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Heat shock protein HSP 90-beta (Heat shock 84 kDa) (HSP 84) (HSP84)

 HS90B_RAT               Reviewed;         724 AA.
P34058; Q1PSW2; Q66H55; Q68GV5; Q9QWC6;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 173.
RecName: Full=Heat shock protein HSP 90-beta;
AltName: Full=Heat shock 84 kDa;
Short=HSP 84;
Short=HSP84;
Name=Hsp90ab1; Synonyms=Hsp84, Hspcb;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1525042; DOI=10.1016/0960-0760(92)90089-2;
McGuire J.A., Poellinger L., Wikstroem A.-C., Gustafsson J.-A.;
"Cloning and regulation by glucocorticoid receptor ligands of a rat
hsp90.";
J. Steroid Biochem. Mol. Biol. 42:813-822(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Brown Norway/NHsdMcwi, and SS/JrHsdMcwi; TISSUE=Heart;
PubMed=15808839; DOI=10.1016/j.yjmcc.2005.02.005;
Shi Y., Hutchins W., Ogawa H., Chang C.-C., Pritchard K.A. Jr.,
Zhang C., Khampang P., Lazar J., Jacob H.J., Rafiee P., Baker J.E.;
"Increased resistance to myocardial ischemia in the Brown Norway vs.
Dahl S rat: role of nitric oxide synthase and Hsp90.";
J. Mol. Cell. Cardiol. 38:625-635(2005).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Chang Y.S., Chao C.C., Wang C.H., Lai Y.K.;
"Promoter analysis and gene regulation of rat 84 kDa heat shock
protein.";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-26.
PubMed=3189818; DOI=10.1016/0003-2697(88)90207-2;
Denis M.;
"Two-step purification and N-terminal amino acid sequence analysis of
the rat Mr 90,000 heat shock protein.";
Anal. Biochem. 173:405-411(1988).
[6]
PROTEIN SEQUENCE OF 2-16.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=11732320; DOI=10.1007/BF01288360;
Langer T., Fasold H.;
"Isolation and quantification of the heat shock protein 90 alpha and
beta isoforms from rat liver.";
Protoplasma 218:54-56(2001).
[7]
PROTEIN SEQUENCE OF 181-196 AND 320-330, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
Lubec G., Afjehi-Sadat L.;
Submitted (NOV-2006) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 205-218; 306-330 AND 413-427, SUBCELLULAR
LOCATION, AND INTERACTION WITH TP53.
TISSUE=Embryo;
PubMed=8663025; DOI=10.1074/jbc.271.25.15084;
Sepehrnia B., Paz I.B., Dasgupta G., Momand J.;
"Heat shock protein 84 forms a complex with mutant p53 protein
predominantly within a cytoplasmic compartment of the cell.";
J. Biol. Chem. 271:15084-15090(1996).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-255; SER-261
AND SER-445, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Molecular chaperone that promotes the maturation,
structural maintenance and proper regulation of specific target
proteins involved for instance in cell cycle control and signal
transduction. Undergoes a functional cycle that is linked to its
ATPase activity. This cycle probably induces conformational
changes in the client proteins, thereby causing their activation.
Interacts dynamically with various co-chaperones that modulate its
substrate recognition, ATPase cycle and chaperone function.
Engages with a range of client protein classes via its interaction
with various co-chaperone proteins or complexes, that act as
adapters, simultaneously able to interact with the specific client
and the central chaperone itself. Recruitment of ATP and co-
chaperone followed by client protein forms a functional chaperone.
After the completion of the chaperoning process, properly folded
client protein and co-chaperone leave HSP90 in an ADP-bound
partially open conformation and finally, ADP is released from
HSP90 which acquires an open conformation for the next cycle.
Apart from its chaperone activity, it also plays a role in the
regulation of the transcription machinery. HSP90 and its co-
chaperones modulate transcription at least at three different
levels. In the first place, they alter the steady-state levels of
certain transcription factors in response to various physiological
cues. Second, they modulate the activity of certain epigenetic
modifiers, such as histone deacetylases or DNA methyl
transferases, and thereby respond to the change in the
environment. Third, they participate in the eviction of histones
from the promoter region of certain genes and thereby turn on gene
expression. Antagonizes STUB1-mediated inhibition of TGF-beta
signaling via inhibition of STUB1-mediated SMAD3 ubiquitination
and degradation. Promotes cell differentiation by chaperoning
BIRC2 and thereby protecting from auto-ubiquitination and
degradation by the proteasomal machinery. Main chaperone that is
involved in the phosphorylation/activation of the STAT1 by
chaperoning both JAK2 and PRKCE under heat shock and in turn,
activates its own transcription. {ECO:0000250|UniProtKB:P08238}.
-!- ENZYME REGULATION: In the resting state, through the dimerization
of its C-terminal domain, HSP90 forms a homodimer which is defined
as the open conformation. Upon ATP-binding, the N-terminal domain
undergoes significant conformational changes and comes in contact
to form an active closed conformation. After HSP90 finishes its
chaperoning tasks of assisting the proper folding, stabilization
and activation of client proteins under the active state, ATP
molecule is hydrolyzed to ADP which then dissociates from HSP90
and directs the protein back to the resting state.
{ECO:0000250|UniProtKB:P08238}.
-!- SUBUNIT: Monomer. Homodimer (By similarity). Forms a complex with
CDK6 and CDC37. Interacts with UNC45A; binding to UNC45A involves
2 UNC45A monomers per HSP90AB1 dimer (By similarity). Interacts
with CHORDC1 (By similarity). Interacts with DNAJC7. Interacts
with FKBP4. May interact with NWD1. Interacts with SGTA. Interacts
with HSF1 in an ATP-dependent manner. Interacts with MET; the
interaction suppresses MET kinase activity. Interacts with ERBB2
in an ATP-dependent manner; the interaction suppresses ERBB2
kinase activity. Interacts with HIF1A, KEAP1 and RHOBTB2.
Interacts with STUB1 and SMAD3. Interacts with XPO1 and AHSA1.
Interacts with BIRC2. Interacts with KCNQ4; promotes cell surface
expression of KCNQ4. Interacts with BIRC2; prevents auto-
ubiquitination and degradation of its client protein BIRC2.
Interacts with NOS3. Interacts with AHR; interaction is inhibited
by HSP90AB1 phosphorylation on Ser-226 and Ser-255. Interacts with
STIP1 and CDC37; upon SMYD2-dependent methylation. Interacts with
JAK2 and PRKCE; promotes functional activation in a heat shock-
dependent manner. Interacts with HSP90AA1; interaction is
constitutive. HSP90AB1-CDC37 chaperone complex interacts with
inactive MAPK7 (via N-terminal half) in resting cells; the
interaction is MAP2K5-independent and prevents from ubiquitination
and proteasomal degradation. Interacts with CDC25A; prevents heat
shock-mediated CDC25A degradation and contributes to cell cycle
progression (By similarity). Interacts with TP53 (via DNA binding
domain); suppresses TP53 aggregation and prevents from
irreversible thermal inactivation (PubMed:8663025). Interacts with
TGFB1 processed form (LAP); inhibits latent TGFB1 activation (By
similarity). Interacts with TRIM8; prevents nucleus translocation
of phosphorylated STAT3 and HSP90AB1 (By similarity).
{ECO:0000250|UniProtKB:P08238, ECO:0000250|UniProtKB:P11499,
ECO:0000269|PubMed:8663025}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8663025}.
Melanosome {ECO:0000250|UniProtKB:P08238}. Nucleus
{ECO:0000250|UniProtKB:P08238}. Secreted
{ECO:0000250|UniProtKB:P08238}. Cell membrane
{ECO:0000250|UniProtKB:P08238}. Note=Translocates with BIRC2 from
the nucleus to the cytoplasm during differentiation. Secreted when
associated with TGFB1 processed form (LAP).
{ECO:0000250|UniProtKB:P08238}.
-!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
repeat-containing proteins. {ECO:0000250|UniProtKB:P07900}.
-!- PTM: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in
vitro). {ECO:0000250|UniProtKB:P08238}.
-!- PTM: ISGylated. {ECO:0000250|UniProtKB:P08238}.
-!- PTM: S-nitrosylated; negatively regulates the ATPase activity.
{ECO:0000250|UniProtKB:P08238}.
-!- PTM: Phosphorylation at Tyr-301 by SRC is induced by
lipopolysaccharide. Phosphorylation at Ser-226 and Ser-255
inhibits AHR interaction. {ECO:0000250|UniProtKB:P08238}.
-!- PTM: Methylated by SMYD2; facilitates dimerization and chaperone
complex formation; promotes cancer cell proliferation.
{ECO:0000250|UniProtKB:P08238}.
-!- PTM: Cleaved following oxidative stress resulting in HSP90AB1
protein radicals formation; disrupts the chaperoning function and
the degradation of its client proteins.
{ECO:0000250|UniProtKB:P08238}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
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EMBL; S45392; AAB23369.1; -; mRNA.
EMBL; AY695392; AAT99568.1; -; mRNA.
EMBL; AY695393; AAT99569.1; -; mRNA.
EMBL; DQ022068; ABE27999.1; -; Genomic_DNA.
EMBL; BC082009; AAH82009.1; -; mRNA.
PIR; S71306; S71306.
RefSeq; NP_001004082.3; NM_001004082.3.
UniGene; Rn.98667; -.
ProteinModelPortal; P34058; -.
SMR; P34058; -.
BioGrid; 256892; 6.
CORUM; P34058; -.
IntAct; P34058; 5.
MINT; MINT-4576429; -.
STRING; 10116.ENSRNOP00000026920; -.
iPTMnet; P34058; -.
PhosphoSitePlus; P34058; -.
World-2DPAGE; 0004:P34058; -.
PaxDb; P34058; -.
PRIDE; P34058; -.
Ensembl; ENSRNOT00000026920; ENSRNOP00000026920; ENSRNOG00000019834.
GeneID; 301252; -.
KEGG; rno:301252; -.
UCSC; RGD:1303075; rat.
CTD; 3326; -.
RGD; 1303075; Hsp90ab1.
eggNOG; KOG0019; Eukaryota.
eggNOG; KOG0020; Eukaryota.
eggNOG; COG0326; LUCA.
GeneTree; ENSGT00900000140936; -.
HOGENOM; HOG000031988; -.
HOVERGEN; HBG007374; -.
InParanoid; P34058; -.
KO; K04079; -.
OMA; LRYHSSQ; -.
OrthoDB; EOG091G0270; -.
PhylomeDB; P34058; -.
TreeFam; TF300686; -.
Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-RNO-3371511; HSF1 activation.
Reactome; R-RNO-3371568; Attenuation phase.
Reactome; R-RNO-3371571; HSF1-dependent transactivation.
Reactome; R-RNO-399954; Sema3A PAK dependent Axon repulsion.
Reactome; R-RNO-6798695; Neutrophil degranulation.
Reactome; R-RNO-844456; The NLRP3 inflammasome.
Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-RNO-8937144; Aryl hydrocarbon receptor signalling.
PRO; PR:P34058; -.
Proteomes; UP000002494; Chromosome 9.
Bgee; ENSRNOG00000019834; -.
ExpressionAtlas; P34058; baseline and differential.
Genevisible; P34058; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0034751; C:aryl hydrocarbon receptor complex; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0031526; C:brush border membrane; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
GO; GO:0016234; C:inclusion body; IDA:RGD.
GO; GO:0005765; C:lysosomal membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:1990917; C:ooplasm; IDA:RGD.
GO; GO:1990913; C:sperm head plasma membrane; IDA:RGD.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0043008; F:ATP-dependent protein binding; IEA:Ensembl.
GO; GO:0045296; F:cadherin binding; IEA:Ensembl.
GO; GO:0002135; F:CTP binding; IDA:RGD.
GO; GO:0032564; F:dATP binding; IDA:RGD.
GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
GO; GO:0070182; F:DNA polymerase binding; IEA:Ensembl.
GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
GO; GO:0008144; F:drug binding; IDA:RGD.
GO; GO:0005525; F:GTP binding; IDA:RGD.
GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:1990226; F:histone methyltransferase binding; IEA:Ensembl.
GO; GO:0044325; F:ion channel binding; IPI:RGD.
GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl.
GO; GO:0042277; F:peptide binding; IEA:Ensembl.
GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0019887; F:protein kinase regulator activity; IEA:Ensembl.
GO; GO:0017098; F:sulfonylurea receptor binding; IPI:RGD.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0002134; F:UTP binding; IDA:RGD.
GO; GO:0035690; P:cellular response to drug; IEP:RGD.
GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0061684; P:chaperone-mediated autophagy; NAS:ParkinsonsUK-UCL.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:Ensembl.
GO; GO:0061741; P:chaperone-mediated protein transport involved in chaperone-mediated autophagy; NAS:ParkinsonsUK-UCL.
GO; GO:0071157; P:negative regulation of cell cycle arrest; ISS:UniProtKB.
GO; GO:1903660; P:negative regulation of complement-dependent cytotoxicity; IMP:RGD.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:1901389; P:negative regulation of transforming growth factor beta activation; ISS:UniProtKB.
GO; GO:0001890; P:placenta development; IEA:Ensembl.
GO; GO:0045597; P:positive regulation of cell differentiation; IEA:Ensembl.
GO; GO:0045793; P:positive regulation of cell size; IMP:RGD.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
GO; GO:0032092; P:positive regulation of protein binding; IMP:RGD.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IMP:RGD.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; IEA:Ensembl.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:RGD.
GO; GO:0051973; P:positive regulation of telomerase activity; IEA:Ensembl.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
GO; GO:0006457; P:protein folding; TAS:RGD.
GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; IEA:Ensembl.
GO; GO:0061635; P:regulation of protein complex stability; NAS:ParkinsonsUK-UCL.
GO; GO:0031396; P:regulation of protein ubiquitination; IEA:Ensembl.
GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
GO; GO:0042220; P:response to cocaine; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0009651; P:response to salt stress; IEP:RGD.
GO; GO:0006986; P:response to unfolded protein; TAS:RGD.
GO; GO:0097435; P:supramolecular fiber organization; IEA:Ensembl.
GO; GO:1905323; P:telomerase holoenzyme complex assembly; IEA:Ensembl.
GO; GO:0007004; P:telomere maintenance via telomerase; IEA:Ensembl.
GO; GO:0019062; P:virion attachment to host cell; IEA:Ensembl.
CDD; cd00075; HATPase_c; 1.
Gene3D; 3.30.565.10; -; 1.
HAMAP; MF_00505; HSP90; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR019805; Heat_shock_protein_90_CS.
InterPro; IPR037196; HSP90_C.
InterPro; IPR001404; Hsp90_fam.
InterPro; IPR020575; Hsp90_N.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
PANTHER; PTHR11528; PTHR11528; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00183; HSP90; 1.
PIRSF; PIRSF002583; Hsp90; 1.
PRINTS; PR00775; HEATSHOCK90.
SMART; SM00387; HATPase_c; 1.
SUPFAM; SSF110942; SSF110942; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
PROSITE; PS00298; HSP90; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Cell membrane; Chaperone; Complete proteome;
Cytoplasm; Direct protein sequencing; Glycoprotein; Membrane;
Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Secreted; Stress response; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:11732320,
ECO:0000269|PubMed:3189818}.
CHAIN 2 724 Heat shock protein HSP 90-beta.
/FTId=PRO_0000062920.
REGION 2 527 Interaction with TP53.
{ECO:0000250|UniProtKB:P08238}.
REGION 2 214 Interaction with BIRC2.
{ECO:0000250|UniProtKB:P08238}.
REGION 215 552 Interaction with AHSA1.
{ECO:0000250|UniProtKB:P08238}.
MOTIF 720 724 TPR repeat-binding.
BINDING 46 46 ATP. {ECO:0000250}.
BINDING 88 88 ATP. {ECO:0000250}.
BINDING 107 107 ATP. {ECO:0000250}.
BINDING 133 133 ATP; via amide nitrogen. {ECO:0000250}.
BINDING 392 392 ATP. {ECO:0000250}.
SITE 126 127 Cleaved under oxidative stress.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 219 219 N6-succinyllysine.
{ECO:0000250|UniProtKB:P11499}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 297 297 Phosphothreonine.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 301 301 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 305 305 Phosphotyrosine.
{ECO:0000250|UniProtKB:P11499}.
MOD_RES 307 307 Phosphoserine.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 399 399 N6-malonyllysine. {ECO:0000250}.
MOD_RES 435 435 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 445 445 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 452 452 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 479 479 Phosphothreonine.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 481 481 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 484 484 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 531 531 N6-methylated lysine; alternate.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 531 531 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P11499}.
MOD_RES 532 532 Phosphoserine.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 574 574 N6-methylated lysine.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 577 577 N6-succinyllysine.
{ECO:0000250|UniProtKB:P11499}.
MOD_RES 624 624 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11499}.
MOD_RES 669 669 Phosphoserine.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 718 718 Phosphoserine; by PLK2 and PLK3.
{ECO:0000250|UniProtKB:P08238}.
CARBOHYD 434 434 O-linked (GlcNAc) serine. {ECO:0000250}.
CARBOHYD 452 452 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CONFLICT 6 7 HH -> QK (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 11 11 E -> P (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 17 17 F -> T (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 20 20 E -> F (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 26 26 S -> F (in Ref. 4; AAH82009).
{ECO:0000305}.
CONFLICT 82 82 R -> A (in Ref. 1; AAB23369).
{ECO:0000305}.
CONFLICT 368 368 E -> D (in Ref. 1; AAB23369).
{ECO:0000305}.
CONFLICT 375 375 N -> D (in Ref. 3; ABE27999).
{ECO:0000305}.
CONFLICT 559 559 K -> R (in Ref. 1; AAB23369).
{ECO:0000305}.
CONFLICT 664 674 LSSGFSLEDPQ -> SSLASHFRRPK (in Ref. 1;
AAB23369). {ECO:0000305}.
SEQUENCE 724 AA; 83281 MW; CE323E81CE173ECB CRC64;
MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT
DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN NLGTIAKSGT KAFMEALQAG
ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVRAD HGEPIGRGTK
VILHLKEDQT EYLEERRVKE VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE
DKEDEEKPKI EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE
YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK NNIKLYVRRV
FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNIVK KCLELFSELA
EDKENYKKFY EAFSKNLKLG IHEDSTNRRR LSELLRYHTS QSGDEMTSLS EYVSRMKETQ
KSIYYITGES KEQVANSAFV ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG
LELPEDEEEK KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA
NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA VKDLVVLLFE
TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVTAEEP SAAVPDEIPP LEGDEDASRM
EEVD


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Catalog number Product name Quantity
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
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
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
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
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
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
27-259 HSF2 binds specifically to the heat-shock element and has homology to HSFs of other species. Heat shock transcription factors activate heat-shock response genes under conditions of heat or other stres 0.05 mg
E0693m ELISA Growth-related 25 kDa protein,Heat shock 25 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,HSP 25,HSP 27,Hsp25,Hsp27,HspB1,Hspb1,Mouse,Mus musculus,p25 96T
U0693m CLIA Growth-related 25 kDa protein,Heat shock 25 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,HSP 25,HSP 27,Hsp25,Hsp27,HspB1,Hspb1,Mouse,Mus musculus,p25 96T
E0693m ELISA kit Growth-related 25 kDa protein,Heat shock 25 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,HSP 25,HSP 27,Hsp25,Hsp27,HspB1,Hspb1,Mouse,Mus musculus,p25 96T
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
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
E0693c ELISA kit 25 kDa IAP,Actin polymerization inhibitor,Chicken,Gallus gallus,Heat shock 25 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,HSP 25,HSP 27,HspB1,HSPB1 96T
U0693c CLIA 25 kDa IAP,Actin polymerization inhibitor,Chicken,Gallus gallus,Heat shock 25 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,HSP 25,HSP 27,HspB1,HSPB1 96T
E0693c ELISA 25 kDa IAP,Actin polymerization inhibitor,Chicken,Gallus gallus,Heat shock 25 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,HSP 25,HSP 27,HspB1,HSPB1 96T
25-272 The heat-shock response is elicited by exposure of cells to thermal and chemical stress and through the activation of HSFs (heat shock factors) results in the elevated expression of heat-shock induced 0.05 mg
hsp-091 Recombinant Human Heat Shock Protein 90kDa Beta (GRP94) Member 1 HEAT SHOCK PROTEINS 10
hsp-091 Recombinant Human Heat Shock Protein 90kDa Beta (GRP94) Member 1 HEAT SHOCK PROTEINS 2
hsp-091 Recombinant Human Heat Shock Protein 90kDa Beta (GRP94) Member 1 HEAT SHOCK PROTEINS 1mg
20-372-60095 heat shock 70kDa protein 1-like - Mouse monoclonal anti-human HSPA1L antibody; Heat shock 70 kDa protein 1-like; Heat shock 70 kDa protein 1-Hom; HSP70-Hom Monoclonal 0.1 mg
PC-084 Heat Shock Protein 90b (HSP90b or HSP84) 500 ug
PC-084 Heat Shock Protein 90b (HSP90b or HSP84) 500 ug
EIAAB11548 DnaJ homolog subfamily B member 5,DNAJB5,Heat shock protein cognate 40,Heat shock protein Hsp40-2,Heat shock protein Hsp40-3,Homo sapiens,Hsc40,HSC40,Human


 

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