PMS1_HUMAN - dbPTM
PMS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PMS1_HUMAN
UniProt AC P54277
Protein Name PMS1 protein homolog 1
Gene Name PMS1
Organism Homo sapiens (Human).
Sequence Length 932
Subcellular Localization Nucleus .
Protein Description Probably involved in the repair of mismatches in DNA..
Protein Sequence MKQLPAATVRLLSSSQIITSVVSVVKELIENSLDAGATSVDVKLENYGFDKIEVRDNGEGIKAVDAPVMAMKYYTSKINSHEDLENLTTYGFRGEALGSICCIAEVLITTRTAADNFSTQYVLDGSGHILSQKPSHLGQGTTVTALRLFKNLPVRKQFYSTAKKCKDEIKKIQDLLMSFGILKPDLRIVFVHNKAVIWQKSRVSDHKMALMSVLGTAVMNNMESFQYHSEESQIYLSGFLPKCDADHSFTSLSTPERSFIFINSRPVHQKDILKLIRHHYNLKCLKESTRLYPVFFLKIDVPTADVDVNLTPDKSQVLLQNKESVLIALENLMTTCYGPLPSTNSYENNKTDVSAADIVLSKTAETDVLFNKVESSGKNYSNVDTSVIPFQNDMHNDESGKNTDDCLNHQISIGDFGYGHCSSEISNIDKNTKNAFQDISMSNVSWENSQTEYSKTCFISSVKHTQSENGNKDHIDESGENEEEAGLENSSEISADEWSRGNILKNSVGENIEPVKILVPEKSLPCKVSNNNYPIPEQMNLNEDSCNKKSNVIDNKSGKVTAYDLLSNRVIKKPMSASALFVQDHRPQFLIENPKTSLEDATLQIEELWKTLSEEEKLKYEEKATKDLERYNSQMKRAIEQESQMSLKDGRKKIKPTSAWNLAQKHKLKTSLSNQPKLDELLQSQIEKRRSQNIKMVQIPFSMKNLKINFKKQNKVDLEEKDEPCLIHNLRFPDAWLMTSKTEVMLLNPYRVEEALLFKRLLENHKLPAEPLEKPIMLTESLFNGSHYLDVLYKMTADDQRYSGSTYLSDPRLTANGFKIKLIPGVSITENYLEIEGMANCLPFYGVADLKEILNAILNRNAKEVYECRPRKVISYLEGEAVRLSRQLPMYLSKEDIQDIIYRMKHQFGNEIKECVHGRPFFHHLTYLPETT
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
2Ubiquitination------MKQLPAATV
------CCCCCHHHH
61.62-
8PhosphorylationMKQLPAATVRLLSSS
CCCCCHHHHHHHCHH
14.31-
13PhosphorylationAATVRLLSSSQIITS
HHHHHHHCHHHHHHH
32.32-
14PhosphorylationATVRLLSSSQIITSV
HHHHHHCHHHHHHHH
26.65-
43UbiquitinationGATSVDVKLENYGFD
CCCEEEEEEECCCCC
45.6921906983
51UbiquitinationLENYGFDKIEVRDNG
EECCCCCEEEEEECC
38.21-
62UbiquitinationRDNGEGIKAVDAPVM
EECCCCCEECCCCEE
53.89-
72UbiquitinationDAPVMAMKYYTSKIN
CCCEEEHHHHHHCCC
26.10-
77UbiquitinationAMKYYTSKINSHEDL
EHHHHHHCCCCHHHH
37.80-
147UbiquitinationGTTVTALRLFKNLPV
CCCHHHHHHHHCCCH
35.3021906983
150UbiquitinationVTALRLFKNLPVRKQ
HHHHHHHHCCCHHHH
63.27-
156UbiquitinationFKNLPVRKQFYSTAK
HHCCCHHHHHHHHHH
45.02-
200UbiquitinationNKAVIWQKSRVSDHK
CCEEEEECCCCCHHH
25.82-
204PhosphorylationIWQKSRVSDHKMALM
EEECCCCCHHHHHHH
32.65-
270UbiquitinationNSRPVHQKDILKLIR
CCCCCCHHHHHHHHH
31.68-
274SuccinylationVHQKDILKLIRHHYN
CCHHHHHHHHHHHCC
42.0527452117
274AcetylationVHQKDILKLIRHHYN
CCHHHHHHHHHHHCC
42.0525953088
280PhosphorylationLKLIRHHYNLKCLKE
HHHHHHHCCHHHHHH
18.96-
283UbiquitinationIRHHYNLKCLKESTR
HHHHCCHHHHHHCCC
33.61-
311PhosphorylationADVDVNLTPDKSQVL
CCCCCCCCCCHHHHH
25.0025159151
314UbiquitinationDVNLTPDKSQVLLQN
CCCCCCCHHHHHHCC
43.95-
315PhosphorylationVNLTPDKSQVLLQNK
CCCCCCHHHHHHCCC
32.6624961811
354PhosphorylationENNKTDVSAADIVLS
CCCCCCCCHHHHHCC
22.1328555341
362UbiquitinationAADIVLSKTAETDVL
HHHHHCCCCCCCHHH
47.8221906983
372SumoylationETDVLFNKVESSGKN
CCHHHHHHHHCCCCC
39.79-
372SumoylationETDVLFNKVESSGKN
CCHHHHHHHHCCCCC
39.79-
372UbiquitinationETDVLFNKVESSGKN
CCHHHHHHHHCCCCC
39.79-
378UbiquitinationNKVESSGKNYSNVDT
HHHHCCCCCCCCCCC
55.44-
380PhosphorylationVESSGKNYSNVDTSV
HHCCCCCCCCCCCCE
12.7127642862
416 (in isoform 4)Phosphorylation-7.3829083192
419 (in isoform 4)Phosphorylation-18.7229083192
442PhosphorylationAFQDISMSNVSWENS
HCHHHCCCCCCCCCC
27.5628450419
445PhosphorylationDISMSNVSWENSQTE
HHCCCCCCCCCCCCC
32.6828450419
449PhosphorylationSNVSWENSQTEYSKT
CCCCCCCCCCCEECE
27.2828450419
451PhosphorylationVSWENSQTEYSKTCF
CCCCCCCCCEECEEE
36.3928450419
453PhosphorylationWENSQTEYSKTCFIS
CCCCCCCEECEEEEE
20.8928450419
454PhosphorylationENSQTEYSKTCFISS
CCCCCCEECEEEEEE
18.4328450419
505SumoylationWSRGNILKNSVGENI
HHHCCHHHCCCCCCC
43.30-
505UbiquitinationWSRGNILKNSVGENI
HHHCCHHHCCCCCCC
43.30-
505MethylationWSRGNILKNSVGENI
HHHCCHHHCCCCCCC
43.30110871769
505SumoylationWSRGNILKNSVGENI
HHHCCHHHCCCCCCC
43.30-
507PhosphorylationRGNILKNSVGENIEP
HCCHHHCCCCCCCCC
29.8825159151
517UbiquitinationENIEPVKILVPEKSL
CCCCCEEEEEECCCC
4.8321906983
522AcetylationVKILVPEKSLPCKVS
EEEEEECCCCCCCCC
51.7423749302
563PhosphorylationKSGKVTAYDLLSNRV
CCCCEEHHHHHHCCC
9.5828796482
567PhosphorylationVTAYDLLSNRVIKKP
EEHHHHHHCCCCCCC
29.8628796482
620PhosphorylationSEEEKLKYEEKATKD
CHHHHHHHHHHHHHH
39.49-
626MethylationKYEEKATKDLERYNS
HHHHHHHHHHHHHHH
66.24116252439
631 (in isoform 2)Phosphorylation-15.1329083192
634 (in isoform 2)Phosphorylation-37.4729083192
645SulfoxidationAIEQESQMSLKDGRK
HHHHHHHCCHHCCCC
7.6421406390
670PhosphorylationAQKHKLKTSLSNQPK
HHHHCCCHHHCCCCC
45.3928450419
671PhosphorylationQKHKLKTSLSNQPKL
HHHCCCHHHCCCCCH
28.3628450419
673PhosphorylationHKLKTSLSNQPKLDE
HCCCHHHCCCCCHHH
32.9428450419
684PhosphorylationKLDELLQSQIEKRRS
CHHHHHHHHHHHHHH
32.8529523821
688UbiquitinationLLQSQIEKRRSQNIK
HHHHHHHHHHHCCCE
55.5321906983
702PhosphorylationKMVQIPFSMKNLKIN
EEEEECCCCCCCEEC
24.4024719451
721UbiquitinationNKVDLEEKDEPCLIH
CCCCCCCCCCCCEEE
59.00-
802PhosphorylationMTADDQRYSGSTYLS
EECCCCCCCCCCCCC
16.2623663014
803PhosphorylationTADDQRYSGSTYLSD
ECCCCCCCCCCCCCC
28.5823663014
805PhosphorylationDDQRYSGSTYLSDPR
CCCCCCCCCCCCCCC
14.1323663014
806PhosphorylationDQRYSGSTYLSDPRL
CCCCCCCCCCCCCCE
31.8223663014
807PhosphorylationQRYSGSTYLSDPRLT
CCCCCCCCCCCCCEE
13.1023663014
809PhosphorylationYSGSTYLSDPRLTAN
CCCCCCCCCCCEECC
34.8423663014
863AcetylationAILNRNAKEVYECRP
HHHCCCCCHHHHCCC
51.797662953
875PhosphorylationCRPRKVISYLEGEAV
CCCHHHHHHHHHHHH
27.01-
885PhosphorylationEGEAVRLSRQLPMYL
HHHHHHHHHHHCCCC
13.86-
891PhosphorylationLSRQLPMYLSKEDIQ
HHHHHCCCCCHHHHH
13.09-
893PhosphorylationRQLPMYLSKEDIQDI
HHHCCCCCHHHHHHH
19.26-
894AcetylationQLPMYLSKEDIQDII
HHCCCCCHHHHHHHH
57.7320167786
894UbiquitinationQLPMYLSKEDIQDII
HHCCCCCHHHHHHHH
57.732190698
905AcetylationQDIIYRMKHQFGNEI
HHHHHHHHHHHCHHH
25.8420167786
913UbiquitinationHQFGNEIKECVHGRP
HHHCHHHHHHHCCCC
38.59-

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PMS1_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 PMS1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MLH1_HUMANMLH1physical
11292842
BRCA2_HUMANBRCA2physical
17148452
PSD2_HUMANPSD2physical
17148452
UBC_HUMANUBCphysical
17148452
EXO1_HUMANEXO1physical
17148452
MLH1_HUMANMLH1physical
17148452
RFC2_HUMANRFC2physical
17148452
PMS1_HUMANPMS1physical
17148452
RFC4_HUMANRFC4physical
17148452
RFC1_HUMANRFC1physical
17148452
RPAC1_HUMANPOLR1Cphysical
17148452
ATR_HUMANATRphysical
17148452
NONO_HUMANNONOphysical
17148452
PGK1_HUMANPGK1physical
17148452
TOP1_HUMANTOP1physical
17148452
MCM6_HUMANMCM6physical
17148452
SMC3_HUMANSMC3physical
17148452
REV3L_HUMANREV3Lphysical
17148452
IPO5_HUMANIPO5physical
17148452
IPO9_HUMANIPO9physical
17148452
RANB9_HUMANRANBP9physical
17148452
RAGP1_HUMANRANGAP1physical
17148452
MMS19_HUMANMMS19physical
17148452
UBP5_HUMANUSP5physical
17148452
UBP13_HUMANUSP13physical
17148452
UBP2L_HUMANUBAP2Lphysical
17148452
HERC2_HUMANHERC2physical
17148452
CUL3_HUMANCUL3physical
17148452
CUL1_HUMANCUL1physical
17148452
USP9Y_HUMANUSP9Yphysical
17148452
BRE1A_HUMANRNF20physical
17148452
HELB_HUMANHELBphysical
17148452
MOV10_HUMANMOV10physical
17148452
FANCJ_HUMANBRIP1physical
17148452
IMA1_HUMANKPNA2physical
17148452
MTMRD_HUMANSBF2physical
17148452
MTMR5_HUMANSBF1physical
17148452
CCNT1_HUMANCCNT1physical
17148452
CDK9_HUMANCDK9physical
17148452
P3C2A_HUMANPIK3C2Aphysical
17148452
CDC5L_HUMANCDC5Lphysical
17148452
AKAP9_HUMANAKAP9physical
17148452
2AAA_HUMANPPP2R1Aphysical
17148452
UBR5_HUMANUBR5physical
17148452
CYLD_HUMANCYLDphysical
17148452
PRS4_HUMANPSMC1physical
17148452
RN123_HUMANRNF123physical
17148452
MSH2_HUMANMSH2physical
10748159
MSH6_HUMANMSH6physical
10748159
H13_HUMANHIST1H1Dphysical
28514442
PRS6A_HUMANPSMC3physical
28514442
PHAG1_HUMANPAG1physical
28514442
AHNK_HUMANAHNAKphysical
28514442
VAMP3_HUMANVAMP3physical
28514442
RASH_HUMANHRASphysical
28514442
GBG5_HUMANGNG5physical
28514442
PYGB_HUMANPYGBphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PMS1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP