2ECT


Conserved Protein Domain Family
RING-H2_RNF126_like

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cd16667: RING-H2_RNF126_like (this model, PSSM-Id:319581 is obsolete and has been replaced by 438329)
Click on image for an interactive view with Cn3D
RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins
The family includes RING finger proteins RNF126, RNF115, and similar proteins. RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP) pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor (CI-MPR). RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation, and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase (AID), a poorly soluble protein that is essential for antibody diversification. RNF115, also known as Rab7-interacting ring finger protein (Rabring 7), or zinc finger protein 364 (ZNF364), or breast cancer-associated gene 2 (BCA2), is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK) activation and its inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a co-factor in the restriction imposed by tetherin on HIV-1, and targets HIV-1 Gag for lysosomal degradation, impairing virus assembly and release, in a tetherin-independent manner. Moreover, RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. RNF115 and RNF126 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. Both of them contain an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.
Statistics
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PSSM-Id: 319581
Aligned: 18 rows
Threshold Bit Score: 83.136
Created: 2-May-2013
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Zn binding siteRING-H2 finger
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Structure:2ECT; Mus musculus RNF126 binds two Zn2+ ions through its RING-H2 finger.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1          #  #                  # #  #  #          #  # 
2ECT_A         17 ECPVCKEDYal----gESVRQLPCNHLFHDSCIVPWLEqHDSCPVCR 59   house mouse
ETO21630      328 TCPICKDEFar----gDKLHLLPCQHRYHCDCILPWLNqHNTCPVCR 370  Reticulomyxa filosa
NP_181961      95 PCAICREDFvv----gESARRLPCNHLYHNDCIIPWLTsHNSCPLCR 137  thale cress
XP_002969956   28 SCAVCKDDYav----gNKVRQMPCKHVYHQDCILPWLAlHGTCPVCR 70   Selaginella moellendorffii
CCI42106      191 ECAVCKDEFnl----aEEARRMPCTHTFHPDCILPWLKqHNSCPICR 233  Albugo candida
XP_001777565  365 QCAVCKDEFel----gALVRQMPCKHMYHADCILPWLAqHNSCPVCR 407  Physcomitrella patens
KJK42186      240 VCTVCQETMs-----gNGTLTLSCGHVFHNDCVVPWLEqRRTCPLCR 281  Lechevalieria aerocolonigenes
EJY83947      407 LCTICQENLpi----gEKAMIIPCGHIFHPDCVLPWLKdHNTCPVCR 449  Oxytricha trifallax
EWC76528      360 SCAICREEYkendevhRITDNERCRHVFHCSCIIPWLKeRNSCPTCR 406  Plasmodium falciparum UGT5.1
KDD74273      147 PCTVCHDTLgv----gDVVMELPCNHCFHPDCIMPWLEsHNTCPICR 189  Helicosporidium sp. ATCC 50920

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