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B-cell lymphoma/leukemia 10 (B-cell CLL/lymphoma 10) (Bcl-10) (CARD-containing molecule enhancing NF-kappa-B) (CARD-like apoptotic protein) (hCLAP) (CED-3/ICH-1 prodomain homologous E10-like regulator) (CIPER) (Cellular homolog of vCARMEN) (cCARMEN) (Cellular-E10) (c-E10) (Mammalian CARD-containing adapter molecule E10) (mE10)

 BCL10_HUMAN             Reviewed;         233 AA.
O95999; Q5VUF1;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-OCT-2017, entry version 160.
RecName: Full=B-cell lymphoma/leukemia 10;
AltName: Full=B-cell CLL/lymphoma 10;
Short=Bcl-10;
AltName: Full=CARD-containing molecule enhancing NF-kappa-B;
AltName: Full=CARD-like apoptotic protein;
Short=hCLAP;
AltName: Full=CED-3/ICH-1 prodomain homologous E10-like regulator;
Short=CIPER;
AltName: Full=Cellular homolog of vCARMEN;
Short=cCARMEN;
AltName: Full=Cellular-E10;
Short=c-E10;
AltName: Full=Mammalian CARD-containing adapter molecule E10;
Short=mE10;
Name=BCL10; Synonyms=CIPER, CLAP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN MALTOMA, AND VARIANTS
ILE-52; GLY-58; GLU-210 DEL AND PHE-218.
TISSUE=Lymphoma;
PubMed=9989495; DOI=10.1016/S0092-8674(00)80957-5;
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.;
"Bcl10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and
mutated in multiple tumor types.";
Cell 96:35-45(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF LEU-41 AND GLY-78.
PubMed=10187770; DOI=10.1074/jbc.274.15.9955;
Koseki T., Inohara N., Chen S., Carrio R., Merino J., Hottiger M.O.,
Nabel G.J., Nunez G.;
"CIPER, a novel NF kappaB-activating protein containing a caspase
recruitment domain with homology to Herpesvirus-2 protein E10.";
J. Biol. Chem. 274:9955-9961(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10187771; DOI=10.1074/jbc.274.15.9962;
Thome M., Martinon F., Hofmann K., Rubio V., Steiner V., Schneider P.,
Mattmann C., Tschopp J.;
"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. 274:9962-9968(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF LEU-28; LEU-41; ILE-46;
LEU-47; GLU-53 AND ILE-55.
PubMed=10187815; DOI=10.1074/jbc.274.15.10287;
Yan M., Lee J., Schilbach S., Goddard A., Dixit V.M.;
"mE10, a novel caspase recruitment domain-containing proapoptotic
molecule.";
J. Biol. Chem. 274:10287-10292(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10364242; DOI=10.1074/jbc.274.25.17946;
Srinivasula S.M., Ahmad M., Lin J.-H., Poyet J.-L.,
Fernandes-Alnemri T., Tsichlis P.N., Alnemri E.S.;
"CLAP, a novel caspase recruitment domain-containing protein in the
tumor necrosis factor receptor pathway, regulates NF-kappaB activation
and apoptosis.";
J. Biol. Chem. 274:17946-17954(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
PubMed=10400625; DOI=10.1074/jbc.274.29.20127;
Costanzo A., Guiet C., Vito P.;
"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. 274:20127-20132(1999).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS SER-5; GLU-16;
GLU-31; ARG-57; LYS-64; GLU-101; PRO-134; ALA-168; SER-174; GLU-213
AND ILE-230.
PubMed=10319863; DOI=10.1038/8767;
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.;
"Inactivating mutations and overexpression of BCL10, a caspase
recruitment domain-containing gene, in MALT lymphoma with
t(1;14)(p22;q32).";
Nat. Genet. 22:63-68(1999).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PHOSPHORYLATION.
PubMed=11466612; DOI=10.1038/sj.onc.1204576;
Yui D., Yoneda T., Oono K., Katayama T., Imaizumi K., Tohyama M.;
"Interchangeable binding of Bcl10 to TRAF2 and cIAPs regulates
apoptosis signaling.";
Oncogene 20:4317-4323(2001).
[13]
IDENTIFICATION IN A MEMBRANE RAFT COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=17287217; DOI=10.1074/jbc.M609157200;
Ohnuma K., Uchiyama M., Yamochi T., Nishibashi K., Hosono O.,
Takahashi N., Kina S., Tanaka H., Lin X., Dang N.H., Morimoto C.;
"Caveolin-1 triggers T-cell activation via CD26 in association with
CARMA1.";
J. Biol. Chem. 282:10117-10131(2007).
[14]
PHOSPHORYLATION BY IKBKB/IKKB, AND MUTAGENESIS OF 81-THR--SER-85.
PubMed=17213322; DOI=10.1073/pnas.0606982104;
Lobry C., Lopez T., Israel A., Weil R.;
"Negative feedback loop in T cell activation through IkappaB kinase-
induced phosphorylation and degradation of Bcl10.";
Proc. Natl. Acad. Sci. U.S.A. 104:908-913(2007).
[15]
FUNCTION, AND MUTAGENESIS OF ARG-228.
PubMed=18264101; DOI=10.1038/ni1568;
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.;
"The proteolytic activity of the paracaspase MALT1 is key in T cell
activation.";
Nat. Immunol. 9:272-281(2008).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
FUNCTION, AND INVOLVEMENT IN IMD37.
PubMed=25365219; DOI=10.1172/JCI77493;
Torres J.M., Martinez-Barricarte R., Garcia-Gomez S., Mazariegos M.S.,
Itan Y., Boisson B., Rholvarez R., Jimenez-Reinoso A., Del Pino L.,
Rodriguez-Pena R., Ferreira A., Hernandez-Jimenez E., Toledano V.,
Cubillos-Zapata C., Diaz-Almiron M., Lopez-Collazo E.,
Unzueta-Roch J.L., Sanchez-Ramon S., Regueiro J.R., Lopez-Granados E.,
Casanova J.L., Perez de Diego R.;
"Inherited BCL10 deficiency impairs hematopoietic and nonhematopoietic
immunity.";
J. Clin. Invest. 124:5239-5248(2014).
[20]
SUBUNIT.
PubMed=27113748; DOI=10.15252/embr.201642109;
Afonina I.S., Van Nuffel E., Baudelet G., Driege Y., Kreike M.,
Staal J., Beyaert R.;
"The paracaspase MALT1 mediates CARD14-induced signaling in
keratinocytes.";
EMBO Rep. 17:914-927(2016).
[21]
VARIANTS SER-5; MET-162 AND GLU-213.
PubMed=10582682;
Lee S.H., Shin M.S., Kim H.S., Park W.S., Kim S.Y., Lee H.K.,
Park J.Y., Oh R.R., Jang J.J., Park K.M., Han J.Y., Kang C.S.,
Lee J.Y., Yoo N.J.;
"Point mutations and deletions of the Bcl10 gene in solid tumors and
malignant lymphomas.";
Cancer Res. 59:5674-5677(1999).
[22]
VARIANTS SER-5; GLN-45; GLN-58; SER-93; VAL-153; GLU-213 AND PHE-218.
PubMed=10380921; DOI=10.1016/S0092-8674(02)09765-9;
Apostolou S., de Rienzo A., Murthy S.S., Jhanwar S.C., Testa J.R.;
"Absence of BCL10 mutations in human malignant mesothelioma.";
Cell 97:684-686(1999).
-!- FUNCTION: Involved in adaptive immune response (PubMed:25365219).
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 (PubMed:18264101).
{ECO:0000269|PubMed:18264101, ECO:0000269|PubMed:25365219}.
-!- SUBUNIT: 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.
Forms a complex with CARD14 and MALT1; resulting in the formation
of a CBM (CARD14-BLC10-MALT1) complex (PubMed:27113748). 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).
{ECO:0000250|UniProtKB:Q9Z0H7, ECO:0000269|PubMed:27113748}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-958922, EBI-958922;
P31749:AKT1; NbExp=5; IntAct=EBI-958922, EBI-296087;
P20749:BCL3; NbExp=3; IntAct=EBI-958922, EBI-958997;
Q9BXL7:CARD11; NbExp=7; IntAct=EBI-958922, EBI-7006141;
Q9H257:CARD9; NbExp=6; IntAct=EBI-958922, EBI-751319;
Q9Y2V7:COG6; NbExp=4; IntAct=EBI-958922, EBI-3866319;
Q66677:E10 (xeno); NbExp=2; IntAct=EBI-958922, EBI-11709474;
Q9Y6K9:IKBKG; NbExp=7; IntAct=EBI-958922, EBI-81279;
Q9UDY8:MALT1; NbExp=18; IntAct=EBI-958922, EBI-1047372;
Q05513:PRKCZ; NbExp=3; IntAct=EBI-958922, EBI-295351;
Q12933:TRAF2; NbExp=8; IntAct=EBI-958922, EBI-355744;
-!- 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.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- PTM: Phosphorylated. Phosphorylation results in dissociation from
TRAF2 and binding to BIRC2/c-IAP2. Phosphorylated by IKBKB/IKKB.
{ECO:0000269|PubMed:11466612, ECO:0000269|PubMed:17213322}.
-!- 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.
-!- 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
mutations 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 mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BCL10ID222ch1p22.html";
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EMBL; AJ006288; CAA06955.1; -; mRNA.
EMBL; AF057700; AAD15800.1; -; mRNA.
EMBL; AF100338; AAD16428.1; -; mRNA.
EMBL; AF127386; AAD32597.1; -; mRNA.
EMBL; AF134395; AAD39147.1; -; mRNA.
EMBL; AF105066; AAF06894.1; -; mRNA.
EMBL; AF082283; AAC99767.1; -; mRNA.
EMBL; AF097732; AAD24918.1; -; Genomic_DNA.
EMBL; AK291346; BAF84035.1; -; mRNA.
EMBL; AL590113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471097; EAW73208.1; -; Genomic_DNA.
EMBL; BC053617; AAH53617.1; -; mRNA.
CCDS; CCDS704.1; -.
RefSeq; NP_003912.1; NM_003921.4.
UniGene; Hs.193516; -.
PDB; 2MB9; NMR; -; A=1-115.
PDBsum; 2MB9; -.
ProteinModelPortal; O95999; -.
SMR; O95999; -.
BioGrid; 114429; 65.
CORUM; O95999; -.
DIP; DIP-29740N; -.
IntAct; O95999; 39.
MINT; MINT-89139; -.
STRING; 9606.ENSP00000271015; -.
iPTMnet; O95999; -.
PhosphoSitePlus; O95999; -.
BioMuta; BCL10; -.
EPD; O95999; -.
PaxDb; O95999; -.
PeptideAtlas; O95999; -.
PRIDE; O95999; -.
DNASU; 8915; -.
Ensembl; ENST00000370580; ENSP00000359612; ENSG00000142867.
GeneID; 8915; -.
KEGG; hsa:8915; -.
UCSC; uc021opd.3; human.
CTD; 8915; -.
DisGeNET; 8915; -.
EuPathDB; HostDB:ENSG00000142867.12; -.
GeneCards; BCL10; -.
HGNC; HGNC:989; BCL10.
HPA; CAB001944; -.
HPA; HPA017925; -.
MalaCards; BCL10; -.
MIM; 137245; phenotype.
MIM; 603517; gene.
MIM; 616098; phenotype.
neXtProt; NX_O95999; -.
OpenTargets; ENSG00000142867; -.
PharmGKB; PA25299; -.
eggNOG; ENOG410IVMM; Eukaryota.
eggNOG; ENOG4111JRA; LUCA.
GeneTree; ENSGT00490000043442; -.
HOGENOM; HOG000008671; -.
HOVERGEN; HBG050680; -.
InParanoid; O95999; -.
KO; K07368; -.
OMA; RHYLCDK; -.
OrthoDB; EOG091G0UTQ; -.
PhylomeDB; O95999; -.
TreeFam; TF328636; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
SignaLink; O95999; -.
SIGNOR; O95999; -.
ChiTaRS; BCL10; human.
GeneWiki; BCL10; -.
GenomeRNAi; 8915; -.
PRO; PR:O95999; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000142867; -.
CleanEx; HS_BCL10; -.
ExpressionAtlas; O95999; baseline and differential.
Genevisible; O95999; HS.
GO; GO:0032449; C:CBM complex; NAS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0051059; F:NF-kappaB binding; IDA:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0043422; F:protein kinase B binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IMP:UniProtKB.
GO; GO:0001783; P:B cell apoptotic process; IEA:Ensembl.
GO; GO:0008219; P:cell death; IDA:UniProtKB.
GO; GO:0006968; P:cellular defense response; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0016064; P:immunoglobulin mediated immune response; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IEP:UniProtKB.
GO; GO:0042226; P:interleukin-6 biosynthetic process; NAS:UniProtKB.
GO; GO:0042109; P:lymphotoxin A biosynthetic process; NAS:UniProtKB.
GO; GO:0002906; P:negative regulation of mature B cell apoptotic process; IDA:UniProtKB.
GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
GO; GO:0045416; P:positive regulation of interleukin-8 biosynthetic process; IMP:UniProtKB.
GO; GO:0032765; P:positive regulation of mast cell cytokine production; NAS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0042327; P:positive regulation of phosphorylation; IDA:UniProtKB.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0050870; P:positive regulation of T cell activation; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IPI:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0032094; P:response to food; IDA:UniProtKB.
GO; GO:0009620; P:response to fungus; IEA:Ensembl.
GO; GO:0002237; P:response to molecule of bacterial origin; IEP:UniProtKB.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0070231; P:T cell apoptotic process; IEA:Ensembl.
GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
GO; GO:0002224; P:toll-like receptor signaling pathway; IC:UniProtKB.
InterPro; IPR033238; BCL10/E10.
InterPro; IPR001315; CARD.
InterPro; IPR011029; DEATH-like_dom.
PANTHER; PTHR34920; PTHR34920; 1.
Pfam; PF00619; CARD; 1.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50209; CARD; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Apoptosis; Chromosomal rearrangement;
Complete proteome; Cytoplasm; Disease mutation; Immunity; Membrane;
Phosphoprotein; Reference proteome; Tumor suppressor.
CHAIN 1 233 B-cell lymphoma/leukemia 10.
/FTId=PRO_0000144074.
DOMAIN 13 101 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 138 138 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
VARIANT 5 5 A -> S (found in a MALT lymphoma sample;
unknown pathological significance;
dbSNP:rs12037217).
{ECO:0000269|PubMed:10319863,
ECO:0000269|PubMed:10380921,
ECO:0000269|PubMed:10582682}.
/FTId=VAR_013208.
VARIANT 16 16 V -> E (found in a MALT lymphoma sample;
unknown pathological significance).
{ECO:0000269|PubMed:10319863}.
/FTId=VAR_013209.
VARIANT 31 31 K -> E (found in a MALT lymphoma sample;
unknown pathological significance).
{ECO:0000269|PubMed:10319863}.
/FTId=VAR_013210.
VARIANT 45 45 K -> Q. {ECO:0000269|PubMed:10380921}.
/FTId=VAR_013211.
VARIANT 52 52 T -> I (found in a mesothelioma sample;
unknown pathological significance).
{ECO:0000269|PubMed:9989495}.
/FTId=VAR_013212.
VARIANT 57 57 C -> R (found in a MALT lymphoma sample;
unknown pathological significance).
{ECO:0000269|PubMed:10319863}.
/FTId=VAR_013213.
VARIANT 58 58 R -> G (found in a germ cell tumor
sample; unknown pathological
significance; dbSNP:rs121918314).
{ECO:0000269|PubMed:9989495}.
/FTId=VAR_013214.
VARIANT 58 58 R -> Q. {ECO:0000269|PubMed:10380921}.
/FTId=VAR_013215.
VARIANT 64 64 R -> K (found in a MALT lymphoma sample;
unknown pathological significance).
{ECO:0000269|PubMed:10319863}.
/FTId=VAR_013216.
VARIANT 93 93 N -> S. {ECO:0000269|PubMed:10380921}.
/FTId=VAR_013217.
VARIANT 101 101 D -> E (found in a MALT lymphoma sample;
unknown pathological significance).
{ECO:0000269|PubMed:10319863}.
/FTId=VAR_013218.
VARIANT 134 134 S -> P (found in a MALT lymphoma sample;
unknown pathological significance).
{ECO:0000269|PubMed:10319863}.
/FTId=VAR_013219.
VARIANT 153 153 M -> V. {ECO:0000269|PubMed:10380921}.
/FTId=VAR_013220.
VARIANT 162 162 T -> M (found in a testicular teratoma
sample; somatic mutation;
dbSNP:rs200837308).
{ECO:0000269|PubMed:10582682}.
/FTId=VAR_077898.
VARIANT 168 168 T -> A (found in a MALT lymphoma sample;
unknown pathological significance).
{ECO:0000269|PubMed:10319863}.
/FTId=VAR_013221.
VARIANT 174 174 L -> S (found in a MALT lymphoma sample;
unknown pathological significance).
{ECO:0000269|PubMed:10319863}.
/FTId=VAR_013222.
VARIANT 210 210 Missing (found in a follicular lymphoma
sample; unknown pathological
significance).
{ECO:0000269|PubMed:9989495}.
/FTId=VAR_013223.
VARIANT 213 213 G -> E (found in a MALT lymphoma sample;
unknown pathological significance;
dbSNP:rs3768235).
{ECO:0000269|PubMed:10319863,
ECO:0000269|PubMed:10380921,
ECO:0000269|PubMed:10582682}.
/FTId=VAR_013224.
VARIANT 218 218 S -> F (found in a germ cell tumor and
other cancer cell lines; unknown
pathological significance).
{ECO:0000269|PubMed:10380921,
ECO:0000269|PubMed:9989495}.
/FTId=VAR_013225.
VARIANT 230 230 V -> I (found in a MALT lymphoma sample;
unknown pathological significance).
{ECO:0000269|PubMed:10319863}.
/FTId=VAR_013226.
MUTAGEN 28 28 L->A: Abolishes cell death-inducing
capability.
{ECO:0000269|PubMed:10187815}.
MUTAGEN 41 41 L->A: Abolishes cell death-inducing
capability. {ECO:0000269|PubMed:10187770,
ECO:0000269|PubMed:10187815}.
MUTAGEN 41 41 L->Q: Abolishes NF-kappa-B activation and
homo/hetero-dimerization.
{ECO:0000269|PubMed:10187770,
ECO:0000269|PubMed:10187815}.
MUTAGEN 46 46 I->A: Abolishes cell death-inducing
capability.
{ECO:0000269|PubMed:10187815}.
MUTAGEN 47 47 L->A: Abolishes cell death-inducing
capability.
{ECO:0000269|PubMed:10187815}.
MUTAGEN 53 53 E->A: Abolishes cell death-inducing
capability.
{ECO:0000269|PubMed:10187815}.
MUTAGEN 55 55 I->A: Abolishes cell death-inducing
capability.
{ECO:0000269|PubMed:10187815}.
MUTAGEN 78 78 G->R: Abolishes NF-kappa-B activation.
{ECO:0000269|PubMed:10187770}.
MUTAGEN 81 85 TLVES->ALVEA: Complete loss of
IKBKB/IKKB-mediated phosphorylation.
{ECO:0000269|PubMed:17213322}.
MUTAGEN 228 228 R->G: Abolishes MALT1-mediated cleavage.
{ECO:0000269|PubMed:18264101}.
MUTAGEN 231 231 S->A: Promotes NF-kappa-B activation.
HELIX 11 14 {ECO:0000244|PDB:2MB9}.
HELIX 17 28 {ECO:0000244|PDB:2MB9}.
TURN 29 31 {ECO:0000244|PDB:2MB9}.
STRAND 32 38 {ECO:0000244|PDB:2MB9}.
HELIX 39 42 {ECO:0000244|PDB:2MB9}.
HELIX 49 53 {ECO:0000244|PDB:2MB9}.
TURN 54 57 {ECO:0000244|PDB:2MB9}.
HELIX 61 72 {ECO:0000244|PDB:2MB9}.
TURN 76 79 {ECO:0000244|PDB:2MB9}.
HELIX 80 86 {ECO:0000244|PDB:2MB9}.
STRAND 89 92 {ECO:0000244|PDB:2MB9}.
HELIX 94 105 {ECO:0000244|PDB:2MB9}.
HELIX 107 113 {ECO:0000244|PDB:2MB9}.
SEQUENCE 233 AA; 26252 MW; F87C97F2B784BA4B CRC64;
MEPTAPSLTE EDLTEVKKDA LENLRVYLCE KIIAERHFDH LRAKKILSRE DTEEISCRTS
SRKRAGKLLD YLQENPKGLD TLVESIRREK TQNFLIQKIT DEVLKLRNIK LEHLKGLKCS
SCEPFPDGAT NNLSRSNSDE SNFSEKLRAS TVMYHPEGES STTPFFSTNS SLNLPVLEVG
RTENTIFSST TLPRPGDPGA PPLPPDLQLE EEGTCANSSE MFLPLRSRTV SRQ


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