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Q9UDY8

- MALT1_HUMAN

UniProt

Q9UDY8 - MALT1_HUMAN

Protein

Mucosa-associated lymphoid tissue lymphoma translocation protein 1

Gene

MALT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Enhances BCL10-induced activation of NF-kappa-B. Involved in nuclear export of BCL10. Binds to TRAF6, inducing TRAF6 oligomerization and activation of its ligase activity. Has ubiquitin ligase activity. MALT1-dependent BCL10 cleavage plays an important role in T-cell antigen receptor-induced integrin adhesion.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei126 – 1272Breakpoint for translocation to form BIRC2-MALT1
    Sitei216 – 2172Breakpoint for translocation to form BIRC2-MALT1
    Sitei320 – 3212Breakpoint for translocation to form BIRC2-MALT1
    Sitei323 – 3242Breakpoint for translocation to form BIRC2-MALT1
    Sitei329 – 3302Breakpoint for translocation to form BIRC2-MALT1
    Active sitei415 – 4151By similarity
    Active sitei464 – 4641By similarity

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: UniProtKB
    2. peptidase activity Source: BHF-UCL
    3. protein binding Source: UniProtKB
    4. protein self-association Source: UniProtKB
    5. signal transducer activity Source: UniProtKB
    6. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. activation of NF-kappaB-inducing kinase activity Source: UniProtKB
    2. B-1 B cell differentiation Source: Ensembl
    3. defense response Source: UniProtKB
    4. Fc-epsilon receptor signaling pathway Source: Reactome
    5. innate immune response Source: Reactome
    6. negative regulation of apoptotic process Source: UniProtKB
    7. nuclear export Source: UniProtKB
    8. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    9. positive regulation of interleukin-2 production Source: UniProtKB
    10. positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
    11. positive regulation of protein ubiquitination Source: BHF-UCL
    12. positive regulation of T cell activation Source: UniProtKB
    13. positive regulation of T cell cytokine production Source: UniProtKB
    14. protein oligomerization Source: UniProtKB
    15. protein ubiquitination Source: GOC
    16. proteolysis Source: BHF-UCL
    17. regulation of apoptotic process Source: MGI
    18. regulation of T cell receptor signaling pathway Source: Ensembl
    19. response to fungus Source: Ensembl
    20. response to molecule of bacterial origin Source: Ensembl
    21. T cell proliferation Source: Ensembl
    22. T cell receptor signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_118656. Activation of NF-kappaB in B cells.
    REACT_12555. Downstream TCR signaling.
    REACT_163994. FCERI mediated NF-kB activation.
    SignaLinkiQ9UDY8.

    Protein family/group databases

    MEROPSiC14.026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mucosa-associated lymphoid tissue lymphoma translocation protein 1 (EC:3.4.22.-)
    Alternative name(s):
    MALT lymphoma-associated translocation
    Paracaspase
    Gene namesi
    Name:MALT1
    Synonyms:MLT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:6819. MALT1.

    Subcellular locationi

    Cytoplasmperinuclear region 1 Publication. Nucleus 1 Publication
    Note: Shuttles between the nucleus and cytoplasm. Found in perinuclear structures together with BCL10.

    GO - Cellular componenti

    1. CBM complex Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: Reactome
    4. nucleolus Source: HPA
    5. nucleus Source: UniProtKB
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    7. plasma membrane Source: Reactome
    8. protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Immunodeficiency 12 (IMD12) [MIM:615468]: A primary immunodeficiency characterized by onset in infancy of recurrent bacterial and candidal infections resulting in bronchiectasis and growth delay. Manifestations include mastoiditis, aphthous ulcers, cheilitis, gingivitis, esophagitis, gastritis, duodenitis, and meningitis. Levels of absolute lymphocytes and serum immunoglobulins are normal, but specific antibody titers are low despite immunization, and T-cells show impaired proliferative responses to mitogens.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891S → I in IMD12. 1 Publication
    VAR_070857
    A chromosomal aberration involving MALT1 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(11;18)(q21;q21) with BIRC2. This translocation is found in approximately 50% of cytogenetically abnormal low-grade MALT lymphoma.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi464 – 4641C → A: Slight decrease in NF-kappa-B activation. 1 Publication
    Mutagenesisi653 – 6531E → A: Abolishes binding to TRAF6. 1 Publication
    Mutagenesisi806 – 8061E → A: Abolishes binding to TRAF6. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi615468. phenotype.
    Orphaneti52417. MALT lymphoma.
    PharmGKBiPA30568.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 824823Mucosa-associated lymphoid tissue lymphoma translocation protein 1PRO_0000072821Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei135 – 1351Phosphoserine1 Publication
    Disulfide bondi147 ↔ 190PROSITE-ProRule annotation
    Disulfide bondi248 ↔ 290PROSITE-ProRule annotation

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UDY8.
    PaxDbiQ9UDY8.
    PRIDEiQ9UDY8.

    PTM databases

    PhosphoSiteiQ9UDY8.

    Expressioni

    Tissue specificityi

    Highly expressed in peripheral blood mononuclear cells. Detected at lower levels in bone marrow, thymus and lymph node, and at very low levels in colon and lung.

    Gene expression databases

    ArrayExpressiQ9UDY8.
    BgeeiQ9UDY8.
    CleanExiHS_MALT1.
    GenevestigatoriQ9UDY8.

    Organism-specific databases

    HPAiCAB004494.
    HPA003865.
    HPA048432.

    Interactioni

    Subunit structurei

    Binds through its Ig-like domains to BCL10. Forms oligomers which bind to TRAF6.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCL10O9599912EBI-1047372,EBI-958922
    CASP8Q1479010EBI-1047372,EBI-78060
    IKBKGQ9Y6K92EBI-1047372,EBI-81279
    SQSTM1Q135012EBI-1047372,EBI-307104
    TRAF6Q9Y4K33EBI-1047372,EBI-359276
    UBCP0CG484EBI-1047372,EBI-3390054

    Protein-protein interaction databases

    BioGridi116098. 31 interactions.
    DIPiDIP-42833N.
    IntActiQ9UDY8. 19 interactions.
    MINTiMINT-2844237.
    STRINGi9606.ENSP00000319279.

    Structurei

    Secondary structure

    1
    824
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 323
    Helixi35 – 4511
    Helixi54 – 607
    Helixi71 – 788
    Helixi79 – 824
    Helixi88 – 9811
    Helixi103 – 12119
    Beta strandi129 – 1313
    Beta strandi136 – 1394
    Beta strandi142 – 1476
    Turni151 – 1544
    Beta strandi155 – 1628
    Beta strandi172 – 1776
    Helixi182 – 1843
    Beta strandi186 – 1938
    Beta strandi204 – 2096
    Helixi213 – 2153
    Beta strandi228 – 2314
    Beta strandi236 – 2383
    Beta strandi244 – 2474
    Beta strandi249 – 2513
    Beta strandi257 – 2626
    Beta strandi272 – 2798
    Helixi282 – 2843
    Beta strandi286 – 2938
    Beta strandi298 – 3003
    Beta strandi304 – 3085
    Beta strandi343 – 3497
    Beta strandi354 – 3563
    Helixi362 – 37514
    Beta strandi379 – 3857
    Helixi388 – 40013
    Beta strandi407 – 4148
    Beta strandi416 – 4194
    Beta strandi422 – 4254
    Helixi436 – 4383
    Beta strandi439 – 4413
    Helixi442 – 45110
    Beta strandi455 – 4639
    Beta strandi486 – 4927
    Beta strandi499 – 5013
    Beta strandi507 – 5093
    Helixi510 – 5156
    Turni516 – 5205
    Beta strandi521 – 5233
    Helixi525 – 53612
    Turni540 – 5456
    Beta strandi549 – 5524
    Turni571 – 5733
    Helixi574 – 5829
    Beta strandi590 – 5934
    Beta strandi599 – 60810
    Beta strandi611 – 62010
    Beta strandi625 – 6339
    Helixi637 – 6393
    Helixi643 – 6453
    Beta strandi646 – 6505
    Helixi651 – 6544
    Helixi660 – 6623
    Beta strandi668 – 6725
    Helixi675 – 6773
    Beta strandi683 – 69210
    Beta strandi695 – 6973
    Beta strandi699 – 7068
    Helixi711 – 7144

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2G7RX-ray2.70A/B29-126[»]
    3BFOX-ray1.15A/B/C/D226-325[»]
    3K0WX-ray2.80A128-337[»]
    3UO8X-ray1.90B/C339-719[»]
    3UOAX-ray1.75B/C339-719[»]
    3V4OX-ray2.10A329-569[»]
    3V55X-ray1.81A334-719[»]
    4I1RX-ray2.70A339-719[»]
    ProteinModelPortaliQ9UDY8.
    SMRiQ9UDY8. Positions 42-124, 128-308, 336-715.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UDY8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 12688DeathAdd
    BLAST
    Domaini125 – 20177Ig-like C2-type 1Add
    BLAST
    Domaini212 – 30594Ig-like C2-type 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni348 – 562215Caspase-likeAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi369 – 3768Nuclear export signal

    Sequence similaritiesi

    Belongs to the peptidase C14B family.Curated
    Contains 1 death domain.Curated

    Keywords - Domaini

    Immunoglobulin domain, Repeat

    Phylogenomic databases

    eggNOGiCOG4249.
    HOGENOMiHOG000113471.
    HOVERGENiHBG052402.
    InParanoidiQ9UDY8.
    KOiK07369.
    OMAiMNKEIPN.
    OrthoDBiEOG7673BH.
    PhylomeDBiQ9UDY8.
    TreeFamiTF319744.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    2.60.40.10. 2 hits.
    3.40.50.1460. 1 hit.
    InterProiIPR029030. Caspase-like_dom.
    IPR011029. DEATH-like_dom.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR011600. Pept_C14_caspase.
    IPR001309. Pept_C14_ICE_p20.
    [Graphical view]
    PfamiPF00656. Peptidase_C14. 1 hit.
    [Graphical view]
    SMARTiSM00409. IG. 1 hit.
    SM00408. IGc2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 1 hit.
    PROSITEiPS50208. CASPASE_P20. 1 hit.
    PS50835. IG_LIKE. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UDY8-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSLLGDPLQA LPPSAAPTGP LLAPPAGATL NRLREPLLRR LSELLDQAPE    50
    GRGWRRLAEL AGSRGRLRLS CLDLEQCSLK VLEPEGSPSL CLLKLMGEKG 100
    CTVTELSDFL QAMEHTEVLQ LLSPPGIKIT VNPESKAVLA GQFVKLCCRA 150
    TGHPFVQYQW FKMNKEIPNG NTSELIFNAV HVKDAGFYVC RVNNNFTFEF 200
    SQWSQLDVCD IPESFQRSVD GVSESKLQIC VEPTSQKLMP GSTLVLQCVA 250
    VGSPIPHYQW FKNELPLTHE TKKLYMVPYV DLEHQGTYWC HVYNDRDSQD 300
    SKKVEIIIGR TDEAVECTED ELNNLGHPDN KEQTTDQPLA KDKVALLIGN 350
    MNYREHPKLK APLVDVYELT NLLRQLDFKV VSLLDLTEYE MRNAVDEFLL 400
    LLDKGVYGLL YYAGHGYENF GNSFMVPVDA PNPYRSENCL CVQNILKLMQ 450
    EKETGLNVFL LDMCRKRNDY DDTIPILDAL KVTANIVFGY ATCQGAEAFE 500
    IQHSGLANGI FMKFLKDRLL EDKKITVLLD EVAEDMGKCH LTKGKQALEI 550
    RSSLSEKRAL TDPIQGTEYS AESLVRNLQW AKAHELPESM CLKFDCGVQI 600
    QLGFAAEFSN VMIIYTSIVY KPPEIIMCDA YVTDFPLDLD IDPKDANKGT 650
    PEETGSYLVS KDLPKHCLYT RLSSLQKLKE HLVFTVCLSY QYSGLEDTVE 700
    DKQEVNVGKP LIAKLDMHRG LGRKTCFQTC LMSNGPYQSS AATSGGAGHY 750
    HSLQDPFHGV YHSHPGNPSN VTPADSCHCS RTPDAFISSF AHHASCHFSR 800
    SNVPVETTDE IPFSFSDRLR ISEK 824
    Length:824
    Mass (Da):92,272
    Last modified:May 1, 2000 - v1
    Checksum:i28AFB80DA025F8AB
    GO
    Isoform 2 (identifier: Q9UDY8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         309-319: Missing.

    Show »
    Length:813
    Mass (Da):91,081
    Checksum:i45D05E0DBF81DF5B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891S → I in IMD12. 1 Publication
    VAR_070857
    Natural varianti641 – 6411I → V.
    Corresponds to variant rs35533328 [ dbSNP | Ensembl ].
    VAR_048620

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei309 – 31911Missing in isoform 2. 2 PublicationsVSP_000844Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF130356 mRNA. Translation: AAD38507.2.
    AB026118 mRNA. Translation: BAA83099.1.
    AF316597 mRNA. Translation: AAG38589.1.
    BC030143 mRNA. Translation: AAH30143.1.
    AL137399 mRNA. Translation: CAB70725.1.
    CCDSiCCDS11967.1. [Q9UDY8-1]
    CCDS11968.1. [Q9UDY8-2]
    PIRiT46456.
    RefSeqiNP_006776.1. NM_006785.3. [Q9UDY8-1]
    NP_776216.1. NM_173844.2. [Q9UDY8-2]
    UniGeneiHs.601217.

    Genome annotation databases

    EnsembliENST00000345724; ENSP00000304161; ENSG00000172175. [Q9UDY8-2]
    ENST00000348428; ENSP00000319279; ENSG00000172175. [Q9UDY8-1]
    GeneIDi10892.
    KEGGihsa:10892.
    UCSCiuc002lhm.1. human. [Q9UDY8-1]
    uc002lhn.1. human. [Q9UDY8-2]

    Polymorphism databases

    DMDMi20455075.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF130356 mRNA. Translation: AAD38507.2 .
    AB026118 mRNA. Translation: BAA83099.1 .
    AF316597 mRNA. Translation: AAG38589.1 .
    BC030143 mRNA. Translation: AAH30143.1 .
    AL137399 mRNA. Translation: CAB70725.1 .
    CCDSi CCDS11967.1. [Q9UDY8-1 ]
    CCDS11968.1. [Q9UDY8-2 ]
    PIRi T46456.
    RefSeqi NP_006776.1. NM_006785.3. [Q9UDY8-1 ]
    NP_776216.1. NM_173844.2. [Q9UDY8-2 ]
    UniGenei Hs.601217.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2G7R X-ray 2.70 A/B 29-126 [» ]
    3BFO X-ray 1.15 A/B/C/D 226-325 [» ]
    3K0W X-ray 2.80 A 128-337 [» ]
    3UO8 X-ray 1.90 B/C 339-719 [» ]
    3UOA X-ray 1.75 B/C 339-719 [» ]
    3V4O X-ray 2.10 A 329-569 [» ]
    3V55 X-ray 1.81 A 334-719 [» ]
    4I1R X-ray 2.70 A 339-719 [» ]
    ProteinModelPortali Q9UDY8.
    SMRi Q9UDY8. Positions 42-124, 128-308, 336-715.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116098. 31 interactions.
    DIPi DIP-42833N.
    IntActi Q9UDY8. 19 interactions.
    MINTi MINT-2844237.
    STRINGi 9606.ENSP00000319279.

    Protein family/group databases

    MEROPSi C14.026.

    PTM databases

    PhosphoSitei Q9UDY8.

    Polymorphism databases

    DMDMi 20455075.

    Proteomic databases

    MaxQBi Q9UDY8.
    PaxDbi Q9UDY8.
    PRIDEi Q9UDY8.

    Protocols and materials databases

    DNASUi 10892.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345724 ; ENSP00000304161 ; ENSG00000172175 . [Q9UDY8-2 ]
    ENST00000348428 ; ENSP00000319279 ; ENSG00000172175 . [Q9UDY8-1 ]
    GeneIDi 10892.
    KEGGi hsa:10892.
    UCSCi uc002lhm.1. human. [Q9UDY8-1 ]
    uc002lhn.1. human. [Q9UDY8-2 ]

    Organism-specific databases

    CTDi 10892.
    GeneCardsi GC18P056339.
    HGNCi HGNC:6819. MALT1.
    HPAi CAB004494.
    HPA003865.
    HPA048432.
    MIMi 604860. gene.
    615468. phenotype.
    neXtProti NX_Q9UDY8.
    Orphaneti 52417. MALT lymphoma.
    PharmGKBi PA30568.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4249.
    HOGENOMi HOG000113471.
    HOVERGENi HBG052402.
    InParanoidi Q9UDY8.
    KOi K07369.
    OMAi MNKEIPN.
    OrthoDBi EOG7673BH.
    PhylomeDBi Q9UDY8.
    TreeFami TF319744.

    Enzyme and pathway databases

    Reactomei REACT_118656. Activation of NF-kappaB in B cells.
    REACT_12555. Downstream TCR signaling.
    REACT_163994. FCERI mediated NF-kB activation.
    SignaLinki Q9UDY8.

    Miscellaneous databases

    ChiTaRSi MALT1. human.
    EvolutionaryTracei Q9UDY8.
    GeneWikii MALT1.
    GenomeRNAii 10892.
    NextBioi 41357.
    PROi Q9UDY8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UDY8.
    Bgeei Q9UDY8.
    CleanExi HS_MALT1.
    Genevestigatori Q9UDY8.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    2.60.40.10. 2 hits.
    3.40.50.1460. 1 hit.
    InterProi IPR029030. Caspase-like_dom.
    IPR011029. DEATH-like_dom.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR011600. Pept_C14_caspase.
    IPR001309. Pept_C14_ICE_p20.
    [Graphical view ]
    Pfami PF00656. Peptidase_C14. 1 hit.
    [Graphical view ]
    SMARTi SM00409. IG. 1 hit.
    SM00408. IGc2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    PROSITEi PS50208. CASPASE_P20. 1 hit.
    PS50835. IG_LIKE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The apoptosis inhibitor gene API2 and a novel 18q gene, MLT, are recurrently rearranged in the t(11;18)(q21;q21) associated with mucosa-associated lymphoid tissue lymphomas."
      Dierlamm J., Baens M., Wlodarska I., Stefanova-Ouzounova M., Hernandez J.M., Hossfeld D.K., De Wolf-Peeters C., Hagemeijer A., Van den Berghe H., Marynen P.
      Blood 93:3601-3609(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION.
    2. "A novel gene, MALT1 at 18q21, is involved in t(11;18)(q21;q21) found in low-grade B-cell lymphoma of mucosa-associated lymphoid tissue."
      Akagi T., Motegi M., Tamura A., Suzuki R., Hosokawa Y., Suzuki H., Ota H., Nakamura S., Morishima Y., Taniwaki M., Seto M.
      Oncogene 18:5785-5794(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHROMOSOMAL TRANSLOCATION.
    3. "Identification of paracaspases and metacaspases. Two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma."
      Uren A.G., O'Rourke K., Aravind L., Pisabarro M.T., Seshagiri S., Koonin E.V., Dixit V.M.
      Mol. Cell 6:961-967(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION.
      Tissue: Kidney.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: B-cell.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 598-824.
      Tissue: Testis.
    6. "API1-MALT1-MLT is involved in mucosa-associated lymphoid tissue lymphoma with t(11;18).(q21;q21)."
      Suzuki H., Motegi M., Akagi T., Hosokawa Y., Seto M.
      Blood 94:3270-3271(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING.
    7. "API2-MALT1 chimeric transcripts involved in mucosa-associated lymphoid tissue type lymphoma predict heterogeneous products."
      Motegi M., Yonezumi M., Suzuki H., Suzuki R., Hosokawa Y., Hosaka S., Kodera Y., Morishima Y., Nakamura S., Seto M.
      Am. J. Pathol. 156:807-812(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION.
    8. "Bcl10 and MALT1, independent targets of chromosomal translocation in MALT lymphoma, cooperate in a novel NF-kappa B signaling pathway."
      Lucas P.C., Yonezumi M., Inohara N., McAllister-Lucas L.M., Abazeed M.E., Chen F.F., Yamaoka S., Seto M., Nunez G.
      J. Biol. Chem. 276:19012-19019(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-464.
    9. "The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes."
      Sun L., Deng L., Ea C.-K., Xia Z.-P., Chen Z.J.
      Mol. Cell 14:289-301(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: OLIGOMERIZATION, INTERACTION WITH TRAF6, MUTAGENESIS OF GLU-653 AND GLU-806.
    10. "Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO."
      Zhou H., Wertz I., O'Rourke K., Ultsch M., Seshagiri S., Eby M., Xiao W., Dixit V.M.
      Nature 427:167-171(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A UBIQUITIN LIGASE.
    11. "MALT1 contains nuclear export signals and regulates cytoplasmic localization of BCL10."
      Nakagawa M., Hosokawa Y., Yonezumi M., Izumiyama K., Suzuki R., Tsuzuki S., Asaka M., Seto M.
      Blood 106:4210-4216(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL.
    12. Cited for: FUNCTION.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. Cited for: VARIANT IMD12 ILE-89.

    Entry informationi

    Entry nameiMALT1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UDY8
    Secondary accession number(s): Q9NTB7, Q9ULX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 150 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

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