trim13

Tripartite motif containing 13

408 amino acids

E3 ubiquitin ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins (By similarity).

46.602 kDa

MEVLEEDLTCPICCSLFDDPRVLPCSHNFCKKCLDGVLEENSRTMQWRPSSFKCPTCRKETPTMGVNGLQVNYLLKGIVEKYNKIKVSPKMPVCKEHSDQPLNIFCSTDLKLICGSCATTGEHKKHVFSSIGDAYIQEKSSLETLFQGVEEWNSKEVHSHLDTLESNKRKALHSLAKESDKVKAYFEKLQYLLEQKKNEILSDFETLKLAVMQAYDTEINKLHTVLSEQRKACNIVEDLKNISDPFMFLQQMQEFRDKMTFIKEAPLTTGQDVNVNPAMKEFDTSMWDSIKLGEVDKLSLPQDTTSKKEPGDAKTLHSLKPILVVACLILLLVTFLCAYPFIDSLPTFTIDLQVISSYFFTTTAKAANLTILFWEQLSEELLILKQRCQTYVSVFLENVAEFVCKYKL

TRIM13

E3 ubiquitin-protein ligase TRIM13

407 amino acids

Endoplasmic reticulum (ER) membrane anchored E3 ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor. Plays also a role in innate immune response by stimulating NF-kappa-B activity in the TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked polyubiquitination chain resulting in NF-kappa-B activation. Participates as well in T-cell receptor-mediated NF-kappa-B activation. In the presence of TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B.

47.078 kDa

MELLEEDLTCPICCSLFDDPRVLPCSHNFCKKCLEGILEGNVRNSLWRSSPFKCPTCRKETSATGVNSLQVNYSLKGIVEKYNKIKVSPKMPVCKGHLGQPLNIFCLTDMQLICGICATRGEHTKHVFCSIEDAYAQERDAFESLFQSFETWRRGDALSRLDTLETSKRKSLQLLTKDSDKVKEFFEKLQYTLDQKKNEILSDFETMKLAVMQAYDPEINKLNTILQEQRMAFNIAEAFKDVSEPIIFLQQMQEFREKIKVIKETPLPPSNLPSSPLMKNFDTSQWEDIKLVDVDKLSLPQDTGTFISKIPWRLYPLFVVVILLGLLIFFSPTMFLEWSLFDEIATWKDNLSNFSSYLTRSADFVEQSVFYWEQLTDGLFIFSERLKSFTLVVLNNVAEFVCKYKLL

TRIM13

E3 ubiquitin-protein ligase TRIM13

407 amino acids

Endoplasmic reticulum (ER) membrane anchored E3 ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor (PubMed:22178386). Plays also a role in innate immune response by stimulating NF-kappa-B activity in the TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked polyubiquitination chain resulting in NF-kappa-B activation (PubMed:28087809). Participates as well in T-cell receptor-mediated NF-kappa-B activation (PubMed:25088585). In the presence of TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B (PubMed:25152375).

Belongs to the TRIM/RBCC family.

46.988 kDa

MELLEEDLTCPICCSLFDDPRVLPCSHNFCKKCLEGILEGSVRNSLWRPAPFKCPTCRKETSATGINSLQVNYSLKGIVEKYNKIKISPKMPVCKGHLGQPLNIFCLTDMQLICGICATRGEHTKHVFCSIEDAYAQERDAFESLFQSFETWRRGDALSRLDTLETSKRKSLQLLTKDSDKVKEFFEKLQHTLDQKKNEILSDFETMKLAVMQAYDPEINKLNTILQEQRMAFNIAEAFKDVSEPIVFLQQMQEFREKIKVIKETPLPPSNLPASPLMKNFDTSQWEDIKLVDVDKLSLPQDTGTFISKIPWSFYKLFLLILLLGLVIVFGPTMFLEWSLFDDLATWKGCLSNFSSYLTKTADFIEQSVFYWEQVTDGFFIFNERFKNFTLVVLNNVAEFVCKYKLL

Trim13

E3 ubiquitin-protein ligase TRIM13

407 amino acids

Endoplasmic reticulum (ER) membrane anchored E3 ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor. Plays also a role in innate immune response by stimulating NF-kappa-B activity in the TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked polyubiquitination chain resulting in NF-kappa-B activation. Participates as well in T-cell receptor-mediated NF-kappa-B activation. In the presence of TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B.

Belongs to the TRIM/RBCC family.

46.958 kDa

MELLEEDLTCPICCSLFDDPRVLPCSHNFCKKCLEGLLEGNVRNSLWRPSPFKCPTCRKETSATGVNSLQVNYSLKGIVEKYNKIKISPKMPVCKGHLGQPLNIFCVTDMQLICGICATRGEHTKHVFSSIEDAYAREKNAFESLFQSFETWRRGDALSRLDTLETNKRKALQLLTKDSDKVKEFFEKLQHTLDQKKNEILSDFETMKLAVMQTYDPEINKINTILQEQRMAFNIAEAFKDVSEPIIFLQQMQEFREKIKVIKETPLPHSNLPTSPLMKNFDTSQWGDIKLVDVDKLSLPQDTGVFTSKIPWYPYLLLMMVVLLGLLIFFGPTVFLEWSPLDELATWKDYLSSFNSYLTKSADFIEQSVFYWEQMTDGFFIFGERVKNVSLVALNNVAEFICKYKLL

Trim13

E3 ubiquitin-protein ligase TRIM13

407 amino acids

Endoplasmic reticulum (ER) membrane anchored E3 ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor. Plays also a role in innate immune response by stimulating NF-kappa-B activity in the TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked polyubiquitination chain resulting in NF-kappa-B activation. Participates as well in T-cell receptor-mediated NF-kappa-B activation. In the presence of TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B.

46.815 kDa

MELLEEDLTCPICCSLFDDPRVLPCSHNFCKKCLEGLLEGNVRNSLWRPSPFKCPTCRKETSATGVNSLQVNYSLKGIVEKYNKIKISPKMPVCKEHLGQPLNIFCVTDMQLICGVCATRGSHTKHVFSSIEDAYTQERDAFEFLFQSFETWRRGDALSRLDTLETNKRKSLQLLTKDSDKVKEFFEKLQHTLDQKKNEILSDFETMKLAVMQTYDPEINKLNSILQEQRMAFNIAEAFKDVSEPIIFLQQMQEFREKIKVIKETPLPPSNLPTSPLMKNFDTSQWEDIKLVDVDKLSLPQDTGVLTSRSPWHPCLLLMAVVLLGLLVFFGPTVFLEWSPLEELATWKDCLSSFNSYLTKSADFVEQSVFYWEQMTDGLFVFSERVKNVSLVALNNVAEFVCKYKLL

trim13

Tripartite motif-containing 13

404 amino acids

E3 ubiquitin ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins (By similarity).

45.867 kDa

MELLEEDLTCPICCCLFEDPRVLPCSHSFCKKCLEGILDGNRSPTWRPPFKCPTCRKETVHNGIASLQVNYSLRGIVEKYNRIRVMPRMSQCRVHSGQPLNIFCATDLKLICGFCATTGDHKGHKFCALEEAYEREKLAFEELFRVVEGWKGAEVHSCLESLESAKKKALERVSRDADRVSEYFDKLLRTLEHKRSEILSDLETLKLAVMQTFDPEINRLRSALEEQRRALNIAESFRSLSDPLTFLQQMQDFREKLRVIQGTPLPSRTDMDVSLSALQSFDVKEWDRVRLGQVDKLCAPYESSAYLSSLPPAAAPRFTRVMWRVVLVVCACLPALNFLPSDCLALSFQDKVVALGGFSLPSPGEIVRWLGFCWKEAASICTLLTELCRNCMLDLINTTSDFIS