ZN444_HUMAN - dbPTM
ZN444_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN444_HUMAN
UniProt AC Q8N0Y2
Protein Name Zinc finger protein 444
Gene Name ZNF444
Organism Homo sapiens (Human).
Sequence Length 327
Subcellular Localization Nucleus .
Protein Description Transcriptional regulator. Binds to the 5'-flanking critical region of the SCARF1 promoter..
Protein Sequence MEVAVPVKQEAEGLALDSPWHRFRRFHLGDAPGPREALGLLRALCRDWLRPEVHTKEQMLELLVLEQFLSALPADTQAWVCSRQPQSGEEAVALLEELWGPAASPDGSSATRVPQDVTQGPGATGGKEDSGMIPLAGTAPGAEGPAPGDSQAVRPYKQEPSSPPLAPGLPAFLAAPGTTSCPECGKTSLKPAHLLRHRQSHSGEKPHACPECGKAFRRKEHLRRHRDTHPGSPGSPGPALRPLPAREKPHACCECGKTFYWREHLVRHRKTHSGARPFACWECGKGFGRREHVLRHQRIHGRAAASAQGAVAPGPDGGGPFPPWPLG
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
1Acetylation-------MEVAVPVK
-------CCCCCCCC		9.3720068231
8SumoylationMEVAVPVKQEAEGLA
CCCCCCCCCCCCCCC		36.03-
8UbiquitinationMEVAVPVKQEAEGLA
CCCCCCCCCCCCCCC		36.03-
8SumoylationMEVAVPVKQEAEGLA
CCCCCCCCCCCCCCC		36.0328112733
18PhosphorylationAEGLALDSPWHRFRR
CCCCCCCCHHHHHHH		30.6428348404
104PhosphorylationELWGPAASPDGSSAT
HHHCCCCCCCCCCCC		26.1527251275
130 (in isoform 2)Phosphorylation-31.2125072903
137 (in isoform 2)Phosphorylation-30.0525072903
149 (in isoform 2)Phosphorylation-36.2025072903
155 (in isoform 2)Phosphorylation-33.7925072903
161PhosphorylationRPYKQEPSSPPLAPG
CCCCCCCCCCCCCCC		55.5126657352
162PhosphorylationPYKQEPSSPPLAPGL
CCCCCCCCCCCCCCC		41.0530278072
178PhosphorylationAFLAAPGTTSCPECG
EEECCCCCCCCCCCC		17.9328111955
179PhosphorylationFLAAPGTTSCPECGK
EECCCCCCCCCCCCC		33.9628111955
180PhosphorylationLAAPGTTSCPECGKT
ECCCCCCCCCCCCCC		27.7528111955
190SumoylationECGKTSLKPAHLLRH
CCCCCCCCHHHHHHH		39.6728112733
200PhosphorylationHLLRHRQSHSGEKPH
HHHHHHHCCCCCCCC		21.4120068231
202PhosphorylationLRHRQSHSGEKPHAC
HHHHHCCCCCCCCCC		54.6220068231
228PhosphorylationHLRRHRDTHPGSPGS
HHHHCCCCCCCCCCC		29.9030266825
232PhosphorylationHRDTHPGSPGSPGPA
CCCCCCCCCCCCCCC		30.4523401153
235PhosphorylationTHPGSPGSPGPALRP
CCCCCCCCCCCCCCC		30.0229255136
273PhosphorylationVRHRKTHSGARPFAC
HHCCCCCCCCCCEEE		39.1025159151
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 ZN444_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN444_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 ZN444_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCDC6_HUMANCCDC6physical
26186194
STRN4_HUMANSTRN4physical
26186194
KLH15_HUMANKLHL15physical
26186194
TGO1_HUMANMIA3physical
26186194
RBM22_HUMANRBM22physical
26186194
YBEY_HUMANYBEYphysical
26186194
STRN3_HUMANSTRN3physical
26186194
ZKSC8_HUMANZKSCAN8physical
26186194
ZN174_HUMANZNF174physical
26186194
ZN446_HUMANZNF446physical
26186194
SCND1_HUMANSCAND1physical
26186194
ZKSC3_HUMANZKSCAN3physical
26186194
ZKSC4_HUMANZKSCAN4physical
26186194
SAHH3_HUMANAHCYL2physical
26186194
SAHH2_HUMANAHCYL1physical
26186194
ZSC30_HUMANZSCAN30physical
26186194
SCND3_HUMANZBED9physical
26186194
ZN579_HUMANZNF579physical
26186194
CCDC6_HUMANCCDC6physical
28514442
ZNF24_HUMANZNF24physical
28514442
SCND1_HUMANSCAND1physical
28514442
ZSC30_HUMANZSCAN30physical
28514442
ZKSC3_HUMANZKSCAN3physical
28514442
ZKSC4_HUMANZKSCAN4physical
28514442
ZN174_HUMANZNF174physical
28514442
SCND3_HUMANZBED9physical
28514442
ZN446_HUMANZNF446physical
28514442
ZKSC8_HUMANZKSCAN8physical
28514442
CUL3_HUMANCUL3physical
28514442
SAHH3_HUMANAHCYL2physical
28514442
RBM22_HUMANRBM22physical
28514442
SAHH2_HUMANAHCYL1physical
28514442
STRN4_HUMANSTRN4physical
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 ZN444_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-232 AND SER-235, ANDMASS SPECTROMETRY.

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