ZN676_HUMAN - dbPTM
ZN676_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN676_HUMAN
UniProt AC Q8N7Q3
Protein Name Zinc finger protein 676
Gene Name ZNF676
Organism Homo sapiens (Human).
Sequence Length 588
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MLENYRNLVFLGIAAFKPDLIIFLEQGKEPWNMKRHEMVEEPPVICSHFSQEFWPEQGIEDSFQKMILRRYDKCGHENLHLKISCTNVDECNVHKEGYNKLNQSLTTTQSKVFQCGKYANVFHKCSNSNRHKIRHTGEKGLKCKEYVRSFCMLSHLSQHERIYTRENSYKCEENGKAFNWSSTLTYYKSIHTGEKPYKCEECGKAFSKFSILTKHKVIHTGEKPYKCEECGKAFNRSSILTKHKIIHTGEKPYKCEECGKGFSSVSTLNTHKAIHAEEKPYKCEECGKASNSSSKLMEHKRIHTGEKPYKCEECGKAFSWSSSLTEHKRIHAGEKPYKCEECGKAFNRSSILTKHKIIHTGEKPYKCEGCGKAFSKVSTLNTHKAIHAEEKPYKCEECGKASNSSSKLMEHKRIHTGEKPYKCEECGKAFSWSSSLTEHKRIHAGEKPYKCEECGKAFTWSSSFTKHKRIHAAEKPYKCEECGKGFSTFSILTKHKIIHTGEKRYKCEECGKAFSWSSILTEHKIIHTGEKPYKCEECGKAFSRSSSLTRHKRIHTGEKPYKCEECGKAFKSSSTVSYHKKIHTGENP
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
98PhosphorylationCNVHKEGYNKLNQSL
CCCCHHHHHHHHHCC		15.37-
104PhosphorylationGYNKLNQSLTTTQSK
HHHHHHHCCCCCHHH		26.9825627689
106PhosphorylationNKLNQSLTTTQSKVF
HHHHHCCCCCHHHHH		32.8024043423
107PhosphorylationKLNQSLTTTQSKVFQ
HHHHCCCCCHHHHHH		28.2924043423
108PhosphorylationLNQSLTTTQSKVFQC
HHHCCCCCHHHHHHC		26.1324043423
110PhosphorylationQSLTTTQSKVFQCGK
HCCCCCHHHHHHCCC		28.7924043423
136PhosphorylationNRHKIRHTGEKGLKC
CCCCCCCCCCCCCCH		36.8723532336
168PhosphorylationRIYTRENSYKCEENG
CEECCCCCEEECCCC		22.63-
169PhosphorylationIYTRENSYKCEENGK
EECCCCCEEECCCCE		31.10-
192PhosphorylationTYYKSIHTGEKPYKC
EEEEECCCCCCCEEC		45.4229496963
195UbiquitinationKSIHTGEKPYKCEEC
EECCCCCCCEECHHH		55.80-
197PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEECHHHHH		39.06-
198SumoylationHTGEKPYKCEECGKA
CCCCCCEECHHHHHC		43.63-
198SumoylationHTGEKPYKCEECGKA
CCCCCCEECHHHHHC		43.63-
198UbiquitinationHTGEKPYKCEECGKA
CCCCCCEECHHHHHC		43.63-
210PhosphorylationGKAFSKFSILTKHKV
HHCCCCHHHHCCCCE		22.0324719451
220PhosphorylationTKHKVIHTGEKPYKC
CCCCEEECCCCCCCH		35.5929496963
223UbiquitinationKVIHTGEKPYKCEEC
CEEECCCCCCCHHHH		55.80-
225PhosphorylationIHTGEKPYKCEECGK
EECCCCCCCHHHHHC		39.06-
226AcetylationHTGEKPYKCEECGKA
ECCCCCCCHHHHHCC		43.6330705445
226SumoylationHTGEKPYKCEECGKA
ECCCCCCCHHHHHCC		43.63-
226UbiquitinationHTGEKPYKCEECGKA
ECCCCCCCHHHHHCC		43.63-
226SumoylationHTGEKPYKCEECGKA
ECCCCCCCHHHHHCC		43.63-
232UbiquitinationYKCEECGKAFNRSSI
CCHHHHHCCCCHHHH		62.5622505724
238PhosphorylationGKAFNRSSILTKHKI
HCCCCHHHHHHCCCE		20.5524719451
244UbiquitinationSSILTKHKIIHTGEK
HHHHHCCCEEECCCC		44.93-
248PhosphorylationTKHKIIHTGEKPYKC
HCCCEEECCCCCEEC		36.3129496963
251UbiquitinationKIIHTGEKPYKCEEC
CEEECCCCCEECCCC		55.80-
253PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECCCCCC		39.06-
254SumoylationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.63-
254SumoylationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.63-
254UbiquitinationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.63-
282SumoylationHAEEKPYKCEECGKA
CCCCCCCCHHHHCCC		43.63-
282UbiquitinationHAEEKPYKCEECGKA
CCCCCCCCHHHHCCC		43.63-
282SumoylationHAEEKPYKCEECGKA
CCCCCCCCHHHHCCC		43.63-
290PhosphorylationCEECGKASNSSSKLM
HHHHCCCCCCCHHHH		40.50-
292PhosphorylationECGKASNSSSKLMEH
HHCCCCCCCHHHHHC		33.23-
293PhosphorylationCGKASNSSSKLMEHK
HCCCCCCCHHHHHCC		35.42-
294PhosphorylationGKASNSSSKLMEHKR
CCCCCCCHHHHHCCC		29.63-
304PhosphorylationMEHKRIHTGEKPYKC
HHCCCCCCCCCCEEC		44.6729496963
307UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCEECHHC		55.80-
309PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEECHHCCC		39.06-
310SumoylationHTGEKPYKCEECGKA
CCCCCCEECHHCCCE		43.63-
310UbiquitinationHTGEKPYKCEECGKA
CCCCCCEECHHCCCE		43.63-
310SumoylationHTGEKPYKCEECGKA
CCCCCCEECHHCCCE		43.63-
337PhosphorylationIHAGEKPYKCEECGK
CCCCCCCCCHHHHHH		39.06-
338SumoylationHAGEKPYKCEECGKA
CCCCCCCCHHHHHHC		43.63-
338SumoylationHAGEKPYKCEECGKA
CCCCCCCCHHHHHHC		43.63-
338UbiquitinationHAGEKPYKCEECGKA
CCCCCCCCHHHHHHC		43.63-
344UbiquitinationYKCEECGKAFNRSSI
CCHHHHHHCCCHHHH		62.5622505724
350PhosphorylationGKAFNRSSILTKHKI
HHCCCHHHHHCCCCE		20.5524719451
356UbiquitinationSSILTKHKIIHTGEK
HHHHCCCCEEECCCC		44.93-
360PhosphorylationTKHKIIHTGEKPYKC
CCCCEEECCCCCEEC		36.3129496963
363UbiquitinationKIIHTGEKPYKCEGC
CEEECCCCCEECCCC		55.80-
394SumoylationHAEEKPYKCEECGKA
CCCCCCCCHHHHCCC		43.63-
394SumoylationHAEEKPYKCEECGKA
CCCCCCCCHHHHCCC		43.63-
394UbiquitinationHAEEKPYKCEECGKA
CCCCCCCCHHHHCCC		43.63-
402PhosphorylationCEECGKASNSSSKLM
HHHHCCCCCCCHHHH		40.50-
404PhosphorylationECGKASNSSSKLMEH
HHCCCCCCCHHHHHC		33.23-
405PhosphorylationCGKASNSSSKLMEHK
HCCCCCCCHHHHHCC		35.42-
406PhosphorylationGKASNSSSKLMEHKR
CCCCCCCHHHHHCCC		29.63-
416PhosphorylationMEHKRIHTGEKPYKC
HHCCCCCCCCCCEEC		44.6729496963
419UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCEECHHC		55.80-
421PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEECHHCCC		39.06-
422SumoylationHTGEKPYKCEECGKA
CCCCCCEECHHCCCE		43.63-
422UbiquitinationHTGEKPYKCEECGKA
CCCCCCEECHHCCCE		43.63-
422SumoylationHTGEKPYKCEECGKA
CCCCCCEECHHCCCE		43.63-
449PhosphorylationIHAGEKPYKCEECGK
CCCCCCCEECCCCCC		39.06-
450SumoylationHAGEKPYKCEECGKA
CCCCCCEECCCCCCE		43.63-
450UbiquitinationHAGEKPYKCEECGKA
CCCCCCEECCCCCCE		43.63-
450SumoylationHAGEKPYKCEECGKA
CCCCCCEECCCCCCE		43.63-
463PhosphorylationKAFTWSSSFTKHKRI
CEEECCCCCCCCCCE		31.2724719451
478UbiquitinationHAAEKPYKCEECGKG
EECCCCCCCCCCCCC		43.63-
478SumoylationHAAEKPYKCEECGKG
EECCCCCCCCCCCCC		43.63-
478SumoylationHAAEKPYKCEECGKG
EECCCCCCCCCCCCC		43.63-
490PhosphorylationGKGFSTFSILTKHKI
CCCCCCCHHHHCCCE		19.4424719451
500PhosphorylationTKHKIIHTGEKRYKC
HCCCEEECCCCEEEC		36.3127251275
524UbiquitinationSSILTEHKIIHTGEK
HHHHCCCEEEECCCC		36.80-
528PhosphorylationTEHKIIHTGEKPYKC
CCCEEEECCCCCCCC		36.3129496963
531UbiquitinationKIIHTGEKPYKCEEC
EEEECCCCCCCCHHH		55.80-
533PhosphorylationIHTGEKPYKCEECGK
EECCCCCCCCHHHCC		39.06-
534SumoylationHTGEKPYKCEECGKA
ECCCCCCCCHHHCCC		43.63-
534UbiquitinationHTGEKPYKCEECGKA
ECCCCCCCCHHHCCC		43.63-
534SumoylationHTGEKPYKCEECGKA
ECCCCCCCCHHHCCC		43.63-
556PhosphorylationTRHKRIHTGEKPYKC
CCCCCCCCCCCCEEC		44.6729496963
559UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCEECHHH		55.80-
561PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEECHHHHH		39.06-
562SumoylationHTGEKPYKCEECGKA
CCCCCCEECHHHHHH		43.63-
562UbiquitinationHTGEKPYKCEECGKA
CCCCCCEECHHHHHH		43.63-
562SumoylationHTGEKPYKCEECGKA
CCCCCCEECHHHHHH		43.63-
581UbiquitinationSTVSYHKKIHTGENP
CCEEEECCCCCCCCC		26.80-
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 ZN676_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN676_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 ZN676_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN676_HUMAN !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN676_HUMAN

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Related Literatures of Post-Translational Modification

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