DBP_HUMAN
ID DBP_HUMAN Reviewed; 325 AA.
AC Q10586; A2I2P4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=D site-binding protein;
DE AltName: Full=Albumin D box-binding protein;
DE AltName: Full=Albumin D-element-binding protein;
DE AltName: Full=Tax-responsive enhancer element-binding protein 302;
DE Short=TaxREB302;
GN Name=DBP;
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 [MRNA].
RX PubMed=7835883; DOI=10.1006/geno.1994.1510;
RA Khatib Z.A., Inaba T., Valentine M., Look A.T.;
RT "Chromosomal localization and cDNA cloning of the human DBP and TEF
RT genes.";
RL Genomics 23:344-351(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8786133; DOI=10.1006/geno.1996.0295;
RA Shutler G., Glassco T., Kang X., Korneluk R., Mueller C.R.;
RT "Genomic structure of the human D-site binding protein (DBP) gene.";
RL Genomics 34:334-339(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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].
RC TISSUE=Ovary;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 132-325.
RX PubMed=8482542; DOI=10.1016/0378-1119(93)90375-d;
RA Nyunoya H., Morita T., Sato T., Honma S., Tsujimoto A., Shimotohno K.;
RT "Cloning of a cDNA encoding a DNA-binding protein TAXREB302 that is
RT specific for the tax-responsive enhancer of HTLV-I.";
RL Gene 126:251-255(1993).
RN [9]
RP SEQUENCE REVISION.
RA Nyunoya H.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP REVIEW.
RX PubMed=10508692; DOI=10.1016/s0959-437x(99)00009-x;
RA Brown S.A., Schibler U.;
RT "The ins and outs of circadian timekeeping.";
RL Curr. Opin. Genet. Dev. 9:588-594(1999).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: This transcriptional activator recognizes and binds to the
CC sequence 5'-RTTAYGTAAY-3' found in the promoter of genes such as
CC albumin, CYP2A4 and CYP2A5. It is not essential for circadian rhythm
CC generation, but modulates important clock output genes. May be a direct
CC target for regulation by the circadian pacemaker component clock. May
CC affect circadian period and sleep regulation.
CC -!- SUBUNIT: Binds DNA as a homodimer or a heterodimer. Can form a
CC heterodimer with TEF.
CC -!- INTERACTION:
CC Q10586; Q16520: BATF; NbExp=2; IntAct=EBI-3908088, EBI-749503;
CC Q10586; Q9NR55: BATF3; NbExp=2; IntAct=EBI-3908088, EBI-10312707;
CC Q10586; P35638: DDIT3; NbExp=4; IntAct=EBI-3908088, EBI-742651;
CC Q10586; Q16534: HLF; NbExp=3; IntAct=EBI-3908088, EBI-2798854;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in the
CC suprachiasmatic nuclei (SCN) and in most peripheral tissues, with a
CC strong circadian rhythmicity.
CC -!- SIMILARITY: Belongs to the bZIP family. PAR subfamily. {ECO:0000305}.
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DR EMBL; U06936; AAA81374.1; -; mRNA.
DR EMBL; U48213; AAB18668.1; -; Genomic_DNA.
DR EMBL; U48212; AAB18668.1; JOINED; Genomic_DNA.
DR EMBL; EF015902; ABM64213.1; -; Genomic_DNA.
DR EMBL; U79283; AAB50219.1; -; mRNA.
DR EMBL; BT006836; AAP35482.1; -; mRNA.
DR EMBL; CH471177; EAW52374.1; -; Genomic_DNA.
DR EMBL; BC011965; AAH11965.1; -; mRNA.
DR EMBL; D28468; BAA05833.1; -; mRNA.
DR CCDS; CCDS12728.1; -.
DR PIR; A55558; A55558.
DR RefSeq; NP_001343.2; NM_001352.4.
DR AlphaFoldDB; Q10586; -.
DR SMR; Q10586; -.
DR BioGRID; 107996; 13.
DR ComplexPortal; CPX-7014; bZIP transcription factor complex, BATF-DBP.
DR ComplexPortal; CPX-7068; bZIP transcription factor complex, BATF2-DBP.
DR ComplexPortal; CPX-7108; bZIP transcription factor complex, BATF3-DBP.
DR IntAct; Q10586; 9.
DR STRING; 9606.ENSP00000222122; -.
DR iPTMnet; Q10586; -.
DR PhosphoSitePlus; Q10586; -.
DR BioMuta; DBP; -.
DR DMDM; 1706312; -.
DR EPD; Q10586; -.
DR jPOST; Q10586; -.
DR MassIVE; Q10586; -.
DR PaxDb; Q10586; -.
DR PeptideAtlas; Q10586; -.
DR PRIDE; Q10586; -.
DR ProteomicsDB; 58862; -.
DR Antibodypedia; 18372; 120 antibodies from 22 providers.
DR DNASU; 1628; -.
DR Ensembl; ENST00000222122.10; ENSP00000222122.4; ENSG00000105516.11.
DR GeneID; 1628; -.
DR KEGG; hsa:1628; -.
DR MANE-Select; ENST00000222122.10; ENSP00000222122.4; NM_001352.5; NP_001343.2.
DR UCSC; uc002pjx.5; human.
DR CTD; 1628; -.
DR DisGeNET; 1628; -.
DR GeneCards; DBP; -.
DR HGNC; HGNC:2697; DBP.
DR HPA; ENSG00000105516; Low tissue specificity.
DR MIM; 124097; gene.
DR neXtProt; NX_Q10586; -.
DR OpenTargets; ENSG00000105516; -.
DR PharmGKB; PA27165; -.
DR VEuPathDB; HostDB:ENSG00000105516; -.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000162136; -.
DR HOGENOM; CLU_051922_0_0_1; -.
DR InParanoid; Q10586; -.
DR OMA; PKEPASX; -.
DR OrthoDB; 1023460at2759; -.
DR PhylomeDB; Q10586; -.
DR TreeFam; TF315869; -.
DR PathwayCommons; Q10586; -.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR SignaLink; Q10586; -.
DR SIGNOR; Q10586; -.
DR BioGRID-ORCS; 1628; 12 hits in 1111 CRISPR screens.
DR ChiTaRS; DBP; human.
DR GeneWiki; DBP_(gene); -.
DR GenomeRNAi; 1628; -.
DR Pharos; Q10586; Tbio.
DR PRO; PR:Q10586; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q10586; protein.
DR Bgee; ENSG00000105516; Expressed in right hemisphere of cerebellum and 177 other tissues.
DR ExpressionAtlas; Q10586; baseline and differential.
DR Genevisible; Q10586; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0007623; P:circadian rhythm; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029830; DBP.
DR InterPro; IPR040223; PAR_bZIP.
DR PANTHER; PTHR11988; PTHR11988; 1.
DR PANTHER; PTHR11988:SF7; PTHR11988:SF7; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Activator; Biological rhythms; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..325
FT /note="D site-binding protein"
FT /id="PRO_0000076507"
FT DOMAIN 255..318
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..279
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 283..297
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 127..151
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT CONFLICT 179
FT /note="S -> T (in Ref. 1; AAA81374)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="R -> K (in Ref. 8; BAA05833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 34349 MW; A6933CE21399ECF3 CRC64;
MARPVSDRTP APLLLGGPAG TPPGGGALLG LRSLLQGTSK PKEPASCLLK EKERKAALPA
ATTPGPGLET AGPADAPAGA VVGGGSPRGR PGPVPAPGLL APLLWERTLP FGDVEYVDLD
AFLLEHGLPP SPPPPGGPSP EPSPARTPAP SPGPGSCGSA SPRSSPGHAP ARAALGTASG
HRAGLTSRDT PSPVDPDTVE VLMTFEPDPA DLALSSIPGH ETFDPRRHRF SEEELKPQPI
MKKARKIQVP EEQKDEKYWS RRYKNNEAAK RSRDARRLKE NQISVRAAFL EKENALLRQE
VVAVRQELSH YRAVLSRYQA QHGAL
