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O95999

- BCL10_HUMAN

UniProt

O95999 - BCL10_HUMAN

Protein

B-cell lymphoma/leukemia 10

Gene

BCL10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (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. Is a substrate for MALT1.1 Publication

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. kinase binding Source: UniProtKB
    3. NF-kappaB binding Source: UniProtKB
    4. protease binding Source: BHF-UCL
    5. protein binding Source: UniProtKB
    6. protein C-terminus binding Source: UniProtKB
    7. protein kinase B binding Source: UniProtKB
    8. protein kinase binding Source: UniProtKB
    9. protein self-association Source: UniProtKB
    10. transcription coactivator activity Source: UniProtKB
    11. transcription factor binding Source: UniProtKB
    12. ubiquitin binding Source: UniProtKB
    13. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. adaptive immune response Source: UniProtKB
    2. B cell apoptotic process Source: Ensembl
    3. cell death Source: UniProtKB
    4. cellular defense response Source: Ensembl
    5. cellular response to mechanical stimulus Source: UniProtKB
    6. Fc-epsilon receptor signaling pathway Source: Reactome
    7. immunoglobulin mediated immune response Source: Ensembl
    8. innate immune response Source: UniProtKB
    9. interleukin-6 biosynthetic process Source: UniProtKB
    10. lymphotoxin A biosynthetic process Source: UniProtKB
    11. negative regulation of mature B cell apoptotic process Source: UniProtKB
    12. neural tube closure Source: UniProtKB
    13. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    14. positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
    15. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    16. positive regulation of interleukin-8 biosynthetic process Source: UniProtKB
    17. positive regulation of mast cell cytokine production 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: Ensembl
    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: Ensembl
    26. response to food Source: UniProtKB
    27. response to fungus Source: Ensembl
    28. response to molecule of bacterial origin Source: UniProtKB
    29. T cell apoptotic process Source: Ensembl
    30. T cell receptor signaling pathway Source: UniProtKB
    31. toll-like receptor signaling pathway Source: UniProtKB

    Keywords - Biological processi

    Apoptosis

    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.
    SignaLinkiO95999.

    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:
    hCLAP
    CED-3/ICH-1 prodomain homologous E10-like regulator
    Short name:
    CIPER
    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:989. BCL10.

    Subcellular locationi

    Cytoplasmperinuclear region 1 Publication. Membrane raft 1 Publication
    Note: Appears to have a perinuclear, compact and filamentous pattern of expression. Also found in the nucleus of several types of tumor cells. Colocalized with DPP4 in membrane rafts.

    GO - Cellular componenti

    1. CBM complex Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic microtubule Source: UniProtKB
    4. cytosol Source: UniProtKB
    5. immunological synapse Source: Ensembl
    6. lysosome Source: UniProtKB
    7. membrane raft Source: UniProtKB-SubCell
    8. nucleus Source: UniProtKB
    9. perinuclear region of cytoplasm Source: UniProtKB
    10. plasma membrane Source: Reactome
    11. protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving BCL10 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(1;14)(p22;q32). Although the BCL10/IgH translocation leaves the coding region of BCL10 intact, frequent BCL10 mutations could be attributed to the Ig somatic hypermutation mechanism resulting in nucleotide transitions.
    Defects in BCL10 are involved in various types of cancer.
    Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive neoplasm of the serosal lining of the chest. It appears as broad sheets of cells, with some regions containing spindle-shaped, sarcoma-like cells and other regions showing adenomatous patterns. Pleural mesotheliomas have been linked to exposure to asbestos.
    Note: The gene represented in this entry may be involved in disease pathogenesis.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi28 – 281L → A: Abolishes cell death-inducing capability. 2 Publications
    Mutagenesisi41 – 411L → A: Abolishes cell death-inducing capability. 3 Publications
    Mutagenesisi41 – 411L → Q: Abolishes NF-kappa-B activation and homo/hetero-dimerization. 3 Publications
    Mutagenesisi46 – 461I → A: Abolishes cell death-inducing capability. 2 Publications
    Mutagenesisi47 – 471L → A: Abolishes cell death-inducing capability. 2 Publications
    Mutagenesisi53 – 531E → A: Abolishes cell death-inducing capability. 2 Publications
    Mutagenesisi55 – 551I → A: Abolishes cell death-inducing capability. 2 Publications
    Mutagenesisi78 – 781G → R: Abolishes NF-kappa-B activation. 2 Publications
    Mutagenesisi81 – 855TLVES → ALVEA: Complete loss of IKBKB/IKKB-mediated phosphorylation. 1 Publication
    Mutagenesisi228 – 2281R → G: Abolishes MALT1-mediated cleavage. 2 Publications
    Mutagenesisi231 – 2311S → A: Promotes NF-kappa-B activation. 1 Publication

    Keywords - Diseasei

    Disease mutation, Tumor suppressor

    Organism-specific databases

    MIMi156240. phenotype.
    PharmGKBiPA25299.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 233233B-cell lymphoma/leukemia 10PRO_0000144074Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei138 – 1381Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated. Phosphorylation results in dissociation from TRAF2 and binding to BIRC2/c-IAP2. Phosphorylated by IKBKB/IKKB.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95999.
    PaxDbiO95999.
    PRIDEiO95999.

    PTM databases

    PhosphoSiteiO95999.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    BgeeiO95999.
    CleanExiHS_BCL10.
    GenevestigatoriO95999.

    Organism-specific databases

    HPAiCAB001944.
    HPA017925.

    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 forms a tight complex with MALT1. 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. Interacts with PELI2 and SOCS3; these interactions may be mutually exclusive By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AKT1P317494EBI-958922,EBI-296087
    BCL3P207493EBI-958922,EBI-958997
    CARD11Q9BXL74EBI-958922,EBI-7006141
    MALT1Q9UDY812EBI-958922,EBI-1047372

    Protein-protein interaction databases

    BioGridi114429. 51 interactions.
    DIPiDIP-29740N.
    IntActiO95999. 17 interactions.
    MINTiMINT-89139.
    STRINGi9606.ENSP00000271015.

    Structurei

    Secondary structure

    1
    233
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 144
    Helixi17 – 2812
    Turni29 – 313
    Beta strandi32 – 387
    Helixi39 – 424
    Helixi49 – 535
    Turni54 – 574
    Helixi61 – 7212
    Turni76 – 794
    Helixi80 – 867
    Beta strandi89 – 924
    Helixi94 – 10512
    Helixi107 – 1137

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2MB9NMR-A1-115[»]
    ProteinModelPortaliO95999.
    SMRiO95999. 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.
    HOGENOMiHOG000008671.
    HOVERGENiHBG050680.
    InParanoidiO95999.
    KOiK07368.
    OMAiGGTCGNS.
    OrthoDBiEOG79W97M.
    PhylomeDBiO95999.
    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.

    O95999-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEPTAPSLTE EDLTEVKKDA LENLRVYLCE KIIAERHFDH LRAKKILSRE    50
    DTEEISCRTS SRKRAGKLLD YLQENPKGLD TLVESIRREK TQNFLIQKIT 100
    DEVLKLRNIK LEHLKGLKCS SCEPFPDGAT NNLSRSNSDE SNFSEKLRAS 150
    TVMYHPEGES STTPFFSTNS SLNLPVLEVG RTENTIFSST TLPRPGDPGA 200
    PPLPPDLQLE EEGTCANSSE MFLPLRSRTV SRQ 233
    Length:233
    Mass (Da):26,252
    Last modified:May 1, 1999 - v1
    Checksum:iF87C97F2B784BA4B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51A → S in MALT lymphoma and mesothelioma. 2 Publications
    Corresponds to variant rs12037217 [ dbSNP | Ensembl ].
    VAR_013208
    Natural varianti16 – 161V → E in MALT lymphoma. 1 Publication
    VAR_013209
    Natural varianti31 – 311K → E in MALT lymphoma. 1 Publication
    VAR_013210
    Natural varianti45 – 451K → Q in mesothelioma. 1 Publication
    VAR_013211
    Natural varianti52 – 521T → I in mesothelioma. 1 Publication
    VAR_013212
    Natural varianti57 – 571C → R in MALT lymphoma. 1 Publication
    VAR_013213
    Natural varianti58 – 581R → G in germ cell tumor. 1 Publication
    VAR_013214
    Natural varianti58 – 581R → Q in mesothelioma. 1 Publication
    VAR_013215
    Natural varianti64 – 641R → K in MALT lymphoma. 1 Publication
    VAR_013216
    Natural varianti93 – 931N → S in mesothelioma. 1 Publication
    VAR_013217
    Natural varianti101 – 1011D → E in MALT lymphoma. 1 Publication
    VAR_013218
    Natural varianti134 – 1341S → P in MALT lymphoma. 1 Publication
    VAR_013219
    Natural varianti153 – 1531M → V in mesothelioma. 1 Publication
    VAR_013220
    Natural varianti168 – 1681T → A in MALT lymphoma. 1 Publication
    VAR_013221
    Natural varianti174 – 1741L → S in MALT lymphoma. 1 Publication
    VAR_013222
    Natural varianti210 – 2101Missing in follicular lymphoma. 1 Publication
    VAR_013223
    Natural varianti213 – 2131G → E in MALT lymphoma and mesothelioma. 2 Publications
    Corresponds to variant rs3768235 [ dbSNP | Ensembl ].
    VAR_013224
    Natural varianti218 – 2181S → F in germ cell tumor, mesothelioma and other cancer cell lines. 2 Publications
    VAR_013225
    Natural varianti230 – 2301V → I in MALT lymphoma. 1 Publication
    VAR_013226

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006288 mRNA. Translation: CAA06955.1.
    AF057700 mRNA. Translation: AAD15800.1.
    AF100338 mRNA. Translation: AAD16428.1.
    AF127386 mRNA. Translation: AAD32597.1.
    AF134395 mRNA. Translation: AAD39147.1.
    AF105066 mRNA. Translation: AAF06894.1.
    AF082283 mRNA. Translation: AAC99767.1.
    AF097732 Genomic DNA. Translation: AAD24918.1.
    AK291346 mRNA. Translation: BAF84035.1.
    AL590113 Genomic DNA. Translation: CAH71557.1.
    CH471097 Genomic DNA. Translation: EAW73208.1.
    BC053617 mRNA. Translation: AAH53617.1.
    CCDSiCCDS704.1.
    RefSeqiNP_003912.1. NM_003921.4.
    UniGeneiHs.193516.

    Genome annotation databases

    EnsembliENST00000370580; ENSP00000359612; ENSG00000142867.
    GeneIDi8915.
    KEGGihsa:8915.
    UCSCiuc021opd.1. human.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006288 mRNA. Translation: CAA06955.1 .
    AF057700 mRNA. Translation: AAD15800.1 .
    AF100338 mRNA. Translation: AAD16428.1 .
    AF127386 mRNA. Translation: AAD32597.1 .
    AF134395 mRNA. Translation: AAD39147.1 .
    AF105066 mRNA. Translation: AAF06894.1 .
    AF082283 mRNA. Translation: AAC99767.1 .
    AF097732 Genomic DNA. Translation: AAD24918.1 .
    AK291346 mRNA. Translation: BAF84035.1 .
    AL590113 Genomic DNA. Translation: CAH71557.1 .
    CH471097 Genomic DNA. Translation: EAW73208.1 .
    BC053617 mRNA. Translation: AAH53617.1 .
    CCDSi CCDS704.1.
    RefSeqi NP_003912.1. NM_003921.4.
    UniGenei Hs.193516.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2MB9 NMR - A 1-115 [» ]
    ProteinModelPortali O95999.
    SMRi O95999. Positions 10-115.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114429. 51 interactions.
    DIPi DIP-29740N.
    IntActi O95999. 17 interactions.
    MINTi MINT-89139.
    STRINGi 9606.ENSP00000271015.

    PTM databases

    PhosphoSitei O95999.

    Proteomic databases

    MaxQBi O95999.
    PaxDbi O95999.
    PRIDEi O95999.

    Protocols and materials databases

    DNASUi 8915.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370580 ; ENSP00000359612 ; ENSG00000142867 .
    GeneIDi 8915.
    KEGGi hsa:8915.
    UCSCi uc021opd.1. human.

    Organism-specific databases

    CTDi 8915.
    GeneCardsi GC01M085731.
    HGNCi HGNC:989. BCL10.
    HPAi CAB001944.
    HPA017925.
    MIMi 156240. phenotype.
    603517. gene.
    neXtProti NX_O95999.
    PharmGKBi PA25299.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44778.
    HOGENOMi HOG000008671.
    HOVERGENi HBG050680.
    InParanoidi O95999.
    KOi K07368.
    OMAi GGTCGNS.
    OrthoDBi EOG79W97M.
    PhylomeDBi O95999.
    TreeFami TF328636.

    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 O95999.

    Miscellaneous databases

    ChiTaRSi BCL10. human.
    GeneWikii BCL10.
    GenomeRNAii 8915.
    NextBioi 33536.
    PROi O95999.
    SOURCEi Search...

    Gene expression databases

    Bgeei O95999.
    CleanExi HS_BCL10.
    Genevestigatori O95999.

    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], VARIANT FOLLICULAR LYMPHOMA GLU-210 DEL, VARIANT MESOTHELIOMA ILE-52, VARIANTS GERM CELL TUMOR GLY-58 AND PHE-218.
      Tissue: Lymphoma.
    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], MUTAGENESIS OF LEU-41 AND GLY-78.
    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], MUTAGENESIS OF LEU-28; LEU-41; ILE-46; LEU-47; GLU-53 AND ILE-55.
    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. "c-E10 is a caspase-recruiting domain-containing protein that interacts with components of death receptors signaling pathway and activates nuclear factor-kappaB."
      Costanzo A., Guiet C., Vito P.
      J. Biol. Chem. 274:20127-20132(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Spleen.
    7. "Inactivating mutations and overexpression of BCL10, a caspase recruitment domain-containing gene, in MALT lymphoma with t(1;14)(p22;q32)."
      Zhang Q., Siebert R., Yan M., Hinzmann B., Cui X., Xue L., Rakestraw K.M., Naeve C.W., Beckmann G., Weisenburger D.D., Sanger W.G., Nowotny H., Vesely M., Callet-Bauchu E., Salles G., Dixit V.M., Rosenthal A., Schlegelberger B., Morris S.W.
      Nat. Genet. 22:63-68(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS MALT LYMPHOMA SER-5; GLU-16; GLU-31; ARG-57; LYS-64; GLU-101; PRO-134; ALA-168; SER-174; GLU-213 AND ILE-230.
    8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Tongue.
    9. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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].
      Tissue: Eye.
    12. "Interchangeable binding of Bcl10 to TRAF2 and cIAPs regulates apoptosis signaling."
      Yui D., Yoneda T., Oono K., Katayama T., Imaizumi K., Tohyama M.
      Oncogene 20:4317-4323(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    13. Cited for: IDENTIFICATION IN A MEMBRANE RAFT COMPLEX, SUBCELLULAR LOCATION.
    14. "Negative feedback loop in T cell activation through IkappaB kinase-induced phosphorylation and degradation of Bcl10."
      Lobry C., Lopez T., Israel A., Weil R.
      Proc. Natl. Acad. Sci. U.S.A. 104:908-913(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY IKBKB/IKKB, MUTAGENESIS OF 81-THR--SER-85.
    15. Cited for: FUNCTION, MUTAGENESIS OF ARG-228.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Absence of BCL10 mutations in human malignant mesothelioma."
      Apostolou S., de Rienzo A., Murthy S.S., Jhanwar S.C., Testa J.R.
      Cell 97:684-686(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MESOTHELIOMA SER-5; GLN-45; GLN-58; SER-93; VAL-153; GLU-213 AND PHE-218.

    Entry informationi

    Entry nameiBCL10_HUMAN
    AccessioniPrimary (citable) accession number: O95999
    Secondary accession number(s): Q5VUF1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 129 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 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3