O95999 (BCL10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	233 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › perinuclear 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 process	Apoptosis
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Chromosomal rearrangement
Disease	Disease mutation Tumor suppressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell receptor signaling pathway Inferred from direct assay PubMed 15125833. Source: UniProtKB adaptive immune response Traceable author statement PubMed 16831874. Source: UniProtKB apoptotic process Inferred from direct assay Ref.12. Source: UniProtKB cellular defense response Inferred from electronic annotation. Source: Compara cellular response to mechanical stimulus Inferred from expression pattern PubMed 19593445. Source: UniProtKB immunoglobulin mediated immune response Inferred from electronic annotation. Source: Compara 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 cascade 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: Compara 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-dependent Inferred from direct assay PubMed 15207693. Source: UniProtKB protein homooligomerization Inferred from sequence or structural similarity PubMed 16831874. Source: UniProtKB regulation of T cell receptor signaling pathway Inferred from electronic annotation. Source: Compara response to fungus Inferred from electronic annotation. Source: Compara 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_component	CBM complex Non-traceable author statement PubMed 15125833. 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: Compara 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
Molecular_function	NF-kappaB binding Inferred from direct assay PubMed 16280327. Source: UniProtKB protein kinase binding Inferred from direct assay PubMed 17052756. Source: UniProtKB transcription coactivator activity Inferred from direct assay PubMed 15207693. Source: UniProtKB ubiquitin binding Inferred from direct assay PubMed 15082780. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AKT1	P31749	4	EBI-958922,EBI-296087
BCL3	P20749	3	EBI-958922,EBI-958997

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 233	233	B-cell lymphoma/leukemia 10		PRO_0000144074
Regions
	Domain	13 – 101	89	CARD
Amino acid modifications
	Modified residue	138	1	Phosphoserine Ref.17
Natural variations
	Natural variant	5	1	A → S in MALT lymphoma and mesothelioma. Ref.7 Ref.18 Corresponds to variant rs12037217 [ dbSNP | Ensembl ].		VAR_013208
	Natural variant	16	1	V → E in MALT lymphoma. Ref.7		VAR_013209
	Natural variant	31	1	K → E in MALT lymphoma. Ref.7		VAR_013210
	Natural variant	45	1	K → Q in mesothelioma. Ref.18		VAR_013211
	Natural variant	52	1	T → I in mesothelioma. Ref.1		VAR_013212
	Natural variant	57	1	C → R in MALT lymphoma. Ref.7		VAR_013213
	Natural variant	58	1	R → G in germ cell tumor. Ref.1		VAR_013214
	Natural variant	58	1	R → Q in mesothelioma. Ref.18		VAR_013215
	Natural variant	64	1	R → K in MALT lymphoma. Ref.7		VAR_013216
	Natural variant	93	1	N → S in mesothelioma. Ref.18		VAR_013217
	Natural variant	101	1	D → E in MALT lymphoma. Ref.7		VAR_013218
	Natural variant	134	1	S → P in MALT lymphoma. Ref.7		VAR_013219
	Natural variant	153	1	M → V in mesothelioma. Ref.18		VAR_013220
	Natural variant	168	1	T → A in MALT lymphoma. Ref.7		VAR_013221
	Natural variant	174	1	L → S in MALT lymphoma. Ref.7		VAR_013222
	Natural variant	210	1	Missing in follicular lymphoma. Ref.1		VAR_013223
	Natural variant	213	1	G → E in MALT lymphoma and mesothelioma. Ref.7 Ref.18 Corresponds to variant rs3768235 [ dbSNP | Ensembl ].		VAR_013224
	Natural variant	218	1	S → F in germ cell tumor, mesothelioma and other cancer cell lines. Ref.1 Ref.18		VAR_013225
	Natural variant	230	1	V → I in MALT lymphoma. Ref.7		VAR_013226
Experimental info
	Mutagenesis	28	1	L → A: Abolishes cell death-inducing capability. Ref.4
	Mutagenesis	41	1	L → A: Abolishes cell death-inducing capability. Ref.2 Ref.4
	Mutagenesis	41	1	L → Q: Abolishes NF-kappa-B activation and homo/hetero-dimerization. Ref.2 Ref.4
	Mutagenesis	46	1	I → A: Abolishes cell death-inducing capability. Ref.4
	Mutagenesis	47	1	L → A: Abolishes cell death-inducing capability. Ref.4
	Mutagenesis	53	1	E → A: Abolishes cell death-inducing capability. Ref.4
	Mutagenesis	55	1	I → A: Abolishes cell death-inducing capability. Ref.4
	Mutagenesis	78	1	G → R: Abolishes NF-kappa-B activation. Ref.2
	Mutagenesis	81 – 85	5	TLVES → ALVEA: Complete loss of IKBKB/IKKB-mediated phosphorylation. Ref.14
	Mutagenesis	228	1	R → G: Abolishes MALT1-mediated cleavage. Ref.15
	Mutagenesis	231	1	S → A: Promotes NF-kappa-B activation.

Sequences

	Sequence		Length	Mass (Da)
	O95999 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: F87C97F2B784BA4B	FASTA	233	26,252
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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].
[17]	"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, MASS SPECTROMETRY.
[18]	"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.
IPI	IPI00022477.
RefSeq	NP_003912.1. NM_003921.4.
UniGene	Hs.193516.
3D structure databases
ProteinModelPortal	O95999.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29740N.
IntAct	O95999. 13 interactions.
MINT	MINT-89139.
STRING	9606.ENSP00000271015.
PTM databases
PhosphoSite	O95999.
Proteomic databases
PaxDb	O95999.
PRIDE	O95999.
Protocols and materials databases
DNASU	8915.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000271015; ENSP00000271015; ENSG00000142867. ENST00000370580; ENSP00000359612; ENSG00000142867.
GeneID	8915.
KEGG	hsa:8915.
UCSC	uc021opd.1. human.
Organism-specific databases
CTD	8915.
GeneCards	GC01M085731.
HGNC	HGNC:989. BCL10.
HPA	CAB001944. HPA017925.
MIM	156240. phenotype. 603517. gene.
neXtProt	NX_O95999.
PharmGKB	PA25299.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG44778.
HOGENOM	HOG000008671.
HOVERGEN	HBG050680.
InParanoid	O95999.
KO	K07368.
OMA	ASTVIYH.
OrthoDB	EOG41JZD7.
PhylomeDB	O95999.
Enzyme and pathway databases
Pathway_Interaction_DB	bcr_5pathway. BCR signaling pathway. nfkappabcanonicalpathway. Canonical NF-kappaB pathway. tcrpathway. TCR signaling in naive CD4+ T cells. cd8tcrpathway. TCR signaling in naive CD8+ T cells.
Reactome	REACT_6900. Immune System.
Gene expression databases
ArrayExpress	O95999.
Bgee	O95999.
CleanEx	HS_BCL10.
Genevestigator	O95999.
GermOnline	ENSG00000142867. Homo sapiens.
Family and domain databases
Gene3D	1.10.533.10. 1 hit.
InterPro	IPR001315. CARD. IPR011029. DEATH-like_dom. [Graphical view]
Pfam	PF00619. CARD. 1 hit. [Graphical view]
SUPFAM	SSF47986. DEATH_like. 1 hit.
PROSITE	PS50209. CARD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	BCL10. human.
GenomeRNAi	8915.
NextBio	33536.
SOURCE	Search...

Entry information

Entry name

BCL10_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.