ZN714_HUMAN - dbPTM
ZN714_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN714_HUMAN
UniProt AC Q96N38
Protein Name Zinc finger protein 714
Gene Name ZNF714
Organism Homo sapiens (Human).
Sequence Length 554
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MNVMLENYKNLVFLAGIAVSKQDPITSLEQEKEPWNMKICEMVDESPAMCSSFTRDLWPEQDIKDSFQQVILRRHGKCEHENLQLRKGSANVVECKVYKKGYELNQCLTTTQSKIFPCDKYIKVFHKIFNSNRHKTRHTGEKPFKCKKCDESFCMLLHLHQHKRIHIRENSYQCEECDKVFKRFSTLTRHKRVHTGEKPFKCEECGKAFKHSSTLTTHKMIHTGEKPYRCEECGKAFYHSSHLTTHKVIHTGEKPFKCEECGKAFNHPSALTTHKFIHVKEKPYKCEECDKAFNRFSYLTKHKIIHSGEKSYKCEQCGKGFNWSSTLTKHKRIHTGEKPYKCEECGKAFNVSSHLTTHKMIHTGEKPYKCEECGKAFNHSSKLTIHKIIHTGEKPYKCEECGKAFNQSSNLTKHKIIHTGEKLYKCEECGKAFNRSSNLTTHKRIHTGEKPYKCEECGKAFNRSSNLTKHNIIHTGEKSYKCEECGKAFNQSSTLTKHRKIQQGMVAHACNPNTLRGLGEQIARSGVQDQPGQHGKTPSLLKIQKFAGCGGRRL
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
100UbiquitinationVECKVYKKGYELNQC
EEEEEEECCEEHHHC		49.27-
139PhosphorylationNRHKTRHTGEKPFKC
CCCCCCCCCCCCCCC		43.3823532336
195PhosphorylationTRHKRVHTGEKPFKC
HCCCCCCCCCCCEEC		31.9923898821
201SumoylationHTGEKPFKCEECGKA
CCCCCCEECHHHHCC		24.38-
201SumoylationHTGEKPFKCEECGKA
CCCCCCEECHHHHCC		24.38-
214PhosphorylationKAFKHSSTLTTHKMI
CCCCCCCCCEECCEE		27.44-
223PhosphorylationTTHKMIHTGEKPYRC
EECCEEECCCCCEEC		25.0729496963
226UbiquitinationKMIHTGEKPYRCEEC
CEEECCCCCEECCHH		52.60-
226SumoylationKMIHTGEKPYRCEEC
CEEECCCCCEECCHH		52.60-
226SumoylationKMIHTGEKPYRCEEC
CEEECCCCCEECCHH		52.60-
251PhosphorylationTTHKVIHTGEKPFKC
CCCCEEECCCCCEEC		30.7018669648
257SumoylationHTGEKPFKCEECGKA
ECCCCCEECCCCCHH		24.38-
257SumoylationHTGEKPFKCEECGKA
ECCCCCEECCCCCHH		24.38-
285SumoylationHVKEKPYKCEECDKA
ECCCCCCCCHHHHHH		39.06-
285SumoylationHVKEKPYKCEECDKA
ECCCCCCCCHHHHHH		39.06-
300PhosphorylationFNRFSYLTKHKIIHS
HHHHHHHHHCCEEEC		5.0824275569
329UbiquitinationNWSSTLTKHKRIHTG
CCCCCCCCCCCCCCC		31.06-
335PhosphorylationTKHKRIHTGEKPYKC
CCCCCCCCCCCCEEC		31.6729496963
338UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCEECCCC		52.60-
340PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEECCCCCC		29.52-
341UbiquitinationHTGEKPYKCEECGKA
CCCCCCEECCCCCCC		39.06-
341SumoylationHTGEKPYKCEECGKA
CCCCCCEECCCCCCC		39.06-
341SumoylationHTGEKPYKCEECGKA
CCCCCCEECCCCCCC		39.06-
363PhosphorylationTTHKMIHTGEKPYKC
CCCCEEECCCCCEEC		25.0729496963
366UbiquitinationKMIHTGEKPYKCEEC
CEEECCCCCEECHHH		52.60-
368PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECHHHHH		29.52-
369SumoylationHTGEKPYKCEECGKA
ECCCCCEECHHHHHC		39.06-
369UbiquitinationHTGEKPYKCEECGKA
ECCCCCEECHHHHHC		39.06-
369SumoylationHTGEKPYKCEECGKA
ECCCCCEECHHHHHC		39.06-
387UbiquitinationSSKLTIHKIIHTGEK
CCCCEEEEEEECCCC		15.27-
391PhosphorylationTIHKIIHTGEKPYKC
EEEEEEECCCCCEEC		31.1529496963
394UbiquitinationKIIHTGEKPYKCEEC
EEEECCCCCEECHHH		52.60-
396PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECHHHHH		29.52-
397UbiquitinationHTGEKPYKCEECGKA
ECCCCCEECHHHHHH		39.06-
397SumoylationHTGEKPYKCEECGKA
ECCCCCEECHHHHHH		39.06-
397SumoylationHTGEKPYKCEECGKA
ECCCCCEECHHHHHH		39.06-
408PhosphorylationCGKAFNQSSNLTKHK
HHHHCCCCCCCCCCC		41.6129083192
409PhosphorylationGKAFNQSSNLTKHKI
HHHCCCCCCCCCCCE		23.4629083192
412PhosphorylationFNQSSNLTKHKIIHT
CCCCCCCCCCCEEEC		7.9329083192
419PhosphorylationTKHKIIHTGEKLYKC
CCCCEEECCCCEEEH		31.1527251275
424PhosphorylationIHTGEKLYKCEECGK
EECCCCEEEHHHHHH		4.26-
425SumoylationHTGEKLYKCEECGKA
ECCCCEEEHHHHHHH		25.35-
425UbiquitinationHTGEKLYKCEECGKA
ECCCCEEEHHHHHHH		25.35-
425SumoylationHTGEKLYKCEECGKA
ECCCCEEEHHHHHHH		25.35-
431UbiquitinationYKCEECGKAFNRSSN
EEHHHHHHHCCCCCC		27.83-
441PhosphorylationNRSSNLTTHKRIHTG
CCCCCCCCCCCEECC		30.9824719451
447PhosphorylationTTHKRIHTGEKPYKC
CCCCCEECCCCCEEH		31.6729496963
450UbiquitinationKRIHTGEKPYKCEEC
CCEECCCCCEEHHHH		52.60-
452PhosphorylationIHTGEKPYKCEECGK
EECCCCCEEHHHHHH		29.52-
453UbiquitinationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		39.06-
453SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		39.06-
453SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		39.06-
459UbiquitinationYKCEECGKAFNRSSN
EEHHHHHHHCCCCCC		27.83-
475PhosphorylationTKHNIIHTGEKSYKC
CCCCEEECCCCEEEH		24.8327251275
478UbiquitinationNIIHTGEKSYKCEEC
CEEECCCCEEEHHHH		39.73-
481SumoylationHTGEKSYKCEECGKA
ECCCCEEEHHHHHHH		30.63-
481SumoylationHTGEKSYKCEECGKA
ECCCCEEEHHHHHHH		30.63-
492PhosphorylationCGKAFNQSSTLTKHR
HHHHHCCCCCCCHHC		32.1029978859
493PhosphorylationGKAFNQSSTLTKHRK
HHHHCCCCCCCHHCH		26.7929978859
494PhosphorylationKAFNQSSTLTKHRKI
HHHCCCCCCCHHCHH		20.0629978859
497UbiquitinationNQSSTLTKHRKIQQG
CCCCCCCHHCHHHCC		25.54-
539PhosphorylationGQHGKTPSLLKIQKF
CCCCCCHHHHHHHHC		26.8524719451
545UbiquitinationPSLLKIQKFAGCGGR
HHHHHHHHCCCCCCC		32.97-
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 ZN714_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN714_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 ZN714_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN714_HUMAN !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN714_HUMAN

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Related Literatures of Post-Translational Modification

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