| UniProt ID | RHBT1_HUMAN | |
|---|---|---|
| UniProt AC | O94844 | |
| Protein Name | Rho-related BTB domain-containing protein 1 | |
| Gene Name | RHOBTB1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 696 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MDADMDYERPNVETIKCVVVGDNAVGKTRLICARACNTTLTQYQLLATHVPTVWAIDQYRVCQEVLERSRDVVDEVSVSLRLWDTFGDHHKDRRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVILVGCQLDLRYADLEAVNRARRPLARPIKRGDILPPEKGREVAKELGLPYYETSVFDQFGIKDVFDNAIRAALISRRHLQFWKSHLKKVQKPLLQAPFLPPKAPPPVIKIPECPSMGTNEAACLLDNPLCADVLFILQDQEHIFAHRIYLATSSSKFYDLFLMECEESPNGSEGACEKEKQSRDFQGRILSVDPEEEREEGPPRIPQADQWKSSNKSLVEALGLEAEGAVPETQTLTGWSKGFIGMHREMQVNPISKRMGPMTVVRMDASVQPGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNKEAFMNQEITKAFHVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLDPLELIALANRFCLPHLVALAEQHAVQELTKAATSGVGIDGEVLSYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKREREKEDIALNKHRSRRKWCFWNSSPAVA | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 69 | Phosphorylation | CQEVLERSRDVVDEV HHHHHHHCCCCHHHH | 24.37 | - | |
| 77 | Phosphorylation | RDVVDEVSVSLRLWD CCCHHHHHHEEEEHH | 12.16 | 24719451 | |
| 79 | Phosphorylation | VVDEVSVSLRLWDTF CHHHHHHEEEEHHCC | 10.56 | 24719451 | |
| 97 | Phosphorylation | HKDRRFAYGRSDVVV CCCCCCCCCCCCEEE | 15.45 | 21712546 | |
| 119 | Ubiquitination | PNSLNHVKSMWYPEI CCCCHHHHHHHCHHH | 27.35 | 21906983 | |
| 352 | Phosphorylation | QWKSSNKSLVEALGL HHHHCCHHHHHHHCC | 41.73 | 28348404 | |
| 398 | Phosphorylation | SKRMGPMTVVRMDAS HHCCCCEEEEECCCC | 20.98 | - | |
| 480 | Phosphorylation | NRIKECLSKGTFSDV HHHHHHHHCCCCCCE | 40.47 | 22817900 | |
| 483 | Phosphorylation | KECLSKGTFSDVTFK HHHHHCCCCCCEEEE | 24.57 | 22817900 | |
| 485 | Phosphorylation | CLSKGTFSDVTFKLD HHHCCCCCCEEEEEC | 30.89 | - | |
| 535 | Phosphorylation | LPNINKISMQAVLDY CCCCCHHCHHHHHHH | 13.37 | 22210691 | |
| 542 | Phosphorylation | SMQAVLDYLYTKQLS CHHHHHHHHHHCCCC | 9.46 | - | |
| 544 | Phosphorylation | QAVLDYLYTKQLSPN HHHHHHHHHCCCCCC | 12.98 | 22210691 | |
| 679 | Ubiquitination | KEDIALNKHRSRRKW HHHHCCHHCHHCCCC | 41.04 | - |
| 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 RHBT1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RHBT1_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 RHBT1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CUL3_HUMAN | CUL3 | physical | 18835386 | |
| CUL5_HUMAN | CUL5 | physical | 18835386 | |
| CUL3_HUMAN | CUL3 | physical | 23040068 | |
| LRC41_MOUSE | Lrrc41 | physical | 22709582 | |
| BPIA2_HUMAN | BPIFA2 | physical | 28514442 | |
| CYTT_HUMAN | CST2 | physical | 28514442 | |
| CYTN_HUMAN | CST1 | physical | 28514442 | |
| CYTS_HUMAN | CST4 | physical | 28514442 | |
| IGJ_HUMAN | IGJ | physical | 28514442 | |
| PIGR_HUMAN | PIGR | physical | 28514442 | |
| CSN7A_HUMAN | COPS7A | physical | 28514442 | |
| CYTD_HUMAN | CST5 | 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 |
| "Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480 AND THR-483, ANDMASS SPECTROMETRY. | |