HUMAN:BCL10

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	BCL10 (synonyms: CIPER, CLAP)
Protein Name(s)	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
External Links
UniProt	O95999
EMBL	AJ006288 AF057700 AF100338 AF127386 AF134395 AF105066 AF082283 AF097732 AK291346 AL590113 CH471097 BC053617
CCDS	CCDS704.1
RefSeq	NP_003912.1
UniGene	Hs.193516
PDB	2MB9
PDBsum	2MB9
ProteinModelPortal	O95999
SMR	O95999
BioGrid	114429
DIP	DIP-29740N
IntAct	O95999
MINT	MINT-89139
STRING	9606.ENSP00000271015
PhosphoSite	O95999
MaxQB	O95999
PaxDb	O95999
PRIDE	O95999
DNASU	8915
Ensembl	ENST00000370580
GeneID	8915
KEGG	hsa:8915
UCSC	uc021opd.1
CTD	8915
GeneCards	GC01M085731
HGNC	HGNC:989
HPA	CAB001944 HPA017925
MIM	156240 603517
neXtProt	NX_O95999
PharmGKB	PA25299
eggNOG	NOG44778
GeneTree	ENSGT00490000043442
HOGENOM	HOG000008671
HOVERGEN	HBG050680
InParanoid	O95999
KO	K07368
OMA	PYLCDKI
OrthoDB	EOG79W97M
PhylomeDB	O95999
TreeFam	TF328636
Reactome	REACT_118656 REACT_12555 REACT_163994
SignaLink	O95999
ChiTaRS	BCL10
GeneWiki	BCL10
GenomeRNAi	8915
NextBio	33536
PRO	PR:O95999
Proteomes	UP000005640
Bgee	O95999
CleanEx	HS_BCL10
Genevestigator	O95999
GO	GO:0032449 GO:0005737 GO:0005881 GO:0005829 GO:0001772 GO:0005764 GO:0045121 GO:0005634 GO:0048471 GO:0005886 GO:0043234 GO:0019899 GO:0019900 GO:0051059 GO:0002020 GO:0008022 GO:0043422 GO:0019901 GO:0043621 GO:0003713 GO:0008134 GO:0043130 GO:0031625 GO:0002250 GO:0001783 GO:0008219 GO:0006968 GO:0071260 GO:0038095 GO:0016064 GO:0045087 GO:0042226 GO:0042109 GO:0002906 GO:0001843 GO:0043280 GO:2001238 GO:0043123 GO:0045416 GO:0032765 GO:0051092 GO:0042327 GO:0031398 GO:0050870 GO:0045893 GO:0051260 GO:0051259 GO:0050856 GO:0032094 GO:0009620 GO:0002237 GO:0070231 GO:0050852 GO:0002224
Gene3D	1.10.533.10
InterPro	IPR001315 IPR011029
Pfam	PF00619
SUPFAM	SSF47986
PROSITE	PS50209

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:11821383^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0032449	CBM complex	PMID:28628108^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:16831874^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:11238466^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002250	adaptive immune response	PMID:25365219^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0050700	CARD domain binding	PMID:12154360^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9BXL7	F	happens_during:(GO:0042110)	Seeded From UniProt	complete
enables	GO:0002020	protease binding	PMID:18223652^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9UDY8	F		Seeded From UniProt	complete
involved_in	GO:2001238	positive regulation of extrinsic apoptotic signaling pathway	PMID:11466612^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071260	cellular response to mechanical stimulus	PMID:19593445^[9]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:16831874^[3]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9Z0H7	P		Seeded From UniProt	complete
involved_in	GO:0051259	protein complex oligomerization	PMID:14695475^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9UDY8	P		Seeded From UniProt	complete
involved_in	GO:0051092	positive regulation of NF-kappaB transcription factor activity	PMID:10400625^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051092	positive regulation of NF-kappaB transcription factor activity	PMID:14695475^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051059	NF-kappaB binding	PMID:16280327^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0050852	T cell receptor signaling pathway	PMID:15125833^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:16127295^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0031663	lipopolysaccharide-mediated signaling pathway	PMID:16831874^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:15207693^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045416	positive regulation of interleukin-8 biosynthetic process	PMID:17095757^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	PMID:16831874^[3]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0043621	protein self-association	PMID:15125833^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O95999	F		Seeded From UniProt	complete
enables	GO:0043422	protein kinase B binding	PMID:16280327^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P31749	F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:14695475^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:16280327^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0043123	positive regulation of I-kappaB kinase/NF-kappaB signaling	PMID:12761501^[17]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042327	positive regulation of phosphorylation	PMID:15125833^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042226	interleukin-6 biosynthetic process	PMID:16647297^[18]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042109	lymphotoxin A biosynthetic process	PMID:16647297^[18]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032765	positive regulation of mast cell cytokine production	PMID:16647297^[18]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0032449	CBM complex	PMID:15125833^[13]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0032094	response to food	PMID:17095757^[16]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(CHEBI:37167) occurs_in:(CL:0011108)	Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:16395405^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13489	F		Seeded From UniProt	complete
involved_in	GO:0031398	positive regulation of protein ubiquitination	PMID:14695475^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:17052756^[20]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0019900	kinase binding	PMID:16831874^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P51617-1	F	happens_during:(GO:0071222)	Seeded From UniProt	complete
enables	GO:0019900	kinase binding	PMID:17052756^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9UQM7	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:14695475^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P61088	F		Seeded From UniProt	complete
contributes_to	GO:0019209	kinase activator activity	PMID:15125833^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0008219	cell death	PMID:10400625^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:15207693^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q00403	F		Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	PMID:11053425^[21]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9H257	F		Seeded From UniProt	complete
part_of	GO:0005881	cytoplasmic microtubule	PMID:23264731^[22]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:12154360^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:15082780^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:15082780^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:11021819^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:11053425^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:11278692^[25]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:16280327^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:15207693^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0002906	negative regulation of mature B cell apoptotic process	PMID:15878976^[26]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0002237	response to molecule of bacterial origin	PMID:16831874^[3]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0002224	toll-like receptor signaling pathway	PMID:16831874^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0001843	neural tube closure	PMID:11163238^[27]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9Z0H7	P		Seeded From UniProt	complete
involved_in	GO:2001238	positive regulation of extrinsic apoptotic signaling pathway	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1337994 PANTHER:PTN002858499 UniProtKB:O95999	P		Seeded From UniProt	complete
enables	GO:0051059	NF-kappaB binding	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002858499 UniProtKB:O95999	F		Seeded From UniProt	complete
enables	GO:0043422	protein kinase B binding	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002858499 UniProtKB:O95999	F		Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002858499 RGD:620544 UniProtKB:O95999	P		Seeded From UniProt	complete
part_of	GO:0032449	CBM complex	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002858499 UniProtKB:O95999	C		Seeded From UniProt	complete
contributes_to	GO:0019209	kinase activator activity	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002858499 UniProtKB:O95999	F		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002858499 UniProtKB:O95999	F		Seeded From UniProt	complete
involved_in	GO:0007249	I-kappaB kinase/NF-kappaB signaling	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1337994 PANTHER:PTN002858499	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1337994 PANTHER:PTN002858499 RGD:620544 UniProtKB:O95999	C		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002858499 UniProtKB:O95999	F		Seeded From UniProt	complete
involved_in	GO:0002250	adaptive immune response	PMID:21873635^[28]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002858499 UniProtKB:O95999	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25416956^[29]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O95999	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:10187771^[30]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O95999	F		Seeded From UniProt	complete
involved_in	GO:0033674	positive regulation of kinase activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0019209	P		Seeded From UniProt	complete
involved_in	GO:0033674	positive regulation of kinase activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0019209	P		Seeded From UniProt	complete
involved_in	GO:0051291	protein heterooligomerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9QYN5 ensembl:ENSRNOP00000019911	P		Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9QYN5 ensembl:ENSRNOP00000019911	P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9QYN5 ensembl:ENSRNOP00000019911	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9QYN5 ensembl:ENSRNOP00000019911	C		Seeded From UniProt	complete
involved_in	GO:2001238	positive regulation of extrinsic apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	P		Seeded From UniProt	complete
involved_in	GO:0070231	T cell apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	P		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	P		Seeded From UniProt	complete
involved_in	GO:0051092	positive regulation of NF-kappaB transcription factor activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	P		Seeded From UniProt	complete
involved_in	GO:0050870	positive regulation of T cell activation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	P		Seeded From UniProt	complete
involved_in	GO:0050856	regulation of T cell receptor signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	P		Seeded From UniProt	complete
part_of	GO:0045121	membrane raft	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	C		Seeded From UniProt	complete
involved_in	GO:0043280	positive regulation of cysteine-type endopeptidase activity involved in apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	P		Seeded From UniProt	complete
involved_in	GO:0016064	immunoglobulin mediated immune response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	P		Seeded From UniProt	complete
involved_in	GO:0009620	response to fungus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	P		Seeded From UniProt	complete
involved_in	GO:0007249	I-kappaB kinase/NF-kappaB signaling	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	P		Seeded From UniProt	complete
involved_in	GO:0006968	cellular defense response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	C		Seeded From UniProt	complete
involved_in	GO:0001843	neural tube closure	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	P		Seeded From UniProt	complete
involved_in	GO:0001783	B cell apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	P		Seeded From UniProt	complete
part_of	GO:0001772	immunological synapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9Z0H7 ensembl:ENSMUSP00000029842	C		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR033238	P		Seeded From UniProt	complete
involved_in	GO:0042981	regulation of apoptotic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001315	P		Seeded From UniProt	complete
involved_in	GO:0051092	positive regulation of NF-kappaB transcription factor activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR033238	P		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:16831874^[3]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0002250	adaptive immune response	PMID:16831874^[3]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050852	T cell receptor signaling pathway	Reactome:R-HSA-202403	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0038095	Fc-epsilon receptor signaling pathway	Reactome:R-HSA-2454202	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	Reactome:R-HSA-8866654	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-8939335 Reactome:R-HSA-8939323 Reactome:R-HSA-5607759 Reactome:R-HSA-5607757 Reactome:R-HSA-5607756 Reactome:R-HSA-5607751 Reactome:R-HSA-5607747 Reactome:R-HSA-5607744 Reactome:R-HSA-5607742 Reactome:R-HSA-5607737 Reactome:R-HSA-5607736 Reactome:R-HSA-5607733 Reactome:R-HSA-5607732 Reactome:R-HSA-2730904 Reactome:R-HSA-2730903 Reactome:R-HSA-2730900 Reactome:R-HSA-2730899 Reactome:R-HSA-2730876 Reactome:R-HSA-2730864 Reactome:R-HSA-2730861 Reactome:R-HSA-202534 Reactome:R-HSA-202510 Reactome:R-HSA-202500 Reactome:R-HSA-202489 Reactome:R-HSA-202478 Reactome:R-HSA-202472 Reactome:R-HSA-202466 Reactome:R-HSA-202459 Reactome:R-HSA-202453 Reactome:R-HSA-1168644	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002223	stimulatory C-type lectin receptor signaling pathway	Reactome:R-HSA-5621481	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0053	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
involved_in	GO:0002376	immune system process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0391	P		Seeded From UniProt	complete
part_of	GO:0045121	membrane raft	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0370	C		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0198	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Razmara, M et al. (2002) CARD-8 protein, a new CARD family member that regulates caspase-1 activation and apoptosis. J. Biol. Chem. 277 13952-8 PubMed GONUTS page
↑ Ma, CA et al. (2017) Germline hypomorphic CARD11 mutations in severe atopic disease. Nat. Genet. 49 1192-1201 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 ^3.8 Dong, W et al. (2006) The IRAK-1-BCL10-MALT1-TRAF6-TAK1 cascade mediates signaling to NF-kappaB from Toll-like receptor 4. J. Biol. Chem. 281 26029-40 PubMed GONUTS page
↑ Thome, M et al. (2001) Equine herpesvirus protein E10 induces membrane recruitment and phosphorylation of its cellular homologue, bcl-10. J. Cell Biol. 152 1115-22 PubMed GONUTS page
↑ Torres, JM et al. (2014) Inherited BCL10 deficiency impairs hematopoietic and nonhematopoietic immunity. J. Clin. Invest. 124 5239-48 PubMed GONUTS page
↑ ^6.0 ^6.1 Gaide, O et al. (2002) CARMA1 is a critical lipid raft-associated regulator of TCR-induced NF-kappa B activation. Nat. Immunol. 3 836-43 PubMed GONUTS page
↑ Coornaert, B et al. (2008) T cell antigen receptor stimulation induces MALT1 paracaspase-mediated cleavage of the NF-kappaB inhibitor A20. Nat. Immunol. 9 263-71 PubMed GONUTS page
↑ Yui, D et al. (2001) Interchangeable binding of Bcl10 to TRAF2 and cIAPs regulates apoptosis signaling. Oncogene 20 4317-23 PubMed GONUTS page
↑ Smith, AJ et al. (2009) Expression of the Bcl-2 protein BAD promotes prostate cancer growth. PLoS ONE 4 e6224 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 Zhou, H et al. (2004) Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO. Nature 427 167-71 PubMed GONUTS page
↑ ^11.0 ^11.1 Costanzo, A et al. (1999) 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 20127-32 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 Yeh, PY et al. (2006) A pathway for tumor necrosis factor-alpha-induced Bcl10 nuclear translocation. Bcl10 is up-regulated by NF-kappaB and phosphorylated by Akt1 and then complexes with Bcl3 to enter the nucleus. J. Biol. Chem. 281 167-75 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 ^13.4 Sun, L et al. (2004) The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes. Mol. Cell 14 289-301 PubMed GONUTS page
↑ Nakamura, K et al. (2005) Accumulation of BCL10 at the perinuclear region is required for the BCL10-mediated nuclear factor-kappa B activation. Pathobiology 72 191-202 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 Liu, Y et al. (2004) Characterization of Bcl10 as a potential transcriptional activator that interacts with general transcription factor TFIIB. Biochem. Biophys. Res. Commun. 320 1-6 PubMed GONUTS page
↑ ^16.0 ^16.1 Borthakur, A et al. (2007) Carrageenan induces interleukin-8 production through distinct Bcl10 pathway in normal human colonic epithelial cells. Am. J. Physiol. Gastrointest. Liver Physiol. 292 G829-38 PubMed GONUTS page
↑ Matsuda, A et al. (2003) Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene 22 3307-18 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 Rivera, J (2006) Adaptors discriminate mast-cell cytokine production from eicosanoid production and degranulation. Trends Immunol. 27 251-3 PubMed GONUTS page
↑ Hu, S et al. (2006) cIAP2 is a ubiquitin protein ligase for BCL10 and is dysregulated in mucosa-associated lymphoid tissue lymphomas. J. Clin. Invest. 116 174-81 PubMed GONUTS page
↑ ^20.0 ^20.1 Ishiguro, K et al. (2007) Bcl10 is phosphorylated on Ser138 by Ca2+/calmodulin-dependent protein kinase II. Mol. Immunol. 44 2095-100 PubMed GONUTS page
↑ ^21.0 ^21.1 Bertin, J et al. (2000) CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B. J. Biol. Chem. 275 41082-6 PubMed GONUTS page
↑ Fong, KW et al. (2013) MTR120/KIAA1383, a novel microtubule-associated protein, promotes microtubule stability and ensures cytokinesis. J. Cell. Sci. 126 825-37 PubMed GONUTS page
↑ ^23.0 ^23.1 Scharschmidt, E et al. (2004) Degradation of Bcl10 induced by T-cell activation negatively regulates NF-kappa B signaling. Mol. Cell. Biol. 24 3860-73 PubMed GONUTS page
↑ Ye, H et al. (2000) BCL10 expression in normal and neoplastic lymphoid tissue. Nuclear localization in MALT lymphoma. Am. J. Pathol. 157 1147-54 PubMed GONUTS page
↑ Bertin, J et al. (2001) CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B. J. Biol. Chem. 276 11877-82 PubMed GONUTS page
↑ Tian, MT et al. (2005) Bcl10 can promote survival of antigen-stimulated B lymphocytes. Blood 106 2105-12 PubMed GONUTS page
↑ Ruland, J et al. (2001) Bcl10 is a positive regulator of antigen receptor-induced activation of NF-kappaB and neural tube closure. Cell 104 33-42 PubMed GONUTS page
↑ ^28.00 ^28.01 ^28.02 ^28.03 ^28.04 ^28.05 ^28.06 ^28.07 ^28.08 ^28.09 ^28.10 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Rolland, T et al. (2014) A proteome-scale map of the human interactome network. Cell 159 1212-26 PubMed GONUTS page
↑ Thome, M et al. (1999) 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 9962-8 PubMed GONUTS page

[PMID:11821383-1] Razmara, M et al. (2002) CARD-8 protein, a new CARD family member that regulates caspase-1 activation and apoptosis. J. Biol. Chem. 277 13952-8 PubMed GONUTS page

[PMID:28628108-2] Ma, CA et al. (2017) Germline hypomorphic CARD11 mutations in severe atopic disease. Nat. Genet. 49 1192-1201 PubMed GONUTS page

[PMID:16831874-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 ^3.8 Dong, W et al. (2006) The IRAK-1-BCL10-MALT1-TRAF6-TAK1 cascade mediates signaling to NF-kappaB from Toll-like receptor 4. J. Biol. Chem. 281 26029-40 PubMed GONUTS page

[PMID:11238466-4] Thome, M et al. (2001) Equine herpesvirus protein E10 induces membrane recruitment and phosphorylation of its cellular homologue, bcl-10. J. Cell Biol. 152 1115-22 PubMed GONUTS page

[PMID:25365219-5] Torres, JM et al. (2014) Inherited BCL10 deficiency impairs hematopoietic and nonhematopoietic immunity. J. Clin. Invest. 124 5239-48 PubMed GONUTS page

[PMID:12154360-6] 6.0 ^6.1 Gaide, O et al. (2002) CARMA1 is a critical lipid raft-associated regulator of TCR-induced NF-kappa B activation. Nat. Immunol. 3 836-43 PubMed GONUTS page

[PMID:18223652-7] Coornaert, B et al. (2008) T cell antigen receptor stimulation induces MALT1 paracaspase-mediated cleavage of the NF-kappaB inhibitor A20. Nat. Immunol. 9 263-71 PubMed GONUTS page

[PMID:11466612-8] Yui, D et al. (2001) Interchangeable binding of Bcl10 to TRAF2 and cIAPs regulates apoptosis signaling. Oncogene 20 4317-23 PubMed GONUTS page

[PMID:19593445-9] Smith, AJ et al. (2009) Expression of the Bcl-2 protein BAD promotes prostate cancer growth. PLoS ONE 4 e6224 PubMed GONUTS page

[PMID:14695475-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 Zhou, H et al. (2004) Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO. Nature 427 167-71 PubMed GONUTS page

[PMID:10400625-11] 11.0 ^11.1 Costanzo, A et al. (1999) 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 20127-32 PubMed GONUTS page

[PMID:16280327-12] 12.0 ^12.1 ^12.2 ^12.3 Yeh, PY et al. (2006) A pathway for tumor necrosis factor-alpha-induced Bcl10 nuclear translocation. Bcl10 is up-regulated by NF-kappaB and phosphorylated by Akt1 and then complexes with Bcl3 to enter the nucleus. J. Biol. Chem. 281 167-75 PubMed GONUTS page

[PMID:15125833-13] 13.0 ^13.1 ^13.2 ^13.3 ^13.4 Sun, L et al. (2004) The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes. Mol. Cell 14 289-301 PubMed GONUTS page

[PMID:16127295-14] Nakamura, K et al. (2005) Accumulation of BCL10 at the perinuclear region is required for the BCL10-mediated nuclear factor-kappa B activation. Pathobiology 72 191-202 PubMed GONUTS page

[PMID:15207693-15] 15.0 ^15.1 ^15.2 Liu, Y et al. (2004) Characterization of Bcl10 as a potential transcriptional activator that interacts with general transcription factor TFIIB. Biochem. Biophys. Res. Commun. 320 1-6 PubMed GONUTS page

[PMID:17095757-16] 16.0 ^16.1 Borthakur, A et al. (2007) Carrageenan induces interleukin-8 production through distinct Bcl10 pathway in normal human colonic epithelial cells. Am. J. Physiol. Gastrointest. Liver Physiol. 292 G829-38 PubMed GONUTS page

[PMID:12761501-17] Matsuda, A et al. (2003) Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene 22 3307-18 PubMed GONUTS page

[PMID:16647297-18] 18.0 ^18.1 ^18.2 Rivera, J (2006) Adaptors discriminate mast-cell cytokine production from eicosanoid production and degranulation. Trends Immunol. 27 251-3 PubMed GONUTS page

[PMID:16395405-19] Hu, S et al. (2006) cIAP2 is a ubiquitin protein ligase for BCL10 and is dysregulated in mucosa-associated lymphoid tissue lymphomas. J. Clin. Invest. 116 174-81 PubMed GONUTS page

[PMID:17052756-20] 20.0 ^20.1 Ishiguro, K et al. (2007) Bcl10 is phosphorylated on Ser138 by Ca2+/calmodulin-dependent protein kinase II. Mol. Immunol. 44 2095-100 PubMed GONUTS page

[PMID:11053425-21] 21.0 ^21.1 Bertin, J et al. (2000) CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B. J. Biol. Chem. 275 41082-6 PubMed GONUTS page

[PMID:23264731-22] Fong, KW et al. (2013) MTR120/KIAA1383, a novel microtubule-associated protein, promotes microtubule stability and ensures cytokinesis. J. Cell. Sci. 126 825-37 PubMed GONUTS page

[PMID:15082780-23] 23.0 ^23.1 Scharschmidt, E et al. (2004) Degradation of Bcl10 induced by T-cell activation negatively regulates NF-kappa B signaling. Mol. Cell. Biol. 24 3860-73 PubMed GONUTS page

[PMID:11021819-24] Ye, H et al. (2000) BCL10 expression in normal and neoplastic lymphoid tissue. Nuclear localization in MALT lymphoma. Am. J. Pathol. 157 1147-54 PubMed GONUTS page

[PMID:11278692-25] Bertin, J et al. (2001) CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B. J. Biol. Chem. 276 11877-82 PubMed GONUTS page

[PMID:15878976-26] Tian, MT et al. (2005) Bcl10 can promote survival of antigen-stimulated B lymphocytes. Blood 106 2105-12 PubMed GONUTS page

[PMID:11163238-27] Ruland, J et al. (2001) Bcl10 is a positive regulator of antigen receptor-induced activation of NF-kappaB and neural tube closure. Cell 104 33-42 PubMed GONUTS page

[PMID:21873635-28] 28.00 ^28.01 ^28.02 ^28.03 ^28.04 ^28.05 ^28.06 ^28.07 ^28.08 ^28.09 ^28.10 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:25416956-29] Rolland, T et al. (2014) A proteome-scale map of the human interactome network. Cell 159 1212-26 PubMed GONUTS page

[PMID:10187771-30] Thome, M et al. (1999) 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 9962-8 PubMed GONUTS page

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