UniProt ID | ZC3HA_HUMAN | |
---|---|---|
UniProt AC | Q96K80 | |
Protein Name | Zinc finger CCCH domain-containing protein 10 | |
Gene Name | ZC3H10 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 434 | |
Subcellular Localization | Nucleus . | |
Protein Description | Specific regulator of miRNA biogenesis. Binds, via the C3H1-type zinc finger domains, to the binding motif 5'-GCAGCGC-3' on microRNA pri-MIR143 and negatively regulates the processing to mature microRNA.. | |
Protein Sequence | MPDRDSYANGTGSSGGGPGGGGSEEASGAGVGSGGASSDAICRDFLRNVCKRGKRCRYRHPDMSEVSNLGVSKNEFIFCHDFQNKECSRPNCRFIHGSKEDEDGYKKTGELPPRLRQKVAAGLGLSPADLPNGKEEVPICRDFLKGDCQRGAKCKFRHLQRDFEFDARGGGGTGGGSTGSVLPGRRHDLYDIYDLPDRGFEDHEPGPKRRRGGCCPPDGPHFESYEYSLAPPRGVECRLLEEENAMLRKRVEELKKQVSNLLATNEVLLEQNAQFRNQAKVITLSSTAPATEQTLAPTVGTVATFNHGIAQTHTTLSSQALQPRPVSQQELVAPAGAPAAPPTNAAPPAAPPPPPPHLTPEITPLSAALAQTIAQGMAPPPVSMAPVAVSVAPVAPVAVSMAQPLAGITMSHTTTPMVTYPIASQSMRITAMPH | |
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 |
---|---|---|---|---|---|
6 | Phosphorylation | --MPDRDSYANGTGS --CCCCCCCCCCCCC | 27.34 | 25278378 | |
7 | Phosphorylation | -MPDRDSYANGTGSS -CCCCCCCCCCCCCC | 14.36 | 22210691 | |
11 | Phosphorylation | RDSYANGTGSSGGGP CCCCCCCCCCCCCCC | 33.43 | 25278378 | |
13 | Phosphorylation | SYANGTGSSGGGPGG CCCCCCCCCCCCCCC | 26.16 | 25278378 | |
14 | Phosphorylation | YANGTGSSGGGPGGG CCCCCCCCCCCCCCC | 42.68 | 22210691 | |
23 | Phosphorylation | GGPGGGGSEEASGAG CCCCCCCCCCCCCCC | 35.22 | 25278378 | |
27 | Phosphorylation | GGGSEEASGAGVGSG CCCCCCCCCCCCCCC | 32.24 | 25278378 | |
33 | Phosphorylation | ASGAGVGSGGASSDA CCCCCCCCCCCCHHH | 31.48 | 25278378 | |
37 | Phosphorylation | GVGSGGASSDAICRD CCCCCCCCHHHHHHH | 31.83 | 25278378 | |
38 | Phosphorylation | VGSGGASSDAICRDF CCCCCCCHHHHHHHH | 30.44 | 22210691 | |
126 | Phosphorylation | VAAGLGLSPADLPNG HHHCCCCCHHHCCCC | 19.08 | 29255136 | |
173 | Phosphorylation | DARGGGGTGGGSTGS ECCCCCCCCCCCCCC | 35.61 | 25159151 | |
177 | Phosphorylation | GGGTGGGSTGSVLPG CCCCCCCCCCCCCCC | 32.63 | 28258704 | |
180 | Phosphorylation | TGGGSTGSVLPGRRH CCCCCCCCCCCCCCC | 22.14 | 28258704 | |
185 | Methylation | TGSVLPGRRHDLYDI CCCCCCCCCCCCCCC | 30.71 | - | |
186 | Methylation | GSVLPGRRHDLYDIY CCCCCCCCCCCCCCC | 33.32 | - | |
190 | Phosphorylation | PGRRHDLYDIYDLPD CCCCCCCCCCCCCCC | 13.32 | - | |
193 | Phosphorylation | RHDLYDIYDLPDRGF CCCCCCCCCCCCCCC | 14.45 | 28796482 | |
227 | Phosphorylation | PHFESYEYSLAPPRG CCCCCEEEECCCCCC | 10.76 | - |
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 ZC3HA_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ZC3HA_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 ZC3HA_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ZC3HA_HUMAN | ZC3H10 | physical | 16189514 | |
DAZP2_HUMAN | DAZAP2 | physical | 19060904 | |
ZC3HA_HUMAN | ZC3H10 | physical | 25416956 | |
PR20E_HUMAN | PRR20A | physical | 25416956 | |
PR20C_HUMAN | PRR20A | physical | 25416956 | |
PR20D_HUMAN | PRR20A | physical | 25416956 | |
PR20B_HUMAN | PRR20A | physical | 25416956 | |
PR20A_HUMAN | PRR20A | physical | 25416956 |
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 |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND MASSSPECTROMETRY. |