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Transcription factor PIF1 (Basic helix-loop-helix protein 15) (AtbHLH15) (bHLH 15) (Protein PHY-INTERACTING FACTOR 1) (Protein PHYTOCHROME INTERACTING FACTOR 3-LIKE 5) (Transcription factor EN 101) (bHLH transcription factor bHLH015)

 PIF1_ARATH              Reviewed;         478 AA.
Q8GZM7; Q0WQ83; Q3EBY0; Q9SL63;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-OCT-2017, entry version 112.
RecName: Full=Transcription factor PIF1;
AltName: Full=Basic helix-loop-helix protein 15;
Short=AtbHLH15;
Short=bHLH 15;
AltName: Full=Protein PHY-INTERACTING FACTOR 1;
AltName: Full=Protein PHYTOCHROME INTERACTING FACTOR 3-LIKE 5;
AltName: Full=Transcription factor EN 101;
AltName: Full=bHLH transcription factor bHLH015;
Name=PIF1; Synonyms=BHLH15, EN101, PIL5; OrderedLocusNames=At2g20180;
ORFNames=T2G17.2;
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), TISSUE SPECIFICITY, GENE
FAMILY, AND NOMENCLATURE.
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=12679534; DOI=10.1093/molbev/msg088;
Heim M.A., Jakoby M., Werber M., Martin C., Weisshaar B., Bailey P.C.;
"The basic helix-loop-helix transcription factor family in plants: a
genome-wide study of protein structure and functional diversity.";
Mol. Biol. Evol. 20:735-747(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH
APRR1/TOC1.
PubMed=12826627; DOI=10.1093/pcp/pcg078;
Yamashino T., Matsushika A., Fujimori T., Sato S., Kato T., Tabata S.,
Mizuno T.;
"A link between circadian-controlled bHLH factors and the APRR1/TOC1
quintet in Arabidopsis thaliana.";
Plant Cell Physiol. 44:619-629(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C.,
Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
[7]
GENE FAMILY.
PubMed=12897250; DOI=10.1105/tpc.013839;
Toledo-Ortiz G., Huq E., Quail P.H.;
"The Arabidopsis basic/helix-loop-helix transcription factor family.";
Plant Cell 15:1749-1770(2003).
[8]
GENE FAMILY, AND NOMENCLATURE.
PubMed=14600211; DOI=10.1105/tpc.151140;
Bailey P.C., Martin C., Toledo-Ortiz G., Quail P.H., Huq E.,
Heim M.A., Jakoby M., Werber M., Weisshaar B.;
"Update on the basic helix-loop-helix transcription factor gene family
in Arabidopsis thaliana.";
Plant Cell 15:2497-2502(2003).
[9]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION BY RED
AND FAR-RED LIGHTS, AND INTERACTION WITH PHYA AND PHYB.
PubMed=15448264; DOI=10.1126/science.1099728;
Huq E., Al-Sady B., Hudson M., Kim C., Apel K., Quail P.H.;
"Phytochrome-interacting factor 1 is a critical bHLH regulator of
chlorophyll biosynthesis.";
Science 305:1937-1941(2004).
[10]
FUNCTION, UBIQUITINATION, AND SUBCELLULAR LOCATION.
PubMed=16359394; DOI=10.1111/j.1365-313X.2005.02606.x;
Shen H., Moon J., Huq E.;
"PIF1 is regulated by light-mediated degradation through the
ubiquitin-26S proteasome pathway to optimize photomorphogenesis of
seedlings in Arabidopsis.";
Plant J. 44:1023-1035(2005).
[11]
FUNCTION.
PubMed=18487351; DOI=10.1105/tpc.108.058859;
Kim D.H., Yamaguchi S., Lim S., Oh E., Park J., Hanada A., Kamiya Y.,
Choi G.;
"SOMNUS, a CCCH-type zinc finger protein in Arabidopsis, negatively
regulates light-dependent seed germination downstream of PIL5.";
Plant Cell 20:1260-1277(2008).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18591656; DOI=10.1073/pnas.0803611105;
Moon J., Zhu L., Shen H., Huq E.;
"PIF1 directly and indirectly regulates chlorophyll biosynthesis to
optimize the greening process in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 105:9433-9438(2008).
[13]
FUNCTION, MUTAGENESIS OF 1-MET--VAL-50; GLU-41; LEU-42; TRP-44;
GLY-47; 85-PHE--LEU-95; LEU-95; 118-ALA--GLY-160; SER-123; ASN-144;
PHE-148; GLY-153; PHE-155 AND GLY-160, INTERACTION WITH PHYA AND PHYB,
PHOSPHORYLATION, AND UBIQUITINATION.
PubMed=18539749; DOI=10.1105/tpc.108.060020;
Shen H., Zhu L., Castillon A., Majee M., Downie B., Huq E.;
"Light-induced phosphorylation and degradation of the negative
regulator PHYTOCHROME-INTERACTING FACTOR1 from Arabidopsis depend upon
its direct physical interactions with photoactivated phytochromes.";
Plant Cell 20:1586-1602(2008).
[14]
INTERACTION WITH RGL2 AND RGA.
STRAIN=cv. Landsberg erecta;
PubMed=20093430; DOI=10.1093/molbev/msq012;
Gallego-Bartolome J., Minguet E.G., Marin J.A., Prat S.,
Blazquez M.A., Alabadi D.;
"Transcriptional diversification and functional conservation between
DELLA proteins in Arabidopsis.";
Mol. Biol. Evol. 27:1247-1256(2010).
[15]
PHOSPHORYLATION AT THR-10; THR-197; SER-202; SER-464; SER-465; SER-466
AND SER-469, UBIQUITINATION, AND MUTAGENESIS OF THR-10; THR-197;
SER-202; SER-464; SER-465; SER-466 AND SER-469.
PubMed=21330376; DOI=10.1074/jbc.M110.186882;
Bu Q., Zhu L., Dennis M.D., Yu L., Lu S.X., Person M.D., Tobin E.M.,
Browning K.S., Huq E.;
"Phosphorylation by CK2 enhances the rapid light-induced degradation
of phytochrome interacting factor 1 in Arabidopsis.";
J. Biol. Chem. 286:12066-12074(2011).
[16]
INTERACTION WITH FHY3.
PubMed=22634759; DOI=10.1105/tpc.112.097022;
Tang W., Wang W., Chen D., Ji Q., Jing Y., Wang H., Lin R.;
"Transposase-derived proteins FHY3/FAR1 interact with PHYTOCHROME-
INTERACTING FACTOR1 to regulate chlorophyll biosynthesis by modulating
HEMB1 during deetiolation in Arabidopsis.";
Plant Cell 24:1984-2000(2012).
-!- FUNCTION: Transcription activator. Regulates negatively
chlorophyll biosynthesis and seed germination in the dark, and
lightinduced degradation of PIF1 relieves this negative regulation
to promote photomorphogenesis. Binds to the G-box motif (5'-
CACGTG-3') found in many light-regulated promoters. Promotes the
expression of SOM, and thus modulates responses to abscisic acid
(ABA) and gibberellic acid (GA). {ECO:0000269|PubMed:15448264,
ECO:0000269|PubMed:16359394, ECO:0000269|PubMed:18487351,
ECO:0000269|PubMed:18539749, ECO:0000269|PubMed:18591656}.
-!- SUBUNIT: Homodimer (Probable). Interacts with the photoactivated
conformer (Pfr) of phytochromes A and B, PHYA and PHYB. Interacts
also with APRR1/TOC1. Binds to RGL2, RGA and FHY3 (via N-
terminus). {ECO:0000269|PubMed:12826627,
ECO:0000269|PubMed:15448264, ECO:0000269|PubMed:18539749,
ECO:0000269|PubMed:20093430, ECO:0000269|PubMed:22634759,
ECO:0000305}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-630400, EBI-630400;
Q8S307:BZR1; NbExp=2; IntAct=EBI-630400, EBI-1803261;
Q9FE22:HFR1; NbExp=3; IntAct=EBI-630400, EBI-626001;
P14713:PHYB; NbExp=3; IntAct=EBI-630400, EBI-300727;
O80536:PIF3; NbExp=6; IntAct=EBI-630400, EBI-625701;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00981, ECO:0000269|PubMed:15448264,
ECO:0000269|PubMed:16359394}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8GZM7-1; Sequence=Displayed;
Name=2;
IsoId=Q8GZM7-2; Sequence=VSP_036107;
Note=May be due to a competing acceptor splice site. No
experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed constitutively in roots, leaves,
stems, and flowers. {ECO:0000269|PubMed:12679534}.
-!- INDUCTION: Repressed by red (R) and far red (FR) light treatments
in a phyB- and phyA-dependent manner.
{ECO:0000269|PubMed:15448264}.
-!- PTM: Phosphorylated at Thr-10, Thr-197, Ser-202, Ser-464, Ser-465,
Ser-466 and Ser-469 by CK2 (PubMed:21330376). Phosphorylated and
ubiquitinated after an exposure to light (especially red and far-
red), in a phytochrome-dependent manner. Modified proteins undergo
a proteasome-dependent degradation. Its stability and degradation
plays a central role in photomorphogenesis of seedlings.
{ECO:0000269|PubMed:16359394, ECO:0000269|PubMed:18539749,
ECO:0000269|PubMed:21330376}.
-!- DISRUPTION PHENOTYPE: Plants overaccumulate free
protochlorophyllide in the darkness and exhibit photooxidative
damage (bleaching) in subsequent light, probably caused by the
photosensitizing activity of this tetrapyrrole intermediate.
{ECO:0000269|PubMed:15448264, ECO:0000269|PubMed:18591656}.
-!- SEQUENCE CAUTION:
Sequence=AAD24380.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF488560; AAN78308.1; -; mRNA.
EMBL; AB103113; BAC56979.1; -; Transcribed_RNA.
EMBL; AC006081; AAD24380.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002685; AEC06977.1; -; Genomic_DNA.
EMBL; CP002685; AEC06978.1; -; Genomic_DNA.
EMBL; CP002685; AEC06979.1; -; Genomic_DNA.
EMBL; CP002685; ANM61700.1; -; Genomic_DNA.
EMBL; CP002685; ANM61701.1; -; Genomic_DNA.
EMBL; CP002685; ANM61702.1; -; Genomic_DNA.
EMBL; CP002685; ANM61703.1; -; Genomic_DNA.
EMBL; AK228820; BAF00716.1; -; mRNA.
EMBL; BT029775; ABM06045.1; -; mRNA.
PIR; A84586; A84586.
RefSeq; NP_001189559.1; NM_001202630.2. [Q8GZM7-1]
RefSeq; NP_001318252.1; NM_001335663.1. [Q8GZM7-1]
RefSeq; NP_001323902.1; NM_001335664.1. [Q8GZM7-1]
RefSeq; NP_001323903.1; NM_001335665.1. [Q8GZM7-2]
RefSeq; NP_001323904.1; NM_001335666.1. [Q8GZM7-1]
RefSeq; NP_001323905.1; NM_001335667.1. [Q8GZM7-2]
RefSeq; NP_849996.1; NM_179665.3. [Q8GZM7-2]
UniGene; At.43003; -.
UniGene; At.69322; -.
ProteinModelPortal; Q8GZM7; -.
SMR; Q8GZM7; -.
BioGrid; 1892; 25.
DIP; DIP-61853N; -.
IntAct; Q8GZM7; 10.
STRING; 3702.AT2G20180.2; -.
iPTMnet; Q8GZM7; -.
PaxDb; Q8GZM7; -.
EnsemblPlants; AT2G20180.1; AT2G20180.1; AT2G20180. [Q8GZM7-2]
EnsemblPlants; AT2G20180.2; AT2G20180.2; AT2G20180. [Q8GZM7-1]
EnsemblPlants; AT2G20180.3; AT2G20180.3; AT2G20180. [Q8GZM7-1]
EnsemblPlants; AT2G20180.4; AT2G20180.4; AT2G20180. [Q8GZM7-1]
EnsemblPlants; AT2G20180.5; AT2G20180.5; AT2G20180. [Q8GZM7-2]
EnsemblPlants; AT2G20180.6; AT2G20180.6; AT2G20180. [Q8GZM7-1]
EnsemblPlants; AT2G20180.7; AT2G20180.7; AT2G20180. [Q8GZM7-2]
GeneID; 816538; -.
Gramene; AT2G20180.1; AT2G20180.1; AT2G20180.
Gramene; AT2G20180.2; AT2G20180.2; AT2G20180.
Gramene; AT2G20180.3; AT2G20180.3; AT2G20180.
Gramene; AT2G20180.4; AT2G20180.4; AT2G20180.
Gramene; AT2G20180.5; AT2G20180.5; AT2G20180.
Gramene; AT2G20180.6; AT2G20180.6; AT2G20180.
Gramene; AT2G20180.7; AT2G20180.7; AT2G20180.
KEGG; ath:AT2G20180; -.
Araport; AT2G20180; -.
TAIR; locus:2061634; AT2G20180.
eggNOG; ENOG410IWC4; Eukaryota.
eggNOG; ENOG41116VE; LUCA.
HOGENOM; HOG000240264; -.
InParanoid; Q8GZM7; -.
OMA; MMYPGMQ; -.
OrthoDB; EOG09360EFL; -.
PhylomeDB; Q8GZM7; -.
PRO; PR:Q8GZM7; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q8GZM7; baseline and differential.
Genevisible; Q8GZM7; AT.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0003677; F:DNA binding; IDA:TAIR.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0010313; F:phytochrome binding; IDA:TAIR.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:TAIR.
GO; GO:0015995; P:chlorophyll biosynthetic process; IMP:TAIR.
GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IMP:TAIR.
GO; GO:0006783; P:heme biosynthetic process; IMP:TAIR.
GO; GO:0009959; P:negative gravitropism; IMP:TAIR.
GO; GO:0010100; P:negative regulation of photomorphogenesis; IMP:TAIR.
GO; GO:0010187; P:negative regulation of seed germination; IMP:TAIR.
GO; GO:0010161; P:red light signaling pathway; IDA:TAIR.
GO; GO:0010099; P:regulation of photomorphogenesis; TAS:TAIR.
GO; GO:0010029; P:regulation of seed germination; TAS:TAIR.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:TAIR.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome; DNA-binding;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 478 Transcription factor PIF1.
/FTId=PRO_0000358829.
DOMAIN 284 333 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
COMPBIAS 339 382 Met-rich.
SITE 47 47 Pfr PHYB binding.
SITE 95 95 Pfr PHYA binding.
SITE 144 144 Pfr PHYA binding.
MOD_RES 10 10 Phosphothreonine; by CK2.
{ECO:0000269|PubMed:21330376}.
MOD_RES 197 197 Phosphothreonine; by CK2.
{ECO:0000269|PubMed:21330376}.
MOD_RES 202 202 Phosphoserine; by CK2.
{ECO:0000269|PubMed:21330376}.
MOD_RES 464 464 Phosphoserine; by CK2.
{ECO:0000269|PubMed:21330376}.
MOD_RES 465 465 Phosphoserine; by CK2.
{ECO:0000269|PubMed:21330376}.
MOD_RES 466 466 Phosphoserine; by CK2.
{ECO:0000269|PubMed:21330376}.
MOD_RES 469 469 Phosphoserine; by CK2.
{ECO:0000269|PubMed:21330376}.
VAR_SEQ 1 71 Missing (in isoform 2).
{ECO:0000303|Ref.5, ECO:0000303|Ref.6}.
/FTId=VSP_036107.
MUTAGEN 1 50 Missing: Normal interaction with PHYA
(Pfr form).
{ECO:0000269|PubMed:18539749}.
MUTAGEN 10 10 T->A: Loss of phosphorylation by CK2.
{ECO:0000269|PubMed:21330376}.
MUTAGEN 41 41 E->A: Loss of interaction with PHYB (Pfr
form). {ECO:0000269|PubMed:18539749}.
MUTAGEN 42 42 L->A: Loss of interaction with PHYB (Pfr
form). {ECO:0000269|PubMed:18539749}.
MUTAGEN 44 44 W->A: Reduced interaction with PHYB (Pfr
form). {ECO:0000269|PubMed:18539749}.
MUTAGEN 47 47 G->A: Loss of interaction with PHYB (Pfr
form). {ECO:0000269|PubMed:18539749}.
MUTAGEN 85 95 Missing: Reduced interaction with PHYA
(Pfr form).
{ECO:0000269|PubMed:18539749}.
MUTAGEN 95 95 L->A: Reduced interaction with PHYA (Pfr
form). Reduced interaction with PHYA (Pfr
form); when associated with A-123; A-153;
or A-160. Loss of interaction with PHYA
(Pfr form); when associated with A-144.
{ECO:0000269|PubMed:18539749}.
MUTAGEN 118 160 Missing: Reduced interaction with PHYA
(Pfr form).
{ECO:0000269|PubMed:18539749}.
MUTAGEN 123 123 S->A: Reduced interaction with PHYA (Pfr
form); when associated with A-95.
{ECO:0000269|PubMed:18539749}.
MUTAGEN 144 144 N->A: Loss of interaction with PHYA (Pfr
form); when associated with A-95.
{ECO:0000269|PubMed:18539749}.
MUTAGEN 148 148 F->A: Normal interaction with PHYA (Pfr
form). {ECO:0000269|PubMed:18539749}.
MUTAGEN 153 153 G->A: Reduced interaction with PHYA (Pfr
form); when associated with A-95.
{ECO:0000269|PubMed:18539749}.
MUTAGEN 155 155 F->A: Normal interaction with PHYA (Pfr
form). {ECO:0000269|PubMed:18539749}.
MUTAGEN 160 160 G->A: Reduced interaction with PHYA (Pfr
form); when associated with A-95.
{ECO:0000269|PubMed:18539749}.
MUTAGEN 197 197 T->A: Loss of phosphorylation by CK2.
{ECO:0000269|PubMed:21330376}.
MUTAGEN 202 202 S->A: Loss of phosphorylation by CK2.
{ECO:0000269|PubMed:21330376}.
MUTAGEN 464 464 S->A: Loss of phosphorylation by CK2.
{ECO:0000269|PubMed:21330376}.
MUTAGEN 465 465 S->A: Loss of phosphorylation by CK2.
{ECO:0000269|PubMed:21330376}.
MUTAGEN 466 466 S->A: Loss of phosphorylation by CK2.
{ECO:0000269|PubMed:21330376}.
MUTAGEN 469 469 S->A: Loss of phosphorylation by CK2.
{ECO:0000269|PubMed:21330376}.
CONFLICT 102 102 D -> G (in Ref. 5; BAF00716).
{ECO:0000305}.
SEQUENCE 478 AA; 52864 MW; 93572A0D4669D350 CRC64;
MHHFVPDFDT DDDYVNNHNS SLNHLPRKSI TTMGEDDDLM ELLWQNGQVV VQNQRLHTKK
PSSSPPKLLP SMDPQQQPSS DQNLFIQEDE MTSWLHYPLR DDDFCSDLLF SAAPTATATA
TVSQVTAARP PVSSTNESRP PVRNFMNFSR LRGDFNNGRG GESGPLLSKA VVRESTQVSP
SATPSAAASE SGLTRRTDGT DSSAVAGGGA YNRKGKAVAM TAPAIEITGT SSSVVSKSEI
EPEKTNVDDR KRKEREATTT DETESRSEET KQARVSTTST KRSRAAEVHN LSERKRRDRI
NERMKALQEL IPRCNKSDKA SMLDEAIEYM KSLQLQIQMM SMGCGMMPMM YPGMQQYMPH
MAMGMGMNQP IPPPSFMPFP NMLAAQRPLP TQTHMAGSGP QYPVHASDPS RVFVPNQQYD
PTSGQPQYPA GYTDPYQQFR GLHPTQPPQF QNQATSYPSS SRVSSSKESE DHGNHTTG


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30-993 SOHLH1 contains 1 basic helix-loop-helix (bHLH) domain. It is a probable transcription factor required during spermatogenesis and oogenesis. 0.05 mg
EIAAB41702 Basic helix-loop-helix transcription factor OUT,Mouse,Mus musculus,Out,Ovary, uterus and testis protein,Tcf23,TCF-23,Transcription factor 23
25-065 NEUROD6 contains 1 basic helix-loop-helix (bHLH) domain. It activates E box-dependent transcription in collaboration with TCF3_E47 and may be a trans-acting factor involved in the development and main 0.05 mg
27-590 NEUROD6 contains 1 basic helix-loop-helix (bHLH) domain. It activates E box-dependent transcription in collaboration with TCF3_E47 and may be a trans-acting factor involved in the development and main 0.05 mg
27-591 NEUROD6 contains 1 basic helix-loop-helix (bHLH) domain. It activates E box-dependent transcription in collaboration with TCF3_E47 and may be a trans-acting factor involved in the development and main 0.05 mg
EIAAB42114 bHLHe34,BHLHE34,Class E basic helix-loop-helix protein 34,Homo sapiens,hTFEC-L,Human,TCFEC,TFEC,TFE-C,TFECL,Transcription factor EC,Transcription factor EC-like
27-568 HES1 belongs to the basic helix-loop-helix family of transcription factors. It is a transcriptional repressor of genes that require a bHLH protein for their transcription. The protein has a particular 0.1 mg
31-179 TCF4 encodes transcription factor 4, a basic helix-turn-helix transcription factor. The protein recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a motif first identified in immunoglobuli 0.05 mg
31-178 TCF4 encodes transcription factor 4, a basic helix-turn-helix transcription factor. The protein recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a motif first identified in immunoglobuli 0.05 mg
EIAAB37697 Basic helix-loop-helix transcription factor scleraxis,bHLHa41,BHLHA41,bHLHa48,Class A basic helix-loop-helix protein 41,Class A basic helix-loop-helix protein 48,Homo sapiens,Human,SCX,SCXA
18-003-44006 Basic helix-loop-helix transcription factor OUT - Transcription factor 23; 11 days pregnant adult female ovary and uterus cDNA. RIKEN full-length enriched library. clone 5031411E05 product transcripti 0.1 mg Protein A
28-090 USF1 encodes a member of the basic helix-loop-helix leucine zipper family, and can function as a cellular transcription factor. The encoded protein can activate transcription through pyrimidine-rich i 0.1 mg
27-413 PTF1A is a pancreas specific transcription factor. Mammalian studies have implicated important roles for the basic helix-loop-helix transcription factor PTF1A-p48 in the development of both exocrine a 0.1 mg
25-056 Transcription factors containing a basic helix-loop-helix (bHLH) motif regulate expression of tissue-specific genes in a number of mammalian and insect systems. DNA-binding activity of the bHLH protei 0.05 mg
28-779 Transcription factors containing a basic helix-loop-helix (bHLH) motif regulate expression of tissue-specific genes in a number of mammalian and insect systems. DNA-binding activity of the bHLH protei 0.1 mg
EIAAB45447 bHLHb11,BHLHB11,Class B basic helix-loop-helix protein 11,Homo sapiens,Human,Major late transcription factor 1,Upstream stimulatory factor 1,USF,USF1


 

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