ZNHI3_HUMAN - dbPTM
ZNHI3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNHI3_HUMAN
UniProt AC Q15649
Protein Name Zinc finger HIT domain-containing protein 3
Gene Name ZNHIT3
Organism Homo sapiens (Human).
Sequence Length 155
Subcellular Localization Cytoplasm . Nucleus .
Protein Description
Protein Sequence MASLKCSTVVCVICLEKPKYRCPACRVPYCSVVCFRKHKEQCNPETRPVEKKIRSALPTKTVKPVENKDDDDSIADFLNSDEEEDRVSLQNLKNLGESATLRSLLLNPHLRQLMVNLDQGEDKAKLMRAYMQEPLFVEFADCCLGIVEPSQNEES
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
55PhosphorylationPVEKKIRSALPTKTV
CCHHHHHHCCCCCCE
37.3221406692
59PhosphorylationKIRSALPTKTVKPVE
HHHHCCCCCCEECCC
39.9521406692
60UbiquitinationIRSALPTKTVKPVEN
HHHCCCCCCEECCCC
49.75-
61PhosphorylationRSALPTKTVKPVENK
HHCCCCCCEECCCCC
35.9224732914
73PhosphorylationENKDDDDSIADFLNS
CCCCCCCCHHHHHCC
27.0323927012
80PhosphorylationSIADFLNSDEEEDRV
CHHHHHCCCCHHHHH
48.8523927012
88PhosphorylationDEEEDRVSLQNLKNL
CCHHHHHCHHHHHHH
25.7323927012
88 (in isoform 2)Phosphorylation-25.7329507054
93UbiquitinationRVSLQNLKNLGESAT
HHCHHHHHHHHHHHH
58.6421890473
123UbiquitinationNLDQGEDKAKLMRAY
HCCCCCHHHHHHHHH
43.0221890473
125UbiquitinationDQGEDKAKLMRAYMQ
CCCCHHHHHHHHHHC
48.8621890473

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 ZNHI3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNHI3_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 ZNHI3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HNF4A_HUMANHNF4Aphysical
11916906
HECD1_HUMANHECTD1physical
26186194
NUFP1_HUMANNUFIP1physical
25170085
NUFP1_HUMANNUFIP1physical
27594683
NH2L1_HUMANNHP2L1physical
27594683
NUFP1_HUMANNUFIP1physical
25404746
NUFP1_HUMANNUFIP1physical
28561026
PRP19_HUMANPRPF19physical
28561026
UBP11_HUMANUSP11physical
28561026
ZNHI3_HUMANZNHIT3physical
28561026

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 ZNHI3_HUMAN

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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-80, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASSSPECTROMETRY.

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