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Probable mediator of RNA polymerase II transcription subunit 37e (Heat shock 70 kDa protein 1) (Heat shock cognate 70 kDa protein 1) (Heat shock cognate protein 70-1) (AtHsc70-1) (Heat shock protein 70-1) (AtHsp70-1) (Protein EARLY-RESPONSIVE TO DEHYDRATION 2)

 MD37E_ARATH             Reviewed;         651 AA.
P22953; Q93VU6; Q9LZ52;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 3.
25-APR-2018, entry version 167.
RecName: Full=Probable mediator of RNA polymerase II transcription subunit 37e;
AltName: Full=Heat shock 70 kDa protein 1;
AltName: Full=Heat shock cognate 70 kDa protein 1;
AltName: Full=Heat shock cognate protein 70-1;
Short=AtHsc70-1;
AltName: Full=Heat shock protein 70-1;
Short=AtHsp70-1;
AltName: Full=Protein EARLY-RESPONSIVE TO DEHYDRATION 2;
Name=MED37E; Synonyms=ERD2, HSC70-1, HSP70-1, MED37_4;
OrderedLocusNames=At5g02500; ORFNames=T22P11.90;
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], AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=8049382; DOI=10.1007/BF00043887;
Wu S.H., Wang C., Chen J., Lin B.-L.;
"Isolation of a cDNA encoding a 70 kDa heat-shock cognate protein
expressed in vegetative tissues of Arabidopsis thaliana.";
Plant Mol. Biol. 25:577-583(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-120, AND INDUCTION.
PubMed=16666375; DOI=10.1104/pp.88.3.731;
Wu C.H., Caspar T., Browse J., Lindquist S., Somerville C.R.;
"Characterization of an hsp70 cognate gene family in Arabidopsis.";
Plant Physiol. 88:731-740(1988).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-651.
STRAIN=cv. Ostwestfalen; TISSUE=Leaf;
King K.;
Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
[7]
INDUCTION BY DEHYDRATION STRESS AND ABA.
PubMed=8075396; DOI=10.1007/BF00028874;
Kiyosue T., Yamaguchi-shinozaki K., Shinozaki K.;
"Cloning of cDNAs for genes that are early-responsive to dehydration
stress (ERDs) in Arabidopsis thaliana L.: identification of three ERDs
as HSP cognate genes.";
Plant Mol. Biol. 25:791-798(1994).
[8]
INTERACTION WITH TIR.
STRAIN=cv. Columbia;
Kroczynska B., Ciesielski A., Stachnik K.;
"The nucleotide sequence of a cDNA encoding the AtTIR, a TIR-like
resistance protein in Arabidopsis thaliana.";
(er) Plant Gene Register PGR99-172(1999).
[9]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11599561; DOI=10.1379/1466-1268(2001)006<0201:GAOTHS>2.0.CO;2;
Lin B.L., Wang J.S., Liu H.C., Chen R.W., Meyer Y., Barakat A.,
Delseny M.;
"Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana.";
Cell Stress Chaperones 6:201-208(2001).
[10]
DNAK GENE SUBFAMILY, INDUCTION, AND DEVELOPMENTAL STAGE.
PubMed=11402207; DOI=10.1104/pp.126.2.789;
Sung D.Y., Vierling E., Guy C.L.;
"Comprehensive expression profile analysis of the Arabidopsis Hsp70
gene family.";
Plant Physiol. 126:789-800(2001).
[11]
INTERACTION WITH HSFA1A/HSF1.
PubMed=11807141; DOI=10.1093/jexbot/53.367.371;
Kim B.H., Schoeffl F.;
"Interaction between Arabidopsis heat shock transcription factor 1 and
70 kDa heat shock proteins.";
J. Exp. Bot. 53:371-375(2002).
[12]
FUNCTION.
PubMed=12805626; DOI=10.1104/pp.102.019398;
Sung D.Y., Guy C.L.;
"Physiological and molecular assessment of altered expression of
Hsc70-1 in Arabidopsis. Evidence for pleiotropic consequences.";
Plant Physiol. 132:979-987(2003).
[13]
INDUCTION.
PubMed=15805473; DOI=10.1104/pp.104.058958;
Aparicio F., Thomas C.L., Lederer C., Niu Y., Wang D., Maule A.J.;
"Virus induction of heat shock protein 70 reflects a general response
to protein accumulation in the plant cytosol.";
Plant Physiol. 138:529-536(2005).
[14]
INTERACTION WITH BAG3 AND BAG5.
PubMed=16003391; DOI=10.1038/sj.cdd.4401712;
Kang C.H., Jung W.Y., Kang Y.H., Kim J.Y., Kim D.G., Jeong J.C.,
Baek D.W., Jin J.B., Lee J.Y., Kim M.O., Chung W.S., Mengiste T.,
Koiwa H., Kwak S.S., Bahk J.D., Lee S.Y., Nam J.S., Yun D.J.,
Cho M.J.;
"AtBAG6, a novel calmodulin-binding protein, induces programmed cell
death in yeast and plants.";
Cell Death Differ. 13:84-95(2006).
[15]
INTERACTION WITH BAG4.
PubMed=16636050; DOI=10.1074/jbc.M511794200;
Doukhanina E.V., Chen S., van der Zalm E., Godzik A., Reed J.,
Dickman M.B.;
"Identification and functional characterization of the BAG protein
family in Arabidopsis thaliana.";
J. Biol. Chem. 281:18793-18801(2006).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[17]
FUNCTION, INTERACTION WITH SGT1B, AND SUBCELLULAR LOCATION.
PubMed=18065690; DOI=10.1105/tpc.107.051896;
Noel L.D., Cagna G., Stuttmann J., Wirthmueller L., Betsuyaku S.,
Witte C.P., Bhat R., Pochon N., Colby T., Parker J.E.;
"Interaction between SGT1 and cytosolic/nuclear HSC70 chaperones
regulates Arabidopsis immune responses.";
Plant Cell 19:4061-4076(2007).
[18]
INTERACTION WITH WPP1; WPP2 AND WIT1, AND FUNCTION.
PubMed=19617588; DOI=10.1104/pp.109.143404;
Brkljacic J., Zhao Q., Meier I.;
"WPP-domain proteins mimic the activity of the HSC70-1 chaperone in
preventing mistargeting of RanGAP1-anchoring protein WIT1.";
Plant Physiol. 151:142-154(2009).
[19]
INTERACTION WITH AMSH3.
PubMed=20543027; DOI=10.1105/tpc.110.075952;
Isono E., Katsiarimpa A., Mueller I.K., Anzenberger F.,
Stierhof Y.-D., Geldner N., Chory J., Schwechheimer C.;
"The deubiquitinating enzyme AMSH3 is required for intracellular
trafficking and vacuole biogenesis in Arabidopsis thaliana.";
Plant Cell 22:1826-1837(2010).
[20]
INTERACTION WITH OEP61.
PubMed=21612577; DOI=10.1042/BJ20110448;
von Loeffelholz O., Kriechbaumer V., Ewan R.A., Jonczyk R.,
Lehmann S., Young J.C., Abell B.M.;
"OEP61 is a chaperone receptor at the plastid outer envelope.";
Biochem. J. 438:143-153(2011).
[21]
SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=21418353; DOI=10.1111/j.1365-313X.2011.04558.x;
Jungkunz I., Link K., Vogel F., Voll L.M., Sonnewald S., Sonnewald U.;
"AtHsp70-15-deficient Arabidopsis plants are characterized by reduced
growth, a constitutive cytosolic protein response and enhanced
resistance to TuMV.";
Plant J. 66:983-995(2011).
[22]
IDENTIFICATION, SUBUNIT, AND NOMENCLATURE.
PubMed=22021418; DOI=10.1104/pp.111.188300;
Mathur S., Vyas S., Kapoor S., Tyagi A.K.;
"The Mediator complex in plants: structure, phylogeny, and expression
profiling of representative genes in a dicot (Arabidopsis) and a
monocot (rice) during reproduction and abiotic stress.";
Plant Physiol. 157:1609-1627(2011).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22092075; DOI=10.1021/pr200917t;
Aryal U.K., Krochko J.E., Ross A.R.;
"Identification of phosphoproteins in Arabidopsis thaliana leaves
using polyethylene glycol fractionation, immobilized metal-ion
affinity chromatography, two-dimensional gel electrophoresis and mass
spectrometry.";
J. Proteome Res. 11:425-437(2012).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: Component of the Mediator complex, a coactivator
involved in the regulated transcription of nearly all RNA
polymerase II-dependent genes. Mediator functions as a bridge to
convey information from gene-specific regulatory proteins to the
basal RNA polymerase II transcription machinery. The Mediator
complex, having a compact conformation in its free form, is
recruited to promoters by direct interactions with regulatory
proteins and serves for the assembly of a functional preinitiation
complex with RNA polymerase II and the general transcription
factors (By similarity). {ECO:0000250}.
-!- FUNCTION: Heat shock protein probably involved in defense
response. Chaperone involved in protein targeting to chloroplasts.
May cooperate with SGT1 and HSP90 in R gene-mediated resistance
towards the oomycete H.parasitica (downy mildew). Plays a role
with WPP-domain proteins in facilitating WIT1 nuclear envelope
targeting. {ECO:0000269|PubMed:12805626,
ECO:0000269|PubMed:18065690, ECO:0000269|PubMed:19617588}.
-!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
preexistent proteins against aggregation and mediate the folding
of newly translated polypeptides in the cytosol as well as within
organelles. These chaperones participate in all these processes
through their ability to recognize nonnative conformations of
other proteins. They bind extended peptide segments with a net
hydrophobic character exposed by polypeptides during translation
and membrane translocation, or following stress-induced damage (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Binds to the deubiquitinating enzyme AMSH3. Interacts
with SGT1B (via SGS domain). Interacts with OEP61. Interacts with
HSFA1A/HSF1. Interacts with BAG3, BAG4 and BAG5. Interacts with
WPP1, WPP2 and WIT1. Component of a ternary complex composed of
WPP1, HSP70-1 and WIT1. Component of the Mediator complex
(Probable). Binds to TIR. {ECO:0000269|PubMed:11807141,
ECO:0000269|PubMed:16003391, ECO:0000269|PubMed:16636050,
ECO:0000269|PubMed:18065690, ECO:0000269|PubMed:19617588,
ECO:0000269|PubMed:20543027, ECO:0000269|PubMed:21612577,
ECO:0000269|PubMed:22021418, ECO:0000269|Ref.8, ECO:0000305}.
-!- INTERACTION:
Q9SUT5:SGT1B; NbExp=3; IntAct=EBI-1238845, EBI-1581364;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=P22953-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Expressed at a substantial level during normal
growth in root, stem, leaf and flower tissues, but not in
siliques. {ECO:0000269|PubMed:8049382}.
-!- DEVELOPMENTAL STAGE: Down-regulated during seed maturation. Up-
regulated during germination. {ECO:0000269|PubMed:11402207}.
-!- INDUCTION: By heat shock, cold, dehydration stress and abscisic
acid (ABA). Up-regulated by virus infection.
{ECO:0000269|PubMed:11402207, ECO:0000269|PubMed:15805473,
ECO:0000269|PubMed:16666375, ECO:0000269|PubMed:8075396}.
-!- DISRUPTION PHENOTYPE: No visible phenotype.
{ECO:0000269|PubMed:21418353}.
-!- MISCELLANEOUS: Plants overexpressing HSC70-1 show disabled immune
responses, enhanced tolerance to heat shock and altered plant
growth and development.
-!- SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33)
family. DnaK subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X74604; CAA52684.1; -; mRNA.
EMBL; AL162971; CAB85987.1; -; Genomic_DNA.
EMBL; CP002688; AED90480.1; -; Genomic_DNA.
EMBL; AY035123; AAK59628.2; -; mRNA.
EMBL; AY057481; AAL09715.1; -; mRNA.
EMBL; AY120747; AAM53305.1; -; mRNA.
EMBL; BT002754; AAO22583.1; -; mRNA.
EMBL; AH001335; AAA32819.1; -; Genomic_DNA.
EMBL; X77199; CAA54419.1; -; Genomic_DNA.
PIR; S46302; S46302.
PIR; T48271; T48271.
RefSeq; NP_195870.1; NM_120328.5. [P22953-1]
UniGene; At.23663; -.
ProteinModelPortal; P22953; -.
SMR; P22953; -.
BioGrid; 16298; 32.
IntAct; P22953; 9.
MINT; P22953; -.
STRING; 3702.AT5G02500.1; -.
TCDB; 1.A.33.1.1; the cation channel-forming heat shock protein-70 (hsp70) family.
iPTMnet; P22953; -.
SWISS-2DPAGE; P22953; -.
World-2DPAGE; 0003:P22953; -.
PaxDb; P22953; -.
PRIDE; P22953; -.
EnsemblPlants; AT5G02500.1; AT5G02500.1; AT5G02500. [P22953-1]
GeneID; 831020; -.
Gramene; AT5G02500.1; AT5G02500.1; AT5G02500. [P22953-1]
KEGG; ath:AT5G02500; -.
Araport; AT5G02500; -.
TAIR; locus:2181833; AT5G02500.
eggNOG; KOG0101; Eukaryota.
eggNOG; COG0443; LUCA.
HOGENOM; HOG000228135; -.
InParanoid; P22953; -.
KO; K03283; -.
OMA; MDKKAIH; -.
OrthoDB; EOG093604KP; -.
PhylomeDB; P22953; -.
Reactome; R-ATH-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-ATH-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-ATH-3371568; Attenuation phase.
Reactome; R-ATH-3371571; HSF1-dependent transactivation.
Reactome; R-ATH-6798695; Neutrophil degranulation.
Reactome; R-ATH-72163; mRNA Splicing - Major Pathway.
Reactome; R-ATH-8876725; Protein methylation.
PRO; PR:P22953; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; P22953; baseline and differential.
Genevisible; P22953; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0022626; C:cytosolic ribosome; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005730; C:nucleolus; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
GO; GO:0098542; P:defense response to other organism; IMP:TAIR.
GO; GO:0010187; P:negative regulation of seed germination; IMP:TAIR.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009409; P:response to cold; IEP:TAIR.
GO; GO:0009408; P:response to heat; IMP:UniProtKB.
GO; GO:0009615; P:response to virus; IEP:TAIR.
GO; GO:0090332; P:stomatal closure; IMP:TAIR.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
PANTHER; PTHR19375; PTHR19375; 1.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Chaperone;
Complete proteome; Cytoplasm; Nucleotide-binding; Nucleus;
Plant defense; Reference proteome; Stress response; Transcription;
Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 651 Probable mediator of RNA polymerase II
transcription subunit 37e.
/FTId=PRO_0000078344.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895}.
CONFLICT 65 65 N -> S (in Ref. 6; CAA54419).
{ECO:0000305}.
CONFLICT 195 195 S -> R (in Ref. 6; CAA54419).
{ECO:0000305}.
CONFLICT 195 195 S -> T (in Ref. 2; CAA52684).
{ECO:0000305}.
CONFLICT 372 372 D -> V (in Ref. 6; CAA54419).
{ECO:0000305}.
CONFLICT 376 376 A -> V (in Ref. 6; CAA54419).
{ECO:0000305}.
CONFLICT 507 507 I -> V (in Ref. 6; CAA54419).
{ECO:0000305}.
SEQUENCE 651 AA; 71358 MW; BD689BA0C936A420 CRC64;
MSGKGEGPAI GIDLGTTYSC VGVWQHDRVE IIANDQGNRT TPSYVAFTDS ERLIGDAAKN
QVAMNPVNTV FDAKRLIGRR FSDSSVQSDM KLWPFKIQAG PADKPMIYVE YKGEEKEFAA
EEISSMVLIK MREIAEAYLG VTIKNAVVTV PAYFNDSQRQ ATKDAGVIAG LNVMRIINEP
TAAAIAYGLD KKATSVGEKN VLIFDLGGGT FDVSLLTIEE GIFEVKATAG DTHLGGEDFD
NRMVNHFVQE FKRKSKKDIT GNPRALRRLR TSCERAKRTL SSTAQTTIEI DSLYEGIDFY
STITRARFEE LNMDLFRKCM EPVEKCLRDA KMDKSTVHDV VLVGGSTRIP KVQQLLQDFF
NGKELCKSIN PDEAVAYGAA VQGAILSGEG NEKVQDLLLL DVTPLSLGLE TAGGVMTTLI
PRNTTIPTKK EQVFSTYSDN QPGVLIQVYE GERARTKDNN LLGKFELSGI PPAPRGVPQI
TVCFDIDANG ILNVSAEDKT TGQKNKITIT NDKGRLSKDE IEKMVQEAEK YKSEDEEHKK
KVEAKNALEN YAYNMRNTIQ DEKIGEKLPA ADKKKIEDSI EQAIQWLEGN QLAEADEFED
KMKELESICN PIIAKMYQGA GGEAGGPGAS GMDDDAPPAS GGAGPKIEEV D


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10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.01 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 1 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.05 mg
18-003-42935 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg Protein A
18-003-43409 Heat shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg Protein A
U0693h CLIA 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive protein 2 96T
E0693h ELISA 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive protein 96T
10-782-55038 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.2 mg
10-782-55038 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.05 mg
E0693h ELISA kit 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive pro 96T
MEDCLA337-1 Heat Shock Protein 70 (HSP70), Heat Shock Cognate Protein 70 (HSC70), Clone 8B11, Mab anti_Hu,Ms,Rt; prfn_NO frzn, IH_WB 1 ml.
MEDCLA337-01 Heat Shock Protein 70 (HSP70), Heat Shock Cognate Protein 70 (HSC70), Clone 8B11, Mab anti_Hu,Ms,Rt; prfn_NO frzn, IH_WB 0.1 ml.
AS05 083A rabbit polyclonal HSP70 per HSC70 Heat shock protein 70 per Heat shock cognate protein 70, Affinity purified 50
AS05 083 rabbit polyclonal HSP70 per HSC70 | Heat shock protein 70 per Heat shock cognate protein 70 (serum) 100
AS07 233 rabbit polyclonal HSC70 per HSP70 | heat shock cognate protein 70 per heat shock protein 70 100
YSGSPP761E Heat Shock Cognate 70 (HSC70), Heat Shock Protein 73 (Hsp73), Bovine recombinant, Biotin conjugate 100 µg.
YSGSPP761B Heat Shock Cognate 70 (HSC70), Heat Shock Protein 73 (Hsp73), Bovine recombinant, Biotin conjugate 20 µg.
YSGSPP752E Heat Shock Cognate 70 (HSC70), Heat Shock Protein 73 (Hsp73), Bovine recombinant ATPase Fragment 100 µg.
YSGSPP752B Heat Shock Cognate 70 (HSC70), Heat Shock Protein 73 (Hsp73), Bovine recombinant ATPase Fragment 20 µg.
YSGSPA758C Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), ~72&73kD, Rabbit anti_Fish; WB 25 µl.
YSGSPA758E Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), ~72&73kD, Rabbit anti_Fish; WB 100 µl.
YSGSPP751E Heat Shock Cognate 70 (HSC70), Heat Shock Protein 73 (Hsp73), Bovine recombinant 100 µg.
YSGSPP751B Heat Shock Cognate 70 (HSC70), Heat Shock Protein 73 (Hsp73), Bovine recombinant 20 µg.
EIAAB11549 DnaJ homolog subfamily B member 5,Dnajb5,Heat shock protein cognate 40,Heat shock protein Hsp40-3,Hsc40,Hsc40,Mouse,Mus musculus


 

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