T3JAM_HUMAN
ID T3JAM_HUMAN Reviewed; 551 AA.
AC Q9Y228; A1L464; A6NIU9; Q2YDB5; Q4VY06; Q7Z706;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=TRAF3-interacting JNK-activating modulator;
DE AltName: Full=TRAF3-interacting protein 3;
GN Name=TRAF3IP3; Synonyms=T3JAM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Rhodes S.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-373.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP GLU-373.
RC TISSUE=Blood, and Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAP2K1.
RX PubMed=26195727; DOI=10.1084/jem.20150110;
RA Zou Q., Jin J., Xiao Y., Hu H., Zhou X., Jie Z., Xie X., Li J.Y., Cheng X.,
RA Sun S.C.;
RT "T cell development involves TRAF3IP3-mediated ERK signaling in the
RT Golgi.";
RL J. Exp. Med. 212:1323-1336(2015).
RN [7]
RP FUNCTION, AND INTERACTION WITH PPP2CA.
RX PubMed=30115741; DOI=10.1084/jem.20180397;
RA Yu X., Teng X.L., Wang F., Zheng Y., Qu G., Zhou Y., Hu Z., Wu Z.,
RA Chang Y., Chen L., Li H.B., Su B., Lu L., Liu Z., Sun S.C., Zou Q.;
RT "Metabolic control of regulatory T cell stability and function by TRAF3IP3
RT at the lysosome.";
RL J. Exp. Med. 215:2463-2476(2018).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TLR4.
RX PubMed=30573680; DOI=10.1074/jbc.ra118.003137;
RA Li Y., Guan J., Wang W., Hou C., Zhou L., Ma J., Cheng Y., Jiao S.,
RA Zhou Z.;
RT "TRAF3-interacting JNK-activating modulator promotes inflammation by
RT stimulating translocation of Toll-like receptor 4 to lipid rafts.";
RL J. Biol. Chem. 294:2744-2756(2019).
RN [9]
RP FUNCTION, INTERACTION WITH MAVS AND TRAF3, AND SUBCELLULAR LOCATION.
RX PubMed=31390091; DOI=10.15252/embj.2019102075;
RA Zhu W., Li J., Zhang R., Cai Y., Wang C., Qi S., Chen S., Liang X., Qi N.,
RA Hou F.;
RT "TRAF3IP3 mediates the recruitment of TRAF3 to MAVS for antiviral innate
RT immunity.";
RL EMBO J. 38:e102075-e102075(2019).
RN [10]
RP FUNCTION, AND INTERACTION WITH TBK1 AND TRAF3.
RX PubMed=32366851; DOI=10.1038/s41467-020-16014-0;
RA Deng M., Tam J.W., Wang L., Liang K., Li S., Zhang L., Guo H., Luo X.,
RA Zhang Y., Petrucelli A., Davis B.K., Conti B.J., June Brickey W., Ko C.C.,
RA Lei Y.L., Sun S., Ting J.P.;
RT "TRAF3IP3 negatively regulates cytosolic RNA induced anti-viral signaling
RT by promoting TBK1 K48 ubiquitination.";
RL Nat. Commun. 11:2193-2193(2020).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] SER-529.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Adapter protein that plays essential roles in both innate and
CC adaptive immunity. Plays a crucial role in the regulation of thymocyte
CC development (PubMed:26195727). Mechanistically, mediates TCR-stimulated
CC activation through recruiting MAP2K1/MEK1 to the Golgi and, thereby,
CC facilitating the interaction of MAP2K1/MEK1 with its activator BRAF
CC (PubMed:26195727). Also plays an essential role in regulatory T-cell
CC stability and function by recruiting the serine-threonine phosphatase
CC catalytic subunit (PPP2CA) to the lysosome, thereby facilitating the
CC interaction of PP2Ac with the mTORC1 component RPTOR and restricting
CC glycolytic metabolism (PubMed:30115741). Positively regulates TLR4
CC signaling activity in macrophage-mediated inflammation by acting as a
CC molecular clamp to facilitate LPS-induced translocation of TLR4 to
CC lipid rafts (PubMed:30573680). In response to viral infection,
CC facilitates the recruitment of TRAF3 to MAVS within mitochondria
CC leading to IRF3 activation and interferon production (PubMed:31390091).
CC However, participates in the maintenance of immune homeostasis and the
CC prevention of overzealous innate immunity by promoting 'Lys-48'-
CC dependent ubiquitination of TBK1 (PubMed:32366851).
CC {ECO:0000269|PubMed:26195727, ECO:0000269|PubMed:30115741,
CC ECO:0000269|PubMed:30573680, ECO:0000269|PubMed:31390091,
CC ECO:0000269|PubMed:32366851}.
CC -!- SUBUNIT: Interacts (via its coiled-coil domain) with TRAF3 (via
CC isoleucine zipper) (PubMed:31390091, PubMed:32366851). Interacts with
CC MAP2K1 (PubMed:26195727). Interacts with PPP2CA; this interaction
CC targets PPP2CA to the lysosomes (PubMed:30115741). Interacts with TLR4
CC (PubMed:30573680). Interacts with MAVS (PubMed:31390091). Interacts
CC with TBK1 (PubMed:32366851). {ECO:0000269|PubMed:26195727,
CC ECO:0000269|PubMed:30115741, ECO:0000269|PubMed:30573680,
CC ECO:0000269|PubMed:31390091, ECO:0000269|PubMed:32366851}.
CC -!- INTERACTION:
CC Q9Y228; Q8N350-4: CBARP; NbExp=3; IntAct=EBI-765817, EBI-19051169;
CC Q9Y228; P45973: CBX5; NbExp=3; IntAct=EBI-765817, EBI-78219;
CC Q9Y228; Q96M89-2: CCDC138; NbExp=3; IntAct=EBI-765817, EBI-10972887;
CC Q9Y228; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-765817, EBI-347573;
CC Q9Y228; P24863: CCNC; NbExp=3; IntAct=EBI-765817, EBI-395261;
CC Q9Y228; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-765817, EBI-5278764;
CC Q9Y228; Q76N32-2: CEP68; NbExp=3; IntAct=EBI-765817, EBI-11975967;
CC Q9Y228; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-765817, EBI-739624;
CC Q9Y228; O75208: COQ9; NbExp=3; IntAct=EBI-765817, EBI-724524;
CC Q9Y228; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-765817, EBI-18013275;
CC Q9Y228; Q68CJ9: CREB3L3; NbExp=3; IntAct=EBI-765817, EBI-852194;
CC Q9Y228; O00559: EBAG9; NbExp=3; IntAct=EBI-765817, EBI-8787095;
CC Q9Y228; P50402: EMD; NbExp=9; IntAct=EBI-765817, EBI-489887;
CC Q9Y228; P34910-2: EVI2B; NbExp=3; IntAct=EBI-765817, EBI-17640610;
CC Q9Y228; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-765817, EBI-18304435;
CC Q9Y228; Q969F0: FATE1; NbExp=6; IntAct=EBI-765817, EBI-743099;
CC Q9Y228; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-765817, EBI-5916454;
CC Q9Y228; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-765817, EBI-3917143;
CC Q9Y228; Q8IUY3: GRAMD2A; NbExp=3; IntAct=EBI-765817, EBI-11984319;
CC Q9Y228; Q8N6L0: KASH5; NbExp=6; IntAct=EBI-765817, EBI-749265;
CC Q9Y228; P43628: KIR2DL3; NbExp=3; IntAct=EBI-765817, EBI-8632435;
CC Q9Y228; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-765817, EBI-3044087;
CC Q9Y228; Q96JM7-2: L3MBTL3; NbExp=5; IntAct=EBI-765817, EBI-11985629;
CC Q9Y228; Q9H400: LIME1; NbExp=3; IntAct=EBI-765817, EBI-2830566;
CC Q9Y228; Q8N386: LRRC25; NbExp=3; IntAct=EBI-765817, EBI-11304917;
CC Q9Y228; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-765817, EBI-11956541;
CC Q9Y228; Q9UPX6: MINAR1; NbExp=3; IntAct=EBI-765817, EBI-11977115;
CC Q9Y228; Q9Y3A3: MOB4; NbExp=2; IntAct=EBI-765817, EBI-713935;
CC Q9Y228; Q9GZM8: NDEL1; NbExp=6; IntAct=EBI-765817, EBI-928842;
CC Q9Y228; P59046: NLRP12; NbExp=2; IntAct=EBI-765817, EBI-6374637;
CC Q9Y228; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-765817, EBI-1051317;
CC Q9Y228; Q53GL0: PLEKHO1; NbExp=3; IntAct=EBI-765817, EBI-949945;
CC Q9Y228; P17612: PRKACA; NbExp=3; IntAct=EBI-765817, EBI-476586;
CC Q9Y228; O43586: PSTPIP1; NbExp=3; IntAct=EBI-765817, EBI-1050964;
CC Q9Y228; Q9H0H5: RACGAP1; NbExp=3; IntAct=EBI-765817, EBI-717233;
CC Q9Y228; P54725: RAD23A; NbExp=3; IntAct=EBI-765817, EBI-746453;
CC Q9Y228; Q7Z5B4-5: RIC3; NbExp=3; IntAct=EBI-765817, EBI-12375429;
CC Q9Y228; Q5EBL4-3: RILPL1; NbExp=3; IntAct=EBI-765817, EBI-12072024;
CC Q9Y228; Q9BRV8: SIKE1; NbExp=2; IntAct=EBI-765817, EBI-1773646;
CC Q9Y228; P23497: SP100; NbExp=4; IntAct=EBI-765817, EBI-751145;
CC Q9Y228; P23497-2: SP100; NbExp=3; IntAct=EBI-765817, EBI-6589365;
CC Q9Y228; Q9Y6E0: STK24; NbExp=2; IntAct=EBI-765817, EBI-740175;
CC Q9Y228; Q9H169-2: STMN4; NbExp=3; IntAct=EBI-765817, EBI-20117546;
CC Q9Y228; Q5VSL9: STRIP1; NbExp=2; IntAct=EBI-765817, EBI-1773588;
CC Q9Y228; O43815: STRN; NbExp=2; IntAct=EBI-765817, EBI-1046642;
CC Q9Y228; Q13033: STRN3; NbExp=2; IntAct=EBI-765817, EBI-1053857;
CC Q9Y228; Q16623: STX1A; NbExp=3; IntAct=EBI-765817, EBI-712466;
CC Q9Y228; Q12846: STX4; NbExp=3; IntAct=EBI-765817, EBI-744942;
CC Q9Y228; Q9UBB9: TFIP11; NbExp=4; IntAct=EBI-765817, EBI-1105213;
CC Q9Y228; P37173: TGFBR2; NbExp=3; IntAct=EBI-765817, EBI-296151;
CC Q9Y228; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-765817, EBI-7238458;
CC Q9Y228; Q9NQ86: TRIM36; NbExp=3; IntAct=EBI-765817, EBI-2341518;
CC Q9Y228; Q9BTA9: WAC; NbExp=3; IntAct=EBI-765817, EBI-749118;
CC Q9Y228; O60232: ZNRD2; NbExp=3; IntAct=EBI-765817, EBI-741415;
CC Q9Y228; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-765817, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30573680}.
CC Golgi apparatus membrane {ECO:0000269|PubMed:26195727}; Single-pass
CC type IV membrane protein {ECO:0000305}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q8C0G2}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:31390091}. Note=Accumulates on the mitochondria
CC after virus infection. {ECO:0000269|PubMed:31390091}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y228-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y228-2; Sequence=VSP_017271;
CC Name=3;
CC IsoId=Q9Y228-3; Sequence=VSP_017272, VSP_017273;
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DR EMBL; AL049667; CAB41242.1; -; mRNA.
DR EMBL; AL022398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93444.1; -; Genomic_DNA.
DR EMBL; BC110302; AAI10303.1; -; mRNA.
DR EMBL; BC130417; AAI30418.1; -; mRNA.
DR EMBL; BC144139; AAI44140.1; -; mRNA.
DR CCDS; CCDS1490.2; -. [Q9Y228-1]
DR CCDS; CCDS81422.1; -. [Q9Y228-2]
DR RefSeq; NP_001274683.1; NM_001287754.1.
DR RefSeq; NP_001307072.1; NM_001320143.1. [Q9Y228-1]
DR RefSeq; NP_001307073.1; NM_001320144.1. [Q9Y228-2]
DR RefSeq; NP_079504.2; NM_025228.3. [Q9Y228-1]
DR AlphaFoldDB; Q9Y228; -.
DR SMR; Q9Y228; -.
DR BioGRID; 123249; 80.
DR IntAct; Q9Y228; 88.
DR MINT; Q9Y228; -.
DR STRING; 9606.ENSP00000355991; -.
DR iPTMnet; Q9Y228; -.
DR MetOSite; Q9Y228; -.
DR PhosphoSitePlus; Q9Y228; -.
DR SwissPalm; Q9Y228; -.
DR BioMuta; TRAF3IP3; -.
DR DMDM; 88984949; -.
DR EPD; Q9Y228; -.
DR jPOST; Q9Y228; -.
DR MassIVE; Q9Y228; -.
DR MaxQB; Q9Y228; -.
DR PaxDb; Q9Y228; -.
DR PeptideAtlas; Q9Y228; -.
DR PRIDE; Q9Y228; -.
DR ProteomicsDB; 85616; -. [Q9Y228-1]
DR ProteomicsDB; 85617; -. [Q9Y228-2]
DR ProteomicsDB; 85618; -. [Q9Y228-3]
DR Antibodypedia; 34596; 208 antibodies from 27 providers.
DR DNASU; 80342; -.
DR Ensembl; ENST00000367024.5; ENSP00000355991.1; ENSG00000009790.15. [Q9Y228-1]
DR Ensembl; ENST00000367025.8; ENSP00000355992.3; ENSG00000009790.15. [Q9Y228-1]
DR Ensembl; ENST00000367026.7; ENSP00000355993.3; ENSG00000009790.15. [Q9Y228-2]
DR Ensembl; ENST00000478359.5; ENSP00000417665.1; ENSG00000009790.15. [Q9Y228-3]
DR GeneID; 80342; -.
DR KEGG; hsa:80342; -.
DR MANE-Select; ENST00000367025.8; ENSP00000355992.3; NM_025228.4; NP_079504.2.
DR UCSC; uc001hhm.4; human. [Q9Y228-1]
DR CTD; 80342; -.
DR DisGeNET; 80342; -.
DR GeneCards; TRAF3IP3; -.
DR HGNC; HGNC:30766; TRAF3IP3.
DR HPA; ENSG00000009790; Tissue enriched (lymphoid).
DR MIM; 608255; gene.
DR neXtProt; NX_Q9Y228; -.
DR OpenTargets; ENSG00000009790; -.
DR PharmGKB; PA142670711; -.
DR VEuPathDB; HostDB:ENSG00000009790; -.
DR eggNOG; ENOG502RG0V; Eukaryota.
DR GeneTree; ENSGT00940000160260; -.
DR HOGENOM; CLU_038582_0_0_1; -.
DR InParanoid; Q9Y228; -.
DR OMA; KEKEWDF; -.
DR OrthoDB; 484467at2759; -.
DR PhylomeDB; Q9Y228; -.
DR TreeFam; TF334641; -.
DR PathwayCommons; Q9Y228; -.
DR SignaLink; Q9Y228; -.
DR BioGRID-ORCS; 80342; 14 hits in 1072 CRISPR screens.
DR ChiTaRS; TRAF3IP3; human.
DR GeneWiki; TRAF3IP3; -.
DR GenomeRNAi; 80342; -.
DR Pharos; Q9Y228; Tbio.
DR PRO; PR:Q9Y228; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y228; protein.
DR Bgee; ENSG00000009790; Expressed in granulocyte and 129 other tissues.
DR ExpressionAtlas; Q9Y228; baseline and differential.
DR Genevisible; Q9Y228; HS.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Golgi apparatus;
KW Lysosome; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..551
FT /note="TRAF3-interacting JNK-activating modulator"
FT /id="PRO_0000072403"
FT TOPO_DOM 1..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..544
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..551
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 73..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 240..436
FT /evidence="ECO:0000255"
FT COILED 464..506
FT /evidence="ECO:0000255"
FT VAR_SEQ 95..114
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_017271"
FT VAR_SEQ 352..353
FT /note="GA -> IN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017272"
FT VAR_SEQ 354..551
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017273"
FT VARIANT 373
FT /note="Q -> E (in dbSNP:rs669694)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_024283"
FT VARIANT 529
FT /note="P -> S (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035664"
SQ SEQUENCE 551 AA; 63626 MW; EA2DFF45A8D6ED19 CRC64;
MISPDPRPSP GLARWAESYE AKCERRQEIR ESRRCRPNVT TCRQVGKTLR IQQREQLQRA
RLQQFFRRRN LELEEKGKAQ HPQAREQGPS RRPGQVTVLK EPLSCARRIS SPREQVTGTS
SEVFPAQHPP PSGICRDLSD HLSSQAGGLP PQDTPIKKPP KHHRGTQTKA EGPTIKNDAS
QQTNYGVAVL DKEIIQLSDY LKEALQRELV LKQKMVILQD LLSTLIQASD SSWKGQLNED
KLKGKLRSLE NQLYTCTQKY SPWGMKKVLL EMEDQKNSYE QKAKESLQKV LEEKMNAEQQ
LQSTQRSLAL AEQKCEEWRS QYEALKEDWR TLGTQHRELE SQLHVLQSKL QGADSRDLQM
NQALRFLENE HQQLQAKIEC LQGDRDLCSL DTQDLQDQLK RSEAEKLTLV TRVQQLQGLL
QNQSLQLQEQ EKLLTKKDQA LPVWSPKSFP NEVEPEGTGK EKDWDLRDQL QKKTLQLQAK
EKECRELHSE LDNLSDEYLS CLRKLQHCRE ELNQSQQLPP RRQCGRWLPV LMVVIAAALA
VFLANKDNLM I
