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Protein

Early E2A DNA-binding protein

Gene

DBP

Organism
Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Binds cooperatively single-stranded DNA in a sequence-independent manner. Involved in DNA-replication, regulation of mRNA formation, and host-range specificity. Zinc is required for DNA binding.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri273 – 28614Sequence AnalysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Early E2A DNA-binding protein
Gene namesi
Name:DBP
OrganismiHuman adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Taxonomic identifieri28285 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000004992 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

  • host cell nucleus Source: UniProtKB-SubCell
  • viral capsid Source: CACAO
Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Early E2A DNA-binding proteinPRO_0000221679Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei195 – 1951PhosphotyrosineCurated

Keywords - PTMi

Phosphoprotein

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Interacts with human SRCAP.By similarity

Protein-protein interaction databases

IntActiP03265. 5 interactions.
MINTiMINT-216016.

Structurei

Secondary structure

1
529
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi180 – 19415Combined sources
Helixi199 – 2046Combined sources
Helixi213 – 22614Combined sources
Helixi237 – 25620Combined sources
Beta strandi268 – 2725Combined sources
Beta strandi275 – 2784Combined sources
Beta strandi287 – 2893Combined sources
Beta strandi291 – 2977Combined sources
Beta strandi331 – 3388Combined sources
Helixi340 – 3423Combined sources
Beta strandi343 – 3464Combined sources
Beta strandi358 – 3603Combined sources
Helixi362 – 37918Combined sources
Beta strandi389 – 3946Combined sources
Helixi397 – 3993Combined sources
Beta strandi401 – 4033Combined sources
Beta strandi415 – 4195Combined sources
Turni421 – 4244Combined sources
Helixi428 – 4303Combined sources
Helixi434 – 4418Combined sources
Beta strandi444 – 4496Combined sources
Beta strandi470 – 4723Combined sources
Helixi473 – 48816Combined sources
Beta strandi491 – 4933Combined sources
Helixi506 – 5083Combined sources
Beta strandi524 – 5263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ADUX-ray3.00A/B174-529[»]
1ADVX-ray3.20A/B174-529[»]
1ANVX-ray2.70A174-529[»]
2WAZX-ray2.30X174-529[»]
2WB0X-ray1.95X174-529[»]
DisProtiDP00003.
ProteinModelPortaliP03265.
SMRiP03265. Positions 179-529.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03265.

Family & Domainsi

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri273 – 28614Sequence AnalysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Family and domain databases

Gene3Di1.10.269.10. 1 hit.
3.90.148.10. 2 hits.
InterProiIPR005376. Adenovirus_DNA-bd_C.
IPR003176. Adenovirus_DNA-bd_N.
[Graphical view]
PfamiPF02236. Viral_DNA_bi. 1 hit.
PF03728. Viral_DNA_Zn_bi. 2 hits.
[Graphical view]
SUPFAMiSSF47724. SSF47724. 1 hit.
SSF57917. SSF57917. 2 hits.

Sequencei

Sequence statusi: Complete.

P03265-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASREEEQRE TTPERGRGAA RRPPTMEDVS SPSPSPPPPR APPKKRMRRR
60 70 80 90 100
IESEDEEDSS QDALVPRTPS PRPSTSAADL AIAPKKKKKR PSPKPERPPS
110 120 130 140 150
PEVIVDSEEE REDVALQMVG FSNPPVLIKH GKGGKRTVRR LNEDDPVARG
160 170 180 190 200
MRTQEEEEEP SEAESEITVM NPLSVPIVSA WEKGMEAARA LMDKYHVDND
210 220 230 240 250
LKANFKLLPD QVEALAAVCK TWLNEEHRGL QLTFTSKKTF VTMMGRFLQA
260 270 280 290 300
YLQSFAEVTY KHHEPTGCAL WLHRCAEIEG ELKCLHGSIM INKEHVIEMD
310 320 330 340 350
VTSENGQRAL KEQSSKAKIV KNRWGRNVVQ ISNTDARCCV HDAACPANQF
360 370 380 390 400
SGKSCGMFFS EGAKAQVAFK QIKAFMQALY PNAQTGHGHL LMPLRCECNS
410 420 430 440 450
KPGHAPFLGR QLPKLTPFAL SNAEDLDADL ISDKSVLASV HHPALIVFQC
460 470 480 490 500
CNPVYRNSRA QGGGPNCDFK ISAPDLLNAL VMVRSLWSEN FTELPRMVVP
510 520
EFKWSTKHQY RNVSLPVAHS DARQNPFDF
Length:529
Mass (Da):59,139
Last modified:July 21, 1986 - v1
Checksum:iAC1582B80F370E23
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73260 Genomic DNA. No translation available.
X02997 Genomic DNA. Translation: CAA26755.1. Sequence problems.
PIRiA03833. W7AD25.
RefSeqiAP_000213.1. AC_000008.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73260 Genomic DNA. No translation available.
X02997 Genomic DNA. Translation: CAA26755.1. Sequence problems.
PIRiA03833. W7AD25.
RefSeqiAP_000213.1. AC_000008.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ADUX-ray3.00A/B174-529[»]
1ADVX-ray3.20A/B174-529[»]
1ANVX-ray2.70A174-529[»]
2WAZX-ray2.30X174-529[»]
2WB0X-ray1.95X174-529[»]
DisProtiDP00003.
ProteinModelPortaliP03265.
SMRiP03265. Positions 179-529.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03265. 5 interactions.
MINTiMINT-216016.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP03265.

Family and domain databases

Gene3Di1.10.269.10. 1 hit.
3.90.148.10. 2 hits.
InterProiIPR005376. Adenovirus_DNA-bd_C.
IPR003176. Adenovirus_DNA-bd_N.
[Graphical view]
PfamiPF02236. Viral_DNA_bi. 1 hit.
PF03728. Viral_DNA_Zn_bi. 2 hits.
[Graphical view]
SUPFAMiSSF47724. SSF47724. 1 hit.
SSF57917. SSF57917. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and organization of the gene coding for the DNA binding protein of adenovirus type 5."
    Kruijer W., van Schaik F.M.A., Sussenbach J.S.
    Nucleic Acids Res. 9:4439-4457(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The sequence of the genome of adenovirus type 5 and its comparison with the genome of adenovirus type 2."
    Chroboczek J., Bieber F., Jacrot B.
    Virology 186:280-285(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding."
    Tucker P.A., Tsernoglou D., Tucker A.D., Coenjaerts F.E.J., Leenders H., van der Vliet P.C.
    EMBO J. 13:2994-3002(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 176-529.

Entry informationi

Entry nameiDNB2_ADE05
AccessioniPrimary (citable) accession number: P03265
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 7, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.