Conserved Protein Domain Family
RING-HC_RBR_TRIAD1

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cd16773: RING-HC_RBR_TRIAD1 
RING finger, HC subclass, found in two RING fingers and DRIL [double RING finger linked] 1 (TRIAD1)
TRIAD1, also known as ariadne-2 (ARI-2), protein ariadne-2 homolog, Ariadne RBR E3 ubiquitin protein ligase 2 (ARIH2), or UbcM4-interacting protein 48, is a RBR-type E3 ubiquitin-protein ligase that catalyzes the formation of polyubiquitin chains linked via lysine-48, as well as lysine-63 residues. Its auto-ubiquitylation can be catalyzed by the E2 conjugating enzyme UBCH7. TRIAD1 has been implicated in hematopoiesis, specifically in myelopoiesis, as well as in embryogenesis. It functions as a regulator of endosomal transport and is required for the proper function of multivesicular bodies. It also acts as a novel ubiquitination target for proteasome-dependent degradation by murine double minute 2 (MDM2). As a proapoptotic protein, TRIAD1 promotes p53 activation, and inhibits MDM2-mediated p53 ubiquitination and degradation. Furthermore, TRIAD1 can inhibit the ubiquitination and proteasomal degradation of growth factor independence 1 (Gfi1), a transcriptional repressor essential for the function and development of many different hematopoietic lineages. TRIAD1 contains a RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain use an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This family corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination.
Statistics
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PSSM-Id: 319687
View PSSM: cd16773
Aligned: 15 rows
Threshold Bit Score: 77.4227
Threshold Setting Gi: 26454612
Created: 5-Aug-2013
Updated: 18-Aug-2016
Structure
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Aligned Rows:
 
Zn binding siteRING-HC finger
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Comment:Based on the structural evidence that Homo sapiens HHARI (4KBL) binds two Zn2+ ions through its RING-HC finger.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
Feature 1           #  #             # #  #  #                   #    #  
gi 18202259   137 HHCAVCMQfvrkENLLSLACQHQFCRSCWEQHCSVLVKDGvg-vgVSCMAQDCPL 190
gi 31419535   128 LQCGVCLQlvrrDALLSLPCQHSFCKGCWEQHCTVLVKDGvg-veISCMAQDCSL 181
gi 198435524  146 KVCGVCLEtlhrSKLLALNCGHQFCDGCWKQHMVFAVKDGms-qgIPCMEPECTL 199
gi 307111790  150 VSCGVCMCdvprQDTTTMDCGHTFCNDCWQEHMRISISEGms-rrLKCMAGSCGV 203
gi 260814179   32 KQCPVCLQaqeeKDLLSLACNHKFCTDCWQRYFQVQVEDGva-tgVECMWSDCRL 85
gi 18202162   151 QMCPVCASsqlgDKFYSLACGHSFCKDCWTIYFETQIFQGis-tqIGCMAQMCNV 204
gi 443728564  132 FVCSVCMQrchtDVISTLNCGHQFCSECWEMYFQVQIKVGis-ttLECMGKDCET 185
gi 308220078  165 GTCLICYAp--nSETIGMLCKHYFCKSCWNIYFTTQIMDNgiaenIQCMETDCST 217
gi 215492132  125 VQCPICLQnspgDRFRGLACGHYFCPDCWAMHFEIQILQGis-taIECMGQYCNI 178
gi 121887226  105 TTCNVCSSevigKNMFSLACEHYFCKKCWKAHIETQMNSGnl--fIHCMEPGCRC 157

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