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Database: UniProt
Entry: P04792
LinkDB: P04792
Original site: P04792 
ID   HSPB1_HUMAN             Reviewed;         205 AA.
AC   P04792; B2R4N8; Q6FI47; Q96C20; Q96EI7; Q9UC31; Q9UC34; Q9UC35; Q9UC36;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   10-FEB-2021, entry version 242.
DE   RecName: Full=Heat shock protein beta-1;
DE            Short=HspB1;
DE   AltName: Full=28 kDa heat shock protein;
DE   AltName: Full=Estrogen-regulated 24 kDa protein;
DE   AltName: Full=Heat shock 27 kDa protein;
DE            Short=HSP 27;
DE   AltName: Full=Stress-responsive protein 27;
DE            Short=SRP27;
GN   Name=HSPB1; Synonyms=HSP27, HSP28;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3714473; DOI=10.1093/nar/14.10.4127;
RA   Hickey E., Brandon S.E., Potter R., Stein G., Stein J., Weber L.A.;
RT   "Sequence and organization of genes encoding the human 27 kDa heat shock
RT   protein.";
RL   Nucleic Acids Res. 14:4127-4145(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=2243808; DOI=10.1093/nar/18.21.6457;
RA   Carper S.W., Rocheleau T.A., Storm F.K.;
RT   "cDNA sequence of a human heat shock protein HSP27.";
RL   Nucleic Acids Res. 18:6457-6457(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND SUBUNIT.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=10777697; DOI=10.1006/bbrc.2000.2553;
RA   Hino M., Kurogi K., Okubo M.-A., Murata-Hori M., Hosoya H.;
RT   "Small heat shock protein 27 (HSP27) associates with tubulin/microtubules
RT   in HeLa cells.";
RL   Biochem. Biophys. Res. Commun. 271:164-169(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary carcinoma;
RA   Briolay J., Chareyron P., Mehlen P., Arrigo A.;
RT   "Identification of a new cDNA sequence from human breast carcinoma cells
RT   encoding the 28kDa heat shock protein.";
RL   Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA   Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA   Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT   "Large-scale concatenation cDNA sequencing.";
RL   Genome Res. 7:353-358(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NIEHS SNPs program;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, Ovary, Pancreas, Skin, and Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [13]
RP   PROTEIN SEQUENCE OF 5-12; 97-112; 141-154 AND 172-188.
RX   PubMed=2295696; DOI=10.1172/jci114413;
RA   Strahler J.R., Kuick R., Eckerskorn C., Lottspeich F., Richardson B.C.,
RA   Fox D.A., Stoolman L.M., Hanson C.A., Nichols D., Tueche H.J., Hanash S.M.;
RT   "Identification of two related markers for common acute lymphoblastic
RT   leukemia as heat shock proteins.";
RL   J. Clin. Invest. 85:200-207(1990).
RN   [14]
RP   PROTEIN SEQUENCE OF 6-37; 57-75; 80-89; 97-127 AND 141-188, PHOSPHORYLATION
RP   AT SER-82, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RA   Bienvenut W.V., Waridel P., Quadroni M.;
RL   Submitted (MAR-2009) to UniProtKB.
RN   [15]
RP   PROTEIN SEQUENCE OF 13-20; 38-46; 97-110; 141-154 AND 172-186,
RP   PHOSPHORYLATION, AND INDUCTION BY HEAT SHOCK.
RC   TISSUE=Mammary carcinoma;
RX   PubMed=8325890;
RA   Faucher C., Capdevielle J., Canal I., Ferrara P., Mazarguil H.,
RA   McGuire W.L., Darbon J.-M.;
RT   "The 28-kDa protein whose phosphorylation is induced by protein kinase C
RT   activators in MCF-7 cells belongs to the family of low molecular mass heat
RT   shock proteins and is the estrogen-regulated 24-kDa protein.";
RL   J. Biol. Chem. 268:15168-15173(1993).
RN   [16]
RP   PROTEIN SEQUENCE OF 21-59; 93-98; 129-134 AND 178-193, INTERACTION WITH
RP   CRYAB, AND TISSUE SPECIFICITY.
RC   TISSUE=Pectoralis muscle;
RX   PubMed=1560006;
RA   Kato K., Shinohara H., Goto S., Inaguma Y., Morishita R., Asano T.;
RT   "Copurification of small heat shock protein with alpha B crystallin from
RT   human skeletal muscle.";
RL   J. Biol. Chem. 267:7718-7725(1992).
RN   [17]
RP   PROTEIN SEQUENCE OF 76-89, AND PHOSPHORYLATION AT SER-78 AND SER-82.
RX   PubMed=1730670;
RA   Landry J., Lambert H., Zhou M., Lavoie J.N., Hickey E., Weber L.A.,
RA   Anderson C.W.;
RT   "Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and
RT   mitogen-activated kinases that recognize the same amino acid motif as S6
RT   kinase II.";
RL   J. Biol. Chem. 267:794-803(1992).
RN   [18]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 109-205, AND INDUCTION BY ESTROGEN.
RC   TISSUE=Mammary carcinoma;
RX   PubMed=2743305;
RA   Fuqua S.A.W., Blum-Salingaros M., McGuire W.L.;
RT   "Induction of the estrogen-regulated '24K' protein by heat shock.";
RL   Cancer Res. 49:4126-4129(1989).
RN   [19]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 122-205.
RX   PubMed=1763035; DOI=10.1073/pnas.88.24.11212;
RA   Mendelsohn M.E., Zhu Y., O'Neill S.;
RT   "The 29-kDa proteins phosphorylated in thrombin-activated human platelets
RT   are forms of the estrogen receptor-related 27-kDa heat shock protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:11212-11216(1991).
RN   [20]
RP   PHOSPHORYLATION AT SER-15; SER-78 AND SER-82 BY MAPKAPK2.
RX   PubMed=1332886; DOI=10.1016/0014-5793(92)81216-9;
RA   Stokoe D., Engel K., Campbell D.G., Cohen P., Gaestel M.;
RT   "Identification of MAPKAP kinase 2 as a major enzyme responsible for the
RT   phosphorylation of the small mammalian heat shock proteins.";
RL   FEBS Lett. 313:307-313(1992).
RN   [21]
RP   PHOSPHORYLATION BY MAPKAPK2.
RX   PubMed=8093612;
RA   Jakob U., Gaestel M., Engel K., Buchner J.;
RT   "Small heat shock proteins are molecular chaperones.";
RL   J. Biol. Chem. 268:1517-1520(1993).
RN   [22]
RP   PHOSPHORYLATION AT SER-15; SER-78 AND SER-82.
RX   PubMed=8774846; DOI=10.1016/0014-5793(96)00816-2;
RA   Clifton A.D., Young P.R., Cohen P.;
RT   "A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP
RT   kinase-3 and their activation by cytokines and cellular stress.";
RL   FEBS Lett. 392:209-214(1996).
RN   [23]
RP   FUNCTION, SUBUNIT, PHOSPHORYLATION AT SER-15; SER-78 AND SER-82, AND
RP   MUTAGENESIS OF SER-15; SER-78 AND SER-82.
RX   PubMed=10383393; DOI=10.1074/jbc.274.27.18947;
RA   Rogalla T., Ehrnsperger M., Preville X., Kotlyarov A., Lutsch G.,
RA   Ducasse C., Paul C., Wieske M., Arrigo A.P., Buchner J., Gaestel M.;
RT   "Regulation of Hsp27 oligomerization, chaperone function, and protective
RT   activity against oxidative stress/tumor necrosis factor alpha by
RT   phosphorylation.";
RL   J. Biol. Chem. 274:18947-18956(1999).
RN   [24]
RP   INTERACTION WITH HSPBAP1.
RX   PubMed=10751411; DOI=10.1074/jbc.m001981200;
RA   Liu C., Gilmont R.R., Benndorf R., Welsh M.J.;
RT   "Identification and characterization of a novel protein from Sertoli cells,
RT   PASS1, that associates with mammalian small stress protein hsp27.";
RL   J. Biol. Chem. 275:18724-18731(2000).
RN   [25]
RP   INTERACTION WITH HSPB8.
RX   PubMed=11342557; DOI=10.1074/jbc.m103001200;
RA   Benndorf R., Sun X., Gilmont R.R., Biederman K.J., Molloy M.P.,
RA   Goodmurphy C.W., Cheng H., Andrews P.C., Welsh M.J.;
RT   "HSP22, a new member of the small heat shock protein superfamily, interacts
RT   with mimic of phosphorylated HSP27 (3DHSP27).";
RL   J. Biol. Chem. 276:26753-26761(2001).
RN   [26]
RP   PHOSPHORYLATION AT SER-78 AND SER-82, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=15976317; DOI=10.1161/01.res.0000174815.10996.08;
RA   De Souza A.I., Wait R., Mitchell A.G., Banner N.R., Dunn M.J., Rose M.L.;
RT   "Heat shock protein 27 is associated with freedom from graft vasculopathy
RT   after human cardiac transplantation.";
RL   Circ. Res. 97:192-198(2005).
RN   [27]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-65, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [28]
RP   INDUCTION (MICROBIAL INFECTION), AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA   Leong W.F., Chow V.T.;
RT   "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal
RT   differential cellular gene expression in response to enterovirus 71
RT   infection.";
RL   Cell. Microbiol. 8:565-580(2006).
RN   [29]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-83, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [30]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17924679; DOI=10.1021/pr070152u;
RA   Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT   "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT   and high confident phosphopeptide identification by cross-validation of
RT   MS/MS and MS/MS/MS spectra.";
RL   J. Proteome Res. 6:4150-4162(2007).
RN   [31]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [32]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-199, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [33]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-199, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [34]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19464326; DOI=10.1016/j.bbamcr.2009.05.005;
RA   Vos M.J., Kanon B., Kampinga H.H.;
RT   "HSPB7 is a SC35 speckle resident small heat shock protein.";
RL   Biochim. Biophys. Acta 1793:1343-1353(2009).
RN   [35]
RP   FUNCTION, AND PHOSPHORYLATION AT SER-78 AND SER-82.
RX   PubMed=19166925; DOI=10.1016/j.cellsig.2009.01.009;
RA   Kostenko S., Johannessen M., Moens U.;
RT   "PKA-induced F-actin rearrangement requires phosphorylation of Hsp27 by the
RT   MAPKAP kinase MK5.";
RL   Cell. Signal. 21:712-718(2009).
RN   [36]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [37]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [38]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-65; SER-78; SER-82
RP   AND SER-199, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [39]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [40]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [41]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-78; SER-82; SER-86;
RP   THR-174; SER-176 AND SER-199, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [42]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-78; SER-82; SER-86;
RP   SER-98 AND SER-199, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [43]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-12, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [44]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [45]
RP   VARIANTS CMT2F PHE-135 AND TRP-136, AND VARIANTS HMN2B TRP-127; PHE-135;
RP   ILE-151 AND LEU-182.
RX   PubMed=15122254; DOI=10.1038/ng1354;
RA   Evgrafov O.V., Mersiyanova I., Irobi J., Van Den Bosch L., Dierick I.,
RA   Leung C.L., Schagina O., Verpoorten N., Van Impe K., Fedotov V., Dadali E.,
RA   Auer-Grumbach M., Windpassinger C., Wagner K., Mitrovic Z.,
RA   Hilton-Jones D., Talbot K., Martin J.-J., Vasserman N., Tverskaya S.,
RA   Polyakov A., Liem R.K.H., Gettemans J., Robberecht W., De Jonghe P.,
RA   Timmerman V.;
RT   "Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth
RT   disease and distal hereditary motor neuropathy.";
RL   Nat. Genet. 36:602-606(2004).
RN   [46]
RP   VARIANTS HMN2B LEU-39; ARG-84; MET-99; PHE-135 AND GLY-140.
RX   PubMed=18832141; DOI=10.1212/01.wnl.0000319696.14225.67;
RA   Houlden H., Laura M., Wavrant-De Vrieze F., Blake J., Wood N., Reilly M.M.;
RT   "Mutations in the HSP27 (HSPB1) gene cause dominant, recessive, and
RT   sporadic distal HMN/CMT type 2.";
RL   Neurology 71:1660-1668(2008).
RN   [47]
RP   VARIANT HMN2B GLN-141.
RX   PubMed=18952241; DOI=10.1016/j.jns.2008.09.031;
RA   Ikeda Y., Abe A., Ishida C., Takahashi K., Hayasaka K., Yamada M.;
RT   "A clinical phenotype of distal hereditary motor neuronopathy type II with
RT   a novel HSPB1 mutation.";
RL   J. Neurol. Sci. 277:9-12(2009).
RN   [48]
RP   VARIANT TYR-156, CHARACTERIZATION OF VARIANT TYR-156, CHARACTERIZATION OF
RP   VARIANTS HMN2B TRP-127; PHE-135; ILE-151 AND LEU-182, CHARACTERIZATION OF
RP   VARIANT CMT2F TRP-136, FUNCTION, AND SUBUNIT.
RX   PubMed=20178975; DOI=10.1074/jbc.m109.082644;
RA   Almeida-Souza L., Goethals S., de Winter V., Dierick I., Gallardo R.,
RA   Van Durme J., Irobi J., Gettemans J., Rousseau F., Schymkowitz J.,
RA   Timmerman V., Janssens S.;
RT   "Increased monomerization of mutant HSPB1 leads to protein hyperactivity in
RT   Charcot-Marie-Tooth neuropathy.";
RL   J. Biol. Chem. 285:12778-12786(2010).
RN   [49]
RP   VARIANT HMN2B ILE-180.
RX   PubMed=20870250; DOI=10.1016/j.jns.2010.09.008;
RA   Luigetti M., Fabrizi G.M., Madia F., Ferrarini M., Conte A., Del Grande A.,
RA   Tasca G., Tonali P.A., Sabatelli M.;
RT   "A novel HSPB1 mutation in an Italian patient with CMT2/dHMN phenotype.";
RL   J. Neurol. Sci. 298:114-117(2010).
RN   [50]
RP   VARIANTS HMN2B ARG-34; LYS-41; LEU-136 AND ILE-180, AND VARIANTS CMT2F
RP   LEU-39; LEU-136 AND TRP-188.
RX   PubMed=22176143; DOI=10.1111/j.1529-8027.2011.00361.x;
RA   Capponi S., Geroldi A., Fossa P., Grandis M., Ciotti P., Gulli R.,
RA   Schenone A., Mandich P., Bellone E.;
RT   "HSPB1 and HSPB8 in inherited neuropathies: study of an Italian cohort of
RT   dHMN and CMT2 patients.";
RL   J. Peripher. Nerv. Syst. 16:287-294(2011).
RN   [51]
RP   VARIANT CMT2F ALA-164.
RX   PubMed=22206013; DOI=10.1371/journal.pone.0029393;
RA   Lin K.P., Soong B.W., Yang C.C., Huang L.W., Chang M.H., Lee I.H.,
RA   Antonellis A., Lee Y.C.;
RT   "The mutational spectrum in a cohort of Charcot-Marie-Tooth disease type 2
RT   among the Han Chinese in Taiwan.";
RL   PLoS ONE 6:E29393-E29393(2011).
RN   [52]
RP   FUNCTION, CHARACTERIZATION OF VARIANTS HMN2B TRP-127 AND LEU-182, AND
RP   CHARACTERIZATION OF VARIANT CMT2F PHE-135.
RX   PubMed=23728742; DOI=10.1007/s00401-013-1133-6;
RA   Holmgren A., Bouhy D., De Winter V., Asselbergh B., Timmermans J.P.,
RA   Irobi J., Timmerman V.;
RT   "Charcot-Marie-Tooth causing HSPB1 mutations increase Cdk5-mediated
RT   phosphorylation of neurofilaments.";
RL   Acta Neuropathol. 126:93-108(2013).
RN   [53]
RP   CHARACTERIZATION OF VARIANTS HMN2B ARG-84 AND MET-99, AND INTERACTION WITH
RP   HSPB6.
RX   PubMed=23948568; DOI=10.1016/j.abb.2013.07.028;
RA   Nefedova V.V., Sudnitsyna M.V., Strelkov S.V., Gusev N.B.;
RT   "Structure and properties of G84R and L99M mutants of human small heat
RT   shock protein HspB1 correlating with motor neuropathy.";
RL   Arch. Biochem. Biophys. 538:16-24(2013).
RN   [54]
RP   CHARACTERIZATION OF VARIANTS HMN2B GLY-140 AND GLN-141.
RX   PubMed=23643870; DOI=10.1016/j.biochi.2013.04.014;
RA   Nefedova V.V., Datskevich P.N., Sudnitsyna M.V., Strelkov S.V., Gusev N.B.;
RT   "Physico-chemical properties of R140G and K141Q mutants of human small heat
RT   shock protein HspB1 associated with hereditary peripheral neuropathies.";
RL   Biochimie 95:1582-1592(2013).
RN   [55]
RP   CHARACTERIZATION OF VARIANTS HMN2B ARG-34; LEU-39 AND LYS-41.
RX   PubMed=25965061; DOI=10.1371/journal.pone.0126248;
RA   Muranova L.K., Weeks S.D., Strelkov S.V., Gusev N.B.;
RT   "Characterization of mutants of human small heat shock protein HspB1
RT   carrying replacements in the n-terminal domain and associated with
RT   hereditary motor neuron diseases.";
RL   PLoS ONE 10:E0126248-E0126248(2015).
RN   [56]
RP   VARIANT HIS-190.
RX   PubMed=27492805; DOI=10.1002/humu.23062;
RA   Capponi S., Geuens T., Geroldi A., Origone P., Verdiani S., Cichero E.,
RA   Adriaenssens E., De Winter V., Bandettini di Poggio M., Barberis M.,
RA   Chio A., Fossa P., Mandich P., Bellone E., Timmerman V.;
RT   "Molecular chaperones in the pathogenesis of amyotrophic lateral sclerosis:
RT   the role of HSPB1.";
RL   Hum. Mutat. 37:1202-1208(2016).
RN   [57]
RP   VARIANTS HMN2B SER-7; LEU-39; ASP-53; TRP-127; ARG-128; ILE-151;
RP   175-GLN--LYS-205 DEL; ILE-180 AND LEU-187, SUBCELLULAR LOCATION, AND
RP   CHARACTERIZATION OF VARIANTS HMN2B SER-7; ASP-53; ARG-128 AND LEU-187.
RX   PubMed=28144995; DOI=10.1002/humu.23189;
RA   Echaniz-Laguna A., Geuens T., Petiot P., Pereon Y., Adriaenssens E.,
RA   Haidar M., Capponi S., Maisonobe T., Fournier E., Dubourg O., Degos B.,
RA   Salachas F., Lenglet T., Eymard B., Delmont E., Pouget J.,
RA   Juntas Morales R., Goizet C., Latour P., Timmerman V., Stojkovic T.;
RT   "Axonal Neuropathies due to Mutations in Small Heat Shock Proteins:
RT   Clinical, Genetic, and Functional Insights into Novel Mutations.";
RL   Hum. Mutat. 38:556-568(2017).
CC   -!- FUNCTION: Small heat shock protein which functions as a molecular
CC       chaperone probably maintaining denatured proteins in a folding-
CC       competent state (PubMed:10383393, PubMed:20178975). Plays a role in
CC       stress resistance and actin organization (PubMed:19166925). Through its
CC       molecular chaperone activity may regulate numerous biological processes
CC       including the phosphorylation and the axonal transport of neurofilament
CC       proteins (PubMed:23728742). {ECO:0000269|PubMed:10383393,
CC       ECO:0000269|PubMed:19166925, ECO:0000269|PubMed:20178975,
CC       ECO:0000269|PubMed:23728742}.
CC   -!- SUBUNIT: Homooligomer (PubMed:10383393). Homodimer; becomes monomeric
CC       upon activation (PubMed:20178975). Heterooligomer; with HSPB6
CC       (PubMed:23948568). Associates with alpha- and beta-tubulin
CC       (PubMed:10777697). Interacts with TGFB1I1 (By similarity). Interacts
CC       with CRYAB (PubMed:1560006). Interacts with HSPB8 (PubMed:11342557).
CC       Interacts with HSPBAP1 (PubMed:10751411).
CC       {ECO:0000250|UniProtKB:P42930, ECO:0000269|PubMed:10383393,
CC       ECO:0000269|PubMed:10751411, ECO:0000269|PubMed:10777697,
CC       ECO:0000269|PubMed:11342557, ECO:0000269|PubMed:1560006,
CC       ECO:0000269|PubMed:20178975, ECO:0000269|PubMed:23948568}.
CC   -!- INTERACTION:
CC       P04792; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-352682, EBI-10173507;
CC       P04792; P31749: AKT1; NbExp=3; IntAct=EBI-352682, EBI-296087;
CC       P04792; Q6ZTN6-2: ANKRD13D; NbExp=3; IntAct=EBI-352682, EBI-25840993;
CC       P04792; Q8N8A2-2: ANKRD44; NbExp=3; IntAct=EBI-352682, EBI-21636328;
CC       P04792; Q92688: ANP32B; NbExp=3; IntAct=EBI-352682, EBI-762428;
CC       P04792; P08758: ANXA5; NbExp=3; IntAct=EBI-352682, EBI-296601;
CC       P04792; P13928: ANXA8; NbExp=3; IntAct=EBI-352682, EBI-2556915;
CC       P04792; D3DTF8: APLN; NbExp=3; IntAct=EBI-352682, EBI-22002556;
CC       P04792; P05067: APP; NbExp=3; IntAct=EBI-352682, EBI-77613;
CC       P04792; O94778: AQP8; NbExp=3; IntAct=EBI-352682, EBI-19124986;
CC       P04792; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-352682, EBI-2875816;
CC       P04792; Q86TN1: ARNT2; NbExp=3; IntAct=EBI-352682, EBI-25844820;
CC       P04792; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-352682, EBI-14199987;
CC       P04792; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-352682, EBI-10254793;
CC       P04792; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-352682, EBI-9089489;
CC       P04792; P15313: ATP6V1B1; NbExp=3; IntAct=EBI-352682, EBI-2891281;
CC       P04792; O95817: BAG3; NbExp=7; IntAct=EBI-352682, EBI-747185;
CC       P04792; P46379-2: BAG6; NbExp=3; IntAct=EBI-352682, EBI-10988864;
CC       P04792; Q16611: BAK1; NbExp=3; IntAct=EBI-352682, EBI-519866;
CC       P04792; Q14457: BECN1; NbExp=3; IntAct=EBI-352682, EBI-949378;
CC       P04792; Q96LC9: BMF; NbExp=3; IntAct=EBI-352682, EBI-3919268;
CC       P04792; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-352682, EBI-10693038;
CC       P04792; Q9H0W9-4: C11orf54; NbExp=3; IntAct=EBI-352682, EBI-25849710;
CC       P04792; Q32Q52: C12orf74; NbExp=3; IntAct=EBI-352682, EBI-12891828;
CC       P04792; Q96LL4: C8orf48; NbExp=3; IntAct=EBI-352682, EBI-751596;
CC       P04792; P27797: CALR; NbExp=2; IntAct=EBI-352682, EBI-1049597;
CC       P04792; Q8N5S9-2: CAMKK1; NbExp=3; IntAct=EBI-352682, EBI-25850646;
CC       P04792; Q9HC96: CAPN10; NbExp=3; IntAct=EBI-352682, EBI-3915761;
CC       P04792; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-352682, EBI-10181422;
CC       P04792; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-352682, EBI-744045;
CC       P04792; Q96DZ5: CLIP3; NbExp=3; IntAct=EBI-352682, EBI-12823145;
CC       P04792; Q6PJW8-3: CNST; NbExp=3; IntAct=EBI-352682, EBI-25836090;
CC       P04792; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-352682, EBI-350590;
CC       P04792; Q9H9Q2: COPS7B; NbExp=3; IntAct=EBI-352682, EBI-2510162;
CC       P04792; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-352682, EBI-2872414;
CC       P04792; A0A140G945: CRYAA2; NbExp=3; IntAct=EBI-352682, EBI-25838900;
CC       P04792; P02511: CRYAB; NbExp=6; IntAct=EBI-352682, EBI-739060;
CC       P04792; P01040: CSTA; NbExp=3; IntAct=EBI-352682, EBI-724303;
CC       P04792; Q9UER7: DAXX; NbExp=4; IntAct=EBI-352682, EBI-77321;
CC       P04792; Q5TAQ9-2: DCAF8; NbExp=3; IntAct=EBI-352682, EBI-25842815;
CC       P04792; O00148: DDX39A; NbExp=3; IntAct=EBI-352682, EBI-348253;
CC       P04792; O00273: DFFA; NbExp=2; IntAct=EBI-352682, EBI-727171;
CC       P04792; Q8NDP9: DKFZp547K2416; NbExp=3; IntAct=EBI-352682, EBI-25842538;
CC       P04792; Q7L591-3: DOK3; NbExp=3; IntAct=EBI-352682, EBI-10694655;
CC       P04792; A0A024RCP2: DOM3Z; NbExp=3; IntAct=EBI-352682, EBI-25847826;
CC       P04792; Q9BPU6: DPYSL5; NbExp=3; IntAct=EBI-352682, EBI-724653;
CC       P04792; Q15029: EFTUD2; NbExp=2; IntAct=EBI-352682, EBI-357897;
CC       P04792; P00533: EGFR; NbExp=3; IntAct=EBI-352682, EBI-297353;
CC       P04792; O00303: EIF3F; NbExp=3; IntAct=EBI-352682, EBI-711990;
CC       P04792; Q14240: EIF4A2; NbExp=2; IntAct=EBI-352682, EBI-73473;
CC       P04792; P78344: EIF4G2; NbExp=3; IntAct=EBI-352682, EBI-296519;
CC       P04792; Q6UXG2-3: ELAPOR1; NbExp=3; IntAct=EBI-352682, EBI-12920100;
CC       P04792; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-352682, EBI-10213520;
CC       P04792; Q6P587-2: FAHD1; NbExp=3; IntAct=EBI-352682, EBI-12902289;
CC       P04792; Q6P1L5: FAM117B; NbExp=3; IntAct=EBI-352682, EBI-3893327;
CC       P04792; Q49AJ0-4: FAM135B; NbExp=3; IntAct=EBI-352682, EBI-25835236;
CC       P04792; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-352682, EBI-11793142;
CC       P04792; Q17RN3: FAM98C; NbExp=3; IntAct=EBI-352682, EBI-5461838;
CC       P04792; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-352682, EBI-8468186;
CC       P04792; O15287: FANCG; NbExp=3; IntAct=EBI-352682, EBI-81610;
CC       P04792; Q8TC84: FANK1; NbExp=3; IntAct=EBI-352682, EBI-21975404;
CC       P04792; O00757: FBP2; NbExp=3; IntAct=EBI-352682, EBI-719781;
CC       P04792; Q02790: FKBP4; NbExp=2; IntAct=EBI-352682, EBI-1047444;
CC       P04792; P02794: FTH1; NbExp=2; IntAct=EBI-352682, EBI-713259;
CC       P04792; P11413: G6PD; NbExp=2; IntAct=EBI-352682, EBI-4289891;
CC       P04792; P15976-2: GATA1; NbExp=3; IntAct=EBI-352682, EBI-9090198;
CC       P04792; Q9NXC2: GFOD1; NbExp=3; IntAct=EBI-352682, EBI-8799578;
CC       P04792; Q9HBQ8: GOLGA2P5; NbExp=4; IntAct=EBI-352682, EBI-22000587;
CC       P04792; O95872: GPANK1; NbExp=3; IntAct=EBI-352682, EBI-751540;
CC       P04792; Q7Z602: GPR141; NbExp=3; IntAct=EBI-352682, EBI-21649723;
CC       P04792; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-352682, EBI-347538;
CC       P04792; P78417: GSTO1; NbExp=2; IntAct=EBI-352682, EBI-712083;
CC       P04792; A0A024R1L7: hCG_41307; NbExp=3; IntAct=EBI-352682, EBI-25849938;
CC       P04792; P04792: HSPB1; NbExp=12; IntAct=EBI-352682, EBI-352682;
CC       P04792; Q9UJY1: HSPB8; NbExp=3; IntAct=EBI-352682, EBI-739074;
CC       P04792; Q96EW2-2: HSPBAP1; NbExp=3; IntAct=EBI-352682, EBI-25835621;
CC       P04792; Q7Z6Z7: HUWE1; NbExp=3; IntAct=EBI-352682, EBI-625934;
CC       P04792; P78318: IGBP1; NbExp=3; IntAct=EBI-352682, EBI-1055954;
CC       P04792; Q14005-2: IL16; NbExp=3; IntAct=EBI-352682, EBI-17178971;
CC       P04792; Q9NXX0: ILF3; NbExp=3; IntAct=EBI-352682, EBI-743980;
CC       P04792; Q8NA54: IQUB; NbExp=3; IntAct=EBI-352682, EBI-10220600;
CC       P04792; Q9UKP3-2: ITGB1BP2; NbExp=3; IntAct=EBI-352682, EBI-25856470;
CC       P04792; P0C870: JMJD7; NbExp=3; IntAct=EBI-352682, EBI-9090173;
CC       P04792; Q9NVX7-2: KBTBD4; NbExp=3; IntAct=EBI-352682, EBI-25871195;
CC       P04792; Q8WZ19: KCTD13; NbExp=3; IntAct=EBI-352682, EBI-742916;
CC       P04792; Q96SI1-2: KCTD15; NbExp=3; IntAct=EBI-352682, EBI-12382297;
CC       P04792; Q06136: KDSR; NbExp=3; IntAct=EBI-352682, EBI-3909166;
CC       P04792; Q6ZU52: KIAA0408; NbExp=3; IntAct=EBI-352682, EBI-739493;
CC       P04792; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-352682, EBI-2796400;
CC       P04792; P57682: KLF3; NbExp=3; IntAct=EBI-352682, EBI-8472267;
CC       P04792; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-352682, EBI-714379;
CC       P04792; Q8N1A0: KRT222; NbExp=3; IntAct=EBI-352682, EBI-8473062;
CC       P04792; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-352682, EBI-10241252;
CC       P04792; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-352682, EBI-10241353;
CC       P04792; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-352682, EBI-10261141;
CC       P04792; Q14847-2: LASP1; NbExp=3; IntAct=EBI-352682, EBI-9088686;
CC       P04792; Q96PV6: LENG8; NbExp=3; IntAct=EBI-352682, EBI-739546;
CC       P04792; Q9UPM6: LHX6; NbExp=3; IntAct=EBI-352682, EBI-10258746;
CC       P04792; Q8N448: LNX2; NbExp=3; IntAct=EBI-352682, EBI-2340947;
CC       P04792; A2RU56: LOC401296; NbExp=3; IntAct=EBI-352682, EBI-9088215;
CC       P04792; Q96JB6: LOXL4; NbExp=3; IntAct=EBI-352682, EBI-749562;
CC       P04792; Q14693: LPIN1; NbExp=3; IntAct=EBI-352682, EBI-5278370;
CC       P04792; Q9UDY8-2: MALT1; NbExp=3; IntAct=EBI-352682, EBI-12056869;
CC       P04792; Q99683: MAP3K5; NbExp=3; IntAct=EBI-352682, EBI-476263;
CC       P04792; P49137: MAPKAPK2; NbExp=3; IntAct=EBI-352682, EBI-993299;
CC       P04792; Q16644: MAPKAPK3; NbExp=3; IntAct=EBI-352682, EBI-1384657;
CC       P04792; Q8IW41: MAPKAPK5; NbExp=2; IntAct=EBI-352682, EBI-1201460;
CC       P04792; P61244-4: MAX; NbExp=3; IntAct=EBI-352682, EBI-25848049;
CC       P04792; Q03112-9: MECOM; NbExp=3; IntAct=EBI-352682, EBI-23820194;
CC       P04792; P51608: MECP2; NbExp=3; IntAct=EBI-352682, EBI-1189067;
CC       P04792; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-352682, EBI-8487781;
CC       P04792; Q15049: MLC1; NbExp=3; IntAct=EBI-352682, EBI-8475277;
CC       P04792; A0A0A0MR05: MLST8; NbExp=3; IntAct=EBI-352682, EBI-25835557;
CC       P04792; P08473: MME; NbExp=4; IntAct=EBI-352682, EBI-353759;
CC       P04792; Q8N594: MPND; NbExp=3; IntAct=EBI-352682, EBI-2512452;
CC       P04792; Q99608: NDN; NbExp=3; IntAct=EBI-352682, EBI-718177;
CC       P04792; Q8N5V2: NGEF; NbExp=3; IntAct=EBI-352682, EBI-718372;
CC       P04792; Q8NBF2-2: NHLRC2; NbExp=3; IntAct=EBI-352682, EBI-10697320;
CC       P04792; Q14995: NR1D2; NbExp=3; IntAct=EBI-352682, EBI-6144053;
CC       P04792; P36639-4: NUDT1; NbExp=3; IntAct=EBI-352682, EBI-25834643;
CC       P04792; Q9NZJ9: NUDT4; NbExp=3; IntAct=EBI-352682, EBI-4280066;
CC       P04792; O15381-5: NVL; NbExp=3; IntAct=EBI-352682, EBI-18577082;
CC       P04792; Q5BJF6-2: ODF2; NbExp=3; IntAct=EBI-352682, EBI-9090919;
CC       P04792; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-352682, EBI-1058491;
CC       P04792; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-352682, EBI-25830200;
CC       P04792; Q8N7H5: PAF1; NbExp=2; IntAct=EBI-352682, EBI-2607770;
CC       P04792; Q9BRX2: PELO; NbExp=4; IntAct=EBI-352682, EBI-1043580;
CC       P04792; O15534: PER1; NbExp=3; IntAct=EBI-352682, EBI-2557276;
CC       P04792; Q96FX8: PERP; NbExp=3; IntAct=EBI-352682, EBI-17183069;
CC       P04792; Q96LB9: PGLYRP3; NbExp=3; IntAct=EBI-352682, EBI-12339509;
CC       P04792; Q96G03: PGM2; NbExp=2; IntAct=EBI-352682, EBI-4399372;
CC       P04792; O75925: PIAS1; NbExp=3; IntAct=EBI-352682, EBI-629434;
CC       P04792; Q9UF11-2: PLEKHB1; NbExp=3; IntAct=EBI-352682, EBI-12832742;
CC       P04792; Q58EX7-2: PLEKHG4; NbExp=3; IntAct=EBI-352682, EBI-21503705;
CC       P04792; Q8NA72-3: POC5; NbExp=3; IntAct=EBI-352682, EBI-11751537;
CC       P04792; Q9H1D9: POLR3F; NbExp=3; IntAct=EBI-352682, EBI-710067;
CC       P04792; O43741: PRKAB2; NbExp=3; IntAct=EBI-352682, EBI-1053424;
CC       P04792; P11908: PRPS2; NbExp=3; IntAct=EBI-352682, EBI-4290895;
CC       P04792; A0A0C4DFM3: PRUNE2; NbExp=3; IntAct=EBI-352682, EBI-25830870;
CC       P04792; P28062-2: PSMB8; NbExp=3; IntAct=EBI-352682, EBI-372312;
CC       P04792; P62333: PSMC6; NbExp=3; IntAct=EBI-352682, EBI-357669;
CC       P04792; P47897: QARS1; NbExp=3; IntAct=EBI-352682, EBI-347462;
CC       P04792; Q86YS6: RAB43; NbExp=2; IntAct=EBI-352682, EBI-4401730;
CC       P04792; Q9Y5P3: RAI2; NbExp=3; IntAct=EBI-352682, EBI-746228;
CC       P04792; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-352682, EBI-17589229;
CC       P04792; Q8TDP1: RNASEH2C; NbExp=3; IntAct=EBI-352682, EBI-9027335;
CC       P04792; Q8N5U6: RNF10; NbExp=3; IntAct=EBI-352682, EBI-714023;
CC       P04792; Q96D59: RNF183; NbExp=3; IntAct=EBI-352682, EBI-743938;
CC       P04792; P62244: RPS15A; NbExp=3; IntAct=EBI-352682, EBI-347895;
CC       P04792; P62979: RPS27A; NbExp=3; IntAct=EBI-352682, EBI-357375;
CC       P04792; P08865: RPSA; NbExp=4; IntAct=EBI-352682, EBI-354112;
CC       P04792; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-352682, EBI-10248967;
CC       P04792; Q8N6K7-2: SAMD3; NbExp=3; IntAct=EBI-352682, EBI-11528848;
CC       P04792; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-352682, EBI-9089805;
CC       P04792; Q12874: SF3A3; NbExp=2; IntAct=EBI-352682, EBI-1051880;
CC       P04792; Q9NUL5-3: SHFL; NbExp=3; IntAct=EBI-352682, EBI-22000547;
CC       P04792; Q8IYI0: SHLD1; NbExp=3; IntAct=EBI-352682, EBI-2560428;
CC       P04792; P08195-4: SLC3A2; NbExp=3; IntAct=EBI-352682, EBI-12832276;
CC       P04792; Q9NSD5-3: SLC6A13; NbExp=3; IntAct=EBI-352682, EBI-25831241;
CC       P04792; Q92966: SNAPC3; NbExp=3; IntAct=EBI-352682, EBI-1760638;
CC       P04792; Q13573: SNW1; NbExp=3; IntAct=EBI-352682, EBI-632715;
CC       P04792; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-352682, EBI-11959123;
CC       P04792; Q6RVD6: SPATA8; NbExp=3; IntAct=EBI-352682, EBI-8635958;
CC       P04792; Q9Y657: SPIN1; NbExp=2; IntAct=EBI-352682, EBI-727129;
CC       P04792; Q8TCT7-2: SPPL2B; NbExp=3; IntAct=EBI-352682, EBI-8345366;
CC       P04792; Q9C004: SPRY4; NbExp=3; IntAct=EBI-352682, EBI-354861;
CC       P04792; Q8IXS7: SRGAP3; NbExp=3; IntAct=EBI-352682, EBI-18616594;
CC       P04792; Q9UNE7: STUB1; NbExp=4; IntAct=EBI-352682, EBI-357085;
CC       P04792; Q8NBJ7: SUMF2; NbExp=3; IntAct=EBI-352682, EBI-723091;
CC       P04792; Q17RD7-3: SYT16; NbExp=3; IntAct=EBI-352682, EBI-25861603;
CC       P04792; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-352682, EBI-745958;
CC       P04792; Q8IYN2: TCEAL8; NbExp=3; IntAct=EBI-352682, EBI-2116184;
CC       P04792; Q13569: TDG; NbExp=3; IntAct=EBI-352682, EBI-348333;
CC       P04792; Q86WV5: TEN1; NbExp=3; IntAct=EBI-352682, EBI-2562799;
CC       P04792; Q96A09: TENT5B; NbExp=3; IntAct=EBI-352682, EBI-752030;
CC       P04792; P21980-2: TGM2; NbExp=3; IntAct=EBI-352682, EBI-25842075;
CC       P04792; O60830: TIMM17B; NbExp=3; IntAct=EBI-352682, EBI-2372529;
CC       P04792; A0AVI4-2: TMEM129; NbExp=3; IntAct=EBI-352682, EBI-25871541;
CC       P04792; Q53NU3: tmp_locus_54; NbExp=3; IntAct=EBI-352682, EBI-10242677;
CC       P04792; Q8IUR5-4: TMTC1; NbExp=3; IntAct=EBI-352682, EBI-9089156;
CC       P04792; Q71RG4-4: TMUB2; NbExp=3; IntAct=EBI-352682, EBI-25831574;
CC       P04792; P04637: TP53; NbExp=3; IntAct=EBI-352682, EBI-366083;
CC       P04792; P13693: TPT1; NbExp=2; IntAct=EBI-352682, EBI-1783169;
CC       P04792; P36406: TRIM23; NbExp=3; IntAct=EBI-352682, EBI-740098;
CC       P04792; Q86WV8: TSC1; NbExp=3; IntAct=EBI-352682, EBI-12806590;
CC       P04792; Q9Y3Q8: TSC22D4; NbExp=3; IntAct=EBI-352682, EBI-739485;
CC       P04792; Q99614: TTC1; NbExp=3; IntAct=EBI-352682, EBI-742074;
CC       P04792; Q9BUF5: TUBB6; NbExp=3; IntAct=EBI-352682, EBI-356735;
CC       P04792; Q5VYS8-5: TUT7; NbExp=3; IntAct=EBI-352682, EBI-9088812;
CC       P04792; Q8NBM4-4: UBAC2; NbExp=3; IntAct=EBI-352682, EBI-25840976;
CC       P04792; Q969T4: UBE2E3; NbExp=3; IntAct=EBI-352682, EBI-348496;
CC       P04792; Q8WVN8: UBE2Q2; NbExp=3; IntAct=EBI-352682, EBI-2130157;
CC       P04792; Q04323-2: UBXN1; NbExp=3; IntAct=EBI-352682, EBI-11530712;
CC       P04792; O75604-3: USP2; NbExp=3; IntAct=EBI-352682, EBI-10696113;
CC       P04792; P45880: VDAC2; NbExp=3; IntAct=EBI-352682, EBI-354022;
CC       P04792; P58304: VSX2; NbExp=3; IntAct=EBI-352682, EBI-6427899;
CC       P04792; Q9BQA1: WDR77; NbExp=3; IntAct=EBI-352682, EBI-1237307;
CC       P04792; Q9BRX9: WDR83; NbExp=4; IntAct=EBI-352682, EBI-7705033;
CC       P04792; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-352682, EBI-12040603;
CC       P04792; P13010: XRCC5; NbExp=2; IntAct=EBI-352682, EBI-357997;
CC       P04792; P63104: YWHAZ; NbExp=4; IntAct=EBI-352682, EBI-347088;
CC       P04792; Q8TBF4: ZCRB1; NbExp=3; IntAct=EBI-352682, EBI-11124401;
CC       P04792; Q96K21: ZFYVE19; NbExp=3; IntAct=EBI-352682, EBI-6448240;
CC       P04792; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-352682, EBI-25831733;
CC       P04792; Q96N77-2: ZNF641; NbExp=3; IntAct=EBI-352682, EBI-12939666;
CC       P04792; Q9BS34: ZNF670; NbExp=3; IntAct=EBI-352682, EBI-745276;
CC       P04792; Q16670: ZSCAN26; NbExp=3; IntAct=EBI-352682, EBI-3920053;
CC       P04792; Q2QGD7: ZXDC; NbExp=3; IntAct=EBI-352682, EBI-1538838;
CC       P04792; A0A384ME25; NbExp=3; IntAct=EBI-352682, EBI-10211777;
CC       P04792; B7Z3E8; NbExp=3; IntAct=EBI-352682, EBI-25831617;
CC       P04792; Q7L8T7; NbExp=3; IntAct=EBI-352682, EBI-25831943;
CC       P04792; Q86V28; NbExp=3; IntAct=EBI-352682, EBI-10259496;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10777697,
CC       ECO:0000269|PubMed:28144995}. Nucleus {ECO:0000269|PubMed:19464326}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10777697}.
CC       Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles
CC       in mitotic cells. Translocates to the nucleus during heat shock and
CC       resides in sub-nuclear structures known as SC35 speckles or nuclear
CC       splicing speckles. {ECO:0000269|PubMed:19464326}.
CC   -!- TISSUE SPECIFICITY: Detected in all tissues tested: skeletal muscle,
CC       heart, aorta, large intestine, small intestine, stomach, esophagus,
CC       bladder, adrenal gland, thyroid, pancreas, testis, adipose tissue,
CC       kidney, liver, spleen, cerebral cortex, blood serum and cerebrospinal
CC       fluid. Highest levels are found in the heart and in tissues composed of
CC       striated and smooth muscle. {ECO:0000269|PubMed:1560006}.
CC   -!- INDUCTION: Up-regulated in response to environmental stresses such as
CC       heat shock (PubMed:8325890). Up-regulated by estrogen stimulation
CC       (PubMed:2743305). {ECO:0000269|PubMed:2743305,
CC       ECO:0000269|PubMed:8325890}.
CC   -!- INDUCTION: (Microbial infection) Up-regulated in response to
CC       enterovirus 71 (EV71) infection (at protein level).
CC       {ECO:0000269|PubMed:16548883}.
CC   -!- PTM: Phosphorylated upon exposure to protein kinase C activators and
CC       heat shock (PubMed:8325890). Phosphorylation by MAPKAPK2 and MAPKAPK3
CC       in response to stress dissociates HSPB1 from large small heat-shock
CC       protein (sHsps) oligomers and impairs its chaperone activity and
CC       ability to protect against oxidative stress effectively.
CC       Phosphorylation by MAPKAPK5 in response to PKA stimulation induces F-
CC       actin rearrangement (PubMed:1332886, PubMed:8093612, PubMed:19166925).
CC       {ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:19166925,
CC       ECO:0000269|PubMed:8093612, ECO:0000269|PubMed:8325890}.
CC   -!- DISEASE: Charcot-Marie-Tooth disease 2F (CMT2F) [MIM:606595]: A
CC       dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the
CC       peripheral nervous system, characterized by progressive weakness and
CC       atrophy, initially of the peroneal muscles and later of the distal
CC       muscles of the arms. Charcot-Marie-Tooth disease is classified in two
CC       main groups on the basis of electrophysiologic properties and
CC       histopathology: primary peripheral demyelinating neuropathies
CC       (designated CMT1 when they are dominantly inherited) and primary
CC       peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group
CC       are characterized by signs of axonal degeneration in the absence of
CC       obvious myelin alterations, normal or slightly reduced nerve conduction
CC       velocities, and progressive distal muscle weakness and atrophy. Onset
CC       of Charcot-Marie-Tooth disease type 2F is between 15 and 25 years with
CC       muscle weakness and atrophy usually beginning in feet and legs
CC       (peroneal distribution). Upper limb involvement occurs later.
CC       {ECO:0000269|PubMed:15122254, ECO:0000269|PubMed:20178975,
CC       ECO:0000269|PubMed:22176143, ECO:0000269|PubMed:22206013,
CC       ECO:0000269|PubMed:23728742}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Neuronopathy, distal hereditary motor, 2B (HMN2B)
CC       [MIM:608634]: A neuromuscular disorder. Distal hereditary motor
CC       neuronopathies constitute a heterogeneous group of neuromuscular
CC       disorders caused by selective degeneration of motor neurons in the
CC       anterior horn of the spinal cord, without sensory deficit in the
CC       posterior horn. The overall clinical picture consists of a classical
CC       distal muscular atrophy syndrome in the legs without clinical sensory
CC       loss. The disease starts with weakness and wasting of distal muscles of
CC       the anterior tibial and peroneal compartments of the legs. Later on,
CC       weakness and atrophy may expand to the proximal muscles of the lower
CC       limbs and/or to the distal upper limbs. {ECO:0000269|PubMed:15122254,
CC       ECO:0000269|PubMed:18832141, ECO:0000269|PubMed:18952241,
CC       ECO:0000269|PubMed:20178975, ECO:0000269|PubMed:20870250,
CC       ECO:0000269|PubMed:22176143, ECO:0000269|PubMed:23643870,
CC       ECO:0000269|PubMed:23728742, ECO:0000269|PubMed:23948568,
CC       ECO:0000269|PubMed:25965061, ECO:0000269|PubMed:28144995}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00285}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA62175.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAB20722.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA34498.1; Type=Frameshift; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
CC       URL="https://uantwerpen.vib.be/CMTMutations";
CC   -!- WEB RESOURCE: Name=NIEHS SNPs;
CC       URL="http://egp.gs.washington.edu/data/hspb1/";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/HSPB1ID40880ch7q11.html";
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DR   EMBL; L39370; AAA62175.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; X54079; CAA38016.1; -; mRNA.
DR   EMBL; Z23090; CAA80636.1; -; mRNA.
DR   EMBL; AB020027; BAB17232.1; -; mRNA.
DR   EMBL; U90906; AAB51056.1; -; mRNA.
DR   EMBL; CR407614; CAG28542.1; -; mRNA.
DR   EMBL; CR536489; CAG38728.1; -; mRNA.
DR   EMBL; BT019888; AAV38691.1; -; mRNA.
DR   EMBL; AK311894; BAG34835.1; -; mRNA.
DR   EMBL; DQ379985; ABC88475.1; -; Genomic_DNA.
DR   EMBL; AC006388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471220; EAW71803.1; -; Genomic_DNA.
DR   EMBL; BC000510; AAH00510.1; -; mRNA.
DR   EMBL; BC012292; AAH12292.1; -; mRNA.
DR   EMBL; BC012768; AAH12768.1; -; mRNA.
DR   EMBL; BC014920; AAH14920.1; -; mRNA.
DR   EMBL; BC073768; AAH73768.1; -; mRNA.
DR   EMBL; X16477; CAA34498.1; ALT_FRAME; mRNA.
DR   EMBL; S74571; AAB20722.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS5583.1; -.
DR   PIR; S12102; HHHU27.
DR   RefSeq; NP_001531.1; NM_001540.3.
DR   PDB; 2N3J; NMR; -; A/B=80-176.
DR   PDB; 3Q9P; X-ray; 2.00 A; A=90-171.
DR   PDB; 3Q9Q; X-ray; 2.20 A; A/B=90-171.
DR   PDB; 4MJH; X-ray; 2.60 A; A/C=84-176, B/D=179-186.
DR   PDB; 6DV5; X-ray; 3.58 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-205.
DR   PDB; 6GJH; X-ray; 2.10 A; A/B/C/D/E/F/G/H=84-170.
DR   PDBsum; 2N3J; -.
DR   PDBsum; 3Q9P; -.
DR   PDBsum; 3Q9Q; -.
DR   PDBsum; 4MJH; -.
DR   PDBsum; 6DV5; -.
DR   PDBsum; 6GJH; -.
DR   SMR; P04792; -.
DR   BioGRID; 109547; 596.
DR   DIP; DIP-412N; -.
DR   IntAct; P04792; 565.
DR   MINT; P04792; -.
DR   STRING; 9606.ENSP00000248553; -.
DR   BindingDB; P04792; -.
DR   ChEMBL; CHEMBL5976; -.
DR   DrugBank; DB06094; Apatorsen.
DR   DrugBank; DB11638; Artenimol.
DR   DrugBank; DB12695; Phenethyl Isothiocyanate.
DR   MoonDB; P04792; Predicted.
DR   iPTMnet; P04792; -.
DR   PhosphoSitePlus; P04792; -.
DR   SwissPalm; P04792; -.
DR   BioMuta; HSPB1; -.
DR   DMDM; 19855073; -.
DR   DOSAC-COBS-2DPAGE; P04792; -.
DR   OGP; P04792; -.
DR   REPRODUCTION-2DPAGE; IPI00025512; -.
DR   REPRODUCTION-2DPAGE; P04792; -.
DR   SWISS-2DPAGE; P04792; -.
DR   UCD-2DPAGE; P04792; -.
DR   CPTAC; CPTAC-1351; -.
DR   CPTAC; CPTAC-1426; -.
DR   CPTAC; CPTAC-1427; -.
DR   CPTAC; CPTAC-1428; -.
DR   CPTAC; CPTAC-1429; -.
DR   CPTAC; CPTAC-1430; -.
DR   CPTAC; CPTAC-702; -.
DR   CPTAC; CPTAC-703; -.
DR   CPTAC; CPTAC-704; -.
DR   CPTAC; CPTAC-970; -.
DR   EPD; P04792; -.
DR   jPOST; P04792; -.
DR   MassIVE; P04792; -.
DR   PaxDb; P04792; -.
DR   PeptideAtlas; P04792; -.
DR   PRIDE; P04792; -.
DR   ProteomicsDB; 51743; -.
DR   TopDownProteomics; P04792; -.
DR   ABCD; P04792; 3 sequenced antibodies.
DR   Antibodypedia; 603; 3045 antibodies.
DR   CPTC; P04792; 6 antibodies.
DR   DNASU; 3315; -.
DR   Ensembl; ENST00000248553; ENSP00000248553; ENSG00000106211.
DR   GeneID; 3315; -.
DR   KEGG; hsa:3315; -.
DR   CTD; 3315; -.
DR   DisGeNET; 3315; -.
DR   GeneCards; HSPB1; -.
DR   GeneReviews; HSPB1; -.
DR   HGNC; HGNC:5246; HSPB1.
DR   HPA; ENSG00000106211; Tissue enhanced (vagina).
DR   MalaCards; HSPB1; -.
DR   MIM; 602195; gene.
DR   MIM; 606595; phenotype.
DR   MIM; 608634; phenotype.
DR   neXtProt; NX_P04792; -.
DR   OpenTargets; ENSG00000106211; -.
DR   Orphanet; 99940; Autosomal dominant Charcot-Marie-Tooth disease type 2F.
DR   Orphanet; 139525; Distal hereditary motor neuropathy type 2.
DR   PharmGKB; PA29511; -.
DR   VEuPathDB; HostDB:ENSG00000106211.8; -.
DR   eggNOG; KOG3591; Eukaryota.
DR   GeneTree; ENSGT00940000155882; -.
DR   HOGENOM; CLU_095001_0_0_1; -.
DR   InParanoid; P04792; -.
DR   OMA; EEWAQWF; -.
DR   OrthoDB; 1187096at2759; -.
DR   PhylomeDB; P04792; -.
DR   TreeFam; TF105049; -.
DR   PathwayCommons; P04792; -.
DR   Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR   SIGNOR; P04792; -.
DR   BioGRID-ORCS; 3315; 6 hits in 876 CRISPR screens.
DR   ChiTaRS; HSPB1; human.
DR   GeneWiki; Hsp27; -.
DR   GenomeRNAi; 3315; -.
DR   Pharos; P04792; Tchem.
DR   PRO; PR:P04792; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P04792; protein.
DR   Bgee; ENSG00000106211; Expressed in myometrium and 241 other tissues.
DR   ExpressionAtlas; P04792; baseline and differential.
DR   Genevisible; P04792; HS.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000502; C:proteasome complex; ISS:BHF-UCL.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IMP:UniProtKB.
DR   GO; GO:0044183; F:protein folding chaperone; IMP:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0005080; F:protein kinase C binding; ISS:BHF-UCL.
DR   GO; GO:0008426; F:protein kinase C inhibitor activity; ISS:BHF-UCL.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:ARUK-UCL.
DR   GO; GO:0043130; F:ubiquitin binding; ISS:BHF-UCL.
DR   GO; GO:0099641; P:anterograde axonal protein transport; IMP:UniProtKB.
DR   GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IMP:BHF-UCL.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IMP:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IMP:BHF-UCL.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR   GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISS:BHF-UCL.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:BHF-UCL.
DR   GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IMP:BHF-UCL.
DR   GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IMP:BHF-UCL.
DR   GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:BHF-UCL.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:BHF-UCL.
DR   GO; GO:0010506; P:regulation of autophagy; NAS:ParkinsonsUK-UCL.
DR   GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:BHF-UCL.
DR   GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IMP:UniProtKB.
DR   GO; GO:0006446; P:regulation of translational initiation; TAS:ProtInc.
DR   GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR   GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR   GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   CDD; cd06475; ACD_HspB1_like; 1.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR   InterPro; IPR037876; ACD_HspB1.
DR   InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   PANTHER; PTHR45640; PTHR45640; 1.
DR   Pfam; PF00011; HSP20; 1.
DR   PRINTS; PR00299; ACRYSTALLIN.
DR   SUPFAM; SSF49764; SSF49764; 1.
DR   PROSITE; PS01031; SHSP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chaperone; Charcot-Marie-Tooth disease;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease variant;
KW   Host-virus interaction; Methylation; Neurodegeneration; Neuropathy;
KW   Nucleus; Phosphoprotein; Reference proteome; Stress response.
FT   CHAIN           1..205
FT                   /note="Heat shock protein beta-1"
FT                   /id="PRO_0000125927"
FT   DOMAIN          76..184
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT   REGION          70..205
FT                   /note="Interaction with TGFB1I1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         12
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000244|PubMed:24129315"
FT   MOD_RES         15
FT                   /note="Phosphoserine; by MAPKAPK2 and MAPKAPK3"
FT                   /evidence="ECO:0000244|PubMed:17081983,
FT                   ECO:0000244|PubMed:18088087, ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163,
FT                   ECO:0000244|PubMed:24275569, ECO:0000269|PubMed:10383393,
FT                   ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:8774846"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42930"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:17081983,
FT                   ECO:0000244|PubMed:20068231"
FT   MOD_RES         78
FT                   /note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569,
FT                   ECO:0000269|PubMed:10383393, ECO:0000269|PubMed:1332886,
FT                   ECO:0000269|PubMed:15976317, ECO:0000269|PubMed:1730670,
FT                   ECO:0000269|PubMed:19166925, ECO:0000269|PubMed:8774846"
FT   MOD_RES         82
FT                   /note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5"
FT                   /evidence="ECO:0000244|PubMed:16964243,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569,
FT                   ECO:0000269|PubMed:10383393, ECO:0000269|PubMed:1332886,
FT                   ECO:0000269|PubMed:15976317, ECO:0000269|PubMed:1730670,
FT                   ECO:0000269|PubMed:19166925, ECO:0000269|PubMed:8774846,
FT                   ECO:0000269|Ref.14"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:16964243"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163,
FT                   ECO:0000244|PubMed:24275569"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         123
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         174
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         176
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569"
FT   VARIANT         7
FT                   /note="P -> S (in HMN2B; induces hyperphosphorylation of
FT                   neurofilaments; no effect on cytoplasmic location; no
FT                   effect on dimerization; dbSNP:rs1563651698)"
FT                   /evidence="ECO:0000269|PubMed:28144995"
FT                   /id="VAR_078128"
FT   VARIANT         34
FT                   /note="G -> R (in HMN2B; increased aggregation; increased
FT                   homooligomerization; changed function in chaperone-mediated
FT                   protein folding; dbSNP:rs1554614432)"
FT                   /evidence="ECO:0000269|PubMed:22176143,
FT                   ECO:0000269|PubMed:25965061"
FT                   /id="VAR_077483"
FT   VARIANT         39
FT                   /note="P -> L (in HMN2B and CMT2F; increased aggregation;
FT                   increased homooligomerization; decreased phosphorylation by
FT                   MAPKAPK2; changed function in chaperone-mediated protein
FT                   folding; dbSNP:rs557327165)"
FT                   /evidence="ECO:0000269|PubMed:18832141,
FT                   ECO:0000269|PubMed:22176143, ECO:0000269|PubMed:25965061,
FT                   ECO:0000269|PubMed:28144995"
FT                   /id="VAR_077484"
FT   VARIANT         41
FT                   /note="E -> K (in HMN2B; increased aggregation; increased
FT                   homooligomerization; changed function in chaperone-mediated
FT                   protein folding; dbSNP:rs1393404971)"
FT                   /evidence="ECO:0000269|PubMed:22176143,
FT                   ECO:0000269|PubMed:25965061"
FT                   /id="VAR_077485"
FT   VARIANT         53
FT                   /note="G -> D (in HMN2B; no effect on dimerization; no
FT                   effect on cytoplasmic location; no effect on dimerization;
FT                   dbSNP:rs375244209)"
FT                   /evidence="ECO:0000269|PubMed:28144995"
FT                   /id="VAR_078129"
FT   VARIANT         84
FT                   /note="G -> R (in HMN2B; decreased homooligomerization;
FT                   decreased heterooligomerization with HSPB6; no effect on
FT                   phosphorylation by MAPKAPK2; decreased function in
FT                   chaperone-mediated protein folding; dbSNP:rs770272088)"
FT                   /evidence="ECO:0000269|PubMed:18832141,
FT                   ECO:0000269|PubMed:23948568"
FT                   /id="VAR_077486"
FT   VARIANT         99
FT                   /note="L -> M (in HMN2B; decreased homooligomerization;
FT                   decreased heterooligomerization with HSPB6; no effect on
FT                   phosphorylation by MAPKAPK2; decreased function in
FT                   chaperone-mediated protein folding; dbSNP:rs121909113)"
FT                   /evidence="ECO:0000269|PubMed:18832141,
FT                   ECO:0000269|PubMed:23948568"
FT                   /id="VAR_077487"
FT   VARIANT         127
FT                   /note="R -> W (in HMN2B; decreased homodimerization;
FT                   increased client proteins binding; increased function in
FT                   chaperone-mediated protein folding; alters CDK5-mediated
FT                   phosphorylation of neurofilament proteins and indirectly
FT                   impairs their anterograde axonal transport;
FT                   dbSNP:rs29001571)"
FT                   /evidence="ECO:0000269|PubMed:15122254,
FT                   ECO:0000269|PubMed:20178975, ECO:0000269|PubMed:23728742,
FT                   ECO:0000269|PubMed:28144995"
FT                   /id="VAR_018506"
FT   VARIANT         128
FT                   /note="Q -> R (in HMN2B; unknown pathological significance;
FT                   no effect on dimerization; no effect on cytoplasmic
FT                   location; no effect on dimerization; dbSNP:rs558882005)"
FT                   /evidence="ECO:0000269|PubMed:28144995"
FT                   /id="VAR_078130"
FT   VARIANT         135
FT                   /note="S -> F (in CMT2F and HMN2B; decreased
FT                   homodimerization; increased client proteins binding;
FT                   increased function in chaperone-mediated protein folding;
FT                   alters CDK5-mediated phosphorylation of neurofilament
FT                   proteins; alters CDK5-mediated phosphorylation of
FT                   neurofilament proteins and indirectly impairs their
FT                   anterograde axonal transport; dbSNP:rs28939680)"
FT                   /evidence="ECO:0000269|PubMed:15122254,
FT                   ECO:0000269|PubMed:18832141, ECO:0000269|PubMed:20178975,
FT                   ECO:0000269|PubMed:23728742"
FT                   /id="VAR_018507"
FT   VARIANT         136
FT                   /note="R -> L (in CMT2F and HMN2B; dbSNP:rs863225022)"
FT                   /evidence="ECO:0000269|PubMed:22176143"
FT                   /id="VAR_077488"
FT   VARIANT         136
FT                   /note="R -> W (in CMT2F; decreased homodimerization only
FT                   with the wild-type protein; increased client proteins
FT                   binding; increased function in chaperone-mediated protein
FT                   folding; dbSNP:rs28939681)"
FT                   /evidence="ECO:0000269|PubMed:15122254,
FT                   ECO:0000269|PubMed:20178975"
FT                   /id="VAR_018508"
FT   VARIANT         140
FT                   /note="R -> G (in HMN2B; decreased thermal stability;
FT                   changed protein structure; changed homooligomerization;
FT                   loss of heterooligomerization with HSPB6; decreased
FT                   function in chaperone-mediated protein folding;
FT                   dbSNP:rs121909112)"
FT                   /evidence="ECO:0000269|PubMed:18832141,
FT                   ECO:0000269|PubMed:23643870"
FT                   /id="VAR_077489"
FT   VARIANT         141
FT                   /note="K -> Q (in HMN2B; decreased thermal stability;
FT                   changed protein structure; no effect on
FT                   homooligomerization; changed heterooligomerization with
FT                   HSPB6; slightly decreased function in chaperone-mediated
FT                   protein folding; dbSNP:rs1554614650)"
FT                   /evidence="ECO:0000269|PubMed:18952241,
FT                   ECO:0000269|PubMed:23643870"
FT                   /id="VAR_077490"
FT   VARIANT         151
FT                   /note="T -> I (in HMN2B; no effect on homodimerization; no
FT                   effect on client proteins binding; no effect on function in
FT                   chaperone-mediated protein folding; dbSNP:rs28937568)"
FT                   /evidence="ECO:0000269|PubMed:15122254,
FT                   ECO:0000269|PubMed:20178975, ECO:0000269|PubMed:28144995"
FT                   /id="VAR_018509"
FT   VARIANT         156
FT                   /note="S -> Y (no effect on oligomerization; no effect on
FT                   client proteins binding; no effect on function in
FT                   chaperone-mediated protein folding; dbSNP:rs374995963)"
FT                   /evidence="ECO:0000269|PubMed:20178975"
FT                   /id="VAR_077491"
FT   VARIANT         164
FT                   /note="T -> A (in CMT2F; dbSNP:rs1032400275)"
FT                   /evidence="ECO:0000269|PubMed:22206013"
FT                   /id="VAR_067085"
FT   VARIANT         175..205
FT                   /note="Missing (in HMN2B)"
FT                   /evidence="ECO:0000269|PubMed:28144995"
FT                   /id="VAR_078131"
FT   VARIANT         180
FT                   /note="T -> I (in HMN2B; unknown pathological significance;
FT                   dbSNP:rs1422978230)"
FT                   /evidence="ECO:0000269|PubMed:20870250,
FT                   ECO:0000269|PubMed:22176143, ECO:0000269|PubMed:28144995"
FT                   /id="VAR_077492"
FT   VARIANT         182
FT                   /note="P -> L (in HMN2B; decreased protein abundance; no
FT                   effect on oligomerization; increased client proteins
FT                   binding; no effect on function in chaperone-mediated
FT                   protein folding; alters CDK5-mediated phosphorylation of
FT                   neurofilament proteins; indirectly impairs their
FT                   anterograde axonal transport; dbSNP:rs28937569)"
FT                   /evidence="ECO:0000269|PubMed:15122254,
FT                   ECO:0000269|PubMed:20178975, ECO:0000269|PubMed:23728742"
FT                   /id="VAR_018510"
FT   VARIANT         187
FT                   /note="S -> L (in HMN2B; formation of large cytoplasmic
FT                   aggregates; no effect on dimerization; dbSNP:rs774585320)"
FT                   /evidence="ECO:0000269|PubMed:28144995"
FT                   /id="VAR_078132"
FT   VARIANT         188
FT                   /note="R -> W (in CMT2F; unknown pathological significance;
FT                   dbSNP:rs772767500)"
FT                   /evidence="ECO:0000269|PubMed:22176143"
FT                   /id="VAR_077493"
FT   VARIANT         190
FT                   /note="Q -> H (found in a patient with sporadic amyotrophic
FT                   lateral sclerosis; unknown pathological significance;
FT                   dbSNP:rs764297134)"
FT                   /evidence="ECO:0000269|PubMed:27492805"
FT                   /id="VAR_077494"
FT   MUTAGEN         15
FT                   /note="S->D: Mimicks phosphorylation state, leading to
FT                   dreased ability to act as molecular chaperones; when
FT                   associated with D-78 and D-82."
FT                   /evidence="ECO:0000269|PubMed:10383393"
FT   MUTAGEN         78
FT                   /note="S->D: Mimicks phosphorylation state, leading to
FT                   dreased ability to act as molecular chaperones; when
FT                   associated with D-15 and D-82."
FT                   /evidence="ECO:0000269|PubMed:10383393"
FT   MUTAGEN         82
FT                   /note="S->D: Mimicks phosphorylation state, leading to
FT                   dreased ability to act as molecular chaperones; when
FT                   associated with D-15 and D-78."
FT                   /evidence="ECO:0000269|PubMed:10383393"
FT   CONFLICT        10
FT                   /note="L -> I (in Ref. 13; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        109
FT                   /note="L -> R (in Ref. 12; AAH12292)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="T -> S (in Ref. 12; AAH12292)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="R -> L (in Ref. 12; AAH12292)"
FT                   /evidence="ECO:0000305"
FT   STRAND          86..88
FT                   /evidence="ECO:0000244|PDB:4MJH"
FT   STRAND          94..100
FT                   /evidence="ECO:0000244|PDB:3Q9P"
FT   TURN            102..104
FT                   /evidence="ECO:0000244|PDB:3Q9P"
FT   STRAND          107..114
FT                   /evidence="ECO:0000244|PDB:3Q9P"
FT   STRAND          117..124
FT                   /evidence="ECO:0000244|PDB:3Q9P"
FT   STRAND          136..143
FT                   /evidence="ECO:0000244|PDB:3Q9P"
FT   TURN            145..147
FT                   /evidence="ECO:0000244|PDB:2N3J"
FT   HELIX           150..152
FT                   /evidence="ECO:0000244|PDB:3Q9P"
FT   STRAND          154..157
FT                   /evidence="ECO:0000244|PDB:3Q9P"
FT   STRAND          161..168
FT                   /evidence="ECO:0000244|PDB:3Q9P"
SQ   SEQUENCE   205 AA;  22783 MW;  1B4DC44A6F6606D5 CRC64;
     MTERRVPFSL LRGPSWDPFR DWYPHSRLFD QAFGLPRLPE EWSQWLGGSS WPGYVRPLPP
     AAIESPAVAA PAYSRALSRQ LSSGVSEIRH TADRWRVSLD VNHFAPDELT VKTKDGVVEI
     TGKHEERQDE HGYISRCFTR KYTLPPGVDP TQVSSSLSPE GTLTVEAPMP KLATQSNEIT
     IPVTFESRAQ LGGPEAAKSD ETAAK
//
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