ZNF8_HUMAN - dbPTM
ZNF8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNF8_HUMAN
UniProt AC P17098
Protein Name Zinc finger protein 8
Gene Name ZNF8
Organism Homo sapiens (Human).
Sequence Length 575
Subcellular Localization Nucleus .
Protein Description Transcriptional repressor. May modulate BMP and TGF-beta signal transduction, through its interaction with SMAD proteins..
Protein Sequence MDPEDEGVAGVMSVGPPAARLQEPVTFRDVAVDFTQEEWGQLDPTQRILYRDVMLETFGHLLSIGPELPKPEVISQLEQGTELWVAERGTTQGCHPAWEPRSESQASRKEEGLPEEEPSHVTGREGFPTDAPYPTTLGKDRECQSQSLALKEQNNLKQLEFGLKEAPVQDQGYKTLRLRENCVLSSSPNPFPEISRGEYLYTYDSQITDSEHNSSLVSQQTGSPGKQPGENSDCHRDSSQAIPITELTKSQVQDKPYKCTDCGKSFNHNAHLTVHKRIHTGERPYMCKECGKAFSQNSSLVQHERIHTGDKPYKCAECGKSFCHSTHLTVHRRIHTGEKPYECQDCGRAFNQNSSLGRHKRTHTGEKPYTCSVCGKSFSRTTCLFLHLRTHTEERPYECNHCGKGFRHSSSLAQHQRKHAGEKPFECRQRLIFEQTPALTKHEWTEALGCDPPLSQDERTHRSDRPFKCNQCGKCFIQSSHLIRHQITHTREEQPHGRSRRREQSSSRNSHLVQHQHPNSRKSSAGGAKAGQPESRALALFDIQKIMQEKNPVHVIGVEEPSVGASMLFDIREST
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
107PhosphorylationPRSESQASRKEEGLP
CCCHHHHHHHHCCCC		35.9328555341
135PhosphorylationPTDAPYPTTLGKDRE
CCCCCCCCCCCCCHH		28.8928555341
157UbiquitinationLKEQNNLKQLEFGLK
HHHHHCHHHHHHCCC		55.77-
164UbiquitinationKQLEFGLKEAPVQDQ
HHHHHCCCCCCCCCC		52.81-
174SumoylationPVQDQGYKTLRLREN
CCCCCCCCEEEEECC		48.1628112733
174AcetylationPVQDQGYKTLRLREN
CCCCCCCCEEEEECC		48.1625953088
174UbiquitinationPVQDQGYKTLRLREN
CCCCCCCCEEEEECC		48.16-
175PhosphorylationVQDQGYKTLRLRENC
CCCCCCCEEEEECCE		14.50-
185PhosphorylationLRENCVLSSSPNPFP
EECCEEECCCCCCCC		14.3628450419
186PhosphorylationRENCVLSSSPNPFPE
ECCEEECCCCCCCCC		45.7323401153
187PhosphorylationENCVLSSSPNPFPEI
CCEEECCCCCCCCCC		25.8923401153
195PhosphorylationPNPFPEISRGEYLYT
CCCCCCCCCCCEEEE		32.3527251275
199PhosphorylationPEISRGEYLYTYDSQ
CCCCCCCEEEEECCC		14.0827080861
201PhosphorylationISRGEYLYTYDSQIT
CCCCCEEEEECCCCC		11.4427080861
202PhosphorylationSRGEYLYTYDSQITD
CCCCEEEEECCCCCC		20.4627080861
203PhosphorylationRGEYLYTYDSQITDS
CCCEEEEECCCCCCC		10.4727080861
205PhosphorylationEYLYTYDSQITDSEH
CEEEEECCCCCCCCC		17.0525002506
208PhosphorylationYTYDSQITDSEHNSS
EEECCCCCCCCCCCC		26.3227080861
210PhosphorylationYDSQITDSEHNSSLV
ECCCCCCCCCCCCCH		31.9127080861
214PhosphorylationITDSEHNSSLVSQQT
CCCCCCCCCCHHCCC		27.2727080861
215PhosphorylationTDSEHNSSLVSQQTG
CCCCCCCCCHHCCCC		37.8027080861
218PhosphorylationEHNSSLVSQQTGSPG
CCCCCCHHCCCCCCC		23.1226074081
221PhosphorylationSSLVSQQTGSPGKQP
CCCHHCCCCCCCCCC		31.8026074081
223PhosphorylationLVSQQTGSPGKQPGE
CHHCCCCCCCCCCCC		33.5930576142
249SumoylationIPITELTKSQVQDKP
CCHHHCCHHHHCCCC		52.0628112733
273PhosphorylationFNHNAHLTVHKRIHT
CCCCCEEEEECCCCC		15.6528555341
280PhosphorylationTVHKRIHTGERPYMC
EEECCCCCCCCCEEH		38.0624719451
295PhosphorylationKECGKAFSQNSSLVQ
HHHHHHHHCCCCCCC		33.0628555341
299PhosphorylationKAFSQNSSLVQHERI
HHHHCCCCCCCCCCC		39.8628555341
308PhosphorylationVQHERIHTGDKPYKC
CCCCCCCCCCCCEEE		44.7124719451
313PhosphorylationIHTGDKPYKCAECGK
CCCCCCCEEECCCCC		25.1722964224
325PhosphorylationCGKSFCHSTHLTVHR
CCCCCCCCCCCEEEC		20.7828555341
336PhosphorylationTVHRRIHTGEKPYEC
EEECCCCCCCCCCCC		44.6728122231
341PhosphorylationIHTGEKPYECQDCGR
CCCCCCCCCCCCHHH		40.1728122231
354PhosphorylationGRAFNQNSSLGRHKR
HHHCCCCCCCCCCCC		19.7125159151
355PhosphorylationRAFNQNSSLGRHKRT
HHCCCCCCCCCCCCC		42.2525159151
362PhosphorylationSLGRHKRTHTGEKPY
CCCCCCCCCCCCCCE		28.70-
364PhosphorylationGRHKRTHTGEKPYTC
CCCCCCCCCCCCEEE		46.5621712546
369PhosphorylationTHTGEKPYTCSVCGK
CCCCCCCEEEEECCC		31.29-
379PhosphorylationSVCGKSFSRTTCLFL
EECCCCCCCEEEEEE		35.4917081983
392PhosphorylationFLHLRTHTEERPYEC
EEECCCCCCCCCCCC		38.64-
409PhosphorylationCGKGFRHSSSLAQHQ
CCCCCCCHHHHHHHH		19.8428555341
423UbiquitinationQRKHAGEKPFECRQR
HHHHCCCCCCHHHHH		54.83-
436PhosphorylationQRLIFEQTPALTKHE
HHHHHCCCCCCCHHH		11.8828555341
441SumoylationEQTPALTKHEWTEAL
CCCCCCCHHHHHHHH		40.1428112733
455PhosphorylationLGCDPPLSQDERTHR
HCCCCCCCCCCCCCC		41.1617525332
488PhosphorylationHLIRHQITHTREEQP
HHHHEECCCCCCCCC		15.6029449344
490PhosphorylationIRHQITHTREEQPHG
HHEECCCCCCCCCCC		31.0029449344
505PhosphorylationRSRRREQSSSRNSHL
CCCCCHHHHHCCCHH		26.0629396449
506PhosphorylationSRRREQSSSRNSHLV
CCCCHHHHHCCCHHH		32.7729396449
507PhosphorylationRRREQSSSRNSHLVQ
CCCHHHHHCCCHHHC		40.5029396449
510PhosphorylationEQSSSRNSHLVQHQH
HHHHHCCCHHHCCCC		19.6529396449
520PhosphorylationVQHQHPNSRKSSAGG
HCCCCCCCCCCCCCC		45.6029396449
522MethylationHQHPNSRKSSAGGAK
CCCCCCCCCCCCCCC		48.89116252149
545SumoylationLALFDIQKIMQEKNP
HHHHHHHHHHHHCCC		40.2428112733
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 ZNF8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNF8_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 ZNF8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZNF8_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 ZNF8_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND MASSSPECTROMETRY.

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