ZN846_HUMAN - dbPTM
ZN846_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN846_HUMAN
UniProt AC Q147U1
Protein Name Zinc finger protein 846
Gene Name ZNF846
Organism Homo sapiens (Human).
Sequence Length 533
Subcellular Localization Nucleus.
Protein Description May be involved in transcriptional regulation..
Protein Sequence MDSSQHLVTFEDVAVDFTQEEWTLLDQAQRDLYRDVMLENYKNLIILAGSELFKRSLMSGLEQMEELRTGVTGVLQELDLQLKTKGSPLLQDISAERSPNGVQLERSNTAEKLYDSNHSGKVFNEHPFLMTHMITHIGEKTSEDNQSGKALRKNFPHSFYKKSHAEGKMPKCVKHEKAFNQFPNLTRQNKTHTQEKLCECKDCWRTFLNQSSLKLHIRSHNGDKHYVCKECGKAFSNSSHLIGHGRIHSGEKPYVCKECGKAFTQSTGLKLHIRTHSGEKPYKCKECGKAFTHSSYLTDHTRIHSGKKPYVCMECGKAFTRSTGLILHMRIHTGEKPYECKECGKAFIHSSYLTKHVRIHSGEKLYLCKACGKAFTRSSGLVLHMRTHTGEKPYECKECGKAFNNSSMLSQHVRIHTGEKPYECKECGKAFTQSSGLSTHLRTHTGEKACECKECGKAFARSTNLNMHMRTHTGEKPYACKECGKAFRYSTYLNVHTRTHTGAKPYECKKCGKNFTQSSALAKHLRTKACEKT
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
98PhosphorylationQDISAERSPNGVQLE
HHHCCCCCCCCEEEE
17.7718669648
140MethylationMITHIGEKTSEDNQS
HEEECCCCCCCCCHH
52.73-
149MethylationSEDNQSGKALRKNFP
CCCCHHCHHHHHHCC
49.87-
190AcetylationPNLTRQNKTHTQEKL
CCCCCCCCCCCCHHH
33.0930593917
252"N6,N6-dimethyllysine"GRIHSGEKPYVCKEC
CCCCCCCCCEEECCC
45.21-
252MethylationGRIHSGEKPYVCKEC
CCCCCCCCCEEECCC
45.21-
254PhosphorylationIHSGEKPYVCKECGK
CCCCCCCEEECCCCC
29.55-
257"N6,N6-dimethyllysine"GEKPYVCKECGKAFT
CCCCEEECCCCCEEE
46.09-
257MethylationGEKPYVCKECGKAFT
CCCCEEECCCCCEEE
46.09-
261MethylationYVCKECGKAFTQSTG
EEECCCCCEEECCCC
52.57-
261"N6,N6-dimethyllysine"YVCKECGKAFTQSTG
EEECCCCCEEECCCC
52.57-
263UbiquitinationCKECGKAFTQSTGLK
ECCCCCEEECCCCCE
7.9122505724
280UbiquitinationIRTHSGEKPYKCKEC
EEECCCCCCEECCCC
58.11-
310PhosphorylationIHSGKKPYVCMECGK
CCCCCCCEEEEECCC
18.37-
333PhosphorylationILHMRIHTGEKPYEC
EEEEEEECCCCCEEC
44.6729496963
335UbiquitinationHMRIHTGEKPYECKE
EEEEECCCCCEECCC
52.6022505724
341SumoylationGEKPYECKECGKAFI
CCCCEECCCCCCEEE
44.06-
341SumoylationGEKPYECKECGKAFI
CCCCEECCCCCCEEE
44.06-
352PhosphorylationKAFIHSSYLTKHVRI
CEEEEHHHCCCEEEE
22.7725627689
356UbiquitinationHSSYLTKHVRIHSGE
EHHHCCCEEEECCCC
14.6222505724
378UbiquitinationCGKAFTRSSGLVLHM
CCCEEHHCCCEEEEE
26.2122505724
379PhosphorylationGKAFTRSSGLVLHMR
CCEEHHCCCEEEEEE
32.6225332170
387PhosphorylationGLVLHMRTHTGEKPY
CEEEEEEECCCCCCE
19.0629396449
389PhosphorylationVLHMRTHTGEKPYEC
EEEEEECCCCCCEEC
46.5629496963
391UbiquitinationHMRTHTGEKPYECKE
EEEECCCCCCEECCH
52.6022505724
392UbiquitinationMRTHTGEKPYECKEC
EEECCCCCCEECCHH
55.0022505724
397SumoylationGEKPYECKECGKAFN
CCCCEECCHHHHCCC
44.06-
397UbiquitinationGEKPYECKECGKAFN
CCCCEECCHHHHCCC
44.06-
397SumoylationGEKPYECKECGKAFN
CCCCEECCHHHHCCC
44.06-
417PhosphorylationSQHVRIHTGEKPYEC
HHCEEEECCCCCCCC
44.6729496963
425SumoylationGEKPYECKECGKAFT
CCCCCCCCHHHCEEH
44.06-
425SumoylationGEKPYECKECGKAFT
CCCCCCCCHHHCEEH
44.06-
443PhosphorylationGLSTHLRTHTGEKAC
CCCHHCHHCCCCCEE
30.10-
445PhosphorylationSTHLRTHTGEKACEC
CHHCHHCCCCCEEEC
46.56-
471PhosphorylationNLNMHMRTHTGEKPY
CCCEEECCCCCCCCE
19.06-
473PhosphorylationNMHMRTHTGEKPYAC
CEEECCCCCCCCEEH
46.5626074081
476UbiquitinationMRTHTGEKPYACKEC
ECCCCCCCCEEHHHH
44.68-
478PhosphorylationTHTGEKPYACKECGK
CCCCCCCEEHHHHCC
35.3826074081
489PhosphorylationECGKAFRYSTYLNVH
HHCCCEEEECEEEEE
10.0225219547
490PhosphorylationCGKAFRYSTYLNVHT
HCCCEEEECEEEEEC
13.3025219547
491PhosphorylationGKAFRYSTYLNVHTR
CCCEEEECEEEEECC
24.0825219547
492PhosphorylationKAFRYSTYLNVHTRT
CCEEEECEEEEECCC
7.1325219547
497PhosphorylationSTYLNVHTRTHTGAK
ECEEEEECCCCCCCC
32.7425219547
499PhosphorylationYLNVHTRTHTGAKPY
EEEEECCCCCCCCCC
25.5829449344
501PhosphorylationNVHTRTHTGAKPYEC
EEECCCCCCCCCCCC
37.9229449344
518PhosphorylationCGKNFTQSSALAKHL
CCCCCCHHHHHHHHH
17.96-
519PhosphorylationGKNFTQSSALAKHLR
CCCCCHHHHHHHHHH
19.9324719451

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 ZN846_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN846_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 ZN846_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR107_HUMANKRTAP10-7physical
25416956

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 ZN846_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASSSPECTROMETRY.

TOP