Type |
Details |
Score |
Publication |
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 |
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 |
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 |
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 |
Organism: |
Mus musculus/domesticus |
Length: |
296
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
80
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
133
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
288
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
Organism: |
Mus musculus/domesticus |
Length: |
1026
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
691
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
448
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
611
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
814
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
606
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
413
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1029
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
414
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
413
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
447
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
232
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
413
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
610
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
434
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1020
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1565
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
727
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
497
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
694
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
727
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
727
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
446
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
556
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
852
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
660
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
772
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
793
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
509
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
496
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
556
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
309
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
428
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
449
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
309
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
556
 |
Fragment?: |
false |
|
•
•
•
•
•
|