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Transcriptional regulatory protein DevR (DosR)

 DEVR_MYCTU              Reviewed;         217 AA.
P9WMF9; L0TBX9; P95193; Q79CX8; Q7D625;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
28-MAR-2018, entry version 33.
RecName: Full=DNA-binding transcriptional activator DevR/DosR {ECO:0000305};
Name=devR {ECO:0000303|PubMed:10970762}; Synonyms=dosR;
OrderedLocusNames=Rv3133c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION (MICROBIAL
INFECTION), AND OPERON STRUCTURE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=10970762; DOI=10.1054/tuld.2000.0240;
Dasgupta N., Kapur V., Singh K.K., Das T.K., Sachdeva S.,
Jyothisri K., Tyagi J.S.;
"Characterization of a two-component system, devR-devS, of
Mycobacterium tuberculosis.";
Tuber. Lung Dis. 80:141-159(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[3]
FUNCTION, REGULON, INDUCTION BY HYPOXIA, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=11416222; DOI=10.1073/pnas.121172498;
Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I.,
Schoolnik G.K.;
"Regulation of the Mycobacterium tuberculosis hypoxic response gene
encoding alpha -crystallin.";
Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001).
[4]
DISRUPTION PHENOTYPE IN DBA/2 MICE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=12595424; DOI=10.1128/IAI.71.3.1134-1140.2003;
Parish T., Smith D.A., Kendall S., Casali N., Bancroft G.J.,
Stoker N.G.;
"Deletion of two-component regulatory systems increases the virulence
of Mycobacterium tuberculosis.";
Infect. Immun. 71:1134-1140(2003).
[5]
INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
STRAIN=ATCC 25618 / H37Rv;
PubMed=12953092; DOI=10.1084/jem.20030205;
Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I.,
Dolganov G.M., Sherman D.R., Schoolnik G.K.;
"Inhibition of respiration by nitric oxide induces a Mycobacterium
tuberculosis dormancy program.";
J. Exp. Med. 198:705-713(2003).
[6]
DNA-BINDING, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-54.
STRAIN=ATCC 27294 / TMC 102 / H37Rv;
PubMed=12694625; DOI=10.1046/j.1365-2958.2003.03474.x;
Park H.D., Guinn K.M., Harrell M.I., Liao R., Voskuil M.I., Tompa M.,
Schoolnik G.K., Sherman D.R.;
"Rv3133c/dosR is a transcription factor that mediates the hypoxic
response of Mycobacterium tuberculosis.";
Mol. Microbiol. 48:833-843(2003).
[7]
FUNCTION, PHOSPHORYLATION AT ASP-54 BY DEVS (DOSS), PHOSPHORYLATION BY
DOST, AND REGULON.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15033981; DOI=10.1074/jbc.M401230200;
Roberts D.M., Liao R.P., Wisedchaisri G., Hol W.G., Sherman D.R.;
"Two sensor kinases contribute to the hypoxic response of
Mycobacterium tuberculosis.";
J. Biol. Chem. 279:23082-23087(2004).
[8]
PHOSPHORYLATION AT ASP-54 BY DEVS (DOSS), AND MUTAGENESIS OF ASP-8;
ASP-9; ASP-54 AND LYS-104.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15073296; DOI=10.1099/mic.0.26218-0;
Saini D.K., Malhotra V., Dey D., Pant N., Das T.K., Tyagi J.S.;
"DevR-DevS is a bona fide two-component system of Mycobacterium
tuberculosis that is hypoxia-responsive in the absence of the DNA-
binding domain of DevR.";
Microbiology 150:865-875(2004).
[9]
INDUCTION BY CARBON MONOXIDE (CO).
STRAIN=ATCC 25618 / H37Rv;
PubMed=17609369; DOI=10.1073/pnas.0705054104;
Kumar A., Toledo J.C., Patel R.P., Lancaster J.R. Jr., Steyn A.J.;
"Mycobacterium tuberculosis DosS is a redox sensor and DosT is a
hypoxia sensor.";
Proc. Natl. Acad. Sci. U.S.A. 104:11568-11573(2007).
[10]
INDUCTION BY CARBON MONOXIDE (CO), AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18474359; DOI=10.1016/j.chom.2008.03.007;
Shiloh M.U., Manzanillo P., Cox J.S.;
"Mycobacterium tuberculosis senses host-derived carbon monoxide during
macrophage infection.";
Cell Host Microbe 3:323-330(2008).
[11]
FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR, AND DNA-BINDING.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18359816; DOI=10.1128/JB.01308-07;
Chauhan S., Tyagi J.S.;
"Cooperative binding of phosphorylated DevR to upstream sites is
necessary and sufficient for activation of the Rv3134c-devRS operon in
Mycobacterium tuberculosis: implication in the induction of DevR
target genes.";
J. Bacteriol. 190:4301-4312(2008).
[12]
INDUCTION BY CARBON MONOXIDE (CO), DISRUPTION PHENOTYPE, AND ROLE IN
DORMANCY REGULON.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18400743; DOI=10.1074/jbc.M802274200;
Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S.,
Kramnik I., Agarwal A., Steyn A.J.;
"Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium
tuberculosis dormancy regulon.";
J. Biol. Chem. 283:18032-18039(2008).
[13]
DISRUPTION PHENOTYPE IN GUINEA PIG; MOUSE AND RABBIT.
STRAIN=ATCC 25618 / H37Rv;
PubMed=19103767; DOI=10.1128/IAI.01117-08;
Converse P.J., Karakousis P.C., Klinkenberg L.G., Kesavan A.K.,
Ly L.H., Allen S.S., Grosset J.H., Jain S.K., Lamichhane G.,
Manabe Y.C., McMurray D.N., Nuermberger E.L., Bishai W.R.;
"Role of the dosR-dosS two-component regulatory system in
Mycobacterium tuberculosis virulence in three animal models.";
Infect. Immun. 77:1230-1237(2009).
[14]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=H37Rv;
PubMed=19487478; DOI=10.1128/IAI.01449-08;
Honaker R.W., Leistikow R.L., Bartek I.L., Voskuil M.I.;
"Unique roles of DosT and DosS in DosR regulon induction and
Mycobacterium tuberculosis dormancy.";
Infect. Immun. 77:3258-3263(2009).
[15]
PHOSPHORYLATION AT THR-198 AND THR-205 BY PKNH, AND MUTAGENESIS OF
THR-198 AND THR-205.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20630871; DOI=10.1074/jbc.M110.132894;
Chao J.D., Papavinasasundaram K.G., Zheng X., Chavez-Steenbock A.,
Wang X., Lee G.Q., Av-Gay Y.;
"Convergence of Ser/Thr and two-component signaling to coordinate
expression of the dormancy regulon in Mycobacterium tuberculosis.";
J. Biol. Chem. 285:29239-29246(2010).
[16]
FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF THR-82, AND DNA-BINDING.
STRAIN=ATCC 25618 / H37Rv;
PubMed=21764934; DOI=10.1128/JB.05051-11;
Gautam U.S., Sikri K., Tyagi J.S.;
"The residue threonine 82 of DevR (DosR) is essential for DevR
activation and function in Mycobacterium tuberculosis despite its
atypical location.";
J. Bacteriol. 193:4849-4858(2011).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[18]
FUNCTION, AND DNA-BINDING.
STRAIN=ATCC 25618 / H37Rv;
PubMed=28977726; DOI=10.1111/febs.14284;
Sousa E.H.S., Gonzalez G., Gilles-Gonzalez M.A.;
"Target DNA stabilizes Mycobacterium tuberculosis DevR/DosR
phosphorylation by the full-length oxygen sensors DevS/DosS and
DosT.";
FEBS J. 284:3954-3967(2017).
[19]
REVIEW.
PubMed=25002970; DOI=10.3390/bios3030259;
Sivaramakrishnan S., de Montellano P.R.;
"The DosS-DosT/DosR mycobacterial sensor system.";
Biosensors 3:259-282(2013).
[20] {ECO:0000244|PDB:1ZLJ, ECO:0000244|PDB:1ZLK}
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 144-217 WITH AND WITHOUT
BOUND DNA.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16246368; DOI=10.1016/j.jmb.2005.09.048;
Wisedchaisri G., Wu M., Rice A.E., Roberts D.M., Sherman D.R.,
Hol W.G.;
"Structures of Mycobacterium tuberculosis DosR and DosR-DNA complex
involved in gene activation during adaptation to hypoxic latency.";
J. Mol. Biol. 354:630-641(2005).
[21] {ECO:0000244|PDB:3C3W, ECO:0000244|PDB:3C57}
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND SUBUNIT.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18353359; DOI=10.1016/j.jmb.2008.02.029;
Wisedchaisri G., Wu M., Sherman D.R., Hol W.G.;
"Crystal structures of the response regulator DosR from Mycobacterium
tuberculosis suggest a helix rearrangement mechanism for
phosphorylation activation.";
J. Mol. Biol. 378:227-242(2008).
-!- FUNCTION: Member of the two-component regulatory system DevR/DevS
(also called DosR/DosS) involved in onset of the dormancy response
(PubMed:15033981). Regulates an approximately 48-member regulon
(PubMed:12953092, PubMed:11416222, PubMed:15033981,
PubMed:18400743). When phosphorylated binds and activates the
promoter of DevR regulon genes in response to hypoxia
(PubMed:18359816, PubMed:21764934, PubMed:28977726). The presence
of target DNA increases stability of phospho-DevR in vitro
(PubMed:28977726). Activates its own transcription under hypoxic
but not aerobic conditions, probably binds as a dimer to tandem
binding sites within the devR and hspX promoters
(PubMed:18359816). Accepts a phosphate group from DevS (DosS) and
from DosT (PubMed:15033981, PubMed:15073296, PubMed:21764934,
PubMed:28977726). Does not regulate transcription of dosT
(PubMed:19487478). {ECO:0000269|PubMed:11416222,
ECO:0000269|PubMed:12953092, ECO:0000269|PubMed:15033981,
ECO:0000269|PubMed:15073296, ECO:0000269|PubMed:18359816,
ECO:0000269|PubMed:18400743, ECO:0000269|PubMed:19487478,
ECO:0000269|PubMed:21764934, ECO:0000269|PubMed:28977726}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18353359}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Host cytoplasmic vesicle, host phagosome
{ECO:0000269|PubMed:10970762}. Note=(Microbial infection) In human
monocytes after in vitro infection (PubMed:10970762).
{ECO:0000269|PubMed:10970762}.
-!- INDUCTION: A member of the dormancy regulon. Moderately expressed
under aerobic conditions, it is strongly induced in response to
reduced oxygen tension (hypoxia), low levels of nitric oxide (NO)
and carbon monoxide (CO) (PubMed:11416222, PubMed:12953092,
PubMed:17609369, PubMed:18474359, PubMed:18400743). It is hoped
that this regulon will give insight into the latent, or dormant
phase of infection. Expression under hypoxic conditions, but not
aerobically, is autoregulated. Member of the Rv3134c-devR-devS
operon (PubMed:10970762). {ECO:0000269|PubMed:10970762,
ECO:0000269|PubMed:11416222, ECO:0000269|PubMed:12953092,
ECO:0000269|PubMed:17609369, ECO:0000269|PubMed:18400743,
ECO:0000269|PubMed:18474359}.
-!- PTM: Phosphorylated on Asp-54 by both DevS (DosS) and DosT
(PubMed:15033981, PubMed:15073296, PubMed:21764934).
Phosphorylated on Thr-198 and Thr-205 by PknH, which enhances DevR
dimerization (PubMed:20630871). Aspartate phosphorylation and
threonine phosphorylation cooperatively enhance DevR binding to
DNA (PubMed:20630871). {ECO:0000269|PubMed:15033981,
ECO:0000269|PubMed:15073296, ECO:0000269|PubMed:20630871,
ECO:0000269|PubMed:21764934}.
-!- DISRUPTION PHENOTYPE: Strains deleted for this gene show
hypervirulence upon intravenous innoculation in the mouse and
DBA/2 model (PubMed:12595424). However contradictory results were
shown for using a devR/devS deletion strain in rabbits, guinea
pigs and C57BL/6 mice (PubMed:19103767). All studies agree that
deletion strains fail to induce the dormancy regulon genes in
response to hypoxia, NO, and CO (PubMed:11416222, PubMed:12694625,
PubMed:18474359, PubMed:18400743, PubMed:19487478). Deletion has
no effect on expression of dosT (PubMed:19487478).
{ECO:0000269|PubMed:11416222, ECO:0000269|PubMed:12595424,
ECO:0000269|PubMed:12694625, ECO:0000269|PubMed:18400743,
ECO:0000269|PubMed:18474359, ECO:0000269|PubMed:19103767,
ECO:0000269|PubMed:19487478}.
-!- MISCELLANEOUS: The dev nomenclature derives from the increased
expression (differentially expressed in virulent strain, dev) of
these genes in virulent H37Rv versus avirulent H37Ra. The dos
nomenclature derives from experiments in M.bovis showing the same
genes are essential for dormancy survival (dos).
{ECO:0000305|PubMed:25002970}.
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EMBL; U22037; AAD17452.1; -; Genomic_DNA.
EMBL; AL123456; CCP45943.1; -; Genomic_DNA.
PIR; F70645; F70645.
RefSeq; NP_217649.1; NC_000962.3.
RefSeq; WP_003416369.1; NZ_KK339370.1.
PDB; 1ZLJ; X-ray; 2.00 A; A/B/C/D/E/F/G/H=144-217.
PDB; 1ZLK; X-ray; 3.10 A; A/B=144-217.
PDB; 3C3W; X-ray; 2.20 A; A/B=1-217.
PDB; 3C57; X-ray; 1.70 A; A/B=144-217.
PDBsum; 1ZLJ; -.
PDBsum; 1ZLK; -.
PDBsum; 3C3W; -.
PDBsum; 3C57; -.
ProteinModelPortal; P9WMF9; -.
SMR; P9WMF9; -.
IntAct; P9WMF9; 1.
STRING; 83332.Rv3133c; -.
ChEMBL; CHEMBL6064; -.
iPTMnet; P9WMF9; -.
PaxDb; P9WMF9; -.
EnsemblBacteria; CCP45943; CCP45943; Rv3133c.
GeneID; 888842; -.
KEGG; mtu:Rv3133c; -.
TubercuList; Rv3133c; -.
eggNOG; ENOG4107NGZ; Bacteria.
eggNOG; COG2197; LUCA.
KO; K07695; -.
OMA; QDRYVFE; -.
PhylomeDB; P9WMF9; -.
PRO; PR:P9WMF9; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005829; C:cytosol; IDA:MTBBASE.
GO; GO:0005615; C:extracellular space; IDA:MTBBASE.
GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-SubCell.
GO; GO:0072493; C:host cell endosome lumen; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
GO; GO:0003700; F:DNA binding transcription factor activity; IMP:MTBBASE.
GO; GO:0022611; P:dormancy process; IDA:MTBBASE.
GO; GO:0009405; P:pathogenesis; IMP:MTBBASE.
GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:MTBBASE.
GO; GO:0019217; P:regulation of fatty acid metabolic process; IDA:MTBBASE.
GO; GO:1902882; P:regulation of response to oxidative stress; IDA:MTBBASE.
GO; GO:0001666; P:response to hypoxia; IMP:MTBBASE.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd06170; LuxR_C_like; 1.
CDD; cd00156; REC; 1.
InterPro; IPR011006; CheY-like_superfamily.
InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
InterPro; IPR000792; Tscrpt_reg_LuxR_C.
Pfam; PF00196; GerE; 1.
Pfam; PF00072; Response_reg; 1.
PRINTS; PR00038; HTHLUXR.
SMART; SM00421; HTH_LUXR; 1.
SMART; SM00448; REC; 1.
SUPFAM; SSF46894; SSF46894; 1.
SUPFAM; SSF52172; SSF52172; 1.
PROSITE; PS00622; HTH_LUXR_1; 1.
PROSITE; PS50043; HTH_LUXR_2; 1.
PROSITE; PS50110; RESPONSE_REGULATORY; 1.
1: Evidence at protein level;
3D-structure; Activator; Complete proteome; Cytoplasm; DNA-binding;
Host cytoplasmic vesicle; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation;
Two-component regulatory system.
CHAIN 1 217 DNA-binding transcriptional activator
DevR/DosR.
/FTId=PRO_0000392625.
DOMAIN 3 119 Response regulatory.
{ECO:0000255|PROSITE-ProRule:PRU00169}.
DOMAIN 143 208 HTH luxR-type. {ECO:0000255|PROSITE-
ProRule:PRU00411}.
DNA_BIND 167 186 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00411}.
MOD_RES 54 54 4-aspartylphosphate.
{ECO:0000255|PROSITE-ProRule:PRU00169,
ECO:0000305|PubMed:15033981,
ECO:0000305|PubMed:15073296}.
MOD_RES 198 198 Phosphothreonine; by PknH.
{ECO:0000269|PubMed:20630871}.
MOD_RES 205 205 Phosphothreonine; by PknH.
{ECO:0000269|PubMed:20630871}.
MUTAGEN 8 8 D->N: No phosphorylation by DevS (DosS).
{ECO:0000269|PubMed:15073296}.
MUTAGEN 9 9 D->N: No phosphorylation by DevS (DosS).
{ECO:0000269|PubMed:15073296}.
MUTAGEN 54 54 D->E: Able to bind DNA, no longer induces
hypoxic response.
{ECO:0000269|PubMed:12694625,
ECO:0000269|PubMed:15073296}.
MUTAGEN 54 54 D->V: No phosphorylation by DevS (DosS)
nor by DosT.
{ECO:0000269|PubMed:12694625,
ECO:0000269|PubMed:15073296}.
MUTAGEN 82 82 T->A: No longer induces expression of
DevR regulon under hypoxic conditions,
phosphorylated slowly and incompletely by
DevS, decreased cooperative binding of
target DNA.
{ECO:0000269|PubMed:21764934}.
MUTAGEN 104 104 K->E: No phosphorylation by DevS (DosS).
{ECO:0000269|PubMed:15073296}.
MUTAGEN 198 198 T->A: Decreases phosphorylation by PknH.
{ECO:0000269|PubMed:20630871}.
MUTAGEN 205 205 T->A: No phosphorylation by PknH.
{ECO:0000269|PubMed:20630871}.
STRAND 2 7 {ECO:0000244|PDB:3C3W}.
HELIX 11 22 {ECO:0000244|PDB:3C3W}.
STRAND 27 35 {ECO:0000244|PDB:3C3W}.
HELIX 36 46 {ECO:0000244|PDB:3C3W}.
STRAND 49 53 {ECO:0000244|PDB:3C3W}.
STRAND 55 57 {ECO:0000244|PDB:3C3W}.
HELIX 62 72 {ECO:0000244|PDB:3C3W}.
STRAND 77 80 {ECO:0000244|PDB:3C3W}.
HELIX 81 83 {ECO:0000244|PDB:3C3W}.
STRAND 84 86 {ECO:0000244|PDB:3C3W}.
HELIX 87 96 {ECO:0000244|PDB:3C3W}.
HELIX 101 121 {ECO:0000244|PDB:3C3W}.
HELIX 122 124 {ECO:0000244|PDB:3C3W}.
HELIX 127 143 {ECO:0000244|PDB:3C3W}.
TURN 146 149 {ECO:0000244|PDB:3C3W}.
HELIX 152 162 {ECO:0000244|PDB:3C57}.
HELIX 167 174 {ECO:0000244|PDB:3C57}.
HELIX 178 192 {ECO:0000244|PDB:3C57}.
HELIX 199 207 {ECO:0000244|PDB:3C3W}.
TURN 208 210 {ECO:0000244|PDB:3C3W}.
SEQUENCE 217 AA; 23294 MW; 1BA535C26CC4EB51 CRC64;
MVKVFLVDDH EVVRRGLVDL LGADPELDVV GEAGSVAEAM ARVPAARPDV AVLDVRLPDG
NGIELCRDLL SRMPDLRCLI LTSYTSDEAM LDAILAGASG YVVKDIKGME LARAVKDVGA
GRSLLDNRAA AALMAKLRGA AEKQDPLSGL TDQERTLLGL LSEGLTNKQI ADRMFLAEKT
VKNYVSRLLA KLGMERRTQA AVFATELKRS RPPGDGP


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H-6096.0001 HTLV_1 Tax (11_19) Salt Trifluoroacetate Binding _ Synonym HTLV_1 Trans_Activating Transcriptional Regulatory Protein (16_24) (strains ATK, Caribbean), HTLV_1 X_Lor Protein (16_24) (strains ATK, Ca 1.0 mg
H-6096.0001 HTLV_1 Tax (11_19) Salt Trifluoroacetate Binding _ Synonym HTLV_1 Trans_Activating Transcriptional Regulatory Protein (16_24) (strains ATK, Caribbean), HTLV_1 X_Lor Protein (16_24) (strains ATK, Ca 1.0 mg
H-6096.0005 HTLV_1 Tax (11_19) Salt Trifluoroacetate Binding _ Synonym HTLV_1 Trans_Activating Transcriptional Regulatory Protein (16_24) (strains ATK, Caribbean), HTLV_1 X_Lor Protein (16_24) (strains ATK, Ca 5.0 mg
H-6096.0005 HTLV_1 Tax (11_19) Salt Trifluoroacetate Binding _ Synonym HTLV_1 Trans_Activating Transcriptional Regulatory Protein (16_24) (strains ATK, Caribbean), HTLV_1 X_Lor Protein (16_24) (strains ATK, Ca 5.0 mg
10-288-22393F Cofactor required for Sp1 transcriptional activation subunit 9 - Transcriptional coactivator CRSP33; RNA polymerase transcriptional regulation mediator subunit 7 homolog; hMED7; Activator-recruited co 0.05 mg
10-288-22393F Cofactor required for Sp1 transcriptional activation subunit 9 - Transcriptional coactivator CRSP33; RNA polymerase transcriptional regulation mediator subunit 7 homolog; hMED7; Activator-recruited co 0.1 mg
18-003-43107 Cofactor required for Sp1 transcriptional activation subunit 9 - Transcriptional coactivator CRSP33; RNA polymerase transcriptional regulation mediator subunit 7 homolog; hMED7; Activator-recruited co 0.05 mg Aff Pur
29-051 ZNF415 is involved in transcriptional regulation. The transcriptional activity differed among the various isoforms. All isoforms except isoform 3 seem to suppress the transcriptional activities of AP- 0.05 mg
25-501 ZNF415 is involved in transcriptional regulation. The transcriptional activity differed among the various isoforms. All isoforms except isoform 3 seem to suppress the transcriptional activities of AP- 0.05 mg
EIAAB27168 Na(+)_H(+) exchange regulatory cofactor NHE-RF2,NHE3 kinase A regulatory protein E3KARP,Nherf2,NHERF-2,Rat,Rattus norvegicus,SIP-1,Slc9a3r2,Sodium-hydrogen exchanger regulatory factor 2,Solute carrier
28-789 Friend leukemia integration 1 (Fli-1) is a member of the ETS family of transcriptional regulatory proteins that contain a highly conserved and structurally unique DNA binding ETS domain. 0.1 mg
EIAAB41255 ADA2-like protein,Homo sapiens,Human,KL04P,TADA2A,TADA2L,Transcriptional adapter 2-alpha,Transcriptional adapter 2-like
EIAAB41259 Homo sapiens,Human,SPT3-associated factor 42,STAF42,TADA1,TADA1L,Transcriptional adapter 1,Transcriptional adapter 1-like protein
EIAAB41253 ADA2-like protein,Mouse,Mus musculus,Tada2a,Tada2l,Transcriptional adapter 2-alpha,Transcriptional adapter 2-like
EIAAB41256 ADA2-like protein,Bos taurus,Bovine,TADA2A,TADA2L,Transcriptional adapter 2-alpha,Transcriptional adapter 2-like
EIAAB41257 ADA2-like protein,Rat,Rattus norvegicus,Tada2a,Tada2l,Transcriptional adapter 2-alpha,Transcriptional adapter 2-like
EIAAB27171 Mouse,Mus musculus,Na(+)_H(+) exchange regulatory cofactor NHE-RF2,NHE3 kinase A regulatory protein E3KARP,Nherf2,NHERF-2,Octs2,SIP-1,Slc9a3r2,Sodium-hydrogen exchanger regulatory factor 2,Solute carr
EIAAB27169 Homo sapiens,Human,Na(+)_H(+) exchange regulatory cofactor NHE-RF2,NHE3 kinase A regulatory protein E3KARP,NHERF2,NHERF-2,SIP-1,SLC9A3R2,Sodium-hydrogen exchanger regulatory factor 2,Solute carrier fa


 

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