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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.
28-MAR-2018, entry version 218.
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;
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:
Self; NbExp=5; IntAct=EBI-352682, EBI-352682;
O95817:BAG3; NbExp=6; IntAct=EBI-352682, EBI-747185;
P27797:CALR; NbExp=2; IntAct=EBI-352682, EBI-1049597;
P02489:CRYAA; NbExp=2; IntAct=EBI-352682, EBI-6875961;
P02511:CRYAB; NbExp=6; IntAct=EBI-352682, EBI-739060;
Q9UER7:DAXX; NbExp=4; IntAct=EBI-352682, EBI-77321;
O00273:DFFA; NbExp=2; IntAct=EBI-352682, EBI-727171;
Q15029:EFTUD2; NbExp=2; IntAct=EBI-352682, EBI-357897;
P00533:EGFR; NbExp=3; IntAct=EBI-352682, EBI-297353;
Q14240:EIF4A2; NbExp=2; IntAct=EBI-352682, EBI-73473;
P78344:EIF4G2; NbExp=3; IntAct=EBI-352682, EBI-296519;
Q02790:FKBP4; NbExp=2; IntAct=EBI-352682, EBI-1047444;
P02794:FTH1; NbExp=2; IntAct=EBI-352682, EBI-713259;
P11413:G6PD; NbExp=2; IntAct=EBI-352682, EBI-4289891;
P78417:GSTO1; NbExp=2; IntAct=EBI-352682, EBI-712083;
Q9UJY1:HSPB8; NbExp=3; IntAct=EBI-352682, EBI-739074;
Q7Z6Z7:HUWE1; NbExp=3; IntAct=EBI-352682, EBI-625934;
P78318:IGBP1; NbExp=3; IntAct=EBI-352682, EBI-1055954;
Q13418:ILK; NbExp=2; IntAct=EBI-352682, EBI-747644;
P49137:MAPKAPK2; NbExp=3; IntAct=EBI-352682, EBI-993299;
Q16644:MAPKAPK3; NbExp=3; IntAct=EBI-352682, EBI-1384657;
Q8IW41:MAPKAPK5; NbExp=2; IntAct=EBI-352682, EBI-1201460;
P08473:MME; NbExp=4; IntAct=EBI-352682, EBI-353759;
Q8N7H5:PAF1; NbExp=2; IntAct=EBI-352682, EBI-2607770;
Q96G03:PGM2; NbExp=2; IntAct=EBI-352682, EBI-4399372;
Q86YS6:RAB43; NbExp=2; IntAct=EBI-352682, EBI-4401730;
Q12874:SF3A3; NbExp=2; IntAct=EBI-352682, EBI-1051880;
Q13573:SNW1; NbExp=3; IntAct=EBI-352682, EBI-632715;
Q9Y657:SPIN1; NbExp=2; IntAct=EBI-352682, EBI-727129;
P04637:TP53; NbExp=3; IntAct=EBI-352682, EBI-366083;
P13693:TPT1; NbExp=2; IntAct=EBI-352682, EBI-1783169;
P13010:XRCC5; NbExp=2; IntAct=EBI-352682, EBI-357997;
P63104:YWHAZ; NbExp=4; IntAct=EBI-352682, EBI-347088;
-!- 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. Nerve conduction velocities are normal or
slightly reduced. 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 mutations 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 mutations 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; Positions=194; Evidence={ECO:0000305};
Sequence=AAB20722.1; Type=Frameshift; Positions=194; Evidence={ECO:0000305};
Sequence=CAA34498.1; Type=Frameshift; Positions=194; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
URL="http://www.molgen.ua.ac.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.
UniGene; Hs.520973; -.
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.
PDBsum; 2N3J; -.
PDBsum; 3Q9P; -.
PDBsum; 3Q9Q; -.
PDBsum; 4MJH; -.
ProteinModelPortal; P04792; -.
SMR; P04792; -.
BioGrid; 109547; 413.
DIP; DIP-412N; -.
IntAct; P04792; 326.
MINT; P04792; -.
STRING; 9606.ENSP00000248553; -.
BindingDB; P04792; -.
ChEMBL; CHEMBL5976; -.
DrugBank; DB06094; OGX-427.
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; -.
EPD; P04792; -.
PaxDb; P04792; -.
PeptideAtlas; P04792; -.
PRIDE; P04792; -.
TopDownProteomics; P04792; -.
DNASU; 3315; -.
Ensembl; ENST00000248553; ENSP00000248553; ENSG00000106211.
GeneID; 3315; -.
KEGG; hsa:3315; -.
CTD; 3315; -.
DisGeNET; 3315; -.
EuPathDB; HostDB:ENSG00000106211.8; -.
GeneCards; HSPB1; -.
GeneReviews; HSPB1; -.
HGNC; HGNC:5246; HSPB1.
HPA; CAB004439; -.
HPA; CAB047330; -.
HPA; CAB047331; -.
HPA; CAB047332; -.
HPA; HPA000497; -.
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; -.
eggNOG; KOG3591; Eukaryota.
eggNOG; ENOG410YERS; LUCA.
GeneTree; ENSGT00760000119238; -.
HOVERGEN; HBG054766; -.
InParanoid; P04792; -.
KO; K04455; -.
OMA; FDQSFGM; -.
OrthoDB; EOG091G0USC; -.
PhylomeDB; P04792; -.
TreeFam; TF105049; -.
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.
SIGNOR; P04792; -.
ChiTaRS; HSPB1; human.
GeneWiki; Hsp27; -.
GenomeRNAi; 3315; -.
PRO; PR:P04792; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000106211; -.
CleanEx; HS_HSPB1; -.
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:0031012; C:extracellular matrix; HDA:BHF-UCL.
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:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0000502; C:proteasome complex; ISS:BHF-UCL.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IMP:UniProtKB.
GO; GO:0044183; F:protein binding involved in protein folding; 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: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:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; 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:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
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/HSP.
InterPro; IPR031107; HSP20.
InterPro; IPR008978; HSP20-like_chaperone.
PANTHER; PTHR11527; PTHR11527; 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;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Disease mutation; Methylation; Neurodegeneration; Neuropathy; Nucleus;
Phosphoprotein; Reference proteome; Stress response.
CHAIN 1 205 Heat shock protein beta-1.
/FTId=PRO_0000125927.
DOMAIN 76 184 sHSP. {ECO:0000255|PROSITE-
ProRule:PRU00285}.
REGION 70 205 Interaction with TGFB1I1. {ECO:0000250}.
MOD_RES 12 12 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 15 15 Phosphoserine; by MAPKAPK2 and MAPKAPK3.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:10383393,
ECO:0000269|PubMed:1332886,
ECO:0000269|PubMed:8774846}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000250|UniProtKB:P42930}.
MOD_RES 65 65 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231}.
MOD_RES 78 78 Phosphoserine; by MAPKAPK2, MAPKAPK3 and
MAPKAPK5. {ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:10383393,
ECO:0000269|PubMed:1332886,
ECO:0000269|PubMed:15976317,
ECO:0000269|PubMed:1730670,
ECO:0000269|PubMed:19166925,
ECO:0000269|PubMed:8774846}.
MOD_RES 82 82 Phosphoserine; by MAPKAPK2, MAPKAPK3 and
MAPKAPK5. {ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
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}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000244|PubMed:16964243}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 123 123 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 174 174 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VARIANT 7 7 P -> S (in HMN2B; induces
hyperphosphorylation of neurofilaments;
no effect on cytoplasmic location; no
effect on dimerization).
{ECO:0000269|PubMed:28144995}.
/FTId=VAR_078128.
VARIANT 34 34 G -> R (in HMN2B; increased aggregation;
increased homooligomerization; changed
function in chaperone-mediated protein
folding). {ECO:0000269|PubMed:22176143,
ECO:0000269|PubMed:25965061}.
/FTId=VAR_077483.
VARIANT 39 39 P -> L (in HMN2B and CMT2F; increased
aggregation; increased
homooligomerization; decreased
phosphorylation by MAPKAPK2; changed
function in chaperone-mediated protein
folding; dbSNP:rs557327165).
{ECO:0000269|PubMed:18832141,
ECO:0000269|PubMed:22176143,
ECO:0000269|PubMed:25965061,
ECO:0000269|PubMed:28144995}.
/FTId=VAR_077484.
VARIANT 41 41 E -> K (in HMN2B; increased aggregation;
increased homooligomerization; changed
function in chaperone-mediated protein
folding). {ECO:0000269|PubMed:22176143,
ECO:0000269|PubMed:25965061}.
/FTId=VAR_077485.
VARIANT 53 53 G -> D (in HMN2B; no effect on
dimerization; no effect on cytoplasmic
location; no effect on dimerization;
dbSNP:rs375244209).
{ECO:0000269|PubMed:28144995}.
/FTId=VAR_078129.
VARIANT 84 84 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).
{ECO:0000269|PubMed:18832141,
ECO:0000269|PubMed:23948568}.
/FTId=VAR_077486.
VARIANT 99 99 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).
{ECO:0000269|PubMed:18832141,
ECO:0000269|PubMed:23948568}.
/FTId=VAR_077487.
VARIANT 127 127 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).
{ECO:0000269|PubMed:15122254,
ECO:0000269|PubMed:20178975,
ECO:0000269|PubMed:23728742,
ECO:0000269|PubMed:28144995}.
/FTId=VAR_018506.
VARIANT 128 128 Q -> R (in HMN2B; unknown pathological
significance; no effect on dimerization;
no effect on cytoplasmic location; no
effect on dimerization;
dbSNP:rs558882005).
{ECO:0000269|PubMed:28144995}.
/FTId=VAR_078130.
VARIANT 135 135 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).
{ECO:0000269|PubMed:15122254,
ECO:0000269|PubMed:18832141,
ECO:0000269|PubMed:20178975,
ECO:0000269|PubMed:23728742}.
/FTId=VAR_018507.
VARIANT 136 136 R -> L (in CMT2F and HMN2B;
dbSNP:rs863225022).
{ECO:0000269|PubMed:22176143}.
/FTId=VAR_077488.
VARIANT 136 136 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).
{ECO:0000269|PubMed:15122254,
ECO:0000269|PubMed:20178975}.
/FTId=VAR_018508.
VARIANT 140 140 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).
{ECO:0000269|PubMed:18832141,
ECO:0000269|PubMed:23643870}.
/FTId=VAR_077489.
VARIANT 141 141 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).
{ECO:0000269|PubMed:18952241,
ECO:0000269|PubMed:23643870}.
/FTId=VAR_077490.
VARIANT 151 151 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).
{ECO:0000269|PubMed:15122254,
ECO:0000269|PubMed:20178975,
ECO:0000269|PubMed:28144995}.
/FTId=VAR_018509.
VARIANT 156 156 S -> Y (rare polymorphism; no effect on
oligomerization; no effect on client
proteins binding; no effect on function
in chaperone-mediated protein folding).
{ECO:0000269|PubMed:20178975}.
/FTId=VAR_077491.
VARIANT 164 164 T -> A (in CMT2F).
{ECO:0000269|PubMed:22206013}.
/FTId=VAR_067085.
VARIANT 175 205 Missing (in HMN2B).
{ECO:0000269|PubMed:28144995}.
/FTId=VAR_078131.
VARIANT 180 180 T -> I (in HMN2B; unknown pathological
significance).
{ECO:0000269|PubMed:20870250,
ECO:0000269|PubMed:22176143,
ECO:0000269|PubMed:28144995}.
/FTId=VAR_077492.
VARIANT 182 182 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).
{ECO:0000269|PubMed:15122254,
ECO:0000269|PubMed:20178975,
ECO:0000269|PubMed:23728742}.
/FTId=VAR_018510.
VARIANT 187 187 S -> L (in HMN2B; formation of large
cytoplasmic aggregates; no effect on
dimerization).
{ECO:0000269|PubMed:28144995}.
/FTId=VAR_078132.
VARIANT 188 188 R -> W (in CMT2F; unknown pathological
significance; dbSNP:rs772767500).
{ECO:0000269|PubMed:22176143}.
/FTId=VAR_077493.
VARIANT 190 190 Q -> H (found in a patient with sporadic
amyotrophic lateral sclerosis; unknown
pathological significance;
dbSNP:rs764297134).
{ECO:0000269|PubMed:27492805}.
/FTId=VAR_077494.
MUTAGEN 15 15 S->D: Mimicks phosphorylation state,
leading to dreased ability to act as
molecular chaperones; when associated
with D-78 and D-82.
{ECO:0000269|PubMed:10383393}.
MUTAGEN 78 78 S->D: Mimicks phosphorylation state,
leading to dreased ability to act as
molecular chaperones; when associated
with D-15 and D-82.
{ECO:0000269|PubMed:10383393}.
MUTAGEN 82 82 S->D: Mimicks phosphorylation state,
leading to dreased ability to act as
molecular chaperones; when associated
with D-15 and D-78.
{ECO:0000269|PubMed:10383393}.
CONFLICT 10 10 L -> I (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 109 109 L -> R (in Ref. 12; AAH12292).
{ECO:0000305}.
CONFLICT 121 121 T -> S (in Ref. 12; AAH12292).
{ECO:0000305}.
CONFLICT 127 127 R -> L (in Ref. 12; AAH12292).
{ECO:0000305}.
STRAND 86 88 {ECO:0000244|PDB:4MJH}.
STRAND 94 100 {ECO:0000244|PDB:3Q9P}.
TURN 102 104 {ECO:0000244|PDB:3Q9P}.
STRAND 107 114 {ECO:0000244|PDB:3Q9P}.
STRAND 117 124 {ECO:0000244|PDB:3Q9P}.
STRAND 136 143 {ECO:0000244|PDB:3Q9P}.
TURN 145 147 {ECO:0000244|PDB:2N3J}.
HELIX 150 152 {ECO:0000244|PDB:3Q9P}.
STRAND 154 157 {ECO:0000244|PDB:3Q9P}.
STRAND 161 168 {ECO:0000244|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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