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Protein

Transcription factor HY5

Gene

HY5

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

Functioni

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

GO - Molecular functioni

  • DNA binding Source: TAIR
  • double-stranded DNA binding Source: TAIR
  • sequence-specific DNA binding Source: InterPro
  • transcription factor activity, sequence-specific DNA binding Source: TAIR

GO - Biological processi

  • gibberellic acid mediated signaling pathway Source: TAIR
  • positive regulation of anthocyanin metabolic process Source: TAIR
  • positive regulation of circadian rhythm Source: TAIR
  • red, far-red light phototransduction Source: UniProtKB-KW
  • red or far-red light signaling pathway Source: TAIR
  • regulation of photomorphogenesis Source: TAIR
  • response to abscisic acid Source: TAIR
  • response to far red light Source: TAIR
  • response to karrikin Source: TAIR
  • response to red light Source: TAIR
  • response to UV-B Source: TAIR
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Phytochrome signaling pathway, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor HY5
Alternative name(s):
Protein LONG HYPOCOTYL 5
bZIP transcription factor 56
Short name:
AtbZIP56
Gene namesi
Name:HY5
Synonyms:BZIP56
Ordered Locus Names:At5g11260
ORF Names:F2I11_150
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G11260.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi43 – 442VP → AA: Abolishes interaction with COP1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 168168Transcription factor HY5PRO_0000076560Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by CK2. Shows a stronger interaction with COP1 when unphosphorylated. However, phosphorylation does not affect its susceptibility to be ubiquitinated.1 Publication
Ubiquitinated by COP1 and/or CIP8. Ubiquitination takes place in darkness and leads to its subsequent degradation, thereby preventing activation of photomorphogenesis signals.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO24646.
PRIDEiO24646.

PTM databases

iPTMnetiO24646.

Expressioni

Tissue specificityi

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

Gene expression databases

ExpressionAtlasiO24646. baseline and differential.
GenevisibleiO24646. AT.

Interactioni

Subunit structurei

Homodimer; homodimerizes via the leucine-zipper domains (PubMed:17261584). Heterodimer; heterodimerizes with HYH via the leucine-zipper domains (PubMed:12023303). Interacts with COP1 WD40 domain (PubMed:11226162). Interacts with BBX21 (PubMed:21632973), BBX24/STO (PubMed:23733077) and BBX25/STH (PubMed:23624715).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BBX21Q9LQZ72EBI-301660,EBI-1994459
BBX22Q9SYM23EBI-301660,EBI-1994217
COP1P432548EBI-301660,EBI-301649

Protein-protein interaction databases

BioGridi16274. 40 interactions.
IntActiO24646. 6 interactions.
MINTiMINT-1536182.
STRINGi3702.AT5G11260.1.

Structurei

Secondary structure

1
168
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi111 – 14939Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OQQX-ray2.00A/B111-150[»]
DisProtiDP00469.
ProteinModelPortaliO24646.
SMRiO24646. Positions 111-150.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO24646.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 15164bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 4612Interaction with COP1Add
BLAST
Regioni90 – 11021Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni116 – 14429Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the bZIP family.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1414. Eukaryota.
ENOG4111CH5. LUCA.
HOGENOMiHOG000272717.
InParanoidiO24646.
KOiK16241.
OMAiRSHADKE.
PhylomeDBiO24646.

Family and domain databases

InterProiIPR004827. bZIP.
IPR001630. Leuzip_CREB.
[Graphical view]
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
PRINTSiPR00041. LEUZIPPRCREB.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O24646-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQEQATSSLA ASSLPSSSER SSSSAPHLEI KEGIESDEEI RRVPEFGGEA
60 70 80 90 100
VGKETSGRES GSATGQERTQ ATVGESQRKR GRTPAEKENK RLKRLLRNRV
110 120 130 140 150
SAQQARERKK AYLSELENRV KDLENKNSEL EERLSTLQNE NQMLRHILKN
160
TTGNKRGGGG GSNADASL
Length:168
Mass (Da):18,463
Last modified:January 1, 1998 - v1
Checksum:i1E3C4672B192D8A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005456 mRNA. Translation: BAA21327.1.
AB005295 mRNA. Translation: BAA21116.1.
AL360314 Genomic DNA. Translation: CAB96661.1.
CP002688 Genomic DNA. Translation: AED91653.1.
PIRiT50922.
RefSeqiNP_568246.1. NM_121164.4.
UniGeneiAt.20257.

Genome annotation databases

EnsemblPlantsiAT5G11260.1; AT5G11260.1; AT5G11260.
GeneIDi830996.
GrameneiAT5G11260.1; AT5G11260.1; AT5G11260.
KEGGiath:AT5G11260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005456 mRNA. Translation: BAA21327.1.
AB005295 mRNA. Translation: BAA21116.1.
AL360314 Genomic DNA. Translation: CAB96661.1.
CP002688 Genomic DNA. Translation: AED91653.1.
PIRiT50922.
RefSeqiNP_568246.1. NM_121164.4.
UniGeneiAt.20257.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OQQX-ray2.00A/B111-150[»]
DisProtiDP00469.
ProteinModelPortaliO24646.
SMRiO24646. Positions 111-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi16274. 40 interactions.
IntActiO24646. 6 interactions.
MINTiMINT-1536182.
STRINGi3702.AT5G11260.1.

PTM databases

iPTMnetiO24646.

Proteomic databases

PaxDbiO24646.
PRIDEiO24646.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G11260.1; AT5G11260.1; AT5G11260.
GeneIDi830996.
GrameneiAT5G11260.1; AT5G11260.1; AT5G11260.
KEGGiath:AT5G11260.

Organism-specific databases

TAIRiAT5G11260.

Phylogenomic databases

eggNOGiKOG1414. Eukaryota.
ENOG4111CH5. LUCA.
HOGENOMiHOG000272717.
InParanoidiO24646.
KOiK16241.
OMAiRSHADKE.
PhylomeDBiO24646.

Miscellaneous databases

EvolutionaryTraceiO24646.
PROiO24646.

Gene expression databases

ExpressionAtlasiO24646. baseline and differential.
GenevisibleiO24646. AT.

Family and domain databases

InterProiIPR004827. bZIP.
IPR001630. Leuzip_CREB.
[Graphical view]
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
PRINTSiPR00041. LEUZIPPRCREB.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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. "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] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, SUBSEQUENT DEGRADATION.
  5. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  6. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COP1, MUTAGENESIS OF 43-VAL-PRO-44.
    Tissue: Etiolated seedling.
  7. "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] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY CIP8.
  8. Cited for: GENE FAMILY, NOMENCLATURE.
  9. "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] [Europe PMC] [Abstract]
    Cited for: HETERODIMERIZATION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Root.
  11. "BBX32, an Arabidopsis B-Box protein, functions in light signaling by suppressing HY5-regulated gene expression and interacting with STH2/BBX21."
    Holtan H.E., Bandong S., Marion C.M., Adam L., Tiwari S., Shen Y., Maloof J.N., Maszle D.R., Ohto M.A., Preuss S., Meister R., Petracek M., Repetti P.P., Reuber T.L., Ratcliffe O.J., Khanna R.
    Plant Physiol. 156:2109-2123(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BBX21.
  12. "The Arabidopsis B-BOX protein BBX25 interacts with HY5, negatively regulating BBX22 expression to suppress seedling photomorphogenesis."
    Gangappa S.N., Crocco C.D., Johansson H., Datta S., Hettiarachchi C., Holm M., Botto J.F.
    Plant Cell 25:1243-1257(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BBX25/STH.
  13. "Molecular interactions of BBX24 and BBX25 with HYH, HY5 HOMOLOG, to modulate Arabidopsis seedling development."
    Gangappa S.N., Holm M., Botto J.F.
    Plant Signal. Behav. 8:0-0(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BBX24/STO.
  14. "Structural basis for the conformational integrity of the Arabidopsis thaliana HY5 leucine zipper homodimer."
    Yoon M.K., Kim H.M., Choi G., Lee J.O., Choi B.S.
    J. Biol. Chem. 282:12989-13002(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 11-150, HOMODIMERIZATION.

Entry informationi

Entry nameiHY5_ARATH
AccessioniPrimary (citable) accession number: O24646
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 1, 1998
Last modified: April 13, 2016
This is version 141 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.