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   27-MAR-2024, entry version 223.
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="https://atlasgeneticsoncology.org/gene/240/MALT1";
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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   PDB; 8CZO; EM; 4.30 A; a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v=29-122.
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   PDBsum; 8CZO; -.
DR   AlphaFoldDB; Q9UDY8; -.
DR   EMDB; EMD-0013; -.
DR   EMDB; EMD-27100; -.
DR   SMR; Q9UDY8; -.
DR   BioGRID; 116098; 68.
DR   CORUM; Q9UDY8; -.
DR   DIP; DIP-42833N; -.
DR   IntAct; Q9UDY8; 43.
DR   MINT; Q9UDY8; -.
DR   STRING; 9606.ENSP00000497997; -.
DR   BindingDB; Q9UDY8; -.
DR   ChEMBL; CHEMBL3632452; -.
DR   GuidetoPHARMACOLOGY; 2983; -.
DR   MEROPS; C14.026; -.
DR   GlyCosmos; Q9UDY8; 1 site, 1 glycan.
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; 9606-ENSP00000319279; -.
DR   PeptideAtlas; Q9UDY8; -.
DR   ProteomicsDB; 84136; -. [Q9UDY8-1]
DR   ProteomicsDB; 84137; -. [Q9UDY8-2]
DR   Pumba; Q9UDY8; -.
DR   Antibodypedia; 1194; 850 antibodies from 45 providers.
DR   DNASU; 10892; -.
DR   Ensembl; ENST00000345724.7; ENSP00000304161.3; ENSG00000172175.16. [Q9UDY8-2]
DR   Ensembl; ENST00000649217.2; ENSP00000497997.1; ENSG00000172175.16. [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   AGR; HGNC:6819; -.
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; CLMSDGP; -.
DR   OrthoDB; 3080800at2759; -.
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; 14 hits in 1170 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 cell types or tissues.
DR   ExpressionAtlas; Q9UDY8; baseline and differential.
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:0036094; F:small molecule binding; EXP:DisProt.
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:0043123; P:positive regulation of canonical NF-kappaB signal transduction; HMP:UniProtKB.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:ARUK-UCL.
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   CDD; cd00096; Ig; 1.
DR   Gene3D; 2.60.40.3360; -; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR037940; MALT1_Death.
DR   InterPro; IPR041077; MALT1_Ig.
DR   InterPro; IPR033540; MALT1_IG-like_dom_sf.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   InterPro; IPR001309; Pept_C14_p20.
DR   PANTHER; PTHR22576; MUCOSA ASSOCIATED LYMPHOID TISSUE LYMPHOMA TRANSLOCATION PROTEIN 1/PARACASPASE; 1.
DR   PANTHER; PTHR22576:SF40; MUCOSA-ASSOCIATED LYMPHOID TISSUE LYMPHOMA TRANSLOCATION PROTEIN 1; 1.
DR   Pfam; PF13895; Ig_2; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF18703; MALT1_Ig; 1.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SUPFAM; SSF52129; Caspase-like; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   PROSITE; PS50208; CASPASE_P20; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   Genevisible; Q9UDY8; HS.
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
//