HSPB8_MOUSE
ID HSPB8_MOUSE Reviewed; 196 AA.
AC Q9JK92;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Heat shock protein beta-8;
DE Short=HspB8;
DE AltName: Full=Alpha-crystallin C chain;
DE AltName: Full=Small stress protein-like protein HSP22;
GN Name=Hspb8; Synonyms=Cryac, Hsp22;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH HSPB1.
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=CD-1; TISSUE=Decidua;
RX PubMed=11133685; DOI=10.1095/biolreprod64.1.284;
RA Bany B.M., Schultz G.A.;
RT "Increased expression of a novel heat shock protein transcript in the mouse
RT uterus during decidualization and in response to progesterone.";
RL Biol. Reprod. 64:284-292(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-71 AND ARG-78, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Displays temperature-dependent chaperone activity.
CC -!- SUBUNIT: Monomer. Interacts with HSPB1 (By similarity). Interacts with
CC DNAJB6 (By similarity). Interacts with BAG3 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UJY1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UJY1}. Nucleus
CC {ECO:0000250|UniProtKB:Q9UJY1}. Note=Translocates to nuclear foci
CC during heat shock. {ECO:0000250|UniProtKB:Q9UJY1}.
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart, uterus,
CC liver, lung and ovary. Low levels found in stomach and brain. Not
CC detected in small intestine, large intestine, kidney, spleen and
CC testis. In the ovary, expression is concentrated in the endometrium and
CC in the connective tissue between the circular and longitudinal muscles
CC of the myometrium. {ECO:0000269|PubMed:11133685}.
CC -!- DEVELOPMENTAL STAGE: Detected in developing heart throughout embryonic
CC development but only detected in developing liver close to time of
CC birth. In the adult ovary, expression is highest during decidualization
CC and early pregnancy. {ECO:0000269|PubMed:11133685}.
CC -!- INDUCTION: By progesterone. {ECO:0000269|PubMed:11133685}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; AF250139; AAF65563.1; -; mRNA.
DR EMBL; AF273453; AAG00233.1; -; mRNA.
DR EMBL; AK005052; BAB23778.1; -; mRNA.
DR EMBL; BC011219; AAH11219.1; -; mRNA.
DR CCDS; CCDS19600.1; -.
DR RefSeq; NP_109629.1; NM_030704.3.
DR AlphaFoldDB; Q9JK92; -.
DR SMR; Q9JK92; -.
DR BioGRID; 219831; 3.
DR IntAct; Q9JK92; 1.
DR MINT; Q9JK92; -.
DR STRING; 10090.ENSMUSP00000037007; -.
DR iPTMnet; Q9JK92; -.
DR PhosphoSitePlus; Q9JK92; -.
DR MaxQB; Q9JK92; -.
DR PaxDb; Q9JK92; -.
DR PeptideAtlas; Q9JK92; -.
DR PRIDE; Q9JK92; -.
DR ProteomicsDB; 273322; -.
DR Antibodypedia; 18895; 635 antibodies from 42 providers.
DR DNASU; 80888; -.
DR Ensembl; ENSMUST00000036991; ENSMUSP00000037007; ENSMUSG00000041548.
DR GeneID; 80888; -.
DR KEGG; mmu:80888; -.
DR UCSC; uc008zez.1; mouse.
DR CTD; 26353; -.
DR MGI; MGI:2135756; Hspb8.
DR VEuPathDB; HostDB:ENSMUSG00000041548; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000160605; -.
DR HOGENOM; CLU_095001_0_1_1; -.
DR InParanoid; Q9JK92; -.
DR OMA; CVNVQSF; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; Q9JK92; -.
DR TreeFam; TF105049; -.
DR Reactome; R-MMU-3371571; HSF1-dependent transactivation.
DR BioGRID-ORCS; 80888; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Hspb8; mouse.
DR PRO; PR:Q9JK92; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JK92; protein.
DR Bgee; ENSMUSG00000041548; Expressed in gastrula and 269 other tissues.
DR Genevisible; Q9JK92; MM.
DR GO; GO:0101031; C:chaperone complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0034620; P:cellular response to unfolded protein; ISO:MGI.
DR GO; GO:1905337; P:positive regulation of aggrephagy; ISO:MGI.
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; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..196
FT /note="Heat shock protein beta-8"
FT /id="PRO_0000125947"
FT DOMAIN 78..185
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJY1"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPX0"
FT MOD_RES 63
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJY1"
FT MOD_RES 71
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 78
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
SQ SEQUENCE 196 AA; 21533 MW; ADE847E9E70D7DAC CRC64;
MADGQLPFPC SYPSRLRRDP FRDSPLSSRL LDDGFGMDPF PDDLTAPWPE WALPRLSSAW
PGTLRSGMVP RGPPATARFG VPAEGRSPPP FPGEPWKVCV NVHSFKPEEL MVKTKDGYVE
VSGKHEEKQQ EGGIVSKNFT KKIQLPAEVD PATVFASLSP EGLLIIEAPQ VPPYSPFGES
SFNNELPQDN QEVTCS
