4QPL,2D8T


Conserved Protein Domain Family
RING-HC_RNF146

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cd16546: RING-HC_RNF146 
Click on image for an interactive view with Cn3D
RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins
RNF146, also known as dactylidin, or iduna, is a cytoplasmic E3 ubiquitin-protein ligase that is responsible for PARylation-dependent ubiquitination (PARdU). It displays neuroprotective property due to its inhibition of Parthanatos, a PAR dependent cell death, via binding with Poly(ADP-ribose) (PAR). It also modulates PAR polymerase-1 (PARP-1)-mediated oxidative cell injury in cardiac myocytes. Moreover, RNF146 mediates tankyrase-dependent degradation of axin, thereby positively regulating Wnt signaling. It also facilitates DNA repair and protects against cell death induced by DNA damaging agents or gamma-irradiation by translocating to the nucleus after cellular injury and promoting the ubiquitination and degradation of various nuclear proteins involved in DNA damage repair. Furthermore, RNF146 is implicated in neurodegenerative disease and cancer development. It regulates the development and progression of non-small cell lung cancer (NSCLC) by enhancing cell growth, invasion, and survival. RNF146 contains an N-terminal C3HC4-type RING-HC finger followed by a WWE domain with a poly(ADP-ribose) (PAR) binding motif at the tail.
Statistics
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PSSM-Id: 438208
Aligned: 17 rows
Threshold Bit Score: 66.6398
Created: 2-May-2013
Updated: 17-Oct-2022
Structure
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Program:
Drawing:
Aligned Rows:
 
Zn binding siteE2 binding site
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1: Zn binding site [ion binding site], 8 residue positions
Conserved feature residue pattern:C C C H C C C CClick to see conserved feature residue pattern help
Evidence:
  • Structure:4QPL; Mus musculus RNF146 binds two Zn2+ ions through its RING-HC finger.
  • Comment:C3HC4-type RING-HC finger consensus motif: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C, where X is any amino acid and the number of X residues varies in different fingers
  • Comment:A RING finger typically binds two zinc atoms, with its Cys and/or His side chains in a unique "cross-brace" arrangement.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1          #  #           # #  #  #            #  #          
4QPL_A         6 PECAICLQTCVHPVSLPCKHVFCYLCVKGASWl--gKRCALCRQEIPEDFLD 55  house mouse
Q7ZUK0        40 PECPICLQSCVHPVRLPCRHIFCFLCVKGASWh--sKRCALCRREVPEDFLE 89  zebrafish
EDO31334       1 PDCPVCLQQASYPVRLPCGHMFCFLCIKGVALr--sRKCAICRQPISPDYLD 50  starlet sea anemone
EEC16573      27 LECAICLQKCIHPAKLPCGHIFCYLCVKGIANq--sKKCAMCRQEIPADFTD 76  black-legged tick
NP_001137978 122 LECPICLQTCIHPARLPCGHIFCFLCVKGVAYk--nRRCAMCRREIPAEFLD 171 fruit fly
XP_002735032  50 LECAVCLQSCIQPVKLPCEHIFCFLCVKGVANq--sKRCALCRKEIPIEFLN 99  Saccoglossus kowalevskii
CBY42318       4 QSCPICLEDLLLPLTLPCSHKFCYLCIKGVALspsgPTCPLCRQVFSNSLII 55  Oikopleura dioica
EFX82026      72 IECAVCLQTCIHPVKLPCSHIFCYLCVKGVAFq--sKRCAMCRQEIPSDFLI 121 common water flea
ELT96980     155 VECPICLQTCIHPVQLPCSHVFCFLCVKGGANq--sKRCALCRSEIPANYLY 204 Capitella sp. I Grassle & Grassle, 1976
XP_013420780  46 LECPVCLQTCVHPVKLPCNHIFCFLCVKGVANq--sKRCALCRTEIPTDYLY 95  Lingula anatina

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