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Q9QYN5 (BCL10_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
R-RCD1
Short name=RCD
Gene names
Name:Bcl10
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length233 AA.
Sequence statusComplete.
Protein existenceEvidence 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

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 By similarity. Interacts with TRAF2 and BIRC2/c-IAP2.

Subcellular location

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

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 processT cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

induction of apoptosis

Inferred from direct assay Ref.1. Source: RGD

innate immune response

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of mature B cell apoptosis

Inferred from sequence or structural similarity. Source: UniProtKB

neural tube closure

Inferred from sequence or structural similarity. 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 interleukin-8 biosynthetic process

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 sequence or structural similarity. Source: UniProtKB

response to molecule of bacterial origin

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

lysosome

Inferred from sequence or structural similarity. Source: UniProtKB

membrane raft

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionNF-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 233233B-cell lymphoma/leukemia 10
PRO_0000144076

Regions

Domain13 – 10189CARD

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9QYN5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: B43274B4B825FC7D

FASTA23325,999
        10         20         30         40         50         60 
MEAPAPSLTE EDLTEVKKDA LENLRVYLCE KIIAERHFDH LRAKKILSRE DTEEISCRTS 

        70         80         90        100        110        120 
SRKRAGKLLD YLQENPKGLD TLVESIRREK TQNFLIQKIT DEVLKLRNIK LEHLKGLKCS 

       130        140        150        160        170        180 
SCEPFAAGAT NNLSRSNSDE SNFSEKQRPS TVIYHPEGES STAPFFSTES SLNLPVLEVG 

       190        200        210        220        230 
RLENSSFSSA SLPRPGDPGA PPLPPDLRLE EGGSCGNSSE MFLPLRSRAL SRQ 

« Hide

References

« Hide 'large scale' references
[1]"Regulatory mechanisms of TRAF2-mediated signal transduction by Bcl10, a MALT lymphoma-associated protein."
Yoneda T., Imaizumi K., Maeda M., Yui D., Manabe T., Katayama T., Sato N., Gomi F., Morihara T., Mori Y., Miyoshi K., Hitomi J., Ugawa S., Yamada S., Okabe M., Tohyama M.
J. Biol. Chem. 275:11114-11120(2000) [PubMed: 10753917] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Embryonic brain.
[2]"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].
Tissue: Prostate.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB016069 mRNA. Translation: BAA88822.1.
BC061772 mRNA. Translation: AAH61772.1.
IPIIPI00214295.
RefSeqNP_112618.1. NM_031328.1.
UniGeneRn.13007.

3D structure databases

ProteinModelPortalQ9QYN5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9QYN5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID83477.
KEGGrno:83477.

Organism-specific databases

CTD8915.
RGD620544. Bcl10.

Phylogenomic databases

eggNOGroNOG16681.
GeneTreeENSGT00490000043442.
HOVERGENHBG050680.
OrthoDBEOG41JZD7.

Gene expression databases

ArrayExpressQ9QYN5.
GenevestigatorQ9QYN5.
GermOnlineENSRNOG00000014613. Rattus norvegicus.

Family and domain databases

InterProIPR001315. CARD.
IPR011029. DEATH-like.
[Graphical view]
Gene3DG3DSA:1.10.533.10. DEATH_like. 1 hit.
KOK07368.
PfamPF00619. CARD. 1 hit.
[Graphical view]
SUPFAMSSF47986. DEATH_like. 1 hit.
PROSITEPS50209. CARD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio615897.

Entry information

Entry nameBCL10_RAT
AccessionPrimary (citable) accession number: Q9QYN5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 1, 2000
Last modified: November 16, 2011
This is version 74 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