ZN415_HUMAN - dbPTM
ZN415_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN415_HUMAN
UniProt AC Q09FC8
Protein Name Zinc finger protein 415
Gene Name ZNF415
Organism Homo sapiens (Human).
Sequence Length 603
Subcellular Localization Nucleus . Cytoplasm . Isoforms 1, isoform 2, isoform 4 and isoform 5 showed both nuclear and cytoplasm localization. Isoform 3 localized only to nucleus.
Protein Description Involved in transcriptional regulation. Transcriptional activity differed among the various isoforms. All isoforms except isoform 3 seem to suppresses the transcriptional activities of AP-1 and p53/TP53..
Protein Sequence MPELYTEDFIQGCDVGELQEPGLPGVLSYVGAQERALDHRKPSTSSKKTKRVEIDQRCENRLECNGAISAHCNLRLPDSNDSPASASRVAGITDLSRNCVIKELAPQQEGNPGEVFHTVTLEQHEKHDIEEFCFREIKKKIHDFDCQWRDDERNCNKVTTAPKENLTCRRDQRDRRGIGNKSIKHQLGLSFLPHPHELQQFQAEGKIYECNHVEKSVNHGSSVSPPQIISSTIKTHVSNKYGTDFICSSLLTQEQKSCIREKPYRYIECDKALNHGSHMTVRQVSHSGEKGYKCDLCGKVFSQKSNLARHWRVHTGEKPYKCNECDRSFSRNSCLALHRRVHTGEKPYKCYECDKVFSRNSCLALHQKTHIGEKPYTCKECGKAFSVRSTLTNHQVIHSGKKPYKCNECGKVFSQTSSLATHQRIHTGEKPYKCNECGKVFSQTSSLARHWRIHTGEKPYKCNECGKVFSYNSHLASHRRVHTGEKPYKCNECGKAFSVHSNLTTHQVIHTGEKPYKCNQCGKGFSVHSSLTTHQVIHTGEKPYKCNECGKSFSVRPNLTRHQIIHTGKKPYKCSDCGKSFSVRPNLFRHQIIHTKEKPYKRN
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
16 (in isoform 5)Phosphorylation-19.3528787133
159PhosphorylationERNCNKVTTAPKENL
CCCCCCCCCCCHHHC		20.8922210691
267PhosphorylationREKPYRYIECDKALN
HCCCEEEEECCHHCC		2.92-
270UbiquitinationPYRYIECDKALNHGS
CEEEEECCHHCCCCC		26.86-
270SumoylationPYRYIECDKALNHGS
CEEEEECCHHCCCCC		26.86-
295PhosphorylationGEKGYKCDLCGKVFS
CCCCEEECCCCCCCC		40.62-
298UbiquitinationGYKCDLCGKVFSQKS
CEEECCCCCCCCCCC		36.14-
298SumoylationGYKCDLCGKVFSQKS
CEEECCCCCCCCCCC		36.14-
315PhosphorylationARHWRVHTGEKPYKC
HHCEEEECCCCCCCC		44.1529496963
318SumoylationWRVHTGEKPYKCNEC
EEEECCCCCCCCCCC		55.80-
330PhosphorylationNECDRSFSRNSCLAL
CCCCCCCCCCCHHHH		31.6217081983
343PhosphorylationALHRRVHTGEKPYKC
HHHHHHHCCCCCCEE		44.1529496963
346SumoylationRRVHTGEKPYKCYEC
HHHHCCCCCCEEEEC		55.80-
357SumoylationCYECDKVFSRNSCLA
EEECCCEECCCCEEE		7.56-
361PhosphorylationDKVFSRNSCLALHQK
CCEECCCCEEEEHHC		14.92-
377PhosphorylationHIGEKPYTCKECGKA
CCCCCCEECCCCCCE		26.15-
379PhosphorylationGEKPYTCKECGKAFS
CCCCEECCCCCCEEE		48.52-
385SumoylationCKECGKAFSVRSTLT
CCCCCCEEEEEEECC		8.70-
386PhosphorylationKECGKAFSVRSTLTN
CCCCCEEEEEEECCC		22.8322468782
389PhosphorylationGKAFSVRSTLTNHQV
CCEEEEEEECCCCCE		26.1322468782
390PhosphorylationKAFSVRSTLTNHQVI
CEEEEEEECCCCCEE		27.3422468782
399PhosphorylationTNHQVIHSGKKPYKC
CCCCEECCCCCCEEC		40.9822468782
404PhosphorylationIHSGKKPYKCNECGK
ECCCCCCEECCCCCC		36.73-
405SumoylationHSGKKPYKCNECGKV
CCCCCCEECCCCCCE		38.83-
407PhosphorylationGKKPYKCNECGKVFS
CCCCEECCCCCCEEE		43.36-
413SumoylationCNECGKVFSQTSSLA
CCCCCCEEECCCCHH		5.23-
427PhosphorylationATHQRIHTGEKPYKC
HHCCCEECCCCCEEC		44.6729496963
432PhosphorylationIHTGEKPYKCNECGK
EECCCCCEECCCCCC		38.9618767875
433SumoylationHTGEKPYKCNECGKV
ECCCCCEECCCCCCE		38.83-
435PhosphorylationGEKPYKCNECGKVFS
CCCCEECCCCCCEEE		43.36-
438UbiquitinationPYKCNECGKVFSQTS
CEECCCCCCEEECCH		24.00-
438SumoylationPYKCNECGKVFSQTS
CEECCCCCCEEECCH		24.00-
441SumoylationCNECGKVFSQTSSLA
CCCCCCEEECCHHHH		5.23-
442PhosphorylationNECGKVFSQTSSLAR
CCCCCEEECCHHHHH		35.22-
444PhosphorylationCGKVFSQTSSLARHW
CCCEEECCHHHHHCE		21.05-
445PhosphorylationGKVFSQTSSLARHWR
CCEEECCHHHHHCEE		18.73-
446PhosphorylationKVFSQTSSLARHWRI
CEEECCHHHHHCEEE		29.45-
455PhosphorylationARHWRIHTGEKPYKC
HHCEEEECCCCCEEC		44.6729496963
460PhosphorylationIHTGEKPYKCNECGK
EECCCCCEECCCCCC		38.9618767875
461SumoylationHTGEKPYKCNECGKV
ECCCCCEECCCCCCE		38.83-
463PhosphorylationGEKPYKCNECGKVFS
CCCCEECCCCCCEEE		43.36-
483PhosphorylationASHRRVHTGEKPYKC
HHCCCCCCCCCCEEC		44.1529496963
486SumoylationRRVHTGEKPYKCNEC
CCCCCCCCCEECCCC		55.80-
489SumoylationHTGEKPYKCNECGKA
CCCCCCEECCCCCCE		38.83-
491PhosphorylationGEKPYKCNECGKAFS
CCCCEECCCCCCEEE		43.36-
497SumoylationCNECGKAFSVHSNLT
CCCCCCEEEEECCCC		9.99-
501PhosphorylationGKAFSVHSNLTTHQV
CCEEEEECCCCCCEE		31.23-
511PhosphorylationTTHQVIHTGEKPYKC
CCCEEEECCCCCEEC		35.5929496963
517AcetylationHTGEKPYKCNQCGKG
ECCCCCEECCCCCCC		34.9230593725
539PhosphorylationTTHQVIHTGEKPYKC
CCCEEEECCCCCEEC		35.5929496963
544PhosphorylationIHTGEKPYKCNECGK
EECCCCCEECCCCCC		38.9618767875
545AcetylationHTGEKPYKCNECGKS
ECCCCCEECCCCCCE		38.8330593729
545SumoylationHTGEKPYKCNECGKS
ECCCCCEECCCCCCE		38.83-
572PhosphorylationIHTGKKPYKCSDCGK
EECCCCCEECCCCCC		33.2430576142
580PhosphorylationKCSDCGKSFSVRPNL
ECCCCCCCEECCCCH		14.1930576142
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 ZN415_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN415_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 ZN415_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR412_HUMANKRTAP4-12physical
25416956
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN415_HUMAN

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Related Literatures of Post-Translational Modification

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