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 29-SEP-2021, entry version 150. 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). Plays also 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 SMR; Q9Y228; -. DR BioGRID; 123249; 73. 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 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; 206 antibodies. DR DNASU; 80342; -. DR Ensembl; ENST00000367024; ENSP00000355991; ENSG00000009790. [Q9Y228-1] DR Ensembl; ENST00000367025; ENSP00000355992; ENSG00000009790. [Q9Y228-1] DR Ensembl; ENST00000367026; ENSP00000355993; ENSG00000009790. [Q9Y228-2] DR Ensembl; ENST00000478359; ENSP00000417665; ENSG00000009790. [Q9Y228-3] DR GeneID; 80342; -. DR KEGG; hsa:80342; -. 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 enhanced (blood, lymphoid tissue). 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; MVMIAIA; -. DR OrthoDB; 484467at2759; -. DR PhylomeDB; Q9Y228; -. DR TreeFam; TF334641; -. DR PathwayCommons; Q9Y228; -. DR BioGRID-ORCS; 80342; 7 hits in 1010 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 172 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 //