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Heat shock protein beta-1 (HspB1) (28 kDa heat shock protein) (Estrogen-regulated 24 kDa protein) (Heat shock 27 kDa protein) (HSP 27) (Stress-responsive protein 27) (SRP27)

 HSPB1_HUMAN             Reviewed;         205 AA.
P04792; B2R4N8; Q6FI47; Q96C20; Q96EI7; Q9UC31; Q9UC34; Q9UC35; Q9UC36;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
26-SEP-2001, sequence version 2.
02-JUN-2021, entry version 244.
RecName: Full=Heat shock protein beta-1;
Short=HspB1;
AltName: Full=28 kDa heat shock protein;
AltName: Full=Estrogen-regulated 24 kDa protein;
AltName: Full=Heat shock 27 kDa protein;
Short=HSP 27;
AltName: Full=Stress-responsive protein 27;
Short=SRP27;
Name=HSPB1; Synonyms=HSP27, HSP28;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3714473; DOI=10.1093/nar/14.10.4127;
Hickey E., Brandon S.E., Potter R., Stein G., Stein J., Weber L.A.;
"Sequence and organization of genes encoding the human 27 kDa heat shock
protein.";
Nucleic Acids Res. 14:4127-4145(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=2243808; DOI=10.1093/nar/18.21.6457;
Carper S.W., Rocheleau T.A., Storm F.K.;
"cDNA sequence of a human heat shock protein HSP27.";
Nucleic Acids Res. 18:6457-6457(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND SUBUNIT.
TISSUE=Cervix carcinoma;
PubMed=10777697; DOI=10.1006/bbrc.2000.2553;
Hino M., Kurogi K., Okubo M.-A., Murata-Hori M., Hosoya H.;
"Small heat shock protein 27 (HSP27) associates with tubulin/microtubules
in HeLa cells.";
Biochem. Biophys. Res. Commun. 271:164-169(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary carcinoma;
Briolay J., Chareyron P., Mehlen P., Arrigo A.;
"Identification of a new cDNA sequence from human breast carcinoma cells
encoding the 28kDa heat shock protein.";
Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=9110174; DOI=10.1101/gr.7.4.353;
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
"Large-scale concatenation cDNA sequencing.";
Genome Res. 7:353-358(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, Ovary, Pancreas, Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
PROTEIN SEQUENCE OF 5-12; 97-112; 141-154 AND 172-188.
PubMed=2295696; DOI=10.1172/jci114413;
Strahler J.R., Kuick R., Eckerskorn C., Lottspeich F., Richardson B.C.,
Fox D.A., Stoolman L.M., Hanson C.A., Nichols D., Tueche H.J., Hanash S.M.;
"Identification of two related markers for common acute lymphoblastic
leukemia as heat shock proteins.";
J. Clin. Invest. 85:200-207(1990).
[14]
PROTEIN SEQUENCE OF 6-37; 57-75; 80-89; 97-127 AND 141-188, PHOSPHORYLATION
AT SER-82, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[15]
PROTEIN SEQUENCE OF 13-20; 38-46; 97-110; 141-154 AND 172-186,
PHOSPHORYLATION, AND INDUCTION BY HEAT SHOCK.
TISSUE=Mammary carcinoma;
PubMed=8325890;
Faucher C., Capdevielle J., Canal I., Ferrara P., Mazarguil H.,
McGuire W.L., Darbon J.-M.;
"The 28-kDa protein whose phosphorylation is induced by protein kinase C
activators in MCF-7 cells belongs to the family of low molecular mass heat
shock proteins and is the estrogen-regulated 24-kDa protein.";
J. Biol. Chem. 268:15168-15173(1993).
[16]
PROTEIN SEQUENCE OF 21-59; 93-98; 129-134 AND 178-193, INTERACTION WITH
CRYAB, AND TISSUE SPECIFICITY.
TISSUE=Pectoralis muscle;
PubMed=1560006;
Kato K., Shinohara H., Goto S., Inaguma Y., Morishita R., Asano T.;
"Copurification of small heat shock protein with alpha B crystallin from
human skeletal muscle.";
J. Biol. Chem. 267:7718-7725(1992).
[17]
PROTEIN SEQUENCE OF 76-89, AND PHOSPHORYLATION AT SER-78 AND SER-82.
PubMed=1730670;
Landry J., Lambert H., Zhou M., Lavoie J.N., Hickey E., Weber L.A.,
Anderson C.W.;
"Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and
mitogen-activated kinases that recognize the same amino acid motif as S6
kinase II.";
J. Biol. Chem. 267:794-803(1992).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 109-205, AND INDUCTION BY ESTROGEN.
TISSUE=Mammary carcinoma;
PubMed=2743305;
Fuqua S.A.W., Blum-Salingaros M., McGuire W.L.;
"Induction of the estrogen-regulated '24K' protein by heat shock.";
Cancer Res. 49:4126-4129(1989).
[19]
NUCLEOTIDE SEQUENCE [MRNA] OF 122-205.
PubMed=1763035; DOI=10.1073/pnas.88.24.11212;
Mendelsohn M.E., Zhu Y., O'Neill S.;
"The 29-kDa proteins phosphorylated in thrombin-activated human platelets
are forms of the estrogen receptor-related 27-kDa heat shock protein.";
Proc. Natl. Acad. Sci. U.S.A. 88:11212-11216(1991).
[20]
PHOSPHORYLATION AT SER-15; SER-78 AND SER-82 BY MAPKAPK2.
PubMed=1332886; DOI=10.1016/0014-5793(92)81216-9;
Stokoe D., Engel K., Campbell D.G., Cohen P., Gaestel M.;
"Identification of MAPKAP kinase 2 as a major enzyme responsible for the
phosphorylation of the small mammalian heat shock proteins.";
FEBS Lett. 313:307-313(1992).
[21]
PHOSPHORYLATION BY MAPKAPK2.
PubMed=8093612;
Jakob U., Gaestel M., Engel K., Buchner J.;
"Small heat shock proteins are molecular chaperones.";
J. Biol. Chem. 268:1517-1520(1993).
[22]
PHOSPHORYLATION AT SER-15; SER-78 AND SER-82.
PubMed=8774846; DOI=10.1016/0014-5793(96)00816-2;
Clifton A.D., Young P.R., Cohen P.;
"A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP
kinase-3 and their activation by cytokines and cellular stress.";
FEBS Lett. 392:209-214(1996).
[23]
FUNCTION, SUBUNIT, PHOSPHORYLATION AT SER-15; SER-78 AND SER-82, AND
MUTAGENESIS OF SER-15; SER-78 AND SER-82.
PubMed=10383393; DOI=10.1074/jbc.274.27.18947;
Rogalla T., Ehrnsperger M., Preville X., Kotlyarov A., Lutsch G.,
Ducasse C., Paul C., Wieske M., Arrigo A.P., Buchner J., Gaestel M.;
"Regulation of Hsp27 oligomerization, chaperone function, and protective
activity against oxidative stress/tumor necrosis factor alpha by
phosphorylation.";
J. Biol. Chem. 274:18947-18956(1999).
[24]
INTERACTION WITH HSPBAP1.
PubMed=10751411; DOI=10.1074/jbc.m001981200;
Liu C., Gilmont R.R., Benndorf R., Welsh M.J.;
"Identification and characterization of a novel protein from Sertoli cells,
PASS1, that associates with mammalian small stress protein hsp27.";
J. Biol. Chem. 275:18724-18731(2000).
[25]
INTERACTION WITH HSPB8.
PubMed=11342557; DOI=10.1074/jbc.m103001200;
Benndorf R., Sun X., Gilmont R.R., Biederman K.J., Molloy M.P.,
Goodmurphy C.W., Cheng H., Andrews P.C., Welsh M.J.;
"HSP22, a new member of the small heat shock protein superfamily, interacts
with mimic of phosphorylated HSP27 (3DHSP27).";
J. Biol. Chem. 276:26753-26761(2001).
[26]
PHOSPHORYLATION AT SER-78 AND SER-82, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=15976317; DOI=10.1161/01.res.0000174815.10996.08;
De Souza A.I., Wait R., Mitchell A.G., Banner N.R., Dunn M.J., Rose M.L.;
"Heat shock protein 27 is associated with freedom from graft vasculopathy
after human cardiac transplantation.";
Circ. Res. 97:192-198(2005).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-65, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[28]
INDUCTION (MICROBIAL INFECTION), AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
Leong W.F., Chow V.T.;
"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal
differential cellular gene expression in response to enterovirus 71
infection.";
Cell. Microbiol. 8:565-580(2006).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-83, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation
analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
and high confident phosphopeptide identification by cross-validation of
MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-199, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-199, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[34]
SUBCELLULAR LOCATION.
PubMed=19464326; DOI=10.1016/j.bbamcr.2009.05.005;
Vos M.J., Kanon B., Kampinga H.H.;
"HSPB7 is a SC35 speckle resident small heat shock protein.";
Biochim. Biophys. Acta 1793:1343-1353(2009).
[35]
FUNCTION, AND PHOSPHORYLATION AT SER-78 AND SER-82.
PubMed=19166925; DOI=10.1016/j.cellsig.2009.01.009;
Kostenko S., Johannessen M., Moens U.;
"PKA-induced F-actin rearrangement requires phosphorylation of Hsp27 by the
MAPKAP kinase MK5.";
Cell. Signal. 21:712-718(2009).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[37]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-65; SER-78; SER-82
AND SER-199, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-78; SER-82; SER-86;
THR-174; SER-176 AND SER-199, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-78; SER-82; SER-86;
SER-98 AND SER-199, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[43]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-12, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[44]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[45]
VARIANTS CMT2F PHE-135 AND TRP-136, AND VARIANTS HMN2B TRP-127; PHE-135;
ILE-151 AND LEU-182.
PubMed=15122254; DOI=10.1038/ng1354;
Evgrafov O.V., Mersiyanova I., Irobi J., Van Den Bosch L., Dierick I.,
Leung C.L., Schagina O., Verpoorten N., Van Impe K., Fedotov V., Dadali E.,
Auer-Grumbach M., Windpassinger C., Wagner K., Mitrovic Z.,
Hilton-Jones D., Talbot K., Martin J.-J., Vasserman N., Tverskaya S.,
Polyakov A., Liem R.K.H., Gettemans J., Robberecht W., De Jonghe P.,
Timmerman V.;
"Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth
disease and distal hereditary motor neuropathy.";
Nat. Genet. 36:602-606(2004).
[46]
VARIANTS HMN2B LEU-39; ARG-84; MET-99; PHE-135 AND GLY-140.
PubMed=18832141; DOI=10.1212/01.wnl.0000319696.14225.67;
Houlden H., Laura M., Wavrant-De Vrieze F., Blake J., Wood N., Reilly M.M.;
"Mutations in the HSP27 (HSPB1) gene cause dominant, recessive, and
sporadic distal HMN/CMT type 2.";
Neurology 71:1660-1668(2008).
[47]
VARIANT HMN2B GLN-141.
PubMed=18952241; DOI=10.1016/j.jns.2008.09.031;
Ikeda Y., Abe A., Ishida C., Takahashi K., Hayasaka K., Yamada M.;
"A clinical phenotype of distal hereditary motor neuronopathy type II with
a novel HSPB1 mutation.";
J. Neurol. Sci. 277:9-12(2009).
[48]
VARIANT TYR-156, CHARACTERIZATION OF VARIANT TYR-156, CHARACTERIZATION OF
VARIANTS HMN2B TRP-127; PHE-135; ILE-151 AND LEU-182, CHARACTERIZATION OF
VARIANT CMT2F TRP-136, FUNCTION, AND SUBUNIT.
PubMed=20178975; DOI=10.1074/jbc.m109.082644;
Almeida-Souza L., Goethals S., de Winter V., Dierick I., Gallardo R.,
Van Durme J., Irobi J., Gettemans J., Rousseau F., Schymkowitz J.,
Timmerman V., Janssens S.;
"Increased monomerization of mutant HSPB1 leads to protein hyperactivity in
Charcot-Marie-Tooth neuropathy.";
J. Biol. Chem. 285:12778-12786(2010).
[49]
VARIANT HMN2B ILE-180.
PubMed=20870250; DOI=10.1016/j.jns.2010.09.008;
Luigetti M., Fabrizi G.M., Madia F., Ferrarini M., Conte A., Del Grande A.,
Tasca G., Tonali P.A., Sabatelli M.;
"A novel HSPB1 mutation in an Italian patient with CMT2/dHMN phenotype.";
J. Neurol. Sci. 298:114-117(2010).
[50]
VARIANTS HMN2B ARG-34; LYS-41; LEU-136 AND ILE-180, AND VARIANTS CMT2F
LEU-39; LEU-136 AND TRP-188.
PubMed=22176143; DOI=10.1111/j.1529-8027.2011.00361.x;
Capponi S., Geroldi A., Fossa P., Grandis M., Ciotti P., Gulli R.,
Schenone A., Mandich P., Bellone E.;
"HSPB1 and HSPB8 in inherited neuropathies: study of an Italian cohort of
dHMN and CMT2 patients.";
J. Peripher. Nerv. Syst. 16:287-294(2011).
[51]
VARIANT CMT2F ALA-164.
PubMed=22206013; DOI=10.1371/journal.pone.0029393;
Lin K.P., Soong B.W., Yang C.C., Huang L.W., Chang M.H., Lee I.H.,
Antonellis A., Lee Y.C.;
"The mutational spectrum in a cohort of Charcot-Marie-Tooth disease type 2
among the Han Chinese in Taiwan.";
PLoS ONE 6:E29393-E29393(2011).
[52]
FUNCTION, CHARACTERIZATION OF VARIANTS HMN2B TRP-127 AND LEU-182, AND
CHARACTERIZATION OF VARIANT CMT2F PHE-135.
PubMed=23728742; DOI=10.1007/s00401-013-1133-6;
Holmgren A., Bouhy D., De Winter V., Asselbergh B., Timmermans J.P.,
Irobi J., Timmerman V.;
"Charcot-Marie-Tooth causing HSPB1 mutations increase Cdk5-mediated
phosphorylation of neurofilaments.";
Acta Neuropathol. 126:93-108(2013).
[53]
CHARACTERIZATION OF VARIANTS HMN2B ARG-84 AND MET-99, AND INTERACTION WITH
HSPB6.
PubMed=23948568; DOI=10.1016/j.abb.2013.07.028;
Nefedova V.V., Sudnitsyna M.V., Strelkov S.V., Gusev N.B.;
"Structure and properties of G84R and L99M mutants of human small heat
shock protein HspB1 correlating with motor neuropathy.";
Arch. Biochem. Biophys. 538:16-24(2013).
[54]
CHARACTERIZATION OF VARIANTS HMN2B GLY-140 AND GLN-141.
PubMed=23643870; DOI=10.1016/j.biochi.2013.04.014;
Nefedova V.V., Datskevich P.N., Sudnitsyna M.V., Strelkov S.V., Gusev N.B.;
"Physico-chemical properties of R140G and K141Q mutants of human small heat
shock protein HspB1 associated with hereditary peripheral neuropathies.";
Biochimie 95:1582-1592(2013).
[55]
CHARACTERIZATION OF VARIANTS HMN2B ARG-34; LEU-39 AND LYS-41.
PubMed=25965061; DOI=10.1371/journal.pone.0126248;
Muranova L.K., Weeks S.D., Strelkov S.V., Gusev N.B.;
"Characterization of mutants of human small heat shock protein HspB1
carrying replacements in the n-terminal domain and associated with
hereditary motor neuron diseases.";
PLoS ONE 10:E0126248-E0126248(2015).
[56]
VARIANT HIS-190.
PubMed=27492805; DOI=10.1002/humu.23062;
Capponi S., Geuens T., Geroldi A., Origone P., Verdiani S., Cichero E.,
Adriaenssens E., De Winter V., Bandettini di Poggio M., Barberis M.,
Chio A., Fossa P., Mandich P., Bellone E., Timmerman V.;
"Molecular chaperones in the pathogenesis of amyotrophic lateral sclerosis:
the role of HSPB1.";
Hum. Mutat. 37:1202-1208(2016).
[57]
VARIANTS HMN2B SER-7; LEU-39; ASP-53; TRP-127; ARG-128; ILE-151;
175-GLN--LYS-205 DEL; ILE-180 AND LEU-187, SUBCELLULAR LOCATION, AND
CHARACTERIZATION OF VARIANTS HMN2B SER-7; ASP-53; ARG-128 AND LEU-187.
PubMed=28144995; DOI=10.1002/humu.23189;
Echaniz-Laguna A., Geuens T., Petiot P., Pereon Y., Adriaenssens E.,
Haidar M., Capponi S., Maisonobe T., Fournier E., Dubourg O., Degos B.,
Salachas F., Lenglet T., Eymard B., Delmont E., Pouget J.,
Juntas Morales R., Goizet C., Latour P., Timmerman V., Stojkovic T.;
"Axonal Neuropathies due to Mutations in Small Heat Shock Proteins:
Clinical, Genetic, and Functional Insights into Novel Mutations.";
Hum. Mutat. 38:556-568(2017).
-!- FUNCTION: Small heat shock protein which functions as a molecular
chaperone probably maintaining denatured proteins in a folding-
competent state (PubMed:10383393, PubMed:20178975). Plays a role in
stress resistance and actin organization (PubMed:19166925). Through its
molecular chaperone activity may regulate numerous biological processes
including the phosphorylation and the axonal transport of neurofilament
proteins (PubMed:23728742). {ECO:0000269|PubMed:10383393,
ECO:0000269|PubMed:19166925, ECO:0000269|PubMed:20178975,
ECO:0000269|PubMed:23728742}.
-!- SUBUNIT: Homooligomer (PubMed:10383393). Homodimer; becomes monomeric
upon activation (PubMed:20178975). Heterooligomer; with HSPB6
(PubMed:23948568). Associates with alpha- and beta-tubulin
(PubMed:10777697). Interacts with TGFB1I1 (By similarity). Interacts
with CRYAB (PubMed:1560006). Interacts with HSPB8 (PubMed:11342557).
Interacts with HSPBAP1 (PubMed:10751411).
{ECO:0000250|UniProtKB:P42930, ECO:0000269|PubMed:10383393,
ECO:0000269|PubMed:10751411, ECO:0000269|PubMed:10777697,
ECO:0000269|PubMed:11342557, ECO:0000269|PubMed:1560006,
ECO:0000269|PubMed:20178975, ECO:0000269|PubMed:23948568}.
-!- INTERACTION:
P04792; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-352682, EBI-10173507;
P04792; Q6ZTN6-2: ANKRD13D; NbExp=3; IntAct=EBI-352682, EBI-25840993;
P04792; Q8N8A2-2: ANKRD44; NbExp=3; IntAct=EBI-352682, EBI-21636328;
P04792; Q92688: ANP32B; NbExp=3; IntAct=EBI-352682, EBI-762428;
P04792; P08758: ANXA5; NbExp=3; IntAct=EBI-352682, EBI-296601;
P04792; P13928: ANXA8; NbExp=3; IntAct=EBI-352682, EBI-2556915;
P04792; D3DTF8: APLN; NbExp=3; IntAct=EBI-352682, EBI-22002556;
P04792; P05067: APP; NbExp=3; IntAct=EBI-352682, EBI-77613;
P04792; O94778: AQP8; NbExp=3; IntAct=EBI-352682, EBI-19124986;
P04792; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-352682, EBI-2875816;
P04792; Q86TN1: ARNT2; NbExp=3; IntAct=EBI-352682, EBI-25844820;
P04792; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-352682, EBI-14199987;
P04792; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-352682, EBI-10254793;
P04792; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-352682, EBI-9089489;
P04792; P15313: ATP6V1B1; NbExp=3; IntAct=EBI-352682, EBI-2891281;
P04792; O95817: BAG3; NbExp=7; IntAct=EBI-352682, EBI-747185;
P04792; P46379-2: BAG6; NbExp=3; IntAct=EBI-352682, EBI-10988864;
P04792; Q16611: BAK1; NbExp=3; IntAct=EBI-352682, EBI-519866;
P04792; Q14457: BECN1; NbExp=3; IntAct=EBI-352682, EBI-949378;
P04792; Q96LC9: BMF; NbExp=3; IntAct=EBI-352682, EBI-3919268;
P04792; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-352682, EBI-10693038;
P04792; Q9H0W9-4: C11orf54; NbExp=3; IntAct=EBI-352682, EBI-25849710;
P04792; Q32Q52: C12orf74; NbExp=3; IntAct=EBI-352682, EBI-12891828;
P04792; Q96LL4: C8orf48; NbExp=3; IntAct=EBI-352682, EBI-751596;
P04792; P27797: CALR; NbExp=2; IntAct=EBI-352682, EBI-1049597;
P04792; Q8N5S9-2: CAMKK1; NbExp=3; IntAct=EBI-352682, EBI-25850646;
P04792; Q9HC96: CAPN10; NbExp=3; IntAct=EBI-352682, EBI-3915761;
P04792; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-352682, EBI-10181422;
P04792; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-352682, EBI-744045;
P04792; Q96DZ5: CLIP3; NbExp=3; IntAct=EBI-352682, EBI-12823145;
P04792; Q6PJW8-3: CNST; NbExp=3; IntAct=EBI-352682, EBI-25836090;
P04792; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-352682, EBI-350590;
P04792; Q9H9Q2: COPS7B; NbExp=3; IntAct=EBI-352682, EBI-2510162;
P04792; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-352682, EBI-2872414;
P04792; A0A140G945: CRYAA2; NbExp=3; IntAct=EBI-352682, EBI-25838900;
P04792; P02511: CRYAB; NbExp=6; IntAct=EBI-352682, EBI-739060;
P04792; P01040: CSTA; NbExp=3; IntAct=EBI-352682, EBI-724303;
P04792; Q9UER7: DAXX; NbExp=4; IntAct=EBI-352682, EBI-77321;
P04792; Q5TAQ9-2: DCAF8; NbExp=3; IntAct=EBI-352682, EBI-25842815;
P04792; O00148: DDX39A; NbExp=3; IntAct=EBI-352682, EBI-348253;
P04792; O00273: DFFA; NbExp=2; IntAct=EBI-352682, EBI-727171;
P04792; Q8NDP9: DKFZp547K2416; NbExp=3; IntAct=EBI-352682, EBI-25842538;
P04792; Q7L591-3: DOK3; NbExp=3; IntAct=EBI-352682, EBI-10694655;
P04792; A0A024RCP2: DOM3Z; NbExp=3; IntAct=EBI-352682, EBI-25847826;
P04792; Q9BPU6: DPYSL5; NbExp=3; IntAct=EBI-352682, EBI-724653;
P04792; Q15029: EFTUD2; NbExp=2; IntAct=EBI-352682, EBI-357897;
P04792; O00303: EIF3F; NbExp=3; IntAct=EBI-352682, EBI-711990;
P04792; Q14240: EIF4A2; NbExp=2; IntAct=EBI-352682, EBI-73473;
P04792; P78344: EIF4G2; NbExp=3; IntAct=EBI-352682, EBI-296519;
P04792; Q6UXG2-3: ELAPOR1; NbExp=3; IntAct=EBI-352682, EBI-12920100;
P04792; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-352682, EBI-10213520;
P04792; Q6P587-2: FAHD1; NbExp=3; IntAct=EBI-352682, EBI-12902289;
P04792; Q6P1L5: FAM117B; NbExp=3; IntAct=EBI-352682, EBI-3893327;
P04792; Q49AJ0-4: FAM135B; NbExp=3; IntAct=EBI-352682, EBI-25835236;
P04792; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-352682, EBI-11793142;
P04792; Q17RN3: FAM98C; NbExp=3; IntAct=EBI-352682, EBI-5461838;
P04792; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-352682, EBI-8468186;
P04792; O15287: FANCG; NbExp=3; IntAct=EBI-352682, EBI-81610;
P04792; Q8TC84: FANK1; NbExp=3; IntAct=EBI-352682, EBI-21975404;
P04792; O00757: FBP2; NbExp=3; IntAct=EBI-352682, EBI-719781;
P04792; Q02790: FKBP4; NbExp=2; IntAct=EBI-352682, EBI-1047444;
P04792; P02794: FTH1; NbExp=2; IntAct=EBI-352682, EBI-713259;
P04792; P11413: G6PD; NbExp=2; IntAct=EBI-352682, EBI-4289891;
P04792; P15976-2: GATA1; NbExp=3; IntAct=EBI-352682, EBI-9090198;
P04792; Q9NXC2: GFOD1; NbExp=3; IntAct=EBI-352682, EBI-8799578;
P04792; Q9HBQ8: GOLGA2P5; NbExp=4; IntAct=EBI-352682, EBI-22000587;
P04792; O95872: GPANK1; NbExp=3; IntAct=EBI-352682, EBI-751540;
P04792; Q7Z602: GPR141; NbExp=3; IntAct=EBI-352682, EBI-21649723;
P04792; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-352682, EBI-347538;
P04792; P78417: GSTO1; NbExp=2; IntAct=EBI-352682, EBI-712083;
P04792; A0A024R1L7: hCG_41307; NbExp=3; IntAct=EBI-352682, EBI-25849938;
P04792; P04792: HSPB1; NbExp=12; IntAct=EBI-352682, EBI-352682;
P04792; Q9UJY1: HSPB8; NbExp=3; IntAct=EBI-352682, EBI-739074;
P04792; Q96EW2-2: HSPBAP1; NbExp=3; IntAct=EBI-352682, EBI-25835621;
P04792; Q7Z6Z7: HUWE1; NbExp=3; IntAct=EBI-352682, EBI-625934;
P04792; P78318: IGBP1; NbExp=3; IntAct=EBI-352682, EBI-1055954;
P04792; Q14005-2: IL16; NbExp=3; IntAct=EBI-352682, EBI-17178971;
P04792; Q9NXX0: ILF3; NbExp=3; IntAct=EBI-352682, EBI-743980;
P04792; Q8NA54: IQUB; NbExp=3; IntAct=EBI-352682, EBI-10220600;
P04792; Q9UKP3-2: ITGB1BP2; NbExp=3; IntAct=EBI-352682, EBI-25856470;
P04792; P0C870: JMJD7; NbExp=3; IntAct=EBI-352682, EBI-9090173;
P04792; Q9NVX7-2: KBTBD4; NbExp=3; IntAct=EBI-352682, EBI-25871195;
P04792; Q8WZ19: KCTD13; NbExp=3; IntAct=EBI-352682, EBI-742916;
P04792; Q96SI1-2: KCTD15; NbExp=3; IntAct=EBI-352682, EBI-12382297;
P04792; Q06136: KDSR; NbExp=3; IntAct=EBI-352682, EBI-3909166;
P04792; Q6ZU52: KIAA0408; NbExp=3; IntAct=EBI-352682, EBI-739493;
P04792; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-352682, EBI-2796400;
P04792; P57682: KLF3; NbExp=3; IntAct=EBI-352682, EBI-8472267;
P04792; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-352682, EBI-714379;
P04792; Q8N1A0: KRT222; NbExp=3; IntAct=EBI-352682, EBI-8473062;
P04792; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-352682, EBI-10241252;
P04792; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-352682, EBI-10241353;
P04792; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-352682, EBI-10261141;
P04792; Q14847-2: LASP1; NbExp=3; IntAct=EBI-352682, EBI-9088686;
P04792; Q96PV6: LENG8; NbExp=3; IntAct=EBI-352682, EBI-739546;
P04792; Q9UPM6: LHX6; NbExp=3; IntAct=EBI-352682, EBI-10258746;
P04792; Q8N448: LNX2; NbExp=3; IntAct=EBI-352682, EBI-2340947;
P04792; A2RU56: LOC401296; NbExp=3; IntAct=EBI-352682, EBI-9088215;
P04792; Q96JB6: LOXL4; NbExp=3; IntAct=EBI-352682, EBI-749562;
P04792; Q14693: LPIN1; NbExp=3; IntAct=EBI-352682, EBI-5278370;
P04792; Q9UDY8-2: MALT1; NbExp=3; IntAct=EBI-352682, EBI-12056869;
P04792; Q99683: MAP3K5; NbExp=3; IntAct=EBI-352682, EBI-476263;
P04792; P49137: MAPKAPK2; NbExp=3; IntAct=EBI-352682, EBI-993299;
P04792; Q16644: MAPKAPK3; NbExp=3; IntAct=EBI-352682, EBI-1384657;
P04792; Q8IW41: MAPKAPK5; NbExp=2; IntAct=EBI-352682, EBI-1201460;
P04792; P61244-4: MAX; NbExp=3; IntAct=EBI-352682, EBI-25848049;
P04792; Q03112-9: MECOM; NbExp=3; IntAct=EBI-352682, EBI-23820194;
P04792; P51608: MECP2; NbExp=3; IntAct=EBI-352682, EBI-1189067;
P04792; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-352682, EBI-8487781;
P04792; Q15049: MLC1; NbExp=3; IntAct=EBI-352682, EBI-8475277;
P04792; A0A0A0MR05: MLST8; NbExp=3; IntAct=EBI-352682, EBI-25835557;
P04792; P08473: MME; NbExp=4; IntAct=EBI-352682, EBI-353759;
P04792; Q8N594: MPND; NbExp=3; IntAct=EBI-352682, EBI-2512452;
P04792; Q99608: NDN; NbExp=3; IntAct=EBI-352682, EBI-718177;
P04792; Q8N5V2: NGEF; NbExp=3; IntAct=EBI-352682, EBI-718372;
P04792; Q8NBF2-2: NHLRC2; NbExp=3; IntAct=EBI-352682, EBI-10697320;
P04792; Q14995: NR1D2; NbExp=3; IntAct=EBI-352682, EBI-6144053;
P04792; P36639-4: NUDT1; NbExp=3; IntAct=EBI-352682, EBI-25834643;
P04792; Q9NZJ9: NUDT4; NbExp=3; IntAct=EBI-352682, EBI-4280066;
P04792; O15381-5: NVL; NbExp=3; IntAct=EBI-352682, EBI-18577082;
P04792; Q5BJF6-2: ODF2; NbExp=3; IntAct=EBI-352682, EBI-9090919;
P04792; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-352682, EBI-1058491;
P04792; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-352682, EBI-25830200;
P04792; Q8N7H5: PAF1; NbExp=2; IntAct=EBI-352682, EBI-2607770;
P04792; Q9BRX2: PELO; NbExp=4; IntAct=EBI-352682, EBI-1043580;
P04792; O15534: PER1; NbExp=3; IntAct=EBI-352682, EBI-2557276;
P04792; Q96FX8: PERP; NbExp=3; IntAct=EBI-352682, EBI-17183069;
P04792; Q96LB9: PGLYRP3; NbExp=3; IntAct=EBI-352682, EBI-12339509;
P04792; Q96G03: PGM2; NbExp=2; IntAct=EBI-352682, EBI-4399372;
P04792; O75925: PIAS1; NbExp=3; IntAct=EBI-352682, EBI-629434;
P04792; Q9UF11-2: PLEKHB1; NbExp=3; IntAct=EBI-352682, EBI-12832742;
P04792; Q58EX7-2: PLEKHG4; NbExp=3; IntAct=EBI-352682, EBI-21503705;
P04792; Q8NA72-3: POC5; NbExp=3; IntAct=EBI-352682, EBI-11751537;
P04792; Q9H1D9: POLR3F; NbExp=3; IntAct=EBI-352682, EBI-710067;
P04792; O43741: PRKAB2; NbExp=3; IntAct=EBI-352682, EBI-1053424;
P04792; P11908: PRPS2; NbExp=3; IntAct=EBI-352682, EBI-4290895;
P04792; A0A0C4DFM3: PRUNE2; NbExp=3; IntAct=EBI-352682, EBI-25830870;
P04792; P28062-2: PSMB8; NbExp=3; IntAct=EBI-352682, EBI-372312;
P04792; P62333: PSMC6; NbExp=3; IntAct=EBI-352682, EBI-357669;
P04792; P47897: QARS1; NbExp=3; IntAct=EBI-352682, EBI-347462;
P04792; Q86YS6: RAB43; NbExp=2; IntAct=EBI-352682, EBI-4401730;
P04792; Q9Y5P3: RAI2; NbExp=3; IntAct=EBI-352682, EBI-746228;
P04792; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-352682, EBI-17589229;
P04792; Q8TDP1: RNASEH2C; NbExp=3; IntAct=EBI-352682, EBI-9027335;
P04792; Q8N5U6: RNF10; NbExp=3; IntAct=EBI-352682, EBI-714023;
P04792; Q96D59: RNF183; NbExp=3; IntAct=EBI-352682, EBI-743938;
P04792; P62244: RPS15A; NbExp=3; IntAct=EBI-352682, EBI-347895;
P04792; P62979: RPS27A; NbExp=3; IntAct=EBI-352682, EBI-357375;
P04792; P08865: RPSA; NbExp=4; IntAct=EBI-352682, EBI-354112;
P04792; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-352682, EBI-10248967;
P04792; Q8N6K7-2: SAMD3; NbExp=3; IntAct=EBI-352682, EBI-11528848;
P04792; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-352682, EBI-9089805;
P04792; Q12874: SF3A3; NbExp=2; IntAct=EBI-352682, EBI-1051880;
P04792; Q9NUL5-3: SHFL; NbExp=3; IntAct=EBI-352682, EBI-22000547;
P04792; Q8IYI0: SHLD1; NbExp=3; IntAct=EBI-352682, EBI-2560428;
P04792; P08195-4: SLC3A2; NbExp=3; IntAct=EBI-352682, EBI-12832276;
P04792; Q9NSD5-3: SLC6A13; NbExp=3; IntAct=EBI-352682, EBI-25831241;
P04792; Q92966: SNAPC3; NbExp=3; IntAct=EBI-352682, EBI-1760638;
P04792; Q13573: SNW1; NbExp=3; IntAct=EBI-352682, EBI-632715;
P04792; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-352682, EBI-11959123;
P04792; Q6RVD6: SPATA8; NbExp=3; IntAct=EBI-352682, EBI-8635958;
P04792; Q9Y657: SPIN1; NbExp=2; IntAct=EBI-352682, EBI-727129;
P04792; Q8TCT7-2: SPPL2B; NbExp=3; IntAct=EBI-352682, EBI-8345366;
P04792; Q9C004: SPRY4; NbExp=3; IntAct=EBI-352682, EBI-354861;
P04792; Q8IXS7: SRGAP3; NbExp=3; IntAct=EBI-352682, EBI-18616594;
P04792; Q9UNE7: STUB1; NbExp=4; IntAct=EBI-352682, EBI-357085;
P04792; Q8NBJ7: SUMF2; NbExp=3; IntAct=EBI-352682, EBI-723091;
P04792; Q17RD7-3: SYT16; NbExp=3; IntAct=EBI-352682, EBI-25861603;
P04792; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-352682, EBI-745958;
P04792; Q8IYN2: TCEAL8; NbExp=3; IntAct=EBI-352682, EBI-2116184;
P04792; Q13569: TDG; NbExp=3; IntAct=EBI-352682, EBI-348333;
P04792; Q86WV5: TEN1; NbExp=3; IntAct=EBI-352682, EBI-2562799;
P04792; Q96A09: TENT5B; NbExp=3; IntAct=EBI-352682, EBI-752030;
P04792; P21980-2: TGM2; NbExp=3; IntAct=EBI-352682, EBI-25842075;
P04792; O60830: TIMM17B; NbExp=3; IntAct=EBI-352682, EBI-2372529;
P04792; A0AVI4-2: TMEM129; NbExp=3; IntAct=EBI-352682, EBI-25871541;
P04792; Q53NU3: tmp_locus_54; NbExp=3; IntAct=EBI-352682, EBI-10242677;
P04792; Q8IUR5-4: TMTC1; NbExp=3; IntAct=EBI-352682, EBI-9089156;
P04792; Q71RG4-4: TMUB2; NbExp=3; IntAct=EBI-352682, EBI-25831574;
P04792; P04637: TP53; NbExp=3; IntAct=EBI-352682, EBI-366083;
P04792; P13693: TPT1; NbExp=2; IntAct=EBI-352682, EBI-1783169;
P04792; P36406: TRIM23; NbExp=3; IntAct=EBI-352682, EBI-740098;
P04792; Q86WV8: TSC1; NbExp=3; IntAct=EBI-352682, EBI-12806590;
P04792; Q9Y3Q8: TSC22D4; NbExp=3; IntAct=EBI-352682, EBI-739485;
P04792; Q99614: TTC1; NbExp=3; IntAct=EBI-352682, EBI-742074;
P04792; Q9BUF5: TUBB6; NbExp=3; IntAct=EBI-352682, EBI-356735;
P04792; Q5VYS8-5: TUT7; NbExp=3; IntAct=EBI-352682, EBI-9088812;
P04792; Q8NBM4-4: UBAC2; NbExp=3; IntAct=EBI-352682, EBI-25840976;
P04792; Q969T4: UBE2E3; NbExp=3; IntAct=EBI-352682, EBI-348496;
P04792; Q8WVN8: UBE2Q2; NbExp=3; IntAct=EBI-352682, EBI-2130157;
P04792; Q04323-2: UBXN1; NbExp=3; IntAct=EBI-352682, EBI-11530712;
P04792; O75604-3: USP2; NbExp=3; IntAct=EBI-352682, EBI-10696113;
P04792; P45880: VDAC2; NbExp=3; IntAct=EBI-352682, EBI-354022;
P04792; P58304: VSX2; NbExp=3; IntAct=EBI-352682, EBI-6427899;
P04792; Q9BQA1: WDR77; NbExp=3; IntAct=EBI-352682, EBI-1237307;
P04792; Q9BRX9: WDR83; NbExp=4; IntAct=EBI-352682, EBI-7705033;
P04792; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-352682, EBI-12040603;
P04792; P13010: XRCC5; NbExp=2; IntAct=EBI-352682, EBI-357997;
P04792; P63104: YWHAZ; NbExp=4; IntAct=EBI-352682, EBI-347088;
P04792; Q8TBF4: ZCRB1; NbExp=3; IntAct=EBI-352682, EBI-11124401;
P04792; Q96K21: ZFYVE19; NbExp=3; IntAct=EBI-352682, EBI-6448240;
P04792; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-352682, EBI-25831733;
P04792; Q96N77-2: ZNF641; NbExp=3; IntAct=EBI-352682, EBI-12939666;
P04792; Q9BS34: ZNF670; NbExp=3; IntAct=EBI-352682, EBI-745276;
P04792; Q16670: ZSCAN26; NbExp=3; IntAct=EBI-352682, EBI-3920053;
P04792; Q2QGD7: ZXDC; NbExp=3; IntAct=EBI-352682, EBI-1538838;
P04792; A0A384ME25; NbExp=3; IntAct=EBI-352682, EBI-10211777;
P04792; B7Z3E8; NbExp=3; IntAct=EBI-352682, EBI-25831617;
P04792; Q7L8T7; NbExp=3; IntAct=EBI-352682, EBI-25831943;
P04792; Q86V28; NbExp=3; IntAct=EBI-352682, EBI-10259496;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10777697,
ECO:0000269|PubMed:28144995}. Nucleus {ECO:0000269|PubMed:19464326}.
Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10777697}.
Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles
in mitotic cells. Translocates to the nucleus during heat shock and
resides in sub-nuclear structures known as SC35 speckles or nuclear
splicing speckles. {ECO:0000269|PubMed:19464326}.
-!- TISSUE SPECIFICITY: Detected in all tissues tested: skeletal muscle,
heart, aorta, large intestine, small intestine, stomach, esophagus,
bladder, adrenal gland, thyroid, pancreas, testis, adipose tissue,
kidney, liver, spleen, cerebral cortex, blood serum and cerebrospinal
fluid. Highest levels are found in the heart and in tissues composed of
striated and smooth muscle. {ECO:0000269|PubMed:1560006}.
-!- INDUCTION: Up-regulated in response to environmental stresses such as
heat shock (PubMed:8325890). Up-regulated by estrogen stimulation
(PubMed:2743305). {ECO:0000269|PubMed:2743305,
ECO:0000269|PubMed:8325890}.
-!- INDUCTION: (Microbial infection) Up-regulated in response to
enterovirus 71 (EV71) infection (at protein level).
{ECO:0000269|PubMed:16548883}.
-!- PTM: Phosphorylated upon exposure to protein kinase C activators and
heat shock (PubMed:8325890). Phosphorylation by MAPKAPK2 and MAPKAPK3
in response to stress dissociates HSPB1 from large small heat-shock
protein (sHsps) oligomers and impairs its chaperone activity and
ability to protect against oxidative stress effectively.
Phosphorylation by MAPKAPK5 in response to PKA stimulation induces F-
actin rearrangement (PubMed:1332886, PubMed:8093612, PubMed:19166925).
{ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:19166925,
ECO:0000269|PubMed:8093612, ECO:0000269|PubMed:8325890}.
-!- DISEASE: Charcot-Marie-Tooth disease 2F (CMT2F) [MIM:606595]: A
dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the
peripheral nervous system, characterized by progressive weakness and
atrophy, initially of the peroneal muscles and later of the distal
muscles of the arms. Charcot-Marie-Tooth disease is classified in two
main groups on the basis of electrophysiologic properties and
histopathology: primary peripheral demyelinating neuropathies
(designated CMT1 when they are dominantly inherited) and primary
peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group
are characterized by signs of axonal degeneration in the absence of
obvious myelin alterations, normal or slightly reduced nerve conduction
velocities, and progressive distal muscle weakness and atrophy. Onset
of Charcot-Marie-Tooth disease type 2F is between 15 and 25 years with
muscle weakness and atrophy usually beginning in feet and legs
(peroneal distribution). Upper limb involvement occurs later.
{ECO:0000269|PubMed:15122254, ECO:0000269|PubMed:20178975,
ECO:0000269|PubMed:22176143, ECO:0000269|PubMed:22206013,
ECO:0000269|PubMed:23728742}. Note=The disease is caused by variants
affecting the gene represented in this entry.
-!- DISEASE: Neuronopathy, distal hereditary motor, 2B (HMN2B)
[MIM:608634]: A neuromuscular disorder. Distal hereditary motor
neuronopathies constitute a heterogeneous group of neuromuscular
disorders caused by selective degeneration of motor neurons in the
anterior horn of the spinal cord, without sensory deficit in the
posterior horn. The overall clinical picture consists of a classical
distal muscular atrophy syndrome in the legs without clinical sensory
loss. The disease starts with weakness and wasting of distal muscles of
the anterior tibial and peroneal compartments of the legs. Later on,
weakness and atrophy may expand to the proximal muscles of the lower
limbs and/or to the distal upper limbs. {ECO:0000269|PubMed:15122254,
ECO:0000269|PubMed:18832141, ECO:0000269|PubMed:18952241,
ECO:0000269|PubMed:20178975, ECO:0000269|PubMed:20870250,
ECO:0000269|PubMed:22176143, ECO:0000269|PubMed:23643870,
ECO:0000269|PubMed:23728742, ECO:0000269|PubMed:23948568,
ECO:0000269|PubMed:25965061, ECO:0000269|PubMed:28144995}. Note=The
disease is caused by variants affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
{ECO:0000255|PROSITE-ProRule:PRU00285}.
-!- SEQUENCE CAUTION:
Sequence=AAA62175.1; Type=Frameshift; Evidence={ECO:0000305};
Sequence=AAB20722.1; Type=Frameshift; Evidence={ECO:0000305};
Sequence=CAA34498.1; Type=Frameshift; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
URL="https://uantwerpen.vib.be/CMTMutations";
-!- WEB RESOURCE: Name=NIEHS SNPs;
URL="http://egp.gs.washington.edu/data/hspb1/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/HSPB1ID40880ch7q11.html";
---------------------------------------------------------------------------
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EMBL; L39370; AAA62175.1; ALT_FRAME; Genomic_DNA.
EMBL; X54079; CAA38016.1; -; mRNA.
EMBL; Z23090; CAA80636.1; -; mRNA.
EMBL; AB020027; BAB17232.1; -; mRNA.
EMBL; U90906; AAB51056.1; -; mRNA.
EMBL; CR407614; CAG28542.1; -; mRNA.
EMBL; CR536489; CAG38728.1; -; mRNA.
EMBL; BT019888; AAV38691.1; -; mRNA.
EMBL; AK311894; BAG34835.1; -; mRNA.
EMBL; DQ379985; ABC88475.1; -; Genomic_DNA.
EMBL; AC006388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471220; EAW71803.1; -; Genomic_DNA.
EMBL; BC000510; AAH00510.1; -; mRNA.
EMBL; BC012292; AAH12292.1; -; mRNA.
EMBL; BC012768; AAH12768.1; -; mRNA.
EMBL; BC014920; AAH14920.1; -; mRNA.
EMBL; BC073768; AAH73768.1; -; mRNA.
EMBL; X16477; CAA34498.1; ALT_FRAME; mRNA.
EMBL; S74571; AAB20722.1; ALT_FRAME; mRNA.
CCDS; CCDS5583.1; -.
PIR; S12102; HHHU27.
RefSeq; NP_001531.1; NM_001540.3.
PDB; 2N3J; NMR; -; A/B=80-176.
PDB; 3Q9P; X-ray; 2.00 A; A=90-171.
PDB; 3Q9Q; X-ray; 2.20 A; A/B=90-171.
PDB; 4MJH; X-ray; 2.60 A; A/C=84-176, B/D=179-186.
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.
PDB; 6GJH; X-ray; 2.10 A; A/B/C/D/E/F/G/H=84-170.
PDBsum; 2N3J; -.
PDBsum; 3Q9P; -.
PDBsum; 3Q9Q; -.
PDBsum; 4MJH; -.
PDBsum; 6DV5; -.
PDBsum; 6GJH; -.
SMR; P04792; -.
BioGRID; 109547; 610.
DIP; DIP-412N; -.
IntAct; P04792; 570.
MINT; P04792; -.
STRING; 9606.ENSP00000248553; -.
BindingDB; P04792; -.
ChEMBL; CHEMBL5976; -.
DrugBank; DB06094; Apatorsen.
DrugBank; DB11638; Artenimol.
DrugBank; DB12695; Phenethyl Isothiocyanate.
MoonDB; P04792; Predicted.
iPTMnet; P04792; -.
PhosphoSitePlus; P04792; -.
SwissPalm; P04792; -.
BioMuta; HSPB1; -.
DMDM; 19855073; -.
DOSAC-COBS-2DPAGE; P04792; -.
OGP; P04792; -.
REPRODUCTION-2DPAGE; IPI00025512; -.
REPRODUCTION-2DPAGE; P04792; -.
SWISS-2DPAGE; P04792; -.
UCD-2DPAGE; P04792; -.
CPTAC; CPTAC-1351; -.
CPTAC; CPTAC-1426; -.
CPTAC; CPTAC-1427; -.
CPTAC; CPTAC-1428; -.
CPTAC; CPTAC-1429; -.
CPTAC; CPTAC-1430; -.
CPTAC; CPTAC-702; -.
CPTAC; CPTAC-703; -.
CPTAC; CPTAC-704; -.
CPTAC; CPTAC-970; -.
EPD; P04792; -.
jPOST; P04792; -.
MassIVE; P04792; -.
PaxDb; P04792; -.
PeptideAtlas; P04792; -.
PRIDE; P04792; -.
ProteomicsDB; 51743; -.
TopDownProteomics; P04792; -.
ABCD; P04792; 3 sequenced antibodies.
Antibodypedia; 603; 3158 antibodies.
CPTC; P04792; 6 antibodies.
DNASU; 3315; -.
Ensembl; ENST00000248553; ENSP00000248553; ENSG00000106211.
GeneID; 3315; -.
KEGG; hsa:3315; -.
CTD; 3315; -.
DisGeNET; 3315; -.
GeneCards; HSPB1; -.
GeneReviews; HSPB1; -.
HGNC; HGNC:5246; HSPB1.
HPA; ENSG00000106211; Tissue enhanced (vagina).
MalaCards; HSPB1; -.
MIM; 602195; gene.
MIM; 606595; phenotype.
MIM; 608634; phenotype.
neXtProt; NX_P04792; -.
OpenTargets; ENSG00000106211; -.
Orphanet; 99940; Autosomal dominant Charcot-Marie-Tooth disease type 2F.
Orphanet; 139525; Distal hereditary motor neuropathy type 2.
PharmGKB; PA29511; -.
VEuPathDB; HostDB:ENSG00000106211.8; -.
eggNOG; KOG3591; Eukaryota.
GeneTree; ENSGT00940000155882; -.
HOGENOM; CLU_095001_0_0_1; -.
InParanoid; P04792; -.
OMA; EEWAQWF; -.
OrthoDB; 1187096at2759; -.
PhylomeDB; P04792; -.
TreeFam; TF105049; -.
PathwayCommons; P04792; -.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
SIGNOR; P04792; -.
BioGRID-ORCS; 3315; 7 hits in 996 CRISPR screens.
ChiTaRS; HSPB1; human.
GeneWiki; Hsp27; -.
GenomeRNAi; 3315; -.
Pharos; P04792; Tchem.
PRO; PR:P04792; -.
Proteomes; UP000005640; Chromosome 7.
RNAct; P04792; protein.
Bgee; ENSG00000106211; Expressed in myometrium and 242 other tissues.
ExpressionAtlas; P04792; baseline and differential.
Genevisible; P04792; HS.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000502; C:proteasome complex; ISS:BHF-UCL.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IMP:UniProtKB.
GO; GO:0044183; F:protein folding chaperone; IMP:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0005080; F:protein kinase C binding; ISS:BHF-UCL.
GO; GO:0008426; F:protein kinase C inhibitor activity; ISS:BHF-UCL.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:ARUK-UCL.
GO; GO:0043130; F:ubiquitin binding; ISS:BHF-UCL.
GO; GO:0099641; P:anterograde axonal protein transport; IMP:UniProtKB.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IMP:BHF-UCL.
GO; GO:0061077; P:chaperone-mediated protein folding; IMP:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IMP:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISS:BHF-UCL.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:BHF-UCL.
GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IMP:BHF-UCL.
GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IMP:BHF-UCL.
GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:BHF-UCL.
GO; GO:0010506; P:regulation of autophagy; NAS:ParkinsonsUK-UCL.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:BHF-UCL.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0001932; P:regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0006446; P:regulation of translational initiation; TAS:ProtInc.
GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
GO; GO:0009615; P:response to virus; IEP:UniProtKB.
GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd06475; ACD_HspB1_like; 1.
Gene3D; 2.60.40.790; -; 1.
InterPro; IPR002068; A-crystallin/Hsp20_dom.
InterPro; IPR037876; ACD_HspB1.
InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
InterPro; IPR008978; HSP20-like_chaperone.
PANTHER; PTHR45640; PTHR45640; 1.
Pfam; PF00011; HSP20; 1.
PRINTS; PR00299; ACRYSTALLIN.
SUPFAM; SSF49764; SSF49764; 1.
PROSITE; PS01031; SHSP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chaperone; Charcot-Marie-Tooth disease;
Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease variant;
Host-virus interaction; Methylation; Neurodegeneration; Neuropathy;
Nucleus; Phosphoprotein; Reference proteome; Stress response.
CHAIN 1..205
/note="Heat shock protein beta-1"
/id="PRO_0000125927"
DOMAIN 76..184
/note="sHSP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
REGION 70..205
/note="Interaction with TGFB1I1"
/evidence="ECO:0000250"
MOD_RES 12
/note="Omega-N-methylarginine"
/evidence="ECO:0007744|PubMed:24129315"
MOD_RES 15
/note="Phosphoserine; by MAPKAPK2 and MAPKAPK3"
/evidence="ECO:0000269|PubMed:10383393,
ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:8774846,
ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087,
ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
MOD_RES 26
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P42930"
MOD_RES 65
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17081983,
ECO:0007744|PubMed:20068231"
MOD_RES 78
/note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5"
/evidence="ECO:0000269|PubMed:10383393,
ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:15976317,
ECO:0000269|PubMed:1730670, ECO:0000269|PubMed:19166925,
ECO:0000269|PubMed:8774846, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
MOD_RES 82
/note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5"
/evidence="ECO:0000269|PubMed:10383393,
ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:15976317,
ECO:0000269|PubMed:1730670, ECO:0000269|PubMed:19166925,
ECO:0000269|PubMed:8774846, ECO:0000269|Ref.14,
ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 83
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:16964243"
MOD_RES 86
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 98
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:24275569"
MOD_RES 123
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 174
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 176
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 199
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
VARIANT 7
/note="P -> S (in HMN2B; induces hyperphosphorylation of
neurofilaments; no effect on cytoplasmic location; no
effect on dimerization; dbSNP:rs1563651698)"
/evidence="ECO:0000269|PubMed:28144995"
/id="VAR_078128"
VARIANT 34
/note="G -> R (in HMN2B; increased aggregation; increased
homooligomerization; changed function in chaperone-mediated
protein folding; dbSNP:rs1554614432)"
/evidence="ECO:0000269|PubMed:22176143,
ECO:0000269|PubMed:25965061"
/id="VAR_077483"
VARIANT 39
/note="P -> L (in HMN2B and CMT2F; increased aggregation;
increased homooligomerization; decreased phosphorylation by
MAPKAPK2; changed function in chaperone-mediated protein
folding; dbSNP:rs557327165)"
/evidence="ECO:0000269|PubMed:18832141,
ECO:0000269|PubMed:22176143, ECO:0000269|PubMed:25965061,
ECO:0000269|PubMed:28144995"
/id="VAR_077484"
VARIANT 41
/note="E -> K (in HMN2B; increased aggregation; increased
homooligomerization; changed function in chaperone-mediated
protein folding; dbSNP:rs1393404971)"
/evidence="ECO:0000269|PubMed:22176143,
ECO:0000269|PubMed:25965061"
/id="VAR_077485"
VARIANT 53
/note="G -> D (in HMN2B; no effect on dimerization; no
effect on cytoplasmic location; no effect on dimerization;
dbSNP:rs375244209)"
/evidence="ECO:0000269|PubMed:28144995"
/id="VAR_078129"
VARIANT 84
/note="G -> R (in HMN2B; decreased homooligomerization;
decreased heterooligomerization with HSPB6; no effect on
phosphorylation by MAPKAPK2; decreased function in
chaperone-mediated protein folding; dbSNP:rs770272088)"
/evidence="ECO:0000269|PubMed:18832141,
ECO:0000269|PubMed:23948568"
/id="VAR_077486"
VARIANT 99
/note="L -> M (in HMN2B; decreased homooligomerization;
decreased heterooligomerization with HSPB6; no effect on
phosphorylation by MAPKAPK2; decreased function in
chaperone-mediated protein folding; dbSNP:rs121909113)"
/evidence="ECO:0000269|PubMed:18832141,
ECO:0000269|PubMed:23948568"
/id="VAR_077487"
VARIANT 127
/note="R -> W (in HMN2B; decreased homodimerization;
increased client proteins binding; increased function in
chaperone-mediated protein folding; alters CDK5-mediated
phosphorylation of neurofilament proteins and indirectly
impairs their anterograde axonal transport;
dbSNP:rs29001571)"
/evidence="ECO:0000269|PubMed:15122254,
ECO:0000269|PubMed:20178975, ECO:0000269|PubMed:23728742,
ECO:0000269|PubMed:28144995"
/id="VAR_018506"
VARIANT 128
/note="Q -> R (in HMN2B; unknown pathological significance;
no effect on dimerization; no effect on cytoplasmic
location; no effect on dimerization; dbSNP:rs558882005)"
/evidence="ECO:0000269|PubMed:28144995"
/id="VAR_078130"
VARIANT 135
/note="S -> F (in CMT2F and HMN2B; decreased
homodimerization; increased client proteins binding;
increased function in chaperone-mediated protein folding;
alters CDK5-mediated phosphorylation of neurofilament
proteins; alters CDK5-mediated phosphorylation of
neurofilament proteins and indirectly impairs their
anterograde axonal transport; dbSNP:rs28939680)"
/evidence="ECO:0000269|PubMed:15122254,
ECO:0000269|PubMed:18832141, ECO:0000269|PubMed:20178975,
ECO:0000269|PubMed:23728742"
/id="VAR_018507"
VARIANT 136
/note="R -> L (in CMT2F and HMN2B; dbSNP:rs863225022)"
/evidence="ECO:0000269|PubMed:22176143"
/id="VAR_077488"
VARIANT 136
/note="R -> W (in CMT2F; decreased homodimerization only
with the wild-type protein; increased client proteins
binding; increased function in chaperone-mediated protein
folding; dbSNP:rs28939681)"
/evidence="ECO:0000269|PubMed:15122254,
ECO:0000269|PubMed:20178975"
/id="VAR_018508"
VARIANT 140
/note="R -> G (in HMN2B; decreased thermal stability;
changed protein structure; changed homooligomerization;
loss of heterooligomerization with HSPB6; decreased
function in chaperone-mediated protein folding;
dbSNP:rs121909112)"
/evidence="ECO:0000269|PubMed:18832141,
ECO:0000269|PubMed:23643870"
/id="VAR_077489"
VARIANT 141
/note="K -> Q (in HMN2B; decreased thermal stability;
changed protein structure; no effect on
homooligomerization; changed heterooligomerization with
HSPB6; slightly decreased function in chaperone-mediated
protein folding; dbSNP:rs1554614650)"
/evidence="ECO:0000269|PubMed:18952241,
ECO:0000269|PubMed:23643870"
/id="VAR_077490"
VARIANT 151
/note="T -> I (in HMN2B; no effect on homodimerization; no
effect on client proteins binding; no effect on function in
chaperone-mediated protein folding; dbSNP:rs28937568)"
/evidence="ECO:0000269|PubMed:15122254,
ECO:0000269|PubMed:20178975, ECO:0000269|PubMed:28144995"
/id="VAR_018509"
VARIANT 156
/note="S -> Y (no effect on oligomerization; no effect on
client proteins binding; no effect on function in
chaperone-mediated protein folding; dbSNP:rs374995963)"
/evidence="ECO:0000269|PubMed:20178975"
/id="VAR_077491"
VARIANT 164
/note="T -> A (in CMT2F; dbSNP:rs1032400275)"
/evidence="ECO:0000269|PubMed:22206013"
/id="VAR_067085"
VARIANT 175..205
/note="Missing (in HMN2B)"
/evidence="ECO:0000269|PubMed:28144995"
/id="VAR_078131"
VARIANT 180
/note="T -> I (in HMN2B; unknown pathological significance;
dbSNP:rs1422978230)"
/evidence="ECO:0000269|PubMed:20870250,
ECO:0000269|PubMed:22176143, ECO:0000269|PubMed:28144995"
/id="VAR_077492"
VARIANT 182
/note="P -> L (in HMN2B; decreased protein abundance; no
effect on oligomerization; increased client proteins
binding; no effect on function in chaperone-mediated
protein folding; alters CDK5-mediated phosphorylation of
neurofilament proteins; indirectly impairs their
anterograde axonal transport; dbSNP:rs28937569)"
/evidence="ECO:0000269|PubMed:15122254,
ECO:0000269|PubMed:20178975, ECO:0000269|PubMed:23728742"
/id="VAR_018510"
VARIANT 187
/note="S -> L (in HMN2B; formation of large cytoplasmic
aggregates; no effect on dimerization; dbSNP:rs774585320)"
/evidence="ECO:0000269|PubMed:28144995"
/id="VAR_078132"
VARIANT 188
/note="R -> W (in CMT2F; unknown pathological significance;
dbSNP:rs772767500)"
/evidence="ECO:0000269|PubMed:22176143"
/id="VAR_077493"
VARIANT 190
/note="Q -> H (found in a patient with sporadic amyotrophic
lateral sclerosis; unknown pathological significance;
dbSNP:rs764297134)"
/evidence="ECO:0000269|PubMed:27492805"
/id="VAR_077494"
MUTAGEN 15
/note="S->D: Mimicks phosphorylation state, leading to
dreased ability to act as molecular chaperones; when
associated with D-78 and D-82."
/evidence="ECO:0000269|PubMed:10383393"
MUTAGEN 78
/note="S->D: Mimicks phosphorylation state, leading to
dreased ability to act as molecular chaperones; when
associated with D-15 and D-82."
/evidence="ECO:0000269|PubMed:10383393"
MUTAGEN 82
/note="S->D: Mimicks phosphorylation state, leading to
dreased ability to act as molecular chaperones; when
associated with D-15 and D-78."
/evidence="ECO:0000269|PubMed:10383393"
CONFLICT 10
/note="L -> I (in Ref. 13; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 109
/note="L -> R (in Ref. 12; AAH12292)"
/evidence="ECO:0000305"
CONFLICT 121
/note="T -> S (in Ref. 12; AAH12292)"
/evidence="ECO:0000305"
CONFLICT 127
/note="R -> L (in Ref. 12; AAH12292)"
/evidence="ECO:0000305"
STRAND 86..88
/evidence="ECO:0007829|PDB:4MJH"
STRAND 94..100
/evidence="ECO:0007829|PDB:3Q9P"
TURN 102..104
/evidence="ECO:0007829|PDB:3Q9P"
STRAND 107..114
/evidence="ECO:0007829|PDB:3Q9P"
STRAND 117..124
/evidence="ECO:0007829|PDB:3Q9P"
STRAND 136..143
/evidence="ECO:0007829|PDB:3Q9P"
TURN 145..147
/evidence="ECO:0007829|PDB:2N3J"
HELIX 150..152
/evidence="ECO:0007829|PDB:3Q9P"
STRAND 154..157
/evidence="ECO:0007829|PDB:3Q9P"
STRAND 161..168
/evidence="ECO:0007829|PDB:3Q9P"
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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[HSPB1 HSP27 HSP28] Heat shock protein beta-1 (HspB1) (28 kDa heat shock protein) (Estrogen-regulated 24 kDa protein) (Heat shock 27 kDa protein) (HSP 27) (Stress-responsive protein 27) (SRP27)
[Hspb1 Hsp25 Hsp27] Heat shock protein beta-1 (HspB1) (Growth-related 25 kDa protein) (Heat shock 25 kDa protein) (HSP 25) (Heat shock 27 kDa protein) (HSP 27) (p25)
[Hspb1 Hsp27] Heat shock protein beta-1 (HspB1) (Heat shock 27 kDa protein) (HSP 27)
[HSPB1] Heat shock protein beta-1 (HspB1) (25 kDa IAP) (Actin polymerization inhibitor) (Heat shock 25 kDa protein) (HSP 25) (Heat shock 27 kDa protein) (HSP 27)
[HSP90AA1 HSP90A HSPC1 HSPCA] Heat shock protein HSP 90-alpha (EC 3.6.4.10) (Heat shock 86 kDa) (HSP 86) (HSP86) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38)
[HSP90AB1 HSP90B HSPC2 HSPCB] Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84)
[Hsp90ab1 Hsp84 Hsp84-1 Hspcb] Heat shock protein HSP 90-beta (Heat shock 84 kDa) (HSP 84) (HSP84) (Tumor-specific transplantation 84 kDa antigen) (TSTA)
[Hsp90b1 Grp94 Tra-1 Tra1] Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Endoplasmic reticulum resident protein 99) (ERp99) (Heat shock protein 90 kDa beta member 1) (Polymorphic tumor rejection antigen 1) (Tumor rejection antigen gp96)
[Hspa1a Hsp70-1 Hspa1] Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 2) (HSP70-2) (HSP70.2)
[Hspa1b Hsp70-2 Hspa2] Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 1) (HSP70-1) (HSP70.1)
[HSPA1A HSP72 HSPA1 HSX70] Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 1) (HSP70-1) (HSP70.1)
[HSPA1B HSP72] Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 2) (HSP70-2) (HSP70.2)
[Hspa9 Grp75 Hsp74 Hspa9a] Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (Peptide-binding protein 74) (PBP74) (p66 MOT)
[Hsp90aa1 Hsp86 Hsp86-1 Hspca] Heat shock protein HSP 90-alpha (EC 3.6.4.10) (Heat shock 86 kDa) (HSP 86) (HSP86) (Tumor-specific transplantation 86 kDa antigen) (TSTA)
[HSPA8 HSC70 HSP73 HSPA10] Heat shock cognate 71 kDa protein (EC 3.6.4.10) (Heat shock 70 kDa protein 8) (Lipopolysaccharide-associated protein 1) (LAP-1) (LPS-associated protein 1)
[HSPB1 HSP27] Heat shock protein beta-1 (HspB1) (Heat shock 27 kDa protein) (HSP 27)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSPD1 HSP60] 60 kDa heat shock protein, mitochondrial (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (Heat shock protein 60) (HSP-60) (Hsp60) (HuCHA60) (Mitochondrial matrix protein P1) (P60 lymphocyte protein)
[Hsp90ab1 Hsp84 Hspcb] Heat shock protein HSP 90-beta (Heat shock 84 kDa) (HSP 84) (HSP84)
[HSP70-4 HSC70-4 HSP70 MED37_2 MED37C At3g12580 T16H11.7 T2E22.11] Heat shock 70 kDa protein 4 (Heat shock cognate 70 kDa protein 4) (Heat shock cognate protein 70-4) (AtHsc70-4) (Heat shock protein 70-4) (AtHsp70-4)
[HSPA1A HSP70-1] Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 1) (HSP70.1)
[Hspa1b Hcp70.1 Hsp70-1 Hsp70a1 Hspa1] Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 1) (HSP70.1)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) (Steroidogenesis-activator polypeptide)
[Hspa1a Hsp70-3 Hsp70A1] Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 3) (HSP70.3) (Hsp68)
[HSPB8 CRYAC E2IG1 HSP22 PP1629] Heat shock protein beta-8 (HspB8) (Alpha-crystallin C chain) (E2-induced gene 1 protein) (Protein kinase H11) (Small stress protein-like protein HSP22)
[Hsp90aa1 Hsp86 Hspca] Heat shock protein HSP 90-alpha (EC 3.6.4.10) (Heat shock 86 kDa) (HSP 86) (HSP86)
[HSPA9 GRP75 HSPA9B mt-HSP70] Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (MOT) (Peptide-binding protein 74) (PBP74)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[Hspa8 Hsc70 Hsc73] Heat shock cognate 71 kDa protein (EC 3.6.4.10) (Heat shock 70 kDa protein 8)

Bibliography :