2MT5,1IYM,1V87,1X4J,2D8S,2ECL,2ECT,2EP4,2JRJ,2L0B,2LXP,3DPL,3J92,3NW0,4CCG,4UI9,5D0K,5D1K,5O6C,6A3Z,6W7Z,5YWR


Conserved Protein Domain Family
RING-H2
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cd16448: RING-H2 
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H2 subclass of RING (RING-H2) fingers and its variants
The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). This family corresponds to the H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.
Links
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Statistics
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PSSM-Id: 438112
Aligned: 74 rows
Threshold Bit Score: 30.0622
Created: 21-Apr-2015
Updated: 17-Oct-2022
Structure
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Program:
Drawing:
Aligned Rows:
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Zn 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 H C C CClick to see conserved feature residue pattern help
Evidence:
  • Structure:2ECT; Mus musculus RNF126 binds two Zn2+ ions through its RING-H2 finger.
  • Structure:2LXP; Homo sapiens AMFR (also known as ubiquitin ligase GP78) binds two Zn2+ through its RING-H2 finger.
  • Comment:C3H2C3-type RING-H2 finger consensus motif: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-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.
Scroll to Sequence Alignment Display
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1      #  #                          # #  #  #                     #  # 
2MT5_A       9 CGICRmafngccpdckv--pgddcplvwgqCsHcFHmhCILkwlhaq--------qvqqhCPMCR 63   human
2ECT_A      18 CPVCKedyalge------------svrqlpCnHlFHdsCIVpwle-----------qhdsCPVCR 59   house mouse
2LXP_C      15 CAICWdsmqa---------------arklpCgHlFHnsCLRswle-----------qdtsCPTCR 53   human
3J92_0    1715 CMICFsvihgfnys--------lpkkacrtCkKkFHsaCLYkwfts---------snkstCPLCR 1762 human
4CCG_X      20 CGICYayqldgtip--------dqvcdnsqCgQpFHqiCLYewlrglltsrqsfniifgeCPYCS 76   human
6A3Z_A      13 CIICReemvtg--------------akrlpCnHiFHtsCLRswfq-----------rqqtCPTCR 52   human
O95159      53 CRLCNiplasr-------------ettrlvCyDlFHwaCLNeraaqlpr---ntapagyqCPSCN 101  human
Q8WU17     547 CAICYheftts--------------aritpCnHyFHalCLRkwly-----------iqdtCPMCH 586  human
Q13702     363 CGLCGesigekn-----------srlqalpCsHiFHlrCLQnng-------------trsCPNCR 403  human
EDO35865     2 CAICIeklsevsgfcqtasstlpevkkltkCnHcFHeeCLLellkns-------kggyiqCPTCK 59   starlet sea anemone

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