BCL10_MOUSE
ID BCL10_MOUSE Reviewed; 233 AA.
AC Q9Z0H7; Q3UBN4;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=B-cell lymphoma/leukemia 10;
DE AltName: Full=B-cell CLL/lymphoma 10;
DE Short=Bcl-10;
DE AltName: Full=CARD-containing molecule enhancing NF-kappa-B;
DE AltName: Full=CARD-like apoptotic protein {ECO:0000303|PubMed:10364242};
DE Short=mCLAP {ECO:0000303|PubMed:10364242};
DE AltName: Full=CED-3/ICH-1 prodomain homologous E10-like regulator {ECO:0000303|PubMed:10187770};
DE Short=mCIPER {ECO:0000303|PubMed:10187770};
DE AltName: Full=Cellular homolog of vCARMEN;
DE Short=cCARMEN;
DE AltName: Full=Cellular-E10;
DE Short=c-E10;
DE AltName: Full=Mammalian CARD-containing adapter molecule E10 {ECO:0000303|PubMed:10187815};
DE Short=mE10 {ECO:0000303|PubMed:10187815};
GN Name=Bcl10;
GN Synonyms=Ciper {ECO:0000303|PubMed:10187770},
GN Clap {ECO:0000303|PubMed:10364242};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9989495; DOI=10.1016/s0092-8674(00)80957-5;
RA Willis T.G., Jadayel D.M., Du M.-Q., Peng H., Perry A.R., Abdul-Rauf M.,
RA Price H., Karran L., Majekodunmi O., Wlodarska I., Pan L., Crook T.,
RA Hamoudi R., Isaacson P., Dyer M.J.S.;
RT "Bcl10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and mutated
RT in multiple tumor types.";
RL Cell 96:35-45(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10187770; DOI=10.1074/jbc.274.15.9955;
RA Koseki T., Inohara N., Chen S., Carrio R., Merino J., Hottiger M.O.,
RA Nabel G.J., Nunez G.;
RT "CIPER, a novel NF kappaB-activating protein containing a caspase
RT recruitment domain with homology to Herpesvirus-2 protein E10.";
RL J. Biol. Chem. 274:9955-9961(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10187771; DOI=10.1074/jbc.274.15.9962;
RA Thome M., Martinon F., Hofmann K., Rubio V., Steiner V., Schneider P.,
RA Mattmann C., Tschopp J.;
RT "Equine herpesvirus-2 E10 gene product, but not its cellular homologue,
RT activates NF-kappaB transcription factor and c-Jun N-terminal kinase.";
RL J. Biol. Chem. 274:9962-9968(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=10187815; DOI=10.1074/jbc.274.15.10287;
RA Yan M., Lee J., Schilbach S., Goddard A., Dixit V.M.;
RT "mE10, a novel caspase recruitment domain-containing proapoptotic
RT molecule.";
RL J. Biol. Chem. 274:10287-10292(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10364242; DOI=10.1074/jbc.274.25.17946;
RA Srinivasula S.M., Ahmad M., Lin J.-H., Poyet J.-L., Fernandes-Alnemri T.,
RA Tsichlis P.N., Alnemri E.S.;
RT "CLAP, a novel caspase recruitment domain-containing protein in the tumor
RT necrosis factor receptor pathway, regulates NF-kappaB activation and
RT apoptosis.";
RL J. Biol. Chem. 274:17946-17954(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Corpora quadrigemina, Liver, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH PELI2 AND SOCS3.
RX PubMed=15213237; DOI=10.1074/jbc.m400241200;
RA Liu Y., Dong W., Chen L., Xiang R., Xiao H., De G., Wang Z., Qi Y.;
RT "BCL10 mediates lipopolysaccharide/toll-like receptor-4 signaling through
RT interaction with Pellino2.";
RL J. Biol. Chem. 279:37436-37444(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, AND INTERACTION WITH CARD9.
RX PubMed=22265677; DOI=10.1016/j.immuni.2011.11.015;
RA Strasser D., Neumann K., Bergmann H., Marakalala M.J., Guler R.,
RA Rojowska A., Hopfner K.P., Brombacher F., Urlaub H., Baier G., Brown G.D.,
RA Leitges M., Ruland J.;
RT "Syk kinase-coupled C-type lectin receptors engage protein kinase C-delta
RT to elicit Card9 adaptor-mediated innate immunity.";
RL Immunity 36:32-42(2012).
RN [11]
RP INTERACTION WITH CARD11, AND MUTAGENESIS OF GLU-50; GLU-53 AND GLU-54.
RX PubMed=22880103; DOI=10.1371/journal.pone.0042775;
RA Li S., Yang X., Shao J., Shen Y.;
RT "Structural insights into the assembly of CARMA1 and BCL10.";
RL PLoS ONE 7:e42775-e42775(2012).
CC -!- FUNCTION: Plays a key role in both adaptive and innate immune signaling
CC by bridging CARD domain-containing proteins to immune activation
CC (PubMed:22265677). Acts by channeling adaptive and innate immune
CC signaling downstream of CARD domain-containing proteins CARD9, CARD11
CC and CARD14 to activate NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12,
CC MAPK13 and/or MAPK14) pathways which stimulate expression of genes
CC encoding pro-inflammatory cytokines and chemokines (PubMed:22265677).
CC Recruited by activated CARD domain-containing proteins:
CC homooligomerized CARD domain-containing proteins form a nucleating
CC helical template that recruits BCL10 via CARD-CARD interaction, thereby
CC promoting polymerization of BCL10, subsequent recruitment of MALT1 and
CC formation of a CBM complex (By similarity). This leads to activation of
CC NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14)
CC pathways which stimulate expression of genes encoding pro-inflammatory
CC cytokines and chemokines (By similarity). Activated by CARD9 downstream
CC of C-type lectin receptors; CARD9-mediated signals are essential for
CC antifungal immunity (PubMed:22265677). Activated by CARD11 downstream
CC of T-cell receptor (TCR) and B-cell receptor (BCR) (By similarity).
CC Promotes apoptosis, pro-caspase-9 maturation and activation of NF-
CC kappa-B via NIK and IKK (By similarity). {ECO:0000250|UniProtKB:O95999,
CC ECO:0000269|PubMed:22265677}.
CC -!- SUBUNIT: Homomultimer; homooligomerized following recruitment by CARD
CC domain-containing proteins that form a nucleating helical template that
CC recruits BCL10 via CARD-CARD interaction (By similarity). Self-
CC associates by CARD-CARD interaction and interacts with other CARD-
CC proteins such as CARD9, CARD10, CARD11 and CARD14 (PubMed:22265677,
CC PubMed:22880103). Forms a complex with CARD14 and MALT1; resulting in
CC the formation of a CBM (CARD14-BCL10-MALT1) complex (By similarity).
CC Forms a complex with CARD11 and MALT1; resulting in the formation of a
CC CBM (CARD11-BCL10-MALT1) complex (By similarity). Forms a complex with
CC CARD9 and MALT1; resulting in the formation of a CBM (CARD9-BCL10-
CC MALT1) complex (PubMed:22265677). Found in a membrane raft complex, at
CC least composed of BCL10, CARD11, DPP4 and IKBKB (By similarity). Binds
CC caspase-9 with its C-terminal domain (By similarity). Interacts with
CC TRAF2 and BIRC2/c-IAP2 (By similarity). Interacts with PELI2 and SOCS3;
CC these interactions may be mutually exclusive (PubMed:15213237).
CC {ECO:0000250|UniProtKB:O95999, ECO:0000269|PubMed:15213237,
CC ECO:0000269|PubMed:22265677, ECO:0000269|PubMed:22880103}.
CC -!- INTERACTION:
CC Q9Z0H7; Q66677: E10; Xeno; NbExp=3; IntAct=EBI-8545413, EBI-11709474;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95999}.
CC Membrane raft {ECO:0000250|UniProtKB:O95999}. Note=Colocalized with
CC DPP4 in membrane rafts. {ECO:0000250|UniProtKB:O95999}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, brain, spleen, lung,
CC liver, skeletal muscle, kidney and testis. Detected in developing
CC brain, olfactory epithelium, tongue, whisker follicles, salivary gland,
CC heart, lung, liver and intestinal epithelia of stage 15 embryos.
CC -!- PTM: Phosphorylated by IKBKB/IKKB. {ECO:0000250|UniProtKB:O95999}.
CC -!- PTM: Ubiquitinated via both 'Lys-63'-linked and linear ('Met-1'-linked)
CC polyubiquitin chains in response to T-cell receptor (TCR) activation.
CC Ubiquitination is recognized by IKBKG/NEMO, the regulatory subunit of
CC I-kappa-B kinase (IKK), and is required for TCR-induced NF-kappa-B
CC activation. Linear ubiquitination at Lys-17, Lys-31 and Lys-63 is
CC mediated by RNF31/HOIP; linear ubiquitination is recognized with much
CC higher affinity than 'Lys-63'-linked ubiquitin by IKBKG/NEMO. CARD11 is
CC required for linear ubiquitination by HOIP by promoting the targeting
CC of BCL10 to RNF31/HOIP. {ECO:0000250|UniProtKB:O95999}.
CC -!- PTM: Proteolytically cleaved by MALT1; required for T-cell activation.
CC {ECO:0000250|UniProtKB:O95999}.
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DR EMBL; AJ006289; CAA06956.1; -; mRNA.
DR EMBL; AF057701; AAD15801.1; -; mRNA.
DR EMBL; AF100339; AAD16429.1; -; mRNA.
DR EMBL; AF127387; AAD32598.1; -; mRNA.
DR EMBL; AF134396; AAD39148.1; -; mRNA.
DR EMBL; AK076082; BAC36168.1; -; mRNA.
DR EMBL; AK140179; BAE24267.1; -; mRNA.
DR EMBL; AK150883; BAE29930.1; -; mRNA.
DR EMBL; AK152563; BAE31316.1; -; mRNA.
DR EMBL; AK152847; BAE31540.1; -; mRNA.
DR EMBL; AK156890; BAE33885.1; -; mRNA.
DR EMBL; AK169126; BAE40905.1; -; mRNA.
DR EMBL; AK172158; BAE42852.1; -; mRNA.
DR EMBL; BC024379; AAH24379.1; -; mRNA.
DR CCDS; CCDS17897.1; -.
DR RefSeq; NP_033870.1; NM_009740.2.
DR AlphaFoldDB; Q9Z0H7; -.
DR SMR; Q9Z0H7; -.
DR BioGRID; 198317; 14.
DR DIP; DIP-60309N; -.
DR IntAct; Q9Z0H7; 4.
DR MINT; Q9Z0H7; -.
DR STRING; 10090.ENSMUSP00000029842; -.
DR iPTMnet; Q9Z0H7; -.
DR PhosphoSitePlus; Q9Z0H7; -.
DR EPD; Q9Z0H7; -.
DR MaxQB; Q9Z0H7; -.
DR PaxDb; Q9Z0H7; -.
DR PRIDE; Q9Z0H7; -.
DR ProteomicsDB; 273478; -.
DR Antibodypedia; 4526; 1327 antibodies from 48 providers.
DR DNASU; 12042; -.
DR Ensembl; ENSMUST00000029842; ENSMUSP00000029842; ENSMUSG00000028191.
DR GeneID; 12042; -.
DR KEGG; mmu:12042; -.
DR UCSC; uc008rqs.2; mouse.
DR CTD; 8915; -.
DR MGI; MGI:1337994; Bcl10.
DR VEuPathDB; HostDB:ENSMUSG00000028191; -.
DR eggNOG; ENOG502RXGH; Eukaryota.
DR GeneTree; ENSGT00490000043442; -.
DR HOGENOM; CLU_103803_0_0_1; -.
DR InParanoid; Q9Z0H7; -.
DR OMA; HPDGEQS; -.
DR OrthoDB; 1472514at2759; -.
DR PhylomeDB; Q9Z0H7; -.
DR TreeFam; TF328636; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR BioGRID-ORCS; 12042; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Bcl10; mouse.
DR PRO; PR:Q9Z0H7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9Z0H7; protein.
DR Bgee; ENSMUSG00000028191; Expressed in saccule of membranous labyrinth and 263 other tissues.
DR ExpressionAtlas; Q9Z0H7; baseline and differential.
DR Genevisible; Q9Z0H7; MM.
DR GO; GO:0032449; C:CBM complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0001772; C:immunological synapse; IDA:MGI.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0002096; C:polkadots; IDA:CACAO.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0050700; F:CARD domain binding; IPI:UniProtKB.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0140296; F:general transcription initiation factor binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0019209; F:kinase activator activity; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISS:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; ISS:UniProtKB.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0043422; F:protein kinase B binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; ISS:UniProtKB.
DR GO; GO:0061760; P:antifungal innate immune response; IDA:UniProtKB.
DR GO; GO:0001783; P:B cell apoptotic process; IDA:MGI.
DR GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR GO; GO:0006968; P:cellular defense response; IMP:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0045576; P:mast cell activation; NAS:UniProtKB.
DR GO; GO:0002906; P:negative regulation of mature B cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISO:MGI.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISS:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0050870; P:positive regulation of T cell activation; IMP:MGI.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IMP:MGI.
DR GO; GO:0032094; P:response to food; ISS:UniProtKB.
DR GO; GO:0009620; P:response to fungus; IMP:MGI.
DR GO; GO:0070231; P:T cell apoptotic process; IDA:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; ISO:MGI.
DR CDD; cd08810; CARD_BCL10; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR033238; BCL10/E10.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR042143; CARD_BCL10.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR PANTHER; PTHR34920; PTHR34920; 1.
DR Pfam; PF00619; CARD; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50209; CARD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Adaptive immunity; Apoptosis; Cytoplasm; Immunity;
KW Innate immunity; Isopeptide bond; Membrane; Phosphoprotein;
KW Reference proteome; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..233
FT /note="B-cell lymphoma/leukemia 10"
FT /id="PRO_0000144075"
FT DOMAIN 13..101
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT REGION 185..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 228..229
FT /note="Cleavage; by MALT1"
FT /evidence="ECO:0000250|UniProtKB:O95999"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O95999"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95999"
FT CROSSLNK 17
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O95999"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O95999"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O95999"
FT MUTAGEN 50
FT /note="E->A: Decreased interaction with CARD11."
FT /evidence="ECO:0000269|PubMed:22880103"
FT MUTAGEN 53
FT /note="E->A: Decreased interaction with CARD11."
FT /evidence="ECO:0000269|PubMed:22880103"
FT MUTAGEN 54
FT /note="E->A: Decreased interaction with CARD11."
FT /evidence="ECO:0000269|PubMed:22880103"
SQ SEQUENCE 233 AA; 25948 MW; C0539BC97102DBB8 CRC64;
MEAPAPSLTE EDLTEVKKDA LENLRVYLCE KIIAERHFDH LRAKKILSRE DTEEISCRTS
SRKRAGKLLD YLQENPRGLD TLVESIRREK TQSFLIQKIT DEVLKLRNIK LEHLKGLKCS
SCEPFAAGAT NNLSRCNSDE SNLSEKQRAS TVMYHPEGES STAPFFSMAS SLNLPVLEVG
RTENSSFSSA TLPRPGDPGA PPLPPDLRLE EGGSCGNSSE MFLPLRSRAL SRQ
