ZNF85_HUMAN - dbPTM
ZNF85_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNF85_HUMAN
UniProt AC Q03923
Protein Name Zinc finger protein 85
Gene Name ZNF85
Organism Homo sapiens (Human).
Sequence Length 595
Subcellular Localization Nucleus .
Protein Description May be a transcriptional repressor..
Protein Sequence MGPLTFRDVAIEFSLKEWQCLDTAQRNLYRNVMLENYRNLVFLGITVSKPDLITCLEQGKEAWSMKRHEIMVAKPTVMCSHFAQDLWPEQNIKDSFQKVTLKRYGKCRHENLPLRKGCESMDECKMHKGGCNGLNQCLTATQSKIFQCDKYVKVAHKFSNSNRHEIRHTKKKPFKCTKCGKSFGMISCLTEHSRIHTRVNFYKCEECGKAFNWSSTLTKHKRIHTGEKPYKCEECGKAFNQSSNLIKHKKIHTGEKPYKCEECGKTFNRFSTLTTHKIIHTGEKPYKCKECGKAFNRSSTLTTHRKIHTGEKPYKCEECGKAFKQSSNLTTHKIIHTGEKPYKCKKCGKAFNQSAHLTTHEVIHTGEKPYKCEKCGKAFNHFSHLTTHKIIHTGEKPYKCKECGKAFKHSSTLTKHKIIHTGEKPYKCKECEKAFNQSSKLTEHKKIHTGEKPYECEKCGKAFNQSSNLTRHKKSHTEEKPYKCEECGKGFKWPSTLTIHKIIHTGEKPYKCEECGKAFNQSSKLTKHKKIHTGEKPYTCEECGKAFNQSSNLTKHKRIHTGEKPYKCEECDKAFKWSSVLTKHKIIHTGEKLQI
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
14PhosphorylationRDVAIEFSLKEWQCL
HHHHHEEECCHHHHH
26.2424719451
29PhosphorylationDTAQRNLYRNVMLEN
HHHHHHHHHHHHHHH
12.04-
46PhosphorylationNLVFLGITVSKPDLI
CEEEEEEEECCCCHH
19.5424719451
48PhosphorylationVFLGITVSKPDLITC
EEEEEEECCCCHHHH
29.8024719451
64PhosphorylationEQGKEAWSMKRHEIM
HHCHHHHHHHCCEEE
22.82-
150UbiquitinationSKIFQCDKYVKVAHK
HHHHCCCCHHHHHHH
60.62-
151PhosphorylationKIFQCDKYVKVAHKF
HHHCCCCHHHHHHHC
7.7022817900
203SumoylationHTRVNFYKCEECGKA
HEEECEEECHHHCCC
30.91-
203UbiquitinationHTRVNFYKCEECGKA
HEEECEEECHHHCCC
30.91-
203SumoylationHTRVNFYKCEECGKA
HEEECEEECHHHCCC
30.91-
219UbiquitinationNWSSTLTKHKRIHTG
CCCCCCCCCCCCCCC
50.68-
225PhosphorylationTKHKRIHTGEKPYKC
CCCCCCCCCCCCCCH
44.6729496963
228UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCCCHHHH
55.80-
230PhosphorylationIHTGEKPYKCEECGK
CCCCCCCCCHHHHHH
39.06-
231SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH
43.63-
231SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH
43.63-
231UbiquitinationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH
43.63-
242PhosphorylationCGKAFNQSSNLIKHK
HHHHHHCCCCCCCCC
23.4627251275
250UbiquitinationSNLIKHKKIHTGEKP
CCCCCCCCCCCCCCC
39.17-
253PhosphorylationIKHKKIHTGEKPYKC
CCCCCCCCCCCCEEH
50.9729496963
256UbiquitinationKKIHTGEKPYKCEEC
CCCCCCCCCEEHHHH
55.80-
258PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEEHHHHCC
39.06-
259SumoylationHTGEKPYKCEECGKT
CCCCCCEEHHHHCCC
43.63-
259SumoylationHTGEKPYKCEECGKT
CCCCCCEEHHHHCCC
43.63-
259UbiquitinationHTGEKPYKCEECGKT
CCCCCCEEHHHHCCC
43.63-
265UbiquitinationYKCEECGKTFNRFST
EEHHHHCCCCCCCHH
62.70-
271PhosphorylationGKTFNRFSTLTTHKI
CCCCCCCHHCCCCEE
21.1924719451
272PhosphorylationKTFNRFSTLTTHKII
CCCCCCHHCCCCEEE
25.9724719451
277UbiquitinationFSTLTTHKIIHTGEK
CHHCCCCEEEECCCC
41.06-
281PhosphorylationTTHKIIHTGEKPYKC
CCCEEEECCCCCEEC
36.3129496963
284UbiquitinationKIIHTGEKPYKCKEC
EEEECCCCCEECCCC
55.80-
286PhosphorylationIHTGEKPYKCKECGK
EECCCCCEECCCCCC
39.83-
306UbiquitinationSTLTTHRKIHTGEKP
CCCCCCCCEECCCCC
31.10-
309PhosphorylationTTHRKIHTGEKPYKC
CCCCCEECCCCCCCH
50.9729496963
312UbiquitinationRKIHTGEKPYKCEEC
CCEECCCCCCCHHHH
55.80-
314PhosphorylationIHTGEKPYKCEECGK
EECCCCCCCHHHHHH
39.06-
315SumoylationHTGEKPYKCEECGKA
ECCCCCCCHHHHHHH
43.63-
315UbiquitinationHTGEKPYKCEECGKA
ECCCCCCCHHHHHHH
43.63-
315SumoylationHTGEKPYKCEECGKA
ECCCCCCCHHHHHHH
43.63-
326PhosphorylationCGKAFKQSSNLTTHK
HHHHHHHCCCCCCCE
23.0627732954
327PhosphorylationGKAFKQSSNLTTHKI
HHHHHHCCCCCCCEE
33.1127732954
330PhosphorylationFKQSSNLTTHKIIHT
HHHCCCCCCCEEEEC
30.9827732954
331PhosphorylationKQSSNLTTHKIIHTG
HHCCCCCCCEEEECC
25.0827732954
333UbiquitinationSSNLTTHKIIHTGEK
CCCCCCCEEEECCCC
41.06-
337PhosphorylationTTHKIIHTGEKPYKC
CCCEEEECCCCCCCC
36.3129496963
340UbiquitinationKIIHTGEKPYKCKKC
EEEECCCCCCCCCCC
55.80-
365PhosphorylationTTHEVIHTGEKPYKC
EECCEEECCCCCEEC
35.5929496963
370PhosphorylationIHTGEKPYKCEKCGK
EECCCCCEECCCCCC
39.06-
371AcetylationHTGEKPYKCEKCGKA
ECCCCCEECCCCCCC
44.4330593921
389UbiquitinationFSHLTTHKIIHTGEK
CHHHCCCCEEECCCC
41.06-
393PhosphorylationTTHKIIHTGEKPYKC
CCCCEEECCCCCCCC
36.3129496963
396UbiquitinationKIIHTGEKPYKCKEC
CEEECCCCCCCCCCC
55.80-
398PhosphorylationIHTGEKPYKCKECGK
EECCCCCCCCCCCCC
39.83-
415UbiquitinationKHSSTLTKHKIIHTG
CCCCCCCCCEEEECC
46.11-
417UbiquitinationSSTLTKHKIIHTGEK
CCCCCCCEEEECCCC
44.93-
421PhosphorylationTKHKIIHTGEKPYKC
CCCEEEECCCCCCCC
36.3129496963
424UbiquitinationKIIHTGEKPYKCKEC
EEEECCCCCCCCHHH
55.80-
449PhosphorylationTEHKKIHTGEKPYEC
CCCCCCCCCCCCCCH
50.97-
475PhosphorylationNLTRHKKSHTEEKPY
CCHHCCCCCCCCCCC
40.21-
483SumoylationHTEEKPYKCEECGKG
CCCCCCCCCCCCCCC
43.63-
483UbiquitinationHTEEKPYKCEECGKG
CCCCCCCCCCCCCCC
43.63-
483SumoylationHTEEKPYKCEECGKG
CCCCCCCCCCCCCCC
43.63-
501UbiquitinationPSTLTIHKIIHTGEK
CCEEEEEEEEECCCC
39.23-
505PhosphorylationTIHKIIHTGEKPYKC
EEEEEEECCCCCEEH
36.3129496963
508UbiquitinationKIIHTGEKPYKCEEC
EEEECCCCCEEHHHH
55.80-
510PhosphorylationIHTGEKPYKCEECGK
EECCCCCEEHHHHHH
39.06-
511SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH
43.63-
511UbiquitinationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH
43.63-
511SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH
43.63-
511AcetylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH
43.6319825631
533PhosphorylationTKHKKIHTGEKPYTC
CCCCCCCCCCCCEEH
50.97-
561PhosphorylationTKHKRIHTGEKPYKC
CCCCCCCCCCCCCCC
44.6729496963
564UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCCCCCCC
55.80-
567SumoylationHTGEKPYKCEECDKA
CCCCCCCCCCCCCCC
43.63-
567SumoylationHTGEKPYKCEECDKA
CCCCCCCCCCCCCCC
43.63-
589PhosphorylationTKHKIIHTGEKLQI-
HHCEEEECCCCCCC-
36.3127251275

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 ZNF85_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNF85_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 ZNF85_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CEP76_HUMANCEP76physical
25416956

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZNF85_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP