ZN675_HUMAN - dbPTM
ZN675_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN675_HUMAN
UniProt AC Q8TD23
Protein Name Zinc finger protein 675
Gene Name ZNF675
Organism Homo sapiens (Human).
Sequence Length 568
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation. May play a role during osteoclast differentiation by modulating TRAF6 signaling activity..
Protein Sequence MGLLTFRDVAIEFSLEEWQCLDTAQRNLYKNVILENYRNLVFLGIAVSKQDLITCLEQEKEPLTVKRHEMVNEPPVMCSHFAQEFWPEQNIKDSFEKVTLRRYEKCGNDNFQLKGCKSVDECKLHKGGYNGLNQCLPTMQSKMFQCDKYVKVFNKFSHSDRHKIKHMENKPFKCKECGRSFCMLSHLTRHERNYTKVNFCKCEECEKAVNQSSKLTKHKRIYTCEKLYKCQECDRTFNQFSNLTEYKKDYAREKPYKCEECGKAFNQSSHLTTHKIIHTGEKPYKCEECGKAFNQFSNLTTHKKIHTGEQPYICEECGKAFTQSSTLTTHKRIHTGEKPYKCEECGKAFNRSSKLTEHKNIHTGEQPYKCEECGKAFNRSSNLTEHRKIHTEEKPYKCKECGKAFKHSSALTTHKRIHTGEKPYKCEECGKAFNRSSKLTEHKKLHTGKKPYKCEECGKAFIQSSKLTEHKKIHSGEIPYKCEECGKAFKHSSSLTTHKRIHTGEKPYKCEECGKAFSRSSKLTEHKIIHTGEKPYKCERCDKAFNQSANLTKHKKIHTGEKLQNWNV
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
30UbiquitinationTAQRNLYKNVILENY
HHHHHHHHHHHHHHH		48.15-
60UbiquitinationITCLEQEKEPLTVKR
HHHHHHCCCCCEEEC		65.4129967540
66UbiquitinationEKEPLTVKRHEMVNE
CCCCCEEECHHHCCC		42.6829967540
103PhosphorylationEKVTLRRYEKCGNDN
HHHHHHHHHHHCCCC		17.2029978859
105UbiquitinationVTLRRYEKCGNDNFQ
HHHHHHHHHCCCCCE		38.21-
155UbiquitinationKYVKVFNKFSHSDRH
HHHHHHHHCCCHHHH		36.46-
180PhosphorylationKCKECGRSFCMLSHL
CCCCCCCHHHHHHHH		14.21-
185PhosphorylationGRSFCMLSHLTRHER
CCHHHHHHHHHHHCC		6.92-
194PhosphorylationLTRHERNYTKVNFCK
HHHHCCCCCEECEEC		17.7329978859
195PhosphorylationTRHERNYTKVNFCKC
HHHCCCCCEECEECH		31.8729978859
201UbiquitinationYTKVNFCKCEECEKA
CCEECEECHHHHHHH		40.31-
226UbiquitinationKRIYTCEKLYKCQEC
CCEEEHHHHHHCHHC		60.30-
257SumoylationYAREKPYKCEECGKA
HHHCCCCCHHHHHHH		43.63-
257UbiquitinationYAREKPYKCEECGKA
HHHCCCCCHHHHHHH		43.63-
257SumoylationYAREKPYKCEECGKA
HHHCCCCCHHHHHHH		43.63-
271UbiquitinationAFNQSSHLTTHKIIH
HCCCCCCCCCCEEEE		6.8022505724
275UbiquitinationSSHLTTHKIIHTGEK
CCCCCCCEEEECCCC		41.06-
279PhosphorylationTTHKIIHTGEKPYKC
CCCEEEECCCCCEEH		36.3129496963
282UbiquitinationKIIHTGEKPYKCEEC
EEEECCCCCEEHHHH		55.80-
284PhosphorylationIHTGEKPYKCEECGK
EECCCCCEEHHHHHH		39.06-
285AcetylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		43.6319825781
285SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		43.63-
285UbiquitinationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		43.63-
285SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		43.63-
299UbiquitinationAFNQFSNLTTHKKIH
HHHHHCCCCCCCCCC		5.9122505724
324PhosphorylationCGKAFTQSSTLTTHK
HCCCCCCCCCCCCCC		23.41-
325PhosphorylationGKAFTQSSTLTTHKR
CCCCCCCCCCCCCCC		20.02-
328PhosphorylationFTQSSTLTTHKRIHT
CCCCCCCCCCCCEEC		27.26-
329PhosphorylationTQSSTLTTHKRIHTG
CCCCCCCCCCCEECC		28.6324719451
335PhosphorylationTTHKRIHTGEKPYKC
CCCCCEECCCCCCCH		44.6729496963
338UbiquitinationKRIHTGEKPYKCEEC
CCEECCCCCCCHHHH		55.80-
340PhosphorylationIHTGEKPYKCEECGK
EECCCCCCCHHHHHH		39.06-
341SumoylationHTGEKPYKCEECGKA
ECCCCCCCHHHHHHH		43.63-
341UbiquitinationHTGEKPYKCEECGKA
ECCCCCCCHHHHHHH		43.63-
341SumoylationHTGEKPYKCEECGKA
ECCCCCCCHHHHHHH		43.63-
347UbiquitinationYKCEECGKAFNRSSK
CCHHHHHHHCCCCCC		62.5622505724
355UbiquitinationAFNRSSKLTEHKNIH
HCCCCCCCCCCCCCC		7.9922505724
363PhosphorylationTEHKNIHTGEQPYKC
CCCCCCCCCCCCCCH		38.32-
369SumoylationHTGEQPYKCEECGKA
CCCCCCCCHHHHHHH		41.68-
369SumoylationHTGEQPYKCEECGKA
CCCCCCCCHHHHHHH		41.68-
369UbiquitinationHTGEQPYKCEECGKA
CCCCCCCCHHHHHHH		41.68-
375UbiquitinationYKCEECGKAFNRSSN
CCHHHHHHHCCCCCC		62.5622505724
406SumoylationKECGKAFKHSSALTT
CHHHHHHCCCCCCCC		47.65-
406SumoylationKECGKAFKHSSALTT
CHHHHHHCCCCCCCC		47.65-
413PhosphorylationKHSSALTTHKRIHTG
CCCCCCCCCCCCCCC		26.6724719451
419PhosphorylationTTHKRIHTGEKPYKC
CCCCCCCCCCCCCCH		44.6729496963
422UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCCCHHHH		55.80-
424PhosphorylationIHTGEKPYKCEECGK
CCCCCCCCCHHHHHH		39.06-
425SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
425UbiquitinationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
425SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
431UbiquitinationYKCEECGKAFNRSSK
CCHHHHHHHCCCCCC		62.5622505724
447PhosphorylationTEHKKLHTGKKPYKC
CCCCCCCCCCCCCCC		62.2226074081
452PhosphorylationLHTGKKPYKCEECGK
CCCCCCCCCCHHHHH		36.8326074081
453UbiquitinationHTGKKPYKCEECGKA
CCCCCCCCCHHHHHH		43.63-
453SumoylationHTGKKPYKCEECGKA
CCCCCCCCCHHHHHH		43.63-
453SumoylationHTGKKPYKCEECGKA
CCCCCCCCCHHHHHH		43.63-
464PhosphorylationCGKAFIQSSKLTEHK
HHHHHHHHCCCCCCC		25.3226074081
465PhosphorylationGKAFIQSSKLTEHKK
HHHHHHHCCCCCCCC		18.4726074081
466SumoylationKAFIQSSKLTEHKKI
HHHHHHCCCCCCCCC		65.75-
466SumoylationKAFIQSSKLTEHKKI
HHHHHHCCCCCCCCC		65.75-
468PhosphorylationFIQSSKLTEHKKIHS
HHHHCCCCCCCCCCC		39.5226074081
475PhosphorylationTEHKKIHSGEIPYKC
CCCCCCCCCCCCEEH		41.4125159151
481SumoylationHSGEIPYKCEECGKA
CCCCCCEEHHHHCHH		29.80-
481SumoylationHSGEIPYKCEECGKA
CCCCCCEEHHHHCHH		29.80-
481UbiquitinationHSGEIPYKCEECGKA
CCCCCCEEHHHHCHH		29.80-
494PhosphorylationKAFKHSSSLTTHKRI
HHHCCCCCCCCCCCE		32.52-
497PhosphorylationKHSSSLTTHKRIHTG
CCCCCCCCCCCEECC		30.6024719451
503PhosphorylationTTHKRIHTGEKPYKC
CCCCCEECCCCCCCC		44.6729496963
506UbiquitinationKRIHTGEKPYKCEEC
CCEECCCCCCCCHHH		55.80-
508PhosphorylationIHTGEKPYKCEECGK
EECCCCCCCCHHHHH		39.06-
509SumoylationHTGEKPYKCEECGKA
ECCCCCCCCHHHHHC		43.63-
509UbiquitinationHTGEKPYKCEECGKA
ECCCCCCCCHHHHHC		43.63-
509SumoylationHTGEKPYKCEECGKA
ECCCCCCCCHHHHHC		43.63-
527UbiquitinationSSKLTEHKIIHTGEK
CCCCCCCEEEECCCC		36.80-
531PhosphorylationTEHKIIHTGEKPYKC
CCCEEEECCCCCCCC		36.3129496963
534UbiquitinationKIIHTGEKPYKCERC
EEEECCCCCCCCCCC		55.80-
537AcetylationHTGEKPYKCERCDKA
ECCCCCCCCCCCHHH		37.8419825787
559PhosphorylationTKHKKIHTGEKLQNW
CCCCCCCCCCCCCCC		50.97-
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 ZN675_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN675_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 ZN675_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAF6_HUMANTRAF6physical
11751921
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN675_HUMAN

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Related Literatures of Post-Translational Modification

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