DPB_ARATH
ID DPB_ARATH Reviewed; 385 AA.
AC Q9FNY2; Q8LDG3; Q9LZE7;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Transcription factor-like protein DPB;
DE AltName: Full=DP-like protein B;
DE Short=AtDPbB;
DE AltName: Full=E2F dimerization partner protein B;
GN Name=DPB; Synonyms=DP1; OrderedLocusNames=At5g03415; ORFNames=F12E4.160;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH E2FA AND E2FB.
RC STRAIN=cv. Columbia;
RX PubMed=11108847; DOI=10.1016/s0014-5793(00)02238-9;
RA Magyar Z., Atanassova A., De Veylder L., Rombauts S., Inze D.;
RT "Characterization of two distinct DP-related genes from Arabidopsis
RT thaliana.";
RL FEBS Lett. 486:79-87(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=11669580; DOI=10.1023/a:1011848528377;
RA de Jager S.M., Menges M., Bauer U.M., Murra J.A.;
RT "Arabidopsis E2F1 binds a sequence present in the promoter of S-phase-
RT regulated gene AtCDC6 and is a member of a multigene family with
RT differential activities.";
RL Plant Mol. Biol. 47:555-568(2001).
RN [8]
RP INTERACTION WITH E2FA; E2FB AND E2FC, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11786543; DOI=10.1074/jbc.m110616200;
RA Mariconti L., Pellegrini B., Cantoni R., Stevens R., Bergounioux C.,
RA Cella R., Albani D.;
RT "The E2F family of transcription factors from Arabidopsis thaliana. Novel
RT and conserved components of the retinoblastoma/E2F pathway in plants.";
RL J. Biol. Chem. 277:9911-9919(2002).
RN [9]
RP FUNCTION, INTERACTION WITH E2FA; E2FB AND E2FC, AND SUBCELLULAR LOCATION.
RX PubMed=11891240; DOI=10.1104/pp.010642;
RA Kosugi S., Ohashi Y.;
RT "Interaction of the Arabidopsis E2F and DP proteins confers their
RT concomitant nuclear translocation and transactivation.";
RL Plant Physiol. 128:833-843(2002).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, SUBUNIT, AND INTERACTION
RP WITH E2FC.
RX PubMed=16920782; DOI=10.1105/tpc.105.039651;
RA del Pozo J.C., Diaz-Trivino S., Cisneros N., Gutierrez C.;
RT "The balance between cell division and endoreplication depends on E2FC-DPB,
RT transcription factors regulated by the ubiquitin-SCFSKP2A pathway in
RT Arabidopsis.";
RL Plant Cell 18:2224-2235(2006).
RN [11]
RP INTERACTION WITH SKP2A.
RX PubMed=21139066; DOI=10.1105/tpc.110.078972;
RA Jurado S., Abraham Z., Manzano C., Lopez-Torrejon G., Pacios L.F.,
RA Del Pozo J.C.;
RT "The Arabidopsis cell cycle F-Box protein SKP2A binds to auxin.";
RL Plant Cell 22:3891-3904(2010).
CC -!- FUNCTION: Involved in the regulation of the G1/S transition. Increases
CC the DNA binding activity of E2F proteins after heterodimerization. The
CC complex DPB/E2FC restricts cell division and lateral root initiation
CC and may function as a negative regulator of E2F-regulated genes. The
CC interaction with SKP2A is controlled by auxin.
CC {ECO:0000269|PubMed:11891240, ECO:0000269|PubMed:16920782}.
CC -!- SUBUNIT: Heterodimer with non-phosphorylated E2FC. No interaction with
CC phosphorylated E2FC. Interacts preferentially with E2FC, but also with
CC E2FA and E2FB. Interacts with SKP2A. Targeted for proteasomal
CC degradation by the SCF(SKP2A) E3 ubiquitin ligase complex.
CC {ECO:0000269|PubMed:11108847, ECO:0000269|PubMed:11786543,
CC ECO:0000269|PubMed:11891240, ECO:0000269|PubMed:16920782,
CC ECO:0000269|PubMed:21139066}.
CC -!- INTERACTION:
CC Q9FNY2; Q9FNY0: E2FA; NbExp=5; IntAct=EBI-1774876, EBI-1774747;
CC Q9FNY2; Q9FV71: E2FB; NbExp=6; IntAct=EBI-1774876, EBI-1774719;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11891240}. Cytoplasm
CC {ECO:0000269|PubMed:11891240}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FNY2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FNY2-2; Sequence=VSP_040734;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16920782}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the whole cell cycle.
CC {ECO:0000269|PubMed:11669580}.
CC -!- DOMAIN: The DIM domain (182-263) is required for heterodimerization.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:16920782}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB83299.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ294532; CAC15484.1; -; mRNA.
DR EMBL; AL162751; CAB83299.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90599.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90600.1; -; Genomic_DNA.
DR EMBL; AY086018; AAM63227.1; -; mRNA.
DR EMBL; AK228148; BAF00104.1; -; mRNA.
DR EMBL; AB493733; BAH30571.1; -; mRNA.
DR PIR; T48364; T48364.
DR RefSeq; NP_001190214.1; NM_001203285.1. [Q9FNY2-2]
DR RefSeq; NP_850757.1; NM_180426.3. [Q9FNY2-1]
DR AlphaFoldDB; Q9FNY2; -.
DR SMR; Q9FNY2; -.
DR BioGRID; 17123; 23.
DR IntAct; Q9FNY2; 14.
DR STRING; 3702.AT5G03415.1; -.
DR PaxDb; Q9FNY2; -.
DR PRIDE; Q9FNY2; -.
DR ProteomicsDB; 220396; -. [Q9FNY2-1]
DR EnsemblPlants; AT5G03415.1; AT5G03415.1; AT5G03415. [Q9FNY2-1]
DR EnsemblPlants; AT5G03415.2; AT5G03415.2; AT5G03415. [Q9FNY2-2]
DR GeneID; 831847; -.
DR Gramene; AT5G03415.1; AT5G03415.1; AT5G03415. [Q9FNY2-1]
DR Gramene; AT5G03415.2; AT5G03415.2; AT5G03415. [Q9FNY2-2]
DR KEGG; ath:AT5G03415; -.
DR Araport; AT5G03415; -.
DR TAIR; locus:1005716177; AT5G03415.
DR eggNOG; KOG1936; Eukaryota.
DR eggNOG; KOG2829; Eukaryota.
DR HOGENOM; CLU_039874_2_1_1; -.
DR InParanoid; Q9FNY2; -.
DR OMA; STPNNYW; -.
DR OrthoDB; 1046304at2759; -.
DR PhylomeDB; Q9FNY2; -.
DR PRO; PR:Q9FNY2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNY2; baseline and differential.
DR Genevisible; Q9FNY2; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0070176; C:DRM complex; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:TAIR.
DR GO; GO:0042023; P:DNA endoreduplication; IMP:TAIR.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:TAIR.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd14458; DP_DD; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.20.140.80; -; 1.
DR InterPro; IPR037241; E2F-DP_heterodim.
DR InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
DR InterPro; IPR038168; TF_DP_C_sf.
DR InterPro; IPR014889; Transc_factor_DP_C.
DR InterPro; IPR015648; Transcrpt_fac_DP.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12548; PTHR12548; 1.
DR Pfam; PF08781; DP; 1.
DR Pfam; PF02319; E2F_TDP; 1.
DR PIRSF; PIRSF009404; Transcription_factor_DP; 1.
DR SMART; SM01138; DP; 1.
DR SMART; SM01372; E2F_TDP; 1.
DR SUPFAM; SSF144074; SSF144074; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Coiled coil; Cytoplasm; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..385
FT /note="Transcription factor-like protein DPB"
FT /id="PRO_0000405865"
FT DNA_BIND 101..184
FT /evidence="ECO:0000255"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 185..234
FT /evidence="ECO:0000255"
FT MOTIF 150..184
FT /note="DEF box"
FT /evidence="ECO:0000250"
FT VAR_SEQ 105..111
FT /note="RQFSMKV -> L (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040734"
FT CONFLICT 40
FT /note="G -> S (in Ref. 4; AAM63227)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="T -> A (in Ref. 4; AAM63227)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="R -> Q (in Ref. 4; AAM63227)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="G -> R (in Ref. 4; AAM63227)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 42755 MW; 5DDB4ACA04C52AF8 CRC64;
MTTTGSNSNH NHHESNNNNN NPSTRSWGTA VSGQSVSTSG SMGSPSSRSE QTITVVTSTS
DTTFQRLNNL DIQGDDAGSQ GASGVKKKKR GQRAAGPDKT GRGLRQFSMK VCEKVESKGR
TTYNEVADEL VAEFALPNND GTSPDQQQYD EKNIRRRVYD ALNVLMAMDI ISKDKKEIQW
RGLPRTSLSD IEELKNERLS LRNRIEKKTA YSQELEEQYV GLQNLIQRNE HLYSSGNAPS
GGVALPFILV QTRPHATVEV EISEDMQLVH FDFNSTPFEL HDDNFVLKTM KFCDQPPQQP
NGRNNSQLVC HNFTPENPNK GPSTGPTPQL DMYETHLQSQ QHQQHSQLQI IPMPETNNVT
SSADTAPVKS PSLPGIMNSS MKPEN
