ZN124_HUMAN - dbPTM
ZN124_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN124_HUMAN
UniProt AC Q15973
Protein Name Zinc finger protein 124
Gene Name ZNF124
Organism Homo sapiens (Human).
Sequence Length 351
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MSGHPGSWEMNSVAFEDVAVNFTQEEWALLDPSQKNLYRDVMQETFRNLASIGNKGEDQSIEDQYKNSSRNLRHIISHSGNNPYGCEECGKKPCTCKQCQKTSLSVTRVHRDTVMHTGNGHYGCTICEKVFNIPSSFQIHQRNHTGEKPYECMECGKALGFSRSLNRHKRIHTGEKRYECKQCGKAFSRSSHLRDHERTHTGEKPYECKHCGKAFRYSNCLHYHERTHTGEKPYVCMECGKAFSCLSSLQGHIKAHAGEEPYPCKQCGKAFRYASSLQKHEKTHIAQKPYVCNNCGKGFRCSSSLRDHERTHTGEKPYECQKCGKAFSRASTLWKHKKTHTGEKPYKCKKM
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
2Phosphorylation------MSGHPGSWE
------CCCCCCCCC
45.8923401153
12PhosphorylationPGSWEMNSVAFEDVA
CCCCCCCCCEEEEEE
17.3222210691
23PhosphorylationEDVAVNFTQEEWALL
EEEEEECCHHHHHCC
29.8422210691
33PhosphorylationEWALLDPSQKNLYRD
HHHCCCHHHHHHHHH
54.1522210691
38PhosphorylationDPSQKNLYRDVMQET
CHHHHHHHHHHHHHH
17.73-
55UbiquitinationNLASIGNKGEDQSIE
HHHHCCCCCCCCCHH
59.47-
79PhosphorylationLRHIISHSGNNPYGC
HHHHHHCCCCCCCCC
36.1028555341
102PhosphorylationTCKQCQKTSLSVTRV
CCCCCCCCCCEEEEE
14.7124275569
103PhosphorylationCKQCQKTSLSVTRVH
CCCCCCCCCEEEEEE
26.1929743597
105PhosphorylationQCQKTSLSVTRVHRD
CCCCCCCEEEEEEEC
22.6224702127
107PhosphorylationQKTSLSVTRVHRDTV
CCCCCEEEEEEECCE
24.4929743597
199PhosphorylationHLRDHERTHTGEKPY
HCCCCCCCCCCCCCC
22.3229396449
201PhosphorylationRDHERTHTGEKPYEC
CCCCCCCCCCCCCCC
46.5629496963
217PhosphorylationHCGKAFRYSNCLHYH
CCCCEEECCCCCCEE
9.5928555341
218PhosphorylationCGKAFRYSNCLHYHE
CCCEEECCCCCCEEE
19.4628555341
227PhosphorylationCLHYHERTHTGEKPY
CCCEEECCCCCCCCE
22.32-
229PhosphorylationHYHERTHTGEKPYVC
CEEECCCCCCCCEEE
46.56-
234PhosphorylationTHTGEKPYVCMECGK
CCCCCCCEEEECCCC
19.8318083107
262PhosphorylationAHAGEEPYPCKQCGK
HCCCCCCCCCCHHHH
25.2518083107
288AcetylationEKTHIAQKPYVCNNC
CCCCCCCCCEECCCC
29.3330593567
302PhosphorylationCGKGFRCSSSLRDHE
CCCCCCCCHHHCCCC
20.7828555341
311PhosphorylationSLRDHERTHTGEKPY
HHCCCCCCCCCCCCC
22.32-
313PhosphorylationRDHERTHTGEKPYEC
CCCCCCCCCCCCCCH
46.56-
339PhosphorylationTLWKHKKTHTGEKPY
HHHHCCCCCCCCCCC
29.4928348404
341PhosphorylationWKHKKTHTGEKPYKC
HHCCCCCCCCCCCCC
52.8724719451

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 ZN124_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN124_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 ZN124_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCDB1_HUMANCCNDBP1physical
25416956
TSG10_HUMANTSGA10physical
25416956
KRA42_HUMANKRTAP4-2physical
25416956
SYCE1_HUMANSYCE1physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
FSD2_HUMANFSD2physical
25416956
K1C40_HUMANKRT40physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
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 ZN124_HUMAN

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Related Literatures of Post-Translational Modification

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