MALT1_HUMAN
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 03-AUG-2022, entry version 214.
DE RecName: Full=Mucosa-associated lymphoid tissue lymphoma translocation protein 1 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000269|PubMed:31133753};
DE AltName: Full=MALT lymphoma-associated translocation {ECO:0000303|PubMed:10339464};
DE AltName: Full=Paracaspase {ECO:0000303|PubMed:11090634};
GN Name=MALT1 {ECO:0000303|PubMed:10523859, ECO:0000312|HGNC:HGNC:6819};
GN Synonyms=MLT {ECO:0000303|PubMed:10339464};
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 [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 mucosa-
RT 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., Ota H.,
RA Nakamura S., Morishima Y., Taniwaki M., Seto M.;
RT "A novel gene, MALT1 at 18q21, is involved in t(11;18)(q21;q21) found in
RT 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(00)00094-0;
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 of
RT caspase-like proteins, one of which plays a key role in MALT 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 project:
RT 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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 lymphoma
RT 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 lymphoid
RT 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., Abazeed M.E.,
RA Chen F.F., Yamaoka S., Seto M., Nunez G.;
RT "Bcl10 and MALT1, independent targets of chromosomal translocation in MALT
RT 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 AND
RP 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 BCL10
RT 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., Xiao W.,
RA Dixit V.M.;
RT "Bcl10 activates the NF-kappaB pathway through ubiquitination of 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., Tsuzuki S.,
RA 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., 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 BY
RP 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., Buerckstuemmer T.,
RA 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 SPECTROMETRY
RP [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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP FUNCTION, AND IDENTIFICATION IN A CBM COMPLEX.
RX PubMed=24074955; DOI=10.1016/j.molcel.2013.08.032;
RA Qiao Q., Yang C., Zheng C., Fontan L., David L., Yu X., Bracken C.,
RA Rosen M., Melnick A., Egelman E.H., Wu H.;
RT "Structural architecture of the CARMA1/Bcl10/MALT1 signalosome: nucleation-
RT induced filamentous assembly.";
RL Mol. Cell 51:766-779(2013).
RN [17]
RP SUBUNIT.
RX PubMed=27113748; DOI=10.15252/embr.201642109;
RA Afonina I.S., Van Nuffel E., Baudelet G., Driege Y., Kreike M., Staal J.,
RA Beyaert R.;
RT "The paracaspase MALT1 mediates CARD14-induced signaling in
RT keratinocytes.";
RL EMBO Rep. 17:914-927(2016).
RN [18]
RP INTERACTION WITH BCL10.
RX PubMed=28628108; DOI=10.1038/ng.3898;
RA Ma C.A., Stinson J.R., Zhang Y., Abbott J.K., Weinreich M.A., Hauk P.J.,
RA Reynolds P.R., Lyons J.J., Nelson C.G., Ruffo E., Dorjbal B., Glauzy S.,
RA Yamakawa N., Arjunaraja S., Voss K., Stoddard J., Niemela J., Zhang Y.,
RA Rosenzweig S.D., McElwee J.J., DiMaggio T., Matthews H.F., Jones N.,
RA Stone K.D., Palma A., Oleastro M., Prieto E., Bernasconi A.R., Dubra G.,
RA Danielian S., Zaiat J., Marti M.A., Kim B., Cooper M.A., Romberg N.,
RA Meffre E., Gelfand E.W., Snow A.L., Milner J.D.;
RT "Germline hypomorphic CARD11 mutations in severe atopic disease.";
RL Nat. Genet. 49:1192-1201(2017).
RN [19]
RP FUNCTION.
RX PubMed=31133753; DOI=10.1038/s41564-019-0460-3;
RA Yamasoba D., Sato K., Ichinose T., Imamura T., Koepke L., Joas S.,
RA Reith E., Hotter D., Misawa N., Akaki K., Uehata T., Mino T., Miyamoto S.,
RA Noda T., Yamashita A., Standley D.M., Kirchhoff F., Sauter D., Koyanagi Y.,
RA Takeuchi O.;
RT "N4BP1 restricts HIV-1 and its inactivation by MALT1 promotes viral
RT reactivation.";
RL Nat. Microbiol. 4:1532-1544(2019).
RN [20]
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., Megarbane A.,
RA Chouery E., Mikhael R., Gorka O., Gewies A., Portales P., Nakayama T.,
RA Hosokawa H., Revy P., Herrod H., Le Deist F., Lefranc G., Ruland J.,
RA Geha R.S.;
RT "A homozygous mucosa-associated lymphoid tissue 1 (MALT1) mutation in a
RT family with combined immunodeficiency.";
RL J. Allergy Clin. Immunol. 132:151-158(2013).
CC -!- FUNCTION: Protease that enhances BCL10-induced activation: acts via
CC formation of CBM complexes that channel adaptive and innate immune
CC signaling downstream of CARD domain-containing proteins (CARD9, CARD11
CC and CARD14) to activate NF-kappa-B and MAP kinase p38 pathways which
CC stimulate expression of genes encoding pro-inflammatory cytokines and
CC chemokines (PubMed:11262391, PubMed:18264101, PubMed:24074955).
CC Mediates BCL10 cleavage: MALT1-dependent BCL10 cleavage plays an
CC important role in T-cell antigen receptor-induced integrin adhesion
CC (PubMed:11262391, PubMed:18264101). Involved in the induction of T
CC helper 17 cells (Th17) differentiation (PubMed:11262391,
CC PubMed:18264101). Cleaves RC3H1 and ZC3H12A in response to T-cell
CC receptor (TCR) stimulation which releases their cooperatively repressed
CC targets to promote Th17 cell differentiation (By similarity). Also
CC mediates cleavage of N4BP1 in T-cells following TCR-mediated
CC activation, leading to N4BP1 inactivation (PubMed:31133753). May also
CC have ubiquitin ligase activity: binds to TRAF6, inducing TRAF6
CC oligomerization and activation of its ligase activity
CC (PubMed:14695475). {ECO:0000250|UniProtKB:Q2TBA3,
CC ECO:0000269|PubMed:11262391, ECO:0000269|PubMed:14695475,
CC ECO:0000269|PubMed:18264101, ECO:0000269|PubMed:24074955,
CC ECO:0000269|PubMed:31133753}.
CC -!- SUBUNIT: Homooligomer; forms oligomers which bind to TRAF6
CC (PubMed:15125833). Forms a complex with CARD14 and MALT1; resulting in
CC the formation of a CBM (CARD14-BCL10-MALT1) complex (PubMed:27113748).
CC Forms a complex with CARD11 and MALT1; resulting in the formation of a
CC CBM (CARD11-BCL10-MALT1) complex (PubMed:28628108, PubMed:24074955).
CC Forms a complex with CARD9 and MALT1; resulting in the formation of a
CC CBM (CARD9-BCL10-MALT1) complex (By similarity).
CC {ECO:0000250|UniProtKB:Q2TBA3, ECO:0000269|PubMed:15125833,
CC ECO:0000269|PubMed:24074955, ECO:0000269|PubMed:27113748,
CC ECO:0000269|PubMed:28628108}.
CC -!- INTERACTION:
CC Q9UDY8; O95999: BCL10; NbExp=19; IntAct=EBI-1047372, EBI-958922;
CC Q9UDY8; Q9BXL7: CARD11; NbExp=2; IntAct=EBI-1047372, EBI-7006141;
CC Q9UDY8; Q14790: CASP8; NbExp=10; IntAct=EBI-1047372, EBI-78060;
CC Q9UDY8; P48729: CSNK1A1; NbExp=7; IntAct=EBI-1047372, EBI-1383726;
CC Q9UDY8; Q9Y6K9: IKBKG; NbExp=4; IntAct=EBI-1047372, EBI-81279;
CC Q9UDY8; Q9UDY8: MALT1; NbExp=2; IntAct=EBI-1047372, EBI-1047372;
CC Q9UDY8; Q96PU8: QKI; NbExp=2; IntAct=EBI-1047372, EBI-945792;
CC Q9UDY8; Q9H0F6: SHARPIN; NbExp=2; IntAct=EBI-1047372, EBI-3942966;
CC Q9UDY8; Q13501: SQSTM1; NbExp=2; IntAct=EBI-1047372, EBI-307104;
CC Q9UDY8; Q9Y4K3: TRAF6; NbExp=5; IntAct=EBI-1047372, EBI-359276;
CC Q9UDY8; P0CG48: UBC; NbExp=4; IntAct=EBI-1047372, EBI-3390054;
CC Q9UDY8-2; P54252: ATXN3; NbExp=3; IntAct=EBI-12056869, EBI-946046;
CC Q9UDY8-2; P46379-2: BAG6; NbExp=3; IntAct=EBI-12056869, EBI-10988864;
CC Q9UDY8-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-12056869, EBI-10976677;
CC Q9UDY8-2; P50570-2: DNM2; NbExp=3; IntAct=EBI-12056869, EBI-10968534;
CC Q9UDY8-2; Q9BSK4: FEM1A; NbExp=3; IntAct=EBI-12056869, EBI-2515349;
CC Q9UDY8-2; Q96JP0: FEM1C; NbExp=3; IntAct=EBI-12056869, EBI-2515330;
CC Q9UDY8-2; P28799: GRN; NbExp=3; IntAct=EBI-12056869, EBI-747754;
CC Q9UDY8-2; P04792: HSPB1; NbExp=3; IntAct=EBI-12056869, EBI-352682;
CC Q9UDY8-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-12056869, EBI-10975473;
CC Q9UDY8-2; O14901: KLF11; NbExp=3; IntAct=EBI-12056869, EBI-948266;
CC Q9UDY8-2; O14832: PHYH; NbExp=3; IntAct=EBI-12056869, EBI-721853;
CC Q9UDY8-2; P60891: PRPS1; NbExp=3; IntAct=EBI-12056869, EBI-749195;
CC Q9UDY8-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-12056869, EBI-5235340;
CC Q9UDY8-2; O76024: WFS1; NbExp=3; IntAct=EBI-12056869, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:16123224}. Nucleus {ECO:0000269|PubMed:16123224}.
CC Note=Shuttles between the nucleus and cytoplasm. Found in perinuclear
CC structures together with BCL10. {ECO:0000269|PubMed:16123224}.
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 mononuclear
CC cells. Detected at lower levels in bone marrow, thymus and lymph node,
CC 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 immunoglobulins
CC are normal, but specific antibody titers are low despite immunization,
CC and T-cells show impaired proliferative responses to mitogens.
CC {ECO:0000269|PubMed:23727036}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving MALT1 is recurrent in
CC low-grade mucosa-associated lymphoid tissue (MALT lymphoma).
CC Translocation t(11;18)(q21;q21) with BIRC2. This translocation is found
CC in approximately 50% of cytogenetically abnormal low-grade MALT
CC lymphoma. {ECO:0000269|PubMed:10339464, ECO:0000269|PubMed:10523859,
CC ECO:0000269|PubMed:10702396, 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 and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MALT1ID240.html";
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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 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 PDB; 6F7I; X-ray; 2.43 A; A/B=329-728.
DR PDB; 6GK2; EM; 4.90 A; F=30-121.
DR PDB; 6H4A; X-ray; 2.65 A; A=329-728.
DR PDB; 6YN8; X-ray; 3.05 A; A=334-719.
DR PDB; 6YN9; X-ray; 2.56 A; A=329-728.
DR PDB; 7A41; X-ray; 2.13 A; A/B=329-728.
DR PDB; 7AK0; X-ray; 2.32 A; A/B=329-728.
DR PDB; 7AK1; X-ray; 2.51 A; A=329-728.
DR PDB; 7PAV; X-ray; 2.20 A; A/B=339-719.
DR PDB; 7PAW; X-ray; 2.19 A; A/B=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 PDBsum; 6F7I; -.
DR PDBsum; 6GK2; -.
DR PDBsum; 6H4A; -.
DR PDBsum; 6YN8; -.
DR PDBsum; 6YN9; -.
DR PDBsum; 7A41; -.
DR PDBsum; 7AK0; -.
DR PDBsum; 7AK1; -.
DR PDBsum; 7PAV; -.
DR PDBsum; 7PAW; -.
DR AlphaFoldDB; Q9UDY8; -.
DR SMR; Q9UDY8; -.
DR BioGRID; 116098; 64.
DR CORUM; Q9UDY8; -.
DR DIP; DIP-42833N; -.
DR IntAct; Q9UDY8; 43.
DR MINT; Q9UDY8; -.
DR STRING; 9606.ENSP00000319279; -.
DR BindingDB; Q9UDY8; -.
DR ChEMBL; CHEMBL3632452; -.
DR GuidetoPHARMACOLOGY; 2983; -.
DR MEROPS; C14.026; -.
DR GlyGen; Q9UDY8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UDY8; -.
DR PhosphoSitePlus; Q9UDY8; -.
DR BioMuta; MALT1; -.
DR DMDM; 20455075; -.
DR EPD; Q9UDY8; -.
DR jPOST; Q9UDY8; -.
DR MassIVE; Q9UDY8; -.
DR MaxQB; Q9UDY8; -.
DR PaxDb; Q9UDY8; -.
DR PeptideAtlas; Q9UDY8; -.
DR PRIDE; Q9UDY8; -.
DR ProteomicsDB; 84136; -. [Q9UDY8-1]
DR ProteomicsDB; 84137; -. [Q9UDY8-2]
DR Antibodypedia; 1194; 772 antibodies from 45 providers.
DR DNASU; 10892; -.
DR Ensembl; ENST00000345724.7; ENSP00000304161.3; ENSG00000172175.15. [Q9UDY8-2]
DR Ensembl; ENST00000649217.2; ENSP00000497997.1; ENSG00000172175.15. [Q9UDY8-1]
DR GeneID; 10892; -.
DR KEGG; hsa:10892; -.
DR MANE-Select; ENST00000649217.2; ENSP00000497997.1; NM_006785.4; NP_006776.1.
DR UCSC; uc002lhm.3; human. [Q9UDY8-1]
DR CTD; 10892; -.
DR DisGeNET; 10892; -.
DR GeneCards; MALT1; -.
DR HGNC; HGNC:6819; MALT1.
DR HPA; ENSG00000172175; Low tissue specificity.
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 VEuPathDB; HostDB:ENSG00000172175; -.
DR eggNOG; ENOG502QUZM; Eukaryota.
DR GeneTree; ENSGT00390000018044; -.
DR HOGENOM; CLU_014796_0_0_1; -.
DR InParanoid; Q9UDY8; -.
DR OMA; PVPHYQW; -.
DR OrthoDB; 531253at2759; -.
DR PhylomeDB; Q9UDY8; -.
DR TreeFam; TF319744; -.
DR PathwayCommons; Q9UDY8; -.
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 BioGRID-ORCS; 10892; 11 hits in 1091 CRISPR screens.
DR ChiTaRS; MALT1; human.
DR EvolutionaryTrace; Q9UDY8; -.
DR GeneWiki; MALT1; -.
DR GenomeRNAi; 10892; -.
DR Pharos; Q9UDY8; Tchem.
DR PRO; PR:Q9UDY8; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9UDY8; protein.
DR Bgee; ENSG00000172175; Expressed in colonic epithelium and 187 other tissues.
DR ExpressionAtlas; Q9UDY8; baseline and differential.
DR Genevisible; Q9UDY8; HS.
DR GO; GO:0032449; C:CBM complex; IDA: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:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002096; C:polkadots; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; NAS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008233; F:peptidase activity; IDA:BHF-UCL.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0043621; F:protein self-association; IPI: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:0042113; P:B cell activation; IBA:GO_Central.
DR GO; GO:0001923; P:B-1 B cell differentiation; IEA:Ensembl.
DR GO; GO:0006952; P:defense response; NAS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; 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:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:ARUK-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:ARUK-UCL.
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:0002726; P:positive regulation of T cell cytokine production; IMP:UniProtKB.
DR GO; GO:2000321; P:positive regulation of T-helper 17 cell differentiation; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:BHF-UCL.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:UniProtKB.
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:0042098; P:T cell proliferation; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
DR CDD; cd08783; Death_MALT1; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR033540; MALT1.
DR InterPro; IPR037940; MALT1_Death.
DR InterPro; IPR041077; MALT1_Ig.
DR InterPro; IPR001309; Pept_C14_p20.
DR PANTHER; PTHR22576:SF40; PTHR22576:SF40; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF18703; MALT1_Ig; 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; Chromosomal rearrangement;
KW Cytoplasm; Disease variant; Disulfide bond; Hydrolase; Immunity;
KW Immunoglobulin domain; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..824
FT /note="Mucosa-associated lymphoid tissue lymphoma
FT translocation protein 1"
FT /id="PRO_0000072821"
FT DOMAIN 39..126
FT /note="Death"
FT DOMAIN 125..201
FT /note="Ig-like C2-type 1"
FT DOMAIN 212..305
FT /note="Ig-like C2-type 2"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..562
FT /note="Caspase-like"
FT MOTIF 369..376
FT /note="Nuclear export signal"
FT ACT_SITE 415
FT /evidence="ECO:0000250"
FT ACT_SITE 464
FT /evidence="ECO:0000250"
FT SITE 126..127
FT /note="Breakpoint for translocation to form BIRC2-MALT1"
FT SITE 216..217
FT /note="Breakpoint for translocation to form BIRC2-MALT1"
FT SITE 320..321
FT /note="Breakpoint for translocation to form BIRC2-MALT1"
FT SITE 323..324
FT /note="Breakpoint for translocation to form BIRC2-MALT1"
FT SITE 329..330
FT /note="Breakpoint for translocation to form BIRC2-MALT1"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT DISULFID 147..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 248..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 309..319
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10523859,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_000844"
FT VARIANT 89
FT /note="S -> I (in IMD12; dbSNP:rs398123058)"
FT /evidence="ECO:0000269|PubMed:23727036"
FT /id="VAR_070857"
FT VARIANT 641
FT /note="I -> V (in dbSNP:rs35533328)"
FT /id="VAR_048620"
FT MUTAGEN 464
FT /note="C->A: Slight decrease in NF-kappa-B activation."
FT /evidence="ECO:0000269|PubMed:11262391"
FT MUTAGEN 653
FT /note="E->A: Abolishes binding to TRAF6."
FT /evidence="ECO:0000269|PubMed:15125833"
FT MUTAGEN 806
FT /note="E->A: Abolishes binding to TRAF6."
FT /evidence="ECO:0000269|PubMed:15125833"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:2G7R"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:2G7R"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:2G7R"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:2G7R"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:2G7R"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:2G7R"
FT HELIX 103..121
FT /evidence="ECO:0007829|PDB:2G7R"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3K0W"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:3K0W"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3K0W"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:3K0W"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:3K0W"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:3K0W"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3K0W"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:3K0W"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:3K0W"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3K0W"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:3BFO"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:3BFO"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:3BFO"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:3BFO"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:3BFO"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:3BFO"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:3BFO"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:3BFO"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:3BFO"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:3BFO"
FT STRAND 343..349
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:3UOA"
FT HELIX 362..375
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:3UOA"
FT HELIX 388..400
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 407..414
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 416..419
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:3UOA"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:3UOA"
FT HELIX 442..451
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 455..463
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:3V55"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:3V55"
FT HELIX 510..515
FT /evidence="ECO:0007829|PDB:3UOA"
FT TURN 516..520
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:3V55"
FT HELIX 525..536
FT /evidence="ECO:0007829|PDB:3UOA"
FT TURN 540..545
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:3UOA"
FT TURN 567..569
FT /evidence="ECO:0007829|PDB:6YN9"
FT TURN 571..573
FT /evidence="ECO:0007829|PDB:3V55"
FT HELIX 574..582
FT /evidence="ECO:0007829|PDB:3V55"
FT STRAND 590..593
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 599..608
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 611..620
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 625..633
FT /evidence="ECO:0007829|PDB:3UOA"
FT HELIX 637..639
FT /evidence="ECO:0007829|PDB:3UOA"
FT HELIX 643..645
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 646..650
FT /evidence="ECO:0007829|PDB:3UOA"
FT HELIX 651..654
FT /evidence="ECO:0007829|PDB:3UOA"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 664..666
FT /evidence="ECO:0007829|PDB:7PAV"
FT STRAND 668..672
FT /evidence="ECO:0007829|PDB:3UOA"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 683..692
FT /evidence="ECO:0007829|PDB:3UOA"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:6H4A"
FT STRAND 699..706
FT /evidence="ECO:0007829|PDB:3UOA"
FT HELIX 711..714
FT /evidence="ECO:0007829|PDB:3UOA"
FT HELIX 717..719
FT /evidence="ECO:0007829|PDB:7PAW"
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
