Q8VDP4 (K1967_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: DBIRD complex subunit KIAA1967 homolog
Organism	Mus musculus (Mouse) [Reference proteome]
Taxonomic identifier	10090 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	922 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 By similarity. Inhibits SUV39H1 methyltransferase activity. Ref.7
Subunit structure	Component of the DBIRD complex. Interacts with ZNF326/ZIRD; the interaction is direct. Interacts (via N-terminus) with SIRT1 By similarity. Interacts (via N-terminus) with SIRT1 By similarity. Interacts (via N-terminus) with SUV39H1; this interaction abolishes the interaction with SIRT1. Ref.7
Subcellular location	Nucleus By similarity.
Sequence caution	The sequence BAC27420.1 differs from that shown. Reason: Erroneous initiation. The sequence BAC34139.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Apoptosis mRNA processing mRNA splicing
Cellular component	Nucleus
Domain	Coiled coil
Molecular function	Metalloenzyme inhibitor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from sequence or structural similarity. Source: UniProtKB apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB regulation of DNA-dependent transcription, elongation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	DBIRD complex Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial matrix Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA polymerase II core binding Inferred from sequence or structural similarity. Source: UniProtKB enzyme inhibitor activity Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 922	922	DBIRD complex subunit KIAA1967 homolog		PRO_0000050814
Regions
	Coiled coil	573 – 596	24	Potential
	Coiled coil	828 – 898	71	Potential
Amino acid modifications
	Modified residue	35	1	Phosphothreonine By similarity
	Modified residue	124	1	Phosphoserine By similarity
	Modified residue	215	1	N6-acetyllysine By similarity
	Modified residue	612	1	Phosphoserine Ref.5
	Modified residue	674	1	Phosphoserine Ref.5 Ref.6
	Modified residue	677	1	Phosphoserine Ref.4 Ref.5 Ref.6
	Modified residue	680	1	Phosphoserine Ref.4 Ref.5 Ref.6
Experimental info
	Sequence conflict	527 – 529	3	RPK → HAS in AAH25471. Ref.2
	Sequence conflict	720	1	H → L in AAH38346. Ref.2
	Sequence conflict	812	1	G → R in BAC27420. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8VDP4 [UniParc]. Last modified March 1, 2004. Version 2. Checksum: 19F43ECEE58F461C	FASTA	922	103,002
	10 20 30 40 50 60 MSQFKRQRIN PLPGGRNFSG AASTSLLGPP PGLLTPPVAT DLSQNARHLQ SGEKQRVFTG 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 LSPYRVHLTP YTVDSPTCDF 250 260 270 280 290 300 LELQRRYRSL LVPSDFLSVH LSWLSAFPLG QPFSLHHPSR IQVSSEKEAA PDTGAEPSPE 310 320 330 340 350 360 DSDPTYSSKV LLLSSPGLEE FYRCCMLFVD DMAEPRETPE HPLKQLKFLL GRKEEEAVLV 370 380 390 400 410 420 GGEWSPSLDG LDPQADPQVL VRTAIRCAQA QTGIDLSTCT KWWRFAEFQY LQPGPPRQLH 430 440 450 460 470 480 TVVVYLPDVW TIMPTLEEWE ALCQQKATEA APQPHEASGE AEATEQAPDV SEQADTSKQN 490 500 510 520 530 540 TETMEATTQQ DVDTDLPEAP PPPLEPAVMA RPRCVNLSLY GIVEDRRPKE RISFEVVVLA 550 560 570 580 590 600 ELFVEMLQRD FGYRIYKTLL SLPEKVVSPP EPEKEEAAKE DAVKEEEAVK EEAVKVSKDE 610 620 630 640 650 660 VQNEGTAAES DSPLKEDGLL PKRPSSGGEE EEKARGEAAE DLCEMALDPD LLLLRDDGED 670 680 690 700 710 720 EFAGAKLEET EVRSVASNQS EMEYSSLQDM PKELDPSTVL PLDCLLAFVF FDANWCGYLH 730 740 750 760 770 780 RRDLERVLLT LGIRLSAEQA KQLVSRVVAQ NICQYRSLQY SRAEVLDDGL PEDVLFGNLD 790 800 810 820 830 840 LLPPSGKSTK PGAAPTEHKG LVPHNGSLIN VGSLLQRAEQ QDSGRLYLEN KIHTLELKLE 850 860 870 880 890 900 ESHNRFSATE VTNKTLAAEM QELRARLAEA EETARTAERQ KNQLQRQMQD FRRRLTPLHL 910 920 EMQRIVEKAD SWVEKEEPTP SN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. , 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. Tissue: Liver and Testis.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[3]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 226-248, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[4]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677 AND SER-680, MASS SPECTROMETRY. Tissue: Embryonic brain.
[5]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612; SER-674; SER-677 AND SER-680, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-677 AND SER-680, MASS SPECTROMETRY. Tissue: Melanoma.
[7]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK031472 mRNA. Translation: BAC27420.1. Different initiation. AK050238 mRNA. Translation: BAC34139.2. Different initiation. BC021475 mRNA. Translation: AAH21475.2. BC025471 mRNA. Translation: AAH25471.1. BC038346 mRNA. Translation: AAH38346.1.
IPI	IPI00123624.
RefSeq	NP_666167.3. NM_146055.3.
UniGene	Mm.218284.
3D structure databases
ProteinModelPortal	Q8VDP4.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8VDP4. 4 interactions.
STRING	10090.ENSMUSP00000036924.
PTM databases
PhosphoSite	Q8VDP4.
Proteomic databases
PaxDb	Q8VDP4.
PRIDE	Q8VDP4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000035612; ENSMUSP00000036924; ENSMUSG00000033712.
GeneID	219158.
KEGG	mmu:219158.
UCSC	uc007unf.1. mouse.
Organism-specific databases
MGI	MGI:2444228. 2610301G19Rik.
Phylogenomic databases
eggNOG	NOG307741.
GeneTree	ENSGT00530000063672.
HOGENOM	HOG000113184.
HOVERGEN	HBG081843.
InParanoid	Q8VDP4.
OMA	MSQFKRQ.
OrthoDB	EOG4WH8K6.
Gene expression databases
Bgee	Q8VDP4.
CleanEx	MM_2610301G19RIK.
Genevestigator	Q8VDP4.
GermOnline	ENSMUSG00000033712. Mus musculus.
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
NextBio	376623.

Entry information

Entry name

K1967_MOUSE

Accession

Primary (citable) accession number: Q8VDP4
Secondary accession number(s): Q6PIB1 , Q8BWR5, Q8C0F0, Q8R3G6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	March 1, 2004
Last modified:	April 3, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program