DBND2_HUMAN
ID DBND2_HUMAN Reviewed; 259 AA.
AC Q9BQY9; Q331S6; Q5QPV4; Q5QPV6; Q9BQZ0; Q9BVL1; Q9H1F6; Q9NWZ0; Q9NY07;
AC Q9NZ31;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Dysbindin domain-containing protein 2;
DE AltName: Full=Casein kinase-1 binding protein;
DE Short=CK1BP;
DE AltName: Full=HSMNP1;
GN Name=DBNDD2; Synonyms=C20orf35;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RX PubMed=16305340; DOI=10.1089/scd.2005.14.556;
RA Lucas T., Pratscher B., Fink D., Wolschek M., Samorapoompichit P.,
RA Schofer C., Pehamberger H., Muller M., Sorensen P., Jansen B.;
RT "The human orthologue of a novel apoptosis response gene induced during rat
RT myelomonocytic stem cell apoptosis maps to 20q13.12.";
RL Stem Cells Dev. 14:556-563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Skeletal muscle;
RA Frigimelica E., Lanfranchi G.;
RT "Full-length sequencing of some human and murine muscular transcripts
RT (Telethon Italy project B41).";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION, SUBUNIT, INTERACTION WITH CSNK1D AND CSNK1E, AND TISSUE
RP SPECIFICITY.
RX PubMed=16618118; DOI=10.1021/bi052354e;
RA Yin H., Laguna K.A., Li G., Kuret J.;
RT "Dysbindin structural homologue CK1BP is an isoform-selective binding
RT partner of human casein kinase-1.";
RL Biochemistry 45:5297-5308(2006).
CC -!- FUNCTION: May modulate the activity of casein kinase-1. Inhibits CSNK1D
CC autophosphorylation (in vitro). {ECO:0000269|PubMed:16618118}.
CC -!- SUBUNIT: Monomer. Interacts with CSNK1D and CSNK1E.
CC {ECO:0000269|PubMed:16618118}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BQY9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQY9-2; Sequence=VSP_007753;
CC Name=3;
CC IsoId=Q9BQY9-3; Sequence=VSP_007753, VSP_040767, VSP_040768;
CC Name=4;
CC IsoId=Q9BQY9-4; Sequence=VSP_046691;
CC -!- TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:16618118}.
CC -!- SIMILARITY: Belongs to the dysbindin family. {ECO:0000305}.
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DR EMBL; AF220191; AAF67656.1; -; mRNA.
DR EMBL; AY113697; AAM77463.1; -; mRNA.
DR EMBL; AK000531; BAA91235.1; -; mRNA.
DR EMBL; AJ276469; CAB83042.1; -; mRNA.
DR EMBL; AL021578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75848.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75854.1; -; Genomic_DNA.
DR EMBL; AL591565; CAC39141.1; -; mRNA.
DR EMBL; BC001105; AAH01105.1; -; mRNA.
DR EMBL; BC012818; AAH12818.1; -; mRNA.
DR EMBL; BG703352; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS42880.1; -. [Q9BQY9-2]
DR CCDS; CCDS42881.1; -. [Q9BQY9-3]
DR CCDS; CCDS56193.1; -. [Q9BQY9-1]
DR CCDS; CCDS56194.1; -. [Q9BQY9-2]
DR RefSeq; NP_001041686.1; NM_001048221.2. [Q9BQY9-2]
DR RefSeq; NP_001041687.1; NM_001048222.2. [Q9BQY9-3]
DR RefSeq; NP_001041688.1; NM_001048223.2. [Q9BQY9-2]
DR RefSeq; NP_001041689.1; NM_001048224.2. [Q9BQY9-3]
DR RefSeq; NP_001041690.2; NM_001048225.2. [Q9BQY9-2]
DR RefSeq; NP_001184068.1; NM_001197139.1. [Q9BQY9-2]
DR RefSeq; NP_001184069.1; NM_001197140.1. [Q9BQY9-2]
DR RefSeq; NP_060948.3; NM_018478.3. [Q9BQY9-1]
DR AlphaFoldDB; Q9BQY9; -.
DR BioGRID; 120963; 11.
DR IntAct; Q9BQY9; 4.
DR MINT; Q9BQY9; -.
DR STRING; 9606.ENSP00000361795; -.
DR iPTMnet; Q9BQY9; -.
DR PhosphoSitePlus; Q9BQY9; -.
DR BioMuta; DBNDD2; -.
DR DMDM; 327478587; -.
DR MassIVE; Q9BQY9; -.
DR PaxDb; Q9BQY9; -.
DR PeptideAtlas; Q9BQY9; -.
DR PRIDE; Q9BQY9; -.
DR ProteomicsDB; 63697; -.
DR ProteomicsDB; 78730; -. [Q9BQY9-1]
DR ProteomicsDB; 78731; -. [Q9BQY9-2]
DR ProteomicsDB; 78732; -. [Q9BQY9-3]
DR Antibodypedia; 51972; 57 antibodies from 14 providers.
DR DNASU; 55861; -.
DR Ensembl; ENST00000357275.6; ENSP00000349822.2; ENSG00000244274.9. [Q9BQY9-2]
DR Ensembl; ENST00000360981.8; ENSP00000354250.4; ENSG00000244274.9. [Q9BQY9-2]
DR Ensembl; ENST00000372710.5; ENSP00000361795.4; ENSG00000244274.9. [Q9BQY9-2]
DR Ensembl; ENST00000372712.6; ENSP00000361797.2; ENSG00000244274.9. [Q9BQY9-2]
DR Ensembl; ENST00000372717.5; ENSP00000361802.1; ENSG00000244274.9. [Q9BQY9-3]
DR Ensembl; ENST00000372720.7; ENSP00000361805.3; ENSG00000244274.9. [Q9BQY9-1]
DR Ensembl; ENST00000372722.7; ENSP00000361807.3; ENSG00000244274.9. [Q9BQY9-3]
DR Ensembl; ENST00000372723.7; ENSP00000361808.3; ENSG00000244274.9. [Q9BQY9-2]
DR GeneID; 55861; -.
DR KEGG; hsa:55861; -.
DR MANE-Select; ENST00000372710.5; ENSP00000361795.4; NM_001048225.4; NP_001041690.3. [Q9BQY9-2]
DR UCSC; uc002xnz.4; human. [Q9BQY9-1]
DR CTD; 55861; -.
DR DisGeNET; 55861; -.
DR GeneCards; DBNDD2; -.
DR HGNC; HGNC:15881; DBNDD2.
DR HPA; ENSG00000244274; Tissue enhanced (brain, choroid plexus).
DR MIM; 611453; gene.
DR neXtProt; NX_Q9BQY9; -.
DR OpenTargets; ENSG00000244274; -.
DR PharmGKB; PA25749; -.
DR VEuPathDB; HostDB:ENSG00000244274; -.
DR eggNOG; ENOG502RZ1K; Eukaryota.
DR GeneTree; ENSGT00940000161212; -.
DR HOGENOM; CLU_097594_1_0_1; -.
DR InParanoid; Q9BQY9; -.
DR OMA; CGTEDNN; -.
DR OrthoDB; 862376at2759; -.
DR PhylomeDB; Q9BQY9; -.
DR TreeFam; TF332997; -.
DR PathwayCommons; Q9BQY9; -.
DR SignaLink; Q9BQY9; -.
DR BioGRID-ORCS; 55861; 10 hits in 1079 CRISPR screens.
DR GeneWiki; DBNDD2; -.
DR GenomeRNAi; 55861; -.
DR Pharos; Q9BQY9; Tdark.
DR PRO; PR:Q9BQY9; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9BQY9; protein.
DR Bgee; ENSG00000244274; Expressed in C1 segment of cervical spinal cord and 95 other tissues.
DR ExpressionAtlas; Q9BQY9; baseline and differential.
DR Genevisible; Q9BQY9; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
DR InterPro; IPR007531; Dysbindin.
DR PANTHER; PTHR16294; PTHR16294; 1.
DR Pfam; PF04440; Dysbindin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Phosphoprotein; Reference proteome.
FT CHAIN 1..259
FT /note="Dysbindin domain-containing protein 2"
FT /id="PRO_0000191003"
FT REGION 27..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..56
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CRD4"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CRD4"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CRD4"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CRD4"
FT VAR_SEQ 1..98
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_007753"
FT VAR_SEQ 1..53
FT /note="MGAGNFLTALEVPVAALAGAASDRRASCERVSPPPPLPHFRLPPLPRSRLPG
FT P -> MESWALAVFPEYRVSLLWCLELASPLWSLGQAPPLHETWFVGHTWFQGRGKRSP
FT RAE (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_046691"
FT VAR_SEQ 193..210
FT /note="DNHLEELSLPVPTSDRTT -> PLCFGDFSASQPEPDVRL (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040767"
FT VAR_SEQ 211..259
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040768"
FT CONFLICT 43
FT /note="P -> GTR (in Ref. 1; AAF67656)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="Q -> H (in Ref. 3; BAA91235)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="M -> V (in Ref. 1; AAF67656, 2; AAM77463, 3;
FT BAA91235, 6; EAW75854/EAW75848 and 7; AAH12818/AAH01105)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="P -> A (in Ref. 1; AAF67656)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="G -> D (in Ref. 3; BAA91235)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 27671 MW; DA1F062426867A2C CRC64;
MGAGNFLTAL EVPVAALAGA ASDRRASCER VSPPPPLPHF RLPPLPRSRL PGPVSRPEPG
APLLGCWLQW GAPSPGPLCL LFRLCSCTCF APLPAGADMD PNPRAALERQ QLRLRERQKF
FEDILQPETE FVFPLSHLHL ESQRPPIGSI SSMEVNVDTL EQVELIDLGD PDAADVFLPC
EDPPPTPQSS GMDNHLEELS LPVPTSDRTT SRTSSSSSSD SSTNLHSPNP SDDGADTPLA
QSDEEEERGD GGAEPGACS
