Ubikitiiniä sitovat sinkkisormet; UZB1, UZB2, UZB 3 ja UZB4 tyyppiset sinkkisormiproteiinit

 https://www.ebi.ac.uk/interpro/entry/InterPro/IPR041641/

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(C)  or histidine (H) residues; depending on their amino acid sequence, UBZ domains are classified into several families

^{[8, 4]}

. Type 1 UBZs are CCHH-type zinc fingers found in tandem UBZ domains of TAX1-binding protein 1 (TAX1BP1) ^{[10, 16, 14]}

, type 2 UBZs are CCHC-type zinc fingers found in FAAP20 which is a subunit of the Fanconi anemia (FA) core complex ^{[6, 12]}

, type 3 UBZs are CCHH-type zinc fingers found only in the Y-family translesion polymerase eta

^{[5, 9, 11]}

, and type 4 UBZs are CCHC-type zinc fingers found in Y-family translesion polymerase kappa, Werner helicase-interacting protein 1 (WRNIP1), and  Rad18 (alias RNF73,  RINGdomaani tyyppinen  sinkkisormi )

* TAX1BP1 

https://www.genecards.org/cgi-bin/carddisp.pl?gene=TAX1BP1&keywords=UBZ1 

makroautofagia tbc ja salmonellaa vastaan  

Ubiquitin-binding adapter that participates in inflammatory, antiviral and innate immune processes as well as selective autophagy regulation (PubMed:29940186, 30459273, 30909570). Plays a key role in the negative regulation of NF-kappa-B and IRF3 signalings by acting as an adapter for the ubiquitin-editing enzyme A20/TNFAIP3 to bind and inactivate its substrates (PubMed:17703191). Disrupts the interactions between the E3 ubiquitin ligase TRAF3 and TBK1/IKBKE to attenuate 'Lys63'-linked polyubiquitination of TBK1 and thereby IFN-beta production (PubMed:21885437). Also recruits A20/TNFAIP3 to ubiquitinated signaling proteins TRAF6 and RIPK1, leading to their deubiquitination and disruption of IL-1 and TNF-induced NF-kappa-B signaling pathways (PubMed:17703191). Inhibits virus-induced apoptosis by inducing the 'Lys-48'-linked polyubiquitination and degradation of MAVS via recruitment of the E3 ligase ITCH, thereby attenuating MAVS-mediated apoptosis signaling (PubMed:27736772). As a macroautophagy/autophagy receptor, facilitates the xenophagic clearance of pathogenic bacteria such as Salmonella typhimurium and Mycobacterium tuberculosis (PubMed:26451915). Upon NBR1 recruitment to the SQSTM1-ubiquitin condensates, acts as the major recruiter of RB1CC1 to these ubiquitin condensates to promote their autophagic degradation (PubMed:33226137, 34471133). Mediates the autophagic degradation of other substrates including TICAM1 (PubMed:28898289). ( TAXB1_HUMAN,Q86VP1 ) 

*WRNIP1 

 https://www.genecards.org/cgi-bin/carddisp.pl?gene=WRNIP1&keywords=UBZ1

 viruksia vastaan 

Functions as a modulator of initiation or reinitiation events during DNA polymerase delta-mediated DNA synthesis. In the presence of ATP, stimulation of DNA polymerase delta-mediated DNA synthesis is decreased. Also plays a role in the innate immune defense against viruses. Stabilizes the RIGI dsRNA interaction and promotes RIGI 'Lys-63'-linked polyubiquitination. In turn, RIGI transmits the signal through mitochondrial MAVS. ( WRIP1_HUMAN,Q96S55  

*POLH  

 https://www.genecards.org/cgi-bin/carddisp.pl?gene=POLH&keywords=UBZ1

Vähentää UV- säteilyn haitallista geenivaikutusta   

 This gene encodes a member of the Y family of specialized DNA polymerases. It copies undamaged DNA with a lower fidelity than other DNA-directed polymerases. However, it accurately replicates UV-damaged DNA; when thymine dimers are present, this polymerase inserts the complementary nucleotides in the newly synthesized DNA, thereby bypassing the lesion and suppressing the mutagenic effect of UV-induced DNA damage. This polymerase is thought to be involved in hypermutation during immunoglobulin class switch recombination. Mutations in this gene result in XPV, a variant type of xeroderma pigmentosum. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2014]

*RAD18, RNF73, Postreplication Repair Protein HRAD18p 

https://www.genecards.org/cgi-bin/carddisp.pl?gene=RAD18&keywords=Rad18

 

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

^{[8, 3]}

. Type 1 UBZs are CCHH-type zinc fingers found in tandem UBZ domains of TAX1-binding protein 1 (TAX1BP1)

^{[10, 5, 14]}

, type 2 UBZs are CCHC-type zinc fingers found in FAAP20 which is a subunit of the Fanconi anemia (FA) core complex

^{[6, 12]}

, type 3 UBZs are CCHH-type zinc fingers found only in the Y-family translesion polymerase eta

^{[4, 9, 11]}

, and type 4 UBZs are CCHC-type zinc fingers found in Y-family translesion polymerase kappa, Werner helicase-interacting protein 1 (WRNIP1), and Rad18

^{[13, 7, 15]}

.

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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

^[2]

. 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

^[1]

Function:

• E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA.
  Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA.
  Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'.
  Has ssDNA binding activity. RAD18_HUMAN,Q9NS91

 

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