HSPB8_HUMAN
ID HSPB8_HUMAN Reviewed; 196 AA.
AC Q9UJY1; B2R6A6; Q6FIH3; Q9UKS3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Heat shock protein beta-8;
DE Short=HspB8;
DE AltName: Full=Alpha-crystallin C chain;
DE AltName: Full=E2-induced gene 1 protein;
DE AltName: Full=Protein kinase H11;
DE AltName: Full=Small stress protein-like protein HSP22;
GN Name=HSPB8; Synonyms=CRYAC, E2IG1, HSP22; ORFNames=PP1629;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11085516;
RA Charpentier A.H., Bednarek A.K., Daniel R.L., Hawkins K.A., Laflin K.J.,
RA Gaddis S., MacLeod M.C., Aldaz C.M.;
RT "Effects of estrogen on global gene expression: identification of novel
RT targets of estrogen action.";
RL Cancer Res. 60:5977-5983(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH HSPB1.
RX PubMed=11342557; DOI=10.1074/jbc.m103001200;
RA Benndorf R., Sun X., Gilmont R.R., Biederman K.J., Molloy M.P.,
RA Goodmurphy C.W., Cheng H., Andrews P.C., Welsh M.J.;
RT "HSP22, a new member of the small heat shock protein superfamily, interacts
RT with mimic of phosphorylated HSP27 (3DHSP27).";
RL J. Biol. Chem. 276:26753-26761(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Melanoma;
RX PubMed=10833516; DOI=10.1074/jbc.m002140200;
RA Smith C.C., Yu Y.X., Kulka M., Aurelian L.;
RT "A novel human gene similar to the protein kinase (PK) coding domain of the
RT large subunit of herpes simplex virus type 2 ribonucleotide reductase
RT (ICP10) codes for a serine-threonine PK and is expressed in melanoma
RT cells.";
RL J. Biol. Chem. 275:25690-25699(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP PHOSPHORYLATION AT THR-63, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11816564; DOI=10.1021/ac0104227;
RA Molloy M.P., Andrews P.C.;
RT "Phosphopeptide derivatization signatures to identify serine and threonine
RT phosphorylated peptides by mass spectrometry.";
RL Anal. Chem. 73:5387-5394(2001).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=11470154; DOI=10.1016/s0167-4781(01)00237-8;
RA Kappe G., Verschuure P., Philipsen R.L.A., Staalduinen A.A.,
RA Van de Boogaart P., Boelens W.C., de Jong W.W.;
RT "Characterization of two novel human small heat shock proteins: protein
RT kinase-related HspB8 and testis-specific HspB9.";
RL Biochim. Biophys. Acta 1520:1-6(2001).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=19464326; DOI=10.1016/j.bbamcr.2009.05.005;
RA Vos M.J., Kanon B., Kampinga H.H.;
RT "HSPB7 is a SC35 speckle resident small heat shock protein.";
RL Biochim. Biophys. Acta 1793:1343-1353(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP INTERACTION WITH DNAJB6.
RX PubMed=22366786; DOI=10.1038/ng.1103;
RA Sarparanta J., Jonson P.H., Golzio C., Sandell S., Luque H., Screen M.,
RA McDonald K., Stajich J.M., Mahjneh I., Vihola A., Raheem O., Penttila S.,
RA Lehtinen S., Huovinen S., Palmio J., Tasca G., Ricci E., Hackman P.,
RA Hauser M., Katsanis N., Udd B.;
RT "Mutations affecting the cytoplasmic functions of the co-chaperone DNAJB6
RT cause limb-girdle muscular dystrophy.";
RL Nat. Genet. 44:450-455(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP VARIANTS HMN2A GLU-141 AND ASN-141.
RX PubMed=15122253; DOI=10.1038/ng1328;
RA Irobi J., Van Impe K., Seeman P., Jordanova A., Dierick I., Verpoorten N.,
RA Michalik A., De Vriendt E., Jacobs A., Van Gerwen V., Vennekens K.,
RA Mazanec R., Tournev I., Hilton-Jones D., Talbot K., Kremensky I.,
RA Van Den Bosch L., Robberecht W., Van Vandekerckhove J., Broeckhoven C.,
RA Gettemans J., De Jonghe P., Timmerman V.;
RT "Hot-spot residue in small heat-shock protein 22 causes distal motor
RT neuropathy.";
RL Nat. Genet. 36:597-601(2004).
RN [20]
RP VARIANT CMT2L ASN-141.
RX PubMed=15565283; DOI=10.1007/s00439-004-1218-3;
RA Tang B.-S., Zhao G.-H., Luo W., Xia K., Cai F., Pan Q., Zhang R.-X.,
RA Zhang F.F., Liu X.-M., Chen B., Zhang C., Shen L., Jiang H., Long Z.G.,
RA Dai H.-P.;
RT "Small heat-shock protein 22 mutated in autosomal dominant Charcot-Marie-
RT Tooth disease type 2L.";
RL Hum. Genet. 116:222-224(2005).
RN [21]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-67 AND MET-78.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [22]
RP VARIANTS HMN2A LEU-90; THR-138; ASN-141 AND MET-141, INTERACTION WITH BAG3,
RP SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS HMN2A LEU-90;
RP THR-138; ASN-141 AND MET-141.
RX PubMed=28144995; DOI=10.1002/humu.23189;
RA Echaniz-Laguna A., Geuens T., Petiot P., Pereon Y., Adriaenssens E.,
RA Haidar M., Capponi S., Maisonobe T., Fournier E., Dubourg O., Degos B.,
RA Salachas F., Lenglet T., Eymard B., Delmont E., Pouget J.,
RA Juntas Morales R., Goizet C., Latour P., Timmerman V., Stojkovic T.;
RT "Axonal Neuropathies due to Mutations in Small Heat Shock Proteins:
RT Clinical, Genetic, and Functional Insights into Novel Mutations.";
RL Hum. Mutat. 38:556-568(2017).
CC -!- FUNCTION: Displays temperature-dependent chaperone activity.
CC -!- SUBUNIT: Monomer. Interacts with HSPB1. Interacts with DNAJB6.
CC Interacts with BAG3 (PubMed:28144995). {ECO:0000269|PubMed:11342557,
CC ECO:0000269|PubMed:22366786, ECO:0000269|PubMed:28144995}.
CC -!- INTERACTION:
CC Q9UJY1; O95817: BAG3; NbExp=11; IntAct=EBI-739074, EBI-747185;
CC Q9UJY1; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-739074, EBI-739879;
CC Q9UJY1; Q9UNI6: DUSP12; NbExp=3; IntAct=EBI-739074, EBI-715161;
CC Q9UJY1; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-739074, EBI-745689;
CC Q9UJY1; P04792: HSPB1; NbExp=3; IntAct=EBI-739074, EBI-352682;
CC Q9UJY1; Q16082: HSPB2; NbExp=3; IntAct=EBI-739074, EBI-739395;
CC Q9UJY1; Q9UBY9: HSPB7; NbExp=11; IntAct=EBI-739074, EBI-739361;
CC Q9UJY1; Q9UJY1: HSPB8; NbExp=6; IntAct=EBI-739074, EBI-739074;
CC Q9UJY1; Q8IVT2: MISP; NbExp=3; IntAct=EBI-739074, EBI-2555085;
CC Q9UJY1; Q15773: MLF2; NbExp=3; IntAct=EBI-739074, EBI-1051875;
CC Q9UJY1; Q9HC29-1: NOD2; NbExp=2; IntAct=EBI-739074, EBI-21496213;
CC Q9UJY1; Q2TAL8: QRICH1; NbExp=6; IntAct=EBI-739074, EBI-2798044;
CC Q9UJY1; P49247: RPIA; NbExp=3; IntAct=EBI-739074, EBI-744831;
CC Q9UJY1; O15375: SLC16A5; NbExp=3; IntAct=EBI-739074, EBI-12874738;
CC Q9UJY1; O14512: SOCS7; NbExp=3; IntAct=EBI-739074, EBI-1539606;
CC Q9UJY1; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-739074, EBI-8451480;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19464326,
CC ECO:0000269|PubMed:28144995}. Nucleus {ECO:0000269|PubMed:19464326}.
CC Note=Translocates to nuclear foci during heat shock.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and
CC heart. {ECO:0000269|PubMed:11470154}.
CC -!- INDUCTION: By 17-beta-estradiol.
CC -!- DISEASE: Neuronopathy, distal hereditary motor, 2A (HMN2A)
CC [MIM:158590]: A neuromuscular disorder. Distal hereditary motor
CC neuronopathies constitute a heterogeneous group of neuromuscular
CC disorders caused by selective degeneration of motor neurons in the
CC anterior horn of the spinal cord, without sensory deficit in the
CC posterior horn. The overall clinical picture consists of a classical
CC distal muscular atrophy syndrome in the legs without clinical sensory
CC loss. The disease starts with weakness and wasting of distal muscles of
CC the anterior tibial and peroneal compartments of the legs. Later on,
CC weakness and atrophy may expand to the proximal muscles of the lower
CC limbs and/or to the distal upper limbs. {ECO:0000269|PubMed:15122253,
CC ECO:0000269|PubMed:28144995}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Charcot-Marie-Tooth disease 2L (CMT2L) [MIM:608673]: An axonal
CC form of Charcot-Marie-Tooth disease, a disorder of the peripheral
CC nervous system, characterized by progressive weakness and atrophy,
CC initially of the peroneal muscles and later of the distal muscles of
CC the arms. Charcot-Marie-Tooth disease is classified in two main groups
CC on the basis of electrophysiologic properties and histopathology:
CC primary peripheral demyelinating neuropathies (designated CMT1 when
CC they are dominantly inherited) and primary peripheral axonal
CC neuropathies (CMT2). Neuropathies of the CMT2 group are characterized
CC by signs of axonal degeneration in the absence of obvious myelin
CC alterations, normal or slightly reduced nerve conduction velocities,
CC and progressive distal muscle weakness and atrophy.
CC {ECO:0000269|PubMed:15565283}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
CC -!- CAUTION: Was reported to have a protein kinase activity and to act as a
CC Mn(2+)-dependent serine-threonine-specific protein kinase.
CC {ECO:0000305|PubMed:10833516}.
CC -!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
CC URL="https://uantwerpen.vib.be/CMTMutations";
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DR EMBL; AF191017; AAF09481.1; -; mRNA.
DR EMBL; AF250138; AAF65562.1; -; mRNA.
DR EMBL; AF133207; AAD55359.1; -; mRNA.
DR EMBL; AL136936; CAB66870.1; -; mRNA.
DR EMBL; AF217987; AAG17230.1; -; mRNA.
DR EMBL; BT006876; AAP35522.1; -; mRNA.
DR EMBL; CR533453; CAG38484.1; -; mRNA.
DR EMBL; AK312501; BAG35403.1; -; mRNA.
DR EMBL; CH471054; EAW98144.1; -; Genomic_DNA.
DR EMBL; BC002673; AAH02673.1; -; mRNA.
DR CCDS; CCDS9189.1; -.
DR RefSeq; NP_055180.1; NM_014365.2.
DR AlphaFoldDB; Q9UJY1; -.
DR SMR; Q9UJY1; -.
DR BioGRID; 117689; 148.
DR CORUM; Q9UJY1; -.
DR ELM; Q9UJY1; -.
DR IntAct; Q9UJY1; 77.
DR MINT; Q9UJY1; -.
DR STRING; 9606.ENSP00000281938; -.
DR GlyGen; Q9UJY1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UJY1; -.
DR PhosphoSitePlus; Q9UJY1; -.
DR BioMuta; HSPB8; -.
DR DMDM; 13431576; -.
DR EPD; Q9UJY1; -.
DR jPOST; Q9UJY1; -.
DR MassIVE; Q9UJY1; -.
DR MaxQB; Q9UJY1; -.
DR PaxDb; Q9UJY1; -.
DR PeptideAtlas; Q9UJY1; -.
DR PRIDE; Q9UJY1; -.
DR ProteomicsDB; 84690; -.
DR Antibodypedia; 18895; 635 antibodies from 42 providers.
DR DNASU; 26353; -.
DR Ensembl; ENST00000281938.7; ENSP00000281938.3; ENSG00000152137.8.
DR GeneID; 26353; -.
DR KEGG; hsa:26353; -.
DR MANE-Select; ENST00000281938.7; ENSP00000281938.3; NM_014365.3; NP_055180.1.
DR UCSC; uc001txb.4; human.
DR CTD; 26353; -.
DR DisGeNET; 26353; -.
DR GeneCards; HSPB8; -.
DR GeneReviews; HSPB8; -.
DR HGNC; HGNC:30171; HSPB8.
DR HPA; ENSG00000152137; Tissue enhanced (skeletal).
DR MalaCards; HSPB8; -.
DR MIM; 158590; phenotype.
DR MIM; 608014; gene.
DR MIM; 608673; phenotype.
DR neXtProt; NX_Q9UJY1; -.
DR OpenTargets; ENSG00000152137; -.
DR Orphanet; 99945; Autosomal dominant Charcot-Marie-Tooth disease type 2L.
DR Orphanet; 476093; Autosomal dominant distal axonal motor neuropathy-myofibrillar myopathy syndrome.
DR Orphanet; 139525; Distal hereditary motor neuropathy type 2.
DR PharmGKB; PA134900173; -.
DR VEuPathDB; HostDB:ENSG00000152137; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000160605; -.
DR HOGENOM; CLU_095001_0_1_1; -.
DR InParanoid; Q9UJY1; -.
DR OMA; CVNVQSF; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; Q9UJY1; -.
DR TreeFam; TF105049; -.
DR PathwayCommons; Q9UJY1; -.
DR Reactome; R-HSA-3371571; HSF1-dependent transactivation.
DR SignaLink; Q9UJY1; -.
DR SIGNOR; Q9UJY1; -.
DR BioGRID-ORCS; 26353; 17 hits in 1079 CRISPR screens.
DR ChiTaRS; HSPB8; human.
DR GeneWiki; HSPB8; -.
DR GenomeRNAi; 26353; -.
DR Pharos; Q9UJY1; Tbio.
DR PRO; PR:Q9UJY1; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9UJY1; protein.
DR Bgee; ENSG00000152137; Expressed in skeletal muscle tissue of rectus abdominis and 194 other tissues.
DR ExpressionAtlas; Q9UJY1; baseline and differential.
DR Genevisible; Q9UJY1; HS.
DR GO; GO:0101031; C:chaperone complex; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:ARUK-UCL.
DR GO; GO:0034620; P:cellular response to unfolded protein; IMP:ARUK-UCL.
DR GO; GO:1905337; P:positive regulation of aggrephagy; IMP:ARUK-UCL.
DR CDD; cd06480; ACD_HspB8_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR043254; HSPB8.
DR InterPro; IPR042790; HspB8_ACD.
DR PANTHER; PTHR46906; PTHR46906; 1.
DR Pfam; PF00011; HSP20; 1.
DR PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW Chaperone; Charcot-Marie-Tooth disease; Cytoplasm; Disease variant;
KW Methylation; Neurodegeneration; Neuropathy; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..196
FT /note="Heat shock protein beta-8"
FT /id="PRO_0000125945"
FT DOMAIN 74..185
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 176..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPX0"
FT MOD_RES 63
FT /note="Phosphothreonine; by PKC; in vitro"
FT /evidence="ECO:0000269|PubMed:11816564"
FT MOD_RES 71
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK92"
FT MOD_RES 78
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK92"
FT VARIANT 67
FT /note="G -> S (in a glioblastoma multiforme sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042244"
FT VARIANT 78
FT /note="R -> M (in dbSNP:rs55826713)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042245"
FT VARIANT 90
FT /note="P -> L (in HMN2A; no effect on cytoskeleton
FT architecture; no effect on cytoplasmic location; no effect
FT on interaction with BAG3; dbSNP:rs1565927080)"
FT /evidence="ECO:0000269|PubMed:28144995"
FT /id="VAR_078133"
FT VARIANT 138
FT /note="N -> T (in HMN2A; no effect on cytoskeleton
FT architecture; no effect on cytoplasmic location; no effect
FT on interaction with BAG3; dbSNP:rs1565929080)"
FT /evidence="ECO:0000269|PubMed:28144995"
FT /id="VAR_078134"
FT VARIANT 141
FT /note="K -> E (in HMN2A; strengthen interaction with HSPB1;
FT dbSNP:rs104894351)"
FT /evidence="ECO:0000269|PubMed:15122253"
FT /id="VAR_018504"
FT VARIANT 141
FT /note="K -> M (in HMN2A; no effect on cytoskeleton
FT architecture; no effect on cytoplasmic location; increased
FT interaction with BAG3; dbSNP:rs1565929090)"
FT /evidence="ECO:0000269|PubMed:28144995"
FT /id="VAR_078135"
FT VARIANT 141
FT /note="K -> N (in HMN2A; strengthen interaction with HSPB1;
FT no effect on cytoskeleton architecture; no effect on
FT cytoplasmic location; increased interaction with BAG3;
FT dbSNP:rs104894345)"
FT /evidence="ECO:0000269|PubMed:15122253,
FT ECO:0000269|PubMed:15565283, ECO:0000269|PubMed:28144995"
FT /id="VAR_018505"
FT CONFLICT 51
FT /note="W -> C (in Ref. 3; AAD55359)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 196 AA; 21604 MW; B76058CED52292CB CRC64;
MADGQMPFSC HYPSRLRRDP FRDSPLSSRL LDDGFGMDPF PDDLTASWPD WALPRLSSAW
PGTLRSGMVP RGPTATARFG VPAEGRTPPP FPGEPWKVCV NVHSFKPEEL MVKTKDGYVE
VSGKHEEKQQ EGGIVSKNFT KKIQLPAEVD PVTVFASLSP EGLLIIEAPQ VPPYSTFGES
SFNNELPQDS QEVTCT
