GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Heat shock protein beta-8 (HspB8) (Alpha-crystallin C chain) (E2-induced gene 1 protein) (Protein kinase H11) (Small stress protein-like protein HSP22)

 HSPB8_HUMAN             Reviewed;         196 AA.
Q9UJY1; B2R6A6; Q6FIH3; Q9UKS3;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
02-JUN-2021, entry version 193.
RecName: Full=Heat shock protein beta-8;
Short=HspB8;
AltName: Full=Alpha-crystallin C chain;
AltName: Full=E2-induced gene 1 protein;
AltName: Full=Protein kinase H11;
AltName: Full=Small stress protein-like protein HSP22;
Name=HSPB8; Synonyms=CRYAC, E2IG1, HSP22; ORFNames=PP1629;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11085516;
Charpentier A.H., Bednarek A.K., Daniel R.L., Hawkins K.A., Laflin K.J.,
Gaddis S., MacLeod M.C., Aldaz C.M.;
"Effects of estrogen on global gene expression: identification of novel
targets of estrogen action.";
Cancer Res. 60:5977-5983(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH HSPB1.
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Melanoma;
PubMed=10833516; DOI=10.1074/jbc.m002140200;
Smith C.C., Yu Y.X., Kulka M., Aurelian L.;
"A novel human gene similar to the protein kinase (PK) coding domain of the
large subunit of herpes simplex virus type 2 ribonucleotide reductase
(ICP10) codes for a serine-threonine PK and is expressed in melanoma
cells.";
J. Biol. Chem. 275:25690-25699(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=11230166; DOI=10.1101/gr.gr1547r;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and analysis of
500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[6]
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thalamus;
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 [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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=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).
[11]
PHOSPHORYLATION AT THR-63, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11816564; DOI=10.1021/ac0104227;
Molloy M.P., Andrews P.C.;
"Phosphopeptide derivatization signatures to identify serine and threonine
phosphorylated peptides by mass spectrometry.";
Anal. Chem. 73:5387-5394(2001).
[12]
TISSUE SPECIFICITY.
PubMed=11470154; DOI=10.1016/s0167-4781(01)00237-8;
Kappe G., Verschuure P., Philipsen R.L.A., Staalduinen A.A.,
Van de Boogaart P., Boelens W.C., de Jong W.W.;
"Characterization of two novel human small heat shock proteins: protein
kinase-related HspB8 and testis-specific HspB9.";
Biochim. Biophys. Acta 1520:1-6(2001).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, 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).
[15]
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).
[16]
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).
[17]
INTERACTION WITH DNAJB6.
PubMed=22366786; DOI=10.1038/ng.1103;
Sarparanta J., Jonson P.H., Golzio C., Sandell S., Luque H., Screen M.,
McDonald K., Stajich J.M., Mahjneh I., Vihola A., Raheem O., Penttila S.,
Lehtinen S., Huovinen S., Palmio J., Tasca G., Ricci E., Hackman P.,
Hauser M., Katsanis N., Udd B.;
"Mutations affecting the cytoplasmic functions of the co-chaperone DNAJB6
cause limb-girdle muscular dystrophy.";
Nat. Genet. 44:450-455(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[19]
VARIANTS HMN2A GLU-141 AND ASN-141.
PubMed=15122253; DOI=10.1038/ng1328;
Irobi J., Van Impe K., Seeman P., Jordanova A., Dierick I., Verpoorten N.,
Michalik A., De Vriendt E., Jacobs A., Van Gerwen V., Vennekens K.,
Mazanec R., Tournev I., Hilton-Jones D., Talbot K., Kremensky I.,
Van Den Bosch L., Robberecht W., Van Vandekerckhove J., Broeckhoven C.,
Gettemans J., De Jonghe P., Timmerman V.;
"Hot-spot residue in small heat-shock protein 22 causes distal motor
neuropathy.";
Nat. Genet. 36:597-601(2004).
[20]
VARIANT CMT2L ASN-141.
PubMed=15565283; DOI=10.1007/s00439-004-1218-3;
Tang B.-S., Zhao G.-H., Luo W., Xia K., Cai F., Pan Q., Zhang R.-X.,
Zhang F.F., Liu X.-M., Chen B., Zhang C., Shen L., Jiang H., Long Z.G.,
Dai H.-P.;
"Small heat-shock protein 22 mutated in autosomal dominant Charcot-Marie-
Tooth disease type 2L.";
Hum. Genet. 116:222-224(2005).
[21]
VARIANTS [LARGE SCALE ANALYSIS] SER-67 AND MET-78.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[22]
VARIANTS HMN2A LEU-90; THR-138; ASN-141 AND MET-141, INTERACTION WITH BAG3,
SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS HMN2A LEU-90;
THR-138; ASN-141 AND MET-141.
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: Displays temperature-dependent chaperone activity.
-!- SUBUNIT: Monomer. Interacts with HSPB1. Interacts with DNAJB6.
Interacts with BAG3 (PubMed:28144995). {ECO:0000269|PubMed:11342557,
ECO:0000269|PubMed:22366786, ECO:0000269|PubMed:28144995}.
-!- INTERACTION:
Q9UJY1; O95817: BAG3; NbExp=10; IntAct=EBI-739074, EBI-747185;
Q9UJY1; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-739074, EBI-739879;
Q9UJY1; Q9UNI6: DUSP12; NbExp=3; IntAct=EBI-739074, EBI-715161;
Q9UJY1; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-739074, EBI-745689;
Q9UJY1; P04792: HSPB1; NbExp=3; IntAct=EBI-739074, EBI-352682;
Q9UJY1; Q16082: HSPB2; NbExp=3; IntAct=EBI-739074, EBI-739395;
Q9UJY1; Q9UBY9: HSPB7; NbExp=11; IntAct=EBI-739074, EBI-739361;
Q9UJY1; Q9UJY1: HSPB8; NbExp=6; IntAct=EBI-739074, EBI-739074;
Q9UJY1; Q8IVT2: MISP; NbExp=3; IntAct=EBI-739074, EBI-2555085;
Q9UJY1; Q15773: MLF2; NbExp=2; IntAct=EBI-739074, EBI-1051875;
Q9UJY1; Q9HC29-1: NOD2; NbExp=2; IntAct=EBI-739074, EBI-21496213;
Q9UJY1; Q2TAL8: QRICH1; NbExp=6; IntAct=EBI-739074, EBI-2798044;
Q9UJY1; P49247: RPIA; NbExp=3; IntAct=EBI-739074, EBI-744831;
Q9UJY1; O15375: SLC16A5; NbExp=3; IntAct=EBI-739074, EBI-12874738;
Q9UJY1; O14512: SOCS7; NbExp=3; IntAct=EBI-739074, EBI-1539606;
Q9UJY1; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-739074, EBI-8451480;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19464326,
ECO:0000269|PubMed:28144995}. Nucleus {ECO:0000269|PubMed:19464326}.
Note=Translocates to nuclear foci during heat shock.
-!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and
heart. {ECO:0000269|PubMed:11470154}.
-!- INDUCTION: By 17-beta-estradiol.
-!- DISEASE: Neuronopathy, distal hereditary motor, 2A (HMN2A)
[MIM:158590]: 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:15122253,
ECO:0000269|PubMed:28144995}. Note=The disease is caused by variants
affecting the gene represented in this entry.
-!- DISEASE: Charcot-Marie-Tooth disease 2L (CMT2L) [MIM:608673]: An 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.
{ECO:0000269|PubMed:15565283}. 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}.
-!- CAUTION: Was reported to have a protein kinase activity and to act as a
Mn(2+)-dependent serine-threonine-specific protein kinase.
{ECO:0000305|PubMed:10833516}.
-!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
URL="https://uantwerpen.vib.be/CMTMutations";
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; AF191017; AAF09481.1; -; mRNA.
EMBL; AF250138; AAF65562.1; -; mRNA.
EMBL; AF133207; AAD55359.1; -; mRNA.
EMBL; AL136936; CAB66870.1; -; mRNA.
EMBL; AF217987; AAG17230.1; -; mRNA.
EMBL; BT006876; AAP35522.1; -; mRNA.
EMBL; CR533453; CAG38484.1; -; mRNA.
EMBL; AK312501; BAG35403.1; -; mRNA.
EMBL; CH471054; EAW98144.1; -; Genomic_DNA.
EMBL; BC002673; AAH02673.1; -; mRNA.
CCDS; CCDS9189.1; -.
RefSeq; NP_055180.1; NM_014365.2.
SMR; Q9UJY1; -.
BioGRID; 117689; 52.
CORUM; Q9UJY1; -.
ELM; Q9UJY1; -.
IntAct; Q9UJY1; 45.
MINT; Q9UJY1; -.
STRING; 9606.ENSP00000281938; -.
iPTMnet; Q9UJY1; -.
PhosphoSitePlus; Q9UJY1; -.
BioMuta; HSPB8; -.
DMDM; 13431576; -.
EPD; Q9UJY1; -.
jPOST; Q9UJY1; -.
MassIVE; Q9UJY1; -.
MaxQB; Q9UJY1; -.
PaxDb; Q9UJY1; -.
PeptideAtlas; Q9UJY1; -.
PRIDE; Q9UJY1; -.
ProteomicsDB; 84690; -.
Antibodypedia; 18895; 618 antibodies.
DNASU; 26353; -.
Ensembl; ENST00000281938; ENSP00000281938; ENSG00000152137.
GeneID; 26353; -.
KEGG; hsa:26353; -.
UCSC; uc001txb.4; human.
CTD; 26353; -.
DisGeNET; 26353; -.
GeneCards; HSPB8; -.
GeneReviews; HSPB8; -.
HGNC; HGNC:30171; HSPB8.
HPA; ENSG00000152137; Tissue enhanced (skeletal).
MalaCards; HSPB8; -.
MIM; 158590; phenotype.
MIM; 608014; gene.
MIM; 608673; phenotype.
neXtProt; NX_Q9UJY1; -.
OpenTargets; ENSG00000152137; -.
Orphanet; 99945; Autosomal dominant Charcot-Marie-Tooth disease type 2L.
Orphanet; 476093; Autosomal dominant distal axonal motor neuropathy-myofibrillar myopathy syndrome.
Orphanet; 139525; Distal hereditary motor neuropathy type 2.
PharmGKB; PA134900173; -.
VEuPathDB; HostDB:ENSG00000152137.6; -.
eggNOG; KOG3591; Eukaryota.
GeneTree; ENSGT00940000160605; -.
HOGENOM; CLU_095001_0_1_1; -.
InParanoid; Q9UJY1; -.
OMA; CVNVQSF; -.
OrthoDB; 1187096at2759; -.
PhylomeDB; Q9UJY1; -.
TreeFam; TF105049; -.
PathwayCommons; Q9UJY1; -.
Reactome; R-HSA-3371571; HSF1-dependent transactivation.
SIGNOR; Q9UJY1; -.
BioGRID-ORCS; 26353; 10 hits in 991 CRISPR screens.
ChiTaRS; HSPB8; human.
GeneWiki; HSPB8; -.
GenomeRNAi; 26353; -.
Pharos; Q9UJY1; Tbio.
PRO; PR:Q9UJY1; -.
Proteomes; UP000005640; Chromosome 12.
RNAct; Q9UJY1; protein.
Bgee; ENSG00000152137; Expressed in quadriceps femoris and 232 other tissues.
ExpressionAtlas; Q9UJY1; baseline and differential.
Genevisible; Q9UJY1; HS.
GO; GO:0101031; C:chaperone complex; IDA:ARUK-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; IDA:ARUK-UCL.
GO; GO:0034620; P:cellular response to unfolded protein; IMP:ARUK-UCL.
GO; GO:1905337; P:positive regulation of aggrephagy; IMP:ARUK-UCL.
GO; GO:0006468; P:protein phosphorylation; IEA:GOC.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
CDD; cd06480; ACD_HspB8_like; 1.
Gene3D; 2.60.40.790; -; 1.
InterPro; IPR002068; A-crystallin/Hsp20_dom.
InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
InterPro; IPR008978; HSP20-like_chaperone.
InterPro; IPR043254; HSPB8.
InterPro; IPR042790; HspB8_ACD.
PANTHER; PTHR46906; PTHR46906; 1.
Pfam; PF00011; HSP20; 1.
PRINTS; PR00299; ACRYSTALLIN.
SUPFAM; SSF49764; SSF49764; 1.
PROSITE; PS01031; SHSP; 1.
1: Evidence at protein level;
Chaperone; Charcot-Marie-Tooth disease; Cytoplasm; Disease variant;
Methylation; Neurodegeneration; Neuropathy; Nucleus; Phosphoprotein;
Reference proteome; Stress response.
CHAIN 1..196
/note="Heat shock protein beta-8"
/id="PRO_0000125945"
DOMAIN 74..185
/note="sHSP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
REGION 176..196
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 24
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18220336,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
MOD_RES 57
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9EPX0"
MOD_RES 63
/note="Phosphothreonine; by PKC; in vitro"
/evidence="ECO:0000269|PubMed:11816564"
MOD_RES 71
/note="Asymmetric dimethylarginine"
/evidence="ECO:0000250|UniProtKB:Q9JK92"
MOD_RES 78
/note="Asymmetric dimethylarginine"
/evidence="ECO:0000250|UniProtKB:Q9JK92"
VARIANT 67
/note="G -> S (in a glioblastoma multiforme sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042244"
VARIANT 78
/note="R -> M (in dbSNP:rs55826713)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042245"
VARIANT 90
/note="P -> L (in HMN2A; no effect on cytoskeleton
architecture; no effect on cytoplasmic location; no effect
on interaction with BAG3; dbSNP:rs1565927080)"
/evidence="ECO:0000269|PubMed:28144995"
/id="VAR_078133"
VARIANT 138
/note="N -> T (in HMN2A; no effect on cytoskeleton
architecture; no effect on cytoplasmic location; no effect
on interaction with BAG3; dbSNP:rs1565929080)"
/evidence="ECO:0000269|PubMed:28144995"
/id="VAR_078134"
VARIANT 141
/note="K -> E (in HMN2A; strengthen interaction with HSPB1;
dbSNP:rs104894351)"
/evidence="ECO:0000269|PubMed:15122253"
/id="VAR_018504"
VARIANT 141
/note="K -> M (in HMN2A; no effect on cytoskeleton
architecture; no effect on cytoplasmic location; increased
interaction with BAG3; dbSNP:rs1565929090)"
/evidence="ECO:0000269|PubMed:28144995"
/id="VAR_078135"
VARIANT 141
/note="K -> N (in HMN2A; strengthen interaction with HSPB1;
no effect on cytoskeleton architecture; no effect on
cytoplasmic location; increased interaction with BAG3;
dbSNP:rs104894345)"
/evidence="ECO:0000269|PubMed:15122253,
ECO:0000269|PubMed:15565283, ECO:0000269|PubMed:28144995"
/id="VAR_018505"
CONFLICT 51
/note="W -> C (in Ref. 3; AAD55359)"
/evidence="ECO:0000305"
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


Related products :

Catalog number Product name Quantity
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.002 mg
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.01 mg
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.1 mg
18-003-42935 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg Protein A
18-003-43409 Heat shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg Protein A
E0693h ELISA 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive protein 96T
U0693h CLIA 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive protein 2 96T
10-782-55038 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.2 mg
10-782-55038 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.05 mg
E0693h ELISA kit 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive pro 96T
HSPB8 HSPB6 Gene heat shock protein, alpha-crystallin-related, B6
18-003-43520 HSPB1-associated protein 1 - 27 KdA heat shock protein-associated protein 1; Protein associated with small stress protein 1 Polyclonal 0.05 mg Aff Pur
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.05 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 1 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.01 mg
18-785-210206 HSP27 (Phospho-Ser78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210207 HSP27 (Phospho-Ser82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210205 HSP27 (Phospho-Ser15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210206 HSP27 (Phospho-Ser78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210207 HSP27 (Phospho-Ser82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210205 HSP27 (Phospho-Ser15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
CSB-E16666h Human heat shock protein beta-8 (HSPB8 per CRYAC per E2IG1 per HSP22 per PP1629) ELISA kit 96T
HH007 Human heat shock protein beta-8 (HSPB8 per CRYAC per E2IG1 per HSP22 per PP1629) ELISA kit 96T
18-785-210210 HSP27 (Ab-82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
10-002-38024 Hsp27 human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.1 mg
Pathways :
WP2199: Seed Development
WP210: Cytoplasmic Ribosomal Proteins
WP1566: Citrate cycle (TCA cycle)
WP1665: Limonene and pinene degradation
WP1502: Mitochondrial biogenesis
WP1673: Naphthalene and anthracene degradation
WP1493: Carbon assimilation C4 pathway
WP1531: Vitamin D synthesis
WP2218: sGC
WP1654: gamma-Hexachlorocyclohexane degradation
WP35: G Protein Signaling Pathways
WP813: G Protein Signaling Pathways
WP73: G Protein Signaling Pathways
WP1909: Signal regulatory protein (SIRP) family interactions
WP1678: Nucleotide excision repair
WP2371: Parkinsons Disease Pathway
WP525: Mitochondrial Unfolded-Protein Response
WP1644: DNA replication
WP1049: G Protein Signaling Pathways
WP1689: Porphyrin and chlorophyll metabolism
WP1613: 1,4-Dichlorobenzene degradation
WP1692: Protein export
WP2032: TSH signaling pathway
WP1657: Glycerolipid metabolism
WP1663: Homologous recombination

Related Genes :
[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)
[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)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[Hspb1 Hsp27] Heat shock protein beta-1 (HspB1) (Heat shock 27 kDa protein) (HSP 27)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[CRYAA CRYA1 HSPB4] Alpha-crystallin A chain (Heat shock protein beta-4) (HspB4) [Cleaved into: Alpha-crystallin A(1-172); Alpha-crystallin A(1-168); Alpha-crystallin A(1-162)]
[CRYAB CRYA2 HSPB5] Alpha-crystallin B chain (Alpha(B)-crystallin) (Heat shock protein beta-5) (HspB5) (Renal carcinoma antigen NY-REN-27) (Rosenthal fiber component)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[HSPB7 CVHSP] Heat shock protein beta-7 (HspB7) (Cardiovascular heat shock protein) (cvHsp)
[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)
[HSP90AB1 HSP90B HSPC2 HSPCB] Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84)
[tat] Protein Tat (Transactivating regulatory protein)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[ZC3H11 Tb927.5.810] RNA-binding protein ZC3H11 (CCCH zinc finger protein ZC3H11)
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[UBE2L6 UBCH8] Ubiquitin/ISG15-conjugating enzyme E2 L6 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme L6) (Retinoic acid-induced gene B protein) (RIG-B) (UbcH8) (Ubiquitin carrier protein L6) (Ubiquitin-protein ligase L6)
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[CRNN C1orf10 DRC1 PDRC1 SEP53] Cornulin (53 kDa putative calcium-binding protein) (53 kDa squamous epithelial-induced stress protein) (58 kDa heat shock protein) (Squamous epithelial heat shock protein 53) (Tumor-related protein)
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protp26663ein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]

Bibliography :
No related Items