BCL10

B-cell CLL/lymphoma 10
Identifiers
Symbols	BCL10; CARMEN; CIPER; CLAP; c-E10; mE10
External IDs	OMIM: 603517 MGI: 1337994 HomoloGene: 2912 GeneCards: BCL10 Gene
Gene Ontology Molecular function • protease binding • transcription coactivator activity • protein binding • protein C-terminus binding • transcription factor binding • kinase activator activity • enzyme binding • kinase binding • protein kinase binding • ubiquitin protein ligase binding • ubiquitin binding • protein kinase B binding • protein self-association • NF-kappaB binding Cellular component • immunological synapse • intracellular • nucleus • cytoplasm • lysosome • cytosol • cytosol • membrane • CBM complex • T cell receptor complex • protein complex • membrane raft • lipopolysaccharide receptor complex • perinuclear region of cytoplasm Biological process • neural tube closure • toll-like receptor signaling pathway • response to molecule of bacterial origin • adaptive immune response • negative regulation of mature B cell apoptosis • apoptotic process • induction of apoptosis • cellular defense response • cell death • response to fungus • immunoglobulin mediated immune response • positive regulation of protein ubiquitination • positive regulation of mast cell cytokine production • lymphotoxin A biosynthetic process • response to chemical stimulus • interleukin-6 biosynthetic process • positive regulation of phosphorylation • regulation of apoptotic process • positive regulation of I-kappaB kinase/NF-kappaB cascade • innate immune response • positive regulation of interleukin-8 biosynthetic process • positive regulation of transcription, DNA-dependent • T cell receptor signaling pathway • T cell receptor signaling pathway • regulation of T cell receptor signaling pathway • positive regulation of T cell activation • positive regulation of NF-kappaB transcription factor activity • protein oligomerization • protein homooligomerization • protein homooligomerization • cellular response to mechanical stimulus Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8915	12042
Ensembl	ENSG00000142867	ENSMUSG00000028191
UniProt	O95999	Q9Z0H7
RefSeq (mRNA)	NM_003921.4	NM_009740.1
RefSeq (protein)	NP_003912.1	NP_033870.1
Location (UCSC)	Chr 1: 85.73 – 85.74 Mb	Chr 3: 145.59 – 145.6 Mb
PubMed search	[1]	[2]

B-cell lymphoma/leukemia 10 is a protein that in humans is encoded by the BCL10 gene.

This gene was identified by its translocation in a case of mucosa-associated lymphoid tissue (MALT) lymphoma. The protein encoded by this gene contains a caspase recruitment domain (CARD), and has been shown to induce apoptosis and to activate NF-kappaB. This protein is reported to interact with other CARD domain containing proteins including CARD9, 10, 11 and 14, which are thought to function as upstream regulators in NF-kappaB signaling. This protein is found to form a complex with MALT1, a protein encoded by another gene known to be translocated in MALT lymphoma. MALT1 and this protein are thought to synergize in the activation of NF-kappaB, and the deregulation of either of them may contribute to the same pathogenetic process that leads to the malignancy.

Interactions

BCL10 has been shown to interact with CARD10, CARD11, MALT1, TRAF2, IKBKG and CARD9.

Further reading

• Bertoni F, Cavalli F, Cotter FE, Zucca E (2003). "Genetic alterations underlying the pathogenesis of MALT lymphoma". Hematol. J. 3 (1): 10–3. doi:10.1038/sj/thj/6200146. PMID 11960389. 
• Lee WC, Balsara B, Liu Z et al (1996). "Loss of heterozygosity analysis defines a critical region in chromosome 1p22 commonly deleted in human malignant mesothelioma". Cancer Res. 56 (19): 4297–301. PMID 8813110. 
• Koseki T, Inohara N, Chen S et al (1999). "CIPER, a novel NF kappaB-activating protein containing a caspase recruitment domain with homology to Herpesvirus-2 protein E10". J. Biol. Chem. 274 (15): 9955–9961. doi:10.1074/jbc.274.15.9955. PMID 10187770. 
• Thome M, Martinon F, Hofmann K et al (1999). "Equine herpesvirus-2 E10 gene product, but not its cellular homologue, activates NF-kappaB transcription factor and c-Jun N-terminal kinase". J. Biol. Chem. 274 (15): 9962–9968. doi:10.1074/jbc.274.15.9962. PMID 10187771. 
• Yan M, Lee J, Schilbach S et al (1999). "mE10, a novel caspase recruitment domain-containing proapoptotic molecule". J. Biol. Chem. 274 (15): 10287–10292. doi:10.1074/jbc.274.15.10287. PMID 10187815. 
• Zhang Q, Siebert R, Yan M et al (1999). "Inactivating mutations and overexpression of BCL10, a caspase recruitment domain-containing gene, in MALT lymphoma with t(1;14)(p22;q32)". Nat. Genet. 22 (1): 63–68. doi:10.1038/8767. PMID 10319863. 
• Srinivasula SM, Ahmad M, Lin JH et al (1999). "CLAP, a novel caspase recruitment domain-containing protein in the tumor necrosis factor receptor pathway, regulates NF-kappaB activation and apoptosis". J. Biol. Chem. 274 (25): 17946–17954. doi:10.1074/jbc.274.25.17946. PMID 10364242. 
• Apostolou S, De Rienzo A, Murthy SS et al (1999). "Absence of BCL10 mutations in human malignant mesothelioma". Cell 97 (6): 684–686. doi:10.1016/S0092-8674(02)09765-9. PMID 10380921. 
• Costanzo A, Guiet C, Vito P (1999). "c-E10 is a caspase-recruiting domain-containing protein that interacts with components of death receptors signaling pathway and activates nuclear factor-kappaB". J. Biol. Chem. 274 (29): 20127–20132. doi:10.1074/jbc.274.29.20127. PMID 10400625. 
• Yoneda T, Imaizumi K, Maeda M et al (2000). "Regulatory mechanisms of TRAF2-mediated signal transduction by Bcl10, a MALT lymphoma-associated protein". J. Biol. Chem. 275 (15): 11114–11120. doi:10.1074/jbc.275.15.11114. PMID 10753917. 
• Ye H, Dogan A, Karran L et al (2000). "BCL10 expression in normal and neoplastic lymphoid tissue. Nuclear localization in MALT lymphoma". Am. J. Pathol. 157 (4): 1147–1154. doi:10.1016/S0002-9440(10)64630-5. PMC 1850175. PMID 11021819. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1850175. 
• Bertin J, Guo Y, Wang L et al (2001). "CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B". J. Biol. Chem. 275 (52): 41082–41086. doi:10.1074/jbc.C000726200. PMID 11053425. 
• Uren AG, O'Rourke K, Aravind LA et al (2000). "Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma". Mol. Cell 6 (4): 961–967. doi:10.1016/S1097-2765(05)00086-9. PMID 11090634. 
• Poyet JL, Srinivasula SM, Alnemri ES (2001). "vCLAP, a caspase-recruitment domain-containing protein of equine Herpesvirus-2, persistently activates the Ikappa B kinases through oligomerization of IKKgamma". J. Biol. Chem. 276 (5): 3183–3187. doi:10.1074/jbc.C000792200. PMID 11113112. 
• Ruland J, Duncan GS, Elia A et al (2001). "Bcl10 is a positive regulator of antigen receptor-induced activation of NF-kappaB and neural tube closure". Cell 104 (1): 33–42. doi:10.1016/S0092-8674(01)00189-1. PMID 11163238. 
• Wang L, Guo Y, Huang WJ et al (2001). "Card10 is a novel caspase recruitment domain/membrane-associated guanylate kinase family member that interacts with BCL10 and activates NF-kappa B". J. Biol. Chem. 276 (24): 21405–21409. doi:10.1074/jbc.M102488200. PMID 11259443. 
• Lucas PC, Yonezumi M, Inohara N et al (2001). "Bcl10 and MALT1, independent targets of chromosomal translocation in malt lymphoma, cooperate in a novel NF-kappa B signaling pathway". J. Biol. Chem. 276 (22): 19012–19019. doi:10.1074/jbc.M009984200. PMID 11262391. 
• Bertin J, Wang L, Guo Y et al (2001). "CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B". J. Biol. Chem. 276 (15): 11877–11882. doi:10.1074/jbc.M010512200. PMID 11278692. 
• Gaide O, Martinon F, Micheau O et al (2001). "Carma1, a CARD-containing binding partner of Bcl10, induces Bcl10 phosphorylation and NF-kappaB activation". FEBS Lett. 496 (2–3): 121–127. doi:10.1016/S0014-5793(01)02414-0. PMID 11356195.