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

Phytochrome A

Gene

PHYA

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

Functioni

Regulatory photoreceptor which exists in two forms that are reversibly interconvertible by light: the Pr form that absorbs maximally in the red region of the spectrum and the Pfr form that absorbs maximally in the far-red region. Photoconversion of Pr to Pfr induces an array of morphogenetic responses, whereas reconversion of Pfr to Pr cancels the induction of those responses. Pfr controls the expression of a number of nuclear genes including those encoding the small subunit of ribulose-bisphosphate carboxylase, chlorophyll A/B binding protein, protochlorophyllide reductase, rRNA, etc. It also controls the expression of its own gene(s) in a negative feedback fashion. Involved in the flowering time regulation. Can phosphorylate FHY1 and, possibly, FHL, in red light conditions; this inactivates their co-shuttling to the nucleus (PubMed:19208901). Regulates phototropic responses both in the nucleus (e.g. hypocotyl elongation and cotyledon opening under high-irradiance conditions and seed germination under very-low-fluence conditions) and in the cytoplasm (e.g. negative gravitropism in blue light and red-enhanced phototropism) (PubMed:17566111).6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei323 – 3231Phytochromobilin chromophore (covalent; via 1 link)By similarity

GO - Molecular functioni

  • far-red light photoreceptor activity Source: TAIR
  • identical protein binding Source: IntAct
  • phosphorelay sensor kinase activity Source: InterPro
  • protein kinase activity Source: UniProtKB
  • red or far-red light photoreceptor activity Source: TAIR

GO - Biological processi

  • detection of visible light Source: InterPro
  • gravitropism Source: TAIR
  • negative regulation of translation Source: TAIR
  • photomorphogenesis Source: TAIR
  • phototropism Source: TAIR
  • protein-chromophore linkage Source: UniProtKB-KW
  • protein-tetrapyrrole linkage Source: InterPro
  • red light signaling pathway Source: TAIR
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • response to arsenic-containing substance Source: TAIR
  • response to continuous far red light stimulus by the high-irradiance response system Source: TAIR
  • response to far red light Source: UniProtKB
  • response to very low fluence red light stimulus Source: TAIR
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Photoreceptor protein, Receptor, Transferase

Keywords - Biological processi

Sensory transduction, Transcription, Transcription regulation

Keywords - Ligandi

Chromophore

Enzyme and pathway databases

BioCyciARA:AT1G09570-MONOMER.
ARA:GQT-1106-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phytochrome A1 Publication
Alternative name(s):
Protein ELONGATED HYPOCOTYL 81 Publication
Protein FAR RED ELONGATED 1
Protein FAR RED ELONGATED HYPOCOTYL 2
Gene namesi
Name:PHYA1 Publication
Synonyms:FHY2, FRE1, HY81 Publication
Ordered Locus Names:At1g09570Imported
ORF Names:F14J9.23Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G09570.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: TAIR
  • nuclear body Source: TAIR
  • nuclear speck Source: UniProtKB-SubCell
  • nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Blind to far-red (FR). Impaired inhibition of hypocotyl elongation and cotyledons expansion under continuous FR light conditions.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301A → V in phyA-5; reduced binding to FHY1 and FHL leading to a reduced nuclear import under low fluences of far-red light (FR) light. Hyposensitivity to continuous low-intensity FR, and reduced very-low-fluence response and high-irradiance response. 1 Publication
Mutagenesisi242 – 2421Y → H: Constitutively active in the Pfr form, leading to a constitutively photomorphogenic (cop) phenotype and reduced accumulation in the nucleus. 1 Publication
Mutagenesisi323 – 3231C → A: Unable to bind the chromophore and cannot be converted to Pfr, fails to accumulate in the nucleus and to interact with FHY1. 1 Publication
Mutagenesisi727 – 7271G → E in HY8-3; no regulatory activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11221122Phytochrome APRO_0000171962Add
BLAST

Post-translational modificationi

Phosphorylated.
Contains one covalently linked phytochromobilin chromophore.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP14712.
PRIDEiP14712.

Expressioni

Gene expression databases

ExpressionAtlasiP14712. baseline and differential.
GenevisibleiP14712. AT.

Interactioni

Subunit structurei

Homodimer. Interacts with NDPK2 and PKS4. Stabilized by interactions with PAPP5 and FYPP3 which are enhanced in the phosphorylated Pfr form. Interacts with COP1/SPA1 complex (PubMed:12468726, PubMed:15465053, PubMed:15707897, PubMed:18390804, PubMed:18722184). Binds, via its photosensory domain, to PTAC12/HMR when photoactivated; this interaction stimulates its localization to photobodies (PubMed:22895253). Interacts with FHY1, FHL and FHY3, especially upon far-red (FR) light illumination; when underphosphorylated (PubMed:18722184, PubMed:19208901, PubMed:21884939, PubMed:19482971). Forms PHYA/FHY1/HFR1 complex (PubMed:19482971).9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-624446,EBI-624446
E1Q809362EBI-624446,EBI-1163369From a different organism.
NDPK2O649033EBI-624446,EBI-349517
PIF3O805368EBI-624446,EBI-625701
PIF4Q8W2F3-22EBI-624446,EBI-625732
PKS1Q9SWI13EBI-624446,EBI-626200
T7H20_250Q9LZL23EBI-624446,EBI-1163353

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi22724. 25 interactions.
DIPiDIP-33461N.
IntActiP14712. 12 interactions.
MINTiMINT-1174780.
STRINGi3702.AT1G09570.1.

Structurei

3D structure databases

ProteinModelPortaliP14712.
SMRiP14712. Positions 68-586, 888-1110.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini218 – 402185GAFSequence analysisAdd
BLAST
Domaini618 – 68871PAS 1PROSITE-ProRule annotationAdd
BLAST
Domaini695 – 74753PACPROSITE-ProRule annotationAdd
BLAST
Domaini748 – 82275PAS 2PROSITE-ProRule annotationAdd
BLAST
Domaini902 – 1119218Histidine kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the phytochrome family.Curated
Contains 1 GAF domain.Sequence analysis
Contains 1 histidine kinase domain.PROSITE-ProRule annotation
Contains 1 PAC (PAS-associated C-terminal) domain.PROSITE-ProRule annotation
Contains 2 PAS (PER-ARNT-SIM) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IHYD. Eukaryota.
COG4251. LUCA.
HOGENOMiHOG000272703.
InParanoidiP14712.
KOiK12120.
OMAiAYLHHIQ.
PhylomeDBiP14712.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
InterProiIPR003018. GAF.
IPR029016. GAF_dom-like.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR000014. PAS.
IPR013654. PAS_2.
IPR013767. PAS_fold.
IPR016132. Phyto_chromo_attachment.
IPR013516. Phyto_chromo_BS.
IPR001294. Phytochrome.
IPR012129. Phytochrome_A-E.
IPR013515. Phytochrome_cen-reg.
[Graphical view]
PfamiPF01590. GAF. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00989. PAS. 2 hits.
PF08446. PAS_2. 1 hit.
PF00360. PHY. 1 hit.
[Graphical view]
PIRSFiPIRSF000084. Phytochrome. 1 hit.
PRINTSiPR01033. PHYTOCHROME.
SMARTiSM00065. GAF. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF55781. SSF55781. 2 hits.
SSF55785. SSF55785. 3 hits.
SSF55874. SSF55874. 1 hit.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
PS50112. PAS. 2 hits.
PS00245. PHYTOCHROME_1. 1 hit.
PS50046. PHYTOCHROME_2. 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: P14712-1) [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
MSGSRPTQSS EGSRRSRHSA RIIAQTTVDA KLHADFEESG SSFDYSTSVR
60 70 80 90 100
VTGPVVENQP PRSDKVTTTY LHHIQKGKLI QPFGCLLALD EKTFKVIAYS
110 120 130 140 150
ENASELLTMA SHAVPSVGEH PVLGIGTDIR SLFTAPSASA LQKALGFGDV
160 170 180 190 200
SLLNPILVHC RTSAKPFYAI IHRVTGSIII DFEPVKPYEV PMTAAGALQS
210 220 230 240 250
YKLAAKAITR LQSLPSGSME RLCDTMVQEV FELTGYDRVM AYKFHEDDHG
260 270 280 290 300
EVVSEVTKPG LEPYLGLHYP ATDIPQAARF LFMKNKVRMI VDCNAKHARV
310 320 330 340 350
LQDEKLSFDL TLCGSTLRAP HSCHLQYMAN MDSIASLVMA VVVNEEDGEG
360 370 380 390 400
DAPDATTQPQ KRKRLWGLVV CHNTTPRFVP FPLRYACEFL AQVFAIHVNK
410 420 430 440 450
EVELDNQMVE KNILRTQTLL CDMLMRDAPL GIVSQSPNIM DLVKCDGAAL
460 470 480 490 500
LYKDKIWKLG TTPSEFHLQE IASWLCEYHM DSTGLSTDSL HDAGFPRALS
510 520 530 540 550
LGDSVCGMAA VRISSKDMIF WFRSHTAGEV RWGGAKHDPD DRDDARRMHP
560 570 580 590 600
RSSFKAFLEV VKTRSLPWKD YEMDAIHSLQ LILRNAFKDS ETTDVNTKVI
610 620 630 640 650
YSKLNDLKID GIQELEAVTS EMVRLIETAT VPILAVDSDG LVNGWNTKIA
660 670 680 690 700
ELTGLSVDEA IGKHFLTLVE DSSVEIVKRM LENALEGTEE QNVQFEIKTH
710 720 730 740 750
LSRADAGPIS LVVNACASRD LHENVVGVCF VAHDLTGQKT VMDKFTRIEG
760 770 780 790 800
DYKAIIQNPN PLIPPIFGTD EFGWCTEWNP AMSKLTGLKR EEVIDKMLLG
810 820 830 840 850
EVFGTQKSCC RLKNQEAFVN LGIVLNNAVT SQDPEKVSFA FFTRGGKYVE
860 870 880 890 900
CLLCVSKKLD REGVVTGVFC FLQLASHELQ QALHVQRLAE RTAVKRLKAL
910 920 930 940 950
AYIKRQIRNP LSGIMFTRKM IEGTELGPEQ RRILQTSALC QKQLSKILDD
960 970 980 990 1000
SDLESIIEGC LDLEMKEFTL NEVLTASTSQ VMMKSNGKSV RITNETGEEV
1010 1020 1030 1040 1050
MSDTLYGDSI RLQQVLADFM LMAVNFTPSG GQLTVSASLR KDQLGRSVHL
1060 1070 1080 1090 1100
ANLEIRLTHT GAGIPEFLLN QMFGTEEDVS EEGLSLMVSR KLVKLMNGDV
1110 1120
QYLRQAGKSS FIITAELAAA NK
Length:1,122
Mass (Da):124,501
Last modified:December 15, 1998 - v2
Checksum:iD8B359713430744B
GO
Isoform 2 (identifier: P14712-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.

Note: Derived from EST data. No experimental confirmation available.
Show »
Length:1,014
Mass (Da):112,622
Checksum:i173404F60475F586
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti835 – 8351E → D in CAA35221 (PubMed:2606345).Curated
Sequence conflicti862 – 8621E → K in CAA35221 (PubMed:2606345).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 108108Missing in isoform 2. CuratedVSP_036311Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17341 mRNA. Translation: CAA35221.1.
L21154 Genomic DNA. Translation: AAA21351.1.
AC003970 Genomic DNA. Translation: AAC33219.1.
CP002684 Genomic DNA. Translation: AEE28462.1.
CP002684 Genomic DNA. Translation: AEE28463.1.
AY039520 mRNA. Translation: AAK62577.1.
PIRiA33473. FKMUA.
D86229.
RefSeqiNP_001117256.1. NM_001123784.1. [P14712-2]
NP_172428.1. NM_100828.3. [P14712-1]
UniGeneiAt.22828.

Genome annotation databases

EnsemblPlantsiAT1G09570.1; AT1G09570.1; AT1G09570. [P14712-1]
GeneIDi837483.
KEGGiath:AT1G09570.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17341 mRNA. Translation: CAA35221.1.
L21154 Genomic DNA. Translation: AAA21351.1.
AC003970 Genomic DNA. Translation: AAC33219.1.
CP002684 Genomic DNA. Translation: AEE28462.1.
CP002684 Genomic DNA. Translation: AEE28463.1.
AY039520 mRNA. Translation: AAK62577.1.
PIRiA33473. FKMUA.
D86229.
RefSeqiNP_001117256.1. NM_001123784.1. [P14712-2]
NP_172428.1. NM_100828.3. [P14712-1]
UniGeneiAt.22828.

3D structure databases

ProteinModelPortaliP14712.
SMRiP14712. Positions 68-586, 888-1110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi22724. 25 interactions.
DIPiDIP-33461N.
IntActiP14712. 12 interactions.
MINTiMINT-1174780.
STRINGi3702.AT1G09570.1.

Proteomic databases

PaxDbiP14712.
PRIDEiP14712.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G09570.1; AT1G09570.1; AT1G09570. [P14712-1]
GeneIDi837483.
KEGGiath:AT1G09570.

Organism-specific databases

TAIRiAT1G09570.

Phylogenomic databases

eggNOGiENOG410IHYD. Eukaryota.
COG4251. LUCA.
HOGENOMiHOG000272703.
InParanoidiP14712.
KOiK12120.
OMAiAYLHHIQ.
PhylomeDBiP14712.

Enzyme and pathway databases

BioCyciARA:AT1G09570-MONOMER.
ARA:GQT-1106-MONOMER.

Miscellaneous databases

PROiP14712.

Gene expression databases

ExpressionAtlasiP14712. baseline and differential.
GenevisibleiP14712. AT.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
InterProiIPR003018. GAF.
IPR029016. GAF_dom-like.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR000014. PAS.
IPR013654. PAS_2.
IPR013767. PAS_fold.
IPR016132. Phyto_chromo_attachment.
IPR013516. Phyto_chromo_BS.
IPR001294. Phytochrome.
IPR012129. Phytochrome_A-E.
IPR013515. Phytochrome_cen-reg.
[Graphical view]
PfamiPF01590. GAF. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00989. PAS. 2 hits.
PF08446. PAS_2. 1 hit.
PF00360. PHY. 1 hit.
[Graphical view]
PIRSFiPIRSF000084. Phytochrome. 1 hit.
PRINTSiPR01033. PHYTOCHROME.
SMARTiSM00065. GAF. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF55781. SSF55781. 2 hits.
SSF55785. SSF55785. 3 hits.
SSF55874. SSF55874. 1 hit.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
PS50112. PAS. 2 hits.
PS00245. PHYTOCHROME_1. 1 hit.
PS50046. PHYTOCHROME_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Novel phytochrome sequences in Arabidopsis thaliana: structure, evolution, and differential expression of a plant regulatory photoreceptor family."
    Sharrock R.A., Quail P.H.
    Genes Dev. 3:1745-1757(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-727.
    Strain: cv. RLD.
  3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "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 1).
    Strain: cv. Columbia.
  6. "A phytochrome-associated protein phosphatase 2A modulates light signals in flowering time control in Arabidopsis."
    Kim D.-H., Kang J.-G., Yang S.-S., Chung K.-S., Song P.-S., Park C.-M.
    Plant Cell 14:3043-3056(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FYPP3.
  7. "Structural analysis of Arabidopsis thaliana nucleoside diphosphate kinase-2 for phytochrome-mediated light signaling."
    Im Y.J., Kim J.I., Shen Y., Na Y., Han Y.J., Kim S.H., Song P.S., Eom S.H.
    J. Mol. Biol. 343:659-670(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NDPK2.
  8. "Phytochrome-specific type 5 phosphatase controls light signal flux by enhancing phytochrome stability and affinity for a signal transducer."
    Ryu J.S., Kim J.-I., Kunkel T., Kim B.C., Cho D.S., Hong S.H., Kim S.-H., Fernandez A.P., Kim Y., Alonso J.M., Ecker J.R., Nagy F., Lim P.O., Song P.-S., Schaefer E., Nam H.G.
    Cell 120:395-406(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PAPP5 AND NDPK2.
  9. "Arabidopsis fhl/fhy1 double mutant reveals a distinct cytoplasmic action of phytochrome A."
    Roesler J., Klein I., Zeidler M.
    Proc. Natl. Acad. Sci. U.S.A. 104:10737-10742(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Arabidopsis COP1/SPA1 complex and FHY1/FHY3 associate with distinct phosphorylated forms of phytochrome A in balancing light signaling."
    Saijo Y., Zhu D., Li J., Rubio V., Zhou Z., Shen Y., Hoecker U., Wang H., Deng X.W.
    Mol. Cell 31:607-613(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COP1; SPA1; FHY1 AND FHY3.
  11. "PHYTOCHROME KINASE SUBSTRATE4 modulates phytochrome-mediated control of hypocotyl growth orientation."
    Schepens I., Boccalandro H.E., Kami C., Casal J.J., Fankhauser C.
    Plant Physiol. 147:661-671(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PKS4.
  12. "Phytochrome A mediates rapid red light-induced phosphorylation of Arabidopsis FAR-RED ELONGATED HYPOCOTYL1 in a low fluence response."
    Shen Y., Zhou Z., Feng S., Li J., Tan-Wilson A., Qu L.J., Wang H., Deng X.W.
    Plant Cell 21:494-506(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PHYA AND FHL.
  13. "FAR-RED ELONGATED HYPOCOTYL1 and FHY1-LIKE associate with the Arabidopsis transcription factors LAF1 and HFR1 to transmit phytochrome A signals for inhibition of hypocotyl elongation."
    Yang S.W., Jang I.-C., Henriques R., Chua N.-H.
    Plant Cell 21:1341-1359(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH FHY1; HFR1 AND FHL.
    Strain: cv. Columbia.
  14. "Photoconversion and nuclear trafficking cycles determine phytochrome A's response profile to far-red light."
    Rausenberger J., Tscheuschler A., Nordmeier W., Wuest F., Timmer J., Schaefer E., Fleck C., Hiltbrunner A.
    Cell 146:813-825(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FHY1 AND FHL, MUTAGENESIS OF TYR-242 AND CYS-323.
  15. "Photoactivated phytochromes interact with HEMERA and promote its accumulation to establish photomorphogenesis in Arabidopsis."
    Galvao R.M., Li M., Kothadia S.M., Haskel J.D., Decker P.V., Van Buskirk E.K., Chen M.
    Genes Dev. 26:1851-1863(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTAC12/HMR.
    Strain: cv. Columbia.
  16. "Missense mutation in the amino terminus of phytochrome A disrupts the nuclear import of the photoreceptor."
    Sokolova V., Bindics J., Kircher S., Adam E., Schaefer E., Nagy F., Viczian A.
    Plant Physiol. 158:107-118(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ALA-30, INTERACTION WITH FHY1 AND FHL, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPHYA_ARATH
AccessioniPrimary (citable) accession number: P14712
Secondary accession number(s): B3H6K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: December 15, 1998
Last modified: July 6, 2016
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

PHYA association with FHY1 and FHY3 protect underphosphorylated PHYA from being recognized by the COP1/SPA complex.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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