HS90B_MOUSE
ID HS90B_MOUSE Reviewed; 724 AA.
AC P11499; O89078; Q3UIQ7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 227.
DE RecName: Full=Heat shock protein HSP 90-beta;
DE AltName: Full=Heat shock 84 kDa;
DE Short=HSP 84;
DE Short=HSP84;
DE AltName: Full=Tumor-specific transplantation 84 kDa antigen;
DE Short=TSTA;
GN Name=Hsp90ab1 {ECO:0000312|MGI:MGI:96247}; Synonyms=Hsp84, Hsp84-1, Hspcb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2469626; DOI=10.1016/0378-1119(88)90182-5;
RA Hoffmann T., Hovemann B.;
RT "Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes
RT encode formerly identified tumour-specific transplantation antigens.";
RL Gene 74:491-501(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-31; 94-156; 158-161;
RP 467-513; 554-566; 622-640; 684-688 AND 690-720.
RX PubMed=2445630; DOI=10.1016/0378-1119(87)90155-7;
RA Moore S.K., Kozak C., Robinson E.A., Ullrich S.J., Appella E.;
RT "Cloning and nucleotide sequence of the murine hsp84 cDNA and chromosome
RT assignment of related sequences.";
RL Gene 56:29-40(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2925609; DOI=10.1016/s0021-9258(18)83551-7;
RA Moore S.K., Kozak C., Robinson E.A., Ullrich S.J., Appella E.;
RT "Murine 86- and 84-kDa heat shock proteins, cDNA sequences, chromosome
RT assignments, and evolutionary origins.";
RL J. Biol. Chem. 264:5343-5351(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1976316; DOI=10.1089/dna.1990.9.387;
RA Moore S.K., Rijli F., Appella E.;
RT "Characterization of the mouse 84-kD heat shock protein gene family.";
RL DNA Cell Biol. 9:387-400(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP PROTEIN SEQUENCE OF 2-31 AND 114-125.
RX PubMed=3458168; DOI=10.1073/pnas.83.10.3121;
RA Ullrich S.J., Robinson E.A., Law L.W., Willingham M., Appella E.;
RT "A mouse tumor-specific transplantation antigen is a heat shock-related
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3121-3125(1986).
RN [8]
RP PROTEIN SEQUENCE OF 2-6, AND HOMODIMERIZATION.
RX PubMed=8289821; DOI=10.1128/mcb.14.2.1459-1464.1994;
RA Minami Y., Kimura Y., Kawasaki H., Suzuki K., Yahara I.;
RT "The carboxy-terminal region of mammalian HSP90 is required for its
RT dimerization and function in vivo.";
RL Mol. Cell. Biol. 14:1459-1464(1994).
RN [9]
RP PROTEIN SEQUENCE OF 42-53; 56-64; 73-95; 149-168; 181-196; 205-219;
RP 250-266; 276-330; 339-347; 360-392; 429-435; 439-448; 457-475; 482-491;
RP 539-552; 558-565; 575-583 AND 624-639.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 272-400.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=9798653; DOI=10.1016/s0161-5890(98)00031-5;
RA Chu C.C., Paul W.E.;
RT "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT representational difference analysis.";
RL Mol. Immunol. 35:487-502(1998).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 531-724.
RC TISSUE=Heart;
RX PubMed=1406681; DOI=10.1128/mcb.12.11.5059-5068.1992;
RA Shaknovich R., Shue G., Kohtz D.S.;
RT "Conformational activation of a basic helix-loop-helix protein (MyoD1) by
RT the C-terminal region of murine HSP90 (HSP84).";
RL Mol. Cell. Biol. 12:5059-5068(1992).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [13]
RP INTERACTION WITH CHORDC1.
RX PubMed=15642353; DOI=10.1016/j.febslet.2004.12.005;
RA Wu J., Luo S., Jiang H., Li H.;
RT "Mammalian CHORD-containing protein 1 is a novel heat shock protein 90-
RT interacting protein.";
RL FEBS Lett. 579:421-426(2005).
RN [14]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-484, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-261, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Teratocarcinoma;
RX PubMed=17622165; DOI=10.1021/pr070122r;
RA Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT cells.";
RL J. Proteome Res. 6:3174-3186(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-305, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [24]
RP INTERACTION WITH TRIM8.
RX PubMed=21689689; DOI=10.1016/j.bbamcr.2011.05.013;
RA Okumura F., Okumura A.J., Matsumoto M., Nakayama K.I., Hatakeyama S.;
RT "TRIM8 regulates Nanog via Hsp90beta-mediated nuclear translocation of
RT STAT3 in embryonic stem cells.";
RL Biochim. Biophys. Acta 1813:1784-1792(2011).
RN [25]
RP GLYCOSYLATION AT SER-434 AND SER-452.
RC TISSUE=Liver;
RX PubMed=22556278; DOI=10.1074/mcp.m111.015966;
RA Overath T., Kuckelkorn U., Henklein P., Strehl B., Bonar D., Kloss A.,
RA Siele D., Kloetzel P.M., Janek K.;
RT "Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a novel
RT biotin-cystamine tag.";
RL Mol. Cell. Proteomics 11:467-477(2012).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-624, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-219; LYS-531 AND LYS-577, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [27]
RP INTERACTION WITH NR3C1 AND NR1D1, AND SUBCELLULAR LOCATION.
RX PubMed=27686098; DOI=10.1242/jcs.190959;
RA Okabe T., Chavan R., Fonseca Costa S.S., Brenna A., Ripperger J.A.,
RA Albrecht U.;
RT "REV-ERBalpha influences the stability and nuclear localization of the
RT glucocorticoid receptor.";
RL J. Cell Sci. 129:4143-4154(2016).
RN [28]
RP INTERACTION WITH PDCL3, AND SUBCELLULAR LOCATION.
RX PubMed=27496612; DOI=10.1002/jcb.25669;
RA Krzemien-Ojak L., Goral A., Joachimiak E., Filipek A., Fabczak H.;
RT "Interaction of a Novel Chaperone PhLP2A With the Heat Shock Protein
RT Hsp90.";
RL J. Cell. Biochem. 118:420-429(2017).
CC -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC maintenance and proper regulation of specific target proteins involved
CC for instance in cell cycle control and signal transduction. Undergoes a
CC functional cycle linked to its ATPase activity. This cycle probably
CC induces conformational changes in the client proteins, thereby causing
CC their activation. Interacts dynamically with various co-chaperones that
CC modulate its substrate recognition, ATPase cycle and chaperone
CC function. Engages with a range of client protein classes via its
CC interaction with various co-chaperone proteins or complexes, that act
CC as adapters, simultaneously able to interact with the specific client
CC and the central chaperone itself. Recruitment of ATP and co-chaperone
CC followed by client protein forms a functional chaperone. After the
CC completion of the chaperoning process, properly folded client protein
CC and co-chaperone leave HSP90 in an ADP-bound partially open
CC conformation and finally, ADP is released from HSP90 which acquires an
CC open conformation for the next cycle. Apart from its chaperone
CC activity, it also plays a role in the regulation of the transcription
CC machinery. HSP90 and its co-chaperones modulate transcription at least
CC at three different levels. They first alter the steady-state levels of
CC certain transcription factors in response to various physiological
CC cues. Second, they modulate the activity of certain epigenetic
CC modifiers, such as histone deacetylases or DNA methyl transferases, and
CC thereby respond to the change in the environment. Third, they
CC participate in the eviction of histones from the promoter region of
CC certain genes and thereby turn on gene expression. Antagonizes STUB1-
CC mediated inhibition of TGF-beta signaling via inhibition of STUB1-
CC mediated SMAD3 ubiquitination and degradation. Promotes cell
CC differentiation by chaperoning BIRC2 and thereby protecting from auto-
CC ubiquitination and degradation by the proteasomal machinery. Main
CC chaperone involved in the phosphorylation/activation of the STAT1 by
CC chaperoning both JAK2 and PRKCE under heat shock and in turn, activates
CC its own transcription. Involved in the translocation into ERGIC
CC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless
CC cargos (lacking the secretion signal sequence) such as the interleukin
CC 1/IL-1; the translocation process is mediated by the cargo receptor
CC TMED10. {ECO:0000250|UniProtKB:P08238}.
CC -!- ACTIVITY REGULATION: In the resting state, through the dimerization of
CC its C-terminal domain, HSP90 forms a homodimer which is defined as the
CC open conformation. Upon ATP-binding, the N-terminal domain undergoes
CC significant conformational changes and comes in contact to form an
CC active closed conformation. After HSP90 finishes its chaperoning tasks
CC of assisting the proper folding, stabilization and activation of client
CC proteins under the active state, ATP molecule is hydrolyzed to ADP
CC which then dissociates from HSP90 and directs the protein back to the
CC resting state. {ECO:0000250|UniProtKB:P08238}.
CC -!- SUBUNIT: Monomer (By similarity). Homodimer (PubMed:8289821). Forms a
CC complex with CDK6 and CDC37. Interacts with UNC45A; binding to UNC45A
CC involves 2 UNC45A monomers per HSP90AB1 dimer (By similarity).
CC Interacts with CHORDC1 (PubMed:15642353). Interacts with DNAJC7.
CC Interacts with FKBP4. May interact with NWD1. Interacts with SGTA.
CC Interacts with HSF1 in an ATP-dependent manner. Interacts with MET; the
CC interaction suppresses MET kinase activity. Interacts with ERBB2 in an
CC ATP-dependent manner; the interaction suppresses ERBB2 kinase activity.
CC Interacts with HIF1A, KEAP1 and RHOBTB2. Interacts with STUB1 and
CC SMAD3. Interacts with XPO1 and AHSA1. Interacts with BIRC2. Interacts
CC with KCNQ4; promotes cell surface expression of KCNQ4. Interacts with
CC BIRC2; prevents auto-ubiquitination and degradation of its client
CC protein BIRC2. Interacts with NOS3. Interacts with AHR; interaction is
CC inhibited by HSP90AB1 phosphorylation on Ser-226 and Ser-255. Interacts
CC with STIP1 and CDC37; upon SMYD2-dependent methylation. Interacts with
CC JAK2 and PRKCE; promotes functional activation in a heat shock-
CC dependent manner. Interacts with HSP90AA1; interaction is constitutive.
CC HSP90AB1-CDC37 chaperone complex interacts with inactive MAPK7 (via N-
CC terminal half) in resting cells; the interaction is MAP2K5-independent
CC and prevents from ubiquitination and proteasomal degradation. Interacts
CC with CDC25A; prevents heat shock-mediated CDC25A degradation and
CC contributes to cell cycle progression. Interacts with TP53 (via DNA
CC binding domain); suppresses TP53 aggregation and prevents from
CC irreversible thermal inactivation. Interacts with TGFB1 processed form
CC (LAP); inhibits latent TGFB1 activation (By similarity). Interacts with
CC TRIM8; prevents nucleus translocation of phosphorylated STAT3 and
CC HSP90AB1 (PubMed:21689689). Interacts with NR3C1 (via domain NR LBD)
CC and NR1D1 (via domain NR LBD) (PubMed:27686098). Interacts with PDCL3
CC (PubMed:27496612). Interacts with TTC4 (via TPR repeats) (By
CC similarity). Interacts with IL1B; the interaction facilitates cargo
CC translocation into the ERGIC (By similarity).
CC {ECO:0000250|UniProtKB:P08238, ECO:0000269|PubMed:15642353,
CC ECO:0000269|PubMed:21689689, ECO:0000269|PubMed:27496612,
CC ECO:0000269|PubMed:27686098, ECO:0000269|PubMed:8289821}.
CC -!- INTERACTION:
CC P11499; P19426: Nelfe; NbExp=2; IntAct=EBI-492813, EBI-6142845;
CC P11499; P06537: Nr3c1; NbExp=2; IntAct=EBI-492813, EBI-492753;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27496612,
CC ECO:0000269|PubMed:27686098}. Melanosome
CC {ECO:0000250|UniProtKB:P08238}. Nucleus {ECO:0000250|UniProtKB:P08238}.
CC Secreted {ECO:0000250|UniProtKB:P08238}. Cell membrane
CC {ECO:0000250|UniProtKB:P08238}. Dynein axonemal particle
CC {ECO:0000250|UniProtKB:Q6AZV1}. Note=Translocates with BIRC2 from the
CC nucleus to the cytoplasm during differentiation. Secreted when
CC associated with TGFB1 processed form (LAP).
CC {ECO:0000250|UniProtKB:P08238}.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins. {ECO:0000250|UniProtKB:P07900}.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC -!- PTM: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro).
CC {ECO:0000250|UniProtKB:P08238}.
CC -!- PTM: S-nitrosylated; negatively regulates the ATPase activity.
CC {ECO:0000250|UniProtKB:P08238}.
CC -!- PTM: Phosphorylation at Tyr-301 by SRC is induced by
CC lipopolysaccharide. Phosphorylation at Ser-226 and Ser-255 inhibits AHR
CC interaction. {ECO:0000250|UniProtKB:P08238}.
CC -!- PTM: Methylated by SMYD2; facilitates dimerization and chaperone
CC complex formation; promotes cancer cell proliferation.
CC {ECO:0000250|UniProtKB:P08238}.
CC -!- PTM: Cleaved following oxidative stress resulting in HSP90AB1 protein
CC radicals formation; disrupts the chaperoning function and the
CC degradation of its client proteins. {ECO:0000250|UniProtKB:P08238}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; M36829; AAA37866.1; -; mRNA.
DR EMBL; M18186; AAA37865.1; -; mRNA.
DR EMBL; AK146809; BAE27449.1; -; mRNA.
DR EMBL; AC163677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U89426; AAC36532.1; -; mRNA.
DR EMBL; S46109; AAB23704.1; -; mRNA.
DR CCDS; CCDS28812.1; -.
DR PIR; A35569; HHMS84.
DR PIR; I57523; I57523.
DR RefSeq; NP_032328.2; NM_008302.3.
DR AlphaFoldDB; P11499; -.
DR SMR; P11499; -.
DR BioGRID; 200454; 117.
DR ComplexPortal; CPX-3287; HSP90B-CDC37 chaperone complex.
DR CORUM; P11499; -.
DR DIP; DIP-461N; -.
DR IntAct; P11499; 32.
DR MINT; P11499; -.
DR STRING; 10090.ENSMUSP00000024739; -.
DR CarbonylDB; P11499; -.
DR GlyGen; P11499; 2 sites.
DR iPTMnet; P11499; -.
DR MetOSite; P11499; -.
DR PhosphoSitePlus; P11499; -.
DR SwissPalm; P11499; -.
DR SWISS-2DPAGE; P11499; -.
DR CPTAC; non-CPTAC-3376; -.
DR CPTAC; non-CPTAC-3377; -.
DR EPD; P11499; -.
DR jPOST; P11499; -.
DR PaxDb; P11499; -.
DR PeptideAtlas; P11499; -.
DR PRIDE; P11499; -.
DR ProteomicsDB; 267066; -.
DR ABCD; P11499; 1 sequenced antibody.
DR Antibodypedia; 3929; 1743 antibodies from 48 providers.
DR DNASU; 15516; -.
DR Ensembl; ENSMUST00000024739; ENSMUSP00000024739; ENSMUSG00000023944.
DR GeneID; 15516; -.
DR KEGG; mmu:15516; -.
DR UCSC; uc008cqz.1; mouse.
DR CTD; 3326; -.
DR MGI; MGI:96247; Hsp90ab1.
DR VEuPathDB; HostDB:ENSMUSG00000023944; -.
DR eggNOG; KOG0019; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P11499; -.
DR OMA; TRMKAEQ; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; P11499; -.
DR TreeFam; TF300686; -.
DR Reactome; R-MMU-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-3371511; HSF1 activation.
DR Reactome; R-MMU-3371568; Attenuation phase.
DR Reactome; R-MMU-3371571; HSF1-dependent transactivation.
DR Reactome; R-MMU-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-844456; The NLRP3 inflammasome.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8937144; Aryl hydrocarbon receptor signalling.
DR Reactome; R-MMU-8939211; ESR-mediated signaling.
DR Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 15516; 19 hits in 71 CRISPR screens.
DR ChiTaRS; Hsp90ab1; mouse.
DR PRO; PR:P11499; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P11499; protein.
DR Bgee; ENSMUSG00000023944; Expressed in metanephric ureteric bud and 263 other tissues.
DR ExpressionAtlas; P11499; baseline and differential.
DR Genevisible; P11499; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; ISS:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; IDA:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0044294; C:dendritic growth cone; IDA:ARUK-UCL.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:1990565; C:HSP90-CDC37 chaperone complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016234; C:inclusion body; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990917; C:ooplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:1990913; C:sperm head plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0043008; F:ATP-dependent protein binding; ISO:MGI.
DR GO; GO:0002135; F:CTP binding; ISO:MGI.
DR GO; GO:0032564; F:dATP binding; ISO:MGI.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
DR GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:1990226; F:histone methyltransferase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISS:UniProtKB.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0044183; F:protein folding chaperone; IMP:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
DR GO; GO:0017098; F:sulfonylurea receptor binding; ISO:MGI.
DR GO; GO:0048156; F:tau protein binding; IPI:ARUK-UCL.
DR GO; GO:0030911; F:TPR domain binding; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0002134; F:UTP binding; ISO:MGI.
DR GO; GO:0048675; P:axon extension; IMP:ARUK-UCL.
DR GO; GO:0034605; P:cellular response to heat; IMP:UniProtKB.
DR GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:ARUK-UCL.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISO:MGI.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:ARUK-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:1903660; P:negative regulation of complement-dependent cytotoxicity; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IMP:ARUK-UCL.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0051248; P:negative regulation of protein metabolic process; ISO:MGI.
DR GO; GO:1901389; P:negative regulation of transforming growth factor beta activation; ISS:UniProtKB.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:MGI.
DR GO; GO:0045793; P:positive regulation of cell size; ISO:MGI.
DR GO; GO:1904031; P:positive regulation of cyclin-dependent protein kinase activity; IMP:ARUK-UCL.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:ARUK-UCL.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:ARUK-UCL.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IMP:ARUK-UCL.
DR GO; GO:0031396; P:regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR GO; GO:0010033; P:response to organic substance; IDA:MGI.
DR GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0097435; P:supramolecular fiber organization; ISO:MGI.
DR GO; GO:1905323; P:telomerase holoenzyme complex assembly; ISO:MGI.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0019062; P:virion attachment to host cell; ISO:MGI.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell membrane; Chaperone; Cytoplasm;
KW Direct protein sequencing; Glycoprotein; Membrane; Methylation;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW S-nitrosylation; Secreted; Stress response; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2445630,
FT ECO:0000269|PubMed:3458168, ECO:0000269|PubMed:8289821"
FT CHAIN 2..724
FT /note="Heat shock protein HSP 90-beta"
FT /id="PRO_0000062918"
FT REGION 2..527
FT /note="Interaction with TP53"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT REGION 2..214
FT /note="Interaction with BIRC2"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT REGION 9..231
FT /note="Interaction with NR3C1"
FT /evidence="ECO:0000269|PubMed:27686098"
FT REGION 215..552
FT /note="Interaction with AHSA1"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT REGION 222..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..608
FT /note="Interaction with NR3C1"
FT /evidence="ECO:0000269|PubMed:27686098"
FT REGION 620..723
FT /note="Interaction with NR1D1"
FT /evidence="ECO:0000269|PubMed:27686098"
FT REGION 694..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 720..724
FT /note="TPR repeat-binding"
FT COMPBIAS 241..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 126..127
FT /note="Cleaved under oxidative stress"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 219
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17208939, ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:17622165, ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17622165"
FT MOD_RES 297
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 301
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 305
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 399
FT /note="N6-malonyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 435
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 481
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 484
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 531
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 531
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 574
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 577
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 590
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 624
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 718
FT /note="Phosphoserine; by PLK2 and PLK3"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT CARBOHYD 434
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:22556278"
FT CARBOHYD 452
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:22556278"
FT CONFLICT 76
FT /note="I -> L (in Ref. 2; AAA37865)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="Q -> R (in Ref. 10; AAC36532)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="K -> R (in Ref. 10; AAC36532)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="V -> I (in Ref. 5; BAE27449)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="L -> F (in Ref. 2; AAA37865)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="Y -> H (in Ref. 10; AAC36532)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="A -> P (in Ref. 2; AAA37865)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="S -> P (in Ref. 1; AAA37866)"
FT /evidence="ECO:0000305"
FT CONFLICT 531..535
FT /note="KSLVS -> GGPGT (in Ref. 11; AAB23704)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="K -> N (in Ref. 11; AAB23704)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="V -> F (in Ref. 11; AAB23704)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="G -> V (in Ref. 2; AAA37865)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="E -> G (in Ref. 5; BAE27449)"
FT /evidence="ECO:0000305"
FT CONFLICT 719
FT /note="R -> P (in Ref. 1; AAA37866)"
FT /evidence="ECO:0000305"
SQ 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
