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Protein

Transcription factor-like protein DPB

Gene

DPB

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the regulation of the G1/S transition. Increases the DNA binding activity of E2F proteins after heterodimerization. The complex DPB/E2FC restricts cell division and lateral root initiation and may function as a negative regulator of E2F-regulated genes. The interaction with SKP2A is controlled by auxin.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi101 – 18484Sequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • DNA endoreduplication Source: TAIR
  • G1/S transition of mitotic cell cycle Source: TAIR
  • regulation of transcription from RNA polymerase II promoter Source: GO_Central
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-ATH-113510. E2F mediated regulation of DNA replication.
R-ATH-1538133. G0 and Early G1.
R-ATH-69205. G1/S-Specific Transcription.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor-like protein DPB
Alternative name(s):
DP-like protein B
Short name:
AtDPbB
E2F dimerization partner protein B
Gene namesi
Name:DPB
Synonyms:DP1
Ordered Locus Names:At5g03415
ORF Names:F12E4.160
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G03415.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: TAIR
  • nucleus Source: TAIR
  • transcription factor complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 385385Transcription factor-like protein DPBPRO_0000405865Add
BLAST

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9FNY2.
PRIDEiQ9FNY2.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Developmental stagei

Expressed during the whole cell cycle.1 Publication

Gene expression databases

GenevisibleiQ9FNY2. AT.

Interactioni

Subunit structurei

Heterodimer with non-phosphorylated E2FC. No interaction with phosphorylated E2FC. Interacts preferentially with E2FC, but also with E2FA and E2FB. Interacts with SKP2A. Targeted for proteasomal degradation by the SCF(SKP2A) E3 ubiquitin ligase complex.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
E2FAQ9FNY05EBI-1774876,EBI-1774747
E2FBQ9FV716EBI-1774876,EBI-1774719

GO - Molecular functioni

  • protein heterodimerization activity Source: TAIR

Protein-protein interaction databases

BioGridi17123. 21 interactions.
IntActiQ9FNY2. 12 interactions.
STRINGi3702.AT5G03415.1.

Structurei

3D structure databases

ProteinModelPortaliQ9FNY2.
SMRiQ9FNY2. Positions 101-184, 190-290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili185 – 23450Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi150 – 18435DEF boxBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi7 – 2115Asn-richAdd
BLAST
Compositional biasi86 – 894Poly-Lys

Domaini

The DIM domain (182-263) is required for heterodimerization.

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2829. Eukaryota.
ENOG410Y9QP. LUCA.
HOGENOMiHOG000029891.
InParanoidiQ9FNY2.
OMAiLIQRNEH.
PhylomeDBiQ9FNY2.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR003316. E2F_WHTH_DNA-bd_dom.
IPR014889. Transc_factor_DP_C.
IPR015648. Transcrpt_fac_DP.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12548. PTHR12548. 1 hit.
PfamiPF08781. DP. 1 hit.
PF02319. E2F_TDP. 1 hit.
[Graphical view]
PIRSFiPIRSF009404. Transcription_factor_DP. 1 hit.
SMARTiSM01138. DP. 1 hit.
SM01372. E2F_TDP. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9FNY2-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTTTGSNSNH NHHESNNNNN NPSTRSWGTA VSGQSVSTSG SMGSPSSRSE
60 70 80 90 100
QTITVVTSTS DTTFQRLNNL DIQGDDAGSQ GASGVKKKKR GQRAAGPDKT
110 120 130 140 150
GRGLRQFSMK VCEKVESKGR TTYNEVADEL VAEFALPNND GTSPDQQQYD
160 170 180 190 200
EKNIRRRVYD ALNVLMAMDI ISKDKKEIQW RGLPRTSLSD IEELKNERLS
210 220 230 240 250
LRNRIEKKTA YSQELEEQYV GLQNLIQRNE HLYSSGNAPS GGVALPFILV
260 270 280 290 300
QTRPHATVEV EISEDMQLVH FDFNSTPFEL HDDNFVLKTM KFCDQPPQQP
310 320 330 340 350
NGRNNSQLVC HNFTPENPNK GPSTGPTPQL DMYETHLQSQ QHQQHSQLQI
360 370 380
IPMPETNNVT SSADTAPVKS PSLPGIMNSS MKPEN
Length:385
Mass (Da):42,755
Last modified:March 1, 2001 - v1
Checksum:i5DDB4ACA04C52AF8
GO
Isoform 2 (identifier: Q9FNY2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     105-111: RQFSMKV → L

Note: Derived from EST data. No experimental confirmation available.
Show »
Length:379
Mass (Da):41,991
Checksum:i6505E31E4E1F8E1E
GO

Sequence cautioni

The sequence CAB83299.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401G → S in AAM63227 (Ref. 4) Curated
Sequence conflicti59 – 591T → A in AAM63227 (Ref. 4) Curated
Sequence conflicti303 – 3031R → Q in AAM63227 (Ref. 4) Curated
Sequence conflicti375 – 3751G → R in AAM63227 (Ref. 4) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei105 – 1117RQFSMKV → L in isoform 2. CuratedVSP_040734

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ294532 mRNA. Translation: CAC15484.1.
AL162751 Genomic DNA. Translation: CAB83299.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED90599.1.
CP002688 Genomic DNA. Translation: AED90600.1.
AY086018 mRNA. Translation: AAM63227.1.
AK228148 mRNA. Translation: BAF00104.1.
AB493733 mRNA. Translation: BAH30571.1.
PIRiT48364.
RefSeqiNP_001190214.1. NM_001203285.1. [Q9FNY2-2]
NP_850757.1. NM_180426.2. [Q9FNY2-1]
UniGeneiAt.4864.

Genome annotation databases

EnsemblPlantsiAT5G03415.1; AT5G03415.1; AT5G03415. [Q9FNY2-1]
GeneIDi831847.
KEGGiath:AT5G03415.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ294532 mRNA. Translation: CAC15484.1.
AL162751 Genomic DNA. Translation: CAB83299.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED90599.1.
CP002688 Genomic DNA. Translation: AED90600.1.
AY086018 mRNA. Translation: AAM63227.1.
AK228148 mRNA. Translation: BAF00104.1.
AB493733 mRNA. Translation: BAH30571.1.
PIRiT48364.
RefSeqiNP_001190214.1. NM_001203285.1. [Q9FNY2-2]
NP_850757.1. NM_180426.2. [Q9FNY2-1]
UniGeneiAt.4864.

3D structure databases

ProteinModelPortaliQ9FNY2.
SMRiQ9FNY2. Positions 101-184, 190-290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi17123. 21 interactions.
IntActiQ9FNY2. 12 interactions.
STRINGi3702.AT5G03415.1.

Proteomic databases

PaxDbiQ9FNY2.
PRIDEiQ9FNY2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G03415.1; AT5G03415.1; AT5G03415. [Q9FNY2-1]
GeneIDi831847.
KEGGiath:AT5G03415.

Organism-specific databases

TAIRiAT5G03415.

Phylogenomic databases

eggNOGiKOG2829. Eukaryota.
ENOG410Y9QP. LUCA.
HOGENOMiHOG000029891.
InParanoidiQ9FNY2.
OMAiLIQRNEH.
PhylomeDBiQ9FNY2.

Enzyme and pathway databases

ReactomeiR-ATH-113510. E2F mediated regulation of DNA replication.
R-ATH-1538133. G0 and Early G1.
R-ATH-69205. G1/S-Specific Transcription.

Miscellaneous databases

PROiQ9FNY2.

Gene expression databases

GenevisibleiQ9FNY2. AT.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR003316. E2F_WHTH_DNA-bd_dom.
IPR014889. Transc_factor_DP_C.
IPR015648. Transcrpt_fac_DP.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12548. PTHR12548. 1 hit.
PfamiPF08781. DP. 1 hit.
PF02319. E2F_TDP. 1 hit.
[Graphical view]
PIRSFiPIRSF009404. Transcription_factor_DP. 1 hit.
SMARTiSM01138. DP. 1 hit.
SM01372. E2F_TDP. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of two distinct DP-related genes from Arabidopsis thaliana."
    Magyar Z., Atanassova A., De Veylder L., Rombauts S., Inze D.
    FEBS Lett. 486:79-87(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH E2FA AND E2FB.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  6. "ORF cloning and analysis of Arabidopsis transcription factor genes."
    Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y., Takagi M.
    Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "Arabidopsis E2F1 binds a sequence present in the promoter of S-phase-regulated gene AtCDC6 and is a member of a multigene family with differential activities."
    de Jager S.M., Menges M., Bauer U.M., Murra J.A.
    Plant Mol. Biol. 47:555-568(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  8. "The E2F family of transcription factors from Arabidopsis thaliana. Novel and conserved components of the retinoblastoma/E2F pathway in plants."
    Mariconti L., Pellegrini B., Cantoni R., Stevens R., Bergounioux C., Cella R., Albani D.
    J. Biol. Chem. 277:9911-9919(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH E2FA; E2FB AND E2FC, GENE FAMILY, NOMENCLATURE.
  9. "Interaction of the Arabidopsis E2F and DP proteins confers their concomitant nuclear translocation and transactivation."
    Kosugi S., Ohashi Y.
    Plant Physiol. 128:833-843(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH E2FA; E2FB AND E2FC, SUBCELLULAR LOCATION.
  10. "The balance between cell division and endoreplication depends on E2FC-DPB, transcription factors regulated by the ubiquitin-SCFSKP2A pathway in Arabidopsis."
    del Pozo J.C., Diaz-Trivino S., Cisneros N., Gutierrez C.
    Plant Cell 18:2224-2235(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, SUBUNIT, INTERACTION WITH E2FC.
  11. "The Arabidopsis cell cycle F-Box protein SKP2A binds to auxin."
    Jurado S., Abraham Z., Manzano C., Lopez-Torrejon G., Pacios L.F., Del Pozo J.C.
    Plant Cell 22:3891-3904(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SKP2A.

Entry informationi

Entry nameiDPB_ARATH
AccessioniPrimary (citable) accession number: Q9FNY2
Secondary accession number(s): Q8LDG3, Q9LZE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.