ZN335_HUMAN - dbPTM
ZN335_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN335_HUMAN
UniProt AC Q9H4Z2
Protein Name Zinc finger protein 335
Gene Name ZNF335
Organism Homo sapiens (Human).
Sequence Length 1342
Subcellular Localization Nucleus .
Protein Description Component or associated component of some histone methyltransferase complexes may regulate transcription through recruitment of those complexes on gene promoters. Enhances ligand-dependent transcriptional activation by nuclear hormone receptors. Plays an important role in neural progenitor cell proliferation and self-renewal through the regulation of specific genes involved brain development, including REST. Also controls the expression of genes involved in somatic development and regulates, for instance, lymphoblast proliferation..
Protein Sequence MEENEVESSSDAAPGPGRPEEPSESGLGVGTSEAVSADSSDAAAAPGQAEADDSGVGQSSDRGSRSQEEVSESSSSADPLPNSYLPDSSSVSHGPVAGVTGGPPALVHSSALPDPNMLVSDCTASSSDLGSAIDKIIESTIGPDLIQNCITVTSAEDGGAETTRYLILQGPDDGAPMTSPMSSSTLAHSLAAIEALADGPTSTSTCLEAQGGPSSPVQLPPASGAEEPDLQSLEAMMEVVVVQQFKCKMCQYRSSTKATLLRHMRERHFRPVAAAAAAAGKKGRLRKWSTSTKSQEEEGPEEEDDDDIVDAGAIDDLEEDSDYNPAEDEPRGRQLRLQRPTPSTPRPRRRPGRPRKLPRLEISDLPDGVEGEPLVSSQSGQSPPEPQDPEAPSSSGPGHLVAMGKVSRTPVEAGVSQSDAENAAPSCPDEHDTLPRRRGRPSRRFLGKKYRKYYYKSPKPLLRPFLCRICGSRFLSHEDLRFHVNSHEAGDPQLFKCLQCSYRSRRWSSLKEHMFNHVGSKPYKCDECSYTSVYRKDVIRHAAVHSRDRKKRPDPTPKLSSFPCPVCGRVYPMQKRLTQHMKTHSTEKPHMCDKCGKSFKKRYTFKMHLLTHIQAVANRRFKCEFCEFVCEDKKALLNHQLSHVSDKPFKCSFCPYRTFREDFLLSHVAVKHTGAKPFACEYCHFSTRHKKNLRLHVRCRHASSFEEWGRRHPEEPPSRRRPFFSLQQIEELKQQHSAAPGPPPSSPGPPEIPPEATTFQSSEAPSLLCSDTLGGATIIYQQGAEESTAMATQTALDLLLNMSAQRELGGTALQVAVVKSEDVEAGLASPGGQPSPEGATPQVVTLHVAEPGGGAAAESQLGPPDLPQITLAPGPFGGTGYSVITAPPMEEGTSAPGTPYSEEPAGEAAQAVVVSDTLKEAGTHYIMATDGTQLHHIELTADGSISFPSPDALASGAKWPLLQCGGLPRDGPEPPSPAKTHCVGDSQSSASSPPATSKALGLAVPPSPPSAATAASKKFSCKICAEAFPGRAEMESHKRAHAGPGAFKCPDCPFSARQWPEVRAHMAQHSSLRPHQCSQCSFASKNKKDLRRHMLTHTKEKPFACHLCGQRFNRNGHLKFHIQRLHSPDGRKSGTPTARAPTQTPTQTIILNSDDETLATLHTALQSSHGVLGPERLQQALSQEHIIVAQEQTVTNQEEAAYIQEITTADGQTVQHLVTSDNQVQYIISQDGVQHLLPQEYVVVPEGHHIQVQEGQITHIQYEQGAPFLQESQIQYVPVSPGQQLVTQAQLEAAAHSAVTAVADAAMAQAQGLFGTDETVPEHIQQLQHQGIEYDVITLADD
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
252PhosphorylationFKCKMCQYRSSTKAT
EECCCCCCCCCCHHH		13.92-
281AcetylationAAAAAAGKKGRLRKW
HHHHHCCCCCCCCCC		47.5326051181
289PhosphorylationKGRLRKWSTSTKSQE
CCCCCCCCCCCCCCC		18.6027794612
290PhosphorylationGRLRKWSTSTKSQEE
CCCCCCCCCCCCCCC		39.0227794612
291PhosphorylationRLRKWSTSTKSQEEE
CCCCCCCCCCCCCCC		28.4627794612
292PhosphorylationLRKWSTSTKSQEEEG
CCCCCCCCCCCCCCC		34.5027794612
341PhosphorylationQLRLQRPTPSTPRPR
CCCCCCCCCCCCCCC		31.8728555341
343PhosphorylationRLQRPTPSTPRPRRR
CCCCCCCCCCCCCCC		54.2223898821
344PhosphorylationLQRPTPSTPRPRRRP
CCCCCCCCCCCCCCC		25.2323898821
376PhosphorylationVEGEPLVSSQSGQSP
CCCCCCCCCCCCCCC		30.2828348404
377PhosphorylationEGEPLVSSQSGQSPP
CCCCCCCCCCCCCCC		22.3828348404
379PhosphorylationEPLVSSQSGQSPPEP
CCCCCCCCCCCCCCC		40.5228348404
382PhosphorylationVSSQSGQSPPEPQDP
CCCCCCCCCCCCCCC		46.0430576142
407PhosphorylationLVAMGKVSRTPVEAG
EEEEEEECCCCCCCC		33.6426714015
409PhosphorylationAMGKVSRTPVEAGVS
EEEEECCCCCCCCCC		24.9530266825
416PhosphorylationTPVEAGVSQSDAENA
CCCCCCCCHHHHHHC		24.0517525332
418PhosphorylationVEAGVSQSDAENAAP
CCCCCCHHHHHHCCC		31.1430266825
426PhosphorylationDAENAAPSCPDEHDT
HHHHCCCCCCCCCCC		33.2930266825
433PhosphorylationSCPDEHDTLPRRRGR
CCCCCCCCCCCCCCC		40.3426074081
642PhosphorylationALLNHQLSHVSDKPF
HHHHCCCCCCCCCCC		18.4428555341
645PhosphorylationNHQLSHVSDKPFKCS
HCCCCCCCCCCCCCC		34.2025159151
686PhosphorylationACEYCHFSTRHKKNL
CCEECCCCHHHCCCE		10.8125627689
687PhosphorylationCEYCHFSTRHKKNLR
CEECCCCHHHCCCEE		35.5325627689
703PhosphorylationHVRCRHASSFEEWGR
EEEEECCHHHHHHHH		29.4528555341
819SumoylationALQVAVVKSEDVEAG
EEEEEEEEHHHHHHH		41.34-
976PhosphorylationRDGPEPPSPAKTHCV
CCCCCCCCCCCCCCC		48.4830266825
980PhosphorylationEPPSPAKTHCVGDSQ
CCCCCCCCCCCCCCC		23.7126552605
986PhosphorylationKTHCVGDSQSSASSP
CCCCCCCCCCCCCCC		26.4923401153
988PhosphorylationHCVGDSQSSASSPPA
CCCCCCCCCCCCCCC		31.6526657352
989PhosphorylationCVGDSQSSASSPPAT
CCCCCCCCCCCCCCC		25.2428450419
991PhosphorylationGDSQSSASSPPATSK
CCCCCCCCCCCCCHH		45.3823401153
992PhosphorylationDSQSSASSPPATSKA
CCCCCCCCCCCCHHH		34.3223401153
996PhosphorylationSASSPPATSKALGLA
CCCCCCCCHHHCCCC		36.2128450419
997PhosphorylationASSPPATSKALGLAV
CCCCCCCHHHCCCCC		20.3128450419
997O-linked_GlycosylationASSPPATSKALGLAV
CCCCCCCHHHCCCCC		20.3130059200
1007PhosphorylationLGLAVPPSPPSAATA
CCCCCCCCCCCHHHH		43.2925159151
1010PhosphorylationAVPPSPPSAATAASK
CCCCCCCCHHHHHCC		33.6423312004
1013PhosphorylationPSPPSAATAASKKFS
CCCCCHHHHHCCCCC		23.6027050516
1016PhosphorylationPSAATAASKKFSCKI
CCHHHHHCCCCCCCC		33.6423312004
1022SumoylationASKKFSCKICAEAFP
HCCCCCCCCCHHHCC		39.3528112733
1038UbiquitinationRAEMESHKRAHAGPG
HHHHHHHCCCCCCCC		61.63-
1098PhosphorylationRRHMLTHTKEKPFAC
HHHHHHCCCCCCCEE		35.3529214152
1127PhosphorylationFHIQRLHSPDGRKSG
EEEEECCCCCCCCCC		29.3130576142
1133PhosphorylationHSPDGRKSGTPTARA
CCCCCCCCCCCCCCC		46.6826074081
1135PhosphorylationPDGRKSGTPTARAPT
CCCCCCCCCCCCCCC		25.2626074081
1137PhosphorylationGRKSGTPTARAPTQT
CCCCCCCCCCCCCCC		28.7226074081
1142PhosphorylationTPTARAPTQTPTQTI
CCCCCCCCCCCCEEE		44.0528450419
1144PhosphorylationTARAPTQTPTQTIIL
CCCCCCCCCCEEEEE		30.6828450419
1146PhosphorylationRAPTQTPTQTIILNS
CCCCCCCCEEEEECC		41.5528450419
1148PhosphorylationPTQTPTQTIILNSDD
CCCCCCEEEEECCCC		16.6828464451
1153PhosphorylationTQTIILNSDDETLAT
CEEEEECCCCHHHHH		42.8922115753
1157PhosphorylationILNSDDETLATLHTA
EECCCCHHHHHHHHH		28.7828450419
1160PhosphorylationSDDETLATLHTALQS
CCCHHHHHHHHHHHH		23.3728464451
1163PhosphorylationETLATLHTALQSSHG
HHHHHHHHHHHHCCC		31.9828450419
1167PhosphorylationTLHTALQSSHGVLGP
HHHHHHHHCCCCCCH		25.7525002506
1168PhosphorylationLHTALQSSHGVLGPE
HHHHHHHCCCCCCHH		15.9925002506
1280PhosphorylationQIQYVPVSPGQQLVT
CCEEEECCCCHHHEH		19.7626074081
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 ZN335_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN335_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 ZN335_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HCFC1_HUMANHCFC1physical
19131338
CCAR2_HUMANCCAR2physical
19131338
EMSY_HUMANC11orf30physical
19131338
RBBP5_HUMANRBBP5physical
19131338
ASH2L_HUMANASH2Lphysical
19131338
WDR5_HUMANWDR5physical
19131338
CNOT9_RATRqcd1physical
18180299
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615095Microcephaly 10, primary, autosomal recessive (MCPH10)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN335_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-976, AND MASSSPECTROMETRY.
"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-1153, AND MASSSPECTROMETRY.
"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-416, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-976, AND MASSSPECTROMETRY.

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