|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 101 to 163 out of 163 for Faap20

<< First    < Previous  |  Next >    Last >>
0.022s

Categories

Hits by Pathway

Hits by Strain

Hits by Category

Type Details Score
Publication
22343915 | -
First Author: Ali AM
Year: 2012
Journal: Blood
Title: FAAP20: a novel ubiquitin-binding FA nuclear core-complex protein required for functional integrity of the FA-BRCA DNA repair pathway.
Volume: 119
Issue: 14
Pages: 3285-94
•
•
•
•
•
Publication
22705371 | -
First Author: Yan Z
Year: 2012
Journal: Mol Cell
Title: A ubiquitin-binding protein, FAAP20, links RNF8-mediated ubiquitination to the Fanconi anemia DNA repair network.
Volume: 47
Issue: 1
Pages: 61-75
•
•
•
•
•
Protein Domain
IPR031490 | UBZ2_FAAP20
Type: Domain
Description: The ubiquitin-binding zinc finger (UBZ) is a type of zinc-coordinating β-β-α fold domain found mainly in proteins involved in DNA repair and transcriptional regulation. UBZ domains coordinate a zinc ion with cysteine or histidine residues; depending on their amino acid sequence, UBZ domains are classified into several families [, ]. Type 1 UBZs are CCHH-type zinc fingers found in tandem UBZ domains of TAX1-binding protein 1 (TAX1BP1) [, , ], type 2 UBZs are CCHC-type zinc fingers found in FAAP20 which is a subunit of the Fanconi anemia (FA) core complex [, ], type 3 UBZs are CCHH-type zinc fingers found only in the Y-family translesion polymerase eta [, , ], and type 4 UBZs are CCHC-type zinc fingers found in Y-family translesion polymerase kappa, Werner helicase-interacting protein 1 (WRNIP1), and Rad18 [, , ]. The UBZ domain consists of two short antiparallel β-strands followed by one α-helix. The α-helix packs against the β-strands with a zinc ion sandwiched between the α-helix and the β-strands. The zinc ion is coordinated by two cysteines located on the fingertip formed by the β-strands and two histidines [, ]or one histidine and one cysteine []on the α-helix [].This domain is the type 2 UBZ found in Fanconi anemia-associated protein of 20kDa (FAAP20) [, , , ].
•
•
•
•
•
Protein Domain
IPR041298 | UBZ3
Type: Domain
Description: The ubiquitin-binding zinc finger (UBZ) is a type of zinc-coordinating β-β-α fold domain found mainly in proteins involved in DNA repair and transcriptional regulation. UBZ domains coordinate a zinc ion with cysteine or histidine residues; depending on their amino acid sequence, UBZ domains are classified into several families [, ]. Type 1 UBZs are CCHH-type zinc fingers found in tandem UBZ domains of TAX1-binding protein 1 (TAX1BP1) [, , ], type 2 UBZs are CCHC-type zinc fingers found in FAAP20 which is a subunit of the Fanconi anemia (FA) core complex [, ], type 3 UBZs are CCHH-type zinc fingers found only in the Y-family translesion polymerase eta [, , ], and type 4 UBZs are CCHC-type zinc fingers found in Y-family translesion polymerase kappa, Werner helicase-interacting protein 1 (WRNIP1), and Rad18 [, , ]. The UBZ domain consists of two short antiparallel β-strands followed by one α-helix. The α-helix packs against the β-strands with a zinc ion sandwiched between the α-helix and the β-strands. The zinc ion is coordinated by two cysteines located on the fingertip formed by the β-strands and two histidines [, ]or one histidine and one cysteine []on the α-helix [].This entry represents type 3 UBZ found in DNA polymerase eta (). It is important in the recruitment of the polymerase to the stalled replication machinery in translesion synthesis. The UBZ domain adopts a classical C2H2 zinc-finger structure characterized by a β-β-α fold [].
•
•
•
•
•
Protein
S4R284
Organism: Mus musculus/domesticus
Length: 296  
Fragment?: false
•
•
•
•
•
Protein
F6R0R3
Organism: Mus musculus/domesticus
Length: 80  
Fragment?: true
•
•
•
•
•
Protein
Q9CRV6
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: true
•
•
•
•
•
Protein
F7A9G8
Organism: Mus musculus/domesticus
Length: 288  
Fragment?: true
•
•
•
•
•
Publication
2970061 | -
First Author: Jones JS
Year: 1988
Journal: Nucleic Acids Res
Title: The Saccharomyces cerevisiae RAD18 gene encodes a protein that contains potential zinc finger domains for nucleic acid binding and a putative nucleotide binding sequence.
Volume: 16
Issue: 14B
Pages: 7119-31
•
•
•
•
•
Publication
16980296 | -
First Author: Nakajima S
Year: 2006
Journal: J Biol Chem
Title: Replication-dependent and -independent responses of RAD18 to DNA damage in human cells.
Volume: 281
Issue: 45
Pages: 34687-95
•
•
•
•
•
Publication
17304240 | -
First Author: Bomar MG
Year: 2007
Journal: EMBO Rep
Title: Structure of the ubiquitin-binding zinc finger domain of human DNA Y-polymerase eta.
Volume: 8
Issue: 3
Pages: 247-51
•
•
•
•
•
Publication
27062441 | J:248713
First Author: Suzuki N
Year: 2016
Journal: FEBS J
Title: A novel mode of ubiquitin recognition by the ubiquitin-binding zinc finger domain of WRNIP1.
Volume: 283
Issue: 11
Pages: 2004-17
•
•
•
•
•
Publication
26506893 | -
First Author: Xie X
Year: 2015
Journal: Autophagy
Title: Molecular basis of ubiquitin recognition by the autophagy receptor CALCOCO2.
Volume: 11
Issue: 10
Pages: 1775-89
•
•
•
•
•
Publication
25162118 | -
First Author: Rizzo AA
Year: 2014
Journal: Biochemistry
Title: NMR structure of the human Rad18 zinc finger in complex with ubiquitin defines a class of UBZ domains in proteins linked to the DNA damage response.
Volume: 53
Issue: 37
Pages: 5895-906
•
•
•
•
•
Publication
19213613 | -
First Author: Hofmann K
Year: 2009
Journal: DNA Repair (Amst)
Title: Ubiquitin-binding domains and their role in the DNA damage response.
Volume: 8
Issue: 4
Pages: 544-56
•
•
•
•
•
Publication
17550419 | -
First Author: García-Ortiz MV
Year: 2007
Journal: FEBS J
Title: The noncatalytic C-terminus of AtPOLK Y-family DNA polymerase affects synthesis fidelity, mismatch extension and translesion replication.
Volume: 274
Issue: 13
Pages: 3340-50
•
•
•
•
•
Publication
24239949 | -
First Author: Ceregido MA
Year: 2014
Journal: J Mol Biol
Title: The structure of TAX1BP1 UBZ1+2 provides insight into target specificity and adaptability.
Volume: 426
Issue: 3
Pages: 674-90
•
•
•
•
•
Publication
20837403 | -
First Author: Woodruff RV
Year: 2010
Journal: DNA Repair (Amst)
Title: The unusual UBZ domain of Saccharomyces cerevisiae polymerase η.
Volume: 9
Issue: 11
Pages: 1130-41
•
•
•
•
•
Publication
25799058 | -
First Author: Toma A
Year: 2015
Journal: PLoS One
Title: Structural basis for ubiquitin recognition by ubiquitin-binding zinc finger of FAAP20.
Volume: 10
Issue: 3
Pages: e0120887
•
•
•
•
•
Publication
20385554 | -
First Author: Yang K
Year: 2010
Journal: J Biol Chem
Title: RAD18-dependent recruitment of SNM1A to DNA repair complexes by a ubiquitin-binding zinc finger.
Volume: 285
Issue: 25
Pages: 19085-91
•
•
•
•
•
Publication
27370208 | -
First Author: Thurston TL
Year: 2016
Journal: EMBO J
Title: Recruitment of TBK1 to cytosol-invading Salmonella induces WIPI2-dependent antibacterial autophagy.
Volume: 35
Issue: 16
Pages: 1779-92
•
•
•
•
•
Publication
24794496 | J:214661
First Author: Lachaud C
Year: 2014
Journal: J Cell Sci
Title: Distinct functional roles for the two SLX4 ubiquitin-binding UBZ domains mutated in Fanconi anemia.
Volume: 127
Issue: Pt 13
Pages: 2811-7
•
•
•
•
•
Publication
28314591 | J:259425
First Author: Whang MI
Year: 2017
Journal: Immunity
Title: The Ubiquitin Binding Protein TAX1BP1 Mediates Autophagasome Induction and the Metabolic Transition of Activated T Cells.
Volume: 46
Issue: 3
Pages: 405-420
•
•
•
•
•
Publication
18796167 | -
 
First Author: Dubin-Bar D
Year: 2008
Journal: BMC Cell Biol
Title: The Drosophila IKK-related kinase (Ik2) and Spindle-F proteins are part of a complex that regulates cytoskeleton organization during oogenesis.
Volume: 9
Pages: 51
•
•
•
•
•
Publication
16540510 | -
First Author: Abdu U
Year: 2006
Journal: Development
Title: spn-F encodes a novel protein that affects oocyte patterning and bristle morphology in Drosophila.
Volume: 133
Issue: 8
Pages: 1477-84
•
•
•
•
•
Protein Domain
IPR006642 | Rad18_UBZ4
Type: Domain
Description: The ubiquitin-binding zinc finger (UBZ) is a type of zinc-coordinating β-β-α fold domain found mainly in proteins involved in DNA repair and transcriptional regulation. UBZ domains coordinate a zinc ion with cysteine or histidine residues; depending on their amino acid sequence, UBZ domains are classified into several families [, ]. Type 1 UBZs are CCHH-type zinc fingers found in tandem UBZ domains of TAX1-binding protein 1 (TAX1BP1) [, , ], type 2 UBZs are CCHC-type zinc fingers found in FAAP20 which is a subunit of the Fanconi anemia (FA) core complex [, ], type 3 UBZs are CCHH-type zinc fingers found only in the Y-family translesion polymerase eta [, , ], and type 4 UBZs are CCHC-type zinc fingers found in Y-family translesion polymerase kappa, Werner helicase-interacting protein 1 (WRNIP1), and Rad18 [, , ]. The UBZ domain consists of two short antiparallel β-strands followed by one α-helix. The α-helix packs against the β-strands with a zinc ion sandwiched between the α-helix and the β-strands. The zinc ion is coordinated by two cysteines located on the fingertip formed by the β-strands and two histidines [, ]or one histidine and one cysteine []on the α-helix [].This entry represents type 4 UBZ found in RAD18. The domain is a potential zinc finger for nucleic acid binding and a putative nucleotide binding sequence []. Human RAD18 accumulates very rapidly and remains for a long period of time at sites of different types of DNA damage, and is required of DNA. RAD18 appears to respond to DNA damage in two distinct ways: replication-dependent and replication-independent. The RAD18-type zinc finger located in the middle of RAD18 is responsible for the replication-independent accumulation of RAD18 following DNA damage, while a second zinc finger, SAP-type, is responsible for replication-dependent accumulation [].
•
•
•
•
•
Protein Domain
IPR041641 | CALCOCO1/2_Zn_UBZ1
Type: Domain
Description: The ubiquitin-binding zinc finger (UBZ) is a type of zinc-coordinating β-β-α fold domain found mainly in proteins involved in DNA repair and transcriptional regulation. UBZ domains coordinate a zinc ion with cysteine or histidine residues; depending on their amino acid sequence, UBZ domains are classified into several families [, ]. Type 1 UBZs are CCHH-type zinc fingers found in tandem UBZ domains of TAX1-binding protein 1 (TAX1BP1) [, , ], type 2 UBZs are CCHC-type zinc fingers found in FAAP20 which is a subunit of the Fanconi anemia (FA) core complex [, ], type 3 UBZs are CCHH-type zinc fingers found only in the Y-family translesion polymerase eta [, , ], and type 4UBZs are CCHC-type zinc fingers found in Y-family translesion polymerase kappa, Werner helicase-interacting protein 1 (WRNIP1), and Rad18 [, , ]. The UBZ domain consists of two short antiparallel β-strands followed by one α-helix. The α-helix packs against the β-strands with a zinc ion sandwiched between the α-helix and the β-strands. The zinc ion is coordinated by two cysteines located on the fingertip formed by the β-strands and two histidines [, ]or one histidine and one cysteine []on the α-helix [].This entry represents the UBZ1 type zinc finger domain found in calcium-binding and coiled-coil domain 1/2 (CALCOCO1/2), tax-binding protein 1 and protein spindle-F.This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal α-helix to interact with the solvent-exposed surface of the central β-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger [].CALCOCO2 (also known as NDP25) is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens []. Tax binding protein 1 is a ubiquitin binding protein []and protein spindle-F plays a role in oocyte axis determination and microtubule organization during oogenesis in Drosophila [, ].
•
•
•
•
•
Protein
Q9JIC3
Organism: Mus musculus/domesticus
Length: 1026  
Fragment?: false
•
•
•
•
•
Protein
Q8CGU1
Organism: Mus musculus/domesticus
Length: 691  
Fragment?: false
•
•
•
•
•
Protein
P70347
Organism: Mus musculus/domesticus
Length: 448  
Fragment?: false
•
•
•
•
•
Protein
A2A9T0
Organism: Mus musculus/domesticus
Length: 611  
Fragment?: false
•
•
•
•
•
Protein
Q3UKC1
Organism: Mus musculus/domesticus
Length: 814  
Fragment?: false
•
•
•
•
•
Protein
A0A2R8VKP5
Organism: Mus musculus/domesticus
Length: 606  
Fragment?: false
•
•
•
•
•
Protein
Q8C2D3
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
•
•
•
•
•
Protein
S4R1N2
Organism: Mus musculus/domesticus
Length: 1029  
Fragment?: false
•
•
•
•
•
Protein
Q3UGW0
Organism: Mus musculus/domesticus
Length: 414  
Fragment?: false
•
•
•
•
•
Protein
Q3TNB4
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
•
•
•
•
•
Protein
A2AR76
Organism: Mus musculus/domesticus
Length: 447  
Fragment?: false
•
•
•
•
•
Protein
F6Q5V4
Organism: Mus musculus/domesticus
Length: 232  
Fragment?: true
•
•
•
•
•
Protein
Q8R383
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
•
•
•
•
•
Protein
Z4YKN2
Organism: Mus musculus/domesticus
Length: 610  
Fragment?: false
•
•
•
•
•
Protein
Q5Q9G9
Organism: Mus musculus/domesticus
Length: 434  
Fragment?: false
•
•
•
•
•
Protein
Q69ZT1
Organism: Mus musculus/domesticus
Length: 1020  
Fragment?: false
•
•
•
•
•
Protein
Q6P1D7
Organism: Mus musculus/domesticus
Length: 1565  
Fragment?: false
•
•
•
•
•
Protein
Q5U5Q9
Organism: Mus musculus/domesticus
Length: 727  
Fragment?: false
•
•
•
•
•
Protein
G3X912
Organism: Mus musculus/domesticus
Length: 497  
Fragment?: false
•
•
•
•
•
Protein
Q9JJN0
Organism: Mus musculus/domesticus
Length: 694  
Fragment?: false
•
•
•
•
•
Protein
E9Q577
Organism: Mus musculus/domesticus
Length: 727  
Fragment?: false
•
•
•
•
•
Protein
A0A0R4J073
Organism: Mus musculus/domesticus
Length: 727  
Fragment?: false
•
•
•
•
•
Protein
A0A0R4J183
Organism: Mus musculus/domesticus
Length: 446  
Fragment?: false
•
•
•
•
•
Protein
I6L9K1
Organism: Mus musculus/domesticus
Length: 556  
Fragment?: false
•
•
•
•
•
Protein
Q9QUG2
Organism: Mus musculus/domesticus
Length: 852  
Fragment?: false
•
•
•
•
•
Protein
Q91XU0
Organism: Mus musculus/domesticus
Length: 660  
Fragment?: false
•
•
•
•
•
Protein
Q5Q9H6
Organism: Mus musculus/domesticus
Length: 772  
Fragment?: false
•
•
•
•
•
Protein
Q5Q9H7
Organism: Mus musculus/domesticus
Length: 793  
Fragment?: false
•
•
•
•
•
Protein
Q9QXK2
Organism: Mus musculus/domesticus
Length: 509  
Fragment?: false
•
•
•
•
•
Protein
Q8CED3
Organism: Mus musculus/domesticus
Length: 496  
Fragment?: true
•
•
•
•
•
Protein
E9Q392
Organism: Mus musculus/domesticus
Length: 556  
Fragment?: false
•
•
•
•
•
Protein
Q921R6
Organism: Mus musculus/domesticus
Length: 309  
Fragment?: false
•
•
•
•
•
Protein
D3Z734
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
•
•
•
•
•
Protein
D3Z733
Organism: Mus musculus/domesticus
Length: 449  
Fragment?: false
•
•
•
•
•
Protein
W4VSP9
Organism: Mus musculus/domesticus
Length: 309  
Fragment?: false
•
•
•
•
•
Protein
Q8CDH2
Organism: Mus musculus/domesticus
Length: 556  
Fragment?: false
•
•
•
•
•




MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom