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

Ultraviolet-B receptor UVR8

Gene

UVR8

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

Functioni

UV-B specific signaling component that acts as UV-B photoreceptor and plays a key role in establishing UV-protective responses in plants. Upon UV-B irradiation, UVR8 undergoes an immediate switch from homodimer to monomer, accumulates in the nucleus, interacts with the photomorphogenic repressor COP1 and regulates the expression of the transcription factor HY5 by associating with chromatin (through histone H2B binding) in the HY5 promoter region. UVR8 is involved in controlling aspects of leaf growth and morphogenesis in response to UV-B, is required for normal progression of endocycle and has a regulatory role in stomatal differentiation. Is required for plant circadian clock response to photomorphogenic UV-B light, partly through the transcriptional activation of responsive clock genes. Promotes photosynthetic efficiency at elevated levels of UV-B. Plays a role in mediating the effects of UV-B radiation on pathogen resistance by controlling the expression of the sinapate biosynthetic pathway. The two tryptophans, Trp-285 and Trp-233, serve collectively as the UV-B chromophore.12 Publications

GO - Molecular functioni

  • chromatin binding Source: TAIR
  • guanyl-nucleotide exchange factor activity Source: TAIR
  • photoreceptor activity Source: UniProtKB-KW
  • protein homodimerization activity Source: TAIR

GO - Biological processi

  • entrainment of circadian clock Source: TAIR
  • protein-chromophore linkage Source: UniProtKB-KW
  • response to UV Source: TAIR
  • response to UV-B Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Photoreceptor protein, Receptor

Keywords - Biological processi

Sensory transduction

Keywords - Ligandi

Chromophore

Names & Taxonomyi

Protein namesi
Recommended name:
Ultraviolet-B receptor UVR8
Alternative name(s):
Protein UV-B RESISTANCE 8
RCC1 domain-containing protein UVR8
Gene namesi
Name:UVR8
Ordered Locus Names:At5g63860
ORF Names:MGI19.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G63860.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: TAIR
  • cytosol Source: TAIR
  • nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Hypersensitivity to UV-B.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391W → A: Loss of function, homodimerization and interaction with COP1. 1 Publication
Mutagenesisi39 – 391W → F: No effect on function, homodimerization and interaction with COP1. 1 Publication
Mutagenesisi39 – 391W → Y: No effect on function, homodimerization and interaction with COP1. 1 Publication
Mutagenesisi92 – 921W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication
Mutagenesisi94 – 941W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication
Mutagenesisi144 – 1441W → A: Cannot interact with COP1. 1 Publication
Mutagenesisi144 – 1441W → F: No effect on the interaction with COP1. 1 Publication
Mutagenesisi144 – 1441W → Y: No effect on the interaction with COP1. 1 Publication
Mutagenesisi145 – 1451G → S in uvr8-15; loss of function and interaction with COP1. 1 Publication
Mutagenesisi196 – 2005Missing in uvr8-1; loss of function. 1 Publication
Mutagenesisi196 – 1961W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication
Mutagenesisi198 – 1981W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication
Mutagenesisi202 – 2021G → R in uvr8-9; loss of function and interaction with COP1. 1 Publication
Mutagenesisi233 – 2331W → A: Reduces response to UV-B. 2 Publications
Mutagenesisi250 – 2501W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication
Mutagenesisi283 – 2831G → E in uvr8-5; loss of response to UV-B. 1 Publication
Mutagenesisi285 – 2851W → A: Loss of function. Constitutive monomer. 3 Publications
Mutagenesisi285 – 2851W → F: Loss of function. Constitutive homodimer and no interaction with COP1. 3 Publications
Mutagenesisi300 – 3001W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication
Mutagenesisi302 – 3021W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication
Mutagenesisi337 – 3371W → A: Reduces response to UV-B. 2 Publications
Mutagenesisi352 – 3521W → A: Cannot interact with COP1. 1 Publication
Mutagenesisi352 – 3521W → F: No effect on the interaction with COP1. 1 Publication
Mutagenesisi352 – 3521W → Y: No effect on the interaction with COP1. 1 Publication
Mutagenesisi400 – 4001W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 440439Ultraviolet-B receptor UVR8PRO_0000421722Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9FN03.
PRIDEiQ9FN03.

PTM databases

iPTMnetiQ9FN03.

Expressioni

Gene expression databases

GenevisibleiQ9FN03. AT.

Interactioni

Subunit structurei

Homodimer in the absence of UV-B, but absorption of UV-B induces monomerization of UVR8 and interaction with COP1. Interacts with RUP1, RUP2 and histone H2B.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
COP1P432543EBI-2407499,EBI-301649

GO - Molecular functioni

  • protein homodimerization activity Source: TAIR

Protein-protein interaction databases

BioGridi21748. 8 interactions.
DIPiDIP-59667N.
IntActiQ9FN03. 1 interaction.
MINTiMINT-7033609.
STRINGi3702.AT5G63860.1.

Structurei

Secondary structure

1
440
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 226Combined sources
Beta strandi24 – 318Combined sources
Turni32 – 343Combined sources
Beta strandi35 – 406Combined sources
Beta strandi49 – 513Combined sources
Beta strandi55 – 606Combined sources
Helixi62 – 643Combined sources
Beta strandi69 – 746Combined sources
Beta strandi76 – 838Combined sources
Turni84 – 874Combined sources
Beta strandi88 – 936Combined sources
Helixi96 – 983Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi108 – 1136Combined sources
Helixi115 – 1173Combined sources
Beta strandi122 – 1276Combined sources
Beta strandi129 – 1368Combined sources
Beta strandi141 – 1455Combined sources
Beta strandi154 – 1563Combined sources
Beta strandi160 – 1656Combined sources
Helixi167 – 1693Combined sources
Beta strandi174 – 1796Combined sources
Beta strandi181 – 1888Combined sources
Beta strandi193 – 1975Combined sources
Beta strandi206 – 2094Combined sources
Beta strandi212 – 2176Combined sources
Beta strandi226 – 2316Combined sources
Beta strandi233 – 2408Combined sources
Beta strandi245 – 2495Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi264 – 2696Combined sources
Helixi271 – 2733Combined sources
Beta strandi278 – 2836Combined sources
Beta strandi285 – 2928Combined sources
Beta strandi297 – 3015Combined sources
Beta strandi310 – 3145Combined sources
Beta strandi316 – 3227Combined sources
Helixi325 – 3273Combined sources
Beta strandi330 – 3356Combined sources
Beta strandi337 – 3448Combined sources
Beta strandi349 – 3535Combined sources
Beta strandi362 – 3643Combined sources
Beta strandi368 – 3736Combined sources
Helixi375 – 3773Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D9SX-ray1.70A/B1-405[»]
4DNUX-ray1.76A10-381[»]
4DNVX-ray2.00A/B/C/D12-381[»]
4DNWX-ray1.77A/B12-385[»]
ProteinModelPortaliQ9FN03.
SMRiQ9FN03. Positions 14-396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati32 – 8453RCC1 1Add
BLAST
Repeati86 – 13752RCC1 2Add
BLAST
Repeati139 – 18951RCC1 3Add
BLAST
Repeati190 – 24152RCC1 4Add
BLAST
Repeati243 – 29351RCC1 5Add
BLAST
Repeati294 – 34552RCC1 6Add
BLAST
Repeati347 – 39953RCC1 7Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni397 – 42327Required for interaction with COP1Add
BLAST

Sequence similaritiesi

Contains 7 RCC1 repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1426. Eukaryota.
COG5184. LUCA.
HOGENOMiHOG000240817.
InParanoidiQ9FN03.
OMAiHGIRIKQ.
PhylomeDBiQ9FN03.

Family and domain databases

Gene3Di2.130.10.30. 1 hit.
InterProiIPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
IPR032996. UVR8.
[Graphical view]
PANTHERiPTHR22870:SF193. PTHR22870:SF193. 1 hit.
PfamiPF00415. RCC1. 7 hits.
[Graphical view]
PRINTSiPR00633. RCCNDNSATION.
SUPFAMiSSF50985. SSF50985. 1 hit.
PROSITEiPS00626. RCC1_2. 5 hits.
PS50012. RCC1_3. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9FN03-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEDMAADEV TAPPRKVLII SAGASHSVAL LSGDIVCSWG RGEDGQLGHG
60 70 80 90 100
DAEDRPSPTQ LSALDGHQIV SVTCGADHTV AYSQSGMEVY SWGWGDFGRL
110 120 130 140 150
GHGNSSDLFT PLPIKALHGI RIKQIACGDS HCLAVTMEGE VQSWGRNQNG
160 170 180 190 200
QLGLGDTEDS LVPQKIQAFE GIRIKMVAAG AEHTAAVTED GDLYGWGWGR
210 220 230 240 250
YGNLGLGDRT DRLVPERVTS TGGEKMSMVA CGWRHTISVS YSGALYTYGW
260 270 280 290 300
SKYGQLGHGD LEDHLIPHKL EALSNSFISQ ISGGWRHTMA LTSDGKLYGW
310 320 330 340 350
GWNKFGQVGV GNNLDQCSPV QVRFPDDQKV VQVSCGWRHT LAVTERNNVF
360 370 380 390 400
AWGRGTNGQL GIGESVDRNF PKIIEALSVD GASGQHIESS NIDPSSGKSW
410 420 430 440
VSPAERYAVV PDETGLTDGS SKGNGGDISV PQTDVKRVRI
Length:440
Mass (Da):47,118
Last modified:March 1, 2001 - v1
Checksum:iD2EA103CCFC92E98
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731R → P in AAD43920 (PubMed:12226503).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF130441 mRNA. Translation: AAD43920.1.
AB007646 Genomic DNA. Translation: BAB11034.1.
CP002688 Genomic DNA. Translation: AED97805.1.
AY125497 mRNA. Translation: AAM78089.1.
BT000600 mRNA. Translation: AAN18169.1.
PIRiT50662.
RefSeqiNP_201191.1. NM_125781.3.
UniGeneiAt.49214.

Genome annotation databases

EnsemblPlantsiAT5G63860.1; AT5G63860.1; AT5G63860.
GeneIDi836506.
GrameneiAT5G63860.1; AT5G63860.1; AT5G63860.
KEGGiath:AT5G63860.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF130441 mRNA. Translation: AAD43920.1.
AB007646 Genomic DNA. Translation: BAB11034.1.
CP002688 Genomic DNA. Translation: AED97805.1.
AY125497 mRNA. Translation: AAM78089.1.
BT000600 mRNA. Translation: AAN18169.1.
PIRiT50662.
RefSeqiNP_201191.1. NM_125781.3.
UniGeneiAt.49214.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D9SX-ray1.70A/B1-405[»]
4DNUX-ray1.76A10-381[»]
4DNVX-ray2.00A/B/C/D12-381[»]
4DNWX-ray1.77A/B12-385[»]
ProteinModelPortaliQ9FN03.
SMRiQ9FN03. Positions 14-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi21748. 8 interactions.
DIPiDIP-59667N.
IntActiQ9FN03. 1 interaction.
MINTiMINT-7033609.
STRINGi3702.AT5G63860.1.

PTM databases

iPTMnetiQ9FN03.

Proteomic databases

PaxDbiQ9FN03.
PRIDEiQ9FN03.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G63860.1; AT5G63860.1; AT5G63860.
GeneIDi836506.
GrameneiAT5G63860.1; AT5G63860.1; AT5G63860.
KEGGiath:AT5G63860.

Organism-specific databases

TAIRiAT5G63860.

Phylogenomic databases

eggNOGiKOG1426. Eukaryota.
COG5184. LUCA.
HOGENOMiHOG000240817.
InParanoidiQ9FN03.
OMAiHGIRIKQ.
PhylomeDBiQ9FN03.

Miscellaneous databases

PROiQ9FN03.

Gene expression databases

GenevisibleiQ9FN03. AT.

Family and domain databases

Gene3Di2.130.10.30. 1 hit.
InterProiIPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
IPR032996. UVR8.
[Graphical view]
PANTHERiPTHR22870:SF193. PTHR22870:SF193. 1 hit.
PfamiPF00415. RCC1. 7 hits.
[Graphical view]
PRINTSiPR00633. RCCNDNSATION.
SUPFAMiSSF50985. SSF50985. 1 hit.
PROSITEiPS00626. RCC1_2. 5 hits.
PS50012. RCC1_3. 7 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Arabidopsis UVR8 regulates ultraviolet-B signal transduction and tolerance and contains sequence similarity to human regulator of chromatin condensation 1."
    Kliebenstein D.J., Lim J.E., Landry L.G., Last R.L.
    Plant Physiol. 130:234-243(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, MUTAGENESIS OF 196-TRP--ARG-200.
    Strain: cv. Landsberg erecta.
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
    Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 4:401-414(1997) [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. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "UV-B promotes rapid nuclear translocation of the Arabidopsis UV-B specific signaling component UVR8 and activates its function in the nucleus."
    Kaiserli E., Jenkins G.I.
    Plant Cell 19:2662-2673(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "UV-B signaling pathways with different fluence-rate response profiles are distinguished in mature Arabidopsis leaf tissue by requirement for UVR8, HY5, and HYH."
    Brown B.A., Jenkins G.I.
    Plant Physiol. 146:576-588(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Interaction of the Arabidopsis UV-B-specific signaling component UVR8 with chromatin."
    Cloix C., Jenkins G.I.
    Mol. Plant 1:118-128(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HISTONE H2B.
  9. "Interaction of COP1 and UVR8 regulates UV-B-induced photomorphogenesis and stress acclimation in Arabidopsis."
    Favory J.J., Stec A., Gruber H., Rizzini L., Oravecz A., Funk M., Albert A., Cloix C., Jenkins G.I., Oakeley E.J., Seidlitz H.K., Nagy F., Ulm R.
    EMBO J. 28:591-601(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH COP1.
    Strain: cv. Wassilewskija.
  10. "UVR8 in Arabidopsis thaliana regulates multiple aspects of cellular differentiation during leaf development in response to ultraviolet B radiation."
    Wargent J.J., Gegas V.C., Jenkins G.I., Doonan J.H., Paul N.D.
    New Phytol. 183:315-326(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Negative feedback regulation of UV-B-induced photomorphogenesis and stress acclimation in Arabidopsis."
    Gruber H., Heijde M., Heller W., Albert A., Seidlitz H.K., Ulm R.
    Proc. Natl. Acad. Sci. U.S.A. 107:20132-20137(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RUP1 AND RUP2.
  12. "Functional interaction of the circadian clock and UV RESISTANCE LOCUS 8-controlled UV-B signaling pathways in Arabidopsis thaliana."
    Feher B., Kozma-Bognar L., Kevei E., Hajdu A., Binkert M., Davis S.J., Schaefer E., Ulm R., Nagy F.
    Plant J. 67:37-48(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. Cited for: FUNCTION, SUBUNIT, INTERACTION WITH COP1, MUTAGENESIS OF GLY-145; GLY-202 AND TRP-285.
  14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "UVR8 mediates UV-B-induced Arabidopsis defense responses against Botrytis cinerea by controlling sinapate accumulation."
    Demkura P.V., Ballare C.L.
    Mol. Plant 5:642-652(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "The UV-B photoreceptor UVR8 promotes photosynthetic efficiency in Arabidopsis thaliana exposed to elevated levels of UV-B."
    Davey M.P., Susanti N.I., Wargent J.J., Findlay J.E., Paul Quick W., Paul N.D., Jenkins G.I.
    Photosyn. Res. 114:121-131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "In vivo function of tryptophans in the Arabidopsis UV-B photoreceptor UVR8."
    O'Hara A., Jenkins G.I.
    Plant Cell 24:3755-3766(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH COP1, MUTAGENESIS OF TRP-39; TRP-92; TRP-94; TRP-144; TRP-196; TRP-198; TRP-233; TRP-250; TRP-285; TRP-300; TRP-302; TRP-337; TRP-352 AND TRP-400.
  18. "C-terminal region of the UV-B photoreceptor UVR8 initiates signaling through interaction with the COP1 protein."
    Cloix C., Kaiserli E., Heilmann M., Baxter K.J., Brown B.A., O'Hara A., Smith B.O., Christie J.M., Jenkins G.I.
    Proc. Natl. Acad. Sci. U.S.A. 109:16366-16370(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH COP1; RUP1 AND RUP2, MUTAGENESIS OF GLY-283.
  19. "Rapid reversion from monomer to dimer regenerates the ultraviolet-B photoreceptor UV RESISTANCE LOCUS8 in intact Arabidopsis plants."
    Heilmann M., Jenkins G.I.
    Plant Physiol. 161:547-555(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  20. "Structural basis of ultraviolet-B perception by UVR8."
    Wu D., Hu Q., Yan Z., Chen W., Yan C., Huang X., Zhang J., Yang P., Deng H., Wang J., Deng X., Shi Y.
    Nature 484:214-219(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 10-381, SUBUNIT, MUTAGENESIS OF TRP-233; TRP-285 AND TRP-337.
  21. "Plant UVR8 photoreceptor senses UV-B by tryptophan-mediated disruption of cross-dimer salt bridges."
    Christie J.M., Arvai A.S., Baxter K.J., Heilmann M., Pratt A.J., O'Hara A., Kelly S.M., Hothorn M., Smith B.O., Hitomi K., Jenkins G.I., Getzoff E.D.
    Science 335:1492-1496(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-405, SUBUNIT.

Entry informationi

Entry nameiUVR8_ARATH
AccessioniPrimary (citable) accession number: Q9FN03
Secondary accession number(s): Q9XHD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 102 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.