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Q9Z0H7 (BCL10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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=mCLAP
CED-3/ICH-1 prodomain homologous E10-like regulator
Short name=mCIPER
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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length233 AA.
Sequence statusComplete.
Protein existenceEvidence 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 By similarity. Is a substrate for MALT1 By similarity.

Subunit structure

Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB. 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. Interacts with PELI2 and SOCS3; these interactions may be mutually exclusive. Ref.8

Subcellular location

Cytoplasm By similarity. Membrane raft By similarity. Note: Colocalized with DPP4 in membrane rafts 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 IKBKB/IKKB By similarity.

Sequence similarities

Contains 1 CARD domain.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Membrane
   DiseaseTumor suppressor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell apoptotic process

Inferred from direct assay PubMed 10753917. Source: MGI

I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 11163238. Source: MGI

T cell apoptotic process

Inferred from direct assay PubMed 10753917. Source: MGI

T cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence alignment Ref.4. Source: MGI

cell death

Inferred from sequence or structural similarity. Source: UniProtKB

cellular defense response

Inferred from mutant phenotype PubMed 11163238. Source: MGI

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

immunoglobulin mediated immune response

Inferred from mutant phenotype PubMed 11163238. Source: MGI

innate immune response

Inferred from sequence or structural similarity. Source: UniProtKB

mast cell activation

Non-traceable author statement PubMed 16432253. Source: UniProtKB

negative regulation of mature B cell apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

neural tube closure

Inferred from mutant phenotype PubMed 11163238. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

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 PubMed 14614861. Source: MGI

positive regulation of apoptotic process

Inferred from sequence alignment Ref.1. Source: MGI

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 10753917. Source: MGI

positive regulation of execution phase of apoptosis

Inferred from sequence orthology Ref.5. Source: MGI

positive regulation of extrinsic apoptotic signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

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-templated

Inferred from sequence or structural similarity. Source: UniProtKB

protein homooligomerization

Inferred from mutant phenotype PubMed 16831874. Source: UniProtKB

protein oligomerization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of T cell receptor signaling pathway

Inferred from mutant phenotype PubMed 14614861. Source: MGI

response to food

Inferred from sequence or structural similarity. Source: UniProtKB

response to fungus

Inferred from mutant phenotype PubMed 16862125. Source: MGI

response to molecule of bacterial origin

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentCBM complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

T cell receptor complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic microtubule

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 16831874. Source: UniProtKB

immunological synapse

Inferred from direct assay PubMed 14724296. Source: MGI

lipopolysaccharide receptor complex

Inferred from electronic annotation. Source: Ensembl

lysosome

Inferred from sequence or structural similarity. Source: UniProtKB

membrane raft

Inferred from direct assay PubMed 12867038. 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_functionNF-kappaB binding

Inferred from sequence or structural similarity. Source: UniProtKB

cysteine-type endopeptidase activator activity involved in apoptotic process

Inferred from sequence alignment Ref.4. Source: MGI

kinase activator activity

Inferred from electronic annotation. Source: Ensembl

kinase binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein C-terminus binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8PubMed 16495340. Source: MGI

protein heterodimerization activity

Inferred from sequence alignment Ref.5. Source: MGI

protein homodimerization activity

Inferred from sequence alignment Ref.5. Source: MGI

protein kinase B binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase 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

transcription factor binding

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 233233B-cell lymphoma/leukemia 10
PRO_0000144075

Regions

Domain13 – 10189CARD

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1381Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z0H7 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: C0539BC97102DBB8

FASTA23325,948
        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 

« Hide

References

« Hide '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].
[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].
[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].
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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"BCL10 mediates lipopolysaccharide/toll-like receptor-4 signaling through interaction with Pellino2."
Liu Y., Dong W., Chen L., Xiang R., Xiao H., De G., Wang Z., Qi Y.
J. Biol. Chem. 279:37436-37444(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PELI2 AND SOCS3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS17897.1.
RefSeqNP_033870.1. NM_009740.2.
UniGeneMm.239141.

3D structure databases

ProteinModelPortalQ9Z0H7.
SMRQ9Z0H7. Positions 10-115.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198317. 12 interactions.
DIPDIP-60309N.
IntActQ9Z0H7. 1 interaction.

PTM databases

PhosphoSiteQ9Z0H7.

Proteomic databases

PaxDbQ9Z0H7.
PRIDEQ9Z0H7.

Protocols and materials databases

DNASU12042.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029842; ENSMUSP00000029842; ENSMUSG00000028191.
GeneID12042.
KEGGmmu:12042.
UCSCuc008rqs.1. mouse.

Organism-specific databases

CTD8915.
MGIMGI:1337994. Bcl10.

Phylogenomic databases

eggNOGNOG44778.
GeneTreeENSGT00490000043442.
HOGENOMHOG000008671.
HOVERGENHBG050680.
InParanoidQ9Z0H7.
KOK07368.
OMAGGTCGNS.
OrthoDBEOG79W97M.
PhylomeDBQ9Z0H7.
TreeFamTF328636.

Gene expression databases

ArrayExpressQ9Z0H7.
BgeeQ9Z0H7.
CleanExMM_BCL10.
GenevestigatorQ9Z0H7.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
InterProIPR001315. CARD.
IPR011029. DEATH-like_dom.
[Graphical view]
PfamPF00619. CARD. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS50209. CARD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio280309.
PROQ9Z0H7.
SOURCESearch...

Entry information

Entry nameBCL10_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot