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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
55 | Phosphorylation | PVEKKIRSALPTKTV CCHHHHHHCCCCCCE | 37.32 | 21406692 | |
59 | Phosphorylation | KIRSALPTKTVKPVE HHHHCCCCCCEECCC | 39.95 | 21406692 | |
60 | Ubiquitination | IRSALPTKTVKPVEN HHHCCCCCCEECCCC | 49.75 | - | |
61 | Phosphorylation | RSALPTKTVKPVENK HHCCCCCCEECCCCC | 35.92 | 24732914 | |
73 | Phosphorylation | ENKDDDDSIADFLNS CCCCCCCCHHHHHCC | 27.03 | 23927012 | |
80 | Phosphorylation | SIADFLNSDEEEDRV CHHHHHCCCCHHHHH | 48.85 | 23927012 | |
88 | Phosphorylation | DEEEDRVSLQNLKNL CCHHHHHCHHHHHHH | 25.73 | 23927012 | |
88 (in isoform 2) | Phosphorylation | - | 25.73 | 29507054 | |
93 | Ubiquitination | RVSLQNLKNLGESAT HHCHHHHHHHHHHHH | 58.64 | 21890473 | |
123 | Ubiquitination | NLDQGEDKAKLMRAY HCCCCCHHHHHHHHH | 43.02 | 21890473 | |
125 | Ubiquitination | DQGEDKAKLMRAYMQ CCCCHHHHHHHHHHC | 48.86 | 21890473 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ZNHI3_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
HNF4A_HUMAN | HNF4A | physical | 11916906 | |
HECD1_HUMAN | HECTD1 | physical | 26186194 | |
NUFP1_HUMAN | NUFIP1 | physical | 25170085 | |
NUFP1_HUMAN | NUFIP1 | physical | 27594683 | |
NH2L1_HUMAN | NHP2L1 | physical | 27594683 | |
NUFP1_HUMAN | NUFIP1 | physical | 25404746 | |
NUFP1_HUMAN | NUFIP1 | physical | 28561026 | |
PRP19_HUMAN | PRPF19 | physical | 28561026 | |
UBP11_HUMAN | USP11 | physical | 28561026 | |
ZNHI3_HUMAN | ZNHIT3 | physical | 28561026 |
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. |
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Phosphorylation | |
Reference | PubMed |
"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. |