Q9BQY9 (DBND2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dysbindin domain-containing protein 2
Short name=Casein kinase-1 binding protein

Alternative name(s):
CK1BP
HSMNP1

Gene names

Name:	DBNDD2
Synonyms:	C20orf35

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	259 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May modulate the activity of casein kinase-1. Inhibits CSNK1D autophosphorylation (in vitro). Ref.6
Subunit structure	Monomer. Interacts with CSNK1D and CSNK1E. Ref.6
Tissue specificity	Detected in brain. Ref.6
Sequence similarities	Belongs to the dysbindin family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of protein kinase activity Inferred from direct assay Ref.6. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Inferred from physical interaction Ref.6. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BQY9-1)

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: Q9BQY9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-98: Missing.

Isoform 3 (identifier: Q9BQY9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-98: Missing.
     193-210: DNHLEELSLPVPTSDRTT → PLCFGDFSASQPEPDVRL
     211-259: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 259	259	Dysbindin domain-containing protein 2		PRO_0000191003
Regions
	Compositional bias	33 – 38	6	Poly-Pro
	Compositional bias	214 – 222	9	Poly-Ser
	Compositional bias	244 – 247	4	Poly-Glu
Amino acid modifications
	Modified residue	215	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 98	98	Missing in isoform 2 and isoform 3.		VSP_007753
	Alternative sequence	193 – 210	18	DNHLE…SDRTT → PLCFGDFSASQPEPDVRL in isoform 3.		VSP_040767
	Alternative sequence	211 – 259	49	Missing in isoform 3.		VSP_040768
Experimental info
	Sequence conflict	43	1	P → GTR in AAF67656. Ref.1
	Sequence conflict	162	1	Q → H in BAA91235. Ref.2
	Sequence conflict	192	1	M → V in AAF67656. Ref.1
	Sequence conflict	192	1	M → V in BAA91235. Ref.2
	Sequence conflict	192	1	M → V in AAH12818. Ref.5
	Sequence conflict	192	1	M → V in AAH01105. Ref.5
	Sequence conflict	204	1	P → A in AAF67656. Ref.1
	Sequence conflict	249	1	G → D in BAA91235. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 5, 2011. Version 3. Checksum: DA1F062426867A2C	FASTA	259	27,671
	10 20 30 40 50 60 MGAGNFLTAL EVPVAALAGA ASDRRASCER VSPPPPLPHF RLPPLPRSRL PGPVSRPEPG 70 80 90 100 110 120 APLLGCWLQW GAPSPGPLCL LFRLCSCTCF APLPAGADMD PNPRAALERQ QLRLRERQKF 130 140 150 160 170 180 FEDILQPETE FVFPLSHLHL ESQRPPIGSI SSMEVNVDTL EQVELIDLGD PDAADVFLPC 190 200 210 220 230 240 EDPPPTPQSS GMDNHLEELS LPVPTSDRTT SRTSSSSSSD SSTNLHSPNP SDDGADTPLA 250 QSDEEEERGD GGAEPGACS
	Isoform 2 [UniParc]. Checksum: 6840B7093720567B	FASTA	161	17,525
	10 20 30 40 50 60 MDPNPRAALE RQQLRLRERQ KFFEDILQPE TEFVFPLSHL HLESQRPPIG SISSMEVNVD 70 80 90 100 110 120 TLEQVELIDL GDPDAADVFL PCEDPPPTPQ SSGMDNHLEE LSLPVPTSDR TTSRTSSSSS 130 140 150 160 SDSSTNLHSP NPSDDGADTP LAQSDEEEER GDGGAEPGAC S
	Isoform 3 [UniParc]. Checksum: BB2C19A23C184395	FASTA	112	12,614
	10 20 30 40 50 60 MDPNPRAALE RQQLRLRERQ KFFEDILQPE TEFVFPLSHL HLESQRPPIG SISSMEVNVD 70 80 90 100 110 TLEQVELIDL GDPDAADVFL PCEDPPPTPQ SSGMPLCFGD FSASQPEPDV RL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L. Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed: 10931946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Hypothalamus.
[2]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
[3]	"Full-length sequencing of some human and murine muscular transcripts (Telethon Italy project B41)." Frigimelica E., Lanfranchi G. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Skeletal muscle.
[4]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Placenta.
[6]	"Dysbindin structural homologue CK1BP is an isoform-selective binding partner of human casein kinase-1." Yin H., Laguna K.A., Li G., Kuret J. Biochemistry 45:5297-5308(2006) [PubMed: 16618118] [Abstract] Cited for: FUNCTION, SUBUNIT, INTERACTION WITH CSNK1D AND CSNK1E, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF220191 mRNA. Translation: AAF67656.1. AK000531 mRNA. Translation: BAA91235.1. AJ276469 mRNA. Translation: CAB83042.1. AL021578 Genomic DNA. Translation: CAC18108.1. AL021578 Genomic DNA. Translation: CAC18109.1. AL591565 mRNA. Translation: CAC39141.1. BC001105 mRNA. Translation: AAH01105.1. BC012818 mRNA. Translation: AAH12818.1. BG703352 mRNA. No translation available.
IPI	IPI00302689. IPI00514216. IPI00983936.
RefSeq	NP_001041686.1. NM_001048221.2. NP_001041688.1. NM_001048223.2. NP_001184068.1. NM_001197139.1. NP_001184069.1. NM_001197140.1. NP_060948.3. NM_018478.3.
UniGene	Hs.655055.
3D structure databases
ProteinModelPortal	Q9BQY9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BQY9. 1 interaction.
MINT	MINT-1476709.
STRING	Q9BQY9.
PTM databases
PhosphoSite	Q9BQY9.
Polymorphism databases
DMDM	32699604.
Proteomic databases
PRIDE	Q9BQY9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000372720; ENSP00000361805; ENSG00000244274.
GeneID	55861.
KEGG	hsa:55861.
UCSC	uc002xnx.1. human.
Organism-specific databases
CTD	55861.
GeneCards	GC20P044034.
H-InvDB	HIX0019509.
HGNC	HGNC:15881. DBNDD2.
HPA	HPA043991.
MIM	611453. gene.
neXtProt	NX_Q9BQY9.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000010667.
PhylomeDB	Q9BQY9.
Gene expression databases
ArrayExpress	Q9BQY9.
CleanEx	HS_DBNDD2.
Genevestigator	Q9BQY9.
GermOnline	ENSG00000204070. Homo sapiens.
Family and domain databases
InterPro	IPR007531. Dysbindin. [Graphical view]
PANTHER	PTHR16294. Dysbindin. 1 hit.
Pfam	PF04440. Dysbindin. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	61155.
SOURCE	Search...

Entry information

Entry name

DBND2_HUMAN

Accession

Primary (citable) accession number: Q9BQY9
Secondary accession number(s): Q9BQZ0 , Q9BVL1, Q9H1F6, Q9NWZ0, Q9NY07, Q9NZ31

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2003
Last sequence update:	April 5, 2011
Last modified:	January 25, 2012
This is version 80 of the entry and version 3 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.