Type |
Details |
Score |
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1450
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1429
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1144
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1437
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
84
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1450
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Yao CJ |
Year: |
2013 |
Journal: |
Pharmazie |
Title: |
Fanconi anemia pathway--the way of DNA interstrand cross-link repair. |
Volume: |
68 |
Issue: |
1 |
Pages: |
5-11 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yamashita T |
Year: |
2001 |
Journal: |
Int J Hematol |
Title: |
Current knowledge on the pathophysiology of Fanconi anemia: from genes to phenotypes. |
Volume: |
74 |
Issue: |
1 |
Pages: |
33-41 |
|
•
•
•
•
•
|
Publication |
First Author: |
Smogorzewska A |
Year: |
2010 |
Journal: |
Mol Cell |
Title: |
A genetic screen identifies FAN1, a Fanconi anemia-associated nuclease necessary for DNA interstrand crosslink repair. |
Volume: |
39 |
Issue: |
1 |
Pages: |
36-47 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kratz K |
Year: |
2010 |
Journal: |
Cell |
Title: |
Deficiency of FANCD2-associated nuclease KIAA1018/FAN1 sensitizes cells to interstrand crosslinking agents. |
Volume: |
142 |
Issue: |
1 |
Pages: |
77-88 |
|
•
•
•
•
•
|
Publication |
First Author: |
MacKay C |
Year: |
2010 |
Journal: |
Cell |
Title: |
Identification of KIAA1018/FAN1, a DNA repair nuclease recruited to DNA damage by monoubiquitinated FANCD2. |
Volume: |
142 |
Issue: |
1 |
Pages: |
65-76 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yamamoto KN |
Year: |
2011 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Involvement of SLX4 in interstrand cross-link repair is regulated by the Fanconi anemia pathway. |
Volume: |
108 |
Issue: |
16 |
Pages: |
6492-6 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sareen A |
Year: |
2012 |
Journal: |
Nucleic Acids Res |
Title: |
Fanconi anemia proteins FANCD2 and FANCI exhibit different DNA damage responses during S-phase. |
Volume: |
40 |
Issue: |
17 |
Pages: |
8425-39 |
|
•
•
•
•
•
|
Publication |
First Author: |
Chaudhury I |
Year: |
2013 |
Journal: |
Nucleic Acids Res |
Title: |
FANCD2 regulates BLM complex functions independently of FANCI to promote replication fork recovery. |
Volume: |
41 |
Issue: |
13 |
Pages: |
6444-59 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yeo JE |
Year: |
2014 |
Journal: |
Hum Mol Genet |
Title: |
CtIP mediates replication fork recovery in a FANCD2-regulated manner. |
Volume: |
23 |
Issue: |
14 |
Pages: |
3695-705 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
The Fanconi Anemia (FA) pathway is responsible for interstrand crosslink DNA repair []. The name originates the recessive syndrome known as Fanconi anemia, which causes developmental problems and cancer predisposition []. In this pathway, the FANCI-FANCD2 (ID) complex is ubiquitinated by the FA core complex and then travels to sites of damage to coordinate repair [, ]. FA pathway activation seems to trigger dissociation of FANCD2 from FANCI, coinciding with FANCD2 monoubiquitination which precedes monoubiquitination of FANCI []. This suggests a functional separation for FANCD2 from FANCI [].Monoubiquitinated FANCD2 functions to recruit DNA repair factors FAN1 (Fanconi-associated nuclease 1) []and SLX4 [], suggesting that chromatin-bound FANCD2Ub is a docking platform for certain DNA repair nucleases. FANCD2 has also a role in replication fork recovery []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This domain is found in Fanconi-anemia-associated nuclease 1 (FAN1) present in Pseudomonas aeruginosa. FAN1 is a nuclease associated with Fanconi anemia (FA), an autosomal recessive genetic disorder caused by defects in FA genes responsible for processing DNA inter-strand cross-links (ICLs). The domain, known as the SAP domain, helps to augment the overall protein DNA interaction by interacting with the 3' and 5' ends of the template strand. Support of the pre-nick segment binding is crucial as multiple mutations in this domain resulted in hypersensitivity to a cross-linking agent in the SAP domain of Caenorhabditis elegans' FAN1. The helix-hairpin-helix of the SAP recognize three consecutive phosphate groups (C19, A20 and A21) at the 3' end of the template via the basic residues K116, K135 and K117 []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Yoshikiyo K |
Year: |
2010 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
KIAA1018/FAN1 nuclease protects cells against genomic instability induced by interstrand cross-linking agents. |
Volume: |
107 |
Issue: |
50 |
Pages: |
21553-7 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
246
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1020
 |
Fragment?: |
false |
|
•
•
•
•
•
|