ZN257_HUMAN - dbPTM
ZN257_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN257_HUMAN
UniProt AC Q9Y2Q1
Protein Name Zinc finger protein 257
Gene Name ZNF257
Organism Homo sapiens (Human).
Sequence Length 563
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MGPLTIRDVTVEFSLEEWHCLDTAQQNLYRDVMLENYRNLVFLGIAVSKPDLITCLEQGKEPCNMKRHEMVAKPPVMCSHIAEDLCPERDIKYFFQKVILRRYDKCEHENLQLRKGCKSVDECKVCKGGYNGLNQCLITTQSKMYQCDKYVKVFYKFSNSDRHKIRHTEKKTCKCKECGKSFCMLSQLTRHKRIHIRENSHKCEECGKAFNQSSALTRHKMTHTGEKPYKCEECGKAFNRSSHLTQHKVIHTREKPYKCEECGKAFNRSSHITQHKRIHNREKPFKYDECCKAFKWSSALTTLTQHKRIHTGEKPYKCEECGKAFNQSSALTRHKMIHTGEKPFQCEECGKAFNRSSHLTQHKIIHTKEKPYKCEECGKAFNRSSHLTKHKRIHTREKAYKCDEYCKAFNWSSALTTLTQHKIIHTGEKPYKCEECGKAFNRSSYLIRHKIIHTGEKPYKCEECGKAFNQSSHLTQHKIIHTGEKPYKCEECGKAFNRSSHLSQHKIIHTGEKPYKCEECGKPFNRFSYLTVHKRIHAGENPNKYEECGKACNHSSNLTKHNS
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
160UbiquitinationVFYKFSNSDRHKIRH
EEEECCCCCHHHCCC		34.5222505724
188UbiquitinationSFCMLSQLTRHKRIH
HHHHHHHHHHCCCEE		4.0022505724
204UbiquitinationRENSHKCEECGKAFN
CCCCCCHHHHHHHHH		62.2122505724
222PhosphorylationALTRHKMTHTGEKPY
HHHHCCCCCCCCCCC		22.5328348404
224PhosphorylationTRHKMTHTGEKPYKC
HHCCCCCCCCCCCCC		37.5629083192
227UbiquitinationKMTHTGEKPYKCEEC
CCCCCCCCCCCCHHH		55.80-
229PhosphorylationTHTGEKPYKCEECGK
CCCCCCCCCCHHHHH		39.06-
230SumoylationHTGEKPYKCEECGKA
CCCCCCCCCHHHHHC		43.63-
230UbiquitinationHTGEKPYKCEECGKA
CCCCCCCCCHHHHHC		43.63-
230SumoylationHTGEKPYKCEECGKA
CCCCCCCCCHHHHHC		43.63-
232UbiquitinationGEKPYKCEECGKAFN
CCCCCCCHHHHHCCC		52.7722505724
236UbiquitinationYKCEECGKAFNRSSH
CCCHHHHHCCCCCCC		62.5622505724
258SumoylationHTREKPYKCEECGKA
ECCCCCCCCHHHHHH		43.63-
258UbiquitinationHTREKPYKCEECGKA
ECCCCCCCCHHHHHH		43.63-
258SumoylationHTREKPYKCEECGKA
ECCCCCCCCHHHHHH		43.63-
264UbiquitinationYKCEECGKAFNRSSH
CCCHHHHHHCCCCCC		62.5622505724
275UbiquitinationRSSHITQHKRIHNRE
CCCCHHHCCHHCCCC		16.8322505724
297PhosphorylationCCKAFKWSSALTTLT
HHHHHCHHHHHHHHH		13.3126074081
298PhosphorylationCKAFKWSSALTTLTQ
HHHHCHHHHHHHHHC		26.6126074081
301PhosphorylationFKWSSALTTLTQHKR
HCHHHHHHHHHCCCC		21.3426074081
302PhosphorylationKWSSALTTLTQHKRI
CHHHHHHHHHCCCCC		28.7626074081
303UbiquitinationWSSALTTLTQHKRIH
HHHHHHHHHCCCCCC		3.5022505724
304PhosphorylationSSALTTLTQHKRIHT
HHHHHHHHCCCCCCC		26.9126074081
311PhosphorylationTQHKRIHTGEKPYKC
HCCCCCCCCCCCCCH		44.6729496963
314UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCCCHHHH		55.80-
316PhosphorylationIHTGEKPYKCEECGK
CCCCCCCCCHHHHHH		39.06-
317SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
317UbiquitinationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
317SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
319UbiquitinationGEKPYKCEECGKAFN
CCCCCCHHHHHHHCC		52.7722505724
339PhosphorylationTRHKMIHTGEKPFQC
HHCCCCCCCCCCCCC		35.7920068231
347UbiquitinationGEKPFQCEECGKAFN
CCCCCCCHHHHHCCC		45.6022505724
351UbiquitinationFQCEECGKAFNRSSH
CCCHHHHHCCCCCCC		62.5622505724
362UbiquitinationRSSHLTQHKIIHTKE
CCCCCCCCCEEECCC		20.3222505724
373UbiquitinationHTKEKPYKCEECGKA
ECCCCCCCCHHHHHH		43.63-
373SumoylationHTKEKPYKCEECGKA
ECCCCCCCCHHHHHH		43.63-
373SumoylationHTKEKPYKCEECGKA
ECCCCCCCCHHHHHH		43.63-
379UbiquitinationYKCEECGKAFNRSSH
CCCHHHHHHCCCCHH		62.5622505724
406UbiquitinationAYKCDEYCKAFNWSS
HHCHHHHHHHCCHHH		2.1122505724
412PhosphorylationYCKAFNWSSALTTLT
HHHHCCHHHHHHHHH		13.5626074081
413PhosphorylationCKAFNWSSALTTLTQ
HHHCCHHHHHHHHHH		20.9326074081
416PhosphorylationFNWSSALTTLTQHKI
CCHHHHHHHHHHCCE		21.3426074081
417PhosphorylationNWSSALTTLTQHKII
CHHHHHHHHHHCCEE		28.7626074081
418UbiquitinationWSSALTTLTQHKIIH
HHHHHHHHHHCCEEE		3.5022505724
419PhosphorylationSSALTTLTQHKIIHT
HHHHHHHHHCCEEEC		26.9126074081
422UbiquitinationLTTLTQHKIIHTGEK
HHHHHHCCEEECCCC		33.27-
426PhosphorylationTQHKIIHTGEKPYKC
HHCCEEECCCCCCCC		36.3129496963
429UbiquitinationKIIHTGEKPYKCEEC
CEEECCCCCCCCHHH		55.80-
431PhosphorylationIHTGEKPYKCEECGK
EECCCCCCCCHHHHH		39.06-
432SumoylationHTGEKPYKCEECGKA
ECCCCCCCCHHHHHC		43.63-
432AcetylationHTGEKPYKCEECGKA
ECCCCCCCCHHHHHC		43.6319825895
432SumoylationHTGEKPYKCEECGKA
ECCCCCCCCHHHHHC		43.63-
432UbiquitinationHTGEKPYKCEECGKA
ECCCCCCCCHHHHHC		43.63-
438UbiquitinationYKCEECGKAFNRSSY
CCCHHHHHCCCCCHH		62.5622505724
450UbiquitinationSSYLIRHKIIHTGEK
CHHHHEEEEEECCCC		33.24-
454PhosphorylationIRHKIIHTGEKPYKC
HEEEEEECCCCCCCC		36.3129496963
457UbiquitinationKIIHTGEKPYKCEEC
EEEECCCCCCCCHHH		55.80-
459PhosphorylationIHTGEKPYKCEECGK
EECCCCCCCCHHHHH		39.06-
460SumoylationHTGEKPYKCEECGKA
ECCCCCCCCHHHHHH		43.63-
460SumoylationHTGEKPYKCEECGKA
ECCCCCCCCHHHHHH		43.63-
460AcetylationHTGEKPYKCEECGKA
ECCCCCCCCHHHHHH		43.6319825901
460UbiquitinationHTGEKPYKCEECGKA
ECCCCCCCCHHHHHH		43.63-
462UbiquitinationGEKPYKCEECGKAFN
CCCCCCCHHHHHHHC		52.7722505724
478UbiquitinationSSHLTQHKIIHTGEK
CCCCCCCCEEECCCC		33.27-
482PhosphorylationTQHKIIHTGEKPYKC
CCCCEEECCCCCCCC		36.3129496963
485UbiquitinationKIIHTGEKPYKCEEC
CEEECCCCCCCCHHH		55.80-
487PhosphorylationIHTGEKPYKCEECGK
EECCCCCCCCHHHHH		39.06-
488SumoylationHTGEKPYKCEECGKA
ECCCCCCCCHHHHHC		43.63-
488UbiquitinationHTGEKPYKCEECGKA
ECCCCCCCCHHHHHC		43.63-
488SumoylationHTGEKPYKCEECGKA
ECCCCCCCCHHHHHC		43.63-
488AcetylationHTGEKPYKCEECGKA
ECCCCCCCCHHHHHC		43.6319825907
494UbiquitinationYKCEECGKAFNRSSH
CCCHHHHHCCCCCCC		62.5622505724
506UbiquitinationSSHLSQHKIIHTGEK
CCCHHCCCEEECCCC		35.40-
510PhosphorylationSQHKIIHTGEKPYKC
HCCCEEECCCCCEEC		36.3129496963
513UbiquitinationKIIHTGEKPYKCEEC
CEEECCCCCEECCCC		55.80-
515PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECCCCCC		39.06-
516SumoylationHTGEKPYKCEECGKP
ECCCCCEECCCCCCC		43.63-
516AcetylationHTGEKPYKCEECGKP
ECCCCCEECCCCCCC		43.6319825913
516SumoylationHTGEKPYKCEECGKP
ECCCCCEECCCCCCC		43.63-
516UbiquitinationHTGEKPYKCEECGKP
ECCCCCEECCCCCCC		43.63-
531PhosphorylationFNRFSYLTVHKRIHA
CCCCEEEEECCCCCC		16.60-
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 ZN257_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN257_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 ZN257_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN257_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN257_HUMAN

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Related Literatures of Post-Translational Modification

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