ZN428_HUMAN - dbPTM
ZN428_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN428_HUMAN
UniProt AC Q96B54
Protein Name Zinc finger protein 428
Gene Name ZNF428
Organism Homo sapiens (Human).
Sequence Length 188
Subcellular Localization
Protein Description
Protein Sequence MTETREPAETGGYASLEEDDEDLSPGPEHSSDSEYTLSEPDSEEEEDEEEEEEETTDDPEYDPGYKVKQRLGGGRGGPSRRAPRAAQPPAQPCQLCGRSPLGEAPPGTPPCRLCCPATAPQEAPAPEGRALGEEEEEPPRAGEGRPAGREEEEEEEEEGTYHCTECEDSFDNLGELHGHFMLHARGEV
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
75MethylationKQRLGGGRGGPSRRA
CCCCCCCCCCCCCCC
50.6116187591
99PhosphorylationPCQLCGRSPLGEAPP
CCCCCCCCCCCCCCC
15.1229255136
108PhosphorylationLGEAPPGTPPCRLCC
CCCCCCCCCCCCEEC
29.8129255136
118PhosphorylationCRLCCPATAPQEAPA
CCEECCCCCCCCCCC
24.8226552605
160PhosphorylationEEEEEEGTYHCTECE
HHHHHHCCEEECCCC
17.2422210691
161PhosphorylationEEEEEGTYHCTECED
HHHHHCCEEECCCCC
13.0222210691

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 ZN428_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN428_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 ZN428_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHAP1_HUMANCHAMP1physical
28514442
POGZ_HUMANPOGZphysical
28514442
FOXK2_HUMANFOXK2physical
28514442
FOXK1_HUMANFOXK1physical
28514442
PI42C_HUMANPIP4K2Cphysical
28514442
PARP2_HUMANPARP2physical
28514442
PI42B_HUMANPIP4K2Bphysical
28514442
H2AY_HUMANH2AFYphysical
28514442
GTF2I_HUMANGTF2Iphysical
28514442
XPC_HUMANXPCphysical
28514442
H2A2B_HUMANHIST2H2ABphysical
28514442
PI42A_HUMANPIP4K2Aphysical
28514442
ACTBL_HUMANACTBL2physical
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 ZN428_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND THR-108, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108, AND MASSSPECTROMETRY.

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