UniProt ID | NR2E1_HUMAN | |
---|---|---|
UniProt AC | Q9Y466 | |
Protein Name | Nuclear receptor subfamily 2 group E member 1 | |
Gene Name | NR2E1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 385 | |
Subcellular Localization | Nucleus . | |
Protein Description | Orphan receptor that binds DNA as a monomer to hormone response elements (HRE) containing an extended core motif half-site sequence 5'-AAGGTCA-3' in which the 5' flanking nucleotides participate in determining receptor specificity (By similarity). May be required to pattern anterior brain differentiation. Involved in the regulation of retinal development and essential for vision. During retinogenesis, regulates PTEN-Cyclin D expression via binding to the promoter region of PTEN and suppressing its activity (By similarity). May be involved in retinoic acid receptor (RAR) regulation in retinal cells.. | |
Protein Sequence | MSKPAGSTSRILDIPCKVCGDRSSGKHYGVYACDGCSGFFKRSIRRNRTYVCKSGNQGGCPVDKTHRNQCRACRLKKCLEVNMNKDAVQHERGPRTSTIRKQVALYFRGHKEENGAAAHFPSAALPAPAFFTAVTQLEPHGLELAAVSTTPERQTLVSLAQPTPKYPHEVNGTPMYLYEVATESVCESAARLLFMSIKWAKSVPAFSTLSLQDQLMLLEDAWRELFVLGIAQWAIPVDANTLLAVSGMNGDNTDSQKLNKIISEIQALQEVVARFRQLRLDATEFACLKCIVTFKAVPTHSGSELRSFRNAAAIAALQDEAQLTLNSYIHTRYPTQPCRFGKLLLLLPALRSISPSTIEEVFFKKTIGNVPITRLLSDMYKSSDI | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSKPAGSTS ------CCCCCCCCC | 47.55 | 30631047 | |
7 | Phosphorylation | -MSKPAGSTSRILDI -CCCCCCCCCEEEEE | 25.89 | 21955146 | |
9 | Phosphorylation | SKPAGSTSRILDIPC CCCCCCCCEEEEEEE | 21.01 | - | |
202 | Phosphorylation | MSIKWAKSVPAFSTL HHHHHHHCCCCCEEC | 26.11 | 30206219 | |
207 | Phosphorylation | AKSVPAFSTLSLQDQ HHCCCCCEECCHHHH | 30.46 | 30206219 | |
208 | Phosphorylation | KSVPAFSTLSLQDQL HCCCCCEECCHHHHH | 17.57 | 30206219 | |
210 | Phosphorylation | VPAFSTLSLQDQLML CCCCEECCHHHHHHH | 24.87 | 30206219 | |
299 | Phosphorylation | VTFKAVPTHSGSELR EEEEECCCCCCHHHH | 23.29 | 28348404 | |
301 | Phosphorylation | FKAVPTHSGSELRSF EEECCCCCCHHHHHH | 46.63 | 18187866 | |
357 | Phosphorylation | LRSISPSTIEEVFFK HHCCCHHHHHHHHCH | 35.47 | - |
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 NR2E1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NR2E1_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 NR2E1_HUMAN !! |
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-301, AND MASSSPECTROMETRY. |