HS71B_HUMAN
ID HS71B_HUMAN Reviewed; 641 AA.
AC P0DMV9; B4E3B6; P08107; P19790; Q5JQI4; Q5SP17; Q9UQL9; Q9UQM0;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Heat shock 70 kDa protein 1B {ECO:0000312|HGNC:HGNC:5233};
DE AltName: Full=Heat shock 70 kDa protein 2;
DE Short=HSP70-2 {ECO:0000303|PubMed:14656967, ECO:0000303|PubMed:2538825};
DE Short=HSP70.2;
GN Name=HSPA1B {ECO:0000312|HGNC:HGNC:5233};
GN Synonyms=HSP72 {ECO:0000303|PubMed:24318877};
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 [GENOMIC DNA].
RX PubMed=1700760; DOI=10.1007/bf00187095;
RA Milner C.M., Campbell R.D.;
RT "Structure and expression of the three MHC-linked HSP70 genes.";
RL Immunogenetics 32:242-251(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-499.
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-95; VAL-467 AND
RP SER-499.
RG NIEHS SNPs program;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Muscle, Pancreas, PNS, and Skin;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 360-424.
RX PubMed=2538825; DOI=10.1073/pnas.86.6.1968;
RA Sargent C.A., Dunham I., Trowsdale J., Campbell R.D.;
RT "Human major histocompatibility complex contains genes for the major heat
RT shock protein HSP70.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1968-1972(1989).
RN [8]
RP PROTEIN SEQUENCE OF 4-49; 57-71; 77-155; 160-187; 221-247; 273-311;
RP 326-342; 349-357; 362-416; 424-447; 459-469; 510-517; 540-550; 574-595 AND
RP 598-641, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 37-49; 57-71; 78-88; 113-126; 160-187; 221-247;
RP 302-311; 329-342; 349-357; 362-384; 540-550 AND 574-589, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 551-567, METHYLATION AT LYS-561, MUTAGENESIS OF
RP LYS-561, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine methyltransferases
RT preferentially interact with molecular chaperones to regulate their
RT activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
RN [11]
RP INTERACTION WITH TERT.
RX PubMed=11274138; DOI=10.1074/jbc.c100055200;
RA Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E.;
RT "Stable association of hsp90 and p23, but Not hsp70, with active human
RT telomerase.";
RL J. Biol. Chem. 276:15571-15574(2001).
RN [12]
RP INTERACTION WITH DNAJC7.
RX PubMed=12853476; DOI=10.1093/emboj/cdg362;
RA Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C.,
RA Obermann W.M.;
RT "Cofactor Tpr2 combines two TPR domains and a J domain to regulate the
RT Hsp70/Hsp90 chaperone system.";
RL EMBO J. 22:3613-3623(2003).
RN [13]
RP INTERACTION WITH TSC2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15963462; DOI=10.1016/j.bbrc.2005.05.175;
RA Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J.,
RA Luider T.M.;
RT "Phosphorylation and binding partner analysis of the TSC1-TSC2 complex.";
RL Biochem. Biophys. Res. Commun. 333:818-826(2005).
RN [14]
RP INTERACTION WITH PPP5C, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15383005; DOI=10.1042/bj20040690;
RA Zeke T., Morrice N., Vazquez-Martin C., Cohen P.T.;
RT "Human protein phosphatase 5 dissociates from heat-shock proteins and is
RT proteolytically activated in response to arachidonic acid and the
RT microtubule-depolymerizing drug nocodazole.";
RL Biochem. J. 385:45-56(2005).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [16]
RP INTERACTION WITH IRAK1BP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17233114; DOI=10.1089/dna.2006.25.704;
RA Haag Breese E., Uversky V.N., Georgiadis M.M., Harrington M.A.;
RT "The disordered amino-terminus of SIMPL interacts with members of the 70-
RT kDa heat-shock protein family.";
RL DNA Cell Biol. 25:704-714(2006).
RN [17]
RP FUNCTION AS A RECEPTOR FOR ROTAVIRUS A.
RX PubMed=16537599; DOI=10.1128/jvi.80.7.3322-3331.2006;
RA Perez-Vargas J., Romero P., Lopez S., Arias C.F.;
RT "The peptide-binding and ATPase domains of recombinant hsc70 are required
RT to interact with rotavirus and reduce its infectivity.";
RL J. Virol. 80:3322-3331(2006).
RN [18]
RP INTERACTION WITH DNAJC9.
RX PubMed=17182002; DOI=10.1016/j.bbrc.2006.12.013;
RA Han C., Chen T., Li N., Yang M., Wan T., Cao X.;
RT "HDJC9, a novel human type C DnaJ/HSP40 member interacts with and
RT cochaperones HSP70 through the J domain.";
RL Biochem. Biophys. Res. Commun. 353:280-285(2007).
RN [19]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [20]
RP INTERACTION WITH DNAJC7.
RX PubMed=18620420; DOI=10.1021/bi800770g;
RA Moffatt N.S., Bruinsma E., Uhl C., Obermann W.M., Toft D.;
RT "Role of the cochaperone Tpr2 in Hsp90 chaperoning.";
RL Biochemistry 47:8203-8213(2008).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108; LYS-246 AND LYS-348, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [24]
RP INTERACTION WITH TRIM5.
RX PubMed=20053985; DOI=10.1074/jbc.m109.040618;
RA Hwang C.Y., Holl J., Rajan D., Lee Y., Kim S., Um M., Kwon K.S., Song B.;
RT "Hsp70 interacts with the retroviral restriction factor TRIM5alpha and
RT assists the folding of TRIM5alpha.";
RL J. Biol. Chem. 285:7827-7837(2010).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631; SER-633 AND THR-636, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [26]
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 [27]
RP INTERACTION WITH CHCHD3.
RX PubMed=21081504; DOI=10.1074/jbc.m110.171975;
RA Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A.,
RA Perkins G.A., Ellisman M.H., Taylor S.S.;
RT "ChChd3, an inner mitochondrial membrane protein, is essential for
RT maintaining crista integrity and mitochondrial function.";
RL J. Biol. Chem. 286:2918-2932(2011).
RN [28]
RP FUNCTION, AND INTERACTION WITH ATF5.
RX PubMed=22528486; DOI=10.1074/jbc.m112.363622;
RA Liu X., Liu D., Qian D., Dai J., An Y., Jiang S., Stanley B., Yang J.,
RA Wang B., Liu X., Liu D.X.;
RT "Nucleophosmin (NPM1/B23) interacts with activating transcription factor 5
RT (ATF5) protein and promotes proteasome- and caspase-dependent ATF5
RT degradation in hepatocellular carcinoma cells.";
RL J. Biol. Chem. 287:19599-19609(2012).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH FOXP3.
RX PubMed=23973223; DOI=10.1016/j.immuni.2013.08.006;
RA Chen Z., Barbi J., Bu S., Yang H.Y., Li Z., Gao Y., Jinasena D., Fu J.,
RA Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J., Gao Z., Tian H.,
RA Li Y., Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J., Dang E., Li Z.,
RA Wang H., Luo W., Li L., Semenza G.L., Zheng S.G., Loser K., Tsun A.,
RA Greene M.I., Pardoll D.M., Pan F., Li B.;
RT "The ubiquitin ligase Stub1 negatively modulates regulatory T cell
RT suppressive activity by promoting degradation of the transcription factor
RT Foxp3.";
RL Immunity 39:272-285(2013).
RN [31]
RP METHYLATION AT LYS-561, MUTAGENESIS OF LYS-561, AND INTERACTION WITH
RP METTL21A.
RX PubMed=23921388; DOI=10.1074/jbc.m113.483248;
RA Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S.,
RA Melki R., Falnes P.O.;
RT "Identification and characterization of a novel human methyltransferase
RT modulating Hsp70 function through lysine methylation.";
RL J. Biol. Chem. 288:27752-27763(2013).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [33]
RP INTERACTION WITH PRKN.
RX PubMed=24270810; DOI=10.1038/nature12748;
RA Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A., Buehler E.,
RA Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E., Youle R.J.;
RT "High-content genome-wide RNAi screens identify regulators of parkin
RT upstream of mitophagy.";
RL Nature 504:291-295(2013).
RN [34]
RP REVIEW.
RX PubMed=24012426; DOI=10.1016/j.tibs.2013.08.001;
RA Mayer M.P.;
RT "Hsp70 chaperone dynamics and molecular mechanism.";
RL Trends Biochem. Sci. 38:507-514(2013).
RN [35]
RP FUNCTION, AND INTERACTION WITH STUB1 AND SMAD3.
RX PubMed=24613385; DOI=10.1016/j.bbrc.2014.02.124;
RA Shang Y., Xu X., Duan X., Guo J., Wang Y., Ren F., He D., Chang Z.;
RT "Hsp70 and Hsp90 oppositely regulate TGF-beta signaling through
RT CHIP/Stub1.";
RL Biochem. Biophys. Res. Commun. 446:387-392(2014).
RN [36]
RP FUNCTION, AND INTERACTION WITH BAG1; BAG2; BAG3 AND HSPH1.
RX PubMed=24318877; DOI=10.1074/jbc.m113.521997;
RA Rauch J.N., Gestwicki J.E.;
RT "Binding of human nucleotide exchange factors to heat shock protein 70
RT (Hsp70) generates functionally distinct complexes in vitro.";
RL J. Biol. Chem. 289:1402-1414(2014).
RN [37]
RP INTERACTION WITH NOD2.
RX PubMed=24790089; DOI=10.1074/jbc.m114.557686;
RA Mohanan V., Grimes C.L.;
RT "The molecular chaperone HSP70 binds to and stabilizes NOD2, an important
RT protein involved in Crohn disease.";
RL J. Biol. Chem. 289:18987-18998(2014).
RN [38]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [39]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-469 AND LYS-561, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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).
RN [40]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [41]
RP INTERACTION WITH DNAJC8.
RX PubMed=27133716; DOI=10.1016/j.bbrc.2016.03.152;
RA Ito N., Kamiguchi K., Nakanishi K., Sokolovskya A., Hirohashi Y.,
RA Tamura Y., Murai A., Yamamoto E., Kanaseki T., Tsukahara T., Kochin V.,
RA Chiba S., Shimohama S., Sato N., Torigoe T.;
RT "A novel nuclear DnaJ protein, DNAJC8, can suppress the formation of
RT spinocerebellar ataxia 3 polyglutamine aggregation in a J-domain
RT independent manner.";
RL Biochem. Biophys. Res. Commun. 474:626-633(2016).
RN [42]
RP REVIEW.
RX PubMed=26865365; DOI=10.1007/s12192-016-0676-6;
RA Radons J.;
RT "The human HSP70 family of chaperones: where do we stand?";
RL Cell Stress Chaperones 21:379-404(2016).
RN [43]
RP FUNCTION, INTERACTION WITH NEDD1, AND SUBCELLULAR LOCATION.
RX PubMed=27137183; DOI=10.1007/s00018-016-2236-8;
RA Fang C.T., Kuo H.H., Pan T.S., Yu F.C., Yih L.H.;
RT "HSP70 regulates the function of mitotic centrosomes.";
RL Cell. Mol. Life Sci. 73:3949-3960(2016).
RN [44]
RP FUNCTION, ACETYLATION AT LYS-77, MUTAGENESIS OF LYS-77, AND INTERACTION
RP WITH NAA10; HSP40; HOPX; STUB1; HSP90 AND HDAC4.
RX PubMed=27708256; DOI=10.1038/ncomms12882;
RA Seo J.H., Park J.H., Lee E.J., Vo T.T., Choi H., Kim J.Y., Jang J.K.,
RA Wee H.J., Lee H.S., Jang S.H., Park Z.Y., Jeong J., Lee K.J., Seok S.H.,
RA Park J.Y., Lee B.J., Lee M.N., Oh G.T., Kim K.W.;
RT "ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding
RT and degradation.";
RL Nat. Commun. 7:12882-12882(2016).
RN [45]
RP INTERACTION WITH DNJC9.
RX PubMed=33857403; DOI=10.1016/j.molcel.2021.03.041;
RA Hammond C.M., Bao H., Hendriks I.A., Carraro M., Garcia-Nieto A., Liu Y.,
RA Reveron-Gomez N., Spanos C., Chen L., Rappsilber J., Nielsen M.L.,
RA Patel D.J., Huang H., Groth A.;
RT "DNAJC9 integrates heat shock molecular chaperones into the histone
RT chaperone network.";
RL Mol. Cell 0:0-0(2021).
RN [46]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-382 IN COMPLEX WITH ADP, AND
RP ATP-BINDING.
RX PubMed=10216320; DOI=10.1107/s0907444999002103;
RA Osipiuk J., Walsh M.A., Freeman B.C., Morimoto R.I., Joachimiak A.;
RT "Structure of a new crystal form of human hsp70 ATPase domain.";
RL Acta Crystallogr. D 55:1105-1107(1999).
RN [47]
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 389-641 IN COMPLEX WITH ATP
RP ANALOG, AND ATP-BINDING.
RX PubMed=20179333; DOI=10.1107/s0907444909053979;
RA Shida M., Arakawa A., Ishii R., Kishishita S., Takagi T.,
RA Kukimoto-Niino M., Sugano S., Tanaka A., Shirouzu M., Yokoyama S.;
RT "Direct inter-subdomain interactions switch between the closed and open
RT forms of the Hsp70 nucleotide-binding domain in the nucleotide-free
RT state.";
RL Acta Crystallogr. D 66:223-232(2010).
RN [48]
RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 1-387 IN COMPLEX WITH ADP, AND
RP ATP-BINDING.
RX PubMed=20072699; DOI=10.1371/journal.pone.0008625;
RA Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T.,
RA Moche M., Schuler H.;
RT "Crystal structures of the ATPase domains of four human Hsp70 isoforms:
RT HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78.";
RL PLoS ONE 5:E8625-E8625(2010).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-388 IN COMPLEX WITH BAG5.
RX PubMed=20223214; DOI=10.1016/j.str.2010.01.004;
RA Arakawa A., Handa N., Ohsawa N., Shida M., Kigawa T., Hayashi F.,
RA Shirouzu M., Yokoyama S.;
RT "The C-terminal BAG domain of BAG5 induces conformational changes of the
RT Hsp70 nucleotide-binding domain for ADP-ATP exchange.";
RL Structure 18:309-319(2010).
RN [50]
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 1-388, ATP-BINDING, AND
RP MUTAGENESIS OF ASP-10 AND ASP-199.
RX PubMed=21608060; DOI=10.1002/pro.663;
RA Arakawa A., Handa N., Shirouzu M., Yokoyama S.;
RT "Biochemical and structural studies on the high affinity of Hsp70 for
RT ADP.";
RL Protein Sci. 20:1367-1379(2011).
CC -!- FUNCTION: Molecular chaperone implicated in a wide variety of cellular
CC processes, including protection of the proteome from stress, folding
CC and transport of newly synthesized polypeptides, activation of
CC proteolysis of misfolded proteins and the formation and dissociation of
CC protein complexes. Plays a pivotal role in the protein quality control
CC system, ensuring the correct folding of proteins, the re-folding of
CC misfolded proteins and controlling the targeting of proteins for
CC subsequent degradation. This is achieved through cycles of ATP binding,
CC ATP hydrolysis and ADP release, mediated by co-chaperones. The co-
CC chaperones have been shown to not only regulate different steps of the
CC ATPase cycle, but they also have an individual specificity such that
CC one co-chaperone may promote folding of a substrate while another may
CC promote degradation. The affinity for polypeptides is regulated by its
CC nucleotide bound state. In the ATP-bound form, it has a low affinity
CC for substrate proteins. However, upon hydrolysis of the ATP to ADP, it
CC undergoes a conformational change that increases its affinity for
CC substrate proteins. It goes through repeated cycles of ATP hydrolysis
CC and nucleotide exchange, which permits cycles of substrate binding and
CC release. The co-chaperones are of three types: J-domain co-chaperones
CC such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide
CC exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70
CC from the ADP-bound to the ATP-bound state thereby promoting substrate
CC release), and the TPR domain chaperones such as HOPX and STUB1
CC (PubMed:24012426, PubMed:26865365, PubMed:24318877). Maintains protein
CC homeostasis during cellular stress through two opposing mechanisms:
CC protein refolding and degradation. Its acetylation/deacetylation state
CC determines whether it functions in protein refolding or protein
CC degradation by controlling the competitive binding of co-chaperones
CC HOPX and STUB1. During the early stress response, the acetylated form
CC binds to HOPX which assists in chaperone-mediated protein refolding,
CC thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that
CC promotes ubiquitin-mediated protein degradation (PubMed:27708256).
CC Regulates centrosome integrity during mitosis, and is required for the
CC maintenance of a functional mitotic centrosome that supports the
CC assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances
CC STUB1-mediated SMAD3 ubiquitination and degradation and facilitates
CC STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385).
CC Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in
CC regulatory T-cells (Treg) during inflammation (PubMed:23973223).
CC {ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23973223,
CC ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24613385,
CC ECO:0000269|PubMed:27137183, ECO:0000269|PubMed:27708256,
CC ECO:0000303|PubMed:24012426, ECO:0000303|PubMed:26865365}.
CC -!- FUNCTION: (Microbial infection) In case of rotavirus A infection,
CC serves as a post-attachment receptor for the virus to facilitate entry
CC into the cell. {ECO:0000269|PubMed:16537599}.
CC -!- SUBUNIT: May be an auxiliary component of the CatSper complex.
CC Identified in a IGF2BP1-dependent mRNP granule complex containing
CC untranslated mRNAs (PubMed:17289661). Interacts with CHCHD3, DNAJC7,
CC IRAK1BP1, PPP5C and TSC2 (PubMed:21081504, PubMed:12853476,
CC PubMed:18620420, PubMed:17233114, PubMed:15383005, PubMed:15963462).
CC Interacts with TERT; the interaction occurs in the absence of the RNA
CC component, TERC, and dissociates once the TERT complex has formed
CC (PubMed:11274138). Interacts with TRIM5 (via B30.2/SPRY domain)
CC (PubMed:20053985). Interacts with METTL21A (PubMed:23921388). Interacts
CC with PRKN (PubMed:24270810). Interacts with FOXP3 (PubMed:23973223).
CC Interacts with NOD2; the interaction enhances NOD2 stability
CC (PubMed:24790089). Interacts with DNAJC9 (via J domain)
CC (PubMed:17182002, PubMed:33857403). Interacts with ATF5; the
CC interaction protects ATF5 from degradation via proteasome-dependent and
CC caspase-dependent processes (PubMed:22528486). Interacts with NAA10,
CC HSP40, HSP90 and HDAC4. The acetylated form and the non-acetylated form
CC interact with HOPX and STUB1 respectively (PubMed:27708256). Interacts
CC with NEDD1 (PubMed:27137183). Interacts (via NBD) with BAG1, BAG2, BAG3
CC and HSPH1/HSP105 (PubMed:24318877). Interacts with SMAD3
CC (PubMed:24613385). Interacts with DNAJC8 (PubMed:27133716).
CC {ECO:0000269|PubMed:10216320, ECO:0000269|PubMed:11274138,
CC ECO:0000269|PubMed:12853476, ECO:0000269|PubMed:15383005,
CC ECO:0000269|PubMed:15963462, ECO:0000269|PubMed:17182002,
CC ECO:0000269|PubMed:17233114, ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:18620420, ECO:0000269|PubMed:20053985,
CC ECO:0000269|PubMed:20072699, ECO:0000269|PubMed:20179333,
CC ECO:0000269|PubMed:20223214, ECO:0000269|PubMed:21081504,
CC ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23921388,
CC ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:24270810,
CC ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24613385,
CC ECO:0000269|PubMed:24790089, ECO:0000269|PubMed:27133716,
CC ECO:0000269|PubMed:27137183, ECO:0000269|PubMed:27708256,
CC ECO:0000269|PubMed:33857403}.
CC -!- INTERACTION:
CC P0DMV9; P55085: F2RL1; NbExp=2; IntAct=EBI-14100688, EBI-4303189;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:27137183}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs.
CC -!- TISSUE SPECIFICITY: HSPA1B is testis-specific.
CC -!- INDUCTION: By heat shock.
CC -!- DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known as
CC the ATPase domain) is responsible for binding and hydrolyzing ATP. The
CC C-terminal substrate-binding domain (SBD) (also known as peptide-
CC binding domain) binds to the client/substrate proteins. The two domains
CC are allosterically coupled so that, when ATP is bound to the NBD, the
CC SBD binds relatively weakly to clients. When ADP is bound in the NBD, a
CC conformational change enhances the affinity of the SBD for client
CC proteins. {ECO:0000305|PubMed:24012426, ECO:0000305|PubMed:26865365}.
CC -!- PTM: In response to cellular stress, acetylated at Lys-77 by NA110 and
CC then gradually deacetylated by HDAC4 at later stages. Acetylation
CC enhances its chaperone activity and also determines whether it will
CC function as a chaperone for protein refolding or degradation by
CC controlling its binding to co-chaperones HOPX and STUB1. The acetylated
CC form and the non-acetylated form bind to HOPX and STUB1 respectively.
CC Acetylation also protects cells against various types of cellular
CC stress. {ECO:0000269|PubMed:27708256}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hspa1b/";
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DR EMBL; M59830; AAA63227.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63299.1; -; Genomic_DNA.
DR EMBL; AF134726; AAD21815.1; -; Genomic_DNA.
DR EMBL; DQ388429; ABD48956.1; -; Genomic_DNA.
DR EMBL; AL671762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009322; AAH09322.1; -; mRNA.
DR EMBL; BC018740; AAH18740.1; -; mRNA.
DR EMBL; BC057397; AAH57397.1; -; mRNA.
DR EMBL; BC063507; AAH63507.1; -; mRNA.
DR EMBL; M24744; AAA59845.1; -; Genomic_DNA.
DR CCDS; CCDS34415.1; -.
DR PIR; A29160; A29160.
DR PIR; A45871; A45871.
DR PIR; I59139; I59139.
DR PIR; I79540; I79540.
DR RefSeq; NP_005336.3; NM_005345.5.
DR RefSeq; NP_005337.2; NM_005346.4.
DR PDB; 4J8F; X-ray; 2.70 A; A=1-382, A=384-600.
DR PDB; 6FDT; NMR; -; B=633-641.
DR PDBsum; 4J8F; -.
DR PDBsum; 6FDT; -.
DR AlphaFoldDB; P0DMV9; -.
DR BMRB; P0DMV9; -.
DR SMR; P0DMV9; -.
DR CORUM; P0DMV9; -.
DR IntAct; P0DMV9; 13.
DR MINT; P0DMV9; -.
DR BindingDB; P0DMV9; -.
DR ChEMBL; CHEMBL3885585; -.
DR GlyConnect; 1296; 2 N-Linked glycans (2 sites).
DR GlyGen; P0DMV9; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P0DMV9; -.
DR MetOSite; P0DMV9; -.
DR SwissPalm; P0DMV9; -.
DR BioMuta; HSPA1B; -.
DR REPRODUCTION-2DPAGE; IPI00304925; -.
DR EPD; P0DMV9; -.
DR jPOST; P0DMV9; -.
DR MassIVE; P0DMV9; -.
DR MaxQB; P0DMV9; -.
DR PRIDE; P0DMV9; -.
DR Antibodypedia; 65941; 111 antibodies from 14 providers.
DR DNASU; 3303; -.
DR Ensembl; ENST00000375650.5; ENSP00000364801.3; ENSG00000204388.7.
DR Ensembl; ENST00000391548.1; ENSP00000375391.1; ENSG00000224501.5.
DR Ensembl; ENST00000391555.1; ENSP00000375399.1; ENSG00000212866.6.
DR Ensembl; ENST00000445736.1; ENSP00000403530.1; ENSG00000231555.4.
DR Ensembl; ENST00000450744.1; ENSP00000393087.1; ENSG00000232804.5.
DR GeneID; 3303; -.
DR GeneID; 3304; -.
DR KEGG; hsa:3303; -.
DR KEGG; hsa:3304; -.
DR MANE-Select; ENST00000375650.5; ENSP00000364801.3; NM_005346.6; NP_005337.2.
DR MANE-Select; ENST00000375651.7; ENSP00000364802.5; NM_005345.6; NP_005336.3.
DR CTD; 3303; -.
DR CTD; 3304; -.
DR DisGeNET; 3303; -.
DR DisGeNET; 3304; -.
DR GeneCards; HSPA1B; -.
DR HGNC; HGNC:5233; HSPA1B.
DR HPA; ENSG00000204388; Low tissue specificity.
DR MIM; 140550; gene.
DR MIM; 603012; gene.
DR neXtProt; NX_P0DMV9; -.
DR OpenTargets; ENSG00000204388; -.
DR OpenTargets; ENSG00000204389; -.
DR VEuPathDB; HostDB:ENSG00000204388; -.
DR GeneTree; ENSGT00940000161215; -.
DR OMA; SHIHEIV; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; P0DMV9; -.
DR PathwayCommons; P0DMV9; -.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-3371568; Attenuation phase.
DR Reactome; R-HSA-3371571; HSF1-dependent transactivation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P0DMV9; -.
DR SIGNOR; P0DMV9; -.
DR BioGRID-ORCS; 3303; 19 hits in 653 CRISPR screens.
DR BioGRID-ORCS; 3304; 7 hits in 641 CRISPR screens.
DR ChiTaRS; HSPA1B; human.
DR Pharos; P0DMV9; Tbio.
DR PRO; PR:P0DMV9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P0DMV9; protein.
DR Bgee; ENSG00000204388; Expressed in lower esophagus mucosa and 95 other tissues.
DR ExpressionAtlas; P0DMV9; baseline and differential.
DR GO; GO:0016235; C:aggresome; IDA:UniProtKB.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016234; C:inclusion body; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; TAS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0140545; F:ATP-dependent protein disaggregase activity; IDA:BHF-UCL.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0055131; F:C3HC4-type RING finger domain binding; IPI:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IDA:BHF-UCL.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0046034; P:ATP metabolic process; IDA:BHF-UCL.
DR GO; GO:0070370; P:cellular heat acclimation; IMP:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; TAS:ParkinsonsUK-UCL.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; TAS:Reactome.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:BHF-UCL.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; IDA:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:UniProtKB.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0042026; P:protein refolding; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IDA:BHF-UCL.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR DisProt; DP02353; -.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Host cell receptor for virus entry;
KW Host-virus interaction; Methylation; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..641
FT /note="Heat shock 70 kDa protein 1B"
FT /id="PRO_0000433115"
FT REGION 2..386
FT /note="Nucleotide-binding domain (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT REGION 394..509
FT /note="Substrate-binding domain (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT REGION 614..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 12..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 202..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 268..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 339..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:27708256"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 246
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 348
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 469
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 561
FT /note="N6,N6,N6-trimethyllysine; by METTL21A; alternate"
FT /evidence="ECO:0000269|PubMed:23349634,
FT ECO:0000269|PubMed:23921388, ECO:0007744|PubMed:24129315"
FT MOD_RES 561
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 636
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VARIANT 95
FT /note="I -> V"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_032152"
FT VARIANT 467
FT /note="A -> V (in dbSNP:rs538280104)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_032153"
FT VARIANT 499
FT /note="N -> S (in dbSNP:rs483638)"
FT /evidence="ECO:0000269|PubMed:14656967, ECO:0000269|Ref.4"
FT /id="VAR_029054"
FT MUTAGEN 10
FT /note="D->A: Reduces affinity for ADP."
FT /evidence="ECO:0000269|PubMed:21608060"
FT MUTAGEN 77
FT /note="K->Q: No loss of acetylation and ATPase activity.
FT Exhibits normal protein refolding activity during the early
FT phase but exhibits defects in ubiquitin-mediated protein
FT degradation during the later phase."
FT /evidence="ECO:0000269|PubMed:27708256"
FT MUTAGEN 77
FT /note="K->R: Significant loss of acetylation and ATPase
FT activity. Decreased binding to HOPX and HSP90 and increased
FT binding to STUB1 and NAA10. Impaired capacity for protein
FT refolding during the early phase after stress but shows
FT normal protein degradation activity in the late phase."
FT /evidence="ECO:0000269|PubMed:27708256"
FT MUTAGEN 199
FT /note="D->A: Reduces affinity for ADP."
FT /evidence="ECO:0000269|PubMed:21608060"
FT MUTAGEN 561
FT /note="K->R: Complete loss of in vitro methylation by
FT METTL21A."
FT /evidence="ECO:0000269|PubMed:23349634,
FT ECO:0000269|PubMed:23921388"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:6FDT"
SQ SEQUENCE 641 AA; 70052 MW; 78F513118C96DE66 CRC64;
MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGE TKAFYPEEIS
SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN
ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE
QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D
