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HS71A_HUMAN
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   03-AUG-2022, entry version 63.
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=HSP72 {ECO:0000303|PubMed:24318877}, HSPA1, HSX70;
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], AND ALTERNATIVE SPLICING (ISOFORM 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 with
RT   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 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 SPLICING
RP   (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., 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   [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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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), AND
RP   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., 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   [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 project:
RT   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 heat
RT   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 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   [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 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   [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 methyltransferases
RT   preferentially interact with molecular chaperones to regulate their
RT   activity.";
RL   PLoS Genet. 9:E1003210-E1003210(2013).
RN   [14]
RP   INTERACTION WITH HSF1.
RX   PubMed=7935376; DOI=10.1128/mcb.14.10.6552-6560.1994;
RA   Rabindran S.K., Wisniewski J., Li L., Li G.C., Wu C.;
RT   "Interaction between heat shock factor and hsp70 is insufficient to
RT   suppress induction of DNA-binding activity in vivo.";
RL   Mol. Cell. Biol. 14:6552-6560(1994).
RN   [15]
RP   FUNCTION, AND INTERACTION WITH HSF1.
RX   PubMed=9499401; DOI=10.1101/gad.12.5.654;
RA   Shi Y., Mosser D.D., Morimoto R.I.;
RT   "Molecular chaperones as HSF1-specific transcriptional repressors.";
RL   Genes Dev. 12:654-666(1998).
RN   [16]
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   [17]
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   [18]
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   [19]
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   [20]
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   [21]
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   [22]
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   [23]
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   [24]
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   [25]
RP   INTERACTION WITH NLRP12.
RX   PubMed=17947705; DOI=10.4049/jimmunol.179.9.6291;
RA   Arthur J.C., Lich J.D., Aziz R.K., Kotb M., Ting J.P.;
RT   "Heat shock protein 90 associates with monarch-1 and regulates its ability
RT   to promote degradation of NF-kappaB-inducing kinase.";
RL   J. Immunol. 179:6291-6296(2007).
RN   [26]
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   [27]
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   [28]
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   [29]
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   [30]
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   [31]
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   [32]
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   [33]
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   [34]
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   [35]
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   [36]
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   [37]
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   [38]
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   [39]
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   [40]
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   [41]
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   [42]
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   [43]
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   [44]
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 excitation.";
RL   J. Biol. Chem. 289:33730-33740(2014).
RN   [45]
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   [46]
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   [47]
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   [48]
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   [49]
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   [50]
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   [51]
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   [52]
RP   FUNCTION, AND INVOLVEMENT IN ABC-DLBCL.
RX   PubMed=28842558; DOI=10.1038/s41467-017-00476-w;
RA   Wang W.F., Yan L., Liu Z., Liu L.X., Lin J., Liu Z.Y., Chen X.P., Zhang W.,
RA   Xu Z.Z., Shi T., Li J.M., Zhao Y.L., Meng G., Xia Y., Li J.Y., Zhu J.;
RT   "HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal
RT   misfolded Blimp-1s in lymphoma cells.";
RL   Nat. Commun. 8:363-363(2017).
RN   [53]
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   [54]
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   [55]
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   [56]
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   [57]
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       Negatively regulates heat shock-induced HSF1 transcriptional activity
CC       during the attenuation and recovery phase period of the heat shock
CC       response (PubMed:9499401). Involved in the clearance of misfolded
CC       PRDM1/Blimp-1 proteins. Sequesters them in the cytoplasm and promotes
CC       their association with SYNV1/HRD1, leading to proteasomal degradation
CC       (PubMed:28842558). {ECO:0000269|PubMed:22528486,
CC       ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:24318877,
CC       ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:27137183,
CC       ECO:0000269|PubMed:27708256, ECO:0000269|PubMed:28842558,
CC       ECO:0000269|PubMed:9499401, ECO:0000303|PubMed:24012426,
CC       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: Component of the CatSper complex. Identified in a IGF2BP1-
CC       dependent mRNP granule complex containing untranslated mRNAs
CC       (PubMed:17289661). Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and
CC       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, TERC,
CC       and dissociates once the TERT complex has formed (PubMed:11274138).
CC       Interacts with TRIM5 (via B30.2/SPRY domain) (PubMed:20053985).
CC       Interacts with METTL21A (PubMed:23921388). Interacts with DNAAF2 (By
CC       similarity). Interacts with PRKN (PubMed:24270810). Interacts with
CC       FOXP3 (PubMed:23973223). Interacts with NOD2; the interaction enhances
CC       NOD2 stability (PubMed:24790089). Interacts with DNAJC9 (via J domain)
CC       (PubMed:17182002). Interacts with ATF5; the interaction protects ATF5
CC       from degradation via proteasome-dependent and caspase-dependent
CC       processes (PubMed:22528486). Interacts with RNF207 (via the C-
CC       terminus); this interaction additively increases KCNH2 expression
CC       (PubMed:25281747). Interacts with HSF1 (via transactivation domain);
CC       this interaction results in the inhibition of heat shock- and HSF1-
CC       induced transcriptional activity during the attenuation and recovery
CC       phase period of the heat shock response (PubMed:7935376,
CC       PubMed:9499401). Interacts with NAA10, HSP40, HSP90 and HDAC4. The
CC       acetylated form and the non-acetylated form interact with HOPX and
CC       STUB1 respectively (PubMed:27708256). Interacts with NEDD1
CC       (PubMed:27137183). Interacts (via NBD) with BAG1, BAG2, BAG3 and
CC       HSPH1/HSP105 (PubMed:24318877). Interacts with SMAD3 (PubMed:24613385).
CC       Interacts with DNAJC8 (PubMed:27133716). Interacts with NLRP12
CC       (PubMed:17947705). Interacts with PGLYRP (By similarity).
CC       {ECO:0000250|UniProtKB:Q61696, ECO:0000269|PubMed:10216320,
CC       ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:12853476,
CC       ECO:0000269|PubMed:15383005, ECO:0000269|PubMed:15963462,
CC       ECO:0000269|PubMed:17182002, ECO:0000269|PubMed:17233114,
CC       ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17947705,
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:25281747,
CC       ECO:0000269|PubMed:27133716, ECO:0000269|PubMed:27137183,
CC       ECO:0000269|PubMed:27708256, ECO:0000269|PubMed:7935376,
CC       ECO:0000269|PubMed:9499401}.
CC   -!- INTERACTION:
CC       P0DMV8; P54253: ATXN1; NbExp=3; IntAct=EBI-11052499, EBI-930964;
CC       P0DMV8; P42858: HTT; NbExp=9; IntAct=EBI-11052499, EBI-466029;
CC       P0DMV8; Q9GZQ8: MAP1LC3B; NbExp=3; IntAct=EBI-11052499, EBI-373144;
CC       P0DMV8; Q9NUX5: POT1; NbExp=2; IntAct=EBI-11052499, EBI-752420;
CC       P0DMV8; O60260-5: PRKN; NbExp=6; IntAct=EBI-11052499, EBI-21251460;
CC       P0DMV8; O75832: PSMD10; NbExp=2; IntAct=EBI-11052499, EBI-752185;
CC       P0DMV8; P04271: S100B; NbExp=3; IntAct=EBI-11052499, EBI-458391;
CC       P0DMV8; Q13501: SQSTM1; NbExp=3; IntAct=EBI-11052499, EBI-307104;
CC       P0DMV8; P43405-2: SYK; NbExp=3; IntAct=EBI-11052499, EBI-25892332;
CC       P0DMV8; P04663: HA; Xeno; NbExp=4; IntAct=EBI-11052499, EBI-13951712;
CC       P0DMV8; P04958: tetX; Xeno; NbExp=3; IntAct=EBI-11052499, EBI-13951617;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661}. Nucleus
CC       {ECO:0000269|PubMed:27137183}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000269|PubMed:27137183}. Secreted
CC       {ECO:0000250|UniProtKB:Q61696}. Note=Localized in cytoplasmic mRNP
CC       granules containing 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   -!- 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   -!- DISEASE: Note=In certain aggressive cases of activated B cell-like
CC       diffuse large B-cell lymphoma (ABC-DLBCL), plays a role in the
CC       cytoplasmic sequestration of misfolded N-terminal mutated PRDM1
CC       proteins, promotes their association with SYNV1/HRD1 and degradation
CC       through the SYNV1-proteasome pathway. HSPA1A inhibition restores PRDM1
CC       nuclear localization and transcriptional activity in lymphoma cell
CC       lines and suppresses growth in xenografts.
CC       {ECO:0000269|PubMed:28842558}.
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/hspa1a/";
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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   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   PDB; 5GJJ; NMR; -; A=385-641.
DR   PDB; 5MKR; X-ray; 1.87 A; A=1-380.
DR   PDB; 5MKS; X-ray; 1.99 A; A=1-380.
DR   PDB; 5XI9; NMR; -; A=381-564.
DR   PDB; 5XIR; NMR; -; A=381-564.
DR   PDB; 6FHK; X-ray; 1.66 A; A/B=1-381.
DR   PDB; 6G3R; X-ray; 1.40 A; A=3-382.
DR   PDB; 6G3S; X-ray; 2.30 A; A=3-382.
DR   PDB; 6JPV; X-ray; 2.15 A; A/B=395-537.
DR   PDB; 6K39; X-ray; 1.40 A; A/B=395-537.
DR   PDB; 6ZYI; X-ray; 1.52 A; A=4-381.
DR   PDB; 7KW7; EM; 3.57 A; C/D=1-641.
DR   PDB; 7Q4R; X-ray; 1.79 A; A=1-380.
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   PDBsum; 5GJJ; -.
DR   PDBsum; 5MKR; -.
DR   PDBsum; 5MKS; -.
DR   PDBsum; 5XI9; -.
DR   PDBsum; 5XIR; -.
DR   PDBsum; 6FHK; -.
DR   PDBsum; 6G3R; -.
DR   PDBsum; 6G3S; -.
DR   PDBsum; 6JPV; -.
DR   PDBsum; 6K39; -.
DR   PDBsum; 6ZYI; -.
DR   PDBsum; 7KW7; -.
DR   PDBsum; 7Q4R; -.
DR   AlphaFoldDB; P0DMV8; -.
DR   BMRB; P0DMV8; -.
DR   SASBDB; P0DMV8; -.
DR   SMR; P0DMV8; -.
DR   CORUM; P0DMV8; -.
DR   IntAct; P0DMV8; 54.
DR   MINT; P0DMV8; -.
DR   STRING; 9606.ENSP00000364801; -.
DR   BindingDB; P0DMV8; -.
DR   ChEMBL; CHEMBL5460; -.
DR   DrugCentral; P0DMV8; -.
DR   CarbonylDB; P0DMV8; -.
DR   GlyConnect; 1295; 2 N-Linked glycans (2 sites).
DR   GlyGen; P0DMV8; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P0DMV8; -.
DR   MetOSite; P0DMV8; -.
DR   PhosphoSitePlus; P0DMV8; -.
DR   SwissPalm; P0DMV8; -.
DR   BioMuta; HSPA1A; -.
DR   REPRODUCTION-2DPAGE; IPI00304925; -.
DR   jPOST; P0DMV8; -.
DR   MassIVE; P0DMV8; -.
DR   MaxQB; P0DMV8; -.
DR   PaxDb; P0DMV8; -.
DR   PeptideAtlas; P0DMV8; -.
DR   PRIDE; P0DMV8; -.
DR   ABCD; P0DMV8; 3 sequenced antibodies.
DR   Antibodypedia; 27819; 2282 antibodies from 44 providers.
DR   DNASU; 3303; -.
DR   Ensembl; ENST00000375651.7; ENSP00000364802.5; ENSG00000204389.10. [P0DMV8-1]
DR   Ensembl; ENST00000400040.1; ENSP00000382915.1; ENSG00000215328.6.
DR   Ensembl; ENST00000430065.1; ENSP00000404524.1; ENSG00000235941.5. [P0DMV8-1]
DR   Ensembl; ENST00000433487.1; ENSP00000408907.1; ENSG00000234475.5. [P0DMV8-1]
DR   Ensembl; ENST00000441618.1; ENSP00000406359.1; ENSG00000237724.5. [P0DMV8-1]
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; HSPA1A; -.
DR   HGNC; HGNC:5232; HSPA1A.
DR   HPA; ENSG00000204389; Low tissue specificity.
DR   MIM; 140550; gene.
DR   MIM; 603012; gene.
DR   neXtProt; NX_P0DMV8; -.
DR   OpenTargets; ENSG00000204388; -.
DR   OpenTargets; ENSG00000204389; -.
DR   VEuPathDB; HostDB:ENSG00000204389; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   OMA; VNEAESY; -.
DR   PhylomeDB; P0DMV8; -.
DR   PathwayCommons; P0DMV8; -.
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-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-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; P0DMV8; -.
DR   SIGNOR; P0DMV8; -.
DR   BioGRID-ORCS; 3303; 19 hits in 653 CRISPR screens.
DR   BioGRID-ORCS; 3304; 7 hits in 641 CRISPR screens.
DR   ChiTaRS; HSPA1A; human.
DR   Pharos; P0DMV8; Tchem.
DR   PRO; PR:P0DMV8; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; P0DMV8; protein.
DR   Bgee; ENSG00000204389; Expressed in lower esophagus mucosa and 93 other tissues.
DR   ExpressionAtlas; P0DMV8; 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:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0031249; F:denatured protein binding; IPI:CAFA.
DR   GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
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; IDA:UniProtKB.
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:0003714; F:transcription corepressor activity; IDA: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; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:CAFA.
DR   GO; GO:0007041; P:lysosomal transport; ISS:UniProtKB.
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; IMP:UniProtKB.
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: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:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; IDA:UniProtKB.
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: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; IDA:UniProtKB.
DR   GO; GO:0033120; P:positive regulation of RNA splicing; IDA:ParkinsonsUK-UCL.
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; IDA:CAFA.
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:0006986; P:response to unfolded protein; IDA:UniProtKB.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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; Alternative splicing; ATP-binding; Chaperone;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Host cell receptor for virus entry; Host-virus interaction; Methylation;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Receptor; Reference proteome;
KW   Secreted; 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 1A"
FT                   /id="PRO_0000078249"
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   VAR_SEQ         96..150
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044427"
FT   VARIANT         110
FT                   /note="E -> D (in dbSNP:rs562047)"
FT                   /evidence="ECO:0000269|PubMed:14656967, ECO:0000269|Ref.6"
FT                   /id="VAR_029053"
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   CONFLICT        7
FT                   /note="I -> V (in Ref. 1; AAA52697 and 10; CAA28381)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        355
FT                   /note="N -> D (in Ref. 5; BAG65428)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        370
FT                   /note="A -> G (in Ref. 1; AAA52697)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        469
FT                   /note="Missing (in Ref. 1; AAA52697)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        497
FT                   /note="K -> N (in Ref. 5; BAG65428)"
FT                   /evidence="ECO:0000305"
FT   STRAND          7..10
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          13..22
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          25..28
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           53..56
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   TURN            57..61
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:6FHK"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           81..86
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          91..97
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          100..107
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          110..114
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           116..135
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          141..146
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           152..164
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          168..174
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           175..182
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           185..187
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          189..191
FT                   /evidence="ECO:0007829|PDB:2E8A"
FT   STRAND          193..200
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          205..213
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          216..225
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           226..228
FT                   /evidence="ECO:0007829|PDB:2E88"
FT   HELIX           230..249
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           253..255
FT                   /evidence="ECO:0007829|PDB:2E88"
FT   HELIX           257..274
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          277..288
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          291..298
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           299..305
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           307..312
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           314..324
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           328..330
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          333..338
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           339..342
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           344..353
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   TURN            354..356
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   TURN            365..367
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   HELIX           368..380
FT                   /evidence="ECO:0007829|PDB:5BN8"
FT   STRAND          391..393
FT                   /evidence="ECO:0007829|PDB:5GJJ"
FT   STRAND          401..405
FT                   /evidence="ECO:0007829|PDB:6K39"
FT   TURN            406..408
FT                   /evidence="ECO:0007829|PDB:6K39"
FT   STRAND          409..414
FT                   /evidence="ECO:0007829|PDB:6K39"
FT   STRAND          419..428
FT                   /evidence="ECO:0007829|PDB:6K39"
FT   STRAND          433..435
FT                   /evidence="ECO:0007829|PDB:5XI9"
FT   STRAND          437..446
FT                   /evidence="ECO:0007829|PDB:6K39"
FT   HELIX           450..452
FT                   /evidence="ECO:0007829|PDB:6K39"
FT   STRAND          453..462
FT                   /evidence="ECO:0007829|PDB:6K39"
FT   STRAND          468..470
FT                   /evidence="ECO:0007829|PDB:5XIR"
FT   STRAND          474..480
FT                   /evidence="ECO:0007829|PDB:6K39"
FT   TURN            482..484
FT                   /evidence="ECO:0007829|PDB:5XIR"
FT   STRAND          486..492
FT                   /evidence="ECO:0007829|PDB:6K39"
FT   TURN            493..495
FT                   /evidence="ECO:0007829|PDB:6K39"
FT   STRAND          498..503
FT                   /evidence="ECO:0007829|PDB:6K39"
FT   HELIX           506..508
FT                   /evidence="ECO:0007829|PDB:6K39"
FT   HELIX           512..524
FT                   /evidence="ECO:0007829|PDB:6K39"
FT   HELIX           526..535
FT                   /evidence="ECO:0007829|PDB:6K39"
FT   HELIX           538..553
FT                   /evidence="ECO:0007829|PDB:2LMG"
FT   HELIX           556..558
FT                   /evidence="ECO:0007829|PDB:3LOF"
FT   HELIX           564..583
FT                   /evidence="ECO:0007829|PDB:3LOF"
FT   HELIX           589..612
FT                   /evidence="ECO:0007829|PDB:3LOF"
FT   STRAND          637..639
FT                   /evidence="ECO:0007829|PDB:3Q49"
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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