MSH6_HUMAN - dbPTM
MSH6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MSH6_HUMAN
UniProt AC P52701
Protein Name DNA mismatch repair protein Msh6 {ECO:0000250|UniProtKB:P54276}
Gene Name MSH6 {ECO:0000312|HGNC:HGNC:7329}
Organism Homo sapiens (Human).
Sequence Length 1360
Subcellular Localization Nucleus . Chromosome . Associates with H3K36me3 via its PWWP domain.
Protein Description Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction..
Protein Sequence MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGASPSPGGDAAWSEAGPGPRPLARSASPPKAKNLNGGLRRSVAPAAPTSCDFSPGDLVWAKMEGYPWWPCLVYNHPFDGTFIREKGKSVRVHVQFFDDSPTRGWVSKRLLKPYTGSKSKEAQKGGHFYSAKPEILRAMQRADEALNKDKIKRLELAVCDEPSEPEEEEEMEVGTTYVTDKSEEDNEIESEEEVQPKTQGSRRSSRQIKKRRVISDSESDIGGSDVEFKPDTKEEGSSDEISSGVGDSESEGLNSPVKVARKRKRMVTGNGSLKRKSSRKETPSATKQATSISSETKNTLRAFSAPQNSESQAHVSGGGDDSSRPTVWYHETLEWLKEEKRRDEHRRRPDHPDFDASTLYVPEDFLNSCTPGMRKWWQIKSQNFDLVICYKVGKFYELYHMDALIGVSELGLVFMKGNWAHSGFPEIAFGRYSDSLVQKGYKVARVEQTETPEMMEARCRKMAHISKYDRVVRREICRIITKGTQTYSVLEGDPSENYSKYLLSLKEKEEDSSGHTRAYGVCFVDTSLGKFFIGQFSDDRHCSRFRTLVAHYPPVQVLFEKGNLSKETKTILKSSLSCSLQEGLIPGSQFWDASKTLRTLLEEEYFREKLSDGIGVMLPQVLKGMTSESDSIGLTPGEKSELALSALGGCVFYLKKCLIDQELLSMANFEEYIPLDSDTVSTTRSGAIFTKAYQRMVLDAVTLNNLEIFLNGTNGSTEGTLLERVDTCHTPFGKRLLKQWLCAPLCNHYAINDRLDAIEDLMVVPDKISEVVELLKKLPDLERLLSKIHNVGSPLKSQNHPDSRAIMYEETTYSKKKIIDFLSALEGFKVMCKIIGIMEEVADGFKSKILKQVISLQTKNPEGRFPDLTVELNRWDTAFDHEKARKTGLITPKAGFDSDYDQALADIRENEQSLLEYLEKQRNRIGCRTIVYWGIGRNRYQLEIPENFTTRNLPEEYELKSTKKGCKRYWTKTIEKKLANLINAEERRDVSLKDCMRRLFYNFDKNYKDWQSAVECIAVLDVLLCLANYSRGGDGPMCRPVILLPEDTPPFLELKGSRHPCITKTFFGDDFIPNDILIGCEEEEQENGKAYCVLVTGPNMGGKSTLMRQAGLLAVMAQMGCYVPAEVCRLTPIDRVFTRLGASDRIMSGESTFFVELSETASILMHATAHSLVLVDELGRGTATFDGTAIANAVVKELAETIKCRTLFSTHYHSLVEDYSQNVAVRLGHMACMVENECEDPSQETITFLYKFIKGACPKSYGFNAARLANLPEEVIQKGHRKAREFEKMNQSLRLFREVCLASERSTVDAEAVHKLLTLIKEL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSRQSTLYS
------CCCCCHHHH		50.7824173317
5Phosphorylation---MSRQSTLYSFFP
---CCCCCHHHHCCC		21.1928152594
6Phosphorylation--MSRQSTLYSFFPK
--CCCCCHHHHCCCC		22.7523403867
8PhosphorylationMSRQSTLYSFFPKSP
CCCCCHHHHCCCCCC		11.9725159151
9PhosphorylationSRQSTLYSFFPKSPA
CCCCHHHHCCCCCCC		24.4322617229
14PhosphorylationLYSFFPKSPALSDAN
HHHCCCCCCCCCHHH		18.6829255136
18PhosphorylationFPKSPALSDANKASA
CCCCCCCCHHHHHHH		36.4630183078
22AcetylationPALSDANKASARASR
CCCCHHHHHHHHHHH		45.5026051181
22UbiquitinationPALSDANKASARASR
CCCCHHHHHHHHHHH		45.50-
33MethylationRASREGGRAAAAPGA
HHHHHCCCCCCCCCC		31.73115483869
41PhosphorylationAAAAPGASPSPGGDA
CCCCCCCCCCCCCCC		31.6523927012
43PhosphorylationAAPGASPSPGGDAAW
CCCCCCCCCCCCCCH		33.4119664994
51PhosphorylationPGGDAAWSEAGPGPR
CCCCCCHHCCCCCCC		16.9123927012
63PhosphorylationGPRPLARSASPPKAK
CCCCCCCCCCCCCHH		27.7327174698
65PhosphorylationRPLARSASPPKAKNL
CCCCCCCCCCCHHCC		42.8728176443
70AcetylationSASPPKAKNLNGGLR
CCCCCCHHCCCCCCC		69.0019608861
79PhosphorylationLNGGLRRSVAPAAPT
CCCCCCCCCCCCCCC		19.0525159151
86PhosphorylationSVAPAAPTSCDFSPG
CCCCCCCCCCCCCCC		36.9425159151
87PhosphorylationVAPAAPTSCDFSPGD
CCCCCCCCCCCCCCC		15.6125159151
88GlutathionylationAPAAPTSCDFSPGDL
CCCCCCCCCCCCCCE		7.2422555962
91PhosphorylationAPTSCDFSPGDLVWA
CCCCCCCCCCCEEEE		18.0925159151
137PhosphorylationHVQFFDDSPTRGWVS
EEEECCCCCCCCCCH		29.9829255136
139PhosphorylationQFFDDSPTRGWVSKR
EECCCCCCCCCCHHH		45.8529255136
140MethylationFFDDSPTRGWVSKRL
ECCCCCCCCCCHHHH		40.12115483889
144PhosphorylationSPTRGWVSKRLLKPY
CCCCCCCHHHHCCCC		12.9222617229
149AcetylationWVSKRLLKPYTGSKS
CCHHHHCCCCCCCCC		40.3426051181
151PhosphorylationSKRLLKPYTGSKSKE
HHHHCCCCCCCCCHH		23.34-
152PhosphorylationKRLLKPYTGSKSKEA
HHHCCCCCCCCCHHH		43.4328555341
155AcetylationLKPYTGSKSKEAQKG
CCCCCCCCCHHHHCC		67.8826051181
161UbiquitinationSKSKEAQKGGHFYSA
CCCHHHHCCCCCCCC		74.12-
169SumoylationGGHFYSAKPEILRAM
CCCCCCCCHHHHHHH		36.92-
169AcetylationGGHFYSAKPEILRAM
CCCCCCCCHHHHHHH		36.9226822725
169SumoylationGGHFYSAKPEILRAM
CCCCCCCCHHHHHHH		36.92-
169UbiquitinationGGHFYSAKPEILRAM
CCCCCCCCHHHHHHH		36.92-
194UbiquitinationKIKRLELAVCDEPSE
HCHHEEEEECCCCCC		7.19-
200PhosphorylationLAVCDEPSEPEEEEE
EEECCCCCCCHHHHH		64.8330266825
202AcetylationVCDEPSEPEEEEEME
ECCCCCCCHHHHHCC		59.6519608861
204UbiquitinationDEPSEPEEEEEMEVG
CCCCCCHHHHHCCCC		79.86-
212PhosphorylationEEEMEVGTTYVTDKS
HHHCCCCCEEECCCC		21.8230266825
213PhosphorylationEEMEVGTTYVTDKSE
HHCCCCCEEECCCCH		15.2930266825
214PhosphorylationEMEVGTTYVTDKSEE
HCCCCCEEECCCCHH		10.9430266825
216PhosphorylationEVGTTYVTDKSEEDN
CCCCEEECCCCHHCC		27.5630266825
219PhosphorylationTTYVTDKSEEDNEIE
CEEECCCCHHCCCCC		49.3722167270
227PhosphorylationEEDNEIESEEEVQPK
HHCCCCCCCHHCCCC		56.8419664994
235PhosphorylationEEEVQPKTQGSRRSS
CHHCCCCCCCCCCCH		44.86-
252PhosphorylationIKKRRVISDSESDIG
HHHCEECCCCCCCCC		32.0229255136
254PhosphorylationKRRVISDSESDIGGS
HCEECCCCCCCCCCC		32.0129255136
256PhosphorylationRVISDSESDIGGSDV
EECCCCCCCCCCCCC		38.1829255136
261PhosphorylationSESDIGGSDVEFKPD
CCCCCCCCCCEECCC		33.0229255136
269PhosphorylationDVEFKPDTKEEGSSD
CCEECCCCCCCCCCC		49.2129255136
274PhosphorylationPDTKEEGSSDEISSG
CCCCCCCCCCCCCCC		37.5825159151
275PhosphorylationDTKEEGSSDEISSGV
CCCCCCCCCCCCCCC		50.5525159151
279PhosphorylationEGSSDEISSGVGDSE
CCCCCCCCCCCCCCC		20.9925159151
280PhosphorylationGSSDEISSGVGDSES
CCCCCCCCCCCCCCC		43.0625159151
285PhosphorylationISSGVGDSESEGLNS
CCCCCCCCCCCCCCC		36.7725159151
287PhosphorylationSGVGDSESEGLNSPV
CCCCCCCCCCCCCHH		40.7020873877
292PhosphorylationSESEGLNSPVKVARK
CCCCCCCCHHHHHHH		35.7925137130
305PhosphorylationRKRKRMVTGNGSLKR
HHCCCCCCCCCCCCC		18.6523927012
309PhosphorylationRMVTGNGSLKRKSSR
CCCCCCCCCCCCCCC		34.4223401153
315PhosphorylationGSLKRKSSRKETPSA
CCCCCCCCCCCCCCC		50.8624719451
324UbiquitinationKETPSATKQATSISS
CCCCCCHHHHHCCCH		37.3421906983
324 (in isoform 1)Ubiquitination-37.3421890473
324 (in isoform 2)Ubiquitination-37.3421890473
327PhosphorylationPSATKQATSISSETK
CCCHHHHHCCCHHHH		24.8921406692
328PhosphorylationSATKQATSISSETKN
CCHHHHHCCCHHHHH		24.4025159151
330PhosphorylationTKQATSISSETKNTL
HHHHHCCCHHHHHHH		23.1425159151
331PhosphorylationKQATSISSETKNTLR
HHHHCCCHHHHHHHH		47.8421815630
333PhosphorylationATSISSETKNTLRAF
HHCCCHHHHHHHHHC		31.3821406692
334SumoylationTSISSETKNTLRAFS
HCCCHHHHHHHHHCC		43.83-
334SumoylationTSISSETKNTLRAFS
HCCCHHHHHHHHHCC		43.83-
334UbiquitinationTSISSETKNTLRAFS
HCCCHHHHHHHHHCC		43.8321906983
334 (in isoform 1)Ubiquitination-43.8321890473
334 (in isoform 2)Ubiquitination-43.8321890473
336PhosphorylationISSETKNTLRAFSAP
CCHHHHHHHHHCCCC		21.1230576142
341PhosphorylationKNTLRAFSAPQNSES
HHHHHHCCCCCCCCC		37.7526714015
346UbiquitinationAFSAPQNSESQAHVS
HCCCCCCCCCCCCCC		33.12-
346PhosphorylationAFSAPQNSESQAHVS
HCCCCCCCCCCCCCC		33.1226714015
348PhosphorylationSAPQNSESQAHVSGG
CCCCCCCCCCCCCCC		32.2717525332
353PhosphorylationSESQAHVSGGGDDSS
CCCCCCCCCCCCCCC		23.1226714015
359PhosphorylationVSGGGDDSSRPTVWY
CCCCCCCCCCCCCCH		32.7426714015
360PhosphorylationSGGGDDSSRPTVWYH
CCCCCCCCCCCCCHH		49.6430576142
363PhosphorylationGDDSSRPTVWYHETL
CCCCCCCCCCHHHHH		23.6626714015
366PhosphorylationSSRPTVWYHETLEWL
CCCCCCCHHHHHHHH		5.8526714015
374AcetylationHETLEWLKEEKRRDE
HHHHHHHHHHHHHHH		65.97-
374UbiquitinationHETLEWLKEEKRRDE
HHHHHHHHHHHHHHH		65.97-
374AcetylationHETLEWLKEEKRRDE
HHHHHHHHHHHHHHH		65.9719608861
374UbiquitinationHETLEWLKEEKRRDE
HHHHHHHHHHHHHHH		65.97-
389UbiquitinationHRRRPDHPDFDASTL
HHCCCCCCCCCHHHC		51.88-
407UbiquitinationEDFLNSCTPGMRKWW
HHHHHHCCCCHHHHH		23.77-
413UbiquitinationCTPGMRKWWQIKSQN
CCCCHHHHHEECCCC		5.05-
468UbiquitinationFPEIAFGRYSDSLVQ
CCHHHCCCCHHHHHH		22.71-
470PhosphorylationEIAFGRYSDSLVQKG
HHHCCCCHHHHHHCC		21.2522210691
476UbiquitinationYSDSLVQKGYKVARV
CHHHHHHCCCEEEEE		57.6421906983
476 (in isoform 1)Ubiquitination-57.6421890473
476 (in isoform 2)Ubiquitination-57.6421890473
479UbiquitinationSLVQKGYKVARVEQT
HHHHCCCEEEEEECC		37.78-
480UbiquitinationLVQKGYKVARVEQTE
HHHCCCEEEEEECCC		2.87-
486PhosphorylationKVARVEQTETPEMME
EEEEEECCCCHHHHH		28.4623186163
488PhosphorylationARVEQTETPEMMEAR
EEEECCCCHHHHHHH		28.1221815630
498UbiquitinationMMEARCRKMAHISKY
HHHHHHHHHHHHHHH		44.03-
502UbiquitinationRCRKMAHISKYDRVV
HHHHHHHHHHHHHHH		2.49-
503O-linked_GlycosylationCRKMAHISKYDRVVR
HHHHHHHHHHHHHHH		18.4623301498
504AcetylationRKMAHISKYDRVVRR
HHHHHHHHHHHHHHH		51.0419608861
504UbiquitinationRKMAHISKYDRVVRR
HHHHHHHHHHHHHHH		51.0419608861
516UbiquitinationVRREICRIITKGTQT
HHHHHHHHHCCCCCE		3.98-
519UbiquitinationEICRIITKGTQTYSV
HHHHHHCCCCCEEEE		49.9422053931
519 (in isoform 1)Ubiquitination-49.9421890473
519 (in isoform 2)Ubiquitination-49.9421890473
530UbiquitinationTYSVLEGDPSENYSK
EEEEEECCCCCCHHH		33.89-
537UbiquitinationDPSENYSKYLLSLKE
CCCCCHHHHHHCHHH		29.5621906983
537 (in isoform 1)Ubiquitination-29.5621890473
537 (in isoform 2)Ubiquitination-29.5621890473
538PhosphorylationPSENYSKYLLSLKEK
CCCCHHHHHHCHHHC		13.6129083192
541PhosphorylationNYSKYLLSLKEKEED
CHHHHHHCHHHCCCC		34.5024719451
543UbiquitinationSKYLLSLKEKEEDSS
HHHHHCHHHCCCCCC		64.46-
545UbiquitinationYLLSLKEKEEDSSGH
HHHCHHHCCCCCCCC		65.89-
549PhosphorylationLKEKEEDSSGHTRAY
HHHCCCCCCCCCCEE		41.3129083192
550PhosphorylationKEKEEDSSGHTRAYG
HHCCCCCCCCCCEEE		47.0929083192
562UbiquitinationAYGVCFVDTSLGKFF
EEEEEEEECCCCCEE		15.43-
563UbiquitinationYGVCFVDTSLGKFFI
EEEEEEECCCCCEEE		22.13-
577MethylationIGQFSDDRHCSRFRT
EEECCCCCCHHHHHH		37.39115483873
598UbiquitinationPVQVLFEKGNLSKET
CEEEEEECCCCCHHH		45.85-
598UbiquitinationPVQVLFEKGNLSKET
CEEEEEECCCCCHHH		45.8521906983
598 (in isoform 1)Ubiquitination-45.8521890473
598 (in isoform 2)Ubiquitination-45.8521890473
603UbiquitinationFEKGNLSKETKTILK
EECCCCCHHHHHHHH		72.99-
610UbiquitinationKETKTILKSSLSCSL
HHHHHHHHHHHHCCC		33.86-
614PhosphorylationTILKSSLSCSLQEGL
HHHHHHHHCCCCCCC		12.0128387310
615GlutathionylationILKSSLSCSLQEGLI
HHHHHHHCCCCCCCC		5.9622555962
625PhosphorylationQEGLIPGSQFWDASK
CCCCCCCHHHHCHHH		19.4928387310
632UbiquitinationSQFWDASKTLRTLLE
HHHHCHHHHHHHHHH		53.9821906983
632 (in isoform 1)Ubiquitination-53.9821890473
632 (in isoform 2)Ubiquitination-53.9821890473
641UbiquitinationLRTLLEEEYFREKLS
HHHHHHHHHHHHHHC		40.37-
642PhosphorylationRTLLEEEYFREKLSD
HHHHHHHHHHHHHCC		15.94-
646UbiquitinationEEEYFREKLSDGIGV
HHHHHHHHHCCCHHC		49.3821906983
646 (in isoform 1)Ubiquitination-49.3821890473
646 (in isoform 2)Ubiquitination-49.3821890473
660UbiquitinationVMLPQVLKGMTSESD
CCHHHHHCCCCCCCC		48.0221906983
660 (in isoform 1)Ubiquitination-48.0221890473
660 (in isoform 2)Ubiquitination-48.0221890473
662SulfoxidationLPQVLKGMTSESDSI
HHHHHCCCCCCCCCC		3.4028183972
663PhosphorylationPQVLKGMTSESDSIG
HHHHCCCCCCCCCCC		37.7020068231
664PhosphorylationQVLKGMTSESDSIGL
HHHCCCCCCCCCCCC		26.6420068231
666PhosphorylationLKGMTSESDSIGLTP
HCCCCCCCCCCCCCC		36.1020068231
668PhosphorylationGMTSESDSIGLTPGE
CCCCCCCCCCCCCCC		28.0321815630
672PhosphorylationESDSIGLTPGEKSEL
CCCCCCCCCCCCHHH		24.8420068231
683UbiquitinationKSELALSALGGCVFY
CHHHHHHHHHHHHHH		15.86-
684UbiquitinationSELALSALGGCVFYL
HHHHHHHHHHHHHHH		5.64-
693UbiquitinationGCVFYLKKCLIDQEL
HHHHHHHHHHHCHHH		31.51-
694UbiquitinationCVFYLKKCLIDQELL
HHHHHHHHHHCHHHH		3.73-
702PhosphorylationLIDQELLSMANFEEY
HHCHHHHHCCCHHHH		28.59-
703UbiquitinationIDQELLSMANFEEYI
HCHHHHHCCCHHHHC		3.40-
709PhosphorylationSMANFEEYIPLDSDT
HCCCHHHHCCCCCCC		10.71-
722AcetylationDTVSTTRSGAIFTKA
CCCCCCCCCCHHHHH		30.40-
722UbiquitinationDTVSTTRSGAIFTKA
CCCCCCCCCCHHHHH		30.40-
723UbiquitinationTVSTTRSGAIFTKAY
CCCCCCCCCHHHHHH		21.28-
724UbiquitinationVSTTRSGAIFTKAYQ
CCCCCCCCHHHHHHH		8.58-
728UbiquitinationRSGAIFTKAYQRMVL
CCCCHHHHHHHHHHC		34.0621890473
728UbiquitinationRSGAIFTKAYQRMVL
CCCCHHHHHHHHHHC		34.0621890473
728 (in isoform 1)Ubiquitination-34.0621890473
728 (in isoform 2)Ubiquitination-34.0621890473
736UbiquitinationAYQRMVLDAVTLNNL
HHHHHHCCEEEECCE		27.81-
740UbiquitinationMVLDAVTLNNLEIFL
HHCCEEEECCEEEEE		3.00-
753UbiquitinationFLNGTNGSTEGTLLE
EECCCCCCCCCCHHH		25.92-
755UbiquitinationNGTNGSTEGTLLERV
CCCCCCCCCCHHHCC		52.45-
758UbiquitinationNGSTEGTLLERVDTC
CCCCCCCHHHCCCCC		7.41-
766UbiquitinationLERVDTCHTPFGKRL
HHCCCCCCCHHHHHH		38.37-
767PhosphorylationERVDTCHTPFGKRLL
HCCCCCCCHHHHHHH		23.5925159151
7712-HydroxyisobutyrylationTCHTPFGKRLLKQWL
CCCCHHHHHHHHHHH		40.01-
771AcetylationTCHTPFGKRLLKQWL
CCCCHHHHHHHHHHH		40.0126051181
771UbiquitinationTCHTPFGKRLLKQWL
CCCCHHHHHHHHHHH		40.01-
790UbiquitinationCNHYAINDRLDAIED
CCHHHHHHHCHHHHH		46.54-
793UbiquitinationYAINDRLDAIEDLMV
HHHHHHCHHHHHCCC		46.52-
800UbiquitinationDAIEDLMVVPDKISE
HHHHHCCCCCHHHHH		8.00-
813UbiquitinationSEVVELLKKLPDLER
HHHHHHHHCCCCHHH		65.9621906983
813 (in isoform 1)Ubiquitination-65.9621890473
813 (in isoform 2)Ubiquitination-65.9621890473
814UbiquitinationEVVELLKKLPDLERL
HHHHHHHCCCCHHHH		66.28-
824UbiquitinationDLERLLSKIHNVGSP
CHHHHHHHHHHCCCC		48.2121890473
824UbiquitinationDLERLLSKIHNVGSP
CHHHHHHHHHHCCCC		48.2121890473
824 (in isoform 1)Ubiquitination-48.2121890473
824 (in isoform 2)Ubiquitination-48.2121890473
827UbiquitinationRLLSKIHNVGSPLKS
HHHHHHHHCCCCCCC		43.23-
830PhosphorylationSKIHNVGSPLKSQNH
HHHHHCCCCCCCCCC		23.8329255136
833MethylationHNVGSPLKSQNHPDS
HHCCCCCCCCCCCCC		54.0724775603
833UbiquitinationHNVGSPLKSQNHPDS
HHCCCCCCCCCCCCC		54.0721906983
833 (in isoform 1)Ubiquitination-54.0721890473
833 (in isoform 2)Ubiquitination-54.0721890473
834PhosphorylationNVGSPLKSQNHPDSR
HCCCCCCCCCCCCCC		43.8523927012
840PhosphorylationKSQNHPDSRAIMYEE
CCCCCCCCCCCCCEE		28.2323927012
849PhosphorylationAIMYEETTYSKKKII
CCCCEECCCCHHHHH		29.1323403867
8522-HydroxyisobutyrylationYEETTYSKKKIIDFL
CEECCCCHHHHHHHH		47.90-
852AcetylationYEETTYSKKKIIDFL
CEECCCCHHHHHHHH		47.9023236377
852UbiquitinationYEETTYSKKKIIDFL
CEECCCCHHHHHHHH		47.9021906983
852 (in isoform 1)Ubiquitination-47.9021890473
852 (in isoform 2)Ubiquitination-47.9021890473
853UbiquitinationEETTYSKKKIIDFLS
EECCCCHHHHHHHHH		43.17-
8542-HydroxyisobutyrylationETTYSKKKIIDFLSA
ECCCCHHHHHHHHHH		48.94-
854UbiquitinationETTYSKKKIIDFLSA
ECCCCHHHHHHHHHH		48.94-
860PhosphorylationKKIIDFLSALEGFKV
HHHHHHHHHHHHHHH		30.7020068231
866UbiquitinationLSALEGFKVMCKIIG
HHHHHHHHHHHHHHH		39.66-
867UbiquitinationSALEGFKVMCKIIGI
HHHHHHHHHHHHHHH		5.20-
870UbiquitinationEGFKVMCKIIGIMEE
HHHHHHHHHHHHHHH		21.18-
879UbiquitinationIGIMEEVADGFKSKI
HHHHHHHHHHHHHHH		17.94-
8832-HydroxyisobutyrylationEEVADGFKSKILKQV
HHHHHHHHHHHHHHH		57.26-
883UbiquitinationEEVADGFKSKILKQV
HHHHHHHHHHHHHHH		57.2621906983
883 (in isoform 1)Ubiquitination-57.2621890473
883 (in isoform 2)Ubiquitination-57.2621890473
884UbiquitinationEVADGFKSKILKQVI
HHHHHHHHHHHHHHH		23.75-
885UbiquitinationVADGFKSKILKQVIS
HHHHHHHHHHHHHHH		53.28-
888UbiquitinationGFKSKILKQVISLQT
HHHHHHHHHHHHCCC		46.09-
892PhosphorylationKILKQVISLQTKNPE
HHHHHHHHCCCCCCC		18.6321406692
895PhosphorylationKQVISLQTKNPEGRF
HHHHHCCCCCCCCCC		37.7720068231
896UbiquitinationQVISLQTKNPEGRFP
HHHHCCCCCCCCCCC		58.5021906983
896 (in isoform 1)Ubiquitination-58.5021890473
896 (in isoform 2)Ubiquitination-58.5021890473
900AcetylationLQTKNPEGRFPDLTV
CCCCCCCCCCCCCEE		37.47-
900UbiquitinationLQTKNPEGRFPDLTV
CCCCCCCCCCCCCEE		37.47-
914PhosphorylationVELNRWDTAFDHEKA
EEECCCCCCCCHHHH		23.43-
920UbiquitinationDTAFDHEKARKTGLI
CCCCCHHHHHHHCCC		50.50-
923UbiquitinationFDHEKARKTGLITPK
CCHHHHHHHCCCCCC		52.37-
924PhosphorylationDHEKARKTGLITPKA
CHHHHHHHCCCCCCC		31.5020068231
928PhosphorylationARKTGLITPKAGFDS
HHHHCCCCCCCCCCC		24.6321815630
930UbiquitinationKTGLITPKAGFDSDY
HHCCCCCCCCCCCCH		53.1121906983
930 (in isoform 1)Ubiquitination-53.1121890473
930 (in isoform 2)Ubiquitination-53.1121890473
935PhosphorylationTPKAGFDSDYDQALA
CCCCCCCCCHHHHHH		35.4919664994
937PhosphorylationKAGFDSDYDQALADI
CCCCCCCHHHHHHHH		17.5730266825
957UbiquitinationSLLEYLEKQRNRIGC
HHHHHHHHHHHCCCC		52.54-
962UbiquitinationLEKQRNRIGCRTIVY
HHHHHHCCCCEEEEE		7.54-
971UbiquitinationCRTIVYWGIGRNRYQ
CEEEEEEECCCCCEE		8.52-
996MethylationNLPEEYELKSTKKGC
CCCHHHCCCCCCCCH		5.34-
997SumoylationLPEEYELKSTKKGCK
CCHHHCCCCCCCCHH		44.11-
997UbiquitinationLPEEYELKSTKKGCK
CCHHHCCCCCCCCHH		44.11-
1008PhosphorylationKGCKRYWTKTIEKKL
CCHHHHHHHHHHHHH		14.9129083192
1009AcetylationGCKRYWTKTIEKKLA
CHHHHHHHHHHHHHH		33.1027452117
1009UbiquitinationGCKRYWTKTIEKKLA
CHHHHHHHHHHHHHH		33.10-
1010UbiquitinationCKRYWTKTIEKKLAN
HHHHHHHHHHHHHHH		27.30-
1010PhosphorylationCKRYWTKTIEKKLAN
HHHHHHHHHHHHHHH		27.3021120944
10142-HydroxyisobutyrylationWTKTIEKKLANLINA
HHHHHHHHHHHHCCH		39.79-
1014UbiquitinationWTKTIEKKLANLINA
HHHHHHHHHHHHCCH		39.79-
10302-HydroxyisobutyrylationERRDVSLKDCMRRLF
HHCCCCHHHHHHHHH		41.18-
1030AcetylationERRDVSLKDCMRRLF
HHCCCCHHHHHHHHH		41.1826822725
1030UbiquitinationERRDVSLKDCMRRLF
HHCCCCHHHHHHHHH		41.18-
1075GlutathionylationRGGDGPMCRPVILLP
CCCCCCCCCCEEECC		5.1122555962
1085PhosphorylationVILLPEDTPPFLELK
EEECCCCCCCCEECC		31.0627732954
1092MethylationTPPFLELKGSRHPCI
CCCCEECCCCCCCCE		45.5282981225
1092UbiquitinationTPPFLELKGSRHPCI
CCCCEECCCCCCCCE		45.52-
1101UbiquitinationSRHPCITKTFFGDDF
CCCCCEEEECCCCCC		24.35-
1103UbiquitinationHPCITKTFFGDDFIP
CCCEEEECCCCCCCC		7.40-
1110UbiquitinationFFGDDFIPNDILIGC
CCCCCCCCCCEEEEC		32.22-
1126MethylationEEEQENGKAYCVLVT
HHHHHCCCEEEEEEE		48.0023583077
1140UbiquitinationTGPNMGGKSTLMRQA
ECCCCCCHHHHHHHH		34.24-
1161UbiquitinationAQMGCYVPAEVCRLT
HHCCCCCCHHHHCCC		9.02-
1166UbiquitinationYVPAEVCRLTPIDRV
CCCHHHHCCCCCCHH		46.93-
1172MethylationCRLTPIDRVFTRLGA
HCCCCCCHHHHHCCC		26.60115483881
1185UbiquitinationGASDRIMSGESTFFV
CCCCCCCCCCCEEEE		36.7221890473
1189UbiquitinationRIMSGESTFFVELSE
CCCCCCCEEEEEHHH		19.45-
1195UbiquitinationSTFFVELSETASILM
CEEEEEHHHHHHHHH		21.28-
1222UbiquitinationLGRGTATFDGTAIAN
CCCCEEEECHHHHHH		8.27-
1228UbiquitinationTFDGTAIANAVVKEL
EECHHHHHHHHHHHH		8.75-
1233UbiquitinationAIANAVVKELAETIK
HHHHHHHHHHHHHHC		40.17-
1240UbiquitinationKELAETIKCRTLFST
HHHHHHHCCHHHHCC		25.69-
1291UbiquitinationTFLYKFIKGACPKSY
HHHHHHHHCCCCHHH		43.52-
1296AcetylationFIKGACPKSYGFNAA
HHHCCCCHHHCCCHH		57.0826051181
1296UbiquitinationFIKGACPKSYGFNAA
HHHCCCCHHHCCCHH		57.08-
1315UbiquitinationLPEEVIQKGHRKARE
CCHHHHHHHHHHHHH		45.6321890473
13152-HydroxyisobutyrylationLPEEVIQKGHRKARE
CCHHHHHHHHHHHHH		45.63-
1315UbiquitinationLPEEVIQKGHRKARE
CCHHHHHHHHHHHHH		45.6321890473
1315 (in isoform 1)Ubiquitination-45.6321890473
1319UbiquitinationVIQKGHRKAREFEKM
HHHHHHHHHHHHHHH		46.23-
1325UbiquitinationRKAREFEKMNQSLRL
HHHHHHHHHHHHHHH		48.77-
1340PhosphorylationFREVCLASERSTVDA
HHHHHHHCCCCCCCH		22.1624719451
1352UbiquitinationVDAEAVHKLLTLIKE
CCHHHHHHHHHHHHH		38.3021890473
1352UbiquitinationVDAEAVHKLLTLIKE
CCHHHHHHHHHHHHH		38.3021890473
1352 (in isoform 1)Ubiquitination-38.3021890473
1358UbiquitinationHKLLTLIKEL-----
HHHHHHHHHC-----		56.95-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of MSH6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MSH6_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MSH6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BLM_HUMANBLMphysical
10783165
ATM_HUMANATMphysical
10783165
MLH1_HUMANMLH1physical
10783165
RFC1_HUMANRFC1physical
10783165
SMC1A_HUMANSMC1Aphysical
14657349
PCNA_HUMANPCNAphysical
11274057
PCNA_HUMANPCNAphysical
11005803
MSH2_HUMANMSH2physical
10029069
ATR_HUMANATRphysical
20029092
TOPB1_HUMANTOPBP1physical
20029092
CLSPN_HUMANCLSPNphysical
20029092
CHK1_HUMANCHEK1physical
20029092
CAF1A_HUMANCHAF1Aphysical
22232658
PCNA_HUMANPCNAphysical
22232658
MSH2_HUMANMSH2physical
10748159
MLH1_HUMANMLH1physical
10748159
PMS2_HUMANPMS2physical
10748159
PMS1_HUMANPMS1physical
10748159
BLM_HUMANBLMphysical
15064730
MSH2_HUMANMSH2physical
15064730
XRCC6_HUMANXRCC6physical
21075794
XRCC5_HUMANXRCC5physical
21075794
PRKDC_HUMANPRKDCphysical
21075794
MLH1_HUMANMLH1physical
12799449
PMS2_HUMANPMS2physical
12799449
PCNA_HUMANPCNAphysical
22939629
SP16H_HUMANSUPT16Hphysical
22939629
PCNA_HUMANPCNAphysical
15225546
SAMH1_HUMANSAMHD1physical
22863883
SPT5H_HUMANSUPT5Hphysical
22863883
ANR17_HUMANANKRD17physical
26344197
FEN1_HUMANFEN1physical
26344197
HDGF_HUMANHDGFphysical
26344197
PCNA_HUMANPCNAphysical
26344197
RAD21_HUMANRAD21physical
26344197
DECR_HUMANDECR1physical
26496610
H33_HUMANH3F3Aphysical
26496610
MSH2_HUMANMSH2physical
26496610
PCNA_HUMANPCNAphysical
26496610
STX3_HUMANSTX3physical
26496610
ARK72_HUMANAKR7A2physical
26496610
RUSC2_HUMANRUSC2physical
26496610
PARP2_HUMANPARP2physical
26496610
P33MX_HUMANKIAA1191physical
26496610
CHD8_HUMANCHD8physical
26496610
BRNP1_HUMANBRINP1physical
26496610
MCM9_HUMANMCM9physical
26300262
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614350Hereditary non-polyposis colorectal cancer 5 (HNPCC5)
608089Endometrial cancer (ENDMC)
276300Mismatch repair cancer syndrome (MMRCS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MSH6_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-504, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-79; SER-91;SER-137; SER-200; SER-219; SER-227; SER-252; SER-254; SER-256 ANDSER-261, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-252; SER-254;SER-256; SER-261; SER-309 AND SER-830, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-41; SER-43;SER-252 AND SER-256, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-219; SER-227;SER-252; SER-254; SER-256; SER-261 AND THR-924, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-252; SER-254;SER-256; SER-261 AND SER-830, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, AND MASSSPECTROMETRY.

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