ZN568_HUMAN - dbPTM
ZN568_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN568_HUMAN
UniProt AC Q3ZCX4
Protein Name Zinc finger protein 568
Gene Name ZNF568
Organism Homo sapiens (Human).
Sequence Length 644
Subcellular Localization Nucleus .
Protein Description Has transcriptional repression activity, partially through the recruitment of the corepressor TRIM28 but has also repression activity independently of this interaction. Essential during embryonic development, where it acts as direct repressor of a placental-specific transcript of IGF2 in early development and regulates convergent extension movements required for axis elongation and tissue morphogenesis in all germ layers. Also important for normal morphogenesis of extraembryonic tissues including the yolk sac, extraembryonic mesoderm and placenta. May enhance proliferation or maintenance of neural stem cells..
Protein Sequence MTSQSSVISNSCVTMERLSHMMERKAWCSQESALSEEEEDTTRPLETVTFKDVAVDLTQEEWEQMKPAQRNLYRDVMLENYSNLVTVGCQVTKPDVIFKLEQEEEPWVMEEEMFGRHCPEVWEVDEQIKKQQETLVRKVTSISKKILIKEKVIECKKVAKIFPLSSDIVTSRQSFYDCDSLDKGLEHNLDLLRYEKGCVREKQSNEFGKPFYHCASYVVTPFKCNQCGQDFSHKFDLIRHERIHAGEKPYECKECGKAFSRKENLITHQKIHTGEKPYKCNECGKAFIQMSNLIRHHRIHTGEKPYACKDCWKAFSQKSNLIEHERIHTGEKPYECKECGKSFSQKQNLIEHEKIHTGEKPYACNECGRAFSRMSSVTLHMRSHTGEKPYKCNKCGKAFSQCSVFIIHMRSHTGEKPYVCSECGKAFSQSSSLTVHMRNHTAEKPYECKECGKAFSRKENLITHQKIHTGEKPYECSECGKAFIQMSNLIRHQRIHTGEKPYACTVCGKAFSQKSNLTEHEKIHTGEKPYHCNQCGKAFSQRQNLLEHEKIHTGEKPFKCNECGKAFSRISSLTLHVRSHTGEKPYECNKCGKAFSQCSLLIIHMRSHTGEKPFECNECGKAFSQRASLSIHKRGHTGERHQVY
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------MTSQSSVIS
------CCCCHHHHH		35.1624043423
3Phosphorylation-----MTSQSSVISN
-----CCCCHHHHHH		27.1124043423
5Phosphorylation---MTSQSSVISNSC
---CCCCHHHHHHHH		26.7524043423
6Phosphorylation--MTSQSSVISNSCV
--CCCCHHHHHHHHH		18.8124043423
9PhosphorylationTSQSSVISNSCVTME
CCCHHHHHHHHHHHH		22.1224043423
11PhosphorylationQSSVISNSCVTMERL
CHHHHHHHHHHHHHH		11.8124043423
14PhosphorylationVISNSCVTMERLSHM
HHHHHHHHHHHHHHH		20.0324043423
19PhosphorylationCVTMERLSHMMERKA
HHHHHHHHHHHHHHH		18.6324043423
35PhosphorylationCSQESALSEEEEDTT
HCCHHHCCCCCCCCC		42.5524719451
74 (in isoform 3)Ubiquitination-32.96-
76 (in isoform 3)Ubiquitination-3.31-
81PhosphorylationRDVMLENYSNLVTVG
HHHHHHCCCCCEEEE		6.9125072903
82PhosphorylationDVMLENYSNLVTVGC
HHHHHCCCCCEEEEC		34.9625072903
86PhosphorylationENYSNLVTVGCQVTK
HCCCCCEEEECEECC		17.8525072903
92PhosphorylationVTVGCQVTKPDVIFK
EEEECEECCCCEEEE		15.8125072903
130AcetylationEVDEQIKKQQETLVR
HHHHHHHHHHHHHHH		59.8620167786
143PhosphorylationVRKVTSISKKILIKE
HHHHHHHCHHHHHCC		27.8822468782
156 (in isoform 3)Phosphorylation-37.1825921289
170PhosphorylationPLSSDIVTSRQSFYD
CCCCCCCCCCCCCCC		20.6522210691
253SumoylationGEKPYECKECGKAFS
CCCCCCCCHHHCCCC		44.06-
253SumoylationGEKPYECKECGKAFS
CCCCCCCCHHHCCCC		44.06-
270UbiquitinationENLITHQKIHTGEKP
HCCCCCCCCCCCCCC		28.93-
273 (in isoform 3)Phosphorylation-50.97-
273PhosphorylationITHQKIHTGEKPYKC
CCCCCCCCCCCCCCC		50.9729496963
278PhosphorylationIHTGEKPYKCNECGK
CCCCCCCCCCCHHHH		38.9618767875
279SumoylationHTGEKPYKCNECGKA
CCCCCCCCCCHHHHH		38.83-
279SumoylationHTGEKPYKCNECGKA
CCCCCCCCCCHHHHH		38.83-
301PhosphorylationIRHHRIHTGEKPYAC
HHHCCCCCCCCCCCC		44.6728111955
314 (in isoform 3)Phosphorylation-5.71-
329PhosphorylationIEHERIHTGEKPYEC
CCCCCCCCCCCCCCC		44.6729496963
337SumoylationGEKPYECKECGKSFS
CCCCCCCCCCCCCCC		44.06-
337SumoylationGEKPYECKECGKSFS
CCCCCCCCCCCCCCC		44.06-
357PhosphorylationIEHEKIHTGEKPYAC
HHHCCCCCCCCCCCC		50.97-
378PhosphorylationFSRMSSVTLHMRSHT
HHHHCCEEEEECCCC		16.9422210691
385PhosphorylationTLHMRSHTGEKPYKC
EEEECCCCCCCCEEC		48.5624719451
430PhosphorylationCGKAFSQSSSLTVHM
CCCCCCCCCCCEEEC		22.2422210691
434PhosphorylationFSQSSSLTVHMRNHT
CCCCCCCEEECCCCC		15.4322210691
449SumoylationAEKPYECKECGKAFS
CCCCEECCCCCCCCC		44.06-
449SumoylationAEKPYECKECGKAFS
CCCCEECCCCCCCCC		44.06-
466UbiquitinationENLITHQKIHTGEKP
HCCCCCCCEECCCCC		28.93-
469PhosphorylationITHQKIHTGEKPYEC
CCCCCEECCCCCCCC		50.9718452278
474PhosphorylationIHTGEKPYECSECGK
EECCCCCCCCCHHHH		40.4129978859
477PhosphorylationGEKPYECSECGKAFI
CCCCCCCCHHHHHHH		24.7929978859
497PhosphorylationIRHQRIHTGEKPYAC
HHHCCCCCCCCCEEE		44.6728111955
525PhosphorylationTEHEKIHTGEKPYHC
CCCCCCCCCCCCCCC		50.97-
553PhosphorylationLEHEKIHTGEKPFKC
HHHCCCCCCCCCEEC		50.9718669648
596PhosphorylationNKCGKAFSQCSLLII
CCCCHHHHHCCEEEE		34.83-
599PhosphorylationGKAFSQCSLLIIHMR
CHHHHHCCEEEEECC		20.69-
612UbiquitinationMRSHTGEKPFECNEC
CCCCCCCCCEECCCC		57.25-
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 ZN568_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN568_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 ZN568_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN568_HUMAN !!
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 ZN568_HUMAN

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Related Literatures of Post-Translational Modification

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