ZN264_HUMAN - dbPTM
ZN264_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN264_HUMAN
UniProt AC O43296
Protein Name Zinc finger protein 264
Gene Name ZNF264
Organism Homo sapiens (Human).
Sequence Length 627
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MAAAVLTDRAQVSVTFDDVAVTFTKEEWGQLDLAQRTLYQEVMLENCGLLVSLGCPVPKAELICHLEHGQEPWTRKEDLSQDTCPGDKGKPKTTEPTTCEPALSEGISLQGQVTQGNSVDSQLGQAEDQDGLSEMQEGHFRPGIDPQEKSPGKMSPECDGLGTADGVCSRIGQEQVSPGDRVRSHNSCESGKDPMIQEEENNFKCSECGKVFNKKHLLAGHEKIHSGVKPYECTECGKTFIKSTHLLQHHMIHTGERPYECMECGKAFNRKSYLTQHQRIHSGEKPYKCNECGKAFTHRSNFVLHNRRHTGEKSFVCTECGQVFRHRPGFLRHYVVHSGENPYECLECGKVFKHRSYLMWHQQTHTGEKPYECSECGKVFLESAALIHHYVIHTGEKPFECLECGKAFNHRSYLKRHQRIHTGEKPFVCSECGKAFTHCSTFILHKRAHTGEKPFECKECGKAFSNRKDLIRHFSIHTGEKPYECVECGKAFTRMSGLTRHKRIHSGEKPYECVECGKSFCWSTNLIRHAIIHTGEKPYKCSECGKAFSRSSSLTQHQRMHTGKNPISVTDVGRPFTSGQTSVTLRELLLGKDFLNVTTEANILPEETSSSASDQPYQRETPQVSSL
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
80PhosphorylationWTRKEDLSQDTCPGD
CCCCHHHCCCCCCCC		38.0317525332
83PhosphorylationKEDLSQDTCPGDKGK
CHHHCCCCCCCCCCC		16.9828111955
150PhosphorylationGIDPQEKSPGKMSPE
CCCCCCCCCCCCCCC		37.8325159151
155PhosphorylationEKSPGKMSPECDGLG
CCCCCCCCCCCCCCC		22.4923401153
163PhosphorylationPECDGLGTADGVCSR
CCCCCCCCCCCHHHH		26.9830108239
169PhosphorylationGTADGVCSRIGQEQV
CCCCCHHHHCCCCCC		25.24-
177PhosphorylationRIGQEQVSPGDRVRS
HCCCCCCCCCCCCCC		23.9019664994
215AcetylationCGKVFNKKHLLAGHE
HHHHHCCHHHHCCCC		40.367429195
223AcetylationHLLAGHEKIHSGVKP
HHHCCCCHHCCCCCC		39.797429203
223UbiquitinationHLLAGHEKIHSGVKP
HHHCCCCHHCCCCCC		39.7929967540
226PhosphorylationAGHEKIHSGVKPYEC
CCCCHHCCCCCCEEC		49.0725159151
229AcetylationEKIHSGVKPYECTEC
CHHCCCCCCEECCCC		45.467429211
229UbiquitinationEKIHSGVKPYECTEC
CHHCCCCCCEECCCC		45.4629967540
231PhosphorylationIHSGVKPYECTECGK
HCCCCCCEECCCCCC		20.2322817900
239PhosphorylationECTECGKTFIKSTHL
ECCCCCCEEEHHHHH		18.84-
243PhosphorylationCGKTFIKSTHLLQHH
CCCEEEHHHHHHHCC		19.08-
244PhosphorylationGKTFIKSTHLLQHHM
CCEEEHHHHHHHCCC		16.13-
259PhosphorylationIHTGERPYECMECGK
CCCCCCCCCHHHHHH		28.16-
271UbiquitinationCGKAFNRKSYLTQHQ
HHHCCCCHHHHCHHC		44.5529967540
272PhosphorylationGKAFNRKSYLTQHQR
HHCCCCHHHHCHHCH		23.3428555341
282PhosphorylationTQHQRIHSGEKPYKC
CHHCHHHCCCCCEEC		46.4029496963
287PhosphorylationIHSGEKPYKCNECGK
HHCCCCCEECCCCCC		38.96-
288SumoylationHSGEKPYKCNECGKA
HCCCCCEECCCCCCE		38.83-
288SumoylationHSGEKPYKCNECGKA
HCCCCCEECCCCCCE		38.83-
310PhosphorylationVLHNRRHTGEKSFVC
EEECCCCCCCCEEEE		45.2723532336
334PhosphorylationRPGFLRHYVVHSGEN
CCCCCCEEEEECCCC		9.57-
338PhosphorylationLRHYVVHSGENPYEC
CCEEEEECCCCCEEH		35.8728152594
343PhosphorylationVHSGENPYECLECGK
EECCCCCEEHHHHCC		30.7528152594
366PhosphorylationMWHQQTHTGEKPYEC
EEECCCCCCCCCEEC		50.8823898821
369UbiquitinationQQTHTGEKPYECSEC
CCCCCCCCCEECCHH		55.00-
394PhosphorylationIHHYVIHTGEKPFEC
HEEHEEECCCCCEEH		35.59-
422PhosphorylationKRHQRIHTGEKPFVC
HHHCCCCCCCCCEEE		44.6719276368
425SumoylationQRIHTGEKPFVCSEC
CCCCCCCCCEEECCC		45.1328112733
449UbiquitinationFILHKRAHTGEKPFE
EEECCCCCCCCCCCC		38.1422505724
450PhosphorylationILHKRAHTGEKPFEC
EECCCCCCCCCCCCC		46.1629496963
453SumoylationKRAHTGEKPFECKEC
CCCCCCCCCCCCCHH		57.25-
453SumoylationKRAHTGEKPFECKEC
CCCCCCCCCCCCCHH		57.25-
453UbiquitinationKRAHTGEKPFECKEC
CCCCCCCCCCCCCHH		57.25-
458SumoylationGEKPFECKECGKAFS
CCCCCCCCHHHHHHC		49.17-
458SumoylationGEKPFECKECGKAFS
CCCCCCCCHHHHHHC		49.17-
458UbiquitinationGEKPFECKECGKAFS
CCCCCCCCHHHHHHC		49.1733845483
475PhosphorylationKDLIRHFSIHTGEKP
HHHHHHEEEECCCCC		13.8228555341
478PhosphorylationIRHFSIHTGEKPYEC
HHHEEEECCCCCEEE		45.4228152594
481UbiquitinationFSIHTGEKPYECVEC
EEEECCCCCEEEEEC		55.0033845483
483PhosphorylationIHTGEKPYECVECGK
EECCCCCEEEEECCC		32.7828152594
496PhosphorylationGKAFTRMSGLTRHKR
CCHHHHHCCCCCCCC		27.6228555341
506PhosphorylationTRHKRIHSGEKPYEC
CCCCCCCCCCCCEEE		46.4028152594
511PhosphorylationIHSGEKPYECVECGK
CCCCCCCEEEEECCC		32.7828112733
534PhosphorylationIRHAIIHTGEKPYKC
HHHHEEECCCCCEEC		36.3129496963
537UbiquitinationAIIHTGEKPYKCSEC
HEEECCCCCEECCCC		55.80-
539PhosphorylationIHTGEKPYKCSECGK
EECCCCCEECCCCCC		35.38-
542PhosphorylationGEKPYKCSECGKAFS
CCCCEECCCCCCCCC		31.59-
546UbiquitinationYKCSECGKAFSRSSS
EECCCCCCCCCCCCC		58.90-
552PhosphorylationGKAFSRSSSLTQHQR
CCCCCCCCCCHHHHH		28.4027251275
553PhosphorylationKAFSRSSSLTQHQRM
CCCCCCCCCHHHHHH		36.3627251275
562PhosphorylationTQHQRMHTGKNPISV
HHHHHHHCCCCCCCE		40.2726425664
584PhosphorylationTSGQTSVTLRELLLG
CCCCCEEEHHHHHCC		21.6224719451
592UbiquitinationLRELLLGKDFLNVTT
HHHHHCCCCCCCCCC		45.3229967540
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 ZN264_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN264_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 ZN264_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NDEL1_HUMANNDEL1physical
25416956
TRI41_HUMANTRIM41physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
ZY11A_HUMANZYG11Aphysical
28514442
CENPB_HUMANCENPBphysical
28514442
TIF1A_HUMANTRIM24physical
28514442
GOPC_HUMANGOPCphysical
28514442
ZN805_HUMANZNF805physical
28514442
TRI41_HUMANTRIM41physical
28514442
TRI39_HUMANTRIM39physical
28514442
ZN460_HUMANZNF460physical
28514442
SORL_HUMANSORL1physical
28514442
ERBIN_HUMANERBB2IPphysical
28514442
TIF1B_HUMANTRIM28physical
28514442
RBM22_HUMANRBM22physical
28514442
LRP2_HUMANLRP2physical
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 ZN264_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-80, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-343; TYR-483 ANDTYR-511, AND MASS SPECTROMETRY.

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