| 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 | ||
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* 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. | |