UniProt ID | FANCG_HUMAN | |
---|---|---|
UniProt AC | O15287 | |
Protein Name | Fanconi anemia group G protein | |
Gene Name | FANCG | |
Organism | Homo sapiens (Human). | |
Sequence Length | 622 | |
Subcellular Localization | Nucleus . Cytoplasm . The major form is nuclear. The minor form is cytoplasmic. | |
Protein Description | DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. Candidate tumor suppressor gene.. | |
Protein Sequence | MSRQTTSVGSSCLDLWREKNDRLVRQAKVAQNSGLTLRRQQLAQDALEGLRGLLHSLQGLPAAVPVLPLELTVTCNFIILRASLAQGFTEDQAQDIQRSLERVLETQEQQGPRLEQGLRELWDSVLRASCLLPELLSALHRLVGLQAALWLSADRLGDLALLLETLNGSQSGASKDLLLLLKTWSPPAEELDAPLTLQDAQGLKDVLLTAFAYRQGLQELITGNPDKALSSLHEAASGLCPRPVLVQVYTALGSCHRKMGNPQRALLYLVAALKEGSAWGPPLLEASRLYQQLGDTTAELESLELLVEALNVPCSSKAPQFLIEVELLLPPPDLASPLHCGTQSQTKHILASRCLQTGRAGDAAEHYLDLLALLLDSSEPRFSPPPSPPGPCMPEVFLEAAVALIQAGRAQDALTLCEELLSRTSSLLPKMSRLWEDARKGTKELPYCPLWVSATHLLQGQAWVQLGAQKVAISEFSRCLELLFRATPEEKEQGAAFNCEQGCKSDAALQQLRAAALISRGLEWVASGQDTKALQDFLLSVQMCPGNRDTYFHLLQTLKRLDRRDEATALWWRLEAQTKGSHEDALWSLPLYLESYLSWIRPSDRDAFLEEFRTSLPKSCDL | |
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 | ------MSRQTTSVG ------CCCCCCCCC | 32.85 | 22210691 | |
5 | Phosphorylation | ---MSRQTTSVGSSC ---CCCCCCCCCHHH | 21.67 | 22210691 | |
7 | Phosphorylation | -MSRQTTSVGSSCLD -CCCCCCCCCHHHHH | 28.06 | 15299017 | |
28 | Ubiquitination | DRLVRQAKVAQNSGL HHHHHHHHHHHHCCC | 29.75 | - | |
182 | Ubiquitination | KDLLLLLKTWSPPAE HHHHHHHHHCCCCHH | 48.17 | - | |
258 | Ubiquitination | ALGSCHRKMGNPQRA HHHHHHHHCCCHHHH | 27.74 | - | |
347 | Ubiquitination | CGTQSQTKHILASRC CCCHHHHHHHHHHHH | 22.47 | - | |
357 | Phosphorylation | LASRCLQTGRAGDAA HHHHHHHCCCCCHHH | 18.71 | 22210691 | |
383 | Phosphorylation | DSSEPRFSPPPSPPG CCCCCCCCCCCCCCC | 37.46 | 22817900 | |
387 | Phosphorylation | PRFSPPPSPPGPCMP CCCCCCCCCCCCCCH | 49.88 | 22817900 | |
422 | Phosphorylation | TLCEELLSRTSSLLP HHHHHHHHHHHHHHH | 46.25 | 24719451 | |
430 | Ubiquitination | RTSSLLPKMSRLWED HHHHHHHHHHHHHHH | 49.86 | - | |
491 | Ubiquitination | FRATPEEKEQGAAFN HHCCHHHHHCCCCCC | 54.39 | - | |
504 | Ubiquitination | FNCEQGCKSDAALQQ CCCCCCCCCHHHHHH | 59.19 | - | |
557 | Phosphorylation | TYFHLLQTLKRLDRR HHHHHHHHHHHHCCH | 33.93 | - | |
559 | Ubiquitination | FHLLQTLKRLDRRDE HHHHHHHHHHCCHHH | 55.06 | 21890473 | |
615 | Phosphorylation | FLEEFRTSLPKSCDL HHHHHHHHCCCCCCC | 38.12 | 24719451 | |
618 | Ubiquitination | EFRTSLPKSCDL--- HHHHHCCCCCCC--- | 69.84 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
387 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FANCG_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 FANCG_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
614082 | Fanconi anemia complementation group G (FANCG) | |||||
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 |
"FANCG promotes formation of a newly identified protein complexcontaining BRCA2, FANCD2 and XRCC3."; Wilson J.B., Yamamoto K., Marriott A.S., Hussain S., Sung P.,Hoatlin M.E., Mathew C.G., Takata M., Thompson L.H., Kupfer G.M.,Jones N.J.; Oncogene 27:3641-3652(2008). Cited for: INTERACTION WITH BRCA2; FANCD2 AND XRCC3, PHOSPHORYLATION AT SER-7,AND MUTAGENESIS OF SER-7; SER-383 AND SER-387. |