FANCG_HUMAN - dbPTM
FANCG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSRQTTSVG
------CCCCCCCCC
32.8522210691
5Phosphorylation---MSRQTTSVGSSC
---CCCCCCCCCHHH
21.6722210691
7Phosphorylation-MSRQTTSVGSSCLD
-CCCCCCCCCHHHHH
28.0615299017
28UbiquitinationDRLVRQAKVAQNSGL
HHHHHHHHHHHHCCC
29.75-
182UbiquitinationKDLLLLLKTWSPPAE
HHHHHHHHHCCCCHH
48.17-
258UbiquitinationALGSCHRKMGNPQRA
HHHHHHHHCCCHHHH
27.74-
347UbiquitinationCGTQSQTKHILASRC
CCCHHHHHHHHHHHH
22.47-
357PhosphorylationLASRCLQTGRAGDAA
HHHHHHHCCCCCHHH
18.7122210691
383PhosphorylationDSSEPRFSPPPSPPG
CCCCCCCCCCCCCCC
37.4622817900
387PhosphorylationPRFSPPPSPPGPCMP
CCCCCCCCCCCCCCH
49.8822817900
422PhosphorylationTLCEELLSRTSSLLP
HHHHHHHHHHHHHHH
46.2524719451
430UbiquitinationRTSSLLPKMSRLWED
HHHHHHHHHHHHHHH
49.86-
491UbiquitinationFRATPEEKEQGAAFN
HHCCHHHHHCCCCCC
54.39-
504UbiquitinationFNCEQGCKSDAALQQ
CCCCCCCCCHHHHHH
59.19-
557PhosphorylationTYFHLLQTLKRLDRR
HHHHHHHHHHHHCCH
33.93-
559UbiquitinationFHLLQTLKRLDRRDE
HHHHHHHHHHCCHHH
55.0621890473
615PhosphorylationFLEEFRTSLPKSCDL
HHHHHHHHCCCCCCC
38.1224719451
618UbiquitinationEFRTSLPKSCDL---
HHHHHCCCCCCC---
69.84-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
387SPhosphorylationKinaseCDK1P06493
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FANCG_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GABP1_HUMANGABPB1physical
16189514
ZBED1_HUMANZBED1physical
16189514
SAMD3_HUMANSAMD3physical
16189514
USBP1_HUMANUSHBP1physical
16189514
K1C19_HUMANKRT19physical
16189514
SPTN1_HUMANSPTAN1physical
11401546
CP2E1_HUMANCYP2E1physical
14499622
FANCA_HUMANFANCAphysical
10373536
FANCA_HUMANFANCAphysical
11739169
FANCA_HUMANFANCAphysical
12649160
FANCC_HUMANFANCCphysical
10373536
FANCF_HUMANFANCFphysical
11063725
FANCF_HUMANFANCFphysical
12649160
FANCG_HUMANFANCGphysical
15138265
FANCG_HUMANFANCGphysical
10652215
RTN2_HUMANRTN2physical
14499622
PSB1_HUMANPSMB1physical
14499622
FANCE_HUMANFANCEphysical
12239156
FANCA_HUMANFANCAphysical
12239156
FANCA_HUMANFANCAphysical
11157805
FANCF_HUMANFANCFphysical
11157805
FANCE_HUMANFANCEphysical
11157805
FANCG_HUMANFANCGphysical
11157805
XPF_HUMANERCC4physical
20518486
ERCC1_HUMANERCC1physical
20518486
FANCA_HUMANFANCAphysical
20450923
BRCA2_HUMANBRCA2physical
20450923
FANCF_HUMANFANCFphysical
20450923
FANCM_HUMANFANCMphysical
20347429
FANCA_HUMANFANCAphysical
20347429
FP100_HUMANC17orf70physical
20347429
FANCL_HUMANFANCLphysical
20347429
CENPS_HUMANAPITD1physical
20347429
CENPX_HUMANSTRA13physical
20347429
SPTN1_HUMANSPTAN1physical
19102630
XRCC3_HUMANXRCC3physical
18212739
FANCF_HUMANFANCFphysical
18212739
PRDX3_HUMANPRDX3physical
17060495
FANCA_HUMANFANCAphysical
16720839
FANCL_HUMANFANCLphysical
16720839
FANCB_HUMANFANCBphysical
16720839
XRCC3_HUMANXRCC3physical
16621732
FANCA_HUMANFANCAphysical
16621732
FANCF_HUMANFANCFphysical
16621732
BRCA2_HUMANBRCA2physical
16621732
FANCA_HUMANFANCAphysical
15367677
FANCA_HUMANFANCAphysical
15299017
FANCC_HUMANFANCCphysical
15299017
FANCF_HUMANFANCFphysical
15262960
FANCA_HUMANFANCAphysical
15192709
TOP3A_HUMANTOP3Aphysical
12724401
FANCA_HUMANFANCAphysical
12724401
BLM_HUMANBLMphysical
12724401
RFA1_HUMANRPA1physical
12724401
FANCA_HUMANFANCAphysical
11438206
FANCC_HUMANFANCCphysical
11438206
FANCA_HUMANFANCAphysical
11181053
FANCA_HUMANFANCAphysical
11167740
FANCA_HUMANFANCAphysical
11063725
FANCA_HUMANFANCAphysical
10961856
FANCA_HUMANFANCAphysical
22705371
FAP20_HUMANC1orf86physical
22705371
SPB1_HUMANFTSJ3physical
19447967
ZBED1_HUMANZBED1physical
19447967
USBP1_HUMANUSHBP1physical
19447967
CP2E1_HUMANCYP2E1physical
11756225
FANCL_HUMANFANCLphysical
24910428
FANCA_HUMANFANCAphysical
24910428
UIMC1_HUMANUIMC1physical
25132264
BRCC3_HUMANBRCC3physical
25132264
ABRX1_HUMANFAM175Aphysical
25132264
FANCA_HUMANFANCAphysical
25132264
CTNB1_HUMANCTNNB1physical
22653977
FANCA_HUMANFANCAphysical
22343915
FANCM_HUMANFANCMphysical
22343915
FANCL_HUMANFANCLphysical
22343915
FAP20_HUMANC1orf86physical
22343915
FP100_HUMANC17orf70physical
22343915
FANCA_HUMANFANCAphysical
28514442
UBB_HUMANUBBphysical
28514442
PAPS1_HUMANPAPSS1physical
28514442
CSTFT_HUMANCSTF2Tphysical
28514442
FANCA_HUMANFANCAphysical
28215707
SPTA1_HUMANSPTA1physical
16889989
AAPK1_HUMANPRKAA1physical
27449087

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614082Fanconi anemia complementation group G (FANCG)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FANCG_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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