Reviewed, UniProtKB/Swiss-Prot Q9Z0H7 (BCL10_MOUSE)

Names and origin

Protein names

Recommended name:
    B-cell lymphoma/leukemia 10
Alternative name(s):
    B-cell CLL/lymphoma 10
      Short name=Bcl-10
    CED-3/ICH-1 prodomain homologous E10-like regulator
      Short name=mCIPER
    CARD-containing molecule enhancing NF-kappa-B
    Cellular homolog of vCARMEN
      Short name=cCARMEN
    Mammalian CARD-containing adapter molecule E10
      Short name=mE10
    Cellular-E10
      Short name=c-E10
    CARD-like apoptotic protein
      Short name=mCLAP

Gene names

Name:	Bcl10
Synonyms:	Ciper, Clap

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	233 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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 By similarity. Is a substrate for MALT1 By similarity.
Subunit structure	Self-associates by CARD-CARD interaction and 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 By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Highly expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. Detected in developing brain, olfactory epithelium, tongue, whisker follicles, salivary gland, heart, lung, liver and intestinal epithelia of stage 15 embryos.
Post-translational modification	Phosphorylated By similarity.
Sequence similarities	Contains 1 CARD domain.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm
Disease	Tumor suppressor
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype. Source: MGI T cell receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB apoptosis Inferred from sequence or structural similarity. Source: UniProtKB cellular defense response Inferred from mutant phenotype. Source: MGI immunoglobulin mediated immune response Inferred from mutant phenotype. Source: MGI innate immune response Inferred from sequence or structural similarity. Source: UniProtKB mast cell activation Non-traceable author statement. Source: UniProtKB negative regulation of mature B cell apoptosis Inferred from sequence or structural similarity. Source: UniProtKB neural tube closure Inferred from mutant phenotype. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of T cell activation Inferred from mutant phenotype. Source: MGI positive regulation of interleukin-8 biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB protein homooligomerization Inferred from mutant phenotype. Source: UniProtKB regulation of T cell receptor signaling pathway Inferred from mutant phenotype. Source: MGI response to fungus Inferred from mutant phenotype. Source: MGI response to molecule of bacterial origin Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB immunological synapse Inferred from direct assay. Source: MGI lysosome Inferred from sequence or structural similarity. Source: UniProtKB membrane raft Inferred from direct assay. Source: MGI nucleus Inferred from sequence or structural similarity. Source: UniProtKB perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB protein complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	NF-kappaB binding Inferred from sequence or structural similarity. Source: UniProtKB protein C-terminus binding Inferred from sequence or structural similarity. Source: UniProtKB protein kinase B binding Inferred from sequence or structural similarity. Source: UniProtKB protein self-association Inferred from sequence or structural similarity. Source: UniProtKB transcription coactivator activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin binding Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin protein ligase binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

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_0000144075
Regions
	Domain	13 – 101	89	CARD

Sequences

	Sequence		Length	Mass (Da)
	Q9Z0H7-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: C0539BC97102DBB8	FASTA	233	25,948
	10 20 30 40 50 60 MEAPAPSLTE EDLTEVKKDA LENLRVYLCE KIIAERHFDH LRAKKILSRE DTEEISCRTS 70 80 90 100 110 120 SRKRAGKLLD YLQENPRGLD TLVESIRREK TQSFLIQKIT DEVLKLRNIK LEHLKGLKCS 130 140 150 160 170 180 SCEPFAAGAT NNLSRCNSDE SNLSEKQRAS TVMYHPEGES STAPFFSMAS SLNLPVLEVG 190 200 210 220 230 RTENSSFSSA TLPRPGDPGA PPLPPDLRLE EGGSCGNSSE MFLPLRSRAL 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: 9989495] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 10187770] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 10187771] [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: 10187815] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Embryo.
[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: 10364242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Bone marrow, Corpora quadrigemina, Liver and Spleen.
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ006289 mRNA. Translation: CAA06956.1. AF057701 mRNA. Translation: AAD15801.1. AF100339 mRNA. Translation: AAD16429.1. AF127387 mRNA. Translation: AAD32598.1. AF134396 mRNA. Translation: AAD39148.1. AK076082 mRNA. Translation: BAC36168.1. AK140179 mRNA. Translation: BAE24267.1. AK150883 mRNA. Translation: BAE29930.1. AK152563 mRNA. Translation: BAE31316.1. AK152847 mRNA. Translation: BAE31540.1. AK156890 mRNA. Translation: BAE33885.1. AK169126 mRNA. Translation: BAE40905.1. AK172158 mRNA. Translation: BAE42852.1. BC024379 mRNA. Translation: AAH24379.1.
IPI	IPI00129152.
RefSeq	NP_033870.1.
UniGene	Mm.239141
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9Z0H7.
PTM databases
PhosphoSite	Q9Z0H7.
Proteomic databases
PRIDE	Q9Z0H7.
Genome annotation databases
Ensembl	ENSMUST00000029842; ENSMUSP00000029842; ENSMUSG00000028191; Mus musculus. [Genome view]
GeneID	12042.
KEGG	mmu:12042.
UCSC	uc008rqs.1. mouse.
Organism-specific databases
CTD	12042.
MGI	MGI:1337994. Bcl10.
Phylogenomic databases
HOVERGEN	Q9Z0H7.
Gene expression databases
ArrayExpress	Q9Z0H7.
Bgee	Q9Z0H7.
CleanEx	MM_BCL10.
Genevestigator	Q9Z0H7.
GermOnline	ENSMUSG00000028191. Mus musculus.
Family and domain databases
InterPro	IPR001315. CARD. IPR011029. DEATH-like. [Graphical view]
Gene3D	G3DSA:1.10.533.10. DEATH_like. 1 hit.
Pfam	PF00619. CARD. 1 hit. [Graphical view]
PROSITE	PS50209. CARD. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	280309.
SOURCE	Search...

Entry information

Entry name

BCL10_MOUSE

Accession

Primary (citable) accession number: Q9Z0H7
Secondary accession number(s): Q3UBN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	May 1, 1999
Last modified:	October 13, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)