Conserved Protein Domain Family
RING-HC_TRIM36_C-I
?
cd16756: RING-HC_TRIM36_C-I 
RING finger, HC subclass, found in tripartite motif-containing protein 36 (TRIM36) and similar proteins
TRIM36, the human ortholog of mouse Haprin, also known as RING finger protein 98 (RNF98) or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in carcinogenesis. TRIM36 functions upstream of Wnt/beta-catenin activation, and plays a role in controlling the stability of proteins regulating microtubule polymerization during cortical rotation, and subsequently dorsal axis formation. It is also potentially associated with chromosome segregation by interacting with the kinetochore protein centromere protein-H (CENP-H), and colocalizing with the microtubule protein alpha-tubulin. Its overexpression may cause chromosomal instability and carcinogenesis. It is, thus, a novel regulator affecting cell cycle progression. Moreover, TRIM36 plays a critical role in the arrangement of somites during embryogenesis. TRIM36 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.
Links
?
Statistics
?
PSSM-Id: 438414
Aligned: 5 rows
Threshold Bit Score: 83.8102
Created: 3-May-2013
Updated: 17-Oct-2022
Structure
?
Aligned Rows:
Download Cn3D
 
Zn binding site
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:
  • Comment:based on the structures of other RING-HC fingers with bound zinc
  • 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.
Scroll to Sequence Alignment Display
Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection: 
Feature 1             #  #           # #  #  #                                                   
Q9NQ86        28 ERELICPACKELFThPLILPCQHSICHKCVKELLltlddsfndvgsdnsnqssprlrlp--------------------- 86  human
NP_001084586  21 ERELVCPSCKELYThPLILPCQHNICHKCLKELLylsledstdvsseastpgsprirltspsver---------idrlvr 91  African clawed ...
EOB04435       4 ERELICPACKELFThPLILPCQHNVCHKCVKEILftledsfadggsessnqsspririsspsmd-----------ridri 72  mallard
XP_007895574  15 ERELICPSCKELFThPLILPCQHSVCHKCAKELLlsredafgetdsefsnpstpissprarrlssasverldrlnrtasm 94  elephant shark
XP_014341623  28 ERELICPVCKELFThPLILPCQHSVCHKCVKELFllyhedsvtevgsessnpgsprsvgfgsp-------------sier 94  coelacanth

Feature 1                                    #  #       
Q9NQ86        87 spsmdkidrinrpgwkrnsltprtTVFPCPGCEHDVDLG 125 human
NP_001084586  92 sasqrnslgrrsigskrnsltpkiTTIACPGCLHDVDLG 130 African clawed frog
EOB04435      73 srsasqrrsfgwrgrkrnsltprtTLFPCPGCQHDIDLG 111 mallard
XP_007895574  95 rrsfrkkgsgthqgwkrtihsqgvTTFPCPSCKHDVDLG 133 elephant shark
XP_014341623  95 idrlvrsgsatyssrkrssltpriTTFPCPGCQCDIDLG 133 coelacanth

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap