ZN107_HUMAN - dbPTM
ZN107_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN107_HUMAN
UniProt AC Q9UII5
Protein Name Zinc finger protein 107
Gene Name ZNF107
Organism Homo sapiens (Human).
Sequence Length 783
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MVAKPPVMSFHFAQDLWPEQNIKDSFQKVTLRRYGKCEYENLQLRKGCKHVDECTGHKGGHNTVNQCLTATPSKIFQCNKYVKVFDKFSNSNRYKRRHTGNKHFKCKECSKSFCVLSQLTQHRRIHTRVNSYKCEECGKAFNWFSTLTKHKRIHTGEKPYKCEECGKAFNQSSQLTRHKIIHTEEKPNKCEECGKAFKQASHLTIHKIIHTGEKPYKYEECGKVFSQSSHLTTQKILHTGENLYKCKECGKAFNLFSNLTNHKRIHAGEKPYKCKECGRAFNISSNLNKQEKIHTGGKLNKCEECDKAFNRSLKLTAHKKILMEEKPYKCEECGKVFNQFSTLTRHKIIHTGEKPYKCKECGKAFNQSSNLTEHKKIHTAEKSYKCEECGKAFNQHSNLINHRKIYSGEKPYKCEECGKAFNRSSTLTRHKKIHTGEKPYKCEECDRAFSQSSNLTEHKKIHTGEKPYKCEECGKAFNRFSTLTKHKRIHTGEKPYKCEECGKAFNQSYQLTRHKIVHTKEKLNKCEEFGKAFKQSSHRTIHKIIHTGEKPYKCEEHGKVFNQSSNLTTQKIIHTGENLYKFEEHGKAFNLFSNITNHKIIYTGEKPHKCEECGKAYNRFSNLTIHKRIHTGEKPYQCAECGKAFNCSSTLNRHKIIHTGEKPYKCKECGKAFNLSSTLTAHKKIHTGEKPYKCEECGKAFNQSSNLTTHKKIHTSEKPYKCEECGKSFNQFSSLNIHKIIHTGEKPYKCGDYGRAFNLSSNLTTHKKIHTGEKPYKCEYGKT
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
28UbiquitinationNIKDSFQKVTLRRYG
CCCHHHHHHHHHHHC		34.87-
36UbiquitinationVTLRRYGKCEYENLQ
HHHHHHCCCCHHCEE		18.24-
58UbiquitinationVDECTGHKGGHNTVN
CHHHCCCCCCCCCHH		68.85-
71PhosphorylationVNQCLTATPSKIFQC
HHHHCCCCHHHHEEC		23.9025159151
74UbiquitinationCLTATPSKIFQCNKY
HCCCCHHHHEECCCC		49.06-
80UbiquitinationSKIFQCNKYVKVFDK
HHHEECCCCCHHHHC		60.07-
83UbiquitinationFQCNKYVKVFDKFSN
EECCCCCHHHHCCCC		33.81-
87UbiquitinationKYVKVFDKFSNSNRY
CCCHHHHCCCCCCCC		38.95-
89PhosphorylationVKVFDKFSNSNRYKR
CHHHHCCCCCCCCCC		45.1224719451
99PhosphorylationNRYKRRHTGNKHFKC
CCCCCCCCCCCCEEC		40.4123532336
127PhosphorylationTQHRRIHTRVNSYKC
HHHCCHHHHHHCEEH		33.66-
131PhosphorylationRIHTRVNSYKCEECG
CHHHHHHCEEHHHHH		24.10-
132PhosphorylationIHTRVNSYKCEECGK
HHHHHHCEEHHHHHH		17.91-
133SumoylationHTRVNSYKCEECGKA
HHHHHCEEHHHHHHH		34.68-
133SumoylationHTRVNSYKCEECGKA
HHHHHCEEHHHHHHH		34.68-
133UbiquitinationHTRVNSYKCEECGKA
HHHHHCEEHHHHHHH		34.68-
149UbiquitinationNWFSTLTKHKRIHTG
CHHHHHHCCCCCCCC		50.68-
155PhosphorylationTKHKRIHTGEKPYKC
HCCCCCCCCCCCCCH		44.6729496963
158UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCCCHHHH		55.80-
160PhosphorylationIHTGEKPYKCEECGK
CCCCCCCCCHHHHHH		39.06-
161SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
161SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
161UbiquitinationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
167UbiquitinationYKCEECGKAFNQSSQ
CCHHHHHHHCCCCCC		62.56-
186SumoylationKIIHTEEKPNKCEEC
CEECCCCCCCCHHHH		47.89-
186SumoylationKIIHTEEKPNKCEEC
CEECCCCCCCCHHHH		47.8928112733
186UbiquitinationKIIHTEEKPNKCEEC
CEECCCCCCCCHHHH		47.89-
189UbiquitinationHTEEKPNKCEECGKA
CCCCCCCCHHHHHHH		52.10-
198UbiquitinationEECGKAFKQASHLTI
HHHHHHHHHHHHCEE		50.22-
207UbiquitinationASHLTIHKIIHTGEK
HHHCEEEEEHHCCCC		39.23-
211PhosphorylationTIHKIIHTGEKPYKY
EEEEEHHCCCCCCCH		36.3129496963
214UbiquitinationKIIHTGEKPYKYEEC
EEHHCCCCCCCHHHH		55.80-
217UbiquitinationHTGEKPYKYEECGKV
HCCCCCCCHHHHCCC		55.50-
223UbiquitinationYKYEECGKVFSQSSH
CCHHHHCCCCCCCCC		52.33-
226PhosphorylationEECGKVFSQSSHLTT
HHHCCCCCCCCCCCH		31.9421712546
312PhosphorylationCDKAFNRSLKLTAHK
HHHHHHHHHHHHHCH		30.84-
329SumoylationLMEEKPYKCEECGKV
HHCCCCCCHHHHHHH		43.63-
329SumoylationLMEEKPYKCEECGKV
HHCCCCCCHHHHHHH		43.63-
329UbiquitinationLMEEKPYKCEECGKV
HHCCCCCCHHHHHHH		43.63-
347UbiquitinationFSTLTRHKIIHTGEK
HHHHHCCEEEECCCC		39.81-
351PhosphorylationTRHKIIHTGEKPYKC
HCCEEEECCCCCCCC		36.3129496963
354UbiquitinationKIIHTGEKPYKCKEC
EEEECCCCCCCCCHH		55.80-
356PhosphorylationIHTGEKPYKCKECGK
EECCCCCCCCCHHHH		39.83-
363UbiquitinationYKCKECGKAFNQSSN
CCCCHHHHHHCCCCC		62.56-
368PhosphorylationCGKAFNQSSNLTEHK
HHHHHCCCCCCHHCC		23.4630622161
369PhosphorylationGKAFNQSSNLTEHKK
HHHHCCCCCCHHCCH		26.5430622161
372PhosphorylationFNQSSNLTEHKKIHT
HCCCCCCHHCCHHHH		40.0530622161
382UbiquitinationKKIHTAEKSYKCEEC
CHHHHCHHHCCHHHH		57.53-
385SumoylationHTAEKSYKCEECGKA
HHCHHHCCHHHHHHH		42.11-
385SumoylationHTAEKSYKCEECGKA
HHCHHHCCHHHHHHH		42.11-
413SumoylationYSGEKPYKCEECGKA
CCCCCCCCHHHHHHC		43.63-
413SumoylationYSGEKPYKCEECGKA
CCCCCCCCHHHHHHC		43.63-
413UbiquitinationYSGEKPYKCEECGKA
CCCCCCCCHHHHHHC		43.63-
419UbiquitinationYKCEECGKAFNRSST
CCHHHHHHCCCCCCC		62.56-
432UbiquitinationSTLTRHKKIHTGEKP
CCCCCCCCCCCCCCC		33.33-
435PhosphorylationTRHKKIHTGEKPYKC
CCCCCCCCCCCCCCH		50.9729496963
438UbiquitinationKKIHTGEKPYKCEEC
CCCCCCCCCCCHHHH		55.80-
460UbiquitinationSNLTEHKKIHTGEKP
CCCCCCCCCCCCCCC		41.44-
463PhosphorylationTEHKKIHTGEKPYKC
CCCCCCCCCCCCCCH		50.9729496963
466UbiquitinationKKIHTGEKPYKCEEC
CCCCCCCCCCCHHHH		55.80-
468PhosphorylationIHTGEKPYKCEECGK
CCCCCCCCCHHHHHH		39.06-
469SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
469SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
469UbiquitinationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
475UbiquitinationYKCEECGKAFNRFST
CCHHHHHHHHHHHHH		62.56-
485UbiquitinationNRFSTLTKHKRIHTG
HHHHHHCCCCCCCCC		50.68-
491PhosphorylationTKHKRIHTGEKPYKC
CCCCCCCCCCCCEEH		44.6729496963
494UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCEEHHHH		55.80-
496PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEEHHHHHH		39.06-
497SumoylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
497SumoylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
497UbiquitinationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
525UbiquitinationHTKEKLNKCEEFGKA
CCHHHHHHHHHHHHH		54.16-
531UbiquitinationNKCEEFGKAFKQSSH
HHHHHHHHHHHHCCC		56.84-
543UbiquitinationSSHRTIHKIIHTGEK
CCCCHHHHHHHCCCC		39.23-
547PhosphorylationTIHKIIHTGEKPYKC
HHHHHHHCCCCCEEC		36.3129496963
550UbiquitinationKIIHTGEKPYKCEEH
HHHHCCCCCEECCCC		55.80-
552PhosphorylationIHTGEKPYKCEEHGK
HHCCCCCEECCCCCC		39.0626657352
553AcetylationHTGEKPYKCEEHGKV
HCCCCCEECCCCCCE		43.6319825873
553UbiquitinationHTGEKPYKCEEHGKV
HCCCCCEECCCCCCE		43.63-
559UbiquitinationYKCEEHGKVFNQSSN
EECCCCCCEEECCCC		45.63-
571UbiquitinationSSNLTTQKIIHTGEN
CCCCCEEEEEECCCC		41.35-
581UbiquitinationHTGENLYKFEEHGKA
ECCCCEEEHHHHCHH		49.84-
599UbiquitinationFSNITNHKIIYTGEK
CCCCCCCEEEECCCC		32.63-
606UbiquitinationKIIYTGEKPHKCEEC
EEEECCCCCCCCCHH		54.49-
609UbiquitinationYTGEKPHKCEECGKA
ECCCCCCCCCHHHHH		52.44-
631PhosphorylationTIHKRIHTGEKPYQC
EEECCCCCCCCCEEE		44.6728111955
634UbiquitinationKRIHTGEKPYQCAEC
CCCCCCCCCEEECCC		50.82-
643UbiquitinationYQCAECGKAFNCSST
EEECCCCCCCCCCCC		62.56-
655UbiquitinationSSTLNRHKIIHTGEK
CCCCCCCCEEECCCC		39.87-
659PhosphorylationNRHKIIHTGEKPYKC
CCCCEEECCCCCEEC		36.3129496963
662UbiquitinationKIIHTGEKPYKCKEC
CEEECCCCCEECCCC		55.80-
664PhosphorylationIHTGEKPYKCKECGK
EECCCCCEECCCCCC		39.83-
684UbiquitinationSTLTAHKKIHTGEKP
CHHCCCCCCCCCCCC		29.83-
687PhosphorylationTAHKKIHTGEKPYKC
CCCCCCCCCCCCEEH		50.9729496963
690UbiquitinationKKIHTGEKPYKCEEC
CCCCCCCCCEEHHHH		55.80-
692PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEEHHHHHH		39.06-
693SumoylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
693SumoylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
693UbiquitinationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
704PhosphorylationCGKAFNQSSNLTTHK
HHHHCCCCCCCCCCC		23.46-
721SumoylationHTSEKPYKCEECGKS
CCCCCCCCCHHHCCC		43.63-
721SumoylationHTSEKPYKCEECGKS
CCCCCCCCCHHHCCC		43.63-
721UbiquitinationHTSEKPYKCEECGKS
CCCCCCCCCHHHCCC		43.63-
739UbiquitinationFSSLNIHKIIHTGEK
CCCCCEEEEEECCCC		39.29-
743PhosphorylationNIHKIIHTGEKPYKC
CEEEEEECCCCCEEC		36.3129496963
746UbiquitinationKIIHTGEKPYKCGDY
EEEECCCCCEECCCC		55.80-
767AcetylationSSNLTTHKKIHTGEK
CCCCCCCCCCCCCCC		51.8625953088
768UbiquitinationSNLTTHKKIHTGEKP
CCCCCCCCCCCCCCC		31.92-
771PhosphorylationTTHKKIHTGEKPYKC
CCCCCCCCCCCCCCC		50.9729496963
777SumoylationHTGEKPYKCEYGKT-
CCCCCCCCCCCCCC-		29.17-
777SumoylationHTGEKPYKCEYGKT-
CCCCCCCCCCCCCC-		29.17-
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 ZN107_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN107_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 ZN107_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN107_HUMAN !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN107_HUMAN

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Related Literatures of Post-Translational Modification

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