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 | ||
* 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. |