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Reviewed, UniProtKB/Swiss-Prot O24646 (HY5_ARATH)

Last modified February 9, 2010. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Transcription factor HY5
Alternative name(s):
    Protein LONG HYPOCOTYL 5
    bZIP transcription factor 56
      Short name=AtbZIP56
Gene names
Name: HY5
Synonyms: BZIP56
Ordered Locus Names: At5g11260
ORF Names: F2I11_150
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Transcription factor that promotes photomorphogenesis in the light. Acts downstream of the light receptor network and directly affects transcription of light-induced genes. Specifically involved in blue-light specific pathway, suggesting that it participates in transmission of cryptochromes (CRY1 and CRY2) signals to downstream responses. In darkness, its degradation prevent the activation of light-induced genes.

Subunit structure

Heterodimer; heterodimerizes with HYH via the leucine-zipper domains. Interacts with COP1 WD40 domain. Ref.5 Ref.8

Subcellular location

Nucleus.

Tissue specificity

Expressed in root, hypocotyl, cotyledon, leaf, stem and floral organs.

Post-translational modification

Phosphorylated by CK2. Shows a stronger interaction with COP1 when unphosphorylated. However, phosphorylation does not affect its susceptibility to be ubiquitinated. Ref.4 Ref.9 Ref.10

Ubiquitinated by COP1 and/or CIP8. Ubiquitination takes place in darkness and leads to its subsequent degradation, thereby preventing to activate photomorphogenesis signals. Ref.3 Ref.6

Sequence similarities

Belongs to the bZIP family.

Contains 1 bZIP domain.

Ontologies

Keywords
   Biological processPhytochrome signaling pathway
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processgibberellic acid mediated signaling pathway

Inferred from mutant phenotype. Source: TAIR

positive regulation of anthocyanin metabolic process

Inferred from mutant phenotype. Source: TAIR

red, far-red light phototransduction

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of photomorphogenesis

Inferred from mutant phenotype. Source: TAIR

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: InterPro

response to UV-B

Inferred from mutant phenotype. Source: TAIR

response to abscisic acid stimulus

Inferred from mutant phenotype. Source: TAIR

response to far red light

Inferred from expression pattern. Source: TAIR

response to red light

Inferred from expression pattern. Source: TAIR

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus Ref.1

Inferred from direct assay. Source: TAIR

   Molecular functiondouble-stranded DNA binding

Inferred from physical interaction. Source: TAIR

protein dimerization activity

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

transcription factor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 168168Transcription factor HY5
PRO_0000076560

Regions

Domain116 – 14429Leucine-zipper
DNA binding93 – 11018Basic motif
Region35 – 4612Interaction with COP1

Amino acid modifications

Modified residue361Phosphoserine Ref.9 Ref.10

Experimental info

Mutagenesis43 – 442VP → AA: Abolishes interaction with COP1. Ref.5

Secondary structure

... 168
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O24646-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 1E3C4672B192D8A9

FASTA16818,463
        10         20         30         40         50         60 
MQEQATSSLA ASSLPSSSER SSSSAPHLEI KEGIESDEEI RRVPEFGGEA VGKETSGRES 

        70         80         90        100        110        120 
GSATGQERTQ ATVGESQRKR GRTPAEKENK RLKRLLRNRV SAQQARERKK AYLSELENRV 

       130        140        150        160 
KDLENKNSEL EERLSTLQNE NQMLRHILKN TTGNKRGGGG GSNADASL 

« Hide

References

« Hide 'large scale' references
[1]"The Arabidopsis HY5 gene encodes a bZIP protein that regulates stimulus-induced development of root and hypocotyl."
Oyama T., Shimura Y., Okada K.
Genes Dev. 11:2983-2995(1997) [PubMed: 9367981] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Landsberg erecta.
Tissue: Seedling.
[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. expand/collapse author list , 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: 11130714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"Targeted destabilization of HY5 during light-regulated development of Arabidopsis."
Osterlund M.T., Hardtke C.S., Wei N., Deng X.-W.
Nature 405:462-466(2000) [PubMed: 10839542] [Abstract]
Cited for: UBIQUITINATION, SUBSEQUENT DEGRADATION.
[4]"HY5 stability and activity in Arabidopsis is regulated by phosphorylation in its COP1 binding domain."
Hardtke C.S., Gohda K., Osterlund M.T., Oyama T., Okada K., Deng X.-W.
EMBO J. 19:4997-5006(2000) [PubMed: 10990463] [Abstract]
Cited for: PHOSPHORYLATION.
[5]"Identification of a structural motif that confers specific interaction with the WD40 repeat domain of Arabidopsis COP1."
Holm M., Hardtke C.S., Gaudet R., Deng X.-W.
EMBO J. 20:118-127(2001) [PubMed: 11226162] [Abstract]
Cited for: INTERACTION WITH COP1, MUTAGENESIS OF 43-VAL-PRO-44.
Tissue: Etiolated seedling.
[6]"Biochemical evidence for ubiquitin ligase activity of the Arabidopsis COP1 interacting protein 8 (CIP8)."
Hardtke C.S., Okamoto H., Stoop-Myer C., Deng X.-W.
Plant J. 30:385-394(2002) [PubMed: 12028569] [Abstract]
Cited for: UBIQUITINATION BY CIP8.
[7]"bZIP transcription factors in Arabidopsis."
Jakoby M., Weisshaar B., Droege-Laser W., Vicente-Carbajosa J., Tiedemann J., Kroj T., Parcy F.
Trends Plant Sci. 7:106-111(2002) [PubMed: 11906833] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[8]"Two interacting bZIP proteins are direct targets of COP1-mediated control of light-dependent gene expression in Arabidopsis."
Holm M., Ma L.-G., Qu L.-J., Deng X.-W.
Genes Dev. 16:1247-1259(2002) [PubMed: 12023303] [Abstract]
Cited for: HETERODIMERIZATION.
[9]"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis."
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.
J. Proteome Res. 7:2458-2470(2008) [PubMed: 18433157] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY.
[10]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY.
Tissue: Seedling.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB005456 mRNA. Translation: BAA21327.1.
AB005295 mRNA. Translation: BAA21116.1.
AL360314 Genomic DNA. Translation: CAB96661.1.
IPIIPI00535293.
PIRT50922.
RefSeqNP_568246.1.
UniGeneAt.20257

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OQQX-ray2.00A/B111-150[»]
DisProtDP00469.
ModBaseSearch...

Protein-protein interaction databases

IntActO24646. 7 interactions.
STRINGO24646.

Proteomic databases

PRIDEO24646.

Genome annotation databases

GeneID830996.
GenomeReviewsGene locus AT5G11260 in contig BA000015_GR.
KEGGath:AT5G11260.

Organism-specific databases

TAIRAt5g11260.

Phylogenomic databases

eggNOGKOG1414.
HOGENOMHBG316354.
InParanoidO24646.
OMARKKAYLS.

Gene expression databases

ArrayExpressO24646.
GenevestigatorO24646.
GermOnlineAT5G11260. Arabidopsis thaliana.

Family and domain databases

InterProIPR011616. bZIP_1.
IPR001630. Leuzip_CREB.
IPR004827. TF_bZIP.
[Graphical view]
PfamPF00170. bZIP_1. 1 hit.
[Graphical view]
PRINTSPR00041. LEUZIPPRCREB.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHY5_ARATH
AccessionPrimary (citable) accession number: O24646
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 1, 1998
Last modified: February 9, 2010
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents