Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Segmentation polarity homeobox protein engrailed

Gene

en

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This protein specifies the body segmentation pattern. It is required for the development of the central nervous system. Transcriptional regulator that represses activated promoters. Wg signaling operates by inactivating the SGG repression of EN autoactivation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi454 – 51360HomeoboxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • enhancer sequence-specific DNA binding Source: FlyBase
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: FlyBase
  • sequence-specific DNA binding Source: FlyBase
  • transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: FlyBase

GO - Biological processi

  • analia development Source: FlyBase
  • anterior/posterior lineage restriction, imaginal disc Source: FlyBase
  • anterior/posterior pattern specification, imaginal disc Source: FlyBase
  • anterior commissure morphogenesis Source: FlyBase
  • anterior head segmentation Source: FlyBase
  • axon guidance Source: FlyBase
  • central nervous system development Source: FlyBase
  • compartment pattern specification Source: FlyBase
  • genital disc anterior/posterior pattern formation Source: FlyBase
  • genital disc development Source: FlyBase
  • gonad development Source: FlyBase
  • imaginal disc-derived female genitalia development Source: FlyBase
  • imaginal disc-derived male genitalia development Source: FlyBase
  • imaginal disc-derived wing vein specification Source: FlyBase
  • imaginal disc pattern formation Source: FlyBase
  • negative regulation of gene expression Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: FlyBase
  • negative regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • neuroblast fate determination Source: FlyBase
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • posterior compartment specification Source: FlyBase
  • posterior head segmentation Source: FlyBase
  • regulation of gene expression Source: FlyBase
  • segment polarity determination Source: FlyBase
  • spiracle morphogenesis, open tracheal system Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
  • trunk segmentation Source: FlyBase
  • ventral midline development Source: FlyBase
  • wing disc anterior/posterior pattern formation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Repressor, Segmentation polarity protein

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

SignaLinkiP02836.

Names & Taxonomyi

Protein namesi
Recommended name:
Segmentation polarity homeobox protein engrailed
Gene namesi
Name:en
ORF Names:CG9015
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0000577. en.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

  • nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi508 – 5081K → Q: Reduced specificity and affinity for DNA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 552552Segmentation polarity homeobox protein engrailedPRO_0000196077Add
BLAST

Post-translational modificationi

Phosphorylated. Phosphorylation may directly or allosterically modify its function.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP02836.

PTM databases

iPTMnetiP02836.

Expressioni

Developmental stagei

Expression initiates prior to the ninth embryonic nuclear division cycle within 1.5 hours after fertilization. By the cellular blastoderm stage (the 14th nuclear division cycle) is localized into 14 stripes, 1-2 cells wide, spaced along the anterior-posterior axis of the embryo.

Gene expression databases

BgeeiP02836.
ExpressionAtlasiP02836. differential.
GenevisibleiP02836. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CG4617Q9W3S41EBI-121995,EBI-102894
CG6506Q9VX121EBI-121995,EBI-159142

Protein-protein interaction databases

BioGridi62028. 16 interactions.
IntActiP02836. 2 interactions.
MINTiMINT-310169.
STRINGi7227.FBpp0087197.

Structurei

Secondary structure

1
552
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni453 – 4553Combined sources
Beta strandi458 – 4603Combined sources
Helixi463 – 47513Combined sources
Helixi481 – 49111Combined sources
Helixi495 – 51016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DU0X-ray2.00A/B456-512[»]
1ENHX-ray2.10A456-509[»]
1HDDX-ray2.80C/D453-512[»]
1P7IX-ray2.10A/B/C/D454-512[»]
1P7JX-ray2.10A/B/C/D454-512[»]
1ZTRNMR-A453-512[»]
2HDDX-ray1.90A/B454-512[»]
2HOSX-ray1.90A/B453-513[»]
2HOTX-ray2.19A/B453-513[»]
2JWTNMR-A453-512[»]
2P81NMR-A469-512[»]
3HDDX-ray2.20A/B454-513[»]
ProteinModelPortaliP02836.
SMRiP02836. Positions 456-509.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02836.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi19 – 5335Gln-richAdd
BLAST
Compositional biasi55 – 8733Ala-richAdd
BLAST
Compositional biasi232 – 2409Ala-rich
Compositional biasi320 – 41192Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the engrailed homeobox family.Curated
Contains 1 homeobox DNA-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Homeobox

Phylogenomic databases

eggNOGiKOG0493. Eukaryota.
ENOG4111P06. LUCA.
GeneTreeiENSGT00840000129733.
InParanoidiP02836.
KOiK09319.
OMAiDTRSETG.
OrthoDBiEOG7VTDN8.
PhylomeDBiP02836.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR019549. Homeobox-engrailed_C-terminal.
IPR017970. Homeobox_CS.
IPR001356. Homeobox_dom.
IPR020479. Homeobox_metazoa.
IPR009057. Homeodomain-like.
IPR000747. Homeodomain_engrailed.
IPR019737. Homoebox-engrailed_CS.
IPR000047. HTH_motif.
[Graphical view]
PfamiPF10525. Engrail_1_C_sig. 1 hit.
PF00046. Homeobox. 1 hit.
[Graphical view]
PRINTSiPR00026. ENGRAILED.
PR00024. HOMEOBOX.
PR00031. HTHREPRESSR.
SMARTiSM00389. HOX. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS00033. ENGRAILED. 1 hit.
PS00027. HOMEOBOX_1. 1 hit.
PS50071. HOMEOBOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02836-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALEDRCSPQ SAPSPITLQM QHLHHQQQQQ QQQQQQMQHL HQLQQLQQLH
60 70 80 90 100
QQQLAAGVFH HPAMAFDAAA AAAAAAAAAA AHAHAAALQQ RLSGSGSPAS
110 120 130 140 150
CSTPASSTPL TIKEEESDSV IGDMSFHNQT HTTNEEEEAE EDDDIDVDVD
160 170 180 190 200
DTSAGGRLPP PAHQQQSTAK PSLAFSISNI LSDRFGDVQK PGKSMENQAS
210 220 230 240 250
IFRPFEASRS QTATPSAFTR VDLLEFSRQQ QAAAAAATAA MMLERANFLN
260 270 280 290 300
CFNPAAYPRI HEEIVQSRLR RSAANAVIPP PMSSKMSDAN PEKSALGSLC
310 320 330 340 350
KAVSQIGQPA APTMTQPPLS SSASSLASPP PASNASTISS TSSVATSSSS
360 370 380 390 400
SSSGCSSAAS SLNSSPSSRL GASGSGVNAS SPQPQPIPPP SAVSRDSGME
410 420 430 440 450
SSDDTRSETG STTTEGGKNE MWPAWVYCTR YSDRPSSGPR YRRPKQPKDK
460 470 480 490 500
TNDEKRPRTA FSSEQLARLK REFNENRYLT ERRRQQLSSE LGLNEAQIKI
510 520 530 540 550
WFQNKRAKIK KSTGSKNPLA LQLMAQGLYN HTTVPLTKEE EELEMRMNGQ

IP
Length:552
Mass (Da):59,411
Last modified:February 2, 2004 - v2
Checksum:i92A94C14AA85C527
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1951M → I in AAA65478 (PubMed:3917855).Curated
Sequence conflicti208 – 2081S → N in AAA65478 (PubMed:3917855).Curated
Sequence conflicti486 – 4861Q → E in CAA25906 (PubMed:2481829).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10017 mRNA. Translation: AAA65478.1.
K03055 Genomic DNA. No translation available.
K03056 Genomic DNA. No translation available.
AE013599 Genomic DNA. Translation: AAF58639.1.
AY069448 mRNA. Translation: AAL39593.1.
X01765 Genomic DNA. Translation: CAA25906.1.
PIRiA90862. WJFFEN.
RefSeqiNP_523700.2. NM_078976.4.
NP_725059.1. NM_165841.2.
UniGeneiDm.22056.

Genome annotation databases

EnsemblMetazoaiFBtr0088095; FBpp0087197; FBgn0000577.
FBtr0088096; FBpp0087198; FBgn0000577.
GeneIDi36240.
KEGGidme:Dmel_CG9015.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10017 mRNA. Translation: AAA65478.1.
K03055 Genomic DNA. No translation available.
K03056 Genomic DNA. No translation available.
AE013599 Genomic DNA. Translation: AAF58639.1.
AY069448 mRNA. Translation: AAL39593.1.
X01765 Genomic DNA. Translation: CAA25906.1.
PIRiA90862. WJFFEN.
RefSeqiNP_523700.2. NM_078976.4.
NP_725059.1. NM_165841.2.
UniGeneiDm.22056.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DU0X-ray2.00A/B456-512[»]
1ENHX-ray2.10A456-509[»]
1HDDX-ray2.80C/D453-512[»]
1P7IX-ray2.10A/B/C/D454-512[»]
1P7JX-ray2.10A/B/C/D454-512[»]
1ZTRNMR-A453-512[»]
2HDDX-ray1.90A/B454-512[»]
2HOSX-ray1.90A/B453-513[»]
2HOTX-ray2.19A/B453-513[»]
2JWTNMR-A453-512[»]
2P81NMR-A469-512[»]
3HDDX-ray2.20A/B454-513[»]
ProteinModelPortaliP02836.
SMRiP02836. Positions 456-509.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62028. 16 interactions.
IntActiP02836. 2 interactions.
MINTiMINT-310169.
STRINGi7227.FBpp0087197.

PTM databases

iPTMnetiP02836.

Proteomic databases

PaxDbiP02836.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088095; FBpp0087197; FBgn0000577.
FBtr0088096; FBpp0087198; FBgn0000577.
GeneIDi36240.
KEGGidme:Dmel_CG9015.

Organism-specific databases

CTDi36240.
FlyBaseiFBgn0000577. en.

Phylogenomic databases

eggNOGiKOG0493. Eukaryota.
ENOG4111P06. LUCA.
GeneTreeiENSGT00840000129733.
InParanoidiP02836.
KOiK09319.
OMAiDTRSETG.
OrthoDBiEOG7VTDN8.
PhylomeDBiP02836.

Enzyme and pathway databases

SignaLinkiP02836.

Miscellaneous databases

EvolutionaryTraceiP02836.
GenomeRNAii36240.
NextBioi797500.
PROiP02836.

Gene expression databases

BgeeiP02836.
ExpressionAtlasiP02836. differential.
GenevisibleiP02836. DM.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR019549. Homeobox-engrailed_C-terminal.
IPR017970. Homeobox_CS.
IPR001356. Homeobox_dom.
IPR020479. Homeobox_metazoa.
IPR009057. Homeodomain-like.
IPR000747. Homeodomain_engrailed.
IPR019737. Homoebox-engrailed_CS.
IPR000047. HTH_motif.
[Graphical view]
PfamiPF10525. Engrail_1_C_sig. 1 hit.
PF00046. Homeobox. 1 hit.
[Graphical view]
PRINTSiPR00026. ENGRAILED.
PR00024. HOMEOBOX.
PR00031. HTHREPRESSR.
SMARTiSM00389. HOX. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS00033. ENGRAILED. 1 hit.
PS00027. HOMEOBOX_1. 1 hit.
PS50071. HOMEOBOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The engrailed locus of Drosophila: structural analysis of an embryonic transcript."
    Poole S.J., Kauvar L.M., Drees B., Kornberg T.
    Cell 40:37-43(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Embryo.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Isolation of a homoeo box-containing gene from the engrailed region of Drosophila and the spatial distribution of its transcripts."
    Fjose A., McGinnis W., Gehring W.J.
    Nature 313:284-289(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 443-518.
  6. "Functional domains of the Drosophila Engrailed protein."
    Han K., Manley J.L.
    EMBO J. 12:2723-2733(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "The Drosophila engrailed protein is phosphorylated by a serine-specific protein kinase."
    Gay N.J., Poole S.J., Kornberg T.B.
    Nucleic Acids Res. 16:6637-6647(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  8. "Development of embryonic pattern in D. melanogaster as revealed by accumulation of the nuclear engrailed protein."
    Dinardo S., Kuner J.M., Theis J., O'Farrell P.H.
    Cell 43:59-69(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "wingless signaling acts through zeste-white 3, the Drosophila homolog of glycogen synthase kinase-3, to regulate engrailed and establish cell fate."
    Siegfried E., Chou T.B., Perrimon N.
    Cell 71:1167-1179(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WG AND EN.
    Tissue: Embryo.
  10. "Crystal structure of an engrailed homeodomain-DNA complex at 2.8-A resolution: a framework for understanding homeodomain-DNA interactions."
    Kissinger C.R., Liu B., Martin-Blanco E., Kornberg T.B., Pabo C.O.
    Cell 63:579-590(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 453-512.
  11. "Engrailed (Gln50-->Lys) homeodomain-DNA complex at 1.9-A resolution: structural basis for enhanced affinity and altered specificity."
    Tucker-Kellogg L., Rould M.A., Chambers K.A., Ades S.E., Sauer R.T., Pabo C.O.
    Structure 5:1047-1054(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 458-512 OF MUTANT LYS-508.
  12. "Engrailed homeodomain-DNA complex at 2.2-A resolution: a detailed view of the interface and comparison with other engrailed structures."
    Fraenkel E., Rould M.A., Chambers K.A., Pabo C.O.
    J. Mol. Biol. 284:351-361(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 455-512.
  13. "Exploring the role of glutamine 50 in the homeodomain-DNA interface: crystal structure of engrailed (Gln50 --> Ala) complex at 2.0 A."
    Grant R.A., Rould M.A., Klemm J.D., Pabo C.O.
    Biochemistry 39:8187-8192(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 456-512.

Entry informationi

Entry nameiHMEN_DROME
AccessioniPrimary (citable) accession number: P02836
Secondary accession number(s): P02837
, Q0E9C0, Q24356, Q9V601
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 2, 2004
Last modified: May 11, 2016
This is version 178 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.