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E3 ubiquitin ligase TRAF3IP2 (EC 2.3.2.27) (Adapter protein CIKS) (Connection to IKK and SAPK/JNK) (E3 ubiquitin-protein ligase CIKS) (Nuclear factor NF-kappa-B activator 1) (ACT1) (TRAF3-interacting protein 2)

 CIKS_HUMAN              Reviewed;         574 AA.
O43734; B2RAY9; E1P555; Q5R3A3; Q7Z6Q1; Q7Z6Q2; Q7Z6Q3; Q9H5W2; Q9H6Y3;
Q9NS14; Q9UG72;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
02-JUN-2021, entry version 184.
RecName: Full=E3 ubiquitin ligase TRAF3IP2 {ECO:0000303|PubMed:19825828};
EC=2.3.2.27 {ECO:0000269|PubMed:19825828};
AltName: Full=Adapter protein CIKS;
AltName: Full=Connection to IKK and SAPK/JNK;
AltName: Full=E3 ubiquitin-protein ligase CIKS;
AltName: Full=Nuclear factor NF-kappa-B activator 1;
Short=ACT1;
AltName: Full=TRAF3-interacting protein 2;
Name=TRAF3IP2 {ECO:0000312|HGNC:HGNC:1343};
Synonyms=C6orf2, C6orf4, C6orf5, C6orf6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=10903453; DOI=10.1016/s0378-1119(00)00231-6;
Morelli C., Magnanini C., Mungall A.J., Negrini M., Barbanti-Brodano G.;
"Cloning and characterization of two overlapping genes in a subregion at
6q21 involved in replicative senescence and schizophrenia.";
Gene 252:217-225(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLN-332.
TISSUE=Embryonic kidney;
PubMed=10962024; DOI=10.1073/pnas.160265197;
Li X., Commane M., Nie H., Hua X., Chatterjee-Kishore M., Wald D., Haag M.,
Stark G.R.;
"Act1, an NF-kappa B-activating protein.";
Proc. Natl. Acad. Sci. U.S.A. 97:10489-10493(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=10962033; DOI=10.1073/pnas.190245697;
Leonardi A., Chariot A., Claudio E., Cunningham K., Siebenlist U.;
"CIKS, a connection to Ikappa B kinase and stress-activated protein
kinase.";
Proc. Natl. Acad. Sci. U.S.A. 97:10494-10499(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 5), AND VARIANT
GLN-332.
TISSUE=Colon, and Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLN-332.
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-332.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND VARIANT
GLN-332.
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH TRAF6.
PubMed=12459498; DOI=10.1016/s0014-5793(02)03688-8;
Kanamori M., Kai C., Hayashizaki Y., Suzuki H.;
"NF-kappaB activator Act1 associates with IL-1/Toll pathway adapter
molecule TRAF6.";
FEBS Lett. 532:241-246(2002).
[10]
FUNCTION, MUTAGENESIS OF LEU-303; PRO-318; VAL-319 AND LEU-324, INTERACTION
WITH IL17RA AND TRAF6, AND CATALYTIC ACTIVITY.
PubMed=19825828; DOI=10.1126/scisignal.2000382;
Liu C., Qian W., Qian Y., Giltiay N.V., Lu Y., Swaidani S., Misra S.,
Deng L., Chen Z.J., Li X.;
"Act1, a U-box E3 ubiquitin ligase for IL-17 signaling.";
Sci. Signal. 2:ra63-ra63(2009).
[11]
INTERACTION WITH IL17RA AND TRAF6, AND FUNCTION.
PubMed=33723527; DOI=10.1016/j.isci.2021.102293;
Lin X., Fu B., Yin S., Li Z., Liu H., Zhang H., Xing N., Wang Y., Xue W.,
Xiong Y., Zhang S., Zhao Q., Xu S., Zhang J., Wang P., Nian W., Wang X.,
Wu H.;
"Title: ORF8 contributes to cytokine storm during SARS-CoV-2 infection by
activating IL-17 pathway.";
IScience 1:102293-102293(2021).
[12]
INVOLVEMENT IN SUSCEPTIBILITY TO PSORS13, VARIANT ASN-19, AND
CHARACTERIZATION OF VARIANT ASN-19.
PubMed=20953186; DOI=10.1038/ng.688;
Huffmeier U., Uebe S., Ekici A.B., Bowes J., Giardina E., Korendowych E.,
Juneblad K., Apel M., McManus R., Ho P., Bruce I.N., Ryan A.W., Behrens F.,
Lascorz J., Bohm B., Traupe H., Lohmann J., Gieger C., Wichmann H.E.,
Herold C., Steffens M., Klareskog L., Wienker T.F., Fitzgerald O.,
Alenius G.M., McHugh N.J., Novelli G., Burkhardt H., Barton A., Reis A.;
"Common variants at TRAF3IP2 are associated with susceptibility to
psoriatic arthritis and psoriasis.";
Nat. Genet. 42:996-999(2010).
[13]
VARIANT PSORS13 ASN-19.
PubMed=20953188; DOI=10.1038/ng.689;
Ellinghaus E., Ellinghaus D., Stuart P.E., Nair R.P., Debrus S.,
Raelson J.V., Belouchi M., Fournier H., Reinhard C., Ding J., Li Y.,
Tejasvi T., Gudjonsson J., Stoll S.W., Voorhees J.J., Lambert S.,
Weidinger S., Eberlein B., Kunz M., Rahman P., Gladman D.D., Gieger C.,
Wichmann H.E., Karlsen T.H., Mayr G., Albrecht M., Kabelitz D.,
Mrowietz U., Abecasis G.R., Elder J.T., Schreiber S., Weichenthal M.,
Franke A.;
"Genome-wide association study identifies a psoriasis susceptibility locus
at TRAF3IP2.";
Nat. Genet. 42:991-995(2010).
[14]
VARIANT CANDF8 ILE-536, CHARACTERIZATION OF VARIANT CANDF8 ILE-536,
FUNCTION, AND INTERACTION WITH IL17RA; IL17RB AND IL17RC.
PubMed=24120361; DOI=10.1016/j.immuni.2013.09.002;
Boisson B., Wang C., Pedergnana V., Wu L., Cypowyj S., Rybojad M.,
Belkadi A., Picard C., Abel L., Fieschi C., Puel A., Li X., Casanova J.L.;
"An ACT1 mutation selectively abolishes interleukin-17 responses in humans
with chronic mucocutaneous candidiasis.";
Immunity 39:676-686(2013).
-!- FUNCTION: E3 ubiquitin ligase that catalyzes 'Lys-63'-linked
polyubiquitination of target protein, enhancing protein-protein
interaction and cell signaling (PubMed:19825828). Transfers ubiquitin
from E2 ubiquitin-conjugating enzyme UBE2V1-UBE2N to substrate protein
(PubMed:19825828). Essential adapter molecule in IL17A-mediated
signaling (PubMed:19825828, PubMed:24120361). Upon IL17A stimulation,
interacts with IL17RA and IL17RC receptor chains through SEFIR domains
and catalyzes 'Lys-63'-linked polyubiquitination of TRAF6, leading to
TRAF6-mediated activation of NF-kappa-B and MAPkinase pathways
(PubMed:19825828). {ECO:0000269|PubMed:19825828,
ECO:0000269|PubMed:24120361, ECO:0000269|PubMed:33723527}.
-!- CATALYTIC ACTIVITY:
Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
[acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
EC=2.3.2.27; Evidence={ECO:0000269|PubMed:19825828};
-!- SUBUNIT: Interacts with IKBKG/NF-kappa B essential modulator, with
CHUK/IKK-alpha and with IKBKB/IKK-beta (PubMed:12459498). Interacts
with TRAF6; this interaction is direct (PubMed:12459498,
PubMed:19825828). Interacts with IL17RA and IL17RC (PubMed:19825828,
PubMed:24120361, PubMed:33723527). Interacts with IL17RB
(PubMed:24120361). {ECO:0000269|PubMed:12459498,
ECO:0000269|PubMed:19825828, ECO:0000269|PubMed:24120361,
ECO:0000269|PubMed:33723527}.
-!- INTERACTION:
O43734; Q96C98: FHL3; NbExp=3; IntAct=EBI-744798, EBI-10229248;
O43734; Q13084: MRPL28; NbExp=3; IntAct=EBI-744798, EBI-723426;
O43734; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-744798, EBI-10182375;
O43734; O75716: STK16; NbExp=3; IntAct=EBI-744798, EBI-749295;
O43734; Q9Y4K3: TRAF6; NbExp=4; IntAct=EBI-744798, EBI-359276;
O43734; Q15654: TRIP6; NbExp=3; IntAct=EBI-744798, EBI-742327;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=C6ORF4;
IsoId=O43734-1; Sequence=Displayed;
Name=2; Synonyms=C6ORF5, C6ORF6;
IsoId=O43734-2; Sequence=VSP_004163;
Name=3;
IsoId=O43734-3; Sequence=VSP_035733;
Name=4;
IsoId=O43734-4; Sequence=VSP_040374;
Name=5;
IsoId=O43734-5; Sequence=VSP_004163, VSP_047098;
-!- TISSUE SPECIFICITY: Widely expressed.
-!- DISEASE: Psoriasis 13 (PSORS13) [MIM:614070]: A common, chronic
inflammatory disease of the skin with multifactorial etiology. It is
characterized by red, scaly plaques usually found on the scalp, elbows
and knees. These lesions are caused by abnormal keratinocyte
proliferation and infiltration of inflammatory cells into the dermis
and epidermis. {ECO:0000269|PubMed:20953186,
ECO:0000269|PubMed:20953188}. Note=Disease susceptibility is associated
with variants affecting the gene represented in this entry.
-!- DISEASE: Candidiasis, familial, 8 (CANDF8) [MIM:615527]: A primary
immunodeficiency disorder with altered immune responses and impaired
clearance of fungal infections, selective against Candida. It is
characterized by persistent and/or recurrent infections of the skin,
nails and mucous membranes caused by organisms of the genus Candida,
mainly Candida albicans. {ECO:0000269|PubMed:24120361}. Note=The
disease is caused by variants affecting the gene represented in this
entry.
-!- CAUTION: The presence of U-box domain is not predicted by SMART and
SWISS-MODEL tools. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB15507.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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EMBL; AF136405; AAF67445.1; -; mRNA.
EMBL; AF136406; AAF67446.1; -; mRNA.
EMBL; AF136407; AAF67447.1; -; mRNA.
EMBL; AF274303; AAG15367.1; -; mRNA.
EMBL; AF272151; AAG15407.1; -; mRNA.
EMBL; AK025351; BAB15117.1; -; mRNA.
EMBL; AK026602; BAB15507.1; ALT_INIT; mRNA.
EMBL; AK314415; BAG37036.1; -; mRNA.
EMBL; AL050289; CAB43390.1; -; mRNA.
EMBL; AL008730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z97989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48285.1; -; Genomic_DNA.
EMBL; CH471051; EAW48287.1; -; Genomic_DNA.
EMBL; BC002823; AAH02823.1; -; mRNA.
EMBL; BI856094; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS5092.1; -. [O43734-1]
CCDS; CCDS5093.1; -. [O43734-2]
CCDS; CCDS55049.1; -. [O43734-4]
CCDS; CCDS55050.1; -. [O43734-5]
PIR; T08794; T08794.
RefSeq; NP_001157753.1; NM_001164281.2. [O43734-5]
RefSeq; NP_001157755.1; NM_001164283.2. [O43734-4]
RefSeq; NP_671733.2; NM_147200.2. [O43734-1]
RefSeq; NP_679211.2; NM_147686.3. [O43734-2]
RefSeq; XP_006715382.1; XM_006715319.3.
RefSeq; XP_011533688.1; XM_011535386.1.
SMR; O43734; -.
BioGRID; 115979; 44.
IntAct; O43734; 18.
MINT; O43734; -.
STRING; 9606.ENSP00000357750; -.
ChEMBL; CHEMBL4523586; -.
GlyConnect; 2015; 3 N-Linked glycans (1 site).
GlyGen; O43734; 1 site, 3 N-linked glycans (1 site).
iPTMnet; O43734; -.
PhosphoSitePlus; O43734; -.
BioMuta; TRAF3IP2; -.
jPOST; O43734; -.
MassIVE; O43734; -.
MaxQB; O43734; -.
PaxDb; O43734; -.
PeptideAtlas; O43734; -.
PRIDE; O43734; -.
ProteomicsDB; 49136; -. [O43734-1]
ProteomicsDB; 49137; -. [O43734-2]
ProteomicsDB; 49138; -. [O43734-3]
ProteomicsDB; 49139; -. [O43734-4]
ProteomicsDB; 69454; -.
Antibodypedia; 19327; 428 antibodies.
DNASU; 10758; -.
Ensembl; ENST00000340026; ENSP00000345984; ENSG00000056972. [O43734-1]
Ensembl; ENST00000359831; ENSP00000352889; ENSG00000056972. [O43734-5]
Ensembl; ENST00000368730; ENSP00000498323; ENSG00000056972. [O43734-4]
Ensembl; ENST00000368734; ENSP00000498345; ENSG00000056972. [O43734-4]
Ensembl; ENST00000368735; ENSP00000357724; ENSG00000056972. [O43734-4]
Ensembl; ENST00000368761; ENSP00000357750; ENSG00000056972. [O43734-2]
Ensembl; ENST00000392556; ENSP00000376339; ENSG00000056972. [O43734-1]
GeneID; 10758; -.
KEGG; hsa:10758; -.
UCSC; uc003pvf.5; human. [O43734-1]
CTD; 10758; -.
DisGeNET; 10758; -.
GeneCards; TRAF3IP2; -.
HGNC; HGNC:1343; TRAF3IP2.
HPA; ENSG00000056972; Low tissue specificity.
MalaCards; TRAF3IP2; -.
MIM; 607043; gene.
MIM; 614070; phenotype.
MIM; 615527; phenotype.
neXtProt; NX_O43734; -.
OpenTargets; ENSG00000056972; -.
Orphanet; 1334; Chronic mucocutaneous candidiasis.
PharmGKB; PA25938; -.
VEuPathDB; HostDB:ENSG00000056972.18; -.
eggNOG; ENOG502QTXH; Eukaryota.
GeneTree; ENSGT00940000161944; -.
HOGENOM; CLU_036721_1_0_1; -.
InParanoid; O43734; -.
OMA; QNTHIYN; -.
OrthoDB; 1353706at2759; -.
PhylomeDB; O43734; -.
TreeFam; TF329063; -.
PathwayCommons; O43734; -.
SignaLink; O43734; -.
SIGNOR; O43734; -.
BioGRID-ORCS; 10758; 6 hits in 989 CRISPR screens.
ChiTaRS; TRAF3IP2; human.
GeneWiki; TRAF3IP2; -.
GenomeRNAi; 10758; -.
Pharos; O43734; Tbio.
PRO; PR:O43734; -.
Proteomes; UP000005640; Chromosome 6.
RNAct; O43734; protein.
Bgee; ENSG00000056972; Expressed in left coronary artery and 225 other tissues.
ExpressionAtlas; O43734; baseline and differential.
Genevisible; O43734; HS.
GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
GO; GO:0002344; P:B cell affinity maturation; IEA:Ensembl.
GO; GO:0001783; P:B cell apoptotic process; IEA:Ensembl.
GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
GO; GO:0023035; P:CD40 signaling pathway; IEA:Ensembl.
GO; GO:1990959; P:eosinophil homeostasis; IEA:Ensembl.
GO; GO:0002447; P:eosinophil mediated immunity; IEA:Ensembl.
GO; GO:0006959; P:humoral immune response; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IDA:MGI.
GO; GO:0097400; P:interleukin-17-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0038173; P:interleukin-17A-mediated signaling pathway; IDA:MGI.
GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
GO; GO:0002269; P:leukocyte activation involved in inflammatory response; IEA:Ensembl.
GO; GO:0048255; P:mRNA stabilization; IEA:Ensembl.
GO; GO:0070254; P:mucus secretion; IEA:Ensembl.
GO; GO:0042119; P:neutrophil activation; IEA:Ensembl.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:CACAO.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
GO; GO:0043588; P:skin development; IEA:Ensembl.
GO; GO:0042110; P:T cell activation; IEA:Ensembl.
GO; GO:0002334; P:transitional two stage B cell differentiation; IEA:Ensembl.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
InterPro; IPR013568; SEFIR_dom.
Pfam; PF08357; SEFIR; 1.
PROSITE; PS51534; SEFIR; 1.
1: Evidence at protein level;
Alternative splicing; Disease variant; Inflammatory response;
Reference proteome; Transferase; Ubl conjugation pathway.
CHAIN 1..574
/note="E3 ubiquitin ligase TRAF3IP2"
/id="PRO_0000089751"
DOMAIN 409..550
/note="SEFIR"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00867"
REGION 1..256
/note="Mediates interaction with TRAF6"
/evidence="ECO:0000269|PubMed:12459498"
REGION 1..67
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 155..211
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 327..403
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 48..67
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 168..190
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 375..395
/note="Pro residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
VAR_SEQ 1..465
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_040374"
VAR_SEQ 1..421
/note="Missing (in isoform 3)"
/evidence="ECO:0000305"
/id="VSP_035733"
VAR_SEQ 1..9
/note="Missing (in isoform 2 and isoform 5)"
/evidence="ECO:0000303|PubMed:10903453,
ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005"
/id="VSP_004163"
VAR_SEQ 463
/note="Missing (in isoform 5)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_047098"
VARIANT 19
/note="D -> N (in PSORS13; there is a reducing binding of
this variant to TRAF6; dbSNP:rs33980500)"
/evidence="ECO:0000269|PubMed:20953186,
ECO:0000269|PubMed:20953188"
/id="VAR_047349"
VARIANT 83
/note="R -> W (in dbSNP:rs13190932)"
/id="VAR_031227"
VARIANT 332
/note="H -> Q (in dbSNP:rs1043730)"
/evidence="ECO:0000269|PubMed:10962024,
ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005, ECO:0000269|Ref.7"
/id="VAR_024307"
VARIANT 536
/note="T -> I (in CANDF8; abolishes homotypic interactions
with the SEFIR domain of IL17RA, IL17RB and IL17RC; does
not affect homodimerization; does not affect SEFIR-
independent interactions with other proteins;
dbSNP:rs397518485)"
/evidence="ECO:0000269|PubMed:24120361"
/id="VAR_070904"
MUTAGEN 303
/note="L->G: Loss of E3 ubiquitin ligase activity."
/evidence="ECO:0000269|PubMed:19825828"
MUTAGEN 318
/note="P->G: Decreases E3 ubiquitin ligase activity."
/evidence="ECO:0000269|PubMed:19825828"
MUTAGEN 319
/note="V->R: Loss of E3 ubiquitin ligase activity."
/evidence="ECO:0000269|PubMed:19825828"
MUTAGEN 324
/note="L->R: Decreases E3 ubiquitin ligase activity."
/evidence="ECO:0000269|PubMed:19825828"
CONFLICT 334
/note="E -> D (in Ref. 3; AAG15407)"
/evidence="ECO:0000305"
CONFLICT 347
/note="P -> S (in Ref. 1; AAF67447)"
/evidence="ECO:0000305"
SEQUENCE 574 AA; 64666 MW; 4985795466D71422 CRC64;
MPPQLQETRM NRSIPVEVDE SEPYPSQLLK PIPEYSPEEE SEPPAPNIRN MAPNSLSAPT
MLHNSSGDFS QAHSTLKLAN HQRPVSRQVT CLRTQVLEDS EDSFCRRHPG LGKAFPSGCS
AVSEPASESV VGALPAEHQF SFMEKRNQWL VSQLSAASPD TGHDSDKSDQ SLPNASADSL
GGSQEMVQRP QPHRNRAGLD LPTIDTGYDS QPQDVLGIRQ LERPLPLTSV CYPQDLPRPL
RSREFPQFEP QRYPACAQML PPNLSPHAPW NYHYHCPGSP DHQVPYGHDY PRAAYQQVIQ
PALPGQPLPG ASVRGLHPVQ KVILNYPSPW DHEERPAQRD CSFPGLPRHQ DQPHHQPPNR
AGAPGESLEC PAELRPQVPQ PPSPAAVPRP PSNPPARGTL KTSNLPEELR KVFITYSMDT
AMEVVKFVNF LLVNGFQTAI DIFEDRIRGI DIIKWMERYL RDKTVMIIVA ISPKYKQDVE
GAESQLDEDE HGLHTKYIHR MMQIEFIKQG SMNFRFIPVL FPNAKKEHVP TWLQNTHVYS
WPKNKKNILL RLLREEEYVA PPRGPLPTLQ VVPL


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Related Genes :
[TRAF3IP2 C6orf2 C6orf4 C6orf5 C6orf6] E3 ubiquitin ligase TRAF3IP2 (EC 2.3.2.27) (Adapter protein CIKS) (Connection to IKK and SAPK/JNK) (E3 ubiquitin-protein ligase CIKS) (Nuclear factor NF-kappa-B activator 1) (ACT1) (TRAF3-interacting protein 2)
[TRAF6 RNF85] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (Interleukin-1 signal transducer) (RING finger protein 85) (RING-type E3 ubiquitin transferase TRAF6)
[TRAF3 CAP1 CRAF1] TNF receptor-associated factor 3 (EC 2.3.2.27) (CAP-1) (CD40 receptor-associated factor 1) (CRAF1) (CD40-binding protein) (CD40BP) (LMP1-associated protein 1) (LAP1) (RING-type E3 ubiquitin transferase TRAF3)
[Traf6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[TRAF6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[Traf6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[Traf2] TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2)
[TRAF2 TRAP3] TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2) (Tumor necrosis factor type 2 receptor-associated protein 3)
[Traf3 Craf1 Trafamn] TNF receptor-associated factor 3 (EC 2.3.2.27) (CD40 receptor-associated factor 1) (CRAF1) (RING-type E3 ubiquitin transferase TRAF3) (TRAFAMN)
[TRAF6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[TRAF6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[TRAF6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[UBE2N BLU] Ubiquitin-conjugating enzyme E2 N (EC 2.3.2.23) (Bendless-like ubiquitin-conjugating enzyme) (E2 ubiquitin-conjugating enzyme N) (Ubc13) (UbcH13) (Ubiquitin carrier protein N) (Ubiquitin-protein ligase N)
[UBE2V1 CROC1 UBE2V UEV1 P/OKcl.19] Ubiquitin-conjugating enzyme E2 variant 1 (UEV-1) (CROC-1) (TRAF6-regulated IKK activator 1 beta Uev1A)
[TRIM28 KAP1 RNF96 TIF1B] Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-associated protein 1) (KAP-1) (KRAB-interacting protein 1) (KRIP-1) (Nuclear corepressor KAP-1) (RING finger protein 96) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)
[RNF4 SNURF RES4-26] E3 ubiquitin-protein ligase RNF4 (EC 2.3.2.27) (RING finger protein 4) (RING-type E3 ubiquitin transferase RNF4) (Small nuclear ring finger protein) (Protein SNURF)
[ITCH] E3 ubiquitin-protein ligase Itchy homolog (Itch) (EC 2.3.2.26) (Atrophin-1-interacting protein 4) (AIP4) (HECT-type E3 ubiquitin transferase Itchy homolog) (NFE2-associated polypeptide 1) (NAPP1)
[IKBKG FIP3 NEMO] NF-kappa-B essential modulator (NEMO) (FIP-3) (IkB kinase-associated protein 1) (IKKAP1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier)
[IKBKB IKKB] Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB) (Serine/threonine protein kinase IKBKB) (EC 2.7.11.1)
[PELI1 PRISM] E3 ubiquitin-protein ligase pellino homolog 1 (Pellino-1) (EC 2.3.2.27) (Pellino-related intracellular-signaling molecule) (RING-type E3 ubiquitin transferase pellino homolog 1)
[XIAP API3 BIRC4 IAP3] E3 ubiquitin-protein ligase XIAP (EC 2.3.2.27) (Baculoviral IAP repeat-containing protein 4) (IAP-like protein) (ILP) (hILP) (Inhibitor of apoptosis protein 3) (IAP-3) (hIAP-3) (hIAP3) (RING-type E3 ubiquitin transferase XIAP) (X-linked inhibitor of apoptosis protein) (X-linked IAP)
[RBX1 RNF75 ROC1] E3 ubiquitin-protein ligase RBX1 (EC 2.3.2.27) (EC 2.3.2.32) (E3 ubiquitin-protein transferase RBX1) (Protein ZYP) (RING finger protein 75) (RING-box protein 1) (Rbx1) (Regulator of cullins 1) (ROC1) [Cleaved into: E3 ubiquitin-protein ligase RBX1, N-terminally processed (E3 ubiquitin-protein transferase RBX1, N-terminally processed)]
[Ikbke Ikke Ikki] Inhibitor of nuclear factor kappa-B kinase subunit epsilon (I-kappa-B kinase epsilon) (IKK-E) (IKK-epsilon) (IkBKE) (EC 2.7.11.10) (Inducible I kappa-B kinase) (IKK-i)
[RBCK1 C20orf18 RNF54 UBCE7IP3 XAP3 XAP4] RanBP-type and C3HC4-type zinc finger-containing protein 1 (EC 2.3.2.31) (HBV-associated factor 4) (Heme-oxidized IRP2 ubiquitin ligase 1) (HOIL-1) (Hepatitis B virus X-associated protein 4) (RING finger protein 54) (RING-type E3 ubiquitin transferase HOIL-1) (Ubiquitin-conjugating enzyme 7-interacting protein 3)
[Peli1] E3 ubiquitin-protein ligase pellino homolog 1 (Pellino-1) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase pellino homolog 1)
[TRIM13 LEU5 RFP2 RNF77] E3 ubiquitin-protein ligase TRIM13 (EC 2.3.2.27) (B-cell chronic lymphocytic leukemia tumor suppressor Leu5) (Leukemia-associated protein 5) (Putative tumor suppressor RFP2) (RING finger protein 77) (RING-type E3 ubiquitin transferase TRIM13) (Ret finger protein 2) (Tripartite motif-containing protein 13)
[Rbck1 Pkcbpb15 Rbck Ubce7ip3] RanBP-type and C3HC4-type zinc finger-containing protein 1 (EC 2.3.2.31) (Heme-oxidized IRP2 ubiquitin ligase 1 homolog) (HOIL-1) (Protein kinase C-binding protein beta-15) (RBCC protein interacting with PKC) (RING-type E3 ubiquitin transferase HOIL-1) (Ubiquitin-conjugating enzyme 7-interacting protein 3)
[Rnf31 Paul] E3 ubiquitin-protein ligase RNF31 (EC 2.3.2.31) (HOIL-1-interacting protein) (HOIP) (Putative Ariadne-like ubiquitin ligase) (PAUL) (RING finger protein 31) (RING-type E3 ubiquitin transferase RNF31)
[STUB1 CHIP PP1131] E3 ubiquitin-protein ligase CHIP (EC 2.3.2.27) (Antigen NY-CO-7) (CLL-associated antigen KW-8) (Carboxy terminus of Hsp70-interacting protein) (RING-type E3 ubiquitin transferase CHIP) (STIP1 homology and U box-containing protein 1)
[ufd-2 T05H10.5] Ubiquitin conjugation factor E4 ufd-2 (EC 2.3.2.27) (E4 ubiquitin-protein ligase ufd-2) (RING-type E3 ubiquitin transferase E4) (Ubiquitin fusion degradation protein 2)

Bibliography :
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