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Protein

Phototropin-2

Gene

PHOT2

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

Functioni

Protein kinase that acts as a blue light photoreceptor in a signal-transduction pathway for photo-induced movements. Phosphorylates BLUS1, a kinase involved in stomatal opening. Mediates calcium spiking of extra- and intracellular origins in response to blue light. Involved in hypocotyl phototropism. Contributes to the chloroplast accumulation in low blue light and mediates their translocation (avoidance response) at high fluence. Regulates stomata opening and photomorphogenesis response of leaf tissue. Not involved in hypocotyl elongation inhibition, anthocyanin accumulation or cotyledon opening.6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

FMNCuratedNote: Binds 2 FMN per subunit.Curated

Absorptioni

Abs(max)=450 nm1 Publication

Exhibits a smaller absorbance peak at 350 nm. The broad fluorescence emission spectrum peaks at 490 nm.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei187 – 1871FMN1 Publication
Binding sitei202 – 2021FMN1 Publication
Binding sitei212 – 2121FMN1 Publication
Binding sitei233 – 2331FMN1 Publication
Binding sitei443 – 4431FMNBy similarity
Binding sitei458 – 4581FMNBy similarity
Binding sitei468 – 4681FMNBy similarity
Binding sitei489 – 4891FMNBy similarity
Binding sitei606 – 6061ATPPROSITE-ProRule annotation
Active sitei702 – 7021Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi169 – 1746FMN1 Publication
Nucleotide bindingi425 – 4306FMNBy similarity
Nucleotide bindingi583 – 5919ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • blue light photoreceptor activity Source: TAIR
  • FMN binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • kinase activity Source: TAIR
  • phosphorelay sensor kinase activity Source: InterPro
  • protein serine/threonine kinase activity Source: TAIR

GO - Biological processi

  • blue light signaling pathway Source: GOC
  • chloroplast relocation Source: TAIR
  • circadian rhythm Source: TAIR
  • intracellular signal transduction Source: GO_Central
  • negative regulation of anion channel activity by blue light Source: TAIR
  • phototropism Source: TAIR
  • protein autophosphorylation Source: TAIR
  • protein-chromophore linkage Source: UniProtKB-KW
  • response to blue light Source: TAIR
  • response to cytokinin Source: TAIR
  • stomatal movement Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Photoreceptor protein, Receptor, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Sensory transduction

Keywords - Ligandi

ATP-binding, Chromophore, Flavoprotein, FMN, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G58140-MONOMER.
ARA:GQT-2687-MONOMER.
ARA:GQT-2830-MONOMER.
ARA:GQT-2831-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phototropin-2 (EC:2.7.11.1)
Alternative name(s):
Defective in chloroplast avoidance protein 1
Non-phototropic hypocotyl 1-like protein 1
Short name:
AtKin7
Short name:
NPH1-like protein 1
Gene namesi
Name:PHOT2
Synonyms:CAV1, KIN7, NPL1
Ordered Locus Names:At5g58140
ORF Names:K21L19.6
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G58140.

Subcellular locationi

GO - Cellular componenti

  • Golgi apparatus Source: TAIR
  • membrane Source: TAIR
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi170 – 1701C → A: No effect on light-dependent autophosphorylation. 1 Publication
Mutagenesisi217 – 2171T → Q: Loss of dimerization. 1 Publication
Mutagenesisi232 – 2321M → V: Loss of dimerization. 1 Publication
Mutagenesisi426 – 4261C → A: Severe loss of light-sensing and light-dependent autophosphorylation. 1 Publication
Mutagenesisi727 – 7271T → I in cav1-2; loss of chloroplast avoidance response in response to high fluence blue light. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 915915Phototropin-2PRO_0000086523Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91PhosphoserineCombined sources
Modified residuei22 – 221PhosphoserineCombined sources
Modified residuei121 – 1211PhosphoserineBy similarity
Modified residuei170 – 1701S-4a-FMN cysteineBy similarity
Modified residuei364 – 3641PhosphoserineCombined sources
Modified residuei426 – 4261S-4a-FMN cysteineBy similarity

Post-translational modificationi

Autophosphorylated in response to blue light irradiation.1 Publication
2 molecules of FMN bind covalently to cysteines after exposure to blue light and are reversed in the dark.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP93025.
PRIDEiP93025.

PTM databases

iPTMnetiP93025.

Expressioni

Tissue specificityi

Expressed in leaves, stems and flowers, and to a lower extent in roots.1 Publication

Inductioni

Light fluence rate-dependent induction, independent of light quality.1 Publication

Gene expression databases

ExpressionAtlasiP93025. baseline and differential.
GenevisibleiP93025. AT.

Interactioni

Subunit structurei

Homodimer. Interacts with PKS1, PKS2, RPT3 and PHOT1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-2270423,EBI-2270423

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi21170. 11 interactions.
DIPiDIP-53468N.
IntActiP93025. 3 interactions.
MINTiMINT-6823418.
STRINGi3702.AT5G58140.1.

Structurei

Secondary structure

1
915
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi124 – 1307Combined sources
Beta strandi134 – 1396Combined sources
Beta strandi147 – 1504Combined sources
Helixi152 – 1587Combined sources
Helixi162 – 1654Combined sources
Helixi170 – 1734Combined sources
Helixi180 – 19112Combined sources
Beta strandi196 – 2038Combined sources
Beta strandi209 – 22012Combined sources
Beta strandi226 – 23510Combined sources
Beta strandi390 – 3945Combined sources
Beta strandi403 – 4064Combined sources
Helixi408 – 4147Combined sources
Helixi418 – 4214Combined sources
Helixi426 – 4294Combined sources
Helixi436 – 44712Combined sources
Beta strandi452 – 4598Combined sources
Beta strandi465 – 47612Combined sources
Beta strandi482 – 49110Combined sources
Turni492 – 4954Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z6DX-ray2.00A/B117-246[»]
4EEPX-ray1.70A385-496[»]
4EERX-ray1.75A385-496[»]
4EESX-ray1.80A385-496[»]
4EETX-ray1.20B/D385-496[»]
4EEUX-ray1.41A385-496[»]
4NXBX-ray2.56A/B388-496[»]
4NXEX-ray2.10A/B388-496[»]
4NXFX-ray1.77A/B388-496[»]
4NXGX-ray2.09A/B388-496[»]
ProteinModelPortaliP93025.
SMRiP93025. Positions 123-276, 380-529, 540-885.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP93025.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini120 – 19374PAS 1PROSITE-ProRule annotationAdd
BLAST
Domaini194 – 24855PAC 1PROSITE-ProRule annotationAdd
BLAST
Domaini376 – 44974PAS 2PROSITE-ProRule annotationAdd
BLAST
Domaini450 – 50455PAC 2PROSITE-ProRule annotationAdd
BLAST
Domaini577 – 864288Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni720 – 77455Activation loopBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi16 – 11499Ser-richAdd
BLAST

Domaini

The activation loop within the kinase domain is the target of phosphorylation (By similarity). The PAS (PER-ARNT-SIM) domains are required for the binding of FMN chromophores.By similarity

Sequence similaritiesi

Contains 2 PAC (PAS-associated C-terminal) domains.PROSITE-ProRule annotation
Contains 2 PAS (PER-ARNT-SIM) domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IH6N. Eukaryota.
COG2202. LUCA.
HOGENOMiHOG000265679.
InParanoidiP93025.
OMAiPRIPDNP.
PhylomeDBiP93025.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR001610. PAC.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13426. PAS_9. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00086. PAC. 2 hits.
SM00091. PAS. 2 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 2 hits.
SSF56112. SSF56112. 2 hits.
TIGRFAMsiTIGR00229. sensory_box. 2 hits.
PROSITEiPS50113. PAC. 2 hits.
PS50112. PAS. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P93025-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERPRAPPSP LNDAESLSER RSLEIFNPSS GKETHGSTSS SSKPPLDGNN
60 70 80 90 100
KGSSSKWMEF QDSAKITERT AEWGLSAVKP DSGDDGISFK LSSEVERSKN
110 120 130 140 150
MSRRSSEEST SSESGAFPRV SQELKTALST LQQTFVVSDA TQPHCPIVYA
160 170 180 190 200
SSGFFTMTGY SSKEIVGRNC RFLQGPDTDK NEVAKIRDCV KNGKSYCGRL
210 220 230 240 250
LNYKKDGTPF WNLLTVTPIK DDQGNTIKFI GMQVEVSKYT EGVNDKALRP
260 270 280 290 300
NGLSKSLIRY DARQKEKALD SITEVVQTIR HRKSQVQESV SNDTMVKPDS
310 320 330 340 350
STTPTPGRQT RQSDEASKSF RTPGRVSTPT GSKLKSSNNR HEDLLRMEPE
360 370 380 390 400
ELMLSTEVIG QRDSWDLSDR ERDIRQGIDL ATTLERIEKN FVISDPRLPD
410 420 430 440 450
NPIIFASDSF LELTEYSREE ILGRNCRFLQ GPETDQATVQ KIRDAIRDQR
460 470 480 490 500
EITVQLINYT KSGKKFWNLF HLQPMRDQKG ELQYFIGVQL DGSDHVEPLQ
510 520 530 540 550
NRLSERTEMQ SSKLVKATAT NVDEAVRELP DANTRPEDLW AAHSKPVYPL
560 570 580 590 600
PHNKESTSWK AIKKIQASGE TVGLHHFKPI KPLGSGDTGS VHLVELKGTG
610 620 630 640 650
ELYAMKAMEK TMMLNRNKAH RACIEREIIS LLDHPFLPTL YASFQTSTHV
660 670 680 690 700
CLITDFCPGG ELFALLDRQP MKILTEDSAR FYAAEVVIGL EYLHCLGIVY
710 720 730 740 750
RDLKPENILL KKDGHIVLAD FDLSFMTTCT PQLIIPAAPS KRRRSKSQPL
760 770 780 790 800
PTFVAEPSTQ SNSFVGTEEY IAPEIITGAG HTSAIDWWAL GILLYEMLYG
810 820 830 840 850
RTPFRGKNRQ KTFANILHKD LTFPSSIPVS LVGRQLINTL LNRDPSSRLG
860 870 880 890 900
SKGGANEIKQ HAFFRGINWP LIRGMSPPPL DAPLSIIEKD PNAKDIKWED
910
DGVLVNSTDL DIDLF
Length:915
Mass (Da):102,472
Last modified:November 22, 2005 - v2
Checksum:iCA163E2596289737
GO
Isoform 2 (identifier: P93025-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     535-549: RPEDLWAAHSKPVYP → VRCTSSLLLNKDGKV
     550-915: Missing.

Note: May be due to a competing acceptor splice site. No experimental confirmation available.
Show »
Length:549
Mass (Da):61,600
Checksum:i3777BA44BAE08C96
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti722 – 7221D → Y in AAB39188 (Ref. 5) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei535 – 54915RPEDL…KPVYP → VRCTSSLLLNKDGKV in isoform 2. 1 PublicationVSP_016306Add
BLAST
Alternative sequencei550 – 915366Missing in isoform 2. 1 PublicationVSP_016307Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053941 mRNA. Translation: AAC27293.2.
AB019228, AB024029 Genomic DNA. Translation: BAB09904.1.
CP002688 Genomic DNA. Translation: AED97002.1.
CP002688 Genomic DNA. Translation: AED97004.1.
AY093141 mRNA. Translation: AAM13140.1.
BT008901 mRNA. Translation: AAP68340.1.
U79744 mRNA. Translation: AAB39188.1.
PIRiT51600.
RefSeqiNP_851210.1. NM_180879.1. [P93025-1]
NP_851211.1. NM_180880.1. [P93025-1]
UniGeneiAt.22044.
At.72500.

Genome annotation databases

EnsemblPlantsiAT5G58140.1; AT5G58140.1; AT5G58140. [P93025-1]
AT5G58140.2; AT5G58140.2; AT5G58140. [P93025-1]
GeneIDi835926.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053941 mRNA. Translation: AAC27293.2.
AB019228, AB024029 Genomic DNA. Translation: BAB09904.1.
CP002688 Genomic DNA. Translation: AED97002.1.
CP002688 Genomic DNA. Translation: AED97004.1.
AY093141 mRNA. Translation: AAM13140.1.
BT008901 mRNA. Translation: AAP68340.1.
U79744 mRNA. Translation: AAB39188.1.
PIRiT51600.
RefSeqiNP_851210.1. NM_180879.1. [P93025-1]
NP_851211.1. NM_180880.1. [P93025-1]
UniGeneiAt.22044.
At.72500.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z6DX-ray2.00A/B117-246[»]
4EEPX-ray1.70A385-496[»]
4EERX-ray1.75A385-496[»]
4EESX-ray1.80A385-496[»]
4EETX-ray1.20B/D385-496[»]
4EEUX-ray1.41A385-496[»]
4NXBX-ray2.56A/B388-496[»]
4NXEX-ray2.10A/B388-496[»]
4NXFX-ray1.77A/B388-496[»]
4NXGX-ray2.09A/B388-496[»]
ProteinModelPortaliP93025.
SMRiP93025. Positions 123-276, 380-529, 540-885.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi21170. 11 interactions.
DIPiDIP-53468N.
IntActiP93025. 3 interactions.
MINTiMINT-6823418.
STRINGi3702.AT5G58140.1.

PTM databases

iPTMnetiP93025.

Proteomic databases

PaxDbiP93025.
PRIDEiP93025.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G58140.1; AT5G58140.1; AT5G58140. [P93025-1]
AT5G58140.2; AT5G58140.2; AT5G58140. [P93025-1]
GeneIDi835926.

Organism-specific databases

TAIRiAT5G58140.

Phylogenomic databases

eggNOGiENOG410IH6N. Eukaryota.
COG2202. LUCA.
HOGENOMiHOG000265679.
InParanoidiP93025.
OMAiPRIPDNP.
PhylomeDBiP93025.

Enzyme and pathway databases

BioCyciARA:AT5G58140-MONOMER.
ARA:GQT-2687-MONOMER.
ARA:GQT-2830-MONOMER.
ARA:GQT-2831-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP93025.
PROiP93025.

Gene expression databases

ExpressionAtlasiP93025. baseline and differential.
GenevisibleiP93025. AT.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR001610. PAC.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13426. PAS_9. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00086. PAC. 2 hits.
SM00091. PAS. 2 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 2 hits.
SSF56112. SSF56112. 2 hits.
TIGRFAMsiTIGR00229. sensory_box. 2 hits.
PROSITEiPS50113. PAC. 2 hits.
PS50112. PAS. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "NPH2: a second member of the NPH serine/threonine kinase family of Arabidopsis."
    Jarillo J.A., Ahmad M., Cashmore A.R.
    Plant Gene Register PGR98-100
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
    DNA Res. 7:31-63(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. "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] (ISOFORM 2).
    Strain: cv. Columbia.
  5. "Arabidopsis thaliana putative serine/threonine protein kinase."
    Winge P., Thangstad O.P.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 560-915 (ISOFORM 1).
  6. "Arabidopsis nph1 and npl1: blue light receptors that mediate both phototropism and chloroplast relocation."
    Sakai T., Kagawa T., Kasahara M., Swartz T.E., Christie J.M., Briggs W.R., Wada M., Okada K.
    Proc. Natl. Acad. Sci. U.S.A. 98:6969-6974(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FMN-BINDING, PHOSPHORYLATION.
  7. "Arabidopsis NPL1: a phototropin homolog controlling the chloroplast high-light avoidance response."
    Kagawa T., Sakai T., Suetsugu N., Oikawa K., Ishiguro S., Kato T., Tabata S., Okada K., Wada M.
    Science 291:2138-2141(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF THR-727.
  8. "Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function."
    Christie J.M., Swartz T.E., Bogomolni R.A., Briggs W.R.
    Plant J. 32:205-219(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION, MUTAGENESIS OF CYS-170 AND CYS-426.
  9. "Photochemical properties of the flavin mononucleotide-binding domains of the phototropins from Arabidopsis, rice, and Chlamydomonas reinhardtii."
    Kasahara M., Swartz T.E., Olney M.A., Onodera A., Mochizuki N., Fukuzawa H., Asamizu E., Tabata S., Kanegae H., Takano M., Christie J.M., Nagatani A., Briggs W.R.
    Plant Physiol. 129:762-773(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  10. "Phot1 and phot2 mediate blue light-induced transient increases in cytosolic Ca2+ differently in Arabidopsis leaves."
    Harada A., Sakai T., Okada K.
    Proc. Natl. Acad. Sci. U.S.A. 100:8583-8588(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "Growth signalling pathways in Arabidopsis and the AGC protein kinases."
    Boegre L., Okresz L., Henriques R., Anthony R.G.
    Trends Plant Sci. 8:424-431(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, REVIEW.
  12. "RPT2 is a signal transducer involved in phototropic response and stomatal opening by association with phototropin 1 in Arabidopsis thaliana."
    Inada S., Ohgishi M., Mayama T., Okada K., Sakai T.
    Plant Cell 16:887-896(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Functional analysis of each blue light receptor, cry1, cry2, phot1, and phot2, by using combinatorial multiple mutants in Arabidopsis."
    Ohgishi M., Saji K., Okada K., Sakai T.
    Proc. Natl. Acad. Sci. U.S.A. 101:2223-2228(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-22 AND SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "The Arabidopsis PHYTOCHROME KINASE SUBSTRATE2 protein is a phototropin signaling element that regulates leaf flattening and leaf positioning."
    de Carbonnel M., Davis P., Roelfsema M.R., Inoue S., Schepens I., Lariguet P., Geisler M., Shimazaki K., Hangarter R., Fankhauser C.
    Plant Physiol. 152:1391-1405(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PKS1; PKS2; RPT3 AND PHOT1.
  16. "Phosphorylation of BLUS1 kinase by phototropins is a primary step in stomatal opening."
    Takemiya A., Sugiyama N., Fujimoto H., Tsutsumi T., Yamauchi S., Hiyama A., Tada Y., Christie J.M., Shimazaki K.
    Nat. Commun. 4:2094-2094(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Structural basis of the LOV1 dimerization of Arabidopsis phototropins 1 and 2."
    Nakasako M., Zikihara K., Matsuoka D., Katsura H., Tokutomi S.
    J. Mol. Biol. 381:718-733(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 117-246 IN COMPLEX WITH FMN, SUBUNIT, MUTAGENESIS OF THR-217 AND MET-232.

Entry informationi

Entry nameiPHOT2_ARATH
AccessioniPrimary (citable) accession number: P93025
Secondary accession number(s): O81204, Q8RWE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: May 11, 2016
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Undergoes a photocycle characterized by fluorescence and absorption changes induced by blue light. Half-time of photoproduct formation is 11 seconds and 15 seconds for dark regeneration.

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.