ZN765_HUMAN - dbPTM
ZN765_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN765_HUMAN
UniProt AC Q7L2R6
Protein Name Zinc finger protein 765
Gene Name ZNF765
Organism Homo sapiens (Human).
Sequence Length 523
Subcellular Localization Nucleus.
Protein Description May be involved in transcriptional regulation..
Protein Sequence MALPQGLLTFRDVAIEFSQEEWKCLDPAQRTLYRDVMLENYRNLVSLDISSKCMMKEFSSTAQGNREVFHAGTSQRHESHHNGDFCFQDIDKDIHDIEFQWQEDERNGHEALMTKIKKLTGSTERYDQNYAGNKPVKYQLGFSFHSHLPELHIFHTEEKIDNQVVKSIHDASLVSTAQRISCRPETHISNDYGNNFLNSSLFTQKQEVHMREKSFQCNDSGKAYNCSSLLRKHQLIHLGEKQYKCDICGKVFNSKRYVARHRRCHTGEKPYKCNECGKTFSQTYYLTCHRRLHTGEKPYKCEECDKAFHFKSKLQIHRRIHTGEKPYKCNECGKTFSQKSYLTCHRRLHTGEKPYKCNECGKTFSRKSHFTCHHRVHTGEKPYKCNECSKTFSHKSSLTYHRRLHTEEKPYKCNECGKTFNQQLTLNICRLHSGEKPYKCEECDKAYSFKSNLEIHQKIHTEENPYKCNECGKTFSRTSSLTYHHRLHTGQKPYKCEDCDEAFSFKSNLERHRRIYTGEKLHV
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
18PhosphorylationRDVAIEFSQEEWKCL
HHHEEECCHHHHHHC		24.7227251275
23UbiquitinationEFSQEEWKCLDPAQR
ECCHHHHHHCCHHHH		28.35-
41PhosphorylationRDVMLENYRNLVSLD
HHHHHHHHHHHEECC		7.4822210691
46PhosphorylationENYRNLVSLDISSKC
HHHHHHEECCCCCCH		24.4022210691
52UbiquitinationVSLDISSKCMMKEFS
EECCCCCCHHHHHHH		21.25-
56UbiquitinationISSKCMMKEFSSTAQ
CCCCHHHHHHHHCCC		28.82-
60PhosphorylationCMMKEFSSTAQGNRE
HHHHHHHHCCCCCCE		32.8430631047
107 (in isoform 3)Phosphorylation-54.8722210691
115UbiquitinationGHEALMTKIKKLTGS
HHHHHHHHHHHHHCC		38.2629967540
117 (in isoform 3)Phosphorylation-43.2022210691
120PhosphorylationMTKIKKLTGSTERYD
HHHHHHHHCCCCCCC		37.66-
134UbiquitinationDQNYAGNKPVKYQLG
CCCCCCCCCEEEEEE		50.7129967540
166UbiquitinationKIDNQVVKSIHDASL
HHCHHHHHHHHHHHH		44.8529967540
167PhosphorylationIDNQVVKSIHDASLV
HCHHHHHHHHHHHHH		17.34-
172PhosphorylationVKSIHDASLVSTAQR
HHHHHHHHHHHHHHH		35.05-
175PhosphorylationIHDASLVSTAQRISC
HHHHHHHHHHHHHCC		24.26-
176PhosphorylationHDASLVSTAQRISCR
HHHHHHHHHHHHCCC		21.23-
205SumoylationNSSLFTQKQEVHMRE
CCHHHCCCCEECCCC		45.4228112733
222UbiquitinationFQCNDSGKAYNCSSL
EEECCCCCCCCCHHH		52.21-
228PhosphorylationGKAYNCSSLLRKHQL
CCCCCCHHHHHHHCC		33.3524719451
232UbiquitinationNCSSLLRKHQLIHLG
CCHHHHHHHCCCCCC		35.35-
272SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC		38.83-
272UbiquitinationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC		38.83-
272SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC		38.83-
294PhosphorylationTCHRRLHTGEKPYKC
EEECCCCCCCCCEEC		52.1827422710
297 (in isoform 1)Ubiquitination-55.8021890473
297SumoylationRRLHTGEKPYKCEEC
CCCCCCCCCEECCCC		55.80-
297SumoylationRRLHTGEKPYKCEEC
CCCCCCCCCEECCCC		55.80-
297UbiquitinationRRLHTGEKPYKCEEC
CCCCCCCCCEECCCC		55.8021890473
300SumoylationHTGEKPYKCEECDKA
CCCCCCEECCCCCCC		43.63-
300SumoylationHTGEKPYKCEECDKA
CCCCCCEECCCCCCC		43.63-
322PhosphorylationQIHRRIHTGEKPYKC
HHHCCCCCCCCCEEC		44.6729496963
327PhosphorylationIHTGEKPYKCNECGK
CCCCCCCEECCCCCC		38.9618767875
328SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC		38.83-
328UbiquitinationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC		38.83-
328SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC		38.83-
340PhosphorylationGKTFSQKSYLTCHRR
CCCCCCCCCCEECCC		20.1027251275
343PhosphorylationFSQKSYLTCHRRLHT
CCCCCCCEECCCCCC		9.68-
350PhosphorylationTCHRRLHTGEKPYKC
EECCCCCCCCCCEEC		52.1827422710
353SumoylationRRLHTGEKPYKCNEC
CCCCCCCCCEECCCC		55.80-
353SumoylationRRLHTGEKPYKCNEC
CCCCCCCCCEECCCC		55.80-
353UbiquitinationRRLHTGEKPYKCNEC
CCCCCCCCCEECCCC		55.8021890473
355PhosphorylationLHTGEKPYKCNECGK
CCCCCCCEECCCCCC		38.96-
356SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC		38.83-
356SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC		38.83-
356UbiquitinationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC		38.83-
362UbiquitinationYKCNECGKTFSRKSH
EECCCCCCCCCCCCC		59.04-
378PhosphorylationTCHHRVHTGEKPYKC
EEECEEECCCCCEEC		44.1529496963
381SumoylationHRVHTGEKPYKCNEC
CEEECCCCCEECCCC		55.80-
381UbiquitinationHRVHTGEKPYKCNEC
CEEECCCCCEECCCC		55.80-
381SumoylationHRVHTGEKPYKCNEC
CEEECCCCCEECCCC		55.80-
412SumoylationHTEEKPYKCNECGKT
CCCCCCEECCCCCCC		38.83-
412SumoylationHTEEKPYKCNECGKT
CCCCCCEECCCCCCC		38.83-
433PhosphorylationLNICRLHSGEKPYKC
EEEEECCCCCCCEEC		53.9227794612
439SumoylationHSGEKPYKCEECDKA
CCCCCCEECCCCCCC		43.63-
439SumoylationHSGEKPYKCEECDKA
CCCCCCEECCCCCCC		43.63-
448PhosphorylationEECDKAYSFKSNLEI
CCCCCCEECCCCCHH		30.9324719451
467SumoylationHTEENPYKCNECGKT
CCCCCCCCCCCCCCE		31.66-
467SumoylationHTEENPYKCNECGKT
CCCCCCCCCCCCCCE		31.66-
473UbiquitinationYKCNECGKTFSRTSS
CCCCCCCCEEECCCC		59.04-
479PhosphorylationGKTFSRTSSLTYHHR
CCEEECCCCCEEEEE		23.4127251275
480PhosphorylationKTFSRTSSLTYHHRL
CEEECCCCCEEEEEC		24.9027251275
495SumoylationHTGQKPYKCEDCDEA
CCCCCCCCCCCCCCC		39.41-
495SumoylationHTGQKPYKCEDCDEA
CCCCCCCCCCCCCCC		39.41-
504PhosphorylationEDCDEAFSFKSNLER
CCCCCCCCCHHHHHH		38.5224719451
506SumoylationCDEAFSFKSNLERHR
CCCCCCCHHHHHHHH		36.92-
506SumoylationCDEAFSFKSNLERHR
CCCCCCCHHHHHHHH		36.92-
520UbiquitinationRRIYTGEKLHV----
HHEECCCCCCC----		45.28-
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 ZN765_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN765_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 ZN765_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN765_HUMAN !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN765_HUMAN

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Related Literatures of Post-Translational Modification

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