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Q9Z0H7

- BCL10_MOUSE

UniProt

Q9Z0H7 - BCL10_MOUSE

Protein

B-cell lymphoma/leukemia 10

Gene

Bcl10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Promotes apoptosis, pro-caspase-9 maturation and activation of NF-kappa-B via NIK and IKK. May be an adapter protein between upstream TNFR1-TRADD-RIP complex and the downstream NIK-IKK-IKAP complex By similarity. Is a substrate for MALT1 By similarity.By similarity

    GO - Molecular functioni

    1. cysteine-type endopeptidase activator activity involved in apoptotic process Source: MGI
    2. kinase activator activity Source: Ensembl
    3. kinase binding Source: UniProtKB
    4. NF-kappaB binding Source: UniProtKB
    5. protein binding Source: MGI
    6. protein C-terminus binding Source: UniProtKB
    7. protein heterodimerization activity Source: MGI
    8. protein homodimerization activity Source: MGI
    9. protein kinase B binding Source: UniProtKB
    10. protein kinase binding Source: UniProtKB
    11. protein self-association Source: UniProtKB
    12. transcription coactivator activity Source: UniProtKB
    13. transcription factor binding Source: UniProtKB
    14. ubiquitin binding Source: UniProtKB
    15. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    2. B cell apoptotic process Source: MGI
    3. cell death Source: UniProtKB
    4. cellular defense response Source: MGI
    5. cellular response to mechanical stimulus Source: Ensembl
    6. I-kappaB kinase/NF-kappaB signaling Source: MGI
    7. immunoglobulin mediated immune response Source: MGI
    8. innate immune response Source: UniProtKB
    9. mast cell activation Source: UniProtKB
    10. negative regulation of mature B cell apoptotic process Source: UniProtKB
    11. neural tube closure Source: UniProtKB
    12. positive regulation of apoptotic process Source: MGI
    13. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    14. positive regulation of execution phase of apoptosis Source: MGI
    15. positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
    16. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    17. positive regulation of interleukin-8 biosynthetic process Source: UniProtKB
    18. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    19. positive regulation of phosphorylation Source: UniProtKB
    20. positive regulation of protein ubiquitination Source: UniProtKB
    21. positive regulation of T cell activation Source: MGI
    22. positive regulation of transcription, DNA-templated Source: UniProtKB
    23. protein homooligomerization Source: UniProtKB
    24. protein oligomerization Source: UniProtKB
    25. regulation of T cell receptor signaling pathway Source: MGI
    26. response to food Source: UniProtKB
    27. response to fungus Source: MGI
    28. response to molecule of bacterial origin Source: UniProtKB
    29. T cell apoptotic process Source: MGI
    30. T cell receptor signaling pathway Source: UniProtKB

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    ReactomeiREACT_199121. Activation of NF-kappaB in B cells.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_225145. Downstream TCR signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    B-cell lymphoma/leukemia 10
    Alternative name(s):
    B-cell CLL/lymphoma 10
    Short name:
    Bcl-10
    CARD-containing molecule enhancing NF-kappa-B
    CARD-like apoptotic protein
    Short name:
    mCLAP
    CED-3/ICH-1 prodomain homologous E10-like regulator
    Short name:
    mCIPER
    Cellular homolog of vCARMEN
    Short name:
    cCARMEN
    Cellular-E10
    Short name:
    c-E10
    Mammalian CARD-containing adapter molecule E10
    Short name:
    mE10
    Gene namesi
    Name:Bcl10
    Synonyms:Ciper, Clap
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1337994. Bcl10.

    Subcellular locationi

    Cytoplasm By similarity. Membrane raft By similarity
    Note: Colocalized with DPP4 in membrane rafts.By similarity

    GO - Cellular componenti

    1. CBM complex Source: RefGenome
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic microtubule Source: UniProtKB
    4. cytosol Source: UniProtKB
    5. immunological synapse Source: MGI
    6. lipopolysaccharide receptor complex Source: Ensembl
    7. lysosome Source: UniProtKB
    8. membrane raft Source: MGI
    9. nucleus Source: UniProtKB
    10. perinuclear region of cytoplasm Source: UniProtKB
    11. protein complex Source: UniProtKB
    12. T cell receptor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 233233B-cell lymphoma/leukemia 10PRO_0000144075Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei138 – 1381PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by IKBKB/IKKB.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ9Z0H7.
    PRIDEiQ9Z0H7.

    PTM databases

    PhosphoSiteiQ9Z0H7.

    Expressioni

    Tissue specificityi

    Highly expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. Detected in developing brain, olfactory epithelium, tongue, whisker follicles, salivary gland, heart, lung, liver and intestinal epithelia of stage 15 embryos.

    Gene expression databases

    ArrayExpressiQ9Z0H7.
    BgeeiQ9Z0H7.
    CleanExiMM_BCL10.
    GenevestigatoriQ9Z0H7.

    Interactioni

    Subunit structurei

    Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB. Self-associates by CARD-CARD interaction and interacts with other CARD-proteins such as CARD9, CARD10, CARD11 and CARD14. Binds caspase-9 with its C-terminal domain. Interacts with TRAF2 and BIRC2/c-IAP2 By similarity. Interacts with PELI2 and SOCS3; these interactions may be mutually exclusive.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi198317. 12 interactions.
    DIPiDIP-60309N.
    IntActiQ9Z0H7. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z0H7.
    SMRiQ9Z0H7. Positions 10-115.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 10189CARDPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CARD domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG44778.
    GeneTreeiENSGT00490000043442.
    HOGENOMiHOG000008671.
    HOVERGENiHBG050680.
    InParanoidiQ9Z0H7.
    KOiK07368.
    OMAiGGTCGNS.
    OrthoDBiEOG79W97M.
    PhylomeDBiQ9Z0H7.
    TreeFamiTF328636.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    InterProiIPR001315. CARD.
    IPR011029. DEATH-like_dom.
    [Graphical view]
    PfamiPF00619. CARD. 1 hit.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 1 hit.
    PROSITEiPS50209. CARD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Z0H7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEAPAPSLTE EDLTEVKKDA LENLRVYLCE KIIAERHFDH LRAKKILSRE    50
    DTEEISCRTS SRKRAGKLLD YLQENPRGLD TLVESIRREK TQSFLIQKIT 100
    DEVLKLRNIK LEHLKGLKCS SCEPFAAGAT NNLSRCNSDE SNLSEKQRAS 150
    TVMYHPEGES STAPFFSMAS SLNLPVLEVG RTENSSFSSA TLPRPGDPGA 200
    PPLPPDLRLE EGGSCGNSSE MFLPLRSRAL SRQ 233
    Length:233
    Mass (Da):25,948
    Last modified:May 1, 1999 - v1
    Checksum:iC0539BC97102DBB8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006289 mRNA. Translation: CAA06956.1.
    AF057701 mRNA. Translation: AAD15801.1.
    AF100339 mRNA. Translation: AAD16429.1.
    AF127387 mRNA. Translation: AAD32598.1.
    AF134396 mRNA. Translation: AAD39148.1.
    AK076082 mRNA. Translation: BAC36168.1.
    AK140179 mRNA. Translation: BAE24267.1.
    AK150883 mRNA. Translation: BAE29930.1.
    AK152563 mRNA. Translation: BAE31316.1.
    AK152847 mRNA. Translation: BAE31540.1.
    AK156890 mRNA. Translation: BAE33885.1.
    AK169126 mRNA. Translation: BAE40905.1.
    AK172158 mRNA. Translation: BAE42852.1.
    BC024379 mRNA. Translation: AAH24379.1.
    CCDSiCCDS17897.1.
    RefSeqiNP_033870.1. NM_009740.2.
    UniGeneiMm.239141.

    Genome annotation databases

    EnsembliENSMUST00000029842; ENSMUSP00000029842; ENSMUSG00000028191.
    GeneIDi12042.
    KEGGimmu:12042.
    UCSCiuc008rqs.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006289 mRNA. Translation: CAA06956.1 .
    AF057701 mRNA. Translation: AAD15801.1 .
    AF100339 mRNA. Translation: AAD16429.1 .
    AF127387 mRNA. Translation: AAD32598.1 .
    AF134396 mRNA. Translation: AAD39148.1 .
    AK076082 mRNA. Translation: BAC36168.1 .
    AK140179 mRNA. Translation: BAE24267.1 .
    AK150883 mRNA. Translation: BAE29930.1 .
    AK152563 mRNA. Translation: BAE31316.1 .
    AK152847 mRNA. Translation: BAE31540.1 .
    AK156890 mRNA. Translation: BAE33885.1 .
    AK169126 mRNA. Translation: BAE40905.1 .
    AK172158 mRNA. Translation: BAE42852.1 .
    BC024379 mRNA. Translation: AAH24379.1 .
    CCDSi CCDS17897.1.
    RefSeqi NP_033870.1. NM_009740.2.
    UniGenei Mm.239141.

    3D structure databases

    ProteinModelPortali Q9Z0H7.
    SMRi Q9Z0H7. Positions 10-115.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198317. 12 interactions.
    DIPi DIP-60309N.
    IntActi Q9Z0H7. 1 interaction.

    PTM databases

    PhosphoSitei Q9Z0H7.

    Proteomic databases

    PaxDbi Q9Z0H7.
    PRIDEi Q9Z0H7.

    Protocols and materials databases

    DNASUi 12042.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029842 ; ENSMUSP00000029842 ; ENSMUSG00000028191 .
    GeneIDi 12042.
    KEGGi mmu:12042.
    UCSCi uc008rqs.1. mouse.

    Organism-specific databases

    CTDi 8915.
    MGIi MGI:1337994. Bcl10.

    Phylogenomic databases

    eggNOGi NOG44778.
    GeneTreei ENSGT00490000043442.
    HOGENOMi HOG000008671.
    HOVERGENi HBG050680.
    InParanoidi Q9Z0H7.
    KOi K07368.
    OMAi GGTCGNS.
    OrthoDBi EOG79W97M.
    PhylomeDBi Q9Z0H7.
    TreeFami TF328636.

    Enzyme and pathway databases

    Reactomei REACT_199121. Activation of NF-kappaB in B cells.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_225145. Downstream TCR signaling.

    Miscellaneous databases

    NextBioi 280309.
    PROi Q9Z0H7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z0H7.
    Bgeei Q9Z0H7.
    CleanExi MM_BCL10.
    Genevestigatori Q9Z0H7.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    InterProi IPR001315. CARD.
    IPR011029. DEATH-like_dom.
    [Graphical view ]
    Pfami PF00619. CARD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    PROSITEi PS50209. CARD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Bcl10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and mutated in multiple tumor types."
      Willis T.G., Jadayel D.M., Du M.-Q., Peng H., Perry A.R., Abdul-Rauf M., Price H., Karran L., Majekodunmi O., Wlodarska I., Pan L., Crook T., Hamoudi R., Isaacson P., Dyer M.J.S.
      Cell 96:35-45(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "CIPER, a novel NF kappaB-activating protein containing a caspase recruitment domain with homology to Herpesvirus-2 protein E10."
      Koseki T., Inohara N., Chen S., Carrio R., Merino J., Hottiger M.O., Nabel G.J., Nunez G.
      J. Biol. Chem. 274:9955-9961(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Equine herpesvirus-2 E10 gene product, but not its cellular homologue, activates NF-kappaB transcription factor and c-Jun N-terminal kinase."
      Thome M., Martinon F., Hofmann K., Rubio V., Steiner V., Schneider P., Mattmann C., Tschopp J.
      J. Biol. Chem. 274:9962-9968(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "mE10, a novel caspase recruitment domain-containing proapoptotic molecule."
      Yan M., Lee J., Schilbach S., Goddard A., Dixit V.M.
      J. Biol. Chem. 274:10287-10292(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Embryo.
    5. "CLAP, a novel caspase recruitment domain-containing protein in the tumor necrosis factor receptor pathway, regulates NF-kappaB activation and apoptosis."
      Srinivasula S.M., Ahmad M., Lin J.-H., Poyet J.-L., Fernandes-Alnemri T., Tsichlis P.N., Alnemri E.S.
      J. Biol. Chem. 274:17946-17954(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Bone marrow, Corpora quadrigemina, Liver and Spleen.
    7. "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].
    8. "BCL10 mediates lipopolysaccharide/toll-like receptor-4 signaling through interaction with Pellino2."
      Liu Y., Dong W., Chen L., Xiang R., Xiao H., De G., Wang Z., Qi Y.
      J. Biol. Chem. 279:37436-37444(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PELI2 AND SOCS3.

    Entry informationi

    Entry nameiBCL10_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z0H7
    Secondary accession number(s): Q3UBN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3