ID HS71A_HUMAN Reviewed; 641 AA.
AC P0DMV8; B4E3B6; P08107; P19790; Q5JQI4; Q5SP17; Q9UQL9; Q9UQM0;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 1.
DT 18-JAN-2017, entry version 19.
DE RecName: Full=Heat shock 70 kDa protein 1A {ECO:0000312|HGNC:HGNC:5232};
DE AltName: Full=Heat shock 70 kDa protein 1;
DE Short=HSP70-1 {ECO:0000303|PubMed:14656967, ECO:0000303|PubMed:2538825};
DE Short=HSP70.1;
GN Name=HSPA1A; Synonyms=HSPA1, HSX70;
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], AND ALTERNATIVE SPLICING (ISOFORM
RP 1).
RX PubMed=3931075; DOI=10.1073/pnas.82.19.6455;
RA Hunt C., Morimoto R.I.;
RT "Conserved features of eukaryotic hsp70 genes revealed by comparison
RT with the nucleotide sequence of human hsp70.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6455-6459(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
RP 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP SPLICING (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-110, AND
RP ALTERNATIVE SPLICING (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1),
RP AND VARIANT ASP-110.
RG NIEHS SNPs program;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22 AND 617-641.
RX PubMed=3786141; DOI=10.1093/nar/14.22.8933;
RA Drabent B., Genthe A., Benecke B.-J.;
RT "In vitro transcription of a human hsp 70 heat shock gene by extracts
RT prepared from heat-shocked and non-heat-shocked human cells.";
RL Nucleic Acids Res. 14:8933-8948(1986).
RN [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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 [27]
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 [28]
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 [29]
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 [30]
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 [31]
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 [32]
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 [33]
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 [34]
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 [35]
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 [36]
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 [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
RT important protein involved in Crohn disease.";
RL J. Biol. Chem. 289:18987-18998(2014).
RN [38]
RP INTERACTION WITH RNF207.
RX PubMed=25281747; DOI=10.1074/jbc.M114.592295;
RA Roder K., Werdich A.A., Li W., Liu M., Kim T.Y., Organ-Darling L.E.,
RA Moshal K.S., Hwang J.M., Lu Y., Choi B.R., MacRae C.A., Koren G.;
RT "RING finger protein RNF207, a novel regulator of cardiac
RT excitation.";
RL J. Biol. Chem. 289:33730-33740(2014).
RN [39]
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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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 [45]
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 [46]
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 DNAAF2 (By similarity). Interacts with PARK2
CC (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). Interacts with ATF5; the interaction protects
CC ATF5 from degradation via proteasome-dependent and caspase-
CC dependent processes (PubMed:22528486). Interacts with RNF207 (via
CC the C-terminus); this interaction additively increases KCNH2
CC expression (PubMed:25281747). {ECO:0000250|UniProtKB:Q61696,
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, ECO:0000269|PubMed:25281747}.
CC -!- INTERACTION:
CC Q9NUX5:POT1; NbExp=2; IntAct=EBI-11052499, EBI-752420;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661}.
CC Note=Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0DMV8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0DMV8-2; Sequence=VSP_044427;
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/hspa1a/";
DR EMBL; M11717; AAA52697.1; -; Genomic_DNA.
DR EMBL; M59828; AAA63226.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63300.1; -; Genomic_DNA.
DR EMBL; AF134726; AAD21816.1; -; Genomic_DNA.
DR EMBL; AK304652; BAG65428.1; -; mRNA.
DR EMBL; DQ451402; ABD96830.1; -; Genomic_DNA.
DR EMBL; AL671762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002453; AAH02453.1; -; mRNA.
DR EMBL; M24743; AAA59844.1; -; Genomic_DNA.
DR EMBL; X04676; CAA28381.1; -; Genomic_DNA.
DR EMBL; X04677; CAA28382.1; -; Genomic_DNA.
DR CCDS; CCDS34414.1; -. [P0DMV8-1]
DR PIR; A29160; A29160.
DR PIR; A45871; A45871.
DR PIR; I59139; I59139.
DR PIR; I79540; I79540.
DR RefSeq; NP_005336.3; NM_005345.5. [P0DMV8-1]
DR RefSeq; NP_005337.2; NM_005346.4. [P0DMV8-1]
DR UniGene; Hs.274402; -.
DR UniGene; Hs.702139; -.
DR UniGene; Hs.719966; -.
DR UniGene; Hs.743411; -.
DR PDB; 1HJO; X-ray; 2.30 A; A=3-382.
DR PDB; 1S3X; X-ray; 1.84 A; A=1-382.
DR PDB; 1XQS; X-ray; 2.90 A; C/D=184-371.
DR PDB; 2E88; X-ray; 1.80 A; A=1-388.
DR PDB; 2E8A; X-ray; 1.77 A; A=1-388.
DR PDB; 2LMG; NMR; -; A=537-610.
DR PDB; 3A8Y; X-ray; 2.30 A; A/B=1-388.
DR PDB; 3ATU; X-ray; 1.65 A; A=1-388.
DR PDB; 3ATV; X-ray; 1.58 A; A=1-388.
DR PDB; 3AY9; X-ray; 1.75 A; A=1-388.
DR PDB; 3D2E; X-ray; 2.35 A; B/D=1-382.
DR PDB; 3D2F; X-ray; 2.30 A; B/D=1-382.
DR PDB; 3JXU; X-ray; 2.14 A; A=1-387.
DR PDB; 3LOF; X-ray; 2.40 A; A/B/C/D/E/F=534-641.
DR PDB; 3Q49; X-ray; 1.54 A; C=634-641.
DR PDB; 4IO8; X-ray; 2.58 A; A=1-382.
DR PDB; 4J8F; X-ray; 2.70 A; A=1-382.
DR PDB; 4PO2; X-ray; 2.00 A; A/B=386-613.
DR PDB; 4WV5; X-ray; 2.04 A; A/B=395-543.
DR PDB; 4WV7; X-ray; 2.42 A; A/B=395-543.
DR PDB; 5AQW; X-ray; 1.53 A; A=1-380.
DR PDB; 5AQX; X-ray; 2.12 A; A=1-380.
DR PDB; 5AQY; X-ray; 1.56 A; A=1-380.
DR PDB; 5AQZ; X-ray; 1.65 A; A=1-380.
DR PDB; 5AR0; X-ray; 1.90 A; A=1-380.
DR PDB; 5BN8; X-ray; 1.34 A; A=1-388.
DR PDB; 5BN9; X-ray; 1.69 A; A=1-388.
DR PDB; 5BPL; X-ray; 1.93 A; A=1-388.
DR PDB; 5BPM; X-ray; 1.83 A; A=1-388.
DR PDB; 5BPN; X-ray; 2.10 A; A=1-388.
DR PDBsum; 1HJO; -.
DR PDBsum; 1S3X; -.
DR PDBsum; 1XQS; -.
DR PDBsum; 2E88; -.
DR PDBsum; 2E8A; -.
DR PDBsum; 2LMG; -.
DR PDBsum; 3A8Y; -.
DR PDBsum; 3ATU; -.
DR PDBsum; 3ATV; -.
DR PDBsum; 3AY9; -.
DR PDBsum; 3D2E; -.
DR PDBsum; 3D2F; -.
DR PDBsum; 3JXU; -.
DR PDBsum; 3LOF; -.
DR PDBsum; 3Q49; -.
DR PDBsum; 4IO8; -.
DR PDBsum; 4J8F; -.
DR PDBsum; 4PO2; -.
DR PDBsum; 4WV5; -.
DR PDBsum; 4WV7; -.
DR PDBsum; 5AQW; -.
DR PDBsum; 5AQX; -.
DR PDBsum; 5AQY; -.
DR PDBsum; 5AQZ; -.
DR PDBsum; 5AR0; -.
DR PDBsum; 5BN8; -.
DR PDBsum; 5BN9; -.
DR PDBsum; 5BPL; -.
DR PDBsum; 5BPM; -.
DR PDBsum; 5BPN; -.
DR ProteinModelPortal; P0DMV8; -.
DR SMR; P0DMV8; -.
DR IntAct; P0DMV8; 14.
DR MINT; MINT-96699; -.
DR BindingDB; P0DMV8; -.
DR ChEMBL; CHEMBL5460; -.
DR iPTMnet; P0DMV8; -.
DR PhosphoSitePlus; P0DMV8; -.
DR SwissPalm; P0DMV8; -.
DR DMDM; 147744565; -.
DR REPRODUCTION-2DPAGE; IPI00304925; -.
DR PeptideAtlas; P0DMV8; -.
DR PRIDE; P0DMV8; -.
DR DNASU; 3303; -.
DR Ensembl; ENST00000375651; ENSP00000364802; ENSG00000204389. [P0DMV8-1]
DR Ensembl; ENST00000400040; ENSP00000382915; ENSG00000215328.
DR Ensembl; ENST00000430065; ENSP00000404524; ENSG00000235941. [P0DMV8-1]
DR Ensembl; ENST00000433487; ENSP00000408907; ENSG00000234475. [P0DMV8-1]
DR Ensembl; ENST00000441618; ENSP00000406359; ENSG00000237724. [P0DMV8-1]
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:5232; HSPA1A.
DR HPA; HPA052504; -.
DR MIM; 140550; gene.
DR MIM; 603012; gene.
DR neXtProt; NX_P0DMV8; -.
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 HOGENOM; HOG000228135; -.
DR HOVERGEN; HBG051845; -.
DR KO; K03283; -.
DR OrthoDB; EOG091G03SF; -.
DR PhylomeDB; P0DMV8; -.
DR TreeFam; TF105042; -.
DR Reactome; R-HSA-168330; Viral RNP Complexes in the Host Cell Nucleus.
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-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR ChiTaRS; HSPA1A; human.
DR ChiTaRS; HSPA1B; human.
DR GeneWiki; HSPA1A; -.
DR PRO; PR:P0DMV8; -.
DR Proteomes; UP000005640; Chromosome 6.
DR CleanEx; HS_HSPA1A; -.
DR ExpressionAtlas; P0DMV8; baseline and differential.
DR GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
DR GO; GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
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:0005739; C:mitochondrion; IEA:GOC.
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:0098641; F:cadherin binding involved in cell-cell adhesion; IDA: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:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
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:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:1902380; P:positive regulation of endoribonuclease activity; 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:1904722; P:positive regulation of mRNA endonucleolytic cleavage involved in unfolded protein response; IDA:ParkinsonsUK-UCL.
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; IDA: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:0043488; P:regulation of mRNA stability; 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; Alternative splicing; ATP-binding;
KW Chaperone; Complete proteome; 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 1A.
FT /FTId=PRO_0000078249.
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 VAR_SEQ 96 150 Missing (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_044427.
FT VARIANT 110 110 E -> D (in dbSNP:rs562047).
FT {ECO:0000269|PubMed:14656967,
FT ECO:0000269|Ref.6}.
FT /FTId=VAR_029053.
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 CONFLICT 7 7 I -> V (in Ref. 1; AAA52697 and 10;
FT CAA28381). {ECO:0000305}.
FT CONFLICT 355 355 N -> D (in Ref. 5; BAG65428).
FT {ECO:0000305}.
FT CONFLICT 370 370 A -> G (in Ref. 1; AAA52697).
FT {ECO:0000305}.
FT CONFLICT 469 469 Missing (in Ref. 1; AAA52697).
FT {ECO:0000305}.
FT CONFLICT 497 497 K -> N (in Ref. 5; BAG65428).
FT {ECO:0000305}.
FT STRAND 7 10 {ECO:0000244|PDB:5BN8}.
FT STRAND 13 22 {ECO:0000244|PDB:5BN8}.
FT STRAND 25 28 {ECO:0000244|PDB:5BN8}.
FT STRAND 36 39 {ECO:0000244|PDB:5BN8}.
FT STRAND 42 44 {ECO:0000244|PDB:5BN8}.
FT STRAND 49 51 {ECO:0000244|PDB:5BN8}.
FT HELIX 53 56 {ECO:0000244|PDB:5BN8}.
FT TURN 57 61 {ECO:0000244|PDB:5BN8}.
FT HELIX 63 65 {ECO:0000244|PDB:5BN8}.
FT HELIX 70 72 {ECO:0000244|PDB:5BN8}.
FT TURN 73 75 {ECO:0000244|PDB:5BN8}.
FT HELIX 81 86 {ECO:0000244|PDB:5BN8}.
FT HELIX 87 89 {ECO:0000244|PDB:5BN8}.
FT STRAND 91 97 {ECO:0000244|PDB:5BN8}.
FT STRAND 100 107 {ECO:0000244|PDB:5BN8}.
FT STRAND 110 114 {ECO:0000244|PDB:5BN8}.
FT HELIX 116 135 {ECO:0000244|PDB:5BN8}.
FT STRAND 141 146 {ECO:0000244|PDB:5BN8}.
FT HELIX 152 164 {ECO:0000244|PDB:5BN8}.
FT STRAND 168 174 {ECO:0000244|PDB:5BN8}.
FT HELIX 175 182 {ECO:0000244|PDB:5BN8}.
FT HELIX 185 187 {ECO:0000244|PDB:5BN8}.
FT STRAND 189 191 {ECO:0000244|PDB:2E8A}.
FT STRAND 193 200 {ECO:0000244|PDB:5BN8}.
FT STRAND 205 213 {ECO:0000244|PDB:5BN8}.
FT STRAND 216 225 {ECO:0000244|PDB:5BN8}.
FT HELIX 226 228 {ECO:0000244|PDB:2E88}.
FT HELIX 230 249 {ECO:0000244|PDB:5BN8}.
FT HELIX 253 255 {ECO:0000244|PDB:2E88}.
FT HELIX 257 274 {ECO:0000244|PDB:5BN8}.
FT STRAND 277 288 {ECO:0000244|PDB:5BN8}.
FT STRAND 291 298 {ECO:0000244|PDB:5BN8}.
FT HELIX 299 305 {ECO:0000244|PDB:5BN8}.
FT HELIX 307 312 {ECO:0000244|PDB:5BN8}.
FT HELIX 314 324 {ECO:0000244|PDB:5BN8}.
FT HELIX 328 330 {ECO:0000244|PDB:5BN8}.
FT STRAND 333 338 {ECO:0000244|PDB:5BN8}.
FT HELIX 339 342 {ECO:0000244|PDB:5BN8}.
FT HELIX 344 353 {ECO:0000244|PDB:5BN8}.
FT TURN 354 356 {ECO:0000244|PDB:5BN8}.
FT TURN 365 367 {ECO:0000244|PDB:5BN8}.
FT HELIX 368 380 {ECO:0000244|PDB:5BN8}.
FT HELIX 390 393 {ECO:0000244|PDB:4PO2}.
FT STRAND 394 396 {ECO:0000244|PDB:4PO2}.
FT STRAND 401 405 {ECO:0000244|PDB:4PO2}.
FT TURN 406 408 {ECO:0000244|PDB:4PO2}.
FT STRAND 409 414 {ECO:0000244|PDB:4PO2}.
FT STRAND 419 432 {ECO:0000244|PDB:4PO2}.
FT STRAND 438 449 {ECO:0000244|PDB:4PO2}.
FT HELIX 450 452 {ECO:0000244|PDB:4PO2}.
FT STRAND 453 461 {ECO:0000244|PDB:4PO2}.
FT STRAND 474 480 {ECO:0000244|PDB:4PO2}.
FT STRAND 486 492 {ECO:0000244|PDB:4PO2}.
FT TURN 493 495 {ECO:0000244|PDB:4PO2}.
FT STRAND 498 503 {ECO:0000244|PDB:4PO2}.
FT HELIX 506 508 {ECO:0000244|PDB:4PO2}.
FT HELIX 512 524 {ECO:0000244|PDB:4PO2}.
FT HELIX 526 554 {ECO:0000244|PDB:4PO2}.
FT HELIX 556 558 {ECO:0000244|PDB:4PO2}.
FT HELIX 564 583 {ECO:0000244|PDB:4PO2}.
FT HELIX 589 608 {ECO:0000244|PDB:4PO2}.
FT HELIX 609 611 {ECO:0000244|PDB:4PO2}.
FT STRAND 637 639 {ECO:0000244|PDB:3Q49}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 334 348 ipat:HSP70_3 [T]
FT MYHIT 6 611 ipfam:HSP70 [T]
FT MYHIT 9 16 ipat:HSP70_1 [T]
FT MYHIT 197 210 ipat:HSP70_2 [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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