ZN543_HUMAN - dbPTM
ZN543_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN543_HUMAN
UniProt AC Q08ER8
Protein Name Zinc finger protein 543
Gene Name ZNF543
Organism Homo sapiens (Human).
Sequence Length 600
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MAASAQVSVTFEDVAVTFTQEEWGQLDAAQRTLYQEVMLETCGLLMSLGCPLFKPELIYQLDHRQELWMATKDLSQSSYPGDNTKPKTTEPTFSHLALPEEVLLQEQLTQGASKNSQLGQSKDQDGPSEMQEVHLKIGIGPQRGKLLEKMSSERDGLGSDDGVCTKITQKQVSTEGDLYECDSHGPVTDALIREEKNSYKCEECGKVFKKNALLVQHERIHTQVKPYECTECGKTFSKSTHLLQHLIIHTGEKPYKCMECGKAFNRRSHLTRHQRIHSGEKPYKCSECGKAFTHRSTFVLHHRSHTGEKPFVCKECGKAFRDRPGFIRHYIIHTGEKPYECIECGKAFNRRSYLTWHQQIHTGVKPFECNECGKAFCESADLIQHYIIHTGEKPYKCMECGKAFNRRSHLKQHQRIHTGEKPYECSECGKAFTHCSTFVLHKRTHTGEKPYECKECGKAFSDRADLIRHFSIHTGEKPYECVECGKAFNRSSHLTRHQQIHTGEKPYECIQCGKAFCRSANLIRHSIIHTGEKPYECSECGKAFNRGSSLTHHQRIHTGRNPTIVTDVGRPFMTAQTSVNIQELLLGKEFLNITTEENLW
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
72UbiquitinationQELWMATKDLSQSSY
HHHHHHCCCCHHCCC
47.32-
77PhosphorylationATKDLSQSSYPGDNT
HCCCCHHCCCCCCCC
28.59-
85UbiquitinationSYPGDNTKPKTTEPT
CCCCCCCCCCCCCCC
51.2622505724
122UbiquitinationNSQLGQSKDQDGPSE
CCCCCCCCCCCCCHH
52.07-
165PhosphorylationGSDDGVCTKITQKQV
CCCCCCCHHEEECCC
24.07-
166UbiquitinationSDDGVCTKITQKQVS
CCCCCCHHEEECCCC
38.3329967540
168PhosphorylationDGVCTKITQKQVSTE
CCCCHHEEECCCCCC
31.13-
170UbiquitinationVCTKITQKQVSTEGD
CCHHEEECCCCCCCC
43.9829967540
200SumoylationREEKNSYKCEECGKV
HHHHHCCCHHHHHHE
34.68-
200SumoylationREEKNSYKCEECGKV
HHHHHCCCHHHHHHE
34.68-
210UbiquitinationECGKVFKKNALLVQH
HHHHEEHHCEEEEEC
35.6729967540
210SumoylationECGKVFKKNALLVQH
HHHHEEHHCEEEEEC
35.67-
210SumoylationECGKVFKKNALLVQH
HHHHEEHHCEEEEEC
35.67-
225UbiquitinationERIHTQVKPYECTEC
CCCCCCCCCEECCCC
31.87-
234UbiquitinationYECTECGKTFSKSTH
EECCCCCCCCCHHHH
59.04-
250PhosphorylationLQHLIIHTGEKPYKC
HHHHHHHCCCCCEEE
36.3129496963
253UbiquitinationLIIHTGEKPYKCMEC
HHHHCCCCCEEEHHC
55.80-
278PhosphorylationTRHQRIHSGEKPYKC
CCCCHHCCCCCCEEC
46.4029496963
283PhosphorylationIHSGEKPYKCSECGK
HCCCCCCEECCCCCC
35.3822817900
286PhosphorylationGEKPYKCSECGKAFT
CCCCEECCCCCCEEE
31.59-
290AcetylationYKCSECGKAFTHRST
EECCCCCCEEECCCE
52.577665163
293PhosphorylationSECGKAFTHRSTFVL
CCCCCEEECCCEEEE
22.6522817900
306PhosphorylationVLHHRSHTGEKPFVC
EEECCCCCCCCCEEE
48.56-
309UbiquitinationHRSHTGEKPFVCKEC
CCCCCCCCCEEECCC
45.13-
309SumoylationHRSHTGEKPFVCKEC
CCCCCCCCCEEECCC
45.13-
309SumoylationHRSHTGEKPFVCKEC
CCCCCCCCCEEECCC
45.13-
314UbiquitinationGEKPFVCKECGKAFR
CCCCEEECCCHHHHH
51.22-
334PhosphorylationIRHYIIHTGEKPYEC
EEEEEEECCCCCEEE
36.3127251275
337UbiquitinationYIIHTGEKPYECIEC
EEEECCCCCEEEEEC
55.00-
365UbiquitinationQQIHTGVKPFECNEC
HHCCCCCCCEECCCH
45.38-
390PhosphorylationIQHYIIHTGEKPYKC
HHHHHCCCCCCCEEE
36.3129496963
393UbiquitinationYIIHTGEKPYKCMEC
HHCCCCCCCEEEHHH
55.80-
408PhosphorylationGKAFNRRSHLKQHQR
HHHHCCHHHHHHHCC
29.9028258704
418PhosphorylationKQHQRIHTGEKPYEC
HHHCCCCCCCCCEEC
44.6729496963
423PhosphorylationIHTGEKPYECSECGK
CCCCCCCEECCCCHH
40.41-
426PhosphorylationGEKPYECSECGKAFT
CCCCEECCCCHHHHH
24.7928258704
444PhosphorylationTFVLHKRTHTGEKPY
EEEEECCCCCCCCCC
28.7029396449
446PhosphorylationVLHKRTHTGEKPYEC
EEECCCCCCCCCCCC
46.5629496963
449UbiquitinationKRTHTGEKPYECKEC
CCCCCCCCCCCCCHH
55.00-
454UbiquitinationGEKPYECKECGKAFS
CCCCCCCCHHHHHHH
44.06-
454SumoylationGEKPYECKECGKAFS
CCCCCCCCHHHHHHH
44.06-
454SumoylationGEKPYECKECGKAFS
CCCCCCCCHHHHHHH
44.06-
471PhosphorylationADLIRHFSIHTGEKP
HHHHHHHCCCCCCCC
13.8228555341
474PhosphorylationIRHFSIHTGEKPYEC
HHHHCCCCCCCCEEE
45.4228152594
477UbiquitinationFSIHTGEKPYECVEC
HCCCCCCCCEEEEEC
55.0022505724
479PhosphorylationIHTGEKPYECVECGK
CCCCCCCEEEEECCC
32.7828152594
486SumoylationYECVECGKAFNRSSH
EEEEECCCCCCCCCC
62.56-
486SumoylationYECVECGKAFNRSSH
EEEEECCCCCCCCCC
62.56-
486UbiquitinationYECVECGKAFNRSSH
EEEEECCCCCCCCCC
62.56-
502PhosphorylationTRHQQIHTGEKPYEC
HHCCCCCCCCCCCHH
48.9829214152
505UbiquitinationQQIHTGEKPYECIQC
CCCCCCCCCCHHHHC
55.00-
514UbiquitinationYECIQCGKAFCRSAN
CHHHHCCHHHHHHHC
46.01-
530PhosphorylationIRHSIIHTGEKPYEC
HHCCCEECCCCCEEC
36.3129496963
533UbiquitinationSIIHTGEKPYECSEC
CCEECCCCCEECCHH
55.00-
535PhosphorylationIHTGEKPYECSECGK
EECCCCCEECCHHHC
40.41-
538PhosphorylationGEKPYECSECGKAFN
CCCCEECCHHHCCCC
24.7927251275
542SumoylationYECSECGKAFNRGSS
EECCHHHCCCCCCCC
62.56-
542SumoylationYECSECGKAFNRGSS
EECCHHHCCCCCCCC
62.56-
542UbiquitinationYECSECGKAFNRGSS
EECCHHHCCCCCCCC
62.5622505724
549PhosphorylationKAFNRGSSLTHHQRI
CCCCCCCCCCCCCHH
39.8630257219
563PhosphorylationIHTGRNPTIVTDVGR
HCCCCCCEEEECCCC
31.46-
574PhosphorylationDVGRPFMTAQTSVNI
CCCCCCCCCCCCCCH
18.92-
578PhosphorylationPFMTAQTSVNIQELL
CCCCCCCCCCHHHHH
10.90-

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 ZN543_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN543_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 ZN543_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR107_HUMANKRTAP10-7physical
25416956

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 ZN543_HUMAN

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Related Literatures of Post-Translational Modification

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