:regulation of cell adhesion; NAS:UniProtKB.
 GO:0045595; P:regulation of cell differentiation; NAS:UniProtKB.
 GO:0006275; P:regulation of DNA replication; NAS:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; NAS:UniProtKB.
 GO:0030111; P:regulation of Wnt receptor signaling pathway; NAS:UniProtKB.
 GO:0008380; P:RNA splicing; NAS:UniProtKB.
 GO:0019932; P:second-messenger-mediated signaling; NAS:UniProtKB. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR000357; HEAT.
 IPR021133; HEAT_type_2. 
Pfam
 PF02985; HEAT 
SMART
  
PROSITE
 PS50077; HEAT_REPEAT 
PRINTS