CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030729
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA mismatch repair protein Msh6 
Protein Synonyms/Alias
 cDNA FLJ55677, highly similar to DNA mismatch repair protein MSH6 
Gene Name
 MSH6 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
194KETPSATKQATSISSubiquitination[1, 2]
204TSISSETKNTLRAFSubiquitination[1, 2, 3, 4]
346YSDSLVQKGYKVARVubiquitination[1, 2, 5]
374RKMAHISKYDRVVRRacetylation[6]
374RKMAHISKYDRVVRRubiquitination[2]
389EICRIITKGTQTYSVubiquitination[1, 2, 3, 4, 5, 7]
407DPSENYSKYLLSLKEubiquitination[1, 2, 3, 5]
413SKYLLSLKEKEEDSSubiquitination[2, 3]
468PVQVLFEKGNLSKETubiquitination[1, 2]
480KETKTILKSSLSCSLubiquitination[2, 3]
502SQFWDASKTLRTLLEubiquitination[1, 2, 3, 4]
516EEEYFREKLSDGIGVubiquitination[1, 2, 3]
530VMLPQVLKGMTSESDubiquitination[1, 3]
562GGCVFYLKKCLIDQEubiquitination[3]
563GCVFYLKKCLIDQELubiquitination[2]
598RSGAIFTKAYQRMVLubiquitination[2, 3, 4, 5, 8, 9]
641TCHTPFGKRLLKQWLubiquitination[2]
683SEVVELLKKLPDLERubiquitination[1]
684EVVELLKKLPDLERLubiquitination[2]
694DLERLLSKIHNVGSPubiquitination[2, 3, 8]
703HNVGSPLKSQNHPDSubiquitination[1, 2, 3, 4]
722YEETTYSKKKIIDFLacetylation[6]
722YEETTYSKKKIIDFLubiquitination[1, 3]
723EETTYSKKKIIDFLSubiquitination[2]
724ETTYSKKKIIDFLSAubiquitination[2]
736LSALEGFKVMCKIIGubiquitination[2]
740EGFKVMCKIIGIMEEubiquitination[2]
753EEVADGFKSKILKQVubiquitination[1, 2]
755VADGFKSKILKQVISubiquitination[2]
758GFKSKILKQVISLQTubiquitination[2]
766QVISLQTKNPEGRFPubiquitination[1, 2, 3]
790DTAFDHEKARKTGLIubiquitination[2, 4]
793FDHEKARKTGLITPKubiquitination[2, 4]
800KTGLITPKAGFDSDYubiquitination[1]
827SLLEYLEKQRNRIGCubiquitination[2]
867LPEEYELKSTKKGCKubiquitination[2, 4]
879GCKRYWTKTIEKKLAubiquitination[2]
884WTKTIEKKLANLINAubiquitination[2]
900ERRDVSLKDCMRRLFacetylation[6]
900ERRDVSLKDCMRRLFubiquitination[2, 3]
962TPPFLELKGSRHPCIubiquitination[2, 3, 4]
971SRHPCITKTFFGDDFubiquitination[3]
996EEEQENGKAYCVLVTmethylation[10]
1010TGPNMGGKSTLMRQAubiquitination[2, 4]
1103AIANAVVKELAETIKubiquitination[2]
1110KELAETIKCRTLFSTubiquitination[2, 4, 9]
1161TFLYKFIKGACPKSYubiquitination[2, 4]
1166FIKGACPKSYGFNAAubiquitination[2, 4, 9]
1185LPEEVIQKGHRKAREubiquitination[1, 2, 3, 4, 8]
1189VIQKGHRKAREFEKMubiquitination[2]
1195RKAREFEKMNQSLRLubiquitination[2]
1222VDAEAVHKLLTLIKEubiquitination[2, 3, 4, 8]
1228HKLLTLIKEL*****ubiquitination[2, 4]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] A general molecular affinity strategy for global detection and proteomic analysis of lysine methylation.
 Moore KE, Carlson SM, Camp ND, Cheung P, James RG, Chua KF, Wolf-Yadlin A, Gozani O.
 Mol Cell. 2013 May 9;50(3):444-56. [PMID: 23583077] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; DNA-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1230 AA 
Protein Sequence
MSRQSTLYSF FPKSPALSDA NKASARASRE GGRAAAAPGA SPSPGGDAAW SEAGPGPRPL 60
ARSASPPKAK NLNGGLRRSV GTTYVTDKSE EDNEIESEEE VQPKTQGSRR SSRQIKKRRV 120
ISDSESDIGG SDVEFKPDTK EEGSSDEISS GVGDSESEGL NSPVKVARKR KRMVTGNGSL 180
KRKSSRKETP SATKQATSIS SETKNTLRAF SAPQNSESQA HVSGGGDDSS RPTVWYHETL 240
EWLKEEKRRD EHRRRPDHPD FDASTLYVPE DFLNSCTPGM RKWWQIKSQN FDLVICYKVG 300
KFYELYHMDA LIGVSELGLV FMKGNWAHSG FPEIAFGRYS DSLVQKGYKV ARVEQTETPE 360
MMEARCRKMA HISKYDRVVR REICRIITKG TQTYSVLEGD PSENYSKYLL SLKEKEEDSS 420
GHTRAYGVCF VDTSLGKFFI GQFSDDRHCS RFRTLVAHYP PVQVLFEKGN LSKETKTILK 480
SSLSCSLQEG LIPGSQFWDA SKTLRTLLEE EYFREKLSDG IGVMLPQVLK GMTSESDSIG 540
LTPGEKSELA LSALGGCVFY LKKCLIDQEL LSMANFEEYI PLDSDTVSTT RSGAIFTKAY 600
QRMVLDAVTL NNLEIFLNGT NGSTEGTLLE RVDTCHTPFG KRLLKQWLCA PLCNHYAIND 660
RLDAIEDLMV VPDKISEVVE LLKKLPDLER LLSKIHNVGS PLKSQNHPDS RAIMYEETTY 720
SKKKIIDFLS ALEGFKVMCK IIGIMEEVAD GFKSKILKQV ISLQTKNPEG RFPDLTVELN 780
RWDTAFDHEK ARKTGLITPK AGFDSDYDQA LADIRENEQS LLEYLEKQRN RIGCRTIVYW 840
GIGRNRYQLE IPENFTTRNL PEEYELKSTK KGCKRYWTKT IEKKLANLIN AEERRDVSLK 900
DCMRRLFYNF DKNYKDWQSA VECIAVLDVL LCLANYSRGG DGPMCRPVIL LPEDTPPFLE 960
LKGSRHPCIT KTFFGDDFIP NDILIGCEEE EQENGKAYCV LVTGPNMGGK STLMRQAGLL 1020
AVMAQMGCYV PAEVCRLTPI DRVFTRLGAS DRIMSGESTF FVELSETASI LMHATAHSLV 1080
LVDELGRGTA TFDGTAIANA VVKELAETIK CRTLFSTHYH SLVEDYSQNV AVRLGHMACM 1140
VENECEDPSQ ETITFLYKFI KGACPKSYGF NAARLANLPE EVIQKGHRKA REFEKMNQSL 1200
RLFREVCLAS ERSTVDAEAV HKLLTLIKEL 1230 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0030983; F:mismatched DNA binding; IEA:InterPro.
 GO:0006298; P:mismatch repair; IEA:InterPro. 
Interpro
 IPR017261; DNA_mismatch_repair_Msh6.
 IPR015536; DNA_mismatch_repair_MSH6_C.
 IPR007695; DNA_mismatch_repair_MutS-lik_N.
 IPR000432; DNA_mismatch_repair_MutS_C.
 IPR007861; DNA_mismatch_repair_MutS_clamp.
 IPR007696; DNA_mismatch_repair_MutS_core.
 IPR016151; DNA_mismatch_repair_MutS_N.
 IPR007860; DNA_mmatch_repair_MutS_con_dom.
 IPR027417; P-loop_NTPase. 
Pfam
 PF01624; MutS_I
 PF05188; MutS_II
 PF05192; MutS_III
 PF05190; MutS_IV
 PF00488; MutS_V 
SMART
 SM00534; MUTSac
 SM00533; MUTSd 
PROSITE
 PS00486; DNA_MISMATCH_REPAIR_2 
PRINTS