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   27-MAR-2024, entry version 162.
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;
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyGen; Q9Y228; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000355991; -.
DR   PeptideAtlas; Q9Y228; -.
DR   ProteomicsDB; 85616; -. [Q9Y228-1]
DR   ProteomicsDB; 85617; -. [Q9Y228-2]
DR   ProteomicsDB; 85618; -. [Q9Y228-3]
DR   Antibodypedia; 34596; 235 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   AGR; HGNC:30766; -.
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; 5308930at2759; -.
DR   PhylomeDB; Q9Y228; -.
DR   TreeFam; TF334641; -.
DR   PathwayCommons; Q9Y228; -.
DR   SignaLink; Q9Y228; -.
DR   BioGRID-ORCS; 80342; 15 hits in 1148 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 130 other cell types or tissues.
DR   ExpressionAtlas; Q9Y228; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProt.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0060090; F:molecular adaptor activity; IDA:UniProt.
DR   GO; GO:0002753; P:cytoplasmic pattern recognition receptor signaling pathway; IDA:UniProt.
DR   GO; GO:0032481; P:positive regulation of type I interferon production; IDA:UniProt.
DR   CDD; cd21912; CC1_T3JAM; 1.
DR   PANTHER; PTHR15715; CENTROSOMAL PROTEIN OF 170 KDA; 1.
DR   PANTHER; PTHR15715:SF21; TRAF3-INTERACTING JNK-ACTIVATING MODULATOR; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   Genevisible; Q9Y228; HS.
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
//