HSPB1_HUMAN
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 03-AUG-2022, entry version 248.
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; DOI=10.1016/s0021-9258(18)82451-6;
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; DOI=10.1016/s0021-9258(18)42574-4;
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; DOI=10.1016/s0021-9258(18)48354-8;
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; DOI=10.1016/s0021-9258(18)53882-5;
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; 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; 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; P02489: CRYAA; NbExp=4; IntAct=EBI-352682, EBI-6875961;
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; 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; Q6ZR37: PLEKHG7; NbExp=3; IntAct=EBI-352682, EBI-12891828;
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 AlphaFoldDB; P04792; -.
DR SMR; P04792; -.
DR BioGRID; 109547; 628.
DR DIP; DIP-412N; -.
DR IntAct; P04792; 586.
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 GlyGen; P04792; 5 sites, 1 O-linked glycan (5 sites).
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; 3223 antibodies from 54 providers.
DR CPTC; P04792; 6 antibodies.
DR DNASU; 3315; -.
DR Ensembl; ENST00000248553.7; ENSP00000248553.6; ENSG00000106211.10.
DR GeneID; 3315; -.
DR KEGG; hsa:3315; -.
DR MANE-Select; ENST00000248553.7; ENSP00000248553.6; NM_001540.5; NP_001531.1.
DR CTD; 3315; -.
DR DisGeNET; 3315; -.
DR GeneCards; HSPB1; -.
DR GeneReviews; HSPB1; -.
DR HGNC; HGNC:5246; HSPB1.
DR HPA; ENSG00000106211; Tissue enhanced (esophagus).
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; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000155882; -.
DR HOGENOM; CLU_095001_0_0_1; -.
DR InParanoid; P04792; -.
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 SignaLink; P04792; -.
DR SIGNOR; P04792; -.
DR BioGRID-ORCS; 3315; 12 hits in 1080 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 lower esophagus mucosa and 205 other tissues.
DR ExpressionAtlas; P04792; baseline and differential.
DR Genevisible; P04792; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0001533; C:cornified envelope; IEA:Ensembl.
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:0030018; C:Z disc; IEA:Ensembl.
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:0051082; F:unfolded protein binding; IBA:GO_Central.
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:0042026; P:protein refolding; IBA:GO_Central.
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:0001932; P:regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0006446; P:regulation of translational initiation; TAS:ProtInc.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
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 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:0007744|PubMed:24129315"
FT MOD_RES 15
FT /note="Phosphoserine; by MAPKAPK2 and MAPKAPK3"
FT /evidence="ECO:0000269|PubMed:10383393,
FT ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:8774846,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42930"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 78
FT /note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5"
FT /evidence="ECO:0000269|PubMed:10383393,
FT ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:15976317,
FT ECO:0000269|PubMed:1730670, ECO:0000269|PubMed:19166925,
FT ECO:0000269|PubMed:8774846, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 82
FT /note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5"
FT /evidence="ECO:0000269|PubMed:10383393,
FT ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:15976317,
FT ECO:0000269|PubMed:1730670, ECO:0000269|PubMed:19166925,
FT ECO:0000269|PubMed:8774846, ECO:0000269|Ref.14,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 174
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|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:0007829|PDB:4MJH"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:3Q9P"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3Q9P"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:3Q9P"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:3Q9P"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:3Q9P"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:2N3J"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:3Q9P"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:3Q9P"
FT STRAND 161..168
FT /evidence="ECO:0007829|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
