BCL10
entrez
8915
canonical
uniprot
O95999
canonical
ensembl
ENSG00000142867
resolver
ensp
ENSP00000480561
resolver
ensp
ENSP00000498104
resolver
enst
ENST00000620248
resolver
enst
ENST00000648566
resolver
genesymbol
BCL10
resolver
genesymbol_syn
CIPER
resolver
genesymbol_syn
CLAP
resolver
hgnc
HGNC:989
resolver
uniprot
A0A087WWW9
resolver
uniprot
A2TDT2
resolver
uniprot
Q5VUF1
resolver
uniprot_entry
A0A087WWW9_HUMAN
resolver
uniprot_entry
A2TDT2_HUMAN
resolver
uniprot_entry
BCL10_HUMAN
resolver
uniprot_sec
Q5VUF1
resolver
amino_acid_sequence
MEPTAPSLTEEDLTEVKKDALENLRVYLCEKIIAERHFDHLRAKKILSREDTEEISCRTSSRKRAGKLLDYLQENPKGLDTLVESIRREKTQNFLIQKITDEVLKLRNIKLEHLKGLKCSSCEPFPDGATNNLSRSNSDESNFSEKLRASTVMYHPEGESSTTPFFSTNSSLNLPVLEVGRTENTIFSSTTLPRPGDPGAPPLPPDLQLEEEGTCANSSEMFLPLRSRTVSRQ
uniprot
proteins
disease_involvement
DISEASE: Note=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. {ECO:0000269|PubMed:9989495}.; DISEASE: Immunodeficiency 37 (IMD37) [MIM:616098]: A form of primary combined immunodeficiency, a group of disorders characterized by severe recurrent infections, with normal numbers or an absence of T and B lymphocytes, and impaired cellular and humoral immunity. IMD37 is characterized by hypogammaglobulinemia without lymphopenia, but with profoundly reduced memory B cells and memory T cells, and increased numbers of circulating naive lymphocytes. Inheritance is autosomal recessive. {ECO:0000269|PubMed:25365219}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Lymphoma, mucosa-associated lymphoid type (MALTOMA) [MIM:137245]: A subtype of non-Hodgkin lymphoma, originating in mucosa-associated lymphoid tissue. MALT lymphomas occur most commonly in the gastro-intestinal tract but have been described in a variety of extranodal sites including the ocular adnexa, salivary gland, thyroid, lung, thymus, and breast. Histologically, they are characterized by an infiltrate of small to medium-sized lymphocytes with abundant cytoplasm and irregularly shaped nuclei. Scattered transformed blasts (large cells) also are present. Non-malignant reactive follicles are observed frequently. A pivotal feature is the presence of lymphoepithelial lesions, with invasion and partial destruction of mucosal glands and crypts by aggregates of tumor cells. {ECO:0000269|PubMed:9989495}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Plays a key role in both adaptive and innate immune signaling by bridging CARD domain-containing proteins to immune activation (PubMed:10187770, PubMed:10364242, PubMed:10400625, PubMed:24074955, PubMed:25365219). Acts by channeling adaptive and innate immune signaling downstream of CARD domain-containing proteins CARD9, CARD11 and CARD14 to activate NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (PubMed:24074955). Recruited by activated CARD domain-containing proteins: homooligomerized CARD domain-containing proteins form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10, subsequent recruitment of MALT1 and formation of a CBM complex (PubMed:24074955). This leads to activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (PubMed:18287044, PubMed:24074955, PubMed:27777308). Activated by CARD9 downstream of C-type lectin receptors; CARD9-mediated signals are essential for antifungal immunity (PubMed:26488816). Activated by CARD11 downstream of T-cell receptor (TCR) and B-cell receptor (BCR) (PubMed:18264101, PubMed:18287044, PubMed:24074955, PubMed:27777308). Promotes apoptosis, pro-caspase-9 maturation and activation of NF-kappa-B via NIK and IKK (PubMed:10187815). {ECO:0000269|PubMed:10187770, ECO:0000269|PubMed:10187815, ECO:0000269|PubMed:10364242, ECO:0000269|PubMed:10400625, ECO:0000269|PubMed:18264101, ECO:0000269|PubMed:18287044, ECO:0000269|PubMed:24074955, ECO:0000269|PubMed:25365219, ECO:0000269|PubMed:26488816, ECO:0000269|PubMed:27777308}.
uniprot
proteins
mass_dalton
26252
uniprot
proteins
mutagenesis
MUTAGEN 17; /note="K->R: Decreased linear ubiquitination and impaired ability to activate NF-kappa-B; when associated with R-31 and R-63."; /evidence="ECO:0000269|PubMed:27777308"; MUTAGEN 28; /note="L->A: Abolishes cell death-inducing capability."; /evidence="ECO:0000269|PubMed:10187815"; MUTAGEN 31; /note="K->R: Decreased ubiquitination and ability to bind NEMO; when associated with 63-R--R-67. Decreased ubiquitination and ability to bind NEMO, impaired ability to activate NF-kappa-B; when associated with R-63. Decreased linear ubiquitination and impaired ability to activate NF-kappa-B; when associated with R-17 and R-63."; /evidence="ECO:0000269|PubMed:18287044, ECO:0000269|PubMed:27777308"; MUTAGEN 36; /note="R->E: Abolished homomultimerization and formation of a CBM complex, abolished ability to activate NF-kappa-B."; /evidence="ECO:0000269|PubMed:24074955"; MUTAGEN 41; /note="L->A: Abolishes cell death-inducing capability."; /evidence="ECO:0000269|PubMed:10187770, ECO:0000269|PubMed:10187815"; MUTAGEN 41; /note="L->Q: Abolishes NF-kappa-B activation and homo/heterodimerization."; /evidence="ECO:0000269|PubMed:10187770, ECO:0000269|PubMed:10187815"; MUTAGEN 46; /note="I->A: Abolishes cell death-inducing capability."; /evidence="ECO:0000269|PubMed:10187815"; MUTAGEN 47; /note="L->A: Abolishes cell death-inducing capability."; /evidence="ECO:0000269|PubMed:10187815"; MUTAGEN 50..51; /note="ED->RR: Abolished homomultimerization and formation of a CBM complex."; /evidence="ECO:0000269|PubMed:24074955"; MUTAGEN 50; /note="E->R: Abolished homomultimerization and formation of a CBM complex, abolished ability to activate NF-kappa-B."; /evidence="ECO:0000269|PubMed:24074955"; MUTAGEN 53; /note="E->A: Abolishes cell death-inducing capability."; /evidence="ECO:0000269|PubMed:10187815"; MUTAGEN 53; /note="E->R: Abolished homomultimerization and formation of a CBM complex, abolished ability to activate NF-kappa-B."; /evidence="ECO:0000269|PubMed:24074955"; MUTAGEN 55; /note="I->A: Abolishes cell death-inducing capability."; /evidence="ECO:0000269|PubMed:10187815"; MUTAGEN 63..67; /note="KRAGK->RRAGR: Decreased ubiquitination and ability to bind NEMO; when associated with R-31."; /evidence="ECO:0000269|PubMed:18287044"; MUTAGEN 63; /note="K->R: Decreased ubiquitination and ability to bind NEMO, impaired ability to activate NF-kappa-B; when associated with R-31. Decreased linear ubiquitination and impaired ability to activate NF-kappa-B; when associated with R-17 and R-31."; /evidence="ECO:0000269|PubMed:18287044, ECO:0000269|PubMed:27777308"; MUTAGEN 78; /note="G->R: Abolishes NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:10187770"; MUTAGEN 81..85; /note="TLVES->ALVEA: Complete loss of IKBKB/IKKB-mediated phosphorylation."; /evidence="ECO:0000269|PubMed:17213322"; MUTAGEN 105..115; /note="KLRNIKLEHLK->RLRNIRLEHLR: Does not affect ubiquitination and ability to bind NEMO."; /evidence="ECO:0000269|PubMed:18287044"; MUTAGEN 228; /note="R->G: Abolishes MALT1-mediated cleavage."; /evidence="ECO:0000269|PubMed:18264101"; MUTAGEN 231; /note="S->A: Promotes NF-kappa-B activation.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Phosphorylation results in dissociation from TRAF2 and binding to BIRC2/c-IAP2 (PubMed:11466612). Phosphorylated by IKBKB/IKKB (PubMed:17213322). {ECO:0000269|PubMed:11466612, ECO:0000269|PubMed:17213322}.; PTM: Ubiquitinated via both 'Lys-63'-linked and linear ('Met-1'-linked) polyubiquitin chains in response to T-cell receptor (TCR) activation (PubMed:18287044, PubMed:27777308). Ubiquitination is recognized by IKBKG/NEMO, the regulatory subunit of I-kappa-B kinase (IKK), and is required for TCR-induced NF-kappa-B activation (PubMed:18287044, PubMed:27777308). Linear ubiquitination at Lys-17, Lys-31 and Lys-63 is mediated by RNF31/HOIP; linear ubiquitination is recognized with much higher affinity than 'Lys-63'-linked ubiquitin by IKBKG/NEMO (PubMed:27777308). CARD11 is required for linear ubiquitination by HOIP by promoting the targeting of BCL10 to RNF31/HOIP (PubMed:27777308). {ECO:0000269|PubMed:18287044, ECO:0000269|PubMed:27777308}.; PTM: Proteolytically cleaved by MALT1; required for T-cell activation. {ECO:0000269|PubMed:18264101}.
uniprot
proteins
pubmed
10187770
uniprot
proteins
pubmed
10187771
uniprot
proteins
pubmed
10187815
uniprot
proteins
pubmed
10319863
uniprot
proteins
pubmed
10364242
uniprot
proteins
pubmed
10380921
uniprot
proteins
pubmed
10400625
uniprot
proteins
pubmed
10582682
uniprot
proteins
pubmed
11466612
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17213322
uniprot
proteins
pubmed
17287217
uniprot
proteins
pubmed
18264101
uniprot
proteins
pubmed
18287044
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
24074955
uniprot
proteins
pubmed
25365219
uniprot
proteins
pubmed
26488816
uniprot
proteins
pubmed
27113748
uniprot
proteins
pubmed
27777308
uniprot
proteins
pubmed
28628108
uniprot
proteins
pubmed
31296852
uniprot
proteins
pubmed
9989495
uniprot
proteins
sequence_length
233
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:17287217}. Membrane raft {ECO:0000269|PubMed:17287217}. 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. {ECO:0000269|PubMed:17287217}.
uniprot
proteins