Q8N163 (K1967_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DBIRD complex subunit KIAA1967

Alternative name(s):
Deleted in breast cancer gene 1 protein
Short name=DBC-1
Short name=DBC.1
p30 DBC

Gene names

Name:	KIAA1967
Synonyms:	DBC1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	923 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis. Inhibits SUV39H1 methyltransferase activity. Ref.9 Ref.10 Ref.12 Ref.18
Subunit structure	Component of the DBIRD complex. Interacts with ZNF326/ZIRD; the interaction is direct. Interacts (via N-terminus) with SIRT1. Interacts (via N-terminus) with SUV39H1; this interaction abolishes the interaction with SIRT1. Ref.9 Ref.10 Ref.12 Ref.18
Subcellular location	Nucleus Probable.
Tissue specificity	Expressed ubiquitously in normal tissues. Expressed in 84 to 100% of neoplastic breast, lung, and colon tissues. Ref.7
Sequence caution	The sequence AAG02472.1 differs from that shown. Reason: Frameshift at positions 610, 622, 794 and 810. The sequence BAB85553.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Apoptosis mRNA processing mRNA splicing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Molecular function	Metalloenzyme inhibitor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from mutant phenotype Ref.18. Source: UniProtKB apoptotic process Inferred from direct assay PubMed 15824730. Source: UniProtKB mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of apoptotic process Inferred from mutant phenotype Ref.9Ref.10. Source: UniProtKB regulation of DNA-dependent transcription, elongation Inferred from mutant phenotype Ref.18. Source: UniProtKB
Cellular_component	DBIRD complex Inferred from direct assay Ref.18. Source: UniProtKB mitochondrial matrix Inferred from direct assay PubMed 15824730. Source: UniProtKB nucleus Inferred from direct assay PubMed 15824730. Source: UniProtKB
Molecular_function	RNA polymerase II core binding Inferred from direct assay Ref.18. Source: UniProtKB enzyme inhibitor activity Inferred from direct assay Ref.9Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MYC	P01106	8	EBI-355410,EBI-447544
ORF	Q9Q2G4	5	EBI-355410,EBI-6248094	From a different organism.
SIRT1	Q96EB6	9	EBI-355410,EBI-1802965

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8N163-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8N163-2)

The sequence of this isoform differs from the canonical sequence as follows:
     910-923: ADSWVEKEEPAPSN → VRWGWTRRQHSSFP

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 923	923	DBIRD complex subunit KIAA1967		PRO_0000050813
Regions
	Coiled coil	829 – 909	81	Potential
Amino acid modifications
	Modified residue	35	1	Phosphothreonine Ref.13 Ref.15
	Modified residue	124	1	Phosphoserine Ref.11 Ref.15
	Modified residue	215	1	N6-acetyllysine Ref.14
	Modified residue	675	1	Phosphoserine Ref.8 Ref.11 Ref.13 Ref.15
	Modified residue	678	1	Phosphoserine Ref.8 Ref.11 Ref.13 Ref.15 Ref.17
	Modified residue	681	1	Phosphoserine Ref.8 Ref.11 Ref.13 Ref.15
Natural variations
	Alternative sequence	910 – 923	14	ADSWV…PAPSN → VRWGWTRRQHSSFP in isoform 2.		VSP_017092
Experimental info
	Mutagenesis	243 – 264	22	Missing: Abolishes binding to SIRT1. Ref.9
	Sequence conflict	47	1	R → S in CAD38866. Ref.2
	Sequence conflict	47	1	R → S in CAD39017. Ref.2
	Sequence conflict	850	1	T → S in AAH65495. Ref.5
	Sequence conflict	908	1	E → G in CAD38866. Ref.2
	Sequence conflict	908	1	E → G in CAD39017. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 24, 2006. Version 2. Checksum: 1733934377E35D21	FASTA	923	102,902
	10 20 30 40 50 60 MSQFKRQRIN PLPGGRNFSG TASTSLLGPP PGLLTPPVAT ELSQNARHLQ GGEKQRVFTG 70 80 90 100 110 120 IVTSLHDYFG VVDEEVFFQL SVVKGRLPQL GEKVLVKAAY NPGQAVPWNA VKVQTLSNQP 130 140 150 160 170 180 LLKSPAPPLL HVAALGQKQG ILGAQPQLIF QPHRIPPLFP QKPLSLFQTS HTLHLSHLNR 190 200 210 220 230 240 FPARGPHGRL DQGRSDDYDS KKRKQRAGGE PWGAKKPRHD LPPYRVHLTP YTVDSPICDF 250 260 270 280 290 300 LELQRRYRSL LVPSDFLSVH LSWLSAFPLS QPFSLHHPSR IQVSSEKEAA PDAGAEPITA 310 320 330 340 350 360 DSDPAYSSKV LLLSSPGLEE LYRCCMLFVD DMAEPRETPE HPLKQIKFLL GRKEEEAVLV 370 380 390 400 410 420 GGEWSPSLDG LDPQADPQVL VRTAIRCAQA QTGIDLSGCT KWWRFAEFQY LQPGPPRRLQ 430 440 450 460 470 480 TVVVYLPDVW TIMPTLEEWE ALCQQKAAEA APPTQEAQGE TEPTEQAPDA LEQAADTSRR 490 500 510 520 530 540 NAETPEATTQ QETDTDLPEA PPPPLEPAVI ARPGCVNLSL HGIVEDRRPK ERISFEVMVL 550 560 570 580 590 600 AELFLEMLQR DFGYRVYKML LSLPEKVVSP PEPEKEEAAK EEATKEEEAI KEEVVKEPKD 610 620 630 640 650 660 EAQNEGPATE SEAPLKEDGL LPKPLSSGGE EEEKPRGEAS EDLCEMALDP ELLLLRDDGE 670 680 690 700 710 720 EEFAGAKLED SEVRSVASNQ SEMEFSSLQD MPKELDPSAV LPLDCLLAFV FFDANWCGYL 730 740 750 760 770 780 HRRDLERILL TLGIRLSAEQ AKQLVSRVVT QNICQYRSLQ YSRQEGLDGG LPEEVLFGNL 790 800 810 820 830 840 DLLPPPGKST KPGAAPTEHK ALVSHNGSLI NVGSLLQRAE QQDSGRLYLE NKIHTLELKL 850 860 870 880 890 900 EESHNRFSAT EVTNKTLAAE MQELRVRLAE AEETARTAER QKSQLQRLLQ ELRRRLTPLQ 910 920 LEIQRVVEKA DSWVEKEEPA PSN
	Isoform 2 [UniParc]. Checksum: 3C1BB0DE06A20926	FASTA	923	103,143
	10 20 30 40 50 60 MSQFKRQRIN PLPGGRNFSG TASTSLLGPP PGLLTPPVAT ELSQNARHLQ GGEKQRVFTG 70 80 90 100 110 120 IVTSLHDYFG VVDEEVFFQL SVVKGRLPQL GEKVLVKAAY NPGQAVPWNA VKVQTLSNQP 130 140 150 160 170 180 LLKSPAPPLL HVAALGQKQG ILGAQPQLIF QPHRIPPLFP QKPLSLFQTS HTLHLSHLNR 190 200 210 220 230 240 FPARGPHGRL DQGRSDDYDS KKRKQRAGGE PWGAKKPRHD LPPYRVHLTP YTVDSPICDF 250 260 270 280 290 300 LELQRRYRSL LVPSDFLSVH LSWLSAFPLS QPFSLHHPSR IQVSSEKEAA PDAGAEPITA 310 320 330 340 350 360 DSDPAYSSKV LLLSSPGLEE LYRCCMLFVD DMAEPRETPE HPLKQIKFLL GRKEEEAVLV 370 380 390 400 410 420 GGEWSPSLDG LDPQADPQVL VRTAIRCAQA QTGIDLSGCT KWWRFAEFQY LQPGPPRRLQ 430 440 450 460 470 480 TVVVYLPDVW TIMPTLEEWE ALCQQKAAEA APPTQEAQGE TEPTEQAPDA LEQAADTSRR 490 500 510 520 530 540 NAETPEATTQ QETDTDLPEA PPPPLEPAVI ARPGCVNLSL HGIVEDRRPK ERISFEVMVL 550 560 570 580 590 600 AELFLEMLQR DFGYRVYKML LSLPEKVVSP PEPEKEEAAK EEATKEEEAI KEEVVKEPKD 610 620 630 640 650 660 EAQNEGPATE SEAPLKEDGL LPKPLSSGGE EEEKPRGEAS EDLCEMALDP ELLLLRDDGE 670 680 690 700 710 720 EEFAGAKLED SEVRSVASNQ SEMEFSSLQD MPKELDPSAV LPLDCLLAFV FFDANWCGYL 730 740 750 760 770 780 HRRDLERILL TLGIRLSAEQ AKQLVSRVVT QNICQYRSLQ YSRQEGLDGG LPEEVLFGNL 790 800 810 820 830 840 DLLPPPGKST KPGAAPTEHK ALVSHNGSLI NVGSLLQRAE QQDSGRLYLE NKIHTLELKL 850 860 870 880 890 900 EESHNRFSAT EVTNKTLAAE MQELRVRLAE AEETARTAER QKSQLQRLLQ ELRRRLTPLQ 910 920 LEIQRVVEKV RWGWTRRQHS SFP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Amygdala and Testis.
[3]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM 1). Tissue: Lymph and Placenta.
[6]	"Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins." Nagase T., Kikuno R., Ohara O. DNA Res. 8:319-327(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-923 (ISOFORM 2). Tissue: Brain.
[7]	"DBC2, a candidate for a tumor suppressor gene involved in breast cancer." Hamaguchi M., Meth J.L., von Klitzing C., Wei W., Esposito D., Rodgers L., Walsh T., Welcsh P., King M.C., Wigler M.H. Proc. Natl. Acad. Sci. U.S.A. 99:13647-13652(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 439-845, TISSUE SPECIFICITY.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675; SER-678 AND SER-681, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"DBC1 is a negative regulator of SIRT1." Kim J.-E., Chen J., Lou Z. Nature 451:583-586(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS SIRT1 INHIBITOR, INTERACTION WITH SIRT1, MUTAGENESIS OF 243-LEU--LEU-264, MASS SPECTROMETRY.
[10]	"Negative regulation of the deacetylase SIRT1 by DBC1." Zhao W., Kruse J.-P., Tang Y., Jung S.Y., Qin J., Gu W. Nature 451:587-590(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH SIRT1.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-675; SER-678 AND SER-681, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Inhibition of SUV39H1 methyltransferase activity by DBC1." Li Z., Chen L., Kabra N., Wang C., Fang J., Chen J. J. Biol. Chem. 284:10361-10366(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS SUV39H1 INHIBITOR, INTERACTION WITH SUV39H1.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35; SER-675; SER-678 AND SER-681, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215, MASS SPECTROMETRY.
[15]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35; SER-124; SER-675; SER-678 AND SER-681, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, MASS SPECTROMETRY.
[18]	"DBIRD complex integrates alternative mRNA splicing with RNA polymerase II transcript elongation." Close P., East P., Dirac-Svejstrup A.B., Hartmann H., Heron M., Maslen S., Chariot A., Soding J., Skehel M., Svejstrup J.Q. Nature 484:386-389(2012) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE DBIRD COMPLEX, FUNCTION, INTERACTION WITH KIAA1967.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK096547 mRNA. No translation available. AK314535 mRNA. Translation: BAG37126.1. AL834162 mRNA. Translation: CAD38866.1. AL834351 mRNA. Translation: CAD39016.1. AL834352 mRNA. Translation: CAD39017.1. BX640952 mRNA. Translation: CAE45976.1. AL137523 mRNA. Translation: CAB70788.3. AC037459 Genomic DNA. No translation available. CH471080 Genomic DNA. Translation: EAW63658.1. CH471080 Genomic DNA. Translation: EAW63661.1. BC018269 mRNA. Translation: AAH18269.2. BC065495 mRNA. Translation: AAH65495.1. AB075847 mRNA. Translation: BAB85553.1. Different initiation. AF293335 mRNA. Translation: AAG02472.1. Frameshift.
IPI	IPI00182757. IPI00873406.
PIR	T46368.
RefSeq	NP_066997.3. NM_021174.5.
UniGene	Hs.433722.
3D structure databases
ProteinModelPortal	Q8N163.
SMR	Q8N163. Positions 57-119.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-38122N.
IntAct	Q8N163. 27 interactions.
MINT	MINT-5003338.
PTM databases
PhosphoSite	Q8N163.
Polymorphism databases
DMDM	85701135.
Proteomic databases
PaxDb	Q8N163.
PRIDE	Q8N163.
Protocols and materials databases
DNASU	57805.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000308511; ENSP00000310670; ENSG00000158941. ENST00000389279; ENSP00000373930; ENSG00000158941.
GeneID	57805.
KEGG	hsa:57805.
UCSC	uc003xch.3. human. uc003xcj.1. human.
Organism-specific databases
CTD	57805.
GeneCards	GC08P022462.
HGNC	HGNC:23360. KIAA1967.
HPA	HPA019907. HPA019943.
MIM	607359. gene.
neXtProt	NX_Q8N163.
PharmGKB	PA134993792.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG307741.
HOVERGEN	HBG081843.
InParanoid	Q8N163.
OMA	MSQFKRQ.
OrthoDB	EOG4WH8K6.
Gene expression databases
ArrayExpress	Q8N163.
Bgee	Q8N163.
CleanEx	HS_DBC1.
Genevestigator	Q8N163.
GermOnline	ENSG00000158941. Homo sapiens.
Family and domain databases
InterPro	IPR025224. DBC1/CARP1. IPR025954. DBC1/CARP1_inactive_NUDIX_dom. IPR025223. S1-like_RNA-bd_dom. [Graphical view]
PANTHER	PTHR14304. PTHR14304. 1 hit.
Pfam	PF14443. DBC1. 1 hit. PF14444. S1-like. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	KIAA1967. human.
GenomeRNAi	57805.
NextBio	64756.
SOURCE	Search...

Entry information

Entry name

K1967_HUMAN

Accession

Primary (citable) accession number: Q8N163
Secondary accession number(s): A6NL03 , B2RB79, D3DSR6, Q6P0Q9, Q8N3G7, Q8N8M1, Q8TF34, Q9H9Q9, Q9HD12, Q9NT55

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.