CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023280
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein phosphatase 6 regulatory subunit 1 
Protein Synonyms/Alias
 SAPS domain family member 1 
Gene Name
 PPP6R1 
Gene Synonyms/Alias
 KIAA1115; PP6R1; SAPS1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
38EDVLQECKVVNRKLLubiquitination[1]
135MGILINRKTDQLVSFubiquitination[1]
190VNWLNEEKIVQRLIEubiquitination[1, 2, 3, 4, 5]
203IEQIHPSKDENQHSNubiquitination[1, 6]
461QCAGGPRKGYMGHLTubiquitination[1, 7, 8]
480ALVQNTEKGPNAEQLubiquitination[1, 3, 4, 6, 7, 8]
492EQLRQLLKELPSEQQubiquitination[1, 3]
515GPLAETNKKNMVDLVubiquitination[1, 3, 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] 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] 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]
 [6] 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]
 [7] 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]
 [8] 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
Functional Description
 Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. Involved in the PP6- mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. 
Sequence Annotation
 REGION 10 403 Interaction with PPP6C.
 MOD_RES 524 524 Phosphothreonine.
 MOD_RES 529 529 Phosphoserine (By similarity).
 MOD_RES 530 530 Phosphoserine (By similarity).
 MOD_RES 531 531 Phosphoserine (By similarity).
 MOD_RES 635 635 Phosphoserine.
 MOD_RES 638 638 Phosphoserine.
 MOD_RES 702 702 Phosphoserine.
 MOD_RES 726 726 Phosphoserine.
 MOD_RES 759 759 Phosphoserine.
 MOD_RES 846 846 Phosphoserine (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 881 AA 
Protein Sequence
MFWKFDLHTS SHLDTLLERE DLSLPELLDE EDVLQECKVV NRKLLDFLLQ PPHLQAMVAW 60
VTQEPPDSGE ERLRYKYPSV ACEILTSDVP QINDALGADE SLLNRLYGFL QSTGSLNPLL 120
ASFFSKVMGI LINRKTDQLV SFLRKKDDFV DLLLQHIGTS AIMDLLLRLL TCVERPQLRQ 180
DVVNWLNEEK IVQRLIEQIH PSKDENQHSN ASQSLCDIIR LSREQMIQVQ DSPEPDQLLA 240
TLEKQETIEQ LLSNMFEGEQ SQSVIVSGIQ VLLTLLEPRR PRSESVTVNS FFSSVDGQLE 300
LLAQGALEST VSSVGALHAL RPRLSCFHQL LLEPPKLEPL QMTWGMLAPP LGNTRLHVVK 360
LLASALSAND AALTHELLAL DVPNTMLDLF FHYVFNNFLH AQVEGCVSTM LSLGPPPDSS 420
PETPIQNPVV KHLLQQCRLV ERILTSWEEN DRVQCAGGPR KGYMGHLTRV AGALVQNTEK 480
GPNAEQLRQL LKELPSEQQE QWEAFVSGPL AETNKKNMVD LVNTHHLHSS SDDEDDRLKE 540
FNFPEEAVLQ QAFMDFQMQR MTSAFIDHFG FNDEEFGEQE ESVNAPFDKT ANITFSLNAD 600
DENPNANLLE ICYKDRIQQF DDDEEEEDEE EAQGSGESDG EDGAWQGSQL ARGARLGQPP 660
GVRSGGSTDS EDEEEEDEEE EEDEEGIGCA ARGGATPLSY PSPGPQPPGP SWTATFDPVP 720
TDAPTSPRVS GEEELHTGPP APQGPLSVPQ GLPTQSLASP PARDALQLRS QDPTPPSAPQ 780
EATEGSKVTE PSAPCQALVS IGDLQATFHG IRSAPSSSDS ATRDPSTSVP ASGAHQPPQT 840
TEGEKSPEPL GLPQSQSAQA LTPPPIPNGS APEGPASPGS Q 881 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0043666; P:regulation of phosphoprotein phosphatase activity; IDA:MGI. 
Interpro
 IPR007587; SAPS. 
Pfam
 PF04499; SAPS 
SMART
  
PROSITE
  
PRINTS