PMS1_YEAST - dbPTM
PMS1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PMS1_YEAST
UniProt AC P14242
Protein Name DNA mismatch repair protein PMS1
Gene Name PMS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 873
Subcellular Localization Nucleus .
Protein Description Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of the MutLalpha heterodimer that forms a ternary complex with the MutS heterodimers, which initially recognize the DNA mismatches. This complex is thought to be responsible for directing the downsteam MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in maintaining the genetic stability of simple sequence repeats and in the repair of heteroduplex sites present in meiotic recombination intermediates..
Protein Sequence MTQIHQINDIDVHRITSGQVITDLTTAVKELVDNSIDANANQIEIIFKDYGLESIECSDNGDGIDPSNYEFLALKHYTSKIAKFQDVAKVQTLGFRGEALSSLCGIAKLSVITTTSPPKADKLEYDMVGHITSKTTTSRNKGTTVLVSQLFHNLPVRQKEFSKTFKRQFTKCLTVIQGYAIINAAIKFSVWNITPKGKKNLILSTMRNSSMRKNISSVFGAGGMRGLEEVDLVLDLNPFKNRMLGKYTDDPDFLDLDYKIRVKGYISQNSFGCGRNSKDRQFIYVNKRPVEYSTLLKCCNEVYKTFNNVQFPAVFLNLELPMSLIDVNVTPDKRVILLHNERAVIDIFKTTLSDYYNRQELALPKRMCSQSEQQAQKRLKTEVFDDRSTTHESDNENYHTARSESNQSNHAHFNSTTGVIDKSNGTELTSVMDGNYTNVTDVIGSECEVSVDSSVVLDEGNSSTPTKKLPSIKTDSQNLSDLNLNNFSNPEFQNITSPDKARSLEKVVEEPVYFDIDGEKFQEKAVLSQADGLVFVDNECHEHTNDCCHQERRGSTDTEQDDEADSIYAEIEPVEINVRTPLKNSRKSISKDNYRSLSDGLTHRKFEDEILEYNLSTKNFKEISKNGKQMSSIISKRKSEAQENIIKNKDELEDFEQGEKYLTLTVSKNDFKKMEVVGQFNLGFIIVTRKVDNKYDLFIVDQHASDEKYNFETLQAVTVFKSQKLIIPQPVELSVIDELVVLDNLPVFEKNGFKLKIDEEEEFGSRVKLLSLPTSKQTLFDLGDFNELIHLIKEDGGLRRDNIRCSKIRSMFAMRACRSSIMIGKPLNKKTMTRVVHNLSELDKPWNCPHGRPTMRHLMELRDWSSFSKDYEI
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
101PhosphorylationGFRGEALSSLCGIAK
CCCHHHHHHHHCEEE		28.4524961812
102PhosphorylationFRGEALSSLCGIAKL
CCHHHHHHHHCEEEE		28.6424961812
125PhosphorylationPKADKLEYDMVGHIT
CCCCCCCEEEEEEEE		21.5627214570
246AcetylationFKNRMLGKYTDDPDF
HCCCCCCCCCCCCCC		40.8022865919
247PhosphorylationKNRMLGKYTDDPDFL
CCCCCCCCCCCCCCC		17.3827017623
248PhosphorylationNRMLGKYTDDPDFLD
CCCCCCCCCCCCCCC		37.0927017623
369PhosphorylationALPKRMCSQSEQQAQ
HCCHHHCCHHHHHHH		27.6523749301
377AcetylationQSEQQAQKRLKTEVF
HHHHHHHHHHHHHCC		63.8125381059
388PhosphorylationTEVFDDRSTTHESDN
HHCCCCCCCCCCCCC		44.6528889911
390PhosphorylationVFDDRSTTHESDNEN
CCCCCCCCCCCCCCC		25.5428132839
393PhosphorylationDRSTTHESDNENYHT
CCCCCCCCCCCCCCC		37.8221082442
405PhosphorylationYHTARSESNQSNHAH
CCCCCCCCCCCCCCC		41.2227017623
408PhosphorylationARSESNQSNHAHFNS
CCCCCCCCCCCCCCC		34.5319779198
476PhosphorylationLPSIKTDSQNLSDLN
CCCCCCCCCCHHHCC		26.6321440633
480PhosphorylationKTDSQNLSDLNLNNF
CCCCCCHHHCCCCCC		47.8321440633
496PhosphorylationNPEFQNITSPDKARS
CHHHCCCCCHHHHHC		41.5821440633
497PhosphorylationPEFQNITSPDKARSL
HHHCCCCCHHHHHCH		27.5725752575
555PhosphorylationCHQERRGSTDTEQDD
CHHCCCCCCCCCCCC		22.6928889911
556PhosphorylationHQERRGSTDTEQDDE
HHCCCCCCCCCCCCH		50.1728889911
558PhosphorylationERRGSTDTEQDDEAD
CCCCCCCCCCCCHHH		35.3228889911
566PhosphorylationEQDDEADSIYAEIEP
CCCCHHHHEEEEEEC		25.2510938116
568PhosphorylationDDEADSIYAEIEPVE
CCHHHHEEEEEECEE		11.3519779198
598PhosphorylationKDNYRSLSDGLTHRK
CCCCCHHHCCCCCCH		30.7728889911
771PhosphorylationGSRVKLLSLPTSKQT
CCEEEEEECCCCCCE		42.6229136822
774PhosphorylationVKLLSLPTSKQTLFD
EEEEECCCCCCEEEE		54.5829136822
775PhosphorylationKLLSLPTSKQTLFDL
EEEECCCCCCEEEEC		22.3429136822
810PhosphorylationIRCSKIRSMFAMRAC
CCHHHHHHHHHHHHH		23.0228889911
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 PMS1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PMS1_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 PMS1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MLH1_YEASTMLH1physical
11805826
MSH2_YEASTMSH2physical
8066446
MLH1_YEASTMLH1physical
11154280
MLH1_YEASTMLH1physical
9234704
MLH1_YEASTMLH1physical
11575920
MLH1_YEASTMLH1physical
10570173
MLH1_YEASTMLH1physical
12454061
MLH1_YEASTMLH1physical
8858149
POLH_YEASTRAD30genetic
11406177
EXO1_YEASTEXO1genetic
11438669
MLH1_YEASTMLH1genetic
11438669
MSH2_YEASTMSH2genetic
11438669
MSH3_YEASTMSH3genetic
11438669
MSH6_YEASTMSH6genetic
11438669
PCNA_YEASTPOL30genetic
9343398
MSH2_YEASTMSH2genetic
8887641
RAD1_YEASTRAD1genetic
8849883
RAD52_YEASTRAD52genetic
8849883
DPOD_YEASTPOL3genetic
8844147
HSM3_YEASTHSM3genetic
15450405
DPOE_YEASTPOL2genetic
16227575
MLH1_YEASTMLH1physical
16429126
HSP72_YEASTSSA2physical
16429126
MSH2_YEASTMSH2genetic
11779795
MED31_YEASTSOH1genetic
17314980
DPOD3_YEASTPOL32genetic
17314980
SPT4_YEASTSPT4genetic
17314980
MNN10_YEASTMNN10genetic
18931302
MLH1_YEASTMLH1physical
19015241
EXO1_YEASTEXO1genetic
19015241
MLH1_YEASTMLH1genetic
19015241
SIS2_YEASTSIS2genetic
21143561
MLH1_YEASTMLH1physical
22659005
MLH1_YEASTMLH1genetic
22659005
MLH3_YEASTMLH3genetic
23307893
DPOE_YEASTPOL2genetic
23307893
MLH3_YEASTMLH3genetic
24204320
MSH6_YEASTMSH6genetic
24204320
YPT7_YEASTYPT7genetic
27708008
RU2A_YEASTLEA1genetic
27708008
CG22_YEASTCLB2genetic
27811238
DCOR_YEASTSPE1genetic
27453043
HFA1_YEASTHFA1genetic
27453043
DCAM_YEASTSPE2genetic
27453043
ALDH4_YEASTALD4genetic
27453043
AIM33_YEASTAIM33genetic
27453043
ERG2_YEASTERG2genetic
27453043
GCR2_YEASTGCR2genetic
27453043
CDC42_YEASTCDC42genetic
27453043
PPA3_YEASTPHO3genetic
27453043
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PMS1_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-393 AND SER-598, ANDMASS 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-393, AND MASSSPECTROMETRY.

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