PMS2_HUMAN - dbPTM
PMS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PMS2_HUMAN
UniProt AC P54278
Protein Name Mismatch repair endonuclease PMS2 {ECO:0000305}
Gene Name PMS2 {ECO:0000312|HGNC:HGNC:9122}
Organism Homo sapiens (Human).
Sequence Length 862
Subcellular Localization Nucleus .
Protein Description Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MLH1 to form MutL alpha. DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH6) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages..
Protein Sequence MERAESSSTEPAKAIKPIDRKSVHQICSGQVVLSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSDNGCGVEEENFEGLTLKHHTSKIQEFADLTQVETFGFRGEALSSLCALSDVTISTCHASAKVGTRLMFDHNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKEFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNQLGQGKRQPVVCTGGSPSIKENIGSVFGQKQLQSLIPFVQLPPSDSVCEEYGLSCSDALHNLFYISGFISQCTHGVGRSSTDRQFFFINRRPCDPAKVCRLVNEVYHMYNRHQYPFVVLNISVDSECVDINVTPDKRQILLQEEKLLLAVLKTSLIGMFDSDVNKLNVSQQPLLDVEGNLIKMHAADLEKPMVEKQDQSPSLRTGEEKKDVSISRLREAFSLRHTTENKPHSPKTPEPRRSPLGQKRGMLSSSTSGAISDKGVLRPQKEAVSSSHGPSDPTDRAEVEKDSGHGSTSVDSEGFSIPDTGSHCSSEYAASSPGDRGSQEHVDSQEKAPKTDDSFSDVDCHSNQEDTGCKFRVLPQPTNLATPNTKRFKKEEILSSSDICQKLVNTQDMSASQVDVAVKINKKVVPLDFSMSSLAKRIKQLHHEAQQSEGEQNYRKFRAKICPGENQAAEDELRKEISKTMFAEMEIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTVLQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFVIDENAPVTERAKLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCRPSRVKQMFASRACRKSVMIGTALNTSEMKKLITHMGEMDHPWNCPHGRPTMRHIANLGVISQN
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
13UbiquitinationSSSTEPAKAIKPIDR
CCCCCCCHHCCCCCH		62.45-
57UbiquitinationGATNIDLKLKDYGVD
CCCCCEEEEHHHCCE		50.14-
57SumoylationGATNIDLKLKDYGVD
CCCCCEEEEHHHCCE		50.14-
142UbiquitinationLMFDHNGKIIQKTPY
EEECCCCCEEECCCC		41.79-
146 (in isoform 4)Ubiquitination-40.8521890473
146UbiquitinationHNGKIIQKTPYPRPR
CCCCEEECCCCCCCC		40.8521890473
146 (in isoform 1)Ubiquitination-40.8521890473
146 (in isoform 2)Ubiquitination-40.8521890473
146 (in isoform 3)Ubiquitination-40.8521890473
210AcetylationTNQLGQGKRQPVVCT
CCCCCCCCCCCEEEC		39.7223749302
220PhosphorylationPVVCTGGSPSIKENI
CEEECCCCCCHHHHH		19.4725159151
224UbiquitinationTGGSPSIKENIGSVF
CCCCCCHHHHHHHHH		49.39-
301UbiquitinationRRPCDPAKVCRLVNE
CCCCCHHHHHHHHHH		47.45-
373PhosphorylationDVNKLNVSQQPLLDV
CHHCCCCCCCCCCCC		23.2528555341
386UbiquitinationDVEGNLIKMHAADLE
CCCCCEEEEEEHHHC		28.00-
394AcetylationMHAADLEKPMVEKQD
EEEHHHCCCCCCCCC		45.7925953088
403PhosphorylationMVEKQDQSPSLRTGE
CCCCCCCCCCCCCCC		25.4229255136
405PhosphorylationEKQDQSPSLRTGEEK
CCCCCCCCCCCCCHH		35.4129255136
408PhosphorylationDQSPSLRTGEEKKDV
CCCCCCCCCCHHHCC		54.9928102081
413SumoylationLRTGEEKKDVSISRL
CCCCCHHHCCCHHHH		67.64-
413SumoylationLRTGEEKKDVSISRL
CCCCCHHHCCCHHHH		67.64-
418PhosphorylationEKKDVSISRLREAFS
HHHCCCHHHHHHHHH		20.1124719451
425PhosphorylationSRLREAFSLRHTTEN
HHHHHHHHCCCCCCC		31.3823186163
429PhosphorylationEAFSLRHTTENKPHS
HHHHCCCCCCCCCCC		29.3923927012
430PhosphorylationAFSLRHTTENKPHSP
HHHCCCCCCCCCCCC		31.2829496963
436PhosphorylationTTENKPHSPKTPEPR
CCCCCCCCCCCCCCC		36.3030278072
439PhosphorylationNKPHSPKTPEPRRSP
CCCCCCCCCCCCCCC		35.9523927012
445PhosphorylationKTPEPRRSPLGQKRG
CCCCCCCCCCCCCCC		26.2530266825
450AcetylationRRSPLGQKRGMLSSS
CCCCCCCCCCCCCCC		49.4718527201
455PhosphorylationGQKRGMLSSSTSGAI
CCCCCCCCCCCCCCC		17.2222210691
456PhosphorylationQKRGMLSSSTSGAIS
CCCCCCCCCCCCCCC		33.4028555341
457PhosphorylationKRGMLSSSTSGAISD
CCCCCCCCCCCCCCC		24.1825627689
458PhosphorylationRGMLSSSTSGAISDK
CCCCCCCCCCCCCCC		32.8822210691
459PhosphorylationGMLSSSTSGAISDKG
CCCCCCCCCCCCCCC		28.3328555341
465AcetylationTSGAISDKGVLRPQK
CCCCCCCCCCCCCHH		44.0925953088
478PhosphorylationQKEAVSSSHGPSDPT
HHHHHHCCCCCCCCC		25.5917525332
482PhosphorylationVSSSHGPSDPTDRAE
HHCCCCCCCCCCHHH		61.89-
485PhosphorylationSHGPSDPTDRAEVEK
CCCCCCCCCHHHHCC		43.01-
494PhosphorylationRAEVEKDSGHGSTSV
HHHHCCCCCCCCCCC		43.7026074081
498PhosphorylationEKDSGHGSTSVDSEG
CCCCCCCCCCCCCCC		16.3126074081
499PhosphorylationKDSGHGSTSVDSEGF
CCCCCCCCCCCCCCC		37.0430576142
500PhosphorylationDSGHGSTSVDSEGFS
CCCCCCCCCCCCCCC		26.1426074081
503PhosphorylationHGSTSVDSEGFSIPD
CCCCCCCCCCCCCCC		37.1523663014
507PhosphorylationSVDSEGFSIPDTGSH
CCCCCCCCCCCCCCC		44.0323663014
511PhosphorylationEGFSIPDTGSHCSSE
CCCCCCCCCCCCCCC		34.9221955146
513PhosphorylationFSIPDTGSHCSSEYA
CCCCCCCCCCCCCCC		24.3423663014
516PhosphorylationPDTGSHCSSEYAASS
CCCCCCCCCCCCCCC		22.3023401153
517PhosphorylationDTGSHCSSEYAASSP
CCCCCCCCCCCCCCC		39.7723663014
519PhosphorylationGSHCSSEYAASSPGD
CCCCCCCCCCCCCCC		14.9321955146
522PhosphorylationCSSEYAASSPGDRGS
CCCCCCCCCCCCCCC		28.9721955146
523PhosphorylationSSEYAASSPGDRGSQ
CCCCCCCCCCCCCCH		28.3321955146
529PhosphorylationSSPGDRGSQEHVDSQ
CCCCCCCCHHCCCCC		33.0323663014
535PhosphorylationGSQEHVDSQEKAPKT
CCHHCCCCCCCCCCC		38.8725849741
542PhosphorylationSQEKAPKTDDSFSDV
CCCCCCCCCCCCCCC		43.9428450419
545PhosphorylationKAPKTDDSFSDVDCH
CCCCCCCCCCCCCCC		29.4728450419
547PhosphorylationPKTDDSFSDVDCHSN
CCCCCCCCCCCCCCC		40.4523663014
553PhosphorylationFSDVDCHSNQEDTGC
CCCCCCCCCCCCCCC		46.6823663014
558PhosphorylationCHSNQEDTGCKFRVL
CCCCCCCCCCEEEEC		43.6728450419
569PhosphorylationFRVLPQPTNLATPNT
EEECCCCCCCCCCCC		37.3030266825
573PhosphorylationPQPTNLATPNTKRFK
CCCCCCCCCCCCCCC		21.9030266825
576PhosphorylationTNLATPNTKRFKKEE
CCCCCCCCCCCCHHH		25.4630266825
577AcetylationNLATPNTKRFKKEEI
CCCCCCCCCCCHHHH		63.5825953088
581UbiquitinationPNTKRFKKEEILSSS
CCCCCCCHHHHCCCH		58.84-
587PhosphorylationKKEEILSSSDICQKL
CHHHHCCCHHHHHHH		28.6928555341
588PhosphorylationKEEILSSSDICQKLV
HHHHCCCHHHHHHHC		27.8425159151
597PhosphorylationICQKLVNTQDMSASQ
HHHHHCCCCCCCHHH		20.6124027009
601PhosphorylationLVNTQDMSASQVDVA
HCCCCCCCHHHCCEE		32.8120068231
603PhosphorylationNTQDMSASQVDVAVK
CCCCCCHHHCCEEEE		24.3530576142
621PhosphorylationKVVPLDFSMSSLAKR
EEECCCCCHHHHHHH		19.8829083192
623PhosphorylationVPLDFSMSSLAKRIK
ECCCCCHHHHHHHHH		22.4729083192
624PhosphorylationPLDFSMSSLAKRIKQ
CCCCCHHHHHHHHHH		24.5721552520
630UbiquitinationSSLAKRIKQLHHEAQ
HHHHHHHHHHHHHHH		51.33-
639PhosphorylationLHHEAQQSEGEQNYR
HHHHHHHCHHHHHHH		35.1721552520
645PhosphorylationQSEGEQNYRKFRAKI
HCHHHHHHHHHHHHC		18.1821552520
647UbiquitinationEGEQNYRKFRAKICP
HHHHHHHHHHHHCCC		28.92-
651SumoylationNYRKFRAKICPGENQ
HHHHHHHHCCCCCCH		40.35-
651UbiquitinationNYRKFRAKICPGENQ
HHHHHHHHCCCCCCH		40.35-
651SumoylationNYRKFRAKICPGENQ
HHHHHHHHCCCCCCH		40.35-
748UbiquitinationENLEIFRKNGFDFVI
CCHHHHHHHCCCEEE		51.15-
766UbiquitinationAPVTERAKLISLPTS
CCCCCCEEEEECCCC		53.20-
769PhosphorylationTERAKLISLPTSKNW
CCCEEEEECCCCCCC		38.4429449344
772PhosphorylationAKLISLPTSKNWTFG
EEEEECCCCCCCCCC		58.5929449344
773PhosphorylationKLISLPTSKNWTFGP
EEEECCCCCCCCCCC		23.2729449344
777PhosphorylationLPTSKNWTFGPQDVD
CCCCCCCCCCCCCHH		28.2724719451
791PhosphorylationDELIFMLSDSPGVMC
HHHHHHHCCCCCCCC		25.0124719451
793PhosphorylationLIFMLSDSPGVMCRP
HHHHHCCCCCCCCCH		21.8524719451
815PhosphorylationASRACRKSVMIGTAL
HHHHHCHHHHEECCC		9.5130206219
820PhosphorylationRKSVMIGTALNTSEM
CHHHHEECCCCHHHH		19.6330206219
824PhosphorylationMIGTALNTSEMKKLI
HEECCCCHHHHHHHH		27.2430206219
825PhosphorylationIGTALNTSEMKKLIT
EECCCCHHHHHHHHH		34.3228165663
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 PMS2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PMS2_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 PMS2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MLH1_HUMANMLH1physical
11292842
MLH1_HUMANMLH1physical
17148452
MSH3_HUMANMSH3physical
17148452
BRCA2_HUMANBRCA2physical
17148452
PSD2_HUMANPSD2physical
17148452
UBC_HUMANUBCphysical
17148452
EXO1_HUMANEXO1physical
17148452
PRKDC_HUMANPRKDCphysical
17148452
IMA1_HUMANKPNA2physical
17148452
IMB1_HUMANKPNB1physical
17148452
RUVB1_HUMANRUVBL1physical
17148452
RUVB2_HUMANRUVBL2physical
17148452
FAN1_HUMANFAN1physical
17148452
PP2AA_HUMANPPP2CAphysical
17148452
AIFM1_HUMANAIFM1physical
17148452
P3C2A_HUMANPIK3C2Aphysical
17148452
ATD3A_HUMANATAD3Aphysical
17148452
MSH2_HUMANMSH2physical
17148452
MSH6_HUMANMSH6physical
17148452
PCNA_HUMANPCNAphysical
17148452
RFC2_HUMANRFC2physical
17148452
DDB1_HUMANDDB1physical
17148452
MCM3_HUMANMCM3physical
17148452
SMCA4_HUMANSMARCA4physical
17148452
XPO1_HUMANXPO1physical
17148452
COPB_HUMANCOPB1physical
17148452
COPG1_HUMANCOPG1physical
17148452
COPG2_HUMANCOPG2physical
17148452
PRS4_HUMANPSMC1physical
17148452
PRS10_HUMANPSMC6physical
17148452
PSMD5_HUMANPSMD5physical
17148452
PSD3_HUMANPSD3physical
17148452
PRS6A_HUMANPSMC3physical
17148452
PRS7_HUMANPSMC2physical
17148452
CYLD_HUMANCYLDphysical
17148452
UBR5_HUMANUBR5physical
17148452
NSUN2_HUMANNSUN2physical
17148452
FANCJ_HUMANBRIP1physical
17148452
MMS19_HUMANMMS19physical
17148452
TOPB1_HUMANTOPBP1physical
20029092
CLSPN_HUMANCLSPNphysical
20029092
FAN1_HUMANFAN1physical
20603073
MLH1_HUMANMLH1physical
14676842
MSH2_HUMANMSH2physical
10748159
MSH6_HUMANMSH6physical
10748159
PCNA_HUMANPCNAphysical
15225546
ABCA2_HUMANABCA2physical
26496610
FYN_HUMANFYNphysical
26496610
MLH1_HUMANMLH1physical
26496610
FAN1_HUMANFAN1physical
26496610
RPA12_HUMANZNRD1physical
26496610
FANCJ_HUMANBRIP1physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614337Hereditary non-polyposis colorectal cancer 4 (HNPCC4)
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 PMS2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-403 AND THR-573, ANDMASS SPECTROMETRY.

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