ZN430_HUMAN - dbPTM
ZN430_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN430_HUMAN
UniProt AC Q9H8G1
Protein Name Zinc finger protein 430
Gene Name ZNF430
Organism Homo sapiens (Human).
Sequence Length 570
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MENLKSGVYPLKEASGCPGADRNLLVYSFYEKGPLTFRDVAIEFSLEEWQCLDTAQQDLYRKVMLENYRNLVFLAGIAVSKPDLITCLEQGKEPWNMKRHAMVDQPPVTYSHFAQDLWPEQGIKDSFQEVILRRYGKCGHEDLQLRTGCKSVDECNLHKECYDELNQCLTTTQSEIFQYDKYVNVFYKFSNPNIQKIRHTGKKPFKCKKCDKSFCMLLHLTQHKRIHIRENSYQCEECGKVFNWFSTLTRHRRIHTGEKPYKCEQCGKAFKQSSTLTTHKIIHTGEKPYRCEECGKTFNRSSHLTTHKRIHTGEKPYRCEECGRAFNRSSHLTTHKIIHTGEKPYKCEECGKAFNQSSTLTTHKIIHAGEKPYKCEECGKAFYRFSYLTKHKIIHTGEKFYKCEECGKGFNWSSTLTKHKRIHTGEKPYKCEQCGKAFNESSNLTAHKIIHTGEKPYKCEECGKAFNRSPKLTAHKVIHSGEKPYKCEECGKAFNQFSNLTKHKITHIGDTSYKYLECDKAFSQSSTLTKHKVIHTGEKPYNCEEYGKAFNQSSNLIEQSNSYWRETLQM
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
1Acetylation-------MENLKSGV
-------CCCCCCCC		7.5122814378
5Ubiquitination---MENLKSGVYPLK
---CCCCCCCCCCCH		57.66-
12UbiquitinationKSGVYPLKEASGCPG
CCCCCCCHHHCCCCC		46.89-
32UbiquitinationLVYSFYEKGPLTFRD
EEEEEEECCCCCHHH		55.22-
60PhosphorylationDTAQQDLYRKVMLEN
HHHHHHHHHHHHHHH		19.3722817900
62UbiquitinationAQQDLYRKVMLENYR
HHHHHHHHHHHHHHH		20.59-
137UbiquitinationVILRRYGKCGHEDLQ
HHHHHHCCCCCCHHH		28.27-
150UbiquitinationLQLRTGCKSVDECNL
HHHHHCCCCHHHCCC		55.66-
188UbiquitinationKYVNVFYKFSNPNIQ
CCEEEEEECCCCCHH		30.7421890473
190PhosphorylationVNVFYKFSNPNIQKI
EEEEEECCCCCHHHC		47.4230206219
206AcetylationHTGKKPFKCKKCDKS
CCCCCCCCCCCCCHH		54.387481505
208AcetylationGKKPFKCKKCDKSFC
CCCCCCCCCCCHHHH		57.967481513
256PhosphorylationTRHRRIHTGEKPYKC
HCCCCCCCCCCCCCH		44.6729496963
259UbiquitinationRRIHTGEKPYKCEQC
CCCCCCCCCCCHHHC		55.80-
262SumoylationHTGEKPYKCEQCGKA
CCCCCCCCHHHCCCC		39.56-
262SumoylationHTGEKPYKCEQCGKA
CCCCCCCCHHHCCCC		39.56-
262UbiquitinationHTGEKPYKCEQCGKA
CCCCCCCCHHHCCCC		39.56-
271SumoylationEQCGKAFKQSSTLTT
HHCCCCHHCCCCCEE		54.88-
271UbiquitinationEQCGKAFKQSSTLTT
HHCCCCHHCCCCCEE		54.88-
271SumoylationEQCGKAFKQSSTLTT
HHCCCCHHCCCCCEE		54.88-
273PhosphorylationCGKAFKQSSTLTTHK
CCCCHHCCCCCEEEE		26.36-
274PhosphorylationGKAFKQSSTLTTHKI
CCCHHCCCCCEEEEE		25.58-
277PhosphorylationFKQSSTLTTHKIIHT
HHCCCCCEEEEEEEC		27.26-
280UbiquitinationSSTLTTHKIIHTGEK
CCCCEEEEEEECCCC		41.06-
280SumoylationSSTLTTHKIIHTGEK
CCCCEEEEEEECCCC		41.06-
280SumoylationSSTLTTHKIIHTGEK
CCCCEEEEEEECCCC		41.06-
284PhosphorylationTTHKIIHTGEKPYRC
EEEEEEECCCCCEEC		36.3129496963
287UbiquitinationKIIHTGEKPYRCEEC
EEEECCCCCEECCCC		49.01-
287SumoylationKIIHTGEKPYRCEEC
EEEECCCCCEECCCC		49.01-
287SumoylationKIIHTGEKPYRCEEC
EEEECCCCCEECCCC		49.01-
296UbiquitinationYRCEECGKTFNRSSH
EECCCCCCCCCCCCC		62.70-
306PhosphorylationNRSSHLTTHKRIHTG
CCCCCCCCCCCCCCC		31.5924719451
312PhosphorylationTTHKRIHTGEKPYRC
CCCCCCCCCCCCCCH		44.6729496963
315UbiquitinationKRIHTGEKPYRCEEC
CCCCCCCCCCCHHHH		49.01-
315SumoylationKRIHTGEKPYRCEEC
CCCCCCCCCCCHHHH		49.01-
315SumoylationKRIHTGEKPYRCEEC
CCCCCCCCCCCHHHH		49.01-
336UbiquitinationSSHLTTHKIIHTGEK
CCCCCCCEEEECCCC		41.06-
340PhosphorylationTTHKIIHTGEKPYKC
CCCEEEECCCCCEEH		36.3129496963
343UbiquitinationKIIHTGEKPYKCEEC
EEEECCCCCEEHHHH		55.80-
345PhosphorylationIHTGEKPYKCEECGK
EECCCCCEEHHHHHH		39.06-
346SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHC		43.63-
346AcetylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHC		43.6319825849
346SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHC		43.63-
346UbiquitinationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHC		43.63-
352UbiquitinationYKCEECGKAFNQSST
EEHHHHHHCCCCCCC		62.56-
357PhosphorylationCGKAFNQSSTLTTHK
HHHCCCCCCCCCEEC		26.79-
358PhosphorylationGKAFNQSSTLTTHKI
HHCCCCCCCCCEECE		20.06-
359PhosphorylationKAFNQSSTLTTHKII
HCCCCCCCCCEECEE		33.11-
361PhosphorylationFNQSSTLTTHKIIHA
CCCCCCCCEECEEEC		27.26-
371UbiquitinationKIIHAGEKPYKCEEC
CEEECCCCCEECCHH		53.37-
373PhosphorylationIHAGEKPYKCEECGK
EECCCCCEECCHHCC		39.06-
374SumoylationHAGEKPYKCEECGKA
ECCCCCEECCHHCCC		43.63-
374UbiquitinationHAGEKPYKCEECGKA
ECCCCCEECCHHCCC		43.63-
374SumoylationHAGEKPYKCEECGKA
ECCCCCEECCHHCCC		43.63-
380UbiquitinationYKCEECGKAFYRFSY
EECCHHCCCHHHHHH		47.16-
396PhosphorylationTKHKIIHTGEKFYKC
HHCCEEECCCCEEEC		36.3127251275
402SumoylationHTGEKFYKCEECGKG
ECCCCEEECCCCCCC		38.00-
402UbiquitinationHTGEKFYKCEECGKG
ECCCCEEECCCCCCC		38.00-
402SumoylationHTGEKFYKCEECGKG
ECCCCEEECCCCCCC		38.00-
418UbiquitinationNWSSTLTKHKRIHTG
CCCCCCCCCCCCCCC		50.68-
424PhosphorylationTKHKRIHTGEKPYKC
CCCCCCCCCCCCCCH		44.6729496963
430SumoylationHTGEKPYKCEQCGKA
CCCCCCCCHHHHHHC		39.56-
430SumoylationHTGEKPYKCEQCGKA
CCCCCCCCHHHHHHC		39.56-
430UbiquitinationHTGEKPYKCEQCGKA
CCCCCCCCHHHHHHC		39.56-
448UbiquitinationSSNLTAHKIIHTGEK
CCCCCEEEEEECCCC		40.67-
452PhosphorylationTAHKIIHTGEKPYKC
CEEEEEECCCCCEEC		36.3129496963
455UbiquitinationKIIHTGEKPYKCEEC
EEEECCCCCEECHHH		55.80-
457PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECHHHHH		39.06-
458SumoylationHTGEKPYKCEECGKA
ECCCCCEECHHHHHH		43.63-
458AcetylationHTGEKPYKCEECGKA
ECCCCCEECHHHHHH		43.6319825855
458SumoylationHTGEKPYKCEECGKA
ECCCCCEECHHHHHH		43.63-
458UbiquitinationHTGEKPYKCEECGKA
ECCCCCEECHHHHHH		43.63-
464UbiquitinationYKCEECGKAFNRSPK
EECHHHHHHCCCCCC		62.56-
469PhosphorylationCGKAFNRSPKLTAHK
HHHHCCCCCCCCEEE		27.7324719451
480PhosphorylationTAHKVIHSGEKPYKC
CEEEEECCCCCCEEH		37.2129496963
483UbiquitinationKVIHSGEKPYKCEEC
EEECCCCCCEEHHHH		58.11-
486SumoylationHSGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
486AcetylationHSGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.637409443
486UbiquitinationHSGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
486SumoylationHSGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
492UbiquitinationYKCEECGKAFNQFSN
EEHHHHHHHHHHHHH		62.56-
502SumoylationNQFSNLTKHKITHIG
HHHHHCCCCCCEEEC		46.17-
502SumoylationNQFSNLTKHKITHIG
HHHHHCCCCCCEEEC		46.17-
504UbiquitinationFSNLTKHKITHIGDT
HHHCCCCCCEEECCC		51.35-
514SumoylationHIGDTSYKYLECDKA
EECCCCCEEEEECCC		43.03-
514UbiquitinationHIGDTSYKYLECDKA
EECCCCCEEEEECCC		43.03-
514SumoylationHIGDTSYKYLECDKA
EECCCCCEEEEECCC		43.03-
520UbiquitinationYKYLECDKAFSQSST
CEEEEECCCCCCCCC		64.09-
530SumoylationSQSSTLTKHKVIHTG
CCCCCCCCCCEEECC		44.53-
530UbiquitinationSQSSTLTKHKVIHTG
CCCCCCCCCCEEECC		44.53-
530SumoylationSQSSTLTKHKVIHTG
CCCCCCCCCCEEECC		44.53-
536PhosphorylationTKHKVIHTGEKPYNC
CCCCEEECCCCCCCH		35.59-
539UbiquitinationKVIHTGEKPYNCEEY
CEEECCCCCCCHHHH		54.89-
548UbiquitinationYNCEEYGKAFNQSSN
CCHHHHHHHHHHCCC		49.23-
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 ZN430_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN430_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 ZN430_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN430_HUMAN !!
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN430_HUMAN

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Related Literatures of Post-Translational Modification

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