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Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8) (Lipopolysaccharide-associated protein 1) (LAP-1) (LPS-associated protein 1)

 HSP7C_HUMAN             Reviewed;         646 AA.
P11142; Q9H3R6;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
22-NOV-2017, entry version 217.
RecName: Full=Heat shock cognate 71 kDa protein;
AltName: Full=Heat shock 70 kDa protein 8;
AltName: Full=Lipopolysaccharide-associated protein 1;
Short=LAP-1;
Short=LPS-associated protein 1;
Name=HSPA8; Synonyms=HSC70, HSP73, HSPA10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=3037489; DOI=10.1093/nar/15.13.5181;
Dworniczak B.P., Mirault M.-E.;
"Structure and expression of a human gene coding for a 71 kd heat
shock 'cognate' protein.";
Nucleic Acids Res. 15:5181-5197(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=11093761;
Tsukahara F., Yoshioka T., Muraki T.;
"Molecular and functional characterization of HSC54, a novel variant
of human heat shock cognate protein 70.";
Mol. Pharmacol. 58:1257-1263(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Niswonger M.L., Berk L.R., Srivastava P.K.;
"Complete coding sequence of human HSC70.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-49; 57-71; 77-102; 103-155; 160-188; 221-247;
273-311; 326-342; 349-416; 424-447; 452-493; 510-517; 540-550; 570-597
AND 602-646, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2,
AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[6]
PROTEIN SEQUENCE OF 2-49; 57-72; 78-88; 113-188; 221-247; 300-319;
326-342; 349-357; 362-384; 424-447; 452-469; 510-517; 540-550 AND
584-609, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon carcinoma, and Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.,
Bilsland A.E., Keith W.N.;
Submitted (JAN-2010) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 4-49; 57-71; 77-88; 113-126; 129-155; 160-187;
221-246; 300-311; 329-342; 362-384; 424-447; 540-550 AND 574-583, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 50-55; 103-107 AND 580-596.
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[9]
PROTEIN SEQUENCE OF 77-86; 221-236 AND 302-311.
PubMed=8713105; DOI=10.1006/bbrc.1996.1082;
Egerton M., Moritz R.L., Druker B., Kelso A., Simpson R.J.;
"Identification of the 70kD heat shock cognate protein (Hsc70) and
alpha-actinin-1 as novel phosphotyrosine-containing proteins in T
lymphocytes.";
Biochem. Biophys. Res. Commun. 224:666-674(1996).
[10]
PROTEIN SEQUENCE OF 551-567, METHYLATION AT LYS-561, MUTAGENESIS OF
LYS-561, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
"A newly uncovered group of distantly related lysine
methyltransferases preferentially interact with molecular chaperones
to regulate their activity.";
PLoS Genet. 9:E1003210-E1003210(2013).
[11]
SUBCELLULAR LOCATION.
PubMed=1586970;
Hattori H., Liu Y.-C., Tohnai I., Ueda M., Kaneda T., Kobayashi T.,
Tanabe K., Ohtsuka K.;
"Intracellular localization and partial amino acid sequence of a
stress-inducible 40-kDa protein in HeLa cells.";
Cell Struct. Funct. 17:77-86(1992).
[12]
INTERACTION WITH BAG1, AND DOMAIN.
PubMed=9305631; DOI=10.1093/emboj/16.16.4887;
Takayama S., Bimston D.N., Matsuzawa S.-I., Freeman B.C.,
Aime-Sempe C., Xie Z., Morimoto R.I., Reed J.C.;
"BAG-1 modulates the chaperone activity of Hsp70/Hsc70.";
EMBO J. 16:4887-4896(1997).
[13]
INTERACTION WITH BAG1.
PubMed=9679980;
Takayama S., Krajewski S., Krajewska M., Kitada S., Zapata J.M.,
Kochel K., Knee D., Scudiero D., Tudor G., Miller G.J., Miyashita T.,
Yamada M., Reed J.C.;
"Expression and location of Hsp70/Hsc-binding anti-apoptotic protein
BAG-1 and its variants in normal tissues and tumor cell lines.";
Cancer Res. 58:3116-3131(1998).
[14]
INTERACTION WITH HSF1.
PubMed=9499401; DOI=10.1101/gad.12.5.654;
Shi Y., Mosser D.D., Morimoto R.I.;
"Molecular chaperones as HSF1-specific transcriptional repressors.";
Genes Dev. 12:654-666(1998).
[15]
INTERACTION WITH SV40 VP1.
PubMed=11147964; DOI=10.1379/1466-1268(2000)005<0132:HIWSVP>2.0.CO;2;
Sainis L., Angelidis C., Pagoulatos G.N., Lazaridis L.;
"HSC70 interactions with SV40 viral proteins differ between permissive
and nonpermissive mammalian cells.";
Cell Stress Chaperones 5:132-138(2000).
[16]
FUNCTION, AND INTERACTION WITH CITED1.
PubMed=10722728; DOI=10.1074/jbc.275.12.8825;
Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S.,
Roberts A.B., Isselbacher K.J., Shioda T.;
"The MSG1 non-DNA-binding transactivator binds to the p300/CBP
coactivators, enhancing their functional link to the Smad
transcription factors.";
J. Biol. Chem. 275:8825-8834(2000).
[17]
FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH CXCR4; GDF5
AND HSP90AA1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11276205; DOI=10.1038/86342;
Triantafilou K., Triantafilou M., Dedrick R.L.;
"A CD14-independent LPS receptor cluster.";
Nat. Immunol. 2:338-345(2001).
[18]
INTERACTION WITH PACRG.
PubMed=14532270; DOI=10.1074/jbc.M309655200;
Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.;
"A product of the human gene adjacent to parkin is a component of Lewy
bodies and suppresses Pael receptor-induced cell death.";
J. Biol. Chem. 278:51901-51910(2003).
[19]
INTERACTION WITH TTC1.
PubMed=15708368; DOI=10.1016/j.abb.2004.12.020;
Liou S.T., Wang C.;
"Small glutamine-rich tetratricopeptide repeat-containing protein is
composed of three structural units with distinct functions.";
Arch. Biochem. Biophys. 435:253-263(2005).
[20]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[21]
INTERACTION WITH TSC2, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15963462; DOI=10.1016/j.bbrc.2005.05.175;
Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J.,
Luider T.M.;
"Phosphorylation and binding partner analysis of the TSC1-TSC2
complex.";
Biochem. Biophys. Res. Commun. 333:818-826(2005).
[22]
INTERACTION WITH DNAJB2.
PubMed=15936278; DOI=10.1016/j.cub.2005.04.058;
Westhoff B., Chapple J.P., van der Spuy J., Hoehfeld J.,
Cheetham M.E.;
"HSJ1 is a neuronal shuttling factor for the sorting of chaperone
clients to the proteasome.";
Curr. Biol. 15:1058-1064(2005).
[23]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[24]
INTERACTION WITH HERC5, AND ISGYLATION.
PubMed=16815975; DOI=10.1073/pnas.0600397103;
Wong J.J., Pung Y.F., Sze N.S., Chin K.C.;
"HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates
type I IFN-induced ISGylation of protein targets.";
Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006).
[25]
INTERACTION WITH DNAJC9.
PubMed=17182002; DOI=10.1016/j.bbrc.2006.12.013;
Han C., Chen T., Li N., Yang M., Wan T., Cao X.;
"HDJC9, a novel human type C DnaJ/HSP40 member interacts with and
cochaperones HSP70 through the J domain.";
Biochem. Biophys. Res. Commun. 353:280-285(2007).
[26]
IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
Johnsen A.H., Christiansen J., Nielsen F.C.;
"Molecular composition of IMP1 ribonucleoprotein granules.";
Mol. Cell. Proteomics 6:798-811(2007).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[29]
IDENTIFICATION IN A COMPLEX WITH HCFC1; MKI67; EMSY; MATR3; ZNF335;
TUBB2A; CCAR2; ASCL2; RBBP5 AND WDR5.
PubMed=19131338; DOI=10.1074/jbc.M805872200;
Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A.,
Samuels H.H.;
"Identification and characterization of a novel nuclear protein
complex involved in nuclear hormone receptor-mediated gene
regulation.";
J. Biol. Chem. 284:7542-7552(2009).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-246; LYS-319; LYS-589;
LYS-597 AND LYS-601, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[32]
INTERACTION WITH DNAJB12.
PubMed=21150129; DOI=10.1247/csf.10023;
Yamamoto Y.H., Kimura T., Momohara S., Takeuchi M., Tani T.,
Kimata Y., Kadokura H., Kohno K.;
"A novel ER J-protein DNAJB12 accelerates ER-associated degradation of
membrane proteins including CFTR.";
Cell Struct. Funct. 35:107-116(2010).
[33]
INTERACTION WITH TRIM5.
PubMed=20053985; DOI=10.1074/jbc.M109.040618;
Hwang C.Y., Holl J., Rajan D., Lee Y., Kim S., Um M., Kwon K.S.,
Song B.;
"Hsp70 interacts with the retroviral restriction factor TRIM5alpha and
assists the folding of TRIM5alpha.";
J. Biol. Chem. 285:7827-7837(2010).
[34]
IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L COMPLEX, AND
SUBCELLULAR LOCATION.
PubMed=20176811; DOI=10.1128/MCB.01505-09;
Grote M., Wolf E., Will C.L., Lemm I., Agafonov D.E., Schomburg A.,
Fischle W., Urlaub H., Luhrmann R.;
"Molecular architecture of the human Prp19/CDC5L complex.";
Mol. Cell. Biol. 30:2105-2119(2010).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[37]
INTERACTION WITH DNAJB12.
PubMed=21148293; DOI=10.1091/mbc.E10-09-0760;
Grove D.E., Fan C.Y., Ren H.Y., Cyr D.M.;
"The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70
cooperate to facilitate RMA1 E3-dependent degradation of nascent
CFTRDeltaF508.";
Mol. Biol. Cell 22:301-314(2011).
[38]
INTERACTION WITH DNAJB14.
PubMed=23018488; DOI=10.1247/csf.12017;
Sopha P., Kadokura H., Yamamoto Y.H., Takeuchi M., Saito M., Tsuru A.,
Kohno K.;
"A novel mammalian ER-located J-protein, DNAJB14, can accelerate ERAD
of misfolded membrane proteins.";
Cell Struct. Funct. 37:177-187(2012).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[40]
REVIEW.
PubMed=24121476; DOI=10.4161/auto.26448;
Stricher F., Macri C., Ruff M., Muller S.;
"HSPA8/HSC70 chaperone protein: structure, function, and chemical
targeting.";
Autophagy 9:1937-1954(2013).
[41]
SUBUNIT, AND INTERACTION WITH STUB1.
PubMed=23865999; DOI=10.1021/bi4009209;
Smith M.C., Scaglione K.M., Assimon V.A., Patury S., Thompson A.D.,
Dickey C.A., Southworth D.R., Paulson H.L., Gestwicki J.E.,
Zuiderweg E.R.;
"The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a
dynamic, tethered complex.";
Biochemistry 52:5354-5364(2013).
[42]
INTERACTION WITH FOXP3.
PubMed=23973223; DOI=10.1016/j.immuni.2013.08.006;
Chen Z., Barbi J., Bu S., Yang H.Y., Li Z., Gao Y., Jinasena D.,
Fu J., Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J.,
Gao Z., Tian H., Li Y., Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J.,
Dang E., Li Z., Wang H., Luo W., Li L., Semenza G.L., Zheng S.G.,
Loser K., Tsun A., Greene M.I., Pardoll D.M., Pan F., Li B.;
"The ubiquitin ligase Stub1 negatively modulates regulatory T cell
suppressive activity by promoting degradation of the transcription
factor Foxp3.";
Immunity 39:272-285(2013).
[43]
METHYLATION AT LYS-561, MUTAGENESIS OF LYS-561, AND INTERACTION WITH
METTL21A.
PubMed=23921388; DOI=10.1074/jbc.M113.483248;
Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S.,
Melki R., Falnes P.O.;
"Identification and characterization of a novel human
methyltransferase modulating Hsp70 function through lysine
methylation.";
J. Biol. Chem. 288:27752-27763(2013).
[44]
FUNCTION IN ERAD, AND INTERACTION WITH STUB1.
PubMed=23990462; DOI=10.1074/jbc.M113.479345;
Matsumura Y., Sakai J., Skach W.R.;
"Endoplasmic reticulum protein quality control is determined by
cooperative interactions between Hsp/c70 protein and the CHIP E3
ligase.";
J. Biol. Chem. 288:31069-31079(2013).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329 AND SER-541, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[46]
INTERACTION WITH PRKN.
PubMed=24270810; DOI=10.1038/nature12748;
Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A.,
Buehler E., Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E.,
Youle R.J.;
"High-content genome-wide RNAi screens identify regulators of parkin
upstream of mitophagy.";
Nature 504:291-295(2013).
[47]
INTERACTION WITH DNAJC12.
PubMed=24122553; DOI=10.1007/s12192-013-0471-6;
Choi J., Djebbar S., Fournier A., Labrie C.;
"The co-chaperone DNAJC12 binds to Hsc70 and is upregulated by
endoplasmic reticulum stress.";
Cell Stress Chaperones 19:439-446(2014).
[48]
INTERACTION WITH MLLT11.
PubMed=24880125; DOI=10.1016/j.yexcr.2014.05.013;
Li P., Ji M., Lu F., Zhang J., Li H., Cui T., Li Wang X., Tang D.,
Ji C.;
"Degradation of AF1Q by chaperone-mediated autophagy.";
Exp. Cell Res. 327:48-56(2014).
[49]
FUNCTION, AND INTERACTION WITH BAG1; BAG2; BAG3 AND HSPH1.
PubMed=24318877; DOI=10.1074/jbc.M113.521997;
Rauch J.N., Gestwicki J.E.;
"Binding of human nucleotide exchange factors to heat shock protein 70
(Hsp70) generates functionally distinct complexes in vitro.";
J. Biol. Chem. 289:1402-1414(2014).
[50]
INTERACTION WITH RNF207.
PubMed=25281747; DOI=10.1074/jbc.M114.592295;
Roder K., Werdich A.A., Li W., Liu M., Kim T.Y., Organ-Darling L.E.,
Moshal K.S., Hwang J.M., Lu Y., Choi B.R., MacRae C.A., Koren G.;
"RING finger protein RNF207, a novel regulator of cardiac
excitation.";
J. Biol. Chem. 289:33730-33740(2014).
[51]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[52]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-469 AND LYS-561, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[53]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-512, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[54]
INTERACTION WITH DNAJB12 AND DNAJB14.
PubMed=24732912; DOI=10.1371/journal.pone.0094322;
Goodwin E.C., Motamedi N., Lipovsky A., Fernandez-Busnadiego R.,
DiMaio D.;
"Expression of DNAJB12 or DNAJB14 causes coordinate invasion of the
nucleus by membranes associated with a novel nuclear pore structure.";
PLoS ONE 9:E94322-E94322(2014).
[55]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-512, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[56]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[57]
INTERACTION WITH DNAJC21.
PubMed=27346687; DOI=10.1016/j.ajhg.2016.05.002;
Tummala H., Walne A.J., Williams M., Bockett N., Collopy L.,
Cardoso S., Ellison A., Wynn R., Leblanc T., Fitzgibbon J.,
Kelsell D.P., van Heel D.A., Payne E., Plagnol V., Dokal I.,
Vulliamy T.;
"DNAJC21 mutations link a cancer-prone bone marrow failure syndrome to
corruption in 60S ribosome subunit maturation.";
Am. J. Hum. Genet. 99:115-124(2016).
[58]
REVIEW.
PubMed=26865365; DOI=10.1007/s12192-016-0676-6;
Radons J.;
"The human HSP70 family of chaperones: where do we stand?";
Cell Stress Chaperones 21:379-404(2016).
[59]
FUNCTION, INTERACTION WITH BAG1 AND BAG3, REGION NBD, AND REGION SBD.
PubMed=27474739; DOI=10.1074/jbc.M116.742502;
Rauch J.N., Zuiderweg E.R., Gestwicki J.E.;
"Non-canonical interactions between heat shock cognate protein 70
(Hsc70) and Bcl2-associated anthanogene (BAG) co-chaperones are
important for client release.";
J. Biol. Chem. 291:19848-19857(2016).
[60]
INTERACTION WITH HOPX; STUB1; HSP40 AND HSP90.
PubMed=27708256; DOI=10.1038/ncomms12882;
Seo J.H., Park J.H., Lee E.J., Vo T.T., Choi H., Kim J.Y., Jang J.K.,
Wee H.J., Lee H.S., Jang S.H., Park Z.Y., Jeong J., Lee K.J.,
Seok S.H., Park J.Y., Lee B.J., Lee M.N., Oh G.T., Kim K.W.;
"ARD1-mediated Hsp70 acetylation balances stress-induced protein
refolding and degradation.";
Nat. Commun. 7:12882-12882(2016).
[61]
INTERACTION WITH DNAJB12 AND DNAJB14.
PubMed=27916661; DOI=10.1016/j.molcel.2016.10.027;
Li K., Jiang Q., Bai X., Yang Y.F., Ruan M.Y., Cai S.Q.;
"Tetrameric assembly of K(+) channels requires ER-located chaperone
proteins.";
Mol. Cell 65:52-65(2017).
[62]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-634.
PubMed=19586912; DOI=10.1074/jbc.M109.033894;
Kajander T., Sachs J.N., Goldman A., Regan L.;
"Electrostatic interactions of Hsp-organizing protein
tetratricopeptide domains with Hsp70 and Hsp90: computational analysis
and protein engineering.";
J. Biol. Chem. 284:25364-25374(2009).
[63]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 4-381 IN COMPLEXES WITH ATP
AND ATP ANALOGS.
PubMed=19256508; DOI=10.1021/jm801627a;
Williamson D.S., Borgognoni J., Clay A., Daniels Z., Dokurno P.,
Drysdale M.J., Foloppe N., Francis G.L., Graham C.J., Howes R.,
Macias A.T., Murray J.B., Parsons R., Shaw T., Surgenor A.E.,
Terry L., Wang Y., Wood M., Massey A.J.;
"Novel adenosine-derived inhibitors of 70 kDa heat shock protein,
discovered through structure-based design.";
J. Med. Chem. 52:1510-1513(2009).
[64]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 4-381 IN COMPLEXES WITH ATP
ANALOGS.
PubMed=21526763; DOI=10.1021/jm101625x;
Macias A.T., Williamson D.S., Allen N., Borgognoni J., Clay A.,
Daniels Z., Dokurno P., Drysdale M.J., Francis G.L., Graham C.J.,
Howes R., Matassova N., Murray J.B., Parsons R., Shaw T.,
Surgenor A.E., Terry L., Wang Y., Wood M., Massey A.J.;
"Adenosine-derived inhibitors of 78 kDa glucose regulated protein
(Grp78) ATPase: insights into isoform selectivity.";
J. Med. Chem. 54:4034-4041(2011).
-!- FUNCTION: Molecular chaperone implicated in a wide variety of
cellular processes, including protection of the proteome from
stress, folding and transport of newly synthesized polypeptides,
activation of proteolysis of misfolded proteins and the formation
and dissociation of protein complexes. Plays a pivotal role in the
protein quality control system, ensuring the correct folding of
proteins, the re-folding of misfolded proteins and controlling the
targeting of proteins for subsequent degradation (PubMed:21150129,
PubMed:21148293, PubMed:24732912, PubMed:27916661,
PubMed:23018488). This is achieved through cycles of ATP binding,
ATP hydrolysis and ADP release, mediated by co-chaperones
(PubMed:21150129, PubMed:21148293, PubMed:24732912,
PubMed:27916661, PubMed:23018488). The co-chaperones have been
shown to not only regulate different steps of the ATPase cycle of
HSP70, but they also have an individual specificity such that one
co-chaperone may promote folding of a substrate while another may
promote degradation (PubMed:21150129, PubMed:21148293,
PubMed:24732912, PubMed:27916661, PubMed:23018488). The affinity
of HSP70 for polypeptides is regulated by its nucleotide bound
state. In the ATP-bound form, it has a low affinity for substrate
proteins. However, upon hydrolysis of the ATP to ADP, it undergoes
a conformational change that increases its affinity for substrate
proteins. HSP70 goes through repeated cycles of ATP hydrolysis and
nucleotide exchange, which permits cycles of substrate binding and
release. The HSP70-associated co-chaperones are of three types: J-
domain co-chaperones HSP40s (stimulate ATPase hydrolysis by
HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3
(facilitate conversion of HSP70 from the ADP-bound to the ATP-
bound state thereby promoting substrate release), and the TPR
domain chaperones such as HOPX and STUB1 (PubMed:24318877,
PubMed:27474739, PubMed:24121476, PubMed:26865365). Acts as a
repressor of transcriptional activation. Inhibits the
transcriptional coactivator activity of CITED1 on Smad-mediated
transcription. Component of the PRP19-CDC5L complex that forms an
integral part of the spliceosome and is required for activating
pre-mRNA splicing. May have a scaffolding role in the spliceosome
assembly as it contacts all other components of the core complex.
Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced
inflammatory response, including TNF secretion by monocytes
(PubMed:10722728, PubMed:11276205). Participates in the ER-
associated degradation (ERAD) quality control pathway in
conjunction with J domain-containing co-chaperones and the E3
ligase STUB1 (PubMed:23990462). {ECO:0000269|PubMed:10722728,
ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:21148293,
ECO:0000269|PubMed:21150129, ECO:0000269|PubMed:23018488,
ECO:0000269|PubMed:23990462, ECO:0000269|PubMed:24318877,
ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27474739,
ECO:0000269|PubMed:27916661, ECO:0000303|PubMed:24121476,
ECO:0000303|PubMed:26865365}.
-!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
containing untranslated mRNAs. Interacts with PACRG. Interacts
with HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1. Interacts
with DNAJC7. Interacts with DNAJB12 (via J domain)
(PubMed:21150129, PubMed:21148293, PubMed:24732912,
PubMed:27916661). Interacts with DNAJB14 (via J domain)
(PubMed:23018488, PubMed:24732912, PubMed:27916661). Interacts
(via C-terminus) with the E3 ligase CHIP forming a 210 kDa complex
of one CHIP and two HSPA8 molecules. Interacts with CITED1 (via N-
terminus); the interaction suppresses the association of CITED1 to
p300/CBP and Smad-mediated transcription transactivation.
Component of the PRP19-CDC5L splicing complex composed of a core
complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and
BCAS2, and at least three less stably associated proteins CTNNBL1,
CWC15 and HSPA8. Interacts with SV40 VP1. Interacts with TRIM5.
Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8,
CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex
may have a histone H3-specific methyltransferase activity.
Interacts with METTL21A. Following LPS binding, may form a complex
with CXCR4, GDF5 and HSP90AA1. Interacts with PRKN. Interacts with
FOXP3. Interacts with DNAJC9 (via J domain) (PubMed:17182002).
Interacts with MLLT11 (PubMed:24880125). Interacts with RNF207
(PubMed:25281747). Interacts with DNAJC21 (PubMed:27346687).
Interacts with DNAJB2 (PubMed:15936278). Interacts with TTC1 (via
TPR repeats) (PubMed:15708368). Interacts with SGTA (via TPR
repeats) (By similarity). Interacts with HSF1 (via transactivation
domain) (PubMed:9499401). Interacts with HOPX, HSP40 and HSP90
(PubMed:27708256). Interacts with STUB1 (PubMed:27708256).
Interacts with BAG2 (PubMed:24318877). Interacts with BAG3
(PubMed:27474739, PubMed:24318877). Interacts with DNAJC12
(PubMed:24122553). {ECO:0000250|UniProtKB:P63018,
ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:11147964,
ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:14532270,
ECO:0000269|PubMed:15708368, ECO:0000269|PubMed:15936278,
ECO:0000269|PubMed:15963462, ECO:0000269|PubMed:16815975,
ECO:0000269|PubMed:17182002, ECO:0000269|PubMed:17289661,
ECO:0000269|PubMed:19131338, ECO:0000269|PubMed:20053985,
ECO:0000269|PubMed:21148293, ECO:0000269|PubMed:21150129,
ECO:0000269|PubMed:23018488, ECO:0000269|PubMed:23865999,
ECO:0000269|PubMed:23921388, ECO:0000269|PubMed:23973223,
ECO:0000269|PubMed:23990462, ECO:0000269|PubMed:24122553,
ECO:0000269|PubMed:24270810, ECO:0000269|PubMed:24318877,
ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:24880125,
ECO:0000269|PubMed:25281747, ECO:0000269|PubMed:27346687,
ECO:0000269|PubMed:27474739, ECO:0000269|PubMed:27708256,
ECO:0000269|PubMed:27916661, ECO:0000269|PubMed:9305631,
ECO:0000269|PubMed:9499401, ECO:0000269|PubMed:9679980}.
-!- INTERACTION:
Q99IB8:- (xeno); NbExp=3; IntAct=EBI-351896, EBI-6927928;
P60709:ACTB; NbExp=2; IntAct=EBI-351896, EBI-353944;
Q9GZX7:AICDA; NbExp=2; IntAct=EBI-351896, EBI-3834328;
P49407:ARRB1; NbExp=4; IntAct=EBI-351896, EBI-743313;
P32121:ARRB2; NbExp=4; IntAct=EBI-351896, EBI-714559;
Q9NQ11:ATP13A2; NbExp=2; IntAct=EBI-351896, EBI-6308763;
Q99933:BAG1; NbExp=10; IntAct=EBI-351896, EBI-1030678;
O95816:BAG2; NbExp=3; IntAct=EBI-351896, EBI-355275;
Q8AZK7:EBNA-LP (xeno); NbExp=3; IntAct=EBI-351896, EBI-1185167;
P00533:EGFR; NbExp=5; IntAct=EBI-351896, EBI-297353;
O14976:GAK; NbExp=5; IntAct=EBI-351896, EBI-714707;
Q9NZL4:HSPBP1; NbExp=7; IntAct=EBI-351896, EBI-356763;
P05412:JUN; NbExp=3; IntAct=EBI-351896, EBI-852823;
P00338:LDHA; NbExp=4; IntAct=EBI-351896, EBI-372327;
Q5S007:LRRK2; NbExp=5; IntAct=EBI-351896, EBI-5323863;
P03485:M (xeno); NbExp=4; IntAct=EBI-351896, EBI-2547543;
P14598:NCF1; NbExp=2; IntAct=EBI-351896, EBI-395044;
Q9UNE7:STUB1; NbExp=5; IntAct=EBI-351896, EBI-357085;
Q9UNE7-1:STUB1; NbExp=4; IntAct=EBI-351908, EBI-15687717;
P61764:STXBP1; NbExp=2; IntAct=EBI-351896, EBI-960169;
O00635:TRIM38; NbExp=5; IntAct=EBI-351896, EBI-2130415;
-!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Nucleus, nucleolus.
Cell membrane. Note=Localized in cytoplasmic mRNP granules
containing untranslated mRNAs. Translocates rapidly from the
cytoplasm to the nuclei, and especially to the nucleoli, upon heat
shock.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P11142-1; Sequence=Displayed;
Name=2; Synonyms=HSC54;
IsoId=P11142-2; Sequence=VSP_002427;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11276205}.
-!- INDUCTION: Constitutively synthesized.
-!- DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known
as the ATPase domain) is responsible for binding and hydrolyzing
ATP. The C-terminal substrate-binding domain (SBD) (also known as
peptide-binding domain) binds to the client/substrate proteins.
The two domains are allosterically coupled so that, when ATP is
bound to the NBD, the SBD binds relatively weakly to clients. When
ADP is bound in the NBD, a conformational change enhances the
affinity of the SBD for client proteins.
{ECO:0000269|PubMed:9305631}.
-!- PTM: Acetylated. {ECO:0000269|Ref.5, ECO:0000269|Ref.6}.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798,
ECO:0000269|PubMed:16815975}.
-!- PTM: Trimethylation at Lys-561 reduces fibrillar SNCA binding.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y00371; CAA68445.1; -; Genomic_DNA.
EMBL; AB034951; BAB18615.1; -; mRNA.
EMBL; AF352832; AAK17898.1; -; mRNA.
EMBL; BC016179; AAH16179.1; -; mRNA.
EMBL; BC016660; AAH16660.1; -; mRNA.
EMBL; BC019816; AAH19816.1; -; mRNA.
CCDS; CCDS44754.1; -. [P11142-2]
CCDS; CCDS8440.1; -. [P11142-1]
PIR; A27077; A27077.
RefSeq; NP_006588.1; NM_006597.5. [P11142-1]
RefSeq; NP_694881.1; NM_153201.3. [P11142-2]
RefSeq; XP_011541100.1; XM_011542798.1. [P11142-1]
UniGene; Hs.180414; -.
PDB; 3AGY; X-ray; 1.85 A; C/D/F=639-646.
PDB; 3AGZ; X-ray; 2.51 A; C/D/E/F=639-646.
PDB; 3ESK; X-ray; 2.05 A; B=635-646.
PDB; 3FZF; X-ray; 2.20 A; A=4-381.
PDB; 3FZH; X-ray; 2.00 A; A=4-381.
PDB; 3FZK; X-ray; 2.10 A; A=4-381.
PDB; 3FZL; X-ray; 2.20 A; A=4-381.
PDB; 3FZM; X-ray; 2.30 A; A=4-381.
PDB; 3LDQ; X-ray; 1.90 A; A=4-381.
PDB; 3M3Z; X-ray; 2.10 A; A=4-381.
PDB; 4H5N; X-ray; 1.86 A; A/B=2-384.
PDB; 4H5R; X-ray; 1.64 A; A/B=2-384.
PDB; 4H5T; X-ray; 1.90 A; A=2-384.
PDB; 4H5V; X-ray; 1.75 A; A=2-384.
PDB; 4H5W; X-ray; 1.94 A; A/B=2-384.
PDB; 4HWI; X-ray; 2.27 A; A=5-381.
PDB; 4KBQ; X-ray; 2.91 A; C/D=541-646.
PDB; 5AQF; X-ray; 1.88 A; A/C=1-381.
PDB; 5AQG; X-ray; 2.24 A; A/C/E=1-381.
PDB; 5AQH; X-ray; 2.00 A; A=1-381.
PDB; 5AQI; X-ray; 1.98 A; A/C=1-381.
PDB; 5AQJ; X-ray; 1.96 A; A/C/E=1-381.
PDB; 5AQK; X-ray; 2.09 A; A=1-381.
PDB; 5AQL; X-ray; 1.69 A; A/C=1-381.
PDB; 5AQM; X-ray; 1.63 A; A/C=1-381.
PDB; 5AQN; X-ray; 2.45 A; A/C/E=1-381.
PDB; 5AQO; X-ray; 2.12 A; A/C/E=1-381.
PDB; 5AQP; X-ray; 2.08 A; A/C/E=1-381.
PDB; 5AQQ; X-ray; 2.72 A; A/C/E=1-381.
PDB; 5AQR; X-ray; 1.91 A; A/C/E=1-381.
PDB; 5AQS; X-ray; 2.00 A; A/C=1-381.
PDB; 5AQT; X-ray; 1.90 A; A=1-381.
PDB; 5AQU; X-ray; 1.92 A; A=1-381.
PDB; 5AQV; X-ray; 1.75 A; A=1-381.
PDBsum; 3AGY; -.
PDBsum; 3AGZ; -.
PDBsum; 3ESK; -.
PDBsum; 3FZF; -.
PDBsum; 3FZH; -.
PDBsum; 3FZK; -.
PDBsum; 3FZL; -.
PDBsum; 3FZM; -.
PDBsum; 3LDQ; -.
PDBsum; 3M3Z; -.
PDBsum; 4H5N; -.
PDBsum; 4H5R; -.
PDBsum; 4H5T; -.
PDBsum; 4H5V; -.
PDBsum; 4H5W; -.
PDBsum; 4HWI; -.
PDBsum; 4KBQ; -.
PDBsum; 5AQF; -.
PDBsum; 5AQG; -.
PDBsum; 5AQH; -.
PDBsum; 5AQI; -.
PDBsum; 5AQJ; -.
PDBsum; 5AQK; -.
PDBsum; 5AQL; -.
PDBsum; 5AQM; -.
PDBsum; 5AQN; -.
PDBsum; 5AQO; -.
PDBsum; 5AQP; -.
PDBsum; 5AQQ; -.
PDBsum; 5AQR; -.
PDBsum; 5AQS; -.
PDBsum; 5AQT; -.
PDBsum; 5AQU; -.
PDBsum; 5AQV; -.
ProteinModelPortal; P11142; -.
SMR; P11142; -.
BioGrid; 109544; 560.
CORUM; P11142; -.
DIP; DIP-32874N; -.
IntAct; P11142; 126.
MINT; MINT-4998609; -.
STRING; 9606.ENSP00000227378; -.
BindingDB; P11142; -.
ChEMBL; CHEMBL1275223; -.
iPTMnet; P11142; -.
PhosphoSitePlus; P11142; -.
SwissPalm; P11142; -.
DMDM; 123648; -.
DOSAC-COBS-2DPAGE; P11142; -.
OGP; P11142; -.
REPRODUCTION-2DPAGE; IPI00003865; -.
SWISS-2DPAGE; P11142; -.
UCD-2DPAGE; P11142; -.
EPD; P11142; -.
PaxDb; P11142; -.
PeptideAtlas; P11142; -.
PRIDE; P11142; -.
TopDownProteomics; P11142-1; -. [P11142-1]
TopDownProteomics; P11142-2; -. [P11142-2]
DNASU; 3312; -.
Ensembl; ENST00000227378; ENSP00000227378; ENSG00000109971. [P11142-1]
Ensembl; ENST00000453788; ENSP00000404372; ENSG00000109971. [P11142-2]
Ensembl; ENST00000532636; ENSP00000437125; ENSG00000109971. [P11142-1]
Ensembl; ENST00000534624; ENSP00000432083; ENSG00000109971. [P11142-1]
GeneID; 3312; -.
KEGG; hsa:3312; -.
UCSC; uc001pyp.5; human. [P11142-1]
CTD; 3312; -.
DisGeNET; 3312; -.
EuPathDB; HostDB:ENSG00000109971.13; -.
GeneCards; HSPA8; -.
H-InvDB; HIX0033867; -.
HGNC; HGNC:5241; HSPA8.
HPA; CAB002056; -.
HPA; HPA052504; -.
MIM; 600816; gene.
neXtProt; NX_P11142; -.
OpenTargets; ENSG00000109971; -.
PharmGKB; PA29507; -.
eggNOG; KOG0101; Eukaryota.
eggNOG; COG0443; LUCA.
GeneTree; ENSGT00900000140908; -.
HOGENOM; HOG000228135; -.
HOVERGEN; HBG051845; -.
InParanoid; P11142; -.
KO; K03283; -.
OMA; AYTKNQD; -.
OrthoDB; EOG091G03SF; -.
PhylomeDB; P11142; -.
TreeFam; TF105042; -.
BRENDA; 3.6.3.51; 2681.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-HSA-3371568; Attenuation phase.
Reactome; R-HSA-3371571; HSF1-dependent transactivation.
Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-HSA-447041; CHL1 interactions.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-8876725; Protein methylation.
Reactome; R-HSA-888590; GABA synthesis, release, reuptake and degradation.
SIGNOR; P11142; -.
ChiTaRS; HSPA8; human.
EvolutionaryTrace; P11142; -.
GeneWiki; HSPA8; -.
GenomeRNAi; 3312; -.
PMAP-CutDB; P11142; -.
PRO; PR:P11142; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000109971; -.
CleanEx; HS_HSPA8; -.
ExpressionAtlas; P11142; baseline and differential.
Genevisible; P11142; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; TAS:ParkinsonsUK-UCL.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0005770; C:late endosome; IEA:Ensembl.
GO; GO:0098575; C:lumenal side of lysosomal membrane; TAS:ParkinsonsUK-UCL.
GO; GO:0043202; C:lysosomal lumen; TAS:ParkinsonsUK-UCL.
GO; GO:0005765; C:lysosomal membrane; ISS:ParkinsonsUK-UCL.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0000974; C:Prp19 complex; IDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
GO; GO:0016887; F:ATPase activity; IDA:BHF-UCL.
GO; GO:0042623; F:ATPase activity, coupled; TAS:Reactome.
GO; GO:0055131; F:C3HC4-type RING finger domain binding; IPI:BHF-UCL.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0001664; F:G-protein coupled receptor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB.
GO; GO:0001786; F:phosphatidylserine binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
GO; GO:0046034; P:ATP metabolic process; IDA:BHF-UCL.
GO; GO:0009267; P:cellular response to starvation; TAS:ParkinsonsUK-UCL.
GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IEA:Ensembl.
GO; GO:0061684; P:chaperone-mediated autophagy; ISS:ParkinsonsUK-UCL.
GO; GO:1904764; P:chaperone-mediated autophagy translocation complex disassembly; ISS:ParkinsonsUK-UCL.
GO; GO:0061741; P:chaperone-mediated protein transport involved in chaperone-mediated autophagy; NAS:ParkinsonsUK-UCL.
GO; GO:0072318; P:clathrin coat disassembly; IEA:Ensembl.
GO; GO:0061738; P:late endosomal microautophagy; IEA:Ensembl.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:1902904; P:negative regulation of supramolecular fiber organization; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0007269; P:neurotransmitter secretion; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0044829; P:positive regulation by host of viral genome replication; IEA:Ensembl.
GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
GO; GO:0006457; P:protein folding; NAS:UniProtKB.
GO; GO:0006479; P:protein methylation; TAS:Reactome.
GO; GO:0042026; P:protein refolding; IDA:UniProtKB.
GO; GO:0061740; P:protein targeting to lysosome involved in chaperone-mediated autophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0043254; P:regulation of protein complex assembly; TAS:ParkinsonsUK-UCL.
GO; GO:0061635; P:regulation of protein complex stability; ISS:ParkinsonsUK-UCL.
GO; GO:1904589; P:regulation of protein import; TAS:ParkinsonsUK-UCL.
GO; GO:0031647; P:regulation of protein stability; IMP:ParkinsonsUK-UCL.
GO; GO:0006986; P:response to unfolded protein; NAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Cell membrane; Chaperone; Complete proteome; Cytoplasm;
Direct protein sequencing; Host-virus interaction; Isopeptide bond;
Membrane; Methylation; mRNA processing; mRNA splicing;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repressor; Spliceosome; Stress response;
Transcription; Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000269|Ref.5, ECO:0000269|Ref.6}.
CHAIN 2 646 Heat shock cognate 71 kDa protein.
/FTId=PRO_0000078270.
NP_BIND 12 15 ATP.
NP_BIND 202 204 ATP.
NP_BIND 268 275 ATP.
NP_BIND 339 342 ATP.
REGION 2 386 Nucleotide-binding domain (NBD).
{ECO:0000305|PubMed:27474739}.
REGION 186 377 Interaction with BAG1.
REGION 394 509 Substrate-binding domain (SBD).
{ECO:0000305|PubMed:27474739}.
BINDING 71 71 ATP.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000269|Ref.5, ECO:0000269|Ref.6}.
MOD_RES 108 108 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 153 153 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 246 246 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 319 319 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 319 319 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 328 328 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 469 469 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 512 512 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 512 512 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 524 524 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 541 541 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A;
alternate. {ECO:0000269|PubMed:23349634,
ECO:0000269|PubMed:23921388}.
MOD_RES 561 561 N6,N6-dimethyllysine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 589 589 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 597 597 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 601 601 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 512 512 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 512 512 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447}.
VAR_SEQ 464 616 Missing (in isoform 2).
{ECO:0000303|PubMed:11093761}.
/FTId=VSP_002427.
VARIANT 32 32 D -> Y (in dbSNP:rs11551602).
/FTId=VAR_049619.
VARIANT 459 459 F -> L (in dbSNP:rs11551598).
/FTId=VAR_049620.
MUTAGEN 561 561 K->R: Complete loss of in vitro
methylation by METTL21A.
{ECO:0000269|PubMed:23349634,
ECO:0000269|PubMed:23921388}.
STRAND 7 10 {ECO:0000244|PDB:5AQM}.
STRAND 13 22 {ECO:0000244|PDB:5AQM}.
STRAND 25 28 {ECO:0000244|PDB:5AQM}.
STRAND 36 39 {ECO:0000244|PDB:5AQM}.
STRAND 42 44 {ECO:0000244|PDB:5AQM}.
STRAND 49 51 {ECO:0000244|PDB:5AQM}.
HELIX 53 57 {ECO:0000244|PDB:5AQM}.
TURN 58 61 {ECO:0000244|PDB:5AQM}.
HELIX 63 65 {ECO:0000244|PDB:5AQM}.
HELIX 70 72 {ECO:0000244|PDB:5AQM}.
TURN 73 75 {ECO:0000244|PDB:5AQM}.
HELIX 81 87 {ECO:0000244|PDB:5AQM}.
STRAND 91 97 {ECO:0000244|PDB:5AQM}.
STRAND 100 107 {ECO:0000244|PDB:5AQM}.
STRAND 110 114 {ECO:0000244|PDB:5AQM}.
HELIX 116 135 {ECO:0000244|PDB:5AQM}.
STRAND 136 138 {ECO:0000244|PDB:5AQF}.
STRAND 141 146 {ECO:0000244|PDB:5AQM}.
HELIX 152 164 {ECO:0000244|PDB:5AQM}.
STRAND 168 174 {ECO:0000244|PDB:5AQM}.
HELIX 175 182 {ECO:0000244|PDB:5AQM}.
HELIX 185 187 {ECO:0000244|PDB:5AQM}.
STRAND 188 191 {ECO:0000244|PDB:5AQL}.
STRAND 193 201 {ECO:0000244|PDB:5AQM}.
STRAND 204 213 {ECO:0000244|PDB:5AQM}.
STRAND 216 225 {ECO:0000244|PDB:5AQM}.
HELIX 230 249 {ECO:0000244|PDB:5AQM}.
HELIX 253 255 {ECO:0000244|PDB:3LDQ}.
HELIX 257 276 {ECO:0000244|PDB:5AQM}.
STRAND 278 288 {ECO:0000244|PDB:5AQM}.
STRAND 291 298 {ECO:0000244|PDB:5AQM}.
HELIX 299 305 {ECO:0000244|PDB:5AQM}.
HELIX 307 312 {ECO:0000244|PDB:5AQM}.
HELIX 314 324 {ECO:0000244|PDB:5AQM}.
HELIX 328 330 {ECO:0000244|PDB:5AQM}.
STRAND 333 338 {ECO:0000244|PDB:5AQM}.
HELIX 339 342 {ECO:0000244|PDB:5AQM}.
HELIX 344 353 {ECO:0000244|PDB:5AQM}.
TURN 354 356 {ECO:0000244|PDB:5AQM}.
STRAND 357 360 {ECO:0000244|PDB:3FZF}.
TURN 365 367 {ECO:0000244|PDB:5AQM}.
HELIX 368 380 {ECO:0000244|PDB:5AQM}.
HELIX 541 556 {ECO:0000244|PDB:4KBQ}.
HELIX 564 582 {ECO:0000244|PDB:4KBQ}.
HELIX 594 612 {ECO:0000244|PDB:4KBQ}.
HELIX 613 616 {ECO:0000244|PDB:4KBQ}.
STRAND 641 644 {ECO:0000244|PDB:3AGY}.
SEQUENCE 646 AA; 70898 MW; 9AA27B210730670C CRC64;
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS
SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA
IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH
FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN
KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI
DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN
SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD


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