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 30-NOV-2016, entry version 16.
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};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Campbell R.D., 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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
RT project: 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
RT heat 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
RP AND 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
RP IDENTIFICATION 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
RT methyltransferases preferentially interact with molecular chaperones
RT to regulate their 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
RT 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
RT is 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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
RT 70-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
RT required 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
RT the 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
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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,
RP AND 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.,
RA Walther T.C., 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.,
RA 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
RP THR-636, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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
RT factor 5 (ATF5) protein and promotes proteasome- and caspase-dependent
RT ATF5 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.,
RA Fischer-Posovszky P., Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion
RT profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH
RP 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.,
RA Fu J., Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J.,
RA Gao Z., Tian H., Li Y., Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J.,
RA Dang E., Li Z., Wang H., Luo W., Li L., Semenza G.L., Zheng S.G.,
RA Loser K., Tsun A., 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
RT factor 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
RT methyltransferase modulating Hsp70 function through lysine
RT 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 PARK2.
RX PubMed=24270810; DOI=10.1038/nature12748;
RA Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A.,
RA Buehler E., Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E.,
RA 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 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
RT important protein involved in Crohn disease.";
RL J. Biol. Chem. 289:18987-18998(2014).
RN [35]
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.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [36]
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.,
RA Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA Vemulapalli V., 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 [37]
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.,
RA Ayoub D., 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 [38]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-382 IN COMPLEX WITH ADP,
RP AND 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 [39]
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
RT open forms of the Hsp70 nucleotide-binding domain in the nucleotide-
RT free state.";
RL Acta Crystallogr. D 66:223-232(2010).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 1-387 IN COMPLEX WITH ADP,
RP AND 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
RT isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and
RT HSPA5/BiP/GRP78.";
RL PLoS ONE 5:E8625-E8625(2010).
RN [41]
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
RT the Hsp70 nucleotide-binding domain for ADP-ATP exchange.";
RL Structure 18:309-319(2010).
RN [42]
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: In cooperation with other chaperones, Hsp70s stabilize
CC preexistent proteins against aggregation and mediate the folding
CC of newly translated polypeptides in the cytosol as well as within
CC organelles. These chaperones participate in all these processes
CC through their ability to recognize nonnative conformations of
CC other proteins. They bind extended peptide segments with a net
CC hydrophobic character exposed by polypeptides during translation
CC and membrane translocation, or following stress-induced damage. In
CC case of rotavirus A infection, serves as a post-attachment
CC receptor for the virus to facilitate entry into the cell.
CC Essential for STUB1-mediated ubiquitination and degradation of
CC FOXP3 in regulatory T-cells (Treg) during inflammation
CC (PubMed:23973223). {ECO:0000269|PubMed:16537599,
CC ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23973223}.
CC -!- SUBUNIT: Component of the CatSper complex. Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated
CC mRNAs (PubMed:17289661). Interacts with CHCHD3, DNAJC7, IRAK1BP1,
CC PPP5C and TSC2 (PubMed:21081504, PubMed:12853476, PubMed:18620420,
CC PubMed:17233114, PubMed:15383005, PubMed:15963462). Interacts with
CC TERT; the interaction occurs in the absence of the RNA component,
CC 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).
CC Interacts with PARK2 (PubMed:24270810). Interacts with FOXP3
CC (PubMed:23973223). Interacts with NOD2; the interaction enhances
CC NOD2 stability (PubMed:24790089). Interacts with DNAJC9 (via J
CC domain) (PubMed:17182002). Interacts with ATF5; the interaction
CC protects ATF5 from degradation via proteasome-dependent and
CC caspase-dependent processes (PubMed:22528486).
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:24790089}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661}.
CC Note=Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs.
CC -!- TISSUE SPECIFICITY: HSPA1B is testis-specific.
CC -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hspa1b/";
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 UniGene; Hs.274402; -.
DR UniGene; Hs.702139; -.
DR UniGene; Hs.719966; -.
DR UniGene; Hs.743411; -.
DR PDB; 4J8F; X-ray; 2.70 A; A=1-382, A=384-600.
DR PDBsum; 4J8F; -.
DR ProteinModelPortal; P0DMV9; -.
DR SMR; P0DMV9; -.
DR MINT; MINT-96699; -.
DR BindingDB; P0DMV9; -.
DR iPTMnet; P0DMV9; -.
DR DMDM; 147744565; -.
DR REPRODUCTION-2DPAGE; IPI00304925; -.
DR MaxQB; P0DMV9; -.
DR PRIDE; P0DMV9; -.
DR DNASU; 3303; -.
DR Ensembl; ENST00000375650; ENSP00000364801; ENSG00000204388.
DR Ensembl; ENST00000391548; ENSP00000375391; ENSG00000224501.
DR Ensembl; ENST00000391555; ENSP00000375399; ENSG00000212866.
DR Ensembl; ENST00000445736; ENSP00000403530; ENSG00000231555.
DR Ensembl; ENST00000450744; ENSP00000393087; ENSG00000232804.
DR GeneID; 3303; -.
DR GeneID; 3304; -.
DR KEGG; hsa:3303; -.
DR KEGG; hsa:3304; -.
DR CTD; 3303; -.
DR CTD; 3304; -.
DR H-InvDB; HIX0058169; -.
DR H-InvDB; HIX0058187; -.
DR H-InvDB; HIX0166160; -.
DR HGNC; HGNC:5233; HSPA1B.
DR HPA; HPA052504; -.
DR MIM; 140550; gene.
DR MIM; 603012; gene.
DR neXtProt; NX_P0DMV9; -.
DR OpenTargets; ENSG00000204388; -.
DR OpenTargets; ENSG00000204389; -.
DR OpenTargets; ENSG00000212866; -.
DR OpenTargets; ENSG00000224501; -.
DR OpenTargets; ENSG00000231555; -.
DR OpenTargets; ENSG00000232804; -.
DR OpenTargets; ENSG00000234475; -.
DR OpenTargets; ENSG00000235941; -.
DR OpenTargets; ENSG00000237724; -.
DR GeneTree; ENSGT00820000127001; -.
DR HOGENOM; HOG000228135; -.
DR HOVERGEN; HBG051845; -.
DR KO; K03283; -.
DR OrthoDB; EOG091G03SF; -.
DR PhylomeDB; P0DMV9; -.
DR TreeFam; TF105042; -.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-3371568; Attenuation phase.
DR Reactome; R-HSA-3371571; HSF1-dependent transactivation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR ChiTaRS; HSPA1A; human.
DR ChiTaRS; HSPA1B; human.
DR GeneWiki; HSPA1A; -.
DR PRO; PR:P0DMV9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR CleanEx; HS_HSPA1A; -.
DR ExpressionAtlas; P0DMV9; baseline and differential.
DR GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0016234; C:inclusion body; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
DR GO; GO:0016887; F:ATPase activity; IDA:BHF-UCL.
DR GO; GO:0042623; F:ATPase activity, coupled; IDA:UniProtKB.
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:0044183; F:protein binding involved in protein folding; IDA:BHF-UCL.
DR GO; GO:0005102; F: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:0060548; P:negative regulation of cell death; 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: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: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: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:1900034; P:regulation of cellular response to heat; TAS:Reactome.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IDA:BHF-UCL.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C.
DR InterPro; IPR029047; HSP70_peptide-bd.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
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; Complete proteome;
KW Cytoplasm; Direct protein sequencing;
KW Host cell receptor for virus entry; Methylation; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Receptor; Reference proteome;
KW Stress response.
FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
FT CHAIN 2 641 Heat shock 70 kDa protein 1B.
FT /FTId=PRO_0000433115.
FT NP_BIND 12 15 ATP.
FT NP_BIND 202 204 ATP.
FT NP_BIND 268 275 ATP.
FT NP_BIND 339 342 ATP.
FT BINDING 71 71 ATP.
FT MOD_RES 2 2 N-acetylalanine.
FT {ECO:0000244|PubMed:19413330}.
FT MOD_RES 108 108 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 246 246 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 348 348 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 469 469 Omega-N-methylarginine.
FT {ECO:0000244|PubMed:24129315}.
FT MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A;
FT alternate. {ECO:0000244|PubMed:24129315,
FT ECO:0000269|PubMed:23349634,
FT ECO:0000269|PubMed:23921388}.
FT MOD_RES 561 561 N6,N6-dimethyllysine; alternate.
FT {ECO:0000244|PubMed:24129315}.
FT MOD_RES 631 631 Phosphoserine.
FT {ECO:0000244|PubMed:20068231}.
FT MOD_RES 633 633 Phosphoserine.
FT {ECO:0000244|PubMed:20068231}.
FT MOD_RES 636 636 Phosphothreonine.
FT {ECO:0000244|PubMed:20068231}.
FT VARIANT 95 95 I -> V. {ECO:0000269|Ref.4}.
FT /FTId=VAR_032152.
FT VARIANT 467 467 A -> V (in dbSNP:rs538280104).
FT {ECO:0000269|Ref.4}.
FT /FTId=VAR_032153.
FT VARIANT 499 499 N -> S (in dbSNP:rs483638).
FT {ECO:0000269|PubMed:14656967,
FT ECO:0000269|Ref.4}.
FT /FTId=VAR_029054.
FT MUTAGEN 10 10 D->A: Reduces affinity for ADP.
FT {ECO:0000269|PubMed:21608060}.
FT MUTAGEN 199 199 D->A: Reduces affinity for ADP.
FT {ECO:0000269|PubMed:21608060}.
FT MUTAGEN 561 561 K->R: Complete loss of in vitro
FT methylation by METTL21A.
FT {ECO:0000269|PubMed:23349634,
FT ECO:0000269|PubMed:23921388}.
FT STRAND 7 11 {ECO:0000244|PDB:4J8F}.
FT STRAND 13 22 {ECO:0000244|PDB:4J8F}.
FT STRAND 25 28 {ECO:0000244|PDB:4J8F}.
FT STRAND 36 39 {ECO:0000244|PDB:4J8F}.
FT STRAND 42 44 {ECO:0000244|PDB:4J8F}.
FT STRAND 49 51 {ECO:0000244|PDB:4J8F}.
FT HELIX 53 57 {ECO:0000244|PDB:4J8F}.
FT HELIX 59 61 {ECO:0000244|PDB:4J8F}.
FT HELIX 63 65 {ECO:0000244|PDB:4J8F}.
FT HELIX 70 73 {ECO:0000244|PDB:4J8F}.
FT HELIX 81 87 {ECO:0000244|PDB:4J8F}.
FT STRAND 91 99 {ECO:0000244|PDB:4J8F}.
FT STRAND 101 107 {ECO:0000244|PDB:4J8F}.
FT STRAND 110 114 {ECO:0000244|PDB:4J8F}.
FT HELIX 116 135 {ECO:0000244|PDB:4J8F}.
FT STRAND 141 146 {ECO:0000244|PDB:4J8F}.
FT HELIX 152 164 {ECO:0000244|PDB:4J8F}.
FT STRAND 168 174 {ECO:0000244|PDB:4J8F}.
FT HELIX 175 182 {ECO:0000244|PDB:4J8F}.
FT TURN 183 187 {ECO:0000244|PDB:4J8F}.
FT STRAND 193 200 {ECO:0000244|PDB:4J8F}.
FT STRAND 205 213 {ECO:0000244|PDB:4J8F}.
FT STRAND 216 225 {ECO:0000244|PDB:4J8F}.
FT HELIX 230 249 {ECO:0000244|PDB:4J8F}.
FT HELIX 257 276 {ECO:0000244|PDB:4J8F}.
FT STRAND 278 288 {ECO:0000244|PDB:4J8F}.
FT STRAND 291 298 {ECO:0000244|PDB:4J8F}.
FT HELIX 299 305 {ECO:0000244|PDB:4J8F}.
FT HELIX 307 311 {ECO:0000244|PDB:4J8F}.
FT HELIX 315 324 {ECO:0000244|PDB:4J8F}.
FT HELIX 328 330 {ECO:0000244|PDB:4J8F}.
FT STRAND 333 338 {ECO:0000244|PDB:4J8F}.
FT HELIX 339 342 {ECO:0000244|PDB:4J8F}.
FT HELIX 344 353 {ECO:0000244|PDB:4J8F}.
FT TURN 354 356 {ECO:0000244|PDB:4J8F}.
FT TURN 365 367 {ECO:0000244|PDB:4J8F}.
FT HELIX 368 382 {ECO:0000244|PDB:4J8F}.
FT HELIX 384 386 {ECO:0000244|PDB:4J8F}.
FT HELIX 426 444 {ECO:0000244|PDB:4J8F}.
FT HELIX 449 457 {ECO:0000244|PDB:4J8F}.
FT HELIX 462 466 {ECO:0000244|PDB:4J8F}.
FT HELIX 475 487 {ECO:0000244|PDB:4J8F}.
FT HELIX 491 504 {ECO:0000244|PDB:4J8F}.
FT HELIX 523 534 {ECO:0000244|PDB:4J8F}.
FT HELIX 538 551 {ECO:0000244|PDB:4J8F}.
FT HELIX 563 578 {ECO:0000244|PDB:4J8F}.
FT HELIX 587 597 {ECO:0000244|PDB:4J8F}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 6 611 ipfam:HSP70 [T]
FT MYHIT 9 16 ipat:HSP70_1 [T]
FT MYHIT 197 210 ipat:HSP70_2 [T]
FT MYHIT 334 348 ipat:HSP70_3 [T]
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
//
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