MSH6_YEAST - dbPTM
MSH6_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MSH6_YEAST
UniProt AC Q03834
Protein Name DNA mismatch repair protein MSH6
Gene Name MSH6
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1242
Subcellular Localization Nucleus .
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. MSH6 provides substrate-binding and substrate specificity to the complex. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs. Acts mainly to repair base-base and single insertion-deletion mismatches that occur during replication, but can also repair longer insertion-deletion loops (IDLs), although with decreasing efficiency as the size of the extrahelical loop increases. 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 by the MutS alpha complex is crucial for MMR. Both subunits bind ATP, but with differing affinities, and their ATPase kinetics are also very different. MSH6 binds and hydrolyzes ATP rapidly, whereas MSH2 catalyzes ATP at a substantially slower rate. Binding to a mismatched base pair suppresses MSH6-catalyzed ATP hydrolysis, but not the activity of MSH2. ATP binding to both subunits is necessary to trigger a change in MutS alpha interaction with mismatched DNA, converting MutS alpha into a sliding clamp capable of hydrolysis-independent movement along DNA, and also facilitates formation of ternary complexes containing MutS and MutL proteins and the mismatch. May also be involved in resolution of recombination intermediates..
Protein Sequence MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKITKNPQGGKTGKLFVDVDEDNDLTIAEETVSTVRSDIMHSQEPQSDTMLNSNTTEPKSTTTDEDLSSSQSRRNHKRRVNYAESDDDDSDTTFTAKRKKGKVVDSESDEDEYLPDKNDGDEDDDIADDKEDIKGELAEDSGDDDDLISLAETTSKKKFSYNTSHSSSPFTRNISRDNSKKKSRPNQAPSRSYNPSHSQPSATSKSSKFNKQNEERYQWLVDERDAQRRPKSDPEYDPRTLYIPSSAWNKFTPFEKQYWEIKSKMWDCIVFFKKGKFFELYEKDALLANALFDLKIAGGGRANMQLAGIPEMSFEYWAAQFIQMGYKVAKVDQRESMLAKEMREGSKGIVKRELQCILTSGTLTDGDMLHSDLATFCLAIREEPGNFYNETQLDSSTIVQKLNTKIFGAAFIDTATGELQMLEFEDDSECTKLDTLMSQVRPMEVVMERNNLSTLANKIVKFNSAPNAIFNEVKAGEEFYDCDKTYAEIISSEYFSTEEDWPEVLKSYYDTGKKVGFSAFGGLLYYLKWLKLDKNLISMKNIKEYDFVKSQHSMVLDGITLQNLEIFSNSFDGSDKGTLFKLFNRAITPMGKRMMKKWLMHPLLRKNDIESRLDSVDSLLQDITLREQLEITFSKLPDLERMLARIHSRTIKVKDFEKVITAFETIIELQDSLKNNDLKGDVSKYISSFPEGLVEAVKSWTNAFERQKAINENIIVPQRGFDIEFDKSMDRIQELEDELMEILMTYRKQFKCSNIQYKDSGKEIYTIEIPISATKNVPSNWVQMAANKTYKRYYSDEVRALARSMAEAKEIHKTLEEDLKNRLCQKFDAHYNTIWMPTIQAISNIDCLLAITRTSEYLGAPSCRPTIVDEVDSKTNTQLNGFLKFKSLRHPCFNLGATTAKDFIPNDIELGKEQPRLGLLTGANAAGKSTILRMACIAVIMAQMGCYVPCESAVLTPIDRIMTRLGANDNIMQGKSTFFVELAETKKILDMATNRSLLVVDELGRGGSSSDGFAIAESVLHHVATHIQSLGFFATHYGTLASSFKHHPQVRPLKMSILVDEATRNVTFLYKMLEGQSEGSFGMHVASMCGISKEIIDNAQIAADNLEHTSRLVKERDLAANNLNGEVVSVPGGLQSDFVRIAYGDGLKNTKLGSGEGVLNYDWNIKRNVLKSLFSIIDDLQS
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
10AcetylationPATPKTSKTAHFENG
CCCCCCCCCCCCCCC		55.7725381059
11PhosphorylationATPKTSKTAHFENGS
CCCCCCCCCCCCCCC		25.7319823750
18PhosphorylationTAHFENGSTSSQKKM
CCCCCCCCCCHHHHH		36.3823749301
19PhosphorylationAHFENGSTSSQKKMK
CCCCCCCCCHHHHHH		33.5223749301
20PhosphorylationHFENGSTSSQKKMKQ
CCCCCCCCHHHHHHH		32.2517287358
21PhosphorylationFENGSTSSQKKMKQS
CCCCCCCHHHHHHHH		46.2217287358
23AcetylationNGSTSSQKKMKQSSL
CCCCCHHHHHHHHHH		57.7025381059
28PhosphorylationSQKKMKQSSLLSFFS
HHHHHHHHHHHHHHH		19.8930377154
29PhosphorylationQKKMKQSSLLSFFSK
HHHHHHHHHHHHHHC		30.7321440633
32PhosphorylationMKQSSLLSFFSKQVP
HHHHHHHHHHHCCCC		29.5530377154
36AcetylationSLLSFFSKQVPSGTP
HHHHHHHCCCCCCCC		50.5924489116
40PhosphorylationFFSKQVPSGTPSKKV
HHHCCCCCCCCCCCC		57.3428889911
42PhosphorylationSKQVPSGTPSKKVQK
HCCCCCCCCCCCCCC		28.8223749301
44PhosphorylationQVPSGTPSKKVQKPT
CCCCCCCCCCCCCCC		44.9728889911
97PhosphorylationETVSTVRSDIMHSQE
HHHHHHHHHHHCCCC		27.4422369663
102PhosphorylationVRSDIMHSQEPQSDT
HHHHHHCCCCCCCCC		20.8922369663
107PhosphorylationMHSQEPQSDTMLNSN
HCCCCCCCCCCCCCC		45.8522369663
109PhosphorylationSQEPQSDTMLNSNTT
CCCCCCCCCCCCCCC		28.8922369663
113PhosphorylationQSDTMLNSNTTEPKS
CCCCCCCCCCCCCCC		31.4322369663
115PhosphorylationDTMLNSNTTEPKSTT
CCCCCCCCCCCCCCC		32.1522369663
116PhosphorylationTMLNSNTTEPKSTTT
CCCCCCCCCCCCCCC		55.3222369663
120PhosphorylationSNTTEPKSTTTDEDL
CCCCCCCCCCCHHHC		41.5219823750
121PhosphorylationNTTEPKSTTTDEDLS
CCCCCCCCCCHHHCC		39.5819823750
122PhosphorylationTTEPKSTTTDEDLSS
CCCCCCCCCHHHCCC		39.0619823750
123PhosphorylationTEPKSTTTDEDLSSS
CCCCCCCCHHHCCCH		37.1625752575
128PhosphorylationTTTDEDLSSSQSRRN
CCCHHHCCCHHHHHH		40.0222369663
129PhosphorylationTTDEDLSSSQSRRNH
CCHHHCCCHHHHHHH		39.4322369663
130PhosphorylationTDEDLSSSQSRRNHK
CHHHCCCHHHHHHHH		28.8822369663
132PhosphorylationEDLSSSQSRRNHKRR
HHCCCHHHHHHHHHC		34.8522369663
142PhosphorylationNHKRRVNYAESDDDD
HHHHCCCCCCCCCCC		14.6422369663
145PhosphorylationRRVNYAESDDDDSDT
HCCCCCCCCCCCCCC		37.8622369663
150PhosphorylationAESDDDDSDTTFTAK
CCCCCCCCCCCEEEE		43.8022369663
152PhosphorylationSDDDDSDTTFTAKRK
CCCCCCCCCEEEEEC		27.9722369663
153PhosphorylationDDDDSDTTFTAKRKK
CCCCCCCCEEEEECC		24.7922890988
155PhosphorylationDDSDTTFTAKRKKGK
CCCCCCEEEEECCCC		29.2222369663
166PhosphorylationKKGKVVDSESDEDEY
CCCCCCCCCCCCCCC		27.6522890988
168PhosphorylationGKVVDSESDEDEYLP
CCCCCCCCCCCCCCC		50.6922890988
173PhosphorylationSESDEDEYLPDKNDG
CCCCCCCCCCCCCCC		35.5428889911
201PhosphorylationKGELAEDSGDDDDLI
CHHHHHCCCCCHHHH		35.3122369663
209PhosphorylationGDDDDLISLAETTSK
CCCHHHHHHHHHCCC		28.9121551504
218AcetylationAETTSKKKFSYNTSH
HHHCCCCCCCCCCCC		43.1925381059
220PhosphorylationTTSKKKFSYNTSHSS
HCCCCCCCCCCCCCC		26.7624961812
221PhosphorylationTSKKKFSYNTSHSSS
CCCCCCCCCCCCCCC		26.1224961812
223PhosphorylationKKKFSYNTSHSSSPF
CCCCCCCCCCCCCCC		21.4223749301
224PhosphorylationKKFSYNTSHSSSPFT
CCCCCCCCCCCCCCC		20.1028889911
226PhosphorylationFSYNTSHSSSPFTRN
CCCCCCCCCCCCCCC		32.0723749301
227PhosphorylationSYNTSHSSSPFTRNI
CCCCCCCCCCCCCCC		36.2821440633
228PhosphorylationYNTSHSSSPFTRNIS
CCCCCCCCCCCCCCC		27.3521440633
231PhosphorylationSHSSSPFTRNISRDN
CCCCCCCCCCCCCCC		26.6224961812
235PhosphorylationSPFTRNISRDNSKKK
CCCCCCCCCCCCCCC		36.8124961812
239PhosphorylationRNISRDNSKKKSRPN
CCCCCCCCCCCCCCC		50.5724961812
240UbiquitinationNISRDNSKKKSRPNQ
CCCCCCCCCCCCCCC		71.1624961812
243PhosphorylationRDNSKKKSRPNQAPS
CCCCCCCCCCCCCCC		62.9521551504
250PhosphorylationSRPNQAPSRSYNPSH
CCCCCCCCCCCCCCC		36.5521551504
252PhosphorylationPNQAPSRSYNPSHSQ
CCCCCCCCCCCCCCC		33.3321551504
256PhosphorylationPSRSYNPSHSQPSAT
CCCCCCCCCCCCCCC		31.9430377154
258PhosphorylationRSYNPSHSQPSATSK
CCCCCCCCCCCCCCC		48.3917563356
261PhosphorylationNPSHSQPSATSKSSK
CCCCCCCCCCCCCCC		36.2221551504
263PhosphorylationSHSQPSATSKSSKFN
CCCCCCCCCCCCCCC		40.8121551504
451PhosphorylationPGNFYNETQLDSSTI
CCCCCCCCCCCHHHH		30.6920190278
552PhosphorylationTYAEIISSEYFSTEE
HHHHHHHCCCCCCCC		26.3819779198
556PhosphorylationIISSEYFSTEEDWPE
HHHCCCCCCCCCHHH		33.7321440633
567PhosphorylationDWPEVLKSYYDTGKK
CHHHHHHHHHHHCCC		25.4321440633
569PhosphorylationPEVLKSYYDTGKKVG
HHHHHHHHHHCCCCC		17.7019779198
848AcetylationWVQMAANKTYKRYYS
HHHHHHCCHHHHHCH		48.8022865919
914PhosphorylationCLLAITRTSEYLGAP
HHHHHHHCHHHCCCC		19.7728889911
917PhosphorylationAITRTSEYLGAPSCR
HHHHCHHHCCCCCCC		15.3728889911
1221PhosphorylationSGEGVLNYDWNIKRN
CCCCCCCCCCCCHHH		20.4128889911
1226UbiquitinationLNYDWNIKRNVLKSL
CCCCCCCHHHHHHHH		34.4124961812
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
102SPhosphorylationKinaseATM/ATR-GPS
130SPhosphorylationKinaseATM/ATR-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MSH6_YEAST !!
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_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LCD1_YEASTLCD1physical
11805826
ATR_YEASTMEC1physical
11805826
MG101_YEASTMGM101physical
11805826
MPH1_YEASTMPH1physical
11805826
MSH2_YEASTMSH2physical
11805826
MSH3_YEASTMSH3physical
11805826
RAD16_YEASTRAD16physical
11805826
RAD52_YEASTRAD52physical
11805826
RFA1_YEASTRFA1physical
11805826
RFA2_YEASTRFA2physical
11805826
RFA3_YEASTRFA3physical
11805826
RIM1_YEASTRIM1physical
11805826
RSC8_YEASTRSC8physical
11805826
RUVB2_YEASTRVB2physical
11805826
SGS1_YEASTSGS1physical
11805826
TOP3_YEASTTOP3physical
11805826
VPS1_YEASTVPS1physical
11805826
CMR1_YEASTCMR1physical
11805826
SHS1_YEASTSHS1physical
11805826
MSH2_YEASTMSH2physical
11805837
MLH1_YEASTMLH1physical
12529393
PCNA_YEASTPOL30physical
11005803
POLH_YEASTRAD30genetic
11406177
PCNA_YEASTPOL30genetic
10523669
OGG1_YEASTOGG1genetic
10518225
RAD59_YEASTRAD59genetic
14704162
MSH3_YEASTMSH3genetic
10615127
MSH2_YEASTMSH2genetic
10615127
MLH1_YEASTMLH1genetic
10615127
OGG1_YEASTOGG1genetic
15749020
MSH2_YEASTMSH2physical
16554755
LCD1_YEASTLCD1physical
16429126
ATR_YEASTMEC1physical
16429126
MPH1_YEASTMPH1physical
16429126
MSH2_YEASTMSH2physical
16429126
MSH3_YEASTMSH3physical
16429126
RAD16_YEASTRAD16physical
16429126
RAD52_YEASTRAD52physical
16429126
RFA1_YEASTRFA1physical
16429126
RFA2_YEASTRFA2physical
16429126
RFA3_YEASTRFA3physical
16429126
RIM1_YEASTRIM1physical
16429126
VPS1_YEASTVPS1physical
16429126
CMR1_YEASTCMR1physical
16429126
MSH2_YEASTMSH2physical
16600868
NUP84_YEASTNUP84genetic
17314980
SSB1_YEASTSSB1physical
19536198
UNG_YEASTUNG1genetic
19547744
MSH3_YEASTMSH3genetic
21414850
PCNA_YEASTPOL30physical
22308326
MG101_YEASTMGM101physical
22912599
DPOE_YEASTPOL2genetic
23307893
PMS1_YEASTPMS1physical
24550389
MLH1_YEASTMLH1physical
24550389
MLH1_YEASTMLH1physical
15811858
PMS1_YEASTPMS1physical
15811858
MLH1_YEASTMLH1physical
24811092
PMS1_YEASTPMS1physical
24811092
MLH2_YEASTMLH2physical
24811092
PCNA_YEASTPOL30physical
23869605
FEN1_YEASTRAD27genetic
26224637
IMB1_YEASTKAP95genetic
27708008
SEC65_YEASTSEC65genetic
27708008
ORC2_YEASTORC2genetic
27708008
MCM7_YEASTMCM7genetic
27708008
SNU23_YEASTSNU23genetic
27708008
DPOD_YEASTPOL3genetic
27708008
NSE4_YEASTNSE4genetic
27708008
GPI19_YEASTGPI19genetic
27708008
CDC20_YEASTCDC20genetic
27708008
PRP18_YEASTPRP18genetic
27708008
RRP4_YEASTRRP4genetic
27708008
DNA2_YEASTDNA2genetic
27708008
MCM10_YEASTMCM10genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
ERG27_YEASTERG27genetic
27708008
UTP13_YEASTUTP13genetic
27708008
CLP1_YEASTCLP1genetic
27708008
ORC4_YEASTORC4genetic
27708008
URA7_YEASTURA7genetic
27708008
YFF2_YEASTYFL052Wgenetic
27708008
ATC1_YEASTPMR1genetic
27708008
THIK_YEASTPOT1genetic
27708008
ELM1_YEASTELM1genetic
27708008
YNO0_YEASTYNL140Cgenetic
27708008
BIOD_YEASTBIO4genetic
27708008
RAX1_YEASTRAX1genetic
27708008
REV1_YEASTREV1physical
26903512
PCNA_YEASTPOL30physical
26903512
MSH2_YEASTMSH2genetic
26680658
MSH3_YEASTMSH3genetic
26680658
DPOD_YEASTPOL3genetic
25827231
IRA2_YEASTIRA2genetic
27453043
DBF2_YEASTDBF2genetic
27453043
RS19B_YEASTRPS19Bgenetic
27453043
SIN3_YEASTSIN3genetic
27453043
YL422_YEASTYLR422Wgenetic
27453043
CDC42_YEASTCDC42genetic
27453043
GCR2_YEASTGCR2genetic
27453043
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MSH6_YEAST

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-21; SER-97;SER-102; SER-107; SER-129; SER-130; SER-145; SER-150; SER-201 ANDTHR-451, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-21; SER-102;SER-130; SER-145; SER-150; THR-152 AND SER-258, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-21; SER-129;SER-130; SER-145 AND SER-150, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-150, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory