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Protein

Protein hairy

Gene

h

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

Functioni

Pair-rule protein that regulates embryonic segmentation and adult bristle patterning. Transcriptional repressor of genes that require a bHLH protein for their transcription (e.g. the Fushi tarazu gene).1 Publication

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • E-box binding Source: FlyBase
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: FlyBase
  • transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: FlyBase
  • transcription factor binding Source: FlyBase

GO - Biological processi

  • cell morphogenesis Source: FlyBase
  • chaeta morphogenesis Source: FlyBase
  • membrane organization Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • nervous system development Source: FlyBase
  • open tracheal system development Source: FlyBase
  • periodic partitioning by pair rule gene Source: FlyBase
  • posterior head segmentation Source: FlyBase
  • R8 cell fate commitment Source: FlyBase
  • regulation of cellular metabolic process Source: FlyBase
  • response to hypoxia Source: FlyBase
  • salivary gland development Source: FlyBase
  • salivary gland morphogenesis Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
  • trunk segmentation Source: FlyBase
  • tube morphogenesis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Pair-rule protein, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

SignaLinkiP14003.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein hairy
Gene namesi
Name:h
ORF Names:CG6494
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0001168. h.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Protein hairyPRO_0000127181Add
BLAST

Post-translational modificationi

Ubiquitinated by Topors.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiP14003.

Expressioni

Gene expression databases

BgeeiP14003.
GenevisibleiP14003. DM.

Interactioni

Subunit structurei

Transcription repression requires formation of a complex with a corepressor protein (Groucho). Interacts with gro (via WPRW motif) and Topors.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CtBPO460364EBI-123011,EBI-159330
dgrnQ9VNJ05EBI-123011,EBI-186615
groP163713EBI-123011,EBI-153866
ToporsQ9V8P94EBI-123011,EBI-147805
UbxP839493EBI-123011,EBI-202590

GO - Molecular functioni

  • transcription factor binding Source: FlyBase

Protein-protein interaction databases

BioGridi64402. 11 interactions.
DIPiDIP-637N.
IntActiP14003. 8 interactions.
MINTiMINT-1542874.
STRINGi7227.FBpp0099504.

Structurei

3D structure databases

ProteinModelPortaliP14003.
SMRiP14003. Positions 23-92.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 8858bHLHPROSITE-ProRule annotationAdd
BLAST
Domaini107 – 13630OrangePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni29 – 4820Interaction with ToporsAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi334 – 3374WRPW motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi149 – 1579Gln-rich
Compositional biasi222 – 23716Gln-richAdd
BLAST
Compositional biasi241 – 25010Poly-Ala

Domaini

Has a particular type of basic domain (presence of a helix-interrupting proline) that binds to the N-box (CACNAG), rather than the canonical E-box (CANNTG).
The C-terminal WRPW motif is a transcriptional repression domain necessary for the interaction with Groucho, a transcriptional corepressor recruited to specific target DNA by Hairy-related proteins.

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation
Contains 1 Orange domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4304. Eukaryota.
ENOG4111F0X. LUCA.
GeneTreeiENSGT00700000104168.
InParanoidiP14003.
KOiK09090.
OMAiEEQPWRP.
OrthoDBiEOG780RN7.
PhylomeDBiP14003.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR003650. Orange_dom.
[Graphical view]
PfamiPF07527. Hairy_orange. 1 hit.
PF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
SM00511. ORANGE. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
PS51054. ORANGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14003-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTGVTAANM TNVLGTAVVP AQLKETPLKS DRRSNKPIME KRRRARINNC
60 70 80 90 100
LNELKTLILD ATKKDPARHS KLEKADILEK TVKHLQELQR QQAAMQQAAD
110 120 130 140 150
PKIVNKFKAG FADCVNEVSR FPGIEPAQRR RLLQHLSNCI NGVKTELHQQ
160 170 180 190 200
QRQQQQQSIH AQMLPSPPSS PEQDSQQGAA APYLFGIQQT ASGYFLPNGM
210 220 230 240 250
QVIPTKLPNG SIALVLPQSL PQQQQQQLLQ HQQQQQQLAV AAAAAAAAAA
260 270 280 290 300
QQQPMLVSMP QRTASTGSAS SHSSAGYESA PGSSSSCSYA PPSPANSSYE
310 320 330
PMDIKPSVIQ RVPMEQQPLS LVIKKQIKEE EQPWRPW
Length:337
Mass (Da):37,005
Last modified:April 18, 2006 - v2
Checksum:i49BECAF7F2D69FC4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211A → S in strain: R3-6, R3-105 and R3-107. 1 Publication
Natural varianti292 – 2921P → S.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15904 Genomic DNA. Translation: CAA34018.1.
X15905 mRNA. Translation: CAA34019.1.
AY055833 Genomic DNA. Translation: AAL17767.1.
AY055834 Genomic DNA. Translation: AAL17768.1.
AY055835 Genomic DNA. Translation: AAL17769.1.
AY055836 Genomic DNA. Translation: AAL17770.1.
AY055837 Genomic DNA. Translation: AAL17771.1.
AY055838 Genomic DNA. Translation: AAL17772.1.
AY055839 Genomic DNA. Translation: AAL17773.1.
AY055840 Genomic DNA. Translation: AAL17774.1.
AY055841 Genomic DNA. Translation: AAL17775.1.
AY055842 Genomic DNA. Translation: AAL17776.1.
AE014296 Genomic DNA. Translation: AAF50378.1.
AE014296 Genomic DNA. Translation: AAX52752.1.
AY119633 mRNA. Translation: AAM50287.1.
PIRiS06956.
RefSeqiNP_001014577.1. NM_001014577.2.
NP_523977.2. NM_079253.4.
UniGeneiDm.2554.

Genome annotation databases

EnsemblMetazoaiFBtr0076569; FBpp0076296; FBgn0001168.
FBtr0100153; FBpp0099504; FBgn0001168.
GeneIDi38995.
KEGGidme:Dmel_CG6494.
UCSCiCG6494-RA. d. melanogaster.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15904 Genomic DNA. Translation: CAA34018.1.
X15905 mRNA. Translation: CAA34019.1.
AY055833 Genomic DNA. Translation: AAL17767.1.
AY055834 Genomic DNA. Translation: AAL17768.1.
AY055835 Genomic DNA. Translation: AAL17769.1.
AY055836 Genomic DNA. Translation: AAL17770.1.
AY055837 Genomic DNA. Translation: AAL17771.1.
AY055838 Genomic DNA. Translation: AAL17772.1.
AY055839 Genomic DNA. Translation: AAL17773.1.
AY055840 Genomic DNA. Translation: AAL17774.1.
AY055841 Genomic DNA. Translation: AAL17775.1.
AY055842 Genomic DNA. Translation: AAL17776.1.
AE014296 Genomic DNA. Translation: AAF50378.1.
AE014296 Genomic DNA. Translation: AAX52752.1.
AY119633 mRNA. Translation: AAM50287.1.
PIRiS06956.
RefSeqiNP_001014577.1. NM_001014577.2.
NP_523977.2. NM_079253.4.
UniGeneiDm.2554.

3D structure databases

ProteinModelPortaliP14003.
SMRiP14003. Positions 23-92.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64402. 11 interactions.
DIPiDIP-637N.
IntActiP14003. 8 interactions.
MINTiMINT-1542874.
STRINGi7227.FBpp0099504.

Proteomic databases

PaxDbiP14003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076569; FBpp0076296; FBgn0001168.
FBtr0100153; FBpp0099504; FBgn0001168.
GeneIDi38995.
KEGGidme:Dmel_CG6494.
UCSCiCG6494-RA. d. melanogaster.

Organism-specific databases

CTDi38995.
FlyBaseiFBgn0001168. h.

Phylogenomic databases

eggNOGiKOG4304. Eukaryota.
ENOG4111F0X. LUCA.
GeneTreeiENSGT00700000104168.
InParanoidiP14003.
KOiK09090.
OMAiEEQPWRP.
OrthoDBiEOG780RN7.
PhylomeDBiP14003.

Enzyme and pathway databases

SignaLinkiP14003.

Miscellaneous databases

GenomeRNAii38995.
PROiP14003.

Gene expression databases

BgeeiP14003.
GenevisibleiP14003. DM.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR003650. Orange_dom.
[Graphical view]
PfamiPF07527. Hairy_orange. 1 hit.
PF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
SM00511. ORANGE. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
PS51054. ORANGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila hairy protein acts in both segmentation and bristle patterning and shows homology to N-myc."
    Rushlow C.A., Hogan A., Pierchin S.M., Howe K.M., Lardelli M., Ish-Horowicz D.
    EMBO J. 8:3095-3103(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT SER-292.
    Strain: Oregon-R.
  2. "hairy. A quantitative trait locus for Drosophila sensory bristle number."
    Robin C., Lyman R.F., Long A.D., Langley C.H., Mackay T.F.C.
    Genetics 162:155-164(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-21.
    Strain: R3-105, R3-107, R3-19, R3-2, R3-24, R3-48, R3-53, R3-6, R3-74 and R3-95.
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Groucho is required for Drosophila neurogenesis, segmentation, and sex determination and interacts directly with hairy-related bHLH proteins."
    Paroush Z., Finley R.L. Jr., Kidd T., Wainwright S.M., Ingham P.W., Brent R., Ish-Horowicz D.
    Cell 79:805-815(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN WRPW MOTIF.
  7. "The WRPW motif of the hairy-related basic helix-loop-helix repressor proteins acts as a 4-amino-acid transcription repression and protein-protein interaction domain."
    Fisher A.L., Ohsako S., Caudy M.
    Mol. Cell. Biol. 16:2670-2677(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GRO, DOMAIN WRPW MOTIF.
  8. "Drosophila Topors is a RING finger-containing protein that functions as a ubiquitin-protein isopeptide ligase for the hairy basic helix-loop-helix repressor protein."
    Secombe J., Parkhurst S.M.
    J. Biol. Chem. 279:17126-17133(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, INTERACTION WITH TOPORS, UBIQUITINATION.

Entry informationi

Entry nameiHAIR_DROME
AccessioniPrimary (citable) accession number: P14003
Secondary accession number(s): A4V1N7
, Q95NH3, Q95NU9, Q9VSN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: April 18, 2006
Last modified: June 8, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.