HUMAN:K1967

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	KIAA1967 (synonyms: DBC1)
Protein Name(s)	DBIRD complex subunit KIAA1967 Deleted in breast cancer gene 1 protein DBC-1 DBC.1 p30 DBC
External Links
UniProt	Q8N163
EMBL	AK096547 AK314535 AL834162 AL834351 AL834352 BX640952 AL137523 AC037459 CH471080 CH471080 BC018269 BC065495 AB075847 AF293335
IPI	IPI00182757 IPI00873406
PIR	T46368
RefSeq	NP_066997.3
UniGene	Hs.744848
ProteinModelPortal	Q8N163
SMR	Q8N163
DIP	DIP-38122N
IntAct	Q8N163
MINT	MINT-5003338
PhosphoSite	Q8N163
DMDM	85701135
PaxDb	Q8N163
PRIDE	Q8N163
DNASU	57805
Ensembl	ENST00000308511 ENST00000389279
GeneID	57805
KEGG	hsa:57805
UCSC	uc003xch.3
CTD	57805
GeneCards	GC08P022462
HGNC	HGNC:23360
HPA	HPA019907 HPA019943
MIM	607359
neXtProt	NX_Q8N163
PharmGKB	PA134993792
eggNOG	NOG307741
HOVERGEN	HBG081843
InParanoid	Q8N163
OMA	MSQFKRQ
OrthoDB	EOG4WH8K6
ChiTaRS	KIAA1967
GeneWiki	KIAA1967
GenomeRNAi	57805
NextBio	64756
ArrayExpress	Q8N163
Bgee	Q8N163
CleanEx	HS_DBC1
Genevestigator	Q8N163
GO	GO:0044609 GO:0005759 GO:0005634 GO:0004857 GO:0000993 GO:0043653 GO:0006397 GO:0043065 GO:0032784 GO:0008380
InterPro	IPR025224 IPR025954 IPR025223
PANTHER	PTHR14304
Pfam	PF14443 PF14444

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0090311	regulation of protein deacetylation	PMID:21030595^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:20160719^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:20160719^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:20160719^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0030308	negative regulation of cell growth	PMID:25661920^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:25661920^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:25661920^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0043086	negative regulation of catalytic activity	PMID:21030595^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:20074560^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:20074560^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:24824780^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:24824780^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0090263	positive regulation of canonical Wnt signaling pathway	PMID:24824780^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042752	regulation of circadian rhythm	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8VDP4	P	Seeded From UniProt	complete
involved_in	GO:0032435	negative regulation of proteasomal ubiquitin-dependent protein catabolic process	PMID:23398316^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0031647	regulation of protein stability	PMID:23398316^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:23382074^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q96EB6	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000054	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:2000003	positive regulation of DNA damage checkpoint	PMID:23352644^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:1902230	negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage	PMID:23352644^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22681889^[9]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[10]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0044609	DBIRD complex	PMID:22446626^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0043653	mitochondrial fragmentation involved in apoptotic process	PMID:15824730^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:18235502^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:18235501^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032784	regulation of DNA-templated transcription, elongation	PMID:22446626^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:18235501^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q96EB6	F	Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:19218236^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O43463	F	Seeded From UniProt	complete
involved_in	GO:0009411	response to UV	PMID:23352644^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0008380	RNA splicing	PMID:22446626^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	PMID:15824730^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:15824730^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15824730^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004857	enzyme inhibitor activity	PMID:19218236^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion	UniProtKB:O43463	F	Seeded From UniProt	complete
enables	GO:0004857	enzyme inhibitor activity	PMID:18235502^[13]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004857	enzyme inhibitor activity	PMID:18235501^[14]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000993	RNA polymerase II complex binding	PMID:22446626^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0000790	nuclear chromatin	PMID:23352644^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0044609	DBIRD complex	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002682436 UniProtKB:Q8N163	C	Seeded From UniProt	complete
enables	GO:0030374	nuclear receptor transcription coactivator activity	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000370966 UniProtKB:Q8IX12	F	Seeded From UniProt	complete
involved_in	GO:0008380	RNA splicing	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002682436 UniProtKB:Q8N163	P	Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000370966 TAIR:locus:2056881	P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000370966 TAIR:locus:2056881 UniProtKB:Q8N163	C	Seeded From UniProt	complete
enables	GO:0000993	RNA polymerase II complex binding	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002682436 UniProtKB:Q8N163	F	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:1903508	positive regulation of nucleic acid-templated transcription	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0030374	P	Seeded From UniProt	complete
involved_in	GO:0043086	negative regulation of catalytic activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VDP4 ensembl:ENSMUSP00000036924	P	Seeded From UniProt	complete
involved_in	GO:0042752	regulation of circadian rhythm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VDP4 ensembl:ENSMUSP00000036924	P	Seeded From UniProt	complete
enables	GO:0004857	enzyme inhibitor activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VDP4 ensembl:ENSMUSP00000036924	F	Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR025224	P	Seeded From UniProt	complete
involved_in	GO:0008380	RNA splicing	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR028811	P	Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR028811	P	Seeded From UniProt	complete
part_of	GO:0044609	DBIRD complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR028811	C	Seeded From UniProt	complete
involved_in	GO:1900034	regulation of cellular response to heat	Reactome:R-HSA-3371453	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-3371567 Reactome:R-HSA-3371537	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0007049	cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0131	P	Seeded From UniProt	complete
enables	GO:0004857	enzyme inhibitor activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0481	F	Seeded From UniProt	complete
involved_in	GO:0006397	mRNA processing	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0507	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
involved_in	GO:0048511	rhythmic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0090	P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
involved_in	GO:0016055	Wnt signaling pathway	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0879	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
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P	Seeded From UniProt	complete
involved_in	GO:0008380	RNA splicing	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0508	P	Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 Chini, CC et al. (2010) HDAC3 is negatively regulated by the nuclear protein DBC1. J. Biol. Chem. 285 40830-7 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Hiraike, H et al. (2010) Identification of DBC1 as a transcriptional repressor for BRCA1. Br. J. Cancer 102 1061-7 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Sakurabashi, A et al. (2015) CCAR2 negatively regulates nuclear receptor LXRα by competing with SIRT1 deacetylase. J. Steroid Biochem. Mol. Biol. 149 80-8 PubMed GONUTS page
↑ ^4.0 ^4.1 Koyama, S et al. (2010) Repression of estrogen receptor beta function by putative tumor suppressor DBC1. Biochem. Biophys. Res. Commun. 392 357-62 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Pangon, L et al. (2015) MCC inhibits beta-catenin transcriptional activity by sequestering DBC1 in the cytoplasm. Int. J. Cancer 136 55-64 PubMed GONUTS page
↑ ^6.0 ^6.1 Chini, CC et al. (2013) DBC1 (Deleted in Breast Cancer 1) modulates the stability and function of the nuclear receptor Rev-erbα. Biochem. J. 451 453-61 PubMed GONUTS page
↑ Armour, SM et al. (2013) A high-confidence interaction map identifies SIRT1 as a mediator of acetylation of USP22 and the SAGA coactivator complex. Mol. Cell. Biol. 33 1487-502 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Kim, W & Kim, JE (2013) Deleted in breast cancer 1 (DBC1) deficiency results in apoptosis of breast cancer cells through impaired responses to UV-induced DNA damage. Cancer Lett. 333 180-6 PubMed GONUTS page
↑ Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
↑ Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 Close, P et al. (2012) DBIRD complex integrates alternative mRNA splicing with RNA polymerase II transcript elongation. Nature 484 386-9 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 Sundararajan, R et al. (2005) Caspase-dependent processing activates the proapoptotic activity of deleted in breast cancer-1 during tumor necrosis factor-alpha-mediated death signaling. Oncogene 24 4908-20 PubMed GONUTS page
↑ ^13.0 ^13.1 Zhao, W et al. (2008) Negative regulation of the deacetylase SIRT1 by DBC1. Nature 451 587-90 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 Kim, JE et al. (2008) DBC1 is a negative regulator of SIRT1. Nature 451 583-6 PubMed GONUTS page
↑ ^15.0 ^15.1 Li, Z et al. (2009) Inhibition of SUV39H1 methyltransferase activity by DBC1. J. Biol. Chem. 284 10361-6 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 ^16.4 ^16.5 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:21030595-1] 1.0 ^1.1 Chini, CC et al. (2010) HDAC3 is negatively regulated by the nuclear protein DBC1. J. Biol. Chem. 285 40830-7 PubMed GONUTS page

[PMID:20160719-2] 2.0 ^2.1 ^2.2 Hiraike, H et al. (2010) Identification of DBC1 as a transcriptional repressor for BRCA1. Br. J. Cancer 102 1061-7 PubMed GONUTS page

[PMID:25661920-3] 3.0 ^3.1 ^3.2 Sakurabashi, A et al. (2015) CCAR2 negatively regulates nuclear receptor LXRα by competing with SIRT1 deacetylase. J. Steroid Biochem. Mol. Biol. 149 80-8 PubMed GONUTS page

[PMID:20074560-4] 4.0 ^4.1 Koyama, S et al. (2010) Repression of estrogen receptor beta function by putative tumor suppressor DBC1. Biochem. Biophys. Res. Commun. 392 357-62 PubMed GONUTS page

[PMID:24824780-5] 5.0 ^5.1 ^5.2 Pangon, L et al. (2015) MCC inhibits beta-catenin transcriptional activity by sequestering DBC1 in the cytoplasm. Int. J. Cancer 136 55-64 PubMed GONUTS page

[PMID:23398316-6] 6.0 ^6.1 Chini, CC et al. (2013) DBC1 (Deleted in Breast Cancer 1) modulates the stability and function of the nuclear receptor Rev-erbα. Biochem. J. 451 453-61 PubMed GONUTS page

[PMID:23382074-7] Armour, SM et al. (2013) A high-confidence interaction map identifies SIRT1 as a mediator of acetylation of USP22 and the SAGA coactivator complex. Mol. Cell. Biol. 33 1487-502 PubMed GONUTS page

[PMID:23352644-8] 8.0 ^8.1 ^8.2 ^8.3 Kim, W & Kim, JE (2013) Deleted in breast cancer 1 (DBC1) deficiency results in apoptosis of breast cancer cells through impaired responses to UV-induced DNA damage. Cancer Lett. 333 180-6 PubMed GONUTS page

[PMID:22681889-9] Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page

[PMID:22658674-10] Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page

[PMID:22446626-11] 11.0 ^11.1 ^11.2 ^11.3 Close, P et al. (2012) DBIRD complex integrates alternative mRNA splicing with RNA polymerase II transcript elongation. Nature 484 386-9 PubMed GONUTS page

[PMID:15824730-12] 12.0 ^12.1 ^12.2 ^12.3 Sundararajan, R et al. (2005) Caspase-dependent processing activates the proapoptotic activity of deleted in breast cancer-1 during tumor necrosis factor-alpha-mediated death signaling. Oncogene 24 4908-20 PubMed GONUTS page

[PMID:18235502-13] 13.0 ^13.1 Zhao, W et al. (2008) Negative regulation of the deacetylase SIRT1 by DBC1. Nature 451 587-90 PubMed GONUTS page

[PMID:18235501-14] 14.0 ^14.1 ^14.2 Kim, JE et al. (2008) DBC1 is a negative regulator of SIRT1. Nature 451 583-6 PubMed GONUTS page

[PMID:19218236-15] 15.0 ^15.1 Li, Z et al. (2009) Inhibition of SUV39H1 methyltransferase activity by DBC1. J. Biol. Chem. 284 10361-6 PubMed GONUTS page

[PMID:21873635-16] 16.0 ^16.1 ^16.2 ^16.3 ^16.4 ^16.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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HUMAN:K1967

Contents

Annotations

Notes

References

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