ID MALT1_HUMAN Reviewed; 824 AA. AC Q9UDY8; Q9NTB7; Q9ULX4; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 15-MAR-2017, entry version 174. DE RecName: Full=Mucosa-associated lymphoid tissue lymphoma translocation protein 1; DE EC=3.4.22.-; DE AltName: Full=MALT lymphoma-associated translocation; DE AltName: Full=Paracaspase; GN Name=MALT1; Synonyms=MLT; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION. RX PubMed=10339464; RA Dierlamm J., Baens M., Wlodarska I., Stefanova-Ouzounova M., RA Hernandez J.M., Hossfeld D.K., De Wolf-Peeters C., Hagemeijer A., RA Van den Berghe H., Marynen P.; RT "The apoptosis inhibitor gene API2 and a novel 18q gene, MLT, are RT recurrently rearranged in the t(11;18)(q21;q21) associated with RT mucosa-associated lymphoid tissue lymphomas."; RL Blood 93:3601-3609(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND CHROMOSOMAL TRANSLOCATION. RX PubMed=10523859; DOI=10.1038/sj.onc.1203018; RA Akagi T., Motegi M., Tamura A., Suzuki R., Hosokawa Y., Suzuki H., RA Ota H., Nakamura S., Morishima Y., Taniwaki M., Seto M.; RT "A novel gene, MALT1 at 18q21, is involved in t(11;18)(q21;q21) found RT in low-grade B-cell lymphoma of mucosa-associated lymphoid tissue."; RL Oncogene 18:5785-5794(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION. RC TISSUE=Kidney; RX PubMed=11090634; DOI=10.1016/S1097-2765(05)00086-9; RA Uren A.G., O'Rourke K., Aravind L., Pisabarro M.T., Seshagiri S., RA Koonin E.V., Dixit V.M.; RT "Identification of paracaspases and metacaspases. Two ancient families RT of caspase-like proteins, one of which plays a key role in MALT RT lymphoma."; RL Mol. Cell 6:961-967(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=B-cell; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 598-824. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP ALTERNATIVE SPLICING. RX PubMed=10610122; RA Suzuki H., Motegi M., Akagi T., Hosokawa Y., Seto M.; RT "API1-MALT1-MLT is involved in mucosa-associated lymphoid tissue RT lymphoma with t(11;18).(q21;q21)."; RL Blood 94:3270-3271(1999). RN [7] RP CHROMOSOMAL TRANSLOCATION. RX PubMed=10702396; DOI=10.1016/S0002-9440(10)64948-6; RA Motegi M., Yonezumi M., Suzuki H., Suzuki R., Hosokawa Y., Hosaka S., RA Kodera Y., Morishima Y., Nakamura S., Seto M.; RT "API2-MALT1 chimeric transcripts involved in mucosa-associated RT lymphoid tissue type lymphoma predict heterogeneous products."; RL Am. J. Pathol. 156:807-812(2000). RN [8] RP FUNCTION, AND MUTAGENESIS OF CYS-464. RX PubMed=11262391; DOI=10.1074/jbc.M009984200; RA Lucas P.C., Yonezumi M., Inohara N., McAllister-Lucas L.M., RA Abazeed M.E., Chen F.F., Yamaoka S., Seto M., Nunez G.; RT "Bcl10 and MALT1, independent targets of chromosomal translocation in RT MALT lymphoma, cooperate in a novel NF-kappa B signaling pathway."; RL J. Biol. Chem. 276:19012-19019(2001). RN [9] RP OLIGOMERIZATION, INTERACTION WITH TRAF6, AND MUTAGENESIS OF GLU-653 RP AND GLU-806. RX PubMed=15125833; DOI=10.1016/S1097-2765(04)00236-9; RA Sun L., Deng L., Ea C.-K., Xia Z.-P., Chen Z.J.; RT "The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by RT BCL10 and MALT1 in T lymphocytes."; RL Mol. Cell 14:289-301(2004). RN [10] RP FUNCTION AS A UBIQUITIN LIGASE. RX PubMed=14695475; DOI=10.1038/nature02273; RA Zhou H., Wertz I., O'Rourke K., Ultsch M., Seshagiri S., Eby M., RA Xiao W., Dixit V.M.; RT "Bcl10 activates the NF-kappaB pathway through ubiquitination of RT NEMO."; RL Nature 427:167-171(2004). RN [11] RP SUBCELLULAR LOCATION, AND NUCLEAR EXPORT SIGNAL. RX PubMed=16123224; DOI=10.1182/blood-2004-12-4785; RA Nakagawa M., Hosokawa Y., Yonezumi M., Izumiyama K., Suzuki R., RA Tsuzuki S., Asaka M., Seto M.; RT "MALT1 contains nuclear export signals and regulates cytoplasmic RT localization of BCL10."; RL Blood 106:4210-4216(2005). RN [12] RP FUNCTION. RX PubMed=18264101; DOI=10.1038/ni1568; RA Rebeaud F., Hailfinger S., Posevitz-Fejfar A., Tapernoux M., Moser R., RA Rueda D., Gaide O., Guzzardi M., Iancu E.M., Rufer N., Fasel N., RA Thome M.; RT "The proteolytic activity of the paracaspase MALT1 is key in T cell RT activation."; RL Nat. Immunol. 9:272-281(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [16] RP VARIANT IMD12 ILE-89. RX PubMed=23727036; DOI=10.1016/j.jaci.2013.04.047; RA Jabara H.H., Ohsumi T., Chou J., Massaad M.J., Benson H., RA Megarbane A., Chouery E., Mikhael R., Gorka O., Gewies A., RA Portales P., Nakayama T., Hosokawa H., Revy P., Herrod H., RA Le Deist F., Lefranc G., Ruland J., Geha R.S.; RT "A homozygous mucosa-associated lymphoid tissue 1 (MALT1) mutation in RT a family with combined immunodeficiency."; RL J. Allergy Clin. Immunol. 132:151-158(2013). CC -!- FUNCTION: Enhances BCL10-induced activation of NF-kappa-B. CC Involved in nuclear export of BCL10. Binds to TRAF6, inducing CC TRAF6 oligomerization and activation of its ligase activity. Has CC ubiquitin ligase activity. MALT1-dependent BCL10 cleavage plays an CC important role in T-cell antigen receptor-induced integrin CC adhesion. {ECO:0000269|PubMed:11262391, CC ECO:0000269|PubMed:14695475, ECO:0000269|PubMed:18264101}. CC -!- SUBUNIT: Binds through its Ig-like domains to BCL10. Forms CC oligomers which bind to TRAF6. CC -!- INTERACTION: CC O95999:BCL10; NbExp=15; IntAct=EBI-1047372, EBI-958922; CC Q9BXL7:CARD11; NbExp=2; IntAct=EBI-1047372, EBI-7006141; CC Q14790:CASP8; NbExp=10; IntAct=EBI-1047372, EBI-78060; CC Q9Y6K9:IKBKG; NbExp=4; IntAct=EBI-1047372, EBI-81279; CC Q9H0F6:SHARPIN; NbExp=2; IntAct=EBI-1047372, EBI-3942966; CC Q13501:SQSTM1; NbExp=2; IntAct=EBI-1047372, EBI-307104; CC Q9Y4K3:TRAF6; NbExp=5; IntAct=EBI-1047372, EBI-359276; CC P0CG48:UBC; NbExp=4; IntAct=EBI-1047372, EBI-3390054; CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:16123224}. Nucleus CC {ECO:0000269|PubMed:16123224}. Note=Shuttles between the nucleus CC and cytoplasm. Found in perinuclear structures together with CC BCL10. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UDY8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UDY8-2; Sequence=VSP_000844; CC -!- TISSUE SPECIFICITY: Highly expressed in peripheral blood CC mononuclear cells. Detected at lower levels in bone marrow, thymus CC and lymph node, and at very low levels in colon and lung. CC -!- DISEASE: Immunodeficiency 12 (IMD12) [MIM:615468]: A primary CC immunodeficiency characterized by onset in infancy of recurrent CC bacterial and candidal infections resulting in bronchiectasis and CC growth delay. Manifestations include mastoiditis, aphthous ulcers, CC cheilitis, gingivitis, esophagitis, gastritis, duodenitis, and CC meningitis. Levels of absolute lymphocytes and serum CC immunoglobulins are normal, but specific antibody titers are low CC despite immunization, and T-cells show impaired proliferative CC responses to mitogens. {ECO:0000269|PubMed:23727036}. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- DISEASE: Note=A chromosomal aberration involving MALT1 is CC recurrent in low-grade mucosa-associated lymphoid tissue (MALT CC lymphoma). Translocation t(11;18)(q21;q21) with BIRC2. This CC translocation is found in approximately 50% of cytogenetically CC abnormal low-grade MALT lymphoma. {ECO:0000269|PubMed:10339464, CC ECO:0000269|PubMed:10523859, ECO:0000269|PubMed:10702396, CC ECO:0000269|PubMed:11090634}. CC -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/MALT1ID240.html"; 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; AF130356; AAD38507.2; -; mRNA. DR EMBL; AB026118; BAA83099.1; -; mRNA. DR EMBL; AF316597; AAG38589.1; -; mRNA. DR EMBL; BC030143; AAH30143.1; -; mRNA. DR EMBL; AL137399; CAB70725.1; -; mRNA. DR CCDS; CCDS11967.1; -. [Q9UDY8-1] DR CCDS; CCDS11968.1; -. [Q9UDY8-2] DR PIR; T46456; T46456. DR RefSeq; NP_006776.1; NM_006785.3. [Q9UDY8-1] DR RefSeq; NP_776216.1; NM_173844.2. [Q9UDY8-2] DR UniGene; Hs.601217; -. DR PDB; 2G7R; X-ray; 2.70 A; A/B=29-126. DR PDB; 3BFO; X-ray; 1.15 A; A/B/C/D=226-325. DR PDB; 3K0W; X-ray; 2.80 A; A=128-337. DR PDB; 3UO8; X-ray; 1.90 A; B/C=339-719. DR PDB; 3UOA; X-ray; 1.75 A; B/C=339-719. DR PDB; 3V4O; X-ray; 2.10 A; A=329-569. DR PDB; 3V55; X-ray; 1.81 A; A=334-719. DR PDB; 4I1P; X-ray; 2.40 A; A/C=339-719. DR PDB; 4I1R; X-ray; 2.70 A; A=339-719. DR PDBsum; 2G7R; -. DR PDBsum; 3BFO; -. DR PDBsum; 3K0W; -. DR PDBsum; 3UO8; -. DR PDBsum; 3UOA; -. DR PDBsum; 3V4O; -. DR PDBsum; 3V55; -. DR PDBsum; 4I1P; -. DR PDBsum; 4I1R; -. DR ProteinModelPortal; Q9UDY8; -. DR SMR; Q9UDY8; -. DR BioGrid; 116098; 34. DR DIP; DIP-42833N; -. DR IntAct; Q9UDY8; 25. DR MINT; MINT-2844237; -. DR STRING; 9606.ENSP00000319279; -. DR ChEMBL; CHEMBL3632452; -. DR MEROPS; C14.026; -. DR iPTMnet; Q9UDY8; -. DR PhosphoSitePlus; Q9UDY8; -. DR BioMuta; MALT1; -. DR DMDM; 20455075; -. DR EPD; Q9UDY8; -. DR PaxDb; Q9UDY8; -. DR PeptideAtlas; Q9UDY8; -. DR PRIDE; Q9UDY8; -. DR DNASU; 10892; -. DR Ensembl; ENST00000345724; ENSP00000304161; ENSG00000172175. [Q9UDY8-2] DR Ensembl; ENST00000348428; ENSP00000319279; ENSG00000172175. [Q9UDY8-1] DR GeneID; 10892; -. DR KEGG; hsa:10892; -. DR UCSC; uc002lhm.3; human. [Q9UDY8-1] DR CTD; 10892; -. DR DisGeNET; 10892; -. DR GeneCards; MALT1; -. DR HGNC; HGNC:6819; MALT1. DR HPA; CAB004494; -. DR HPA; HPA048432; -. DR MalaCards; MALT1; -. DR MIM; 604860; gene. DR MIM; 615468; phenotype. DR neXtProt; NX_Q9UDY8; -. DR OpenTargets; ENSG00000172175; -. DR Orphanet; 397964; Combined immunodeficiency due to MALT1 deficiency. DR Orphanet; 52417; MALT lymphoma. DR PharmGKB; PA30568; -. DR eggNOG; ENOG410IG3U; Eukaryota. DR eggNOG; COG4249; LUCA. DR GeneTree; ENSGT00390000018044; -. DR HOGENOM; HOG000113471; -. DR HOVERGEN; HBG052402; -. DR InParanoid; Q9UDY8; -. DR KO; K07369; -. DR OMA; HPDNKEQ; -. DR OrthoDB; EOG091G01PI; -. DR PhylomeDB; Q9UDY8; -. DR TreeFam; TF319744; -. DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation. DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling. DR Reactome; R-HSA-5660668; CLEC7A/inflammasome pathway. DR SignaLink; Q9UDY8; -. DR SIGNOR; Q9UDY8; -. DR ChiTaRS; MALT1; human. DR EvolutionaryTrace; Q9UDY8; -. DR GeneWiki; MALT1; -. DR GenomeRNAi; 10892; -. DR PRO; PR:Q9UDY8; -. DR Proteomes; UP000005640; Chromosome 18. DR Bgee; ENSG00000172175; -. DR CleanEx; HS_MALT1; -. DR ExpressionAtlas; Q9UDY8; baseline and differential. DR Genevisible; Q9UDY8; HS. DR GO; GO:0032449; C:CBM complex; NAS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0043234; C:protein complex; IDA:UniProtKB. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; NAS:UniProtKB. DR GO; GO:0008233; F:peptidase activity; IDA:BHF-UCL. DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB. DR GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IMP:UniProtKB. DR GO; GO:0001923; P:B-1 B cell differentiation; IEA:Ensembl. DR GO; GO:0006952; P:defense response; NAS:UniProtKB. DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome. DR GO; GO:0045087; P:innate immune response; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; NAS:UniProtKB. DR GO; GO:0051168; P:nuclear export; IDA:UniProtKB. DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB. DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:UniProtKB. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL. DR GO; GO:0031398; P:positive regulation of protein ubiquitination; NAS:BHF-UCL. DR GO; GO:0050870; P:positive regulation of T cell activation; IC:UniProtKB. DR GO; GO:0002726; P:positive regulation of T cell cytokine production; IMP:UniProtKB. DR GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB. DR GO; GO:0006508; P:proteolysis; IDA:BHF-UCL. DR GO; GO:0042981; P:regulation of apoptotic process; IDA:MGI. DR GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IEA:Ensembl. DR GO; GO:0009620; P:response to fungus; IEA:Ensembl. DR GO; GO:0002237; P:response to molecule of bacterial origin; IEA:Ensembl. DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome. DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl. DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB. DR Gene3D; 1.10.533.10; -; 1. DR Gene3D; 2.60.40.10; -; 2. DR Gene3D; 3.40.50.1460; -; 1. DR InterPro; IPR029030; Caspase-like_dom. DR InterPro; IPR011029; DEATH-like_dom. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR033540; MALT1. DR InterPro; IPR001309; Pept_C14_p20. DR PANTHER; PTHR22576:SF33; PTHR22576:SF33; 1. DR Pfam; PF13895; Ig_2; 1. DR SMART; SM00409; IG; 2. DR SMART; SM00408; IGc2; 2. DR SUPFAM; SSF47986; SSF47986; 1. DR SUPFAM; SSF48726; SSF48726; 2. DR SUPFAM; SSF52129; SSF52129; 1. DR PROSITE; PS50208; CASPASE_P20; 1. DR PROSITE; PS50835; IG_LIKE; 2. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; KW Chromosomal rearrangement; Complete proteome; Cytoplasm; KW Disease mutation; Disulfide bond; Hydrolase; Immunoglobulin domain; KW Nucleus; Phosphoprotein; Polymorphism; Protease; Reference proteome; KW Repeat; Ubl conjugation pathway. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}. FT CHAIN 2 824 Mucosa-associated lymphoid tissue FT lymphoma translocation protein 1. FT /FTId=PRO_0000072821. FT DOMAIN 39 126 Death. FT DOMAIN 125 201 Ig-like C2-type 1. FT DOMAIN 212 305 Ig-like C2-type 2. FT REGION 348 562 Caspase-like. FT MOTIF 369 376 Nuclear export signal. FT ACT_SITE 415 415 {ECO:0000250}. FT ACT_SITE 464 464 {ECO:0000250}. FT SITE 126 127 Breakpoint for translocation to form FT BIRC2-MALT1. FT SITE 216 217 Breakpoint for translocation to form FT BIRC2-MALT1. FT SITE 320 321 Breakpoint for translocation to form FT BIRC2-MALT1. FT SITE 323 324 Breakpoint for translocation to form FT BIRC2-MALT1. FT SITE 329 330 Breakpoint for translocation to form FT BIRC2-MALT1. FT MOD_RES 2 2 N-acetylserine. FT {ECO:0000244|PubMed:22814378}. FT MOD_RES 135 135 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT DISULFID 147 190 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 248 290 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VAR_SEQ 309 319 Missing (in isoform 2). FT {ECO:0000303|PubMed:10523859, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_000844. FT VARIANT 89 89 S -> I (in IMD12; dbSNP:rs398123058). FT {ECO:0000269|PubMed:23727036}. FT /FTId=VAR_070857. FT VARIANT 641 641 I -> V (in dbSNP:rs35533328). FT /FTId=VAR_048620. FT MUTAGEN 464 464 C->A: Slight decrease in NF-kappa-B FT activation. FT {ECO:0000269|PubMed:11262391}. FT MUTAGEN 653 653 E->A: Abolishes binding to TRAF6. FT {ECO:0000269|PubMed:15125833}. FT MUTAGEN 806 806 E->A: Abolishes binding to TRAF6. FT {ECO:0000269|PubMed:15125833}. FT HELIX 30 32 {ECO:0000244|PDB:2G7R}. FT HELIX 35 45 {ECO:0000244|PDB:2G7R}. FT HELIX 54 60 {ECO:0000244|PDB:2G7R}. FT HELIX 71 78 {ECO:0000244|PDB:2G7R}. FT HELIX 79 82 {ECO:0000244|PDB:2G7R}. FT HELIX 88 98 {ECO:0000244|PDB:2G7R}. FT HELIX 103 121 {ECO:0000244|PDB:2G7R}. FT STRAND 129 131 {ECO:0000244|PDB:3K0W}. FT STRAND 136 139 {ECO:0000244|PDB:3K0W}. FT STRAND 142 147 {ECO:0000244|PDB:3K0W}. FT TURN 151 154 {ECO:0000244|PDB:3K0W}. FT STRAND 155 162 {ECO:0000244|PDB:3K0W}. FT STRAND 172 177 {ECO:0000244|PDB:3K0W}. FT HELIX 182 184 {ECO:0000244|PDB:3K0W}. FT STRAND 186 193 {ECO:0000244|PDB:3K0W}. FT STRAND 204 209 {ECO:0000244|PDB:3K0W}. FT HELIX 213 215 {ECO:0000244|PDB:3K0W}. FT STRAND 228 231 {ECO:0000244|PDB:3BFO}. FT STRAND 236 238 {ECO:0000244|PDB:3BFO}. FT STRAND 244 247 {ECO:0000244|PDB:3BFO}. FT STRAND 249 251 {ECO:0000244|PDB:3BFO}. FT STRAND 257 262 {ECO:0000244|PDB:3BFO}. FT STRAND 272 279 {ECO:0000244|PDB:3BFO}. FT HELIX 282 284 {ECO:0000244|PDB:3BFO}. FT STRAND 286 293 {ECO:0000244|PDB:3BFO}. FT STRAND 298 300 {ECO:0000244|PDB:3BFO}. FT STRAND 304 308 {ECO:0000244|PDB:3BFO}. FT STRAND 343 349 {ECO:0000244|PDB:3UOA}. FT STRAND 354 356 {ECO:0000244|PDB:3UOA}. FT HELIX 362 375 {ECO:0000244|PDB:3UOA}. FT STRAND 379 385 {ECO:0000244|PDB:3UOA}. FT HELIX 388 400 {ECO:0000244|PDB:3UOA}. FT STRAND 407 414 {ECO:0000244|PDB:3UOA}. FT STRAND 416 419 {ECO:0000244|PDB:3UOA}. FT STRAND 422 425 {ECO:0000244|PDB:3UOA}. FT HELIX 436 438 {ECO:0000244|PDB:3UOA}. FT STRAND 439 441 {ECO:0000244|PDB:3UOA}. FT HELIX 442 451 {ECO:0000244|PDB:3UOA}. FT STRAND 455 463 {ECO:0000244|PDB:3UOA}. FT STRAND 486 492 {ECO:0000244|PDB:3UOA}. FT STRAND 499 501 {ECO:0000244|PDB:3V55}. FT STRAND 507 509 {ECO:0000244|PDB:3V55}. FT HELIX 510 515 {ECO:0000244|PDB:3UOA}. FT TURN 516 520 {ECO:0000244|PDB:3UOA}. FT STRAND 521 523 {ECO:0000244|PDB:3V55}. FT HELIX 525 536 {ECO:0000244|PDB:3UOA}. FT TURN 540 545 {ECO:0000244|PDB:3UOA}. FT STRAND 549 552 {ECO:0000244|PDB:3UOA}. FT TURN 571 573 {ECO:0000244|PDB:3V55}. FT HELIX 574 582 {ECO:0000244|PDB:3V55}. FT STRAND 590 593 {ECO:0000244|PDB:3UOA}. FT STRAND 599 608 {ECO:0000244|PDB:3UOA}. FT STRAND 611 620 {ECO:0000244|PDB:3UOA}. FT STRAND 625 633 {ECO:0000244|PDB:3UOA}. FT HELIX 637 639 {ECO:0000244|PDB:3UOA}. FT HELIX 643 645 {ECO:0000244|PDB:3UOA}. FT STRAND 646 650 {ECO:0000244|PDB:3UOA}. FT HELIX 651 654 {ECO:0000244|PDB:3UOA}. FT HELIX 660 662 {ECO:0000244|PDB:3UOA}. FT STRAND 668 672 {ECO:0000244|PDB:3UOA}. FT HELIX 675 677 {ECO:0000244|PDB:3UOA}. FT STRAND 683 692 {ECO:0000244|PDB:3UOA}. FT STRAND 695 697 {ECO:0000244|PDB:4I1R}. FT STRAND 699 706 {ECO:0000244|PDB:3UOA}. FT HELIX 711 714 {ECO:0000244|PDB:3UOA}. SQ SEQUENCE 824 AA; 92272 MW; 28AFB80DA025F8AB CRC64; MSLLGDPLQA LPPSAAPTGP LLAPPAGATL NRLREPLLRR LSELLDQAPE GRGWRRLAEL AGSRGRLRLS CLDLEQCSLK VLEPEGSPSL CLLKLMGEKG CTVTELSDFL QAMEHTEVLQ LLSPPGIKIT VNPESKAVLA GQFVKLCCRA TGHPFVQYQW FKMNKEIPNG NTSELIFNAV HVKDAGFYVC RVNNNFTFEF SQWSQLDVCD IPESFQRSVD GVSESKLQIC VEPTSQKLMP GSTLVLQCVA VGSPIPHYQW FKNELPLTHE TKKLYMVPYV DLEHQGTYWC HVYNDRDSQD SKKVEIIIGR TDEAVECTED ELNNLGHPDN KEQTTDQPLA KDKVALLIGN MNYREHPKLK APLVDVYELT NLLRQLDFKV VSLLDLTEYE MRNAVDEFLL LLDKGVYGLL YYAGHGYENF GNSFMVPVDA PNPYRSENCL CVQNILKLMQ EKETGLNVFL LDMCRKRNDY DDTIPILDAL KVTANIVFGY ATCQGAEAFE IQHSGLANGI FMKFLKDRLL EDKKITVLLD EVAEDMGKCH LTKGKQALEI RSSLSEKRAL TDPIQGTEYS AESLVRNLQW AKAHELPESM CLKFDCGVQI QLGFAAEFSN VMIIYTSIVY KPPEIIMCDA YVTDFPLDLD IDPKDANKGT PEETGSYLVS KDLPKHCLYT RLSSLQKLKE HLVFTVCLSY QYSGLEDTVE DKQEVNVGKP LIAKLDMHRG LGRKTCFQTC LMSNGPYQSS AATSGGAGHY HSLQDPFHGV YHSHPGNPSN VTPADSCHCS RTPDAFISSF AHHASCHFSR SNVPVETTDE IPFSFSDRLR ISEK //