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LOCUS       NP_006588                646 aa            linear   PRI 28-JAN-2005
DEFINITION  heat shock 70kDa protein 8 isoform 1 [Homo sapiens].
ACCESSION   NP_006588
VERSION     NP_006588.1  GI:5729877
DBSOURCE    REFSEQ: accession NM_006597.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (sites)
  AUTHORS   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. and Elledge,S.J.
  TITLE     ATM and ATR substrate analysis reveals extensive protein networks
            responsive to DNA damage
  JOURNAL   Science 316 (5828), 1160-1166 (2007)
   PUBMED   17525332
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Yamagishi,N., Ishihara,K. and Hatayama,T.
  TITLE     Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70
            ATPase activity
  JOURNAL   J. Biol. Chem. 279 (40), 41727-41733 (2004)
   PUBMED   15292236
  REMARK    GeneRIF: Hsp105alpha is suggested to regulate the substrate binding
            cycle of Hsp70/Hsc70 by inhibiting the ATPase activity of
            Hsp70/Hsc70, thereby functioning as a negative regulator of the
            Hsp70/Hsc70 chaperone system.
REFERENCE   3  (sites)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Burch,A.D. and Weller,S.K.
  TITLE     Nuclear sequestration of cellular chaperone and proteasomal
            machinery during herpes simplex virus type 1 infection
  JOURNAL   J. Virol. 78 (13), 7175-7185 (2004)
   PUBMED   15194794
  REMARK    GeneRIF: sequestered in discrete foci in the nucleus of the
            infected cell in herpes simplex virus type 1 infection.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Tsukahara,F. and Maru,Y.
  TITLE     Identification of novel nuclear export and nuclear
            localization-related signals in human heat shock cognate protein 70
  JOURNAL   J. Biol. Chem. 279 (10), 8867-8872 (2004)
   PUBMED   14684748
  REMARK    GeneRIF: a novel nuclear export and nuclear localization-related
            signals in human Hsp70
REFERENCE   6  (residues 1 to 646)
  AUTHORS   G, De Gassart,A., Blanc,L. and Vidal,M.
  TITLE     Degradation of AP2 during reticulocyte maturation enhances binding
            of hsc70 and Alix to a common site on TFR for sorting into exosomes
  JOURNAL   Traffic 5 (3), 181-193 (2004)
   PUBMED   15086793
  REMARK    GeneRIF: a region of the TfR that can potentially interact with
            hsc70
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Shimura,H., Schwartz,D., Gygi,S.P. and Kosik,K.S.
  TITLE     CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances
            cell survival
  JOURNAL   J. Biol. Chem. 279 (6), 4869-4876 (2004)
   PUBMED   14612456
  REMARK    GeneRIF: tau binds to Hsc70, and its phosphorylation is a
            recognition requirement for the addition of ubiquitin
REFERENCE   8  (residues 1 to 646)
  AUTHORS   Wehner,P.S., Nielsen,B. and Hokland,M.
  TITLE     Expression levels of hsc70 and hsp60 are developmentally regulated
            during B-cell maturation and not associated to childhood c-ALL at
            presentation or relapse
  JOURNAL   Eur. J. Haematol. 71 (2), 100-108 (2003)
   PUBMED   12890148
  REMARK    GeneRIF: no abnormal levels of hsc70 and hsp60 were detectable in
            pediatric c-ALL pre B-cells at diagnosis nor at relapse. In
            contrast, developmentally regulated levels of hsc70 and hsp60
            expression during B-cell ontogenesis were observed
REFERENCE   9  (residues 1 to 646)
  AUTHORS   Kim,C.D., Lee,M.H. and Roh,S.S.
  TITLE     Identification of androgen-regulated genes in SV40-transformed
            human hair dermal papilla cells
  JOURNAL   J. Dermatol. Sci. 32 (2), 143-149 (2003)
   PUBMED   12850307
  REMARK    GeneRIF: Hsc70 may be involved in androgen action on dermal papilla
            cells.
REFERENCE   10 (residues 1 to 646)
  AUTHORS   Shin,B.K., Wang,H., Yim,A.M., Le Naour,F., Brichory,F., Jang,J.H.,
            Zhao,R., Puravs,E., Tra,J., Michael,C.W., Misek,D.E. and
            Hanash,S.M.
  TITLE     Global profiling of the cell surface proteome of cancer cells
            uncovers an abundance of proteins with chaperone function
  JOURNAL   J. Biol. Chem. 278 (9), 7607-7616 (2003)
   PUBMED   12493773
REFERENCE   11 (residues 1 to 646)
  AUTHORS   Noessner,E., Gastpar,R., Milani,V., Brandl,A., Hutzler,P.J.,
            Kuppner,M.C., Roos,M., Kremmer,E., Asea,A., Calderwood,S.K. and
            Issels,R.D.
  TITLE     Tumor-derived heat shock protein 70 peptide complexes are
            cross-presented by human dendritic cells
  JOURNAL   J. Immunol. 169 (10), 5424-5432 (2002)
   PUBMED   12421917
  REMARK    GeneRIF: Tumor-derived HSP70 peptide complexes have the immunogenic
            potential to instruct dendritic cells to cross-present endogenously
            expressed, nonmutated, and tumor antigenic peptides shared among
            tumors of the melanocytic lineage for T cell recognition.
REFERENCE   12 (residues 1 to 646)
  AUTHORS   Gurer,C., Cimarelli,A. and Luban,J.
  TITLE     Specific incorporation of heat shock protein 70 family members into
            primate lentiviral virions
  JOURNAL   J. Virol. 76 (9), 4666-4670 (2002)
   PUBMED   11932435
REFERENCE   13 (residues 1 to 646)
  AUTHORS   Triantafilou,K., Triantafilou,M. and Dedrick,R.L.
  TITLE     A CD14-independent LPS receptor cluster
  JOURNAL   Nat. Immunol. 2 (4), 338-345 (2001)
   PUBMED   11276205
REFERENCE   14 (residues 1 to 646)
  AUTHORS   Tsukahara,F., Yoshioka,T. and Muraki,T.
  TITLE     Molecular and functional characterization of HSC54, a novel variant
            of human heat-shock cognate protein 70
  JOURNAL   Mol. Pharmacol. 58 (6), 1257-1263 (2000)
   PUBMED   11093761
REFERENCE   15 (residues 1 to 646)
  AUTHORS   Agostini,I., Popov,S., Li,J., Dubrovsky,L., Hao,T. and Bukrinsky,M.
  TITLE     Heat-shock protein 70 can replace viral protein R of HIV-1 during
            nuclear import of the viral preintegration complex
  JOURNAL   Exp. Cell Res. 259 (2), 398-403 (2000)
   PUBMED   10964507
REFERENCE   16 (residues 1 to 646)
  AUTHORS   O'Keeffe,B., Fong,Y., Chen,D., Zhou,S. and Zhou,Q.
  TITLE     Requirement for a kinase-specific chaperone pathway in the
            production of a Cdk9/cyclin T1 heterodimer responsible for
            P-TEFb-mediated tat stimulation of HIV-1 transcription
  JOURNAL   J. Biol. Chem. 275 (1), 279-287 (2000)
   PUBMED   10617616
REFERENCE   17 (residues 1 to 646)
  AUTHORS   Egerton,M., Moritz,R.L., Druker,B., Kelso,A. and Simpson,R.J.
  TITLE     Identification of the 70kD heat shock cognate protein (Hsc70) and
            alpha-actinin-1 as novel phosphotyrosine-containing proteins in T
            lymphocytes
  JOURNAL   Biochem. Biophys. Res. Commun. 224 (3), 666-674 (1996)
   PUBMED   8713105
REFERENCE   18 (residues 1 to 646)
  AUTHORS   Tavaria,M., Gabriele,T., Anderson,R.L., Mirault,M.E., Baker,E.,
            Sutherland,G. and Kola,I.
  TITLE     Localization of the gene encoding the human heat shock cognate
            protein, HSP73, to chromosome 11
  JOURNAL   Genomics 29 (1), 266-268 (1995)
   PUBMED   8530083
REFERENCE   19 (residues 1 to 646)
  AUTHORS   Rensing,S.A. and Maier,U.G.
  TITLE     Phylogenetic analysis of the stress-70 protein family
  JOURNAL   J. Mol. Evol. 39 (1), 80-86 (1994)
   PUBMED   7545947
REFERENCE   20 (residues 1 to 646)
  AUTHORS   Dworniczak,B. and Mirault,M.E.
  TITLE     Structure and expression of a human gene coding for a 71 kd heat
            shock 'cognate' protein
  JOURNAL   Nucleic Acids Res. 15 (13), 5181-5197 (1987)
   PUBMED   3037489
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC019816.2 and AK096100.1.
            
            Summary: The product encoded by this gene belongs to the heat shock
            protein 70 family which contains both heat-inducible and
            constitutively expressed members. The latter are called heat-shock
            cognate proteins. This gene encodes a heat-shock cognate protein.
            This protein binds to nascent polypeptides to facilitate correct
            folding. It also functions as an ATPase in the disassembly of
            clathrin-coated vesicles during transport of membrane components
            through the cell. Two alternatively spliced variants have been
            characterized to date.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.1"
     Protein         1..646
                     /product="heat shock 70kDa protein 8 isoform 1"
                     /note="heat shock cognate protein, 71-kDa; heat shock 70kD
                     protein 8; heat shock 70kd protein 10; heat shock cognate
                     protein 54; constitutive heat shock protein 70;
                     lipopolysaccharide-associated protein 1; LPS-associated
                     protein 1; uncharacterized bone marrow protein BM034;
                     N-myristoyltransferase inhibitor protein 71"
                     /calculated_mol_wt=70767
     Region          1..613
                     /region_name="PTZ00009"
                     /note="heat shock 70 kDa protein; Provisional"
                     /db_xref="CDD:240227"
     Region          6..381
                     /region_name="HSPA1-2_6-8-like_NBD"
                     /note="Nucleotide-binding domain of HSPA1-A, -B, -L,
                     HSPA-2, -6, -7, -8, and similar proteins; cd10233"
                     /db_xref="CDD:212675"
     Site            order(10,12..15,71,147,175,199..204,206,230..231,268,
                     271..272,275,338..340,342..343,366)
                     /site_type="other"
                     /note="nucleotide binding site [chemical binding]"
                     /db_xref="CDD:212675"
     Site            order(23,25,27,32..34,36,50,54,57,133..134,258,262,269,
                     272..273,276,281,283,285..286,290,342)
                     /site_type="other"
                     /note="NEF/HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:212675"
     Site            order(33,35,57,60..61,257..258,261..262,265..266,269,
                     283..286,292,294)
                     /site_type="other"
                     /note="BAG/HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:212675"
     Site            order(152,192,213,215..217,219..220,325)
                     /site_type="other"
                     /note="SBD interface [polypeptide binding]"
                     /db_xref="CDD:212675"
     Site            153
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /citation=[1]
     Site            477
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /citation=[3]
     CDS             1..646
                     /gene="HSPA8"
                     /gene_synonym="HSC54; HSC70; HSC71; HSP71; HSP73; HSPA10;
                     LAP1; MGC29929; NIP71"
                     /coded_by="NM_006597.3:79..2019"
                     /GO_component="GO:0005634 - nucleus [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA];
                     GO:0042623 - ATPase activity, coupled [Evidence NAS] [PMID
                     8530083]; GO:0051082 - unfolded protein binding [Evidence
                     IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence NAS]
                     [PMID 8530083]; GO:0006986 - response to unfolded protein
                     [Evidence IEA]"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:3312"
                     /db_xref="MIM:600816"
ORIGIN      
        1 mskgpavgid lgttyscvgv fqhgkveiia ndqgnrttps yvaftdterl igdaaknqva
       61 mnptntvfda krligrrfdd avvqsdmkhw pfmvvndagr pkvqveykge tksfypeevs
      121 smvltkmkei aeaylgktvt navvtvpayf ndsqrqatkd agtiaglnvl riineptaaa
      181 iaygldkkvg aernvlifdl gggtfdvsil tiedgifevk stagdthlgg edfdnrmvnh
      241 fiaefkrkhk kdisenkrav rrlrtacera krtlssstqa sieidslyeg idfytsitra
      301 rfeelnadlf rgtldpveka lrdakldksq ihdivlvggs tripkiqkll qdffngkeln
      361 ksinpdeava ygaavqaail sgdksenvqd lllldvtpls lgietaggvm tvlikrntti
      421 ptkqtqtftt ysdnqpgvli qvyegeramt kdnnllgkfe ltgippaprg vpqievtfdi
      481 dangilnvsa vdkstgkenk ititndkgrl skediermvq eaekykaede kqrdkvsskn
      541 slesyafnmk atvedeklqg kindedkqki ldkcneiinw ldknqtaeke efehqqkele
      601 kvcnpiitkl yqsaggmpgg mpggfpggga ppsggassgp tieevd
//