UniProt ID | FBW1A_HUMAN | |
---|---|---|
UniProt AC | Q9Y297 | |
Protein Name | F-box/WD repeat-containing protein 1A | |
Gene Name | BTRC | |
Organism | Homo sapiens (Human). | |
Sequence Length | 605 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds to phosphorylated target proteins. [PubMed: 10066435] | |
Protein Sequence | MDPAEAVLQEKALKFMCSMPRSLWLGCSSLADSMPSLRCLYNPGTGALTAFQNSSEREDCNNGEPPRKIIPEKNSLRQTYNSCARLCLNQETVCLASTAMKTENCVAKTKLANGTSSMIVPKQRKLSASYEKEKELCVKYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVRTDSLWRGLAERRGWGQYLFKNKPPDGNAPPNSFYRALYPKIIQDIETIESNWRCGRHSLQRIHCRSETSKGVYCLQYDDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQYDERVIITGSSDSTVRVWDVNTGEMLNTLIHHCEAVLHLRFNNGMMVTCSKDRSIAVWDMASPTDITLRRVLVGHRAAVNVVDFDDKYIVSASGDRTIKVWNTSTCEFVRTLNGHKRGIACLQYRDRLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRFDNKRIVSGAYDGKIKVWDLVAALDPRAPAGTLCLRTLVEHSGRVFRLQFDEFQIVSSSHDDTILIWDFLNDPAAQAEPPRSPSRTYTYISR | |
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 |
---|---|---|---|---|---|
11 | Ubiquitination | AEAVLQEKALKFMCS HHHHHHHHHHHHHHC | 46.16 | - | |
14 | Ubiquitination | VLQEKALKFMCSMPR HHHHHHHHHHHCCCC | 35.59 | - | |
36 | Phosphorylation | SLADSMPSLRCLYNP HHHHHCCCCEEEECC | 21.58 | 24719451 | |
73 | Ubiquitination | PRKIIPEKNSLRQTY CCCCCCCCCCHHHHH | 46.62 | - | |
127 | Phosphorylation | VPKQRKLSASYEKEK CCCCCCCCCCHHHHH | 20.43 | 25849741 | |
129 | Phosphorylation | KQRKLSASYEKEKEL CCCCCCCCHHHHHHH | 30.37 | 23927012 | |
130 | Phosphorylation | QRKLSASYEKEKELC CCCCCCCHHHHHHHH | 30.64 | 28102081 | |
235 | Phosphorylation | LIERMVRTDSLWRGL HHHHHHHCCCHHHHH | 20.66 | 28060719 | |
237 | Phosphorylation | ERMVRTDSLWRGLAE HHHHHCCCHHHHHHH | 29.26 | 24719451 | |
315 | Ubiquitination | CLQYDDQKIVSGLRD EEEECCEEEECCCCC | 52.66 | - | |
326 | Ubiquitination | GLRDNTIKIWDKNTL CCCCCCEEEEECCCE | 35.39 | - | |
474 | Phosphorylation | RGIACLQYRDRLVVS CEEEEEEECCEEEEE | 11.09 | 22817900 | |
527 | Ubiquitination | VSGAYDGKIKVWDLV ECCCCCCCEEEEEHH | 36.13 | - | |
555 | Phosphorylation | LRTLVEHSGRVFRLQ HHHHHHHCCEEEEEE | 18.13 | - | |
595 | Phosphorylation | AQAEPPRSPSRTYTY HHCCCCCCCCCCEEE | 32.76 | 21945579 | |
597 | Phosphorylation | AEPPRSPSRTYTYIS CCCCCCCCCCEEEEC | 38.20 | 21945579 | |
599 | Phosphorylation | PPRSPSRTYTYISR- CCCCCCCCEEEECC- | 25.26 | 21945579 | |
600 | Phosphorylation | PRSPSRTYTYISR-- CCCCCCCEEEECC-- | 9.09 | 21945579 | |
601 | Phosphorylation | RSPSRTYTYISR--- CCCCCCEEEECC--- | 17.48 | 21945579 | |
602 | Phosphorylation | SPSRTYTYISR---- CCCCCEEEECC---- | 6.10 | 21945579 | |
604 | Phosphorylation | SRTYTYISR------ CCCEEEECC------ | 22.86 | 21945579 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
- | K | Ubiquitination | E3 ubiquitin ligase | CDC34 | P49427 | PMID:10531035 |
- | K | Ubiquitination | E3 ubiquitin ligase | SMURF2 | Q9HAU4 | PMID:24709419 |
- | K | Ubiquitination | E3 ubiquitin ligase | SKP2 | Q13309 | PMID:24658274 |
- | K | Ubiquitination | E3 ubiquitin ligase | FBXW11 | Q9UKB1 | PMID:31406304 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FBW1A_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 FBW1A_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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