Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Phytochrome A (Protein ELONGATED HYPOCOTYL 8) (Protein FAR RED ELONGATED 1) (Protein FAR RED ELONGATED HYPOCOTYL 2)

 PHYA_ARATH              Reviewed;        1122 AA.
P14712; B3H6K9;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
23-MAY-2018, entry version 186.
RecName: Full=Phytochrome A {ECO:0000303|PubMed:2606345};
AltName: Full=Protein ELONGATED HYPOCOTYL 8 {ECO:0000303|PubMed:8400877};
AltName: Full=Protein FAR RED ELONGATED 1;
AltName: Full=Protein FAR RED ELONGATED HYPOCOTYL 2;
Name=PHYA {ECO:0000303|PubMed:2606345};
Synonyms=FHY2, FRE1, HY8 {ECO:0000303|PubMed:8400877};
OrderedLocusNames=At1g09570 {ECO:0000312|Araport:AT1G09570};
ORFNames=F14J9.23 {ECO:0000312|EMBL:AAC33219.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=2606345; DOI=10.1101/gad.3.11.1745;
Sharrock R.A., Quail P.H.;
"Novel phytochrome sequences in Arabidopsis thaliana: structure,
evolution, and differential expression of a plant regulatory
photoreceptor family.";
Genes Dev. 3:1745-1757(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-727.
STRAIN=cv. RLD;
PubMed=8400877; DOI=10.1105/tpc.5.9.1081;
Dehesh K., Franci C., Parks B.M., Seeley K.A., Short T.W.,
Tepperman J.M., Quail P.H.;
"Arabidopsis HY8 locus encodes phytochrome A.";
Plant Cell 5:1081-1088(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
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.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
FUNCTION, AND INTERACTION WITH FYPP3.
PubMed=12468726; DOI=10.1105/tpc.005306;
Kim D.-H., Kang J.-G., Yang S.-S., Chung K.-S., Song P.-S.,
Park C.-M.;
"A phytochrome-associated protein phosphatase 2A modulates light
signals in flowering time control in Arabidopsis.";
Plant Cell 14:3043-3056(2002).
[7]
INTERACTION WITH NDPK2.
PubMed=15465053; DOI=10.1016/j.jmb.2004.08.054;
Im Y.J., Kim J.I., Shen Y., Na Y., Han Y.J., Kim S.H., Song P.S.,
Eom S.H.;
"Structural analysis of Arabidopsis thaliana nucleoside diphosphate
kinase-2 for phytochrome-mediated light signaling.";
J. Mol. Biol. 343:659-670(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PAPP5 AND NDPK2.
PubMed=15707897; DOI=10.1016/j.cell.2004.12.019;
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.;
"Phytochrome-specific type 5 phosphatase controls light signal flux by
enhancing phytochrome stability and affinity for a signal
transducer.";
Cell 120:395-406(2005).
[9]
FUNCTION.
PubMed=17566111; DOI=10.1073/pnas.0703855104;
Roesler J., Klein I., Zeidler M.;
"Arabidopsis fhl/fhy1 double mutant reveals a distinct cytoplasmic
action of phytochrome A.";
Proc. Natl. Acad. Sci. U.S.A. 104:10737-10742(2007).
[10]
INTERACTION WITH COP1; SPA1; FHY1 AND FHY3.
PubMed=18722184; DOI=10.1016/j.molcel.2008.08.003;
Saijo Y., Zhu D., Li J., Rubio V., Zhou Z., Shen Y., Hoecker U.,
Wang H., Deng X.W.;
"Arabidopsis COP1/SPA1 complex and FHY1/FHY3 associate with distinct
phosphorylated forms of phytochrome A in balancing light signaling.";
Mol. Cell 31:607-613(2008).
[11]
INTERACTION WITH PKS4.
PubMed=18390804; DOI=10.1104/pp.108.118166;
Schepens I., Boccalandro H.E., Kami C., Casal J.J., Fankhauser C.;
"PHYTOCHROME KINASE SUBSTRATE4 modulates phytochrome-mediated control
of hypocotyl growth orientation.";
Plant Physiol. 147:661-671(2008).
[12]
FUNCTION, AND INTERACTION WITH PHYA AND FHL.
PubMed=19208901; DOI=10.1105/tpc.108.061259;
Shen Y., Zhou Z., Feng S., Li J., Tan-Wilson A., Qu L.J., Wang H.,
Deng X.W.;
"Phytochrome A mediates rapid red light-induced phosphorylation of
Arabidopsis FAR-RED ELONGATED HYPOCOTYL1 in a low fluence response.";
Plant Cell 21:494-506(2009).
[13]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION
WITH FHY1; HFR1 AND FHL.
STRAIN=cv. Columbia;
PubMed=19482971; DOI=10.1105/tpc.109.067215;
Yang S.W., Jang I.-C., Henriques R., Chua N.-H.;
"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.";
Plant Cell 21:1341-1359(2009).
[14]
INTERACTION WITH FHY1 AND FHL, AND MUTAGENESIS OF TYR-242 AND CYS-323.
PubMed=21884939; DOI=10.1016/j.cell.2011.07.023;
Rausenberger J., Tscheuschler A., Nordmeier W., Wuest F., Timmer J.,
Schaefer E., Fleck C., Hiltbrunner A.;
"Photoconversion and nuclear trafficking cycles determine phytochrome
A's response profile to far-red light.";
Cell 146:813-825(2011).
[15]
INTERACTION WITH PTAC12/HMR.
STRAIN=cv. Columbia;
PubMed=22895253; DOI=10.1101/gad.193219.112;
Galvao R.M., Li M., Kothadia S.M., Haskel J.D., Decker P.V.,
Van Buskirk E.K., Chen M.;
"Photoactivated phytochromes interact with HEMERA and promote its
accumulation to establish photomorphogenesis in Arabidopsis.";
Genes Dev. 26:1851-1863(2012).
[16]
FUNCTION, MUTAGENESIS OF ALA-30, INTERACTION WITH FHY1 AND FHL, AND
SUBCELLULAR LOCATION.
PubMed=21969386; DOI=10.1104/pp.111.186288;
Sokolova V., Bindics J., Kircher S., Adam E., Schaefer E., Nagy F.,
Viczian A.;
"Missense mutation in the amino terminus of phytochrome A disrupts the
nuclear import of the photoreceptor.";
Plant Physiol. 158:107-118(2012).
-!- FUNCTION: 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).
{ECO:0000269|PubMed:12468726, ECO:0000269|PubMed:15707897,
ECO:0000269|PubMed:17566111, ECO:0000269|PubMed:19208901,
ECO:0000269|PubMed:19482971, ECO:0000269|PubMed:21969386}.
-!- SUBUNIT: 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).
{ECO:0000269|PubMed:12468726, ECO:0000269|PubMed:15465053,
ECO:0000269|PubMed:15707897, ECO:0000269|PubMed:18390804,
ECO:0000269|PubMed:18722184, ECO:0000269|PubMed:19208901,
ECO:0000269|PubMed:19482971, ECO:0000269|PubMed:21884939,
ECO:0000269|PubMed:22895253}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-624446, EBI-624446;
Q80936:E1 (xeno); NbExp=2; IntAct=EBI-624446, EBI-1163369;
A8MR65:FHL; NbExp=3; IntAct=EBI-624446, EBI-1163353;
Q8S4Q6:FHY1; NbExp=4; IntAct=EBI-624446, EBI-1163379;
O64903:NDPK2; NbExp=3; IntAct=EBI-624446, EBI-349517;
O80536:PIF3; NbExp=8; IntAct=EBI-624446, EBI-625701;
Q8W2F3-2:PIF4; NbExp=2; IntAct=EBI-624446, EBI-625732;
Q9SWI1:PKS1; NbExp=3; IntAct=EBI-624446, EBI-626200;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15707897,
ECO:0000269|PubMed:21969386}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:15707897, ECO:0000269|PubMed:21969386}.
Nucleus speckle {ECO:0000269|PubMed:15707897}. Note=Cytoplasmic in
darkness, but translocated to the nucleus upon illumination, when
associated with PAPP5 into speckles. {ECO:0000269|PubMed:15707897,
ECO:0000269|PubMed:21969386}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P14712-1; Sequence=Displayed;
Name=2;
IsoId=P14712-2; Sequence=VSP_036311;
Note=Derived from EST data. No experimental confirmation
available.;
-!- PTM: Phosphorylated.
-!- PTM: Contains one covalently linked phytochromobilin chromophore.
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Blind to far-red (FR). Impaired inhibition
of hypocotyl elongation and cotyledons expansion under continuous
FR light conditions. {ECO:0000269|PubMed:19482971}.
-!- MISCELLANEOUS: PHYA association with FHY1 and FHY3 protect
underphosphorylated PHYA from being recognized by the COP1/SPA
complex.
-!- SIMILARITY: Belongs to the phytochrome family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X17341; CAA35221.1; -; mRNA.
EMBL; L21154; AAA21351.1; -; Genomic_DNA.
EMBL; AC003970; AAC33219.1; -; Genomic_DNA.
EMBL; CP002684; AEE28462.1; -; Genomic_DNA.
EMBL; CP002684; AEE28463.1; -; Genomic_DNA.
EMBL; CP002684; ANM60635.1; -; Genomic_DNA.
EMBL; CP002684; ANM60636.1; -; Genomic_DNA.
EMBL; CP002684; ANM60637.1; -; Genomic_DNA.
EMBL; AY039520; AAK62577.1; -; mRNA.
PIR; A33473; FKMUA.
PIR; D86229; D86229.
RefSeq; NP_001117256.1; NM_001123784.1. [P14712-2]
RefSeq; NP_001322907.1; NM_001331843.1. [P14712-1]
RefSeq; NP_001322908.1; NM_001331842.1. [P14712-1]
RefSeq; NP_001322909.1; NM_001331841.1. [P14712-1]
RefSeq; NP_172428.1; NM_100828.4. [P14712-1]
UniGene; At.22828; -.
ProteinModelPortal; P14712; -.
SMR; P14712; -.
BioGrid; 22724; 25.
DIP; DIP-33461N; -.
IntAct; P14712; 11.
MINT; P14712; -.
STRING; 3702.AT1G09570.1; -.
PaxDb; P14712; -.
PRIDE; P14712; -.
EnsemblPlants; AT1G09570.1; AT1G09570.1; AT1G09570. [P14712-1]
EnsemblPlants; AT1G09570.2; AT1G09570.2; AT1G09570. [P14712-2]
EnsemblPlants; AT1G09570.3; AT1G09570.3; AT1G09570.
EnsemblPlants; AT1G09570.4; AT1G09570.4; AT1G09570. [P14712-1]
EnsemblPlants; AT1G09570.5; AT1G09570.5; AT1G09570. [P14712-1]
EnsemblPlants; AT1G09570.6; AT1G09570.6; AT1G09570. [P14712-1]
GeneID; 837483; -.
Gramene; AT1G09570.1; AT1G09570.1; AT1G09570. [P14712-1]
Gramene; AT1G09570.2; AT1G09570.2; AT1G09570. [P14712-2]
Gramene; AT1G09570.3; AT1G09570.3; AT1G09570.
Gramene; AT1G09570.4; AT1G09570.4; AT1G09570. [P14712-1]
Gramene; AT1G09570.5; AT1G09570.5; AT1G09570. [P14712-1]
Gramene; AT1G09570.6; AT1G09570.6; AT1G09570. [P14712-1]
KEGG; ath:AT1G09570; -.
Araport; AT1G09570; -.
TAIR; locus:2012300; AT1G09570.
eggNOG; ENOG410IHYD; Eukaryota.
eggNOG; COG4251; LUCA.
HOGENOM; HOG000272703; -.
InParanoid; P14712; -.
KO; K12120; -.
OMA; AYLHHIQ; -.
OrthoDB; EOG093600OD; -.
PhylomeDB; P14712; -.
PRO; PR:P14712; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; P14712; baseline and differential.
Genevisible; P14712; AT.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0016604; C:nuclear body; IDA:TAIR.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0031516; F:far-red light photoreceptor activity; IMP:TAIR.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003729; F:mRNA binding; IDA:TAIR.
GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0009883; F:red or far-red light photoreceptor activity; TAS:TAIR.
GO; GO:0009584; P:detection of visible light; IEA:InterPro.
GO; GO:0009630; P:gravitropism; IMP:TAIR.
GO; GO:0017148; P:negative regulation of translation; IMP:TAIR.
GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
GO; GO:0009638; P:phototropism; IMP:TAIR.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
GO; GO:0017006; P:protein-tetrapyrrole linkage; IEA:InterPro.
GO; GO:0010161; P:red light signaling pathway; IMP:TAIR.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0046685; P:response to arsenic-containing substance; IMP:TAIR.
GO; GO:0010201; P:response to continuous far red light stimulus by the high-irradiance response system; IMP:TAIR.
GO; GO:0010218; P:response to far red light; IDA:UniProtKB.
GO; GO:0010203; P:response to very low fluence red light stimulus; IMP:TAIR.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00075; HATPase_c; 1.
CDD; cd00082; HisKA; 1.
CDD; cd00130; PAS; 2.
Gene3D; 3.30.450.40; -; 3.
Gene3D; 3.30.565.10; -; 1.
InterPro; IPR003018; GAF.
InterPro; IPR029016; GAF-like_dom_sf.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR005467; His_kinase_dom.
InterPro; IPR003661; HisK_dim/P.
InterPro; IPR000014; PAS.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR013654; PAS_2.
InterPro; IPR013767; PAS_fold.
InterPro; IPR016132; Phyto_chromo_attachment.
InterPro; IPR013516; Phyto_chromo_BS.
InterPro; IPR001294; Phytochrome.
InterPro; IPR012129; Phytochrome_A-E.
InterPro; IPR013515; Phytochrome_cen-reg.
Pfam; PF01590; GAF; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00989; PAS; 2.
Pfam; PF08446; PAS_2; 1.
Pfam; PF00360; PHY; 1.
PIRSF; PIRSF000084; Phytochrome; 1.
PRINTS; PR01033; PHYTOCHROME.
SMART; SM00065; GAF; 1.
SMART; SM00387; HATPase_c; 1.
SMART; SM00388; HisKA; 1.
SMART; SM00091; PAS; 2.
SUPFAM; SSF55785; SSF55785; 3.
SUPFAM; SSF55874; SSF55874; 1.
TIGRFAMs; TIGR00229; sensory_box; 1.
PROSITE; PS50109; HIS_KIN; 1.
PROSITE; PS50112; PAS; 2.
PROSITE; PS00245; PHYTOCHROME_1; 1.
PROSITE; PS50046; PHYTOCHROME_2; 1.
1: Evidence at protein level;
Alternative splicing; Chromophore; Complete proteome; Cytoplasm;
Kinase; Nucleus; Phosphoprotein; Photoreceptor protein; Receptor;
Reference proteome; Repeat; Sensory transduction; Transcription;
Transcription regulation; Transferase.
CHAIN 1 1122 Phytochrome A.
/FTId=PRO_0000171962.
DOMAIN 218 402 GAF. {ECO:0000255}.
DOMAIN 618 688 PAS 1. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 695 747 PAC. {ECO:0000255|PROSITE-
ProRule:PRU00141}.
DOMAIN 748 822 PAS 2. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 902 1119 Histidine kinase. {ECO:0000255|PROSITE-
ProRule:PRU00107}.
BINDING 323 323 Phytochromobilin chromophore (covalent;
via 1 link). {ECO:0000250}.
VAR_SEQ 1 108 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_036311.
MUTAGEN 30 30 A->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.
{ECO:0000269|PubMed:21969386}.
MUTAGEN 242 242 Y->H: Constitutively active in the Pfr
form, leading to a constitutively
photomorphogenic (cop) phenotype and
reduced accumulation in the nucleus.
{ECO:0000269|PubMed:21884939}.
MUTAGEN 323 323 C->A: Unable to bind the chromophore and
cannot be converted to Pfr, fails to
accumulate in the nucleus and to interact
with FHY1. {ECO:0000269|PubMed:21884939}.
MUTAGEN 727 727 G->E: In HY8-3; no regulatory activity.
{ECO:0000269|PubMed:8400877}.
CONFLICT 835 835 E -> D (in Ref. 1; CAA35221).
{ECO:0000305}.
CONFLICT 862 862 E -> K (in Ref. 1; CAA35221).
{ECO:0000305}.
SEQUENCE 1122 AA; 124501 MW; D8B359713430744B CRC64;
MSGSRPTQSS EGSRRSRHSA RIIAQTTVDA KLHADFEESG SSFDYSTSVR VTGPVVENQP
PRSDKVTTTY LHHIQKGKLI QPFGCLLALD EKTFKVIAYS ENASELLTMA SHAVPSVGEH
PVLGIGTDIR SLFTAPSASA LQKALGFGDV SLLNPILVHC RTSAKPFYAI IHRVTGSIII
DFEPVKPYEV PMTAAGALQS YKLAAKAITR LQSLPSGSME RLCDTMVQEV FELTGYDRVM
AYKFHEDDHG EVVSEVTKPG LEPYLGLHYP ATDIPQAARF LFMKNKVRMI VDCNAKHARV
LQDEKLSFDL TLCGSTLRAP HSCHLQYMAN MDSIASLVMA VVVNEEDGEG DAPDATTQPQ
KRKRLWGLVV CHNTTPRFVP FPLRYACEFL AQVFAIHVNK EVELDNQMVE KNILRTQTLL
CDMLMRDAPL GIVSQSPNIM DLVKCDGAAL LYKDKIWKLG TTPSEFHLQE IASWLCEYHM
DSTGLSTDSL HDAGFPRALS LGDSVCGMAA VRISSKDMIF WFRSHTAGEV RWGGAKHDPD
DRDDARRMHP RSSFKAFLEV VKTRSLPWKD YEMDAIHSLQ LILRNAFKDS ETTDVNTKVI
YSKLNDLKID GIQELEAVTS EMVRLIETAT VPILAVDSDG LVNGWNTKIA ELTGLSVDEA
IGKHFLTLVE DSSVEIVKRM LENALEGTEE QNVQFEIKTH LSRADAGPIS LVVNACASRD
LHENVVGVCF VAHDLTGQKT VMDKFTRIEG DYKAIIQNPN PLIPPIFGTD EFGWCTEWNP
AMSKLTGLKR EEVIDKMLLG EVFGTQKSCC RLKNQEAFVN LGIVLNNAVT SQDPEKVSFA
FFTRGGKYVE CLLCVSKKLD REGVVTGVFC FLQLASHELQ QALHVQRLAE RTAVKRLKAL
AYIKRQIRNP LSGIMFTRKM IEGTELGPEQ RRILQTSALC QKQLSKILDD SDLESIIEGC
LDLEMKEFTL NEVLTASTSQ VMMKSNGKSV RITNETGEEV MSDTLYGDSI RLQQVLADFM
LMAVNFTPSG GQLTVSASLR KDQLGRSVHL ANLEIRLTHT GAGIPEFLLN QMFGTEEDVS
EEGLSLMVSR KLVKLMNGDV QYLRQAGKSS FIITAELAAA NK


Related products :

Catalog number Product name Quantity
AS12 1867 Antibody: HY5 | ELONGATED HYPOCOTYL 5 , Host: rabbit, polyclonal, Confirmed reactivity: Arabidopsis thaliana
B15275 Bismuth Shot Elongated 99.9 percent
B15275 Bismuth Shot Elongated 99.9 percent
B15275 Bismuth Shot Elongated 99.9 percent 500 G
B15275 Bismuth Shot Elongated 99.9 percent 100 G
AS12 1867 rabbit polyclonal HY5 | Protein long hypocotyl 5 50
MB-X0812D Neuron Culture Set _ Hippocampus(Rat) Primary nerve cells derived from rat hippocampus provided with medium and dissociation solutions. System provides highly viable, fully elongated neurons in cultu kit
MB-X0810D Neuron Culture Set _ Cerebral cortex(Rat) Primary nerve cells derived from rat cerebral cortex provided with medium and dissociation solutions. System provides highly viable, fully elongated neurons kit
MB-X0813D Neuron Culture Set _ Hippocampus(Mouse) Primary nerve cells derived from mouse hippocampus provided with medium and dissociation solutions. System provides highly viable, fully elongated neurons in c kit
MB-X0811D Neuron Culture Set _ Cerebral cortex(Mouse) Primary nerve cells derived from mouse cerebral cortex provided with medium and dissociation solutions. System provides highly viable, fully elongated neur kit
AS07 220 Phytochrome A | photoreceptor PhyA protein 200 ug
AS07220 Phytochrome A | photoreceptor PhyA protein 200 ug
AS07 220 Antibody: Phytochrome A | photoreceptor PhyA protein, Immunogen: synthetic peptide derived from conserved plant PhyA protein sequences including A. thaliana (At1g59070); peptide sequence is not presen 200
AS07 220 rabbit polyclonal Phytochrome A | photoreceptor PhyA protein 200
PAH-G1-2 Protein Arrays containing 234 Human Protein for simultaneous detection of Protein function, including Protein-protein interaction, Protein modification, antibody specificity, auto-antibody and small m 1 glass slide with 2 sub-arrays
29-850 The protein contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions.The protein encoded by this 0.1 mg
29-844 RNF40 contains a RING finger, a motif known to be involved in protein-protein and protein-DNA interactions. This protein was reported to interact with the tumor suppressor protein RB1. Studies of the 0.1 mg
EIAAB10617 DCN1-like protein 1,DCUN1 domain-containing protein 1,Dcun1d1,Dcun1l1,Defective in cullin neddylation protein 1-like protein 1,Mouse,Mus musculus,Rp42,Tes3,Testis-specific protein 3
EIAAB44668 Dap12,DNAX-activation protein 12,Karap,KAR-associated protein,Killer-activating receptor-associated protein,Mouse,Mus musculus,TYRO protein tyrosine kinase-binding protein,Tyrobp
EIAAB44667 DAP12,DNAX-activation protein 12,Homo sapiens,Human,KARAP,KAR-associated protein,Killer-activating receptor-associated protein,TYRO protein tyrosine kinase-binding protein,TYROBP
18-003-43520 HSPB1-associated protein 1 - 27 KdA heat shock protein-associated protein 1; Protein associated with small stress protein 1 Polyclonal 0.05 mg Aff Pur
EIAAB25665 AML1T1,CBFA2T1,CDR,Cyclin-D-related protein,Eight twenty one protein,ETO,Homo sapiens,Human,MTG8,Protein CBFA2T1,Protein ETO,Protein MTG8,RUNX1T1,Zinc finger MYND domain-containing protein 2,ZMYND2
EIAAB46018 C6orf55,Dopamine-responsive gene 1 protein,DRG-1,Homo sapiens,HSPC228,Human,LIP5,LYST-interacting protein 5,My012,SBP1,SKD1-binding protein 1,Vacuolar protein sorting-associated protein VTA1 homolog,V
18-003-43690 Guanine nucleotide-binding protein subunit beta-like protein 1 - G protein subunit beta-like protein 1; WD40 repeat-containing protein deleted in VCFS; Protein WDVCF; WD repeat-containing protein 14; 0.1 mg Protein A
U1773h CLIA G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur