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Heat shock protein HSP 90-beta (Heat shock 84 kDa) (HSP 84) (HSP84) (Tumor-specific transplantation 84 kDa antigen) (TSTA)

 HS90B_MOUSE             Reviewed;         724 AA.
P11499; O89078; Q3UIQ7;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
30-AUG-2017, entry version 192.
RecName: Full=Heat shock protein HSP 90-beta;
AltName: Full=Heat shock 84 kDa;
Short=HSP 84;
Short=HSP84;
AltName: Full=Tumor-specific transplantation 84 kDa antigen;
Short=TSTA;
Name=Hsp90ab1; Synonyms=Hsp84, Hsp84-1, Hspcb;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2469626; DOI=10.1016/0378-1119(88)90182-5;
Hoffmann T., Hovemann B.;
"Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related
genes encode formerly identified tumour-specific transplantation
antigens.";
Gene 74:491-501(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-31; 94-156;
158-161; 467-513; 554-566; 622-640; 684-688 AND 690-720.
PubMed=2445630; DOI=10.1016/0378-1119(87)90155-7;
Moore S.K., Kozak C., Robinson E.A., Ullrich S.J., Appella E.;
"Cloning and nucleotide sequence of the murine hsp84 cDNA and
chromosome assignment of related sequences.";
Gene 56:29-40(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2925609;
Moore S.K., Kozak C., Robinson E.A., Ullrich S.J., Appella E.;
"Murine 86- and 84-kDa heat shock proteins, cDNA sequences, chromosome
assignments, and evolutionary origins.";
J. Biol. Chem. 264:5343-5351(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1976316; DOI=10.1089/dna.1990.9.387;
Moore S.K., Rijli F., Appella E.;
"Characterization of the mouse 84-kD heat shock protein gene family.";
DNA Cell Biol. 9:387-400(1990).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[7]
PROTEIN SEQUENCE OF 2-31 AND 114-125.
PubMed=3458168; DOI=10.1073/pnas.83.10.3121;
Ullrich S.J., Robinson E.A., Law L.W., Willingham M., Appella E.;
"A mouse tumor-specific transplantation antigen is a heat shock-
related protein.";
Proc. Natl. Acad. Sci. U.S.A. 83:3121-3125(1986).
[8]
PROTEIN SEQUENCE OF 2-6, AND HOMODIMERIZATION.
PubMed=8289821; DOI=10.1128/MCB.14.2.1459;
Minami Y., Kimura Y., Kawasaki H., Suzuki K., Yahara I.;
"The carboxy-terminal region of mammalian HSP90 is required for its
dimerization and function in vivo.";
Mol. Cell. Biol. 14:1459-1464(1994).
[9]
PROTEIN SEQUENCE OF 42-53; 56-64; 73-95; 149-168; 181-196; 205-219;
250-266; 276-330; 339-347; 360-392; 429-435; 439-448; 457-475;
482-491; 539-552; 558-565; 575-583 AND 624-639.
STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B.,
Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 272-400.
STRAIN=BALB/cJ; TISSUE=Spleen;
PubMed=9798653; DOI=10.1016/S0161-5890(98)00031-5;
Chu C.C., Paul W.E.;
"Expressed genes in interleukin-4 treated B cells identified by cDNA
representational difference analysis.";
Mol. Immunol. 35:487-502(1998).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 531-724.
TISSUE=Heart;
PubMed=1406681; DOI=10.1128/MCB.12.11.5059;
Shaknovich R., Shue G., Kohtz D.S.;
"Conformational activation of a basic helix-loop-helix protein (MyoD1)
by the C-terminal region of murine HSP90 (HSP84).";
Mol. Cell. Biol. 12:5059-5068(1992).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[13]
INTERACTION WITH CHORDC1.
PubMed=15642353; DOI=10.1016/j.febslet.2004.12.005;
Wu J., Luo S., Jiang H., Li H.;
"Mammalian CHORD-containing protein 1 is a novel heat shock protein
90-interacting protein.";
FEBS Lett. 579:421-426(2005).
[14]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-484, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-261, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Teratocarcinoma;
PubMed=17622165; DOI=10.1021/pr070122r;
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
"A differential phosphoproteomic analysis of retinoic acid-treated P19
cells.";
J. Proteome Res. 6:3174-3186(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
"Mitochondrial phosphoproteome revealed by an improved IMAC method and
MS/MS/MS.";
Mol. Cell. Proteomics 6:669-676(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-305, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[24]
INTERACTION WITH TRIM8.
PubMed=21689689; DOI=10.1016/j.bbamcr.2011.05.013;
Okumura F., Okumura A.J., Matsumoto M., Nakayama K.I., Hatakeyama S.;
"TRIM8 regulates Nanog via Hsp90beta-mediated nuclear translocation of
STAT3 in embryonic stem cells.";
Biochim. Biophys. Acta 1813:1784-1792(2011).
[25]
GLYCOSYLATION AT SER-434 AND SER-452.
TISSUE=Liver;
PubMed=22556278; DOI=10.1074/mcp.M111.015966;
Overath T., Kuckelkorn U., Henklein P., Strehl B., Bonar D., Kloss A.,
Siele D., Kloetzel P.M., Janek K.;
"Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a
novel biotin-cystamine tag.";
Mol. Cell. Proteomics 11:467-477(2012).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-624, SUCCINYLATION [LARGE
SCALE ANALYSIS] AT LYS-219; LYS-531 AND LYS-577, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- 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 (By similarity). Homodimer (PubMed:8289821).
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 (PubMed:15642353).
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. Interacts with TP53 (via
DNA binding domain); suppresses TP53 aggregation and prevents from
irreversible thermal inactivation. Interacts with TGFB1 processed
form (LAP); inhibits latent TGFB1 activation (By similarity).
Interacts with TRIM8; prevents nucleus translocation of
phosphorylated STAT3 and HSP90AB1 (PubMed:21689689).
{ECO:0000250|UniProtKB:P08238, ECO:0000269|PubMed:15642353,
ECO:0000269|PubMed:21689689, ECO:0000269|PubMed:8289821}.
-!- INTERACTION:
P19426:Nelfe; NbExp=2; IntAct=EBI-492813, EBI-6142845;
P06537:Nr3c1; NbExp=2; IntAct=EBI-492813, EBI-492753;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08238}.
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: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- PTM: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in
vitro). {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; M36829; AAA37866.1; -; mRNA.
EMBL; M18186; AAA37865.1; -; mRNA.
EMBL; AK146809; BAE27449.1; -; mRNA.
EMBL; AC163677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U89426; AAC36532.1; -; mRNA.
EMBL; S46109; AAB23704.1; -; mRNA.
CCDS; CCDS28812.1; -.
PIR; A35569; HHMS84.
PIR; I57523; I57523.
RefSeq; NP_032328.2; NM_008302.3.
UniGene; Mm.2180; -.
ProteinModelPortal; P11499; -.
SMR; P11499; -.
BioGrid; 200454; 41.
DIP; DIP-461N; -.
IntAct; P11499; 30.
MINT; MINT-152750; -.
STRING; 10090.ENSMUSP00000024739; -.
iPTMnet; P11499; -.
PhosphoSitePlus; P11499; -.
SwissPalm; P11499; -.
SWISS-2DPAGE; P11499; -.
EPD; P11499; -.
PaxDb; P11499; -.
PeptideAtlas; P11499; -.
PRIDE; P11499; -.
Ensembl; ENSMUST00000024739; ENSMUSP00000024739; ENSMUSG00000023944.
GeneID; 15516; -.
KEGG; mmu:15516; -.
UCSC; uc008cqz.1; mouse.
CTD; 3326; -.
MGI; MGI:96247; Hsp90ab1.
eggNOG; KOG0019; Eukaryota.
eggNOG; KOG0020; Eukaryota.
eggNOG; COG0326; LUCA.
GeneTree; ENSGT00840000129758; -.
HOGENOM; HOG000031988; -.
HOVERGEN; HBG007374; -.
InParanoid; P11499; -.
KO; K04079; -.
OMA; LRYHSSQ; -.
OrthoDB; EOG091G0270; -.
TreeFam; TF300686; -.
Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-MMU-3371511; HSF1 activation.
Reactome; R-MMU-3371568; Attenuation phase.
Reactome; R-MMU-3371571; HSF1-dependent transactivation.
Reactome; R-MMU-399954; Sema3A PAK dependent Axon repulsion.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-844456; The NLRP3 inflammasome.
Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-MMU-8937144; Aryl hydrocarbon receptor signalling.
ChiTaRS; Hsp90ab1; mouse.
PRO; PR:P11499; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000023944; -.
ExpressionAtlas; P11499; baseline and differential.
Genevisible; P11499; MM.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0034751; C:aryl hydrocarbon receptor complex; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
GO; GO:0016234; C:inclusion body; IEA:Ensembl.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:1990917; C:ooplasm; IEA:Ensembl.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:1990913; C:sperm head plasma membrane; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0043008; F:ATP-dependent protein binding; ISO:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0002135; F:CTP binding; IEA:Ensembl.
GO; GO:0032564; F:dATP binding; IEA:Ensembl.
GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
GO; GO:0008144; F:drug binding; IEA:Ensembl.
GO; GO:0001948; F:glycoprotein binding; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; IEA:Ensembl.
GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:1990226; F:histone methyltransferase binding; ISO:MGI.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0019900; F:kinase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0023026; F:MHC class II protein complex binding; ISO:MGI.
GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISS:UniProtKB.
GO; GO:0042277; F:peptide binding; ISO:MGI.
GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0017098; F:sulfonylurea receptor binding; IEA:Ensembl.
GO; GO:0030911; F:TPR domain binding; ISS:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0002134; F:UTP binding; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0071157; P:negative regulation of cell cycle arrest; ISS:UniProtKB.
GO; GO:1903660; P:negative regulation of complement-dependent cytotoxicity; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
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; IMP:MGI.
GO; GO:0045597; P:positive regulation of cell differentiation; ISO:MGI.
GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:MGI.
GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IEA:Ensembl.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:MGI.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; IEA:Ensembl.
GO; GO:0031396; P:regulation of protein ubiquitination; ISO:MGI.
GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0010033; P:response to organic substance; IDA:MGI.
GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
GO; GO:0097435; P:supramolecular fiber organization; ISO:MGI.
GO; GO:1905323; P:telomerase holoenzyme complex assembly; ISO:MGI.
GO; GO:0007004; P:telomere maintenance via telomerase; ISO:MGI.
GO; GO:0019062; P:virion attachment to host cell; ISO:MGI.
Gene3D; 3.30.565.10; -; 1.
HAMAP; MF_00505; HSP90; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR019805; Heat_shock_protein_90_CS.
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; 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:2445630,
ECO:0000269|PubMed:3458168,
ECO:0000269|PubMed:8289821}.
CHAIN 2 724 Heat shock protein HSP 90-beta.
/FTId=PRO_0000062918.
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:0000244|PubMed:23806337}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:17208939,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:17622165,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000244|PubMed:17622165}.
MOD_RES 297 297 Phosphothreonine.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 301 301 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 305 305 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
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:0000250|UniProtKB:P08238}.
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:0000244|PubMed:17947660}.
MOD_RES 531 531 N6-methylated lysine; alternate.
{ECO:0000250|UniProtKB:P08238}.
MOD_RES 531 531 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
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:0000244|PubMed:23806337}.
MOD_RES 624 624 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
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:0000269|PubMed:22556278}.
CARBOHYD 452 452 O-linked (GlcNAc) serine; alternate.
{ECO:0000269|PubMed:22556278}.
CONFLICT 76 76 I -> L (in Ref. 2; AAA37865).
{ECO:0000305}.
CONFLICT 279 279 Q -> R (in Ref. 10; AAC36532).
{ECO:0000305}.
CONFLICT 306 306 K -> R (in Ref. 10; AAC36532).
{ECO:0000305}.
CONFLICT 318 318 V -> I (in Ref. 5; BAE27449).
{ECO:0000305}.
CONFLICT 332 332 L -> F (in Ref. 2; AAA37865).
{ECO:0000305}.
CONFLICT 356 356 Y -> H (in Ref. 10; AAC36532).
{ECO:0000305}.
CONFLICT 495 495 A -> P (in Ref. 2; AAA37865).
{ECO:0000305}.
CONFLICT 497 497 S -> P (in Ref. 1; AAA37866).
{ECO:0000305}.
CONFLICT 531 535 KSLVS -> GGPGT (in Ref. 11; AAB23704).
{ECO:0000305}.
CONFLICT 538 538 K -> N (in Ref. 11; AAB23704).
{ECO:0000305}.
CONFLICT 575 575 V -> F (in Ref. 11; AAB23704).
{ECO:0000305}.
CONFLICT 667 667 G -> V (in Ref. 2; AAA37865).
{ECO:0000305}.
CONFLICT 699 699 E -> G (in Ref. 5; BAE27449).
{ECO:0000305}.
CONFLICT 719 719 R -> P (in Ref. 1; AAA37866).
{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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