Conserved Protein Domain Family
RING-H2_RNF13_like

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cd16665: RING-H2_RNF13_like 
RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), and similar proteins
This subfamily includes RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), Zinc/RING finger protein 4 (ZNRF4), and similar proteins, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane domain (TM), and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence. RNF13 is a widely expressed membrane-associated E3 ubiquitin-protein ligase that is functionally significant in the regulation of cancer development, muscle cell growth, and neuronal development. Its expression is developmentally regulated during myogenesis and is upregulated in various tumors. RNF13 negatively regulates cell proliferation through its E3 ligase activity. RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) ubiquitination. It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA; also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. ZNRF4, also known as RING finger protein 204 (RNF204), or Nixin, is an endoplasmic reticulum (ER) membrane-anchored ubiquitin ligase that physically interacts with the ER-localized chaperone calnexin in a glycosylation-independent manner, induces calnexin ubiquitination, and p97-dependent degradation, indicating an ER-associated degradation-like mechanism of calnexin turnover. The murine protein sperizin (spermatid-specific ring zinc finger) is a homolog of human ZNRF4. It is specifically expressed in Haploid germ cells and involved in spermatogenesis.
Statistics
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PSSM-Id: 319579
View PSSM: cd16665
Aligned: 15 rows
Threshold Bit Score: 81.2999
Threshold Setting Gi: 544217250
Created: 2-May-2013
Updated: 18-Aug-2016
Structure
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Aligned Rows:
 
Zn binding siteRING-H2 finger
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Comment:Based on the structural evidence that Mus musculus RNF126 (2ECT) binds two Zn2+ ions through its RING-H2 finger.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
Feature 1          #  #              # #  #  #            #  #  
gi 21362880  238 DVCAICLDEYeDGDKLRILPCSHAYHCKCVDPWLTkt-kKTCPVCKQ 283
gi 7298919   233 DTCVICLEDFiEDDKLRVLPCSHPYHTHCIDPWLTen-rRVCPICKR 278
gi 321465867 231 DTCAICLEDYvDGDKLRILPCSHAYHTKCIDPWLTrn-rRVCPVCKR 276
gi 699238109 234 DVCAICLDDYeEGDTLRILPCQHAYHCKCVDPWLTss-rRVCPLCKR 279
gi 675365164 234 DVCAICLEDYnEGDKLRLLPCSHAYHAKCIDPWLMnn-rRNCPLCKR 279
gi 126253848 307 DLCAICLDEYeEGDQLKILPCSHTYHCKCIDPWFSqaprRSCPVCKQ 353
gi 675876150 233 EVCAVCLEDYsFFDKLRILPCSHAFHQKCIDPWLTrn-kQTCPLCNK 278
gi 156215418 264 DVCAICLDEYkEGDKLRILPCDHAYHCKCVDPWLTeg-kRTCPVCKR 309
gi 353231475 111 DVCCICLEDYvDRDKLRLLPCQHAFHMKCIDPWLLcn-rRRCPICNQ 156
gi 919061444 328 DTCAICLDDYeDGEKLRLLPCQHAYHQQCVDPWLTkn-kRVCPVCKA 373

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