ZN460_HUMAN - dbPTM
ZN460_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN460_HUMAN
UniProt AC Q14592
Protein Name Zinc finger protein 460
Gene Name ZNF460
Organism Homo sapiens (Human).
Sequence Length 562
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MAAAWMAPAQESVTFEDVAVTFTQEEWGQLDVTQRALYVEVMLETCGLLVALGDSTKPETVEPIPSHLALPEEVSLQEQLAQGVPRYSYLGQAMDQDGPSEMQEYFLRPGTDPQSEKLHGKMSLEHEGLATADGICSMMIQNQVSPEDALYGFDSYGPVTDSLIHEGENSYKFEEMFNENCFLVQHEQILPRVKPYDCPECGKAFGKSKHLLQHHIIHTGEKPYKCLECGKDFNRRSHLTRHQRTHNGDKPFVCSECGRTFNRGSHLTRHQRVHSGEKPFVCNECGKAFTYRSNFVLHNKSHNEKKPFACSECGKGFYESTALIQHFIIHTGERPFKCLECGKAFNCRSHLKQHERIHTGEKPFVCSQCGKAFTHYSTYVLHERAHTGEKPFECKECGKAFSIRKDLIRHFNIHTGEKPYECLQCGKAFTRMSGLTRHQWIHTGEKPYVCIQCGKAFCRTTNLIRHFSIHTGEKPYECVECGKAFNRRSPLTRHQRIHTAEKSHEPIQSGNVSCESTDLIQHSIIHTESSPVSAVNMETPSIAAHSSSLDINGFIVEETLPL
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
76UbiquitinationALPEEVSLQEQLAQG
CCCCCCCHHHHHHCC		8.63-
117SumoylationGTDPQSEKLHGKMSL
CCCCCHHHHCCCCCC		51.5428112733
117UbiquitinationGTDPQSEKLHGKMSL
CCCCCHHHHCCCCCC		51.54-
153UbiquitinationPEDALYGFDSYGPVT
HHHHCCCCCCCCCCH		3.40-
153UbiquitinationPEDALYGFDSYGPVT
HHHHCCCCCCCCCCH		3.4033845483
162UbiquitinationSYGPVTDSLIHEGEN
CCCCCHHHEECCCCC		21.62-
162UbiquitinationSYGPVTDSLIHEGEN
CCCCCHHHEECCCCC		21.6233845483
166UbiquitinationVTDSLIHEGENSYKF
CHHHEECCCCCCCCH		62.3027667366
170PhosphorylationLIHEGENSYKFEEMF
EECCCCCCCCHHHHH		25.95-
171PhosphorylationIHEGENSYKFEEMFN
ECCCCCCCCHHHHHC		31.14-
181UbiquitinationEEMFNENCFLVQHEQ
HHHHCCCEEEEEHHH		1.9729967540
190UbiquitinationLVQHEQILPRVKPYD
EEEHHHHCCCCCCCC		1.90-
194SumoylationEQILPRVKPYDCPEC
HHHCCCCCCCCCCCH		38.86-
194SumoylationEQILPRVKPYDCPEC
HHHCCCCCCCCCCCH		38.8628112733
194UbiquitinationEQILPRVKPYDCPEC
HHHCCCCCCCCCCCH		38.8633845483
200UbiquitinationVKPYDCPECGKAFGK
CCCCCCCCHHHHHCC		63.3327667366
203SumoylationYDCPECGKAFGKSKH
CCCCCHHHHHCCCHH		52.80-
203SumoylationYDCPECGKAFGKSKH
CCCCCHHHHHCCCHH		52.8028112733
203UbiquitinationYDCPECGKAFGKSKH
CCCCCHHHHHCCCHH		52.8033845483
207SumoylationECGKAFGKSKHLLQH
CHHHHHCCCHHHHHC		50.2928112733
207UbiquitinationECGKAFGKSKHLLQH
CHHHHHCCCHHHHHC		50.2927667366
209UbiquitinationGKAFGKSKHLLQHHI
HHHHCCCHHHHHCCE		41.58-
209SumoylationGKAFGKSKHLLQHHI
HHHHCCCHHHHHCCE		41.58-
209SumoylationGKAFGKSKHLLQHHI
HHHHCCCHHHHHCCE		41.5828112733
219PhosphorylationLQHHIIHTGEKPYKC
HHCCEEECCCCCEEE		36.3129496963
222UbiquitinationHIIHTGEKPYKCLEC
CEEECCCCCEEEECC		55.8029967540
224PhosphorylationIHTGEKPYKCLECGK
EECCCCCEEEECCCC		25.9615592455
225SumoylationHTGEKPYKCLECGKD
ECCCCCEEEECCCCC		40.65-
225SumoylationHTGEKPYKCLECGKD
ECCCCCEEEECCCCC		40.65-
231UbiquitinationYKCLECGKDFNRRSH
EEEECCCCCCCCHHH		71.46-
237UbiquitinationGKDFNRRSHLTRHQR
CCCCCCHHHHHHCCC		21.44-
237PhosphorylationGKDFNRRSHLTRHQR
CCCCCCHHHHHHCCC		21.4428555341
237UbiquitinationGKDFNRRSHLTRHQR
CCCCCCHHHHHHCCC		21.4429901268
246UbiquitinationLTRHQRTHNGDKPFV
HHHCCCCCCCCCCEE		38.16-
246UbiquitinationLTRHQRTHNGDKPFV
HHHCCCCCCCCCCEE		38.1633845483
250SumoylationQRTHNGDKPFVCSEC
CCCCCCCCCEEECCC		41.58-
250SumoylationQRTHNGDKPFVCSEC
CCCCCCCCCEEECCC		41.5828112733
250UbiquitinationQRTHNGDKPFVCSEC
CCCCCCCCCEEECCC		41.58-
259UbiquitinationFVCSECGRTFNRGSH
EEECCCCCCCCCCCC		48.04-
259UbiquitinationFVCSECGRTFNRGSH
EEECCCCCCCCCCCC		48.0433845483
264UbiquitinationCGRTFNRGSHLTRHQ
CCCCCCCCCCCCCCC		22.11-
265UbiquitinationGRTFNRGSHLTRHQR
CCCCCCCCCCCCCCC		16.46-
275PhosphorylationTRHQRVHSGEKPFVC
CCCCCCCCCCCCEEE		45.8726055452
278SumoylationQRVHSGEKPFVCNEC
CCCCCCCCCEEECCC		47.48-
278SumoylationQRVHSGEKPFVCNEC
CCCCCCCCCEEECCC		47.4828112733
278UbiquitinationQRVHSGEKPFVCNEC
CCCCCCCCCEEECCC		47.4829901268
287SumoylationFVCNECGKAFTYRSN
EEECCCCCEEEEECC		52.5728112733
287UbiquitinationFVCNECGKAFTYRSN
EEECCCCCEEEEECC		52.5733845483
296UbiquitinationFTYRSNFVLHNKSHN
EEEECCEEECCCCCC		6.59-
296UbiquitinationFTYRSNFVLHNKSHN
EEEECCEEECCCCCC		6.5921890473
300SumoylationSNFVLHNKSHNEKKP
CCEEECCCCCCCCCC		42.20-
300SumoylationSNFVLHNKSHNEKKP
CCEEECCCCCCCCCC		42.2028112733
300UbiquitinationSNFVLHNKSHNEKKP
CCEEECCCCCCCCCC		42.2033845483
302UbiquitinationFVLHNKSHNEKKPFA
EEECCCCCCCCCCCC		48.34-
302UbiquitinationFVLHNKSHNEKKPFA
EEECCCCCCCCCCCC		48.3422505724
305SumoylationHNKSHNEKKPFACSE
CCCCCCCCCCCCCCC		71.6828112733
305UbiquitinationHNKSHNEKKPFACSE
CCCCCCCCCCCCCCC		71.68-
306SumoylationNKSHNEKKPFACSEC
CCCCCCCCCCCCCCC		38.91-
306SumoylationNKSHNEKKPFACSEC
CCCCCCCCCCCCCCC		38.9128112733
306UbiquitinationNKSHNEKKPFACSEC
CCCCCCCCCCCCCCC		38.91-
321UbiquitinationGKGFYESTALIQHFI
CCCHHHHHHHHEEEE		17.34-
330UbiquitinationLIQHFIIHTGERPFK
HHEEEEECCCCCCEE		24.0121890473
331PhosphorylationIQHFIIHTGERPFKC
HEEEEECCCCCCEEE		30.2623186163
336UbiquitinationIHTGERPFKCLECGK
ECCCCCCEEEECCCC		12.5122505724
337SumoylationHTGERPFKCLECGKA
CCCCCCEEEECCCCE		40.36-
337SumoylationHTGERPFKCLECGKA
CCCCCCEEEECCCCE		40.36-
337UbiquitinationHTGERPFKCLECGKA
CCCCCCEEEECCCCE		40.3621890473
343UbiquitinationFKCLECGKAFNCRSH
EEEECCCCEECCHHH		62.5622505724
349UbiquitinationGKAFNCRSHLKQHER
CCEECCHHHHHHHCC		35.06-
354UbiquitinationCRSHLKQHERIHTGE
CHHHHHHHCCCCCCC		25.39-
358UbiquitinationLKQHERIHTGEKPFV
HHHHCCCCCCCCCEE		33.76-
358UbiquitinationLKQHERIHTGEKPFV
HHHHCCCCCCCCCEE		33.7633845483
359PhosphorylationKQHERIHTGEKPFVC
HHHCCCCCCCCCEEE		44.6721712546
360UbiquitinationQHERIHTGEKPFVCS
HHCCCCCCCCCEEEC		27.1121890473
360UbiquitinationQHERIHTGEKPFVCS
HHCCCCCCCCCEEEC		27.1121890473
362SumoylationERIHTGEKPFVCSQC
CCCCCCCCCEEECCC		45.13-
362SumoylationERIHTGEKPFVCSQC
CCCCCCCCCEEECCC		45.1328112733
362UbiquitinationERIHTGEKPFVCSQC
CCCCCCCCCEEECCC		45.13-
367PhosphorylationGEKPFVCSQCGKAFT
CCCCEEECCCCCCCC		24.1717525332
371SumoylationFVCSQCGKAFTHYST
EEECCCCCCCCEEEE		48.2128112733
377UbiquitinationGKAFTHYSTYVLHER
CCCCCEEEEEEHHCC		12.98-
377UbiquitinationGKAFTHYSTYVLHER
CCCCCEEEEEEHHCC		12.9822505724
386UbiquitinationYVLHERAHTGEKPFE
EEHHCCCCCCCCCCC		40.40-
387PhosphorylationVLHERAHTGEKPFEC
EHHCCCCCCCCCCCC		46.1629496963
390SumoylationERAHTGEKPFECKEC
CCCCCCCCCCCCCCC		57.25-
390SumoylationERAHTGEKPFECKEC
CCCCCCCCCCCCCCC		57.25-
390UbiquitinationERAHTGEKPFECKEC
CCCCCCCCCCCCCCC		57.25-
395SumoylationGEKPFECKECGKAFS
CCCCCCCCCCCCEEE		49.17-
395SumoylationGEKPFECKECGKAFS
CCCCCCCCCCCCEEE		49.17-
395UbiquitinationGEKPFECKECGKAFS
CCCCCCCCCCCCEEE		49.17-
399SumoylationFECKECGKAFSIRKD
CCCCCCCCEEEECHH		58.90-
399SumoylationFECKECGKAFSIRKD
CCCCCCCCEEEECHH		58.90-
399UbiquitinationFECKECGKAFSIRKD
CCCCCCCCEEEECHH		58.9033845483
405UbiquitinationGKAFSIRKDLIRHFN
CCEEEECHHHHHHCC		56.04-
411UbiquitinationRKDLIRHFNIHTGEK
CHHHHHHCCCCCCCC		7.0622505724
415PhosphorylationIRHFNIHTGEKPYEC
HHHCCCCCCCCCEEH		43.1528152594
418UbiquitinationFNIHTGEKPYECLQC
CCCCCCCCCEEHHHC		55.0022505724
420PhosphorylationIHTGEKPYECLQCGK
CCCCCCCEEHHHCCC		30.2728152594
427SumoylationYECLQCGKAFTRMSG
EEHHHCCCCHHHHCC		48.21-
427SumoylationYECLQCGKAFTRMSG
EEHHHCCCCHHHHCC		48.21-
427UbiquitinationYECLQCGKAFTRMSG
EEHHHCCCCHHHHCC		48.21-
433UbiquitinationGKAFTRMSGLTRHQW
CCCHHHHCCCCCEEE		27.62-
433PhosphorylationGKAFTRMSGLTRHQW
CCCHHHHCCCCCEEE		27.6228555341
433UbiquitinationGKAFTRMSGLTRHQW
CCCHHHHCCCCCEEE		27.6222505724
442UbiquitinationLTRHQWIHTGEKPYV
CCCEEEEECCCCCEE		25.51-
442UbiquitinationLTRHQWIHTGEKPYV
CCCEEEEECCCCCEE		25.5133845483
443PhosphorylationTRHQWIHTGEKPYVC
CCEEEEECCCCCEEE		37.5918669648
446SumoylationQWIHTGEKPYVCIQC
EEEECCCCCEEEEEC		42.89-
446SumoylationQWIHTGEKPYVCIQC
EEEECCCCCEEEEEC		42.8928112733
446UbiquitinationQWIHTGEKPYVCIQC
EEEECCCCCEEEEEC		42.89-
455SumoylationYVCIQCGKAFCRTTN
EEEEECCCEEHHHHH		46.01-
455SumoylationYVCIQCGKAFCRTTN
EEEEECCCEEHHHHH		46.0128112733
467UbiquitinationTTNLIRHFSIHTGEK
HHHHHEEEEEECCCC		5.4322505724
468PhosphorylationTNLIRHFSIHTGEKP
HHHHEEEEEECCCCC		13.8228555341
471PhosphorylationIRHFSIHTGEKPYEC
HEEEEEECCCCCEEE		45.4228152594
474UbiquitinationFSIHTGEKPYECVEC
EEEECCCCCEEEEEC		55.0022505724
476PhosphorylationIHTGEKPYECVECGK
EECCCCCEEEEECCC		32.7828152594
483SumoylationYECVECGKAFNRRSP
EEEEECCCCCCCCCC		62.56-
483SumoylationYECVECGKAFNRRSP
EEEEECCCCCCCCCC		62.56-
483UbiquitinationYECVECGKAFNRRSP
EEEEECCCCCCCCCC		62.5633845483
489PhosphorylationGKAFNRRSPLTRHQR
CCCCCCCCCCHHHHH		22.4823898821
492PhosphorylationFNRRSPLTRHQRIHT
CCCCCCCHHHHHHCC		29.5023403867
523PhosphorylationSTDLIQHSIIHTESS
CCCCEEEEEEECCCC		13.5826074081
527PhosphorylationIQHSIIHTESSPVSA
EEEEEEECCCCCCEE		27.4426074081
529PhosphorylationHSIIHTESSPVSAVN
EEEEECCCCCCEEEC		40.8926074081
530PhosphorylationSIIHTESSPVSAVNM
EEEECCCCCCEEECC		24.0826074081
533PhosphorylationHTESSPVSAVNMETP
ECCCCCCEEECCCCC		29.8626074081
539PhosphorylationVSAVNMETPSIAAHS
CEEECCCCCCHHCCC		16.1526074081
541PhosphorylationAVNMETPSIAAHSSS
EECCCCCCHHCCCCC		32.0726074081
546PhosphorylationTPSIAAHSSSLDING
CCCHHCCCCCCCCCC		19.5226074081
547PhosphorylationPSIAAHSSSLDINGF
CCHHCCCCCCCCCCE		25.6726074081
548PhosphorylationSIAAHSSSLDINGFI
CHHCCCCCCCCCCEE		32.8326074081
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 ZN460_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN460_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 ZN460_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN250_HUMANZNF250physical
25416956
DEUP1_HUMANCCDC67physical
25416956
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 ZN460_HUMAN

loading...

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-367, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory