UniProt ID | EHF_HUMAN | |
---|---|---|
UniProt AC | Q9NZC4 | |
Protein Name | ETS homologous factor | |
Gene Name | EHF {ECO:0000312|HGNC:HGNC:3246} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 300 | |
Subcellular Localization | Nucleus . | |
Protein Description | Transcriptional activator that may play a role in regulating epithelial cell differentiation and proliferation. May act as a repressor for a specific subset of ETS/AP-1-responsive genes and as a modulator of the nuclear response to mitogen-activated protein kinase signaling cascades. Binds to DNA sequences containing the consensus nucleotide core sequence GGAA. Involved in regulation of TNFRSF10B/DR5 expression through Ets-binding sequences on the TNFRSF10B/DR5 promoter. May contribute to development and carcinogenesis by acting as a tumor suppressor gene or anti-oncogene.. | |
Protein Sequence | MILEGGGVMNLNPGNNLLHQPPAWTDSYSTCNVSSGFFGGQWHEIHPQYWTKYQVWEWLQHLLDTNQLDANCIPFQEFDINGEHLCSMSLQEFTRAAGTAGQLLYSNLQHLKWNGQCSSDLFQSTHNVIVKTEQTEPSIMNTWKDENYLYDTNYGSTVDLLDSKTFCRAQISMTTTSHLPVAESPDMKKEQDPPAKCHTKKHNPRGTHLWEFIRDILLNPDKNPGLIKWEDRSEGVFRFLKSEAVAQLWGKKKNNSSMTYEKLSRAMRYYYKREILERVDGRRLVYKFGKNARGWRENEN | |
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 |
---|---|---|---|---|---|
127 | Phosphorylation | DLFQSTHNVIVKTEQ HHHHHCCCEEEEECC | 25.87 | 27642862 | |
148 (in isoform 2) | Phosphorylation | - | 12.46 | 26552605 | |
150 (in isoform 2) | Phosphorylation | - | 15.45 | 26552605 | |
152 (in isoform 2) | Phosphorylation | - | 19.45 | 26552605 | |
154 (in isoform 2) | Phosphorylation | - | 17.97 | 26552605 | |
156 (in isoform 2) | Phosphorylation | - | 18.20 | 26552605 | |
157 (in isoform 2) | Phosphorylation | - | 17.42 | 26552605 | |
161 (in isoform 2) | Phosphorylation | - | 6.38 | 26552605 | |
164 | Acetylation | TVDLLDSKTFCRAQI CEEEECCCCEEEEEE | 45.33 | 20167786 | |
184 | Phosphorylation | SHLPVAESPDMKKEQ CCCCCCCCCCCCCCC | 19.23 | 22617229 | |
188 | Acetylation | VAESPDMKKEQDPPA CCCCCCCCCCCCCCC | 61.61 | 20167786 | |
196 | Acetylation | KEQDPPAKCHTKKHN CCCCCCCCCCCCCCC | 32.11 | 20167786 | |
199 | Phosphorylation | DPPAKCHTKKHNPRG CCCCCCCCCCCCCCC | 51.78 | - | |
206 | Phosphorylation | TKKHNPRGTHLWEFI CCCCCCCCCCHHHHH | 20.81 | 24719451 | |
242 | Phosphorylation | GVFRFLKSEAVAQLW CHHHHHHHHHHHHHH | 32.70 | 22817900 | |
256 | Phosphorylation | WGKKKNNSSMTYEKL HCCCCCCCCCCHHHH | 30.77 | 29083192 | |
257 | Phosphorylation | GKKKNNSSMTYEKLS CCCCCCCCCCHHHHH | 19.78 | 29083192 | |
259 | Phosphorylation | KKNNSSMTYEKLSRA CCCCCCCCHHHHHHH | 30.40 | 29083192 | |
260 | Phosphorylation | KNNSSMTYEKLSRAM CCCCCCCHHHHHHHH | 11.48 | 29759185 | |
262 | Ubiquitination | NSSMTYEKLSRAMRY CCCCCHHHHHHHHHH | 41.15 | - |
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 EHF_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EHF_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 EHF_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
XRCC6_HUMAN | XRCC6 | physical | 15075319 | |
XRCC5_HUMAN | XRCC5 | physical | 15075319 | |
CYTM_HUMAN | CST6 | physical | 26186194 | |
KPRP_HUMAN | KPRP | physical | 26186194 | |
KPRP_HUMAN | KPRP | physical | 28514442 | |
CYTM_HUMAN | CST6 | physical | 28514442 | |
ARGI1_HUMAN | ARG1 | physical | 28514442 |
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 |
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND MASSSPECTROMETRY. |