MLH1_YEAST - dbPTM
MLH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MLH1_YEAST
UniProt AC P38920
Protein Name DNA mismatch repair protein MLH1
Gene Name MLH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 769
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 different MutL heterodimers that form 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, the repair of heteroduplex sites present in meiotic recombination intermediates, and the promotion of meiotic crossing-over..
Protein Sequence MSLRIKALDASVVNKIAAGEIIISPVNALKEMMENSIDANATMIDILVKEGGIKVLQITDNGSGINKADLPILCERFTTSKLQKFEDLSQIQTYGFRGEALASISHVARVTVTTKVKEDRCAWRVSYAEGKMLESPKPVAGKDGTTILVEDLFFNIPSRLRALRSHNDEYSKILDVVGRYAIHSKDIGFSCKKFGDSNYSLSVKPSYTVQDRIRTVFNKSVASNLITFHISKVEDLNLESVDGKVCNLNFISKKSISPIFFINNRLVTCDLLRRALNSVYSNYLPKGNRPFIYLGIVIDPAAVDVNVHPTKREVRFLSQDEIIEKIANQLHAELSAIDTSRTFKASSISTNKPESLIPFNDTIESDRNRKSLRQAQVVENSYTTANSQLRKAKRQENKLVRIDASQAKITSFLSSSQQFNFEGSSTKRQLSEPKVTNVSHSQEAEKLTLNESEQPRDANTINDNDLKDQPKKKQKLGDYKVPSIADDEKNALPISKDGYIRVPKERVNVNLTSIKKLREKVDDSIHRELTDIFANLNYVGVVDEERRLAAIQHDLKLFLIDYGSVCYELFYQIGLTDFANFGKINLQSTNVSDDIVLYNLLSEFDELNDDASKEKIISKIWDMSSMLNEYYSIELVNDGLDNDLKSVKLKSLPLLLKGYIPSLVKLPFFIYRLGKEVDWEDEQECLDGILREIALLYIPDMVPKVDTSDASLSEDEKAQFINRKEHISSLLEHVLFPCIKRRFLAPRHILKDVVEIANLPDLYKVFERC
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
135PhosphorylationAEGKMLESPKPVAGK
CCCCCCCCCCCCCCC		33.9723749301
362PhosphorylationSLIPFNDTIESDRNR
HHCCCCCCCCCHHCH		27.9627214570
371PhosphorylationESDRNRKSLRQAQVV
CCHHCHHHHHHHHHH		26.0824961812
431PhosphorylationSSTKRQLSEPKVTNV
CCCCCCCCCCCCCCC		43.4419795423
439PhosphorylationEPKVTNVSHSQEAEK
CCCCCCCCCCHHHHH		21.3528889911
441PhosphorylationKVTNVSHSQEAEKLT
CCCCCCCCHHHHHCC		23.3925521595
446AcetylationSHSQEAEKLTLNESE
CCCHHHHHCCCCCCC		54.5424489116
483PhosphorylationLGDYKVPSIADDEKN
CCCCCCCCCCCCCCC		33.1425752575
496AcetylationKNALPISKDGYIRVP
CCCCCCCCCCEEECC		56.7624489116
764UbiquitinationANLPDLYKVFERC--
HCCHHHHHHHHCC--		47.9824961812
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
441SPhosphorylationKinaseATMP38110
Uniprot
441SPhosphorylationKinaseATRP38111
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MLH1_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 MLH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PMS1_YEASTPMS1physical
11805826
GRPE_YEASTMGE1physical
11805837
ISN1_YEASTISN1physical
11805837
MLH2_YEASTMLH2physical
10570173
MLH3_YEASTMLH3physical
10570173
PMS1_YEASTPMS1physical
10570173
MLH1_YEASTMLH1physical
12682353
MSH2_YEASTMSH2physical
8066446
PMS1_YEASTPMS1physical
8066446
MLH1_YEASTMLH1physical
11154280
PMS1_YEASTPMS1physical
9234704
EXO1_YEASTEXO1physical
12529393
EXO1_YEASTEXO1physical
11901110
MLH3_YEASTMLH3physical
12529393
SGS1_YEASTSGS1physical
12529393
SGS1_YEASTSGS1physical
11901110
PMS1_YEASTPMS1physical
11901110
EXO1_YEASTEXO1physical
11481425
PMS1_YEASTPMS1physical
10938116
PCNA_YEASTPOL30physical
8858149
PMS1_YEASTPMS1physical
16227575
PMS1_YEASTPMS1physical
9545323
PMS1_YEASTPMS1physical
9368761
PMS1_YEASTPMS1physical
11237696
HSP71_YEASTSSA1physical
11237696
PMS1_YEASTPMS1genetic
11154280
RAD1_YEASTRAD1genetic
8849883
RAD52_YEASTRAD52genetic
8849883
DPOD_YEASTPOL3genetic
11901110
RAD59_YEASTRAD59genetic
14704162
RAD51_YEASTRAD51genetic
14704162
MMS4_YEASTMMS4genetic
15611158
PMS1_YEASTPMS1physical
16429126
HSP72_YEASTSSA2physical
16429126
MLH3_YEASTMLH3genetic
16702432
PMS1_YEASTPMS1genetic
16702432
CSM3_YEASTCSM3genetic
17314980
UBP3_YEASTUBP3genetic
17314980
RAD34_YEASTRAD34genetic
17314980
SWI4_YEASTSWI4genetic
17314980
GET2_YEASTGET2genetic
17314980
PFD5_YEASTGIM5genetic
17314980
PFD6_YEASTYKE2genetic
17314980
EXO1_YEASTEXO1physical
17602897
MLH3_YEASTMLH3physical
18505871
CSM4_YEASTCSM4genetic
18818741
NTH2_YEASTNTG2physical
19015241
EXO1_YEASTEXO1physical
19015241
SGS1_YEASTSGS1physical
19015241
PMS1_YEASTPMS1physical
19015241
BLM_HUMANBLMphysical
19015241
NTH2_YEASTNTG2genetic
19015241
EXO1_YEASTEXO1genetic
19015241
MSH2_YEASTMSH2genetic
20176959
PMS1_YEASTPMS1genetic
20176959
MSH6_YEASTMSH6genetic
20176959
SIS2_YEASTSIS2genetic
21143561
SGS1_YEASTSGS1genetic
21172664
MDM10_YEASTMDM10genetic
21987634
LONM_YEASTPIM1genetic
21987634
PIN4_YEASTPIN4genetic
21987634
VATB_YEASTVMA2genetic
21987634
FZO1_YEASTFZO1genetic
21987634
SHR3_YEASTSHR3genetic
21987634
GYP7_YEASTGYP7genetic
21987634
DOP1_YEASTDOP1genetic
21987634
PEP7_YEASTPEP7genetic
21987634
RV167_YEASTRVS167genetic
21987634
UGO1_YEASTUGO1genetic
21987634
VPS52_YEASTVPS52genetic
21987634
GET2_YEASTGET2genetic
21987634
UBP3_YEASTUBP3genetic
21987634
CHO2_YEASTCHO2genetic
21987634
ZUO1_YEASTZUO1genetic
21987634
PT130_YEASTPET130genetic
21987634
ILM1_YEASTILM1genetic
21987634
MG101_YEASTMGM101genetic
21987634
VPH2_YEASTVPH2genetic
21987634
SAC1_YEASTSAC1genetic
21987634
MMM1_YEASTMMM1genetic
21987634
GEP5_YEASTGEP5genetic
21987634
PFD6_YEASTYKE2genetic
21987634
YPT6_YEASTYPT6genetic
21987634
ACON_YEASTACO1genetic
21987634
CYK2_YEASTHOF1genetic
21987634
IPYR2_YEASTPPA2genetic
21987634
H2AZ_YEASTHTZ1genetic
21987634
VATL2_YEASTVMA11genetic
21987634
YME1_YEASTYME1genetic
21987634
PCNA_YEASTPOL30genetic
8858149
PMS1_YEASTPMS1physical
23435383
RNH2A_YEASTRNH201genetic
23603115
PMS1_YEASTPMS1physical
24204293
MLH3_YEASTMLH3physical
24443562
MLH3_YEASTMLH3physical
24403070
PMS1_YEASTPMS1physical
24550389
PMS1_YEASTPMS1physical
15811858
MLH2_YEASTMLH2physical
24811092
PMS1_YEASTPMS1physical
24811092
EXO1_YEASTEXO1physical
23435383
NTH2_YEASTNTG2physical
23435383
PMS1_YEASTPMS1physical
24981171
PMS1_YEASTPMS1physical
18206974
URA7_YEASTURA7genetic
27708008
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
RMD1_YEASTRMD1genetic
27708008
RL41A_YEASTRPL41Agenetic
27708008
RL41B_YEASTRPL41Agenetic
27708008
TRM1_YEASTTRM1genetic
27708008
MKC7_YEASTMKC7genetic
27708008
ATC1_YEASTPMR1genetic
27708008
VMA21_YEASTVMA21genetic
27708008
MED20_YEASTSRB2genetic
27708008
URM1_YEASTURM1genetic
27708008
YKE44_YEASTYKL044Wgenetic
27708008
RM49_YEASTMRP49genetic
27708008
UPS1_YEASTUPS1genetic
27708008
ORM2_YEASTORM2genetic
27708008
BUL2_YEASTBUL2genetic
27708008
LIPA_YEASTLIP5genetic
27708008
PMS1_YEASTPMS1physical
28051769
MLH2_YEASTMLH2physical
28051769
MLH3_YEASTMLH3physical
28051769
HFM1_YEASTHFM1physical
28051769
SGS1_YEASTSGS1genetic
28781235
MRE11_YEASTMRE11genetic
28781235
EXO1_YEASTEXO1genetic
28781235
DPOD3_YEASTPOL32genetic
28781235
FLX1_YEASTFLX1genetic
27453043
RXT2_YEASTRXT2genetic
27453043
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MLH1_YEAST

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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-439 AND SER-441, 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-441, AND MASSSPECTROMETRY.

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