Gene name:
TRIM22(RNF94;STAF50);
Protein name:
E3 ubiquitin-protein ligase TRIM22;
Alternative:
RING finger protein 94;50 kDa-stimulated trans-acting factor;Tripartite motif-containing protein 22;Staf-50;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Interacts with HIV-1 Gag polyprotein; this interaction seems to reduce gag production or virus budding. Interacts with EMCV protease 3C; this interaction leads to viral protease ubiquitination.
Function:
Interferon-induced antiviral protein involved in cell innate immunity. The antiviral activity could in part be mediated by TRIM22-dependent ubiquitination of viral proteins. Plays a role in restricting the replication of HIV-1, encephalomyocarditis virus (EMCV) and hepatitis B virus (HBV). Acts as a transcriptional repressor of HBV core promoter. May have E3 ubiquitin-protein ligase activity.
Subcellular Location:
Cytoplasm
Nucleus
Nucleus speckle
Nucleus
Cajal body
Localizes predominanltly into the nucleus, found in cytoplasm to some extent. Forms distinct nuclear bodies that undergo dynamic changes during cell cycle progression. Nuclear bodies start to form in the early G0/G1 phase but become speckle-like in the S-phase and completely dispersed in mitosis. 35% of TRIM22 nuclear bodies overlap or are found adjacent to Cajal bodies.
Protein Attributes:
50:
MDFSVKVDIE | KEVTCPICLE | LLTEPLSLDC | GHSFCQACIT | AKIKESVIIS |
100:
RGESSCPVCQ | TRFQPGNLRP | NRHLANIVER | VKEVKMSPQE | GQKRDVCEHH |
150:
GKKLQIFCKE | DGKVICWVCE | LSQEHQGHQT | FRINEVVKEC | QEKLQVALQR |
200:
LIKEDQEAEK | LEDDIRQERT | AWKNYIQIER | QKILKGFNEM | RVILDNEEQR |
250:
ELQKLEEGEV | NVLDNLAAAT | DQLVQQRQDA | STLISDLQRR | LRGSSVEMLQ |
300:
DVIDVMKRSE | SWTLKKPKSV | SKKLKSVFRV | PDLSGMLQVL | KELTDVQYYW |
350:
VDVMLNPGSA | TSNVAISVDQ | RQVKTVRTCT | FKNSNPCDFS | AFGVFGCQYF |
400:
SSGKYYWEVD | VSGKIAWILG | VHSKISSLNK | RKSSGFAFDP | SVNYSKVYSR |
450:
YRPQYGYWVI | GLQNTCEYNA | FEDSSSSDPK | VLTLFMAVPP | CRIGVFLDYE |
498:
AGIVSFFNVT | NHGALIYKFS | GCRFSRPAYP | YFNPWNCLVP | MTVCPPSS

Vaild Sequence:
Related Databases
Uniprot: