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O95999 (BCL10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:BCL10
Synonyms:CIPER, CLAP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length233 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.15

Subunit structure

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. Ref.13

Subcellular location

Cytoplasmperinuclear region. Membrane raft. 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. Ref.13

Tissue specificity

Ubiquitous.

Post-translational modification

Phosphorylated. Phosphorylation results in dissociation from TRAF2 and binding to BIRC2/c-IAP2. Phosphorylated by IKBKB/IKKB. Ref.12 Ref.14

Involvement in disease

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.

Sequence similarities

Contains 1 CARD domain.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityChromosomal rearrangement
   DiseaseDisease mutation
Tumor suppressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

T cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

T cell receptor signaling pathway

Inferred from direct assay PubMed 15125833. Source: UniProtKB

adaptive immune response

Traceable author statement PubMed 16831874. Source: UniProtKB

cell death

Inferred from direct assay Ref.6. Source: UniProtKB

cellular defense response

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

immunoglobulin mediated immune response

Inferred from electronic annotation. Source: Ensembl

innate immune response

Inferred from expression pattern PubMed 16831874. Source: UniProtKB

interleukin-6 biosynthetic process

Non-traceable author statement PubMed 16647297. Source: UniProtKB

lymphotoxin A biosynthetic process

Non-traceable author statement PubMed 16647297. Source: UniProtKB

negative regulation of mature B cell apoptotic process

Inferred from direct assay PubMed 15878976. Source: UniProtKB

neural tube closure

Inferred from sequence or structural similarity PubMed 11163238. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from expression pattern PubMed 12761501. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay Ref.6PubMed 14695475. Source: UniProtKB

positive regulation of T cell activation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of extrinsic apoptotic signaling pathway

Inferred from direct assay Ref.12. Source: UniProtKB

positive regulation of interleukin-8 biosynthetic process

Inferred from mutant phenotype PubMed 17095757. Source: UniProtKB

positive regulation of mast cell cytokine production

Non-traceable author statement PubMed 16647297. Source: UniProtKB

positive regulation of phosphorylation

Inferred from direct assay PubMed 15125833. Source: UniProtKB

positive regulation of protein ubiquitination

Inferred from direct assay PubMed 14695475. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15207693. Source: UniProtKB

protein homooligomerization

Inferred from sequence or structural similarity PubMed 16831874. Source: UniProtKB

protein oligomerization

Inferred from physical interaction PubMed 14695475. Source: UniProtKB

regulation of T cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

response to food

Inferred from direct assay PubMed 17095757. Source: UniProtKB

response to fungus

Inferred from electronic annotation. Source: Ensembl

response to molecule of bacterial origin

Inferred from expression pattern PubMed 16831874. Source: UniProtKB

toll-like receptor signaling pathway

Inferred by curator PubMed 16831874. Source: UniProtKB

   Cellular_componentCBM complex

Non-traceable author statement PubMed 15125833. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 11021819PubMed 11053425PubMed 11278692PubMed 15082780. Source: UniProtKB

cytoplasmic microtubule

Inferred from direct assay PubMed 23264731. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 12154360. Source: UniProtKB

immunological synapse

Inferred from electronic annotation. Source: Ensembl

lysosome

Inferred from direct assay PubMed 15082780. Source: UniProtKB

membrane raft

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 16280327. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 16127295. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

protein complex

Inferred from direct assay PubMed 14695475PubMed 16280327. Source: UniProtKB

   Molecular_functionNF-kappaB binding

Inferred from direct assay PubMed 16280327. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 14695475. Source: UniProtKB

kinase binding

Inferred from physical interaction PubMed 16831874PubMed 17052756. Source: UniProtKB

protease binding

Inferred from physical interaction PubMed 18223652. Source: BHF-UCL

protein C-terminus binding

Inferred from physical interaction PubMed 11053425. Source: UniProtKB

protein kinase B binding

Inferred from physical interaction PubMed 16280327. Source: UniProtKB

protein kinase binding

Inferred from direct assay PubMed 17052756. Source: UniProtKB

protein self-association

Inferred from physical interaction PubMed 15125833. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay PubMed 15207693. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 15207693. Source: UniProtKB

ubiquitin binding

Inferred from direct assay PubMed 15082780. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 16395405. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 233233B-cell lymphoma/leukemia 10
PRO_0000144074

Regions

Domain13 – 10189CARD

Amino acid modifications

Modified residue11N-acetylmethionine Ref.16
Modified residue1381Phosphoserine Ref.18

Natural variations

Natural variant51A → S in MALT lymphoma and mesothelioma. Ref.7 Ref.19
Corresponds to variant rs12037217 [ dbSNP | Ensembl ].
VAR_013208
Natural variant161V → E in MALT lymphoma. Ref.7
VAR_013209
Natural variant311K → E in MALT lymphoma. Ref.7
VAR_013210
Natural variant451K → Q in mesothelioma. Ref.19
VAR_013211
Natural variant521T → I in mesothelioma. Ref.1
VAR_013212
Natural variant571C → R in MALT lymphoma. Ref.7
VAR_013213
Natural variant581R → G in germ cell tumor. Ref.1
VAR_013214
Natural variant581R → Q in mesothelioma. Ref.19
VAR_013215
Natural variant641R → K in MALT lymphoma. Ref.7
VAR_013216
Natural variant931N → S in mesothelioma. Ref.19
VAR_013217
Natural variant1011D → E in MALT lymphoma. Ref.7
VAR_013218
Natural variant1341S → P in MALT lymphoma. Ref.7
VAR_013219
Natural variant1531M → V in mesothelioma. Ref.19
VAR_013220
Natural variant1681T → A in MALT lymphoma. Ref.7
VAR_013221
Natural variant1741L → S in MALT lymphoma. Ref.7
VAR_013222
Natural variant2101Missing in follicular lymphoma. Ref.1
VAR_013223
Natural variant2131G → E in MALT lymphoma and mesothelioma. Ref.7 Ref.19
Corresponds to variant rs3768235 [ dbSNP | Ensembl ].
VAR_013224
Natural variant2181S → F in germ cell tumor, mesothelioma and other cancer cell lines. Ref.1 Ref.19
VAR_013225
Natural variant2301V → I in MALT lymphoma. Ref.7
VAR_013226

Experimental info

Mutagenesis281L → A: Abolishes cell death-inducing capability. Ref.4
Mutagenesis411L → A: Abolishes cell death-inducing capability. Ref.2 Ref.4
Mutagenesis411L → Q: Abolishes NF-kappa-B activation and homo/hetero-dimerization. Ref.2 Ref.4
Mutagenesis461I → A: Abolishes cell death-inducing capability. Ref.4
Mutagenesis471L → A: Abolishes cell death-inducing capability. Ref.4
Mutagenesis531E → A: Abolishes cell death-inducing capability. Ref.4
Mutagenesis551I → A: Abolishes cell death-inducing capability. Ref.4
Mutagenesis781G → R: Abolishes NF-kappa-B activation. Ref.2
Mutagenesis81 – 855TLVES → ALVEA: Complete loss of IKBKB/IKKB-mediated phosphorylation. Ref.14
Mutagenesis2281R → G: Abolishes MALT1-mediated cleavage. Ref.15
Mutagenesis2311S → A: Promotes NF-kappa-B activation.

Secondary structure

...................... 233
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O95999 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: F87C97F2B784BA4B

FASTA23326,252
        10         20         30         40         50         60 
MEPTAPSLTE EDLTEVKKDA LENLRVYLCE KIIAERHFDH LRAKKILSRE DTEEISCRTS 

        70         80         90        100        110        120 
SRKRAGKLLD YLQENPKGLD TLVESIRREK TQNFLIQKIT DEVLKLRNIK LEHLKGLKCS 

       130        140        150        160        170        180 
SCEPFPDGAT NNLSRSNSDE SNFSEKLRAS TVMYHPEGES STTPFFSTNS SLNLPVLEVG 

       190        200        210        220        230 
RTENTIFSST TLPRPGDPGA PPLPPDLQLE EEGTCANSSE MFLPLRSRTV SRQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Caveolin-1 triggers T-cell activation via CD26 in association with CARMA1."
Ohnuma K., Uchiyama M., Yamochi T., Nishibashi K., Hosono O., Takahashi N., Kina S., Tanaka H., Lin X., Dang N.H., Morimoto C.
J. Biol. Chem. 282:10117-10131(2007) [PubMed] [Europe PMC] [Abstract]
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]"The proteolytic activity of the paracaspase MALT1 is key in T cell activation."
Rebeaud F., Hailfinger S., Posevitz-Fejfar A., Tapernoux M., Moser R., Rueda D., Gaide O., Guzzardi M., Iancu E.M., Rufer N., Fasel N., Thome M.
Nat. Immunol. 9:272-281(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_003912.1. NM_003921.4.
UniGeneHs.193516.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2MB9NMR-A1-115[»]
ProteinModelPortalO95999.
SMRO95999. Positions 10-115.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114429. 48 interactions.
DIPDIP-29740N.
IntActO95999. 17 interactions.
MINTMINT-89139.
STRING9606.ENSP00000271015.

PTM databases

PhosphoSiteO95999.

Proteomic databases

PaxDbO95999.
PRIDEO95999.

Protocols and materials databases

DNASU8915.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370580; ENSP00000359612; ENSG00000142867.
GeneID8915.
KEGGhsa:8915.
UCSCuc021opd.1. human.

Organism-specific databases

CTD8915.
GeneCardsGC01M085731.
HGNCHGNC:989. BCL10.
HPACAB001944.
HPA017925.
MIM156240. phenotype.
603517. gene.
neXtProtNX_O95999.
PharmGKBPA25299.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44778.
HOGENOMHOG000008671.
HOVERGENHBG050680.
InParanoidO95999.
KOK07368.
OMAGGTCGNS.
OrthoDBEOG79W97M.
PhylomeDBO95999.
TreeFamTF328636.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkO95999.

Gene expression databases

BgeeO95999.
CleanExHS_BCL10.
GenevestigatorO95999.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
InterProIPR001315. CARD.
IPR011029. DEATH-like_dom.
[Graphical view]
PfamPF00619. CARD. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS50209. CARD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBCL10. human.
GeneWikiBCL10.
GenomeRNAi8915.
NextBio33536.
PROO95999.
SOURCESearch...

Entry information

Entry nameBCL10_HUMAN
AccessionPrimary (citable) accession number: O95999
Secondary accession number(s): Q5VUF1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM