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LOCUS       NP_006588                646 aa            linear   PRI 21-FEB-2010
DEFINITION  heat shock 70kDa protein 8 isoform 1 [Homo sapiens].
VERSION     NP_006588.1
DBSOURCE    REFSEQ: accession NM_006597.3
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Nirde,P., Derocq,D., Maynadier,M., Chambon,M., Basile,I.,
            Gary-Bobo,M. and Garcia,M.
  TITLE     Heat shock cognate 70 protein secretion as a new growth arrest
            signal for cancer cells
  JOURNAL   Oncogene 29 (1), 117-127 (2010)
   PUBMED   19802014
  REMARK    GeneRIF: Data show that Hsc70 appears active in breast cancer cells
            and hypersecreted by direct cath D inhibition.
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nishigaki,Y., Nozawa,Y. and
  TITLE     Association of genetic variants with chronic kidney disease in
            individuals with different lipid profiles
  JOURNAL   Int. J. Mol. Med. 24 (2), 233-246 (2009)
   PUBMED   19578796
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Imamura,Y., Fujigaki,Y., Oomori,Y., Usui,S. and Wang,P.L.
  TITLE     Cooperation of salivary protein histatin 3 with heat shock cognate
            protein 70 relative to the G1/S transition in human gingival
  JOURNAL   J. Biol. Chem. 284 (21), 14316-14325 (2009)
   PUBMED   19321452
  REMARK    GeneRIF: These findings suggest that histatin 3 may be involved in
            cell proliferation through the regulation of HSC70 and p27(Kip1) in
            oral cells.
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Hayashi,Y., Horie,M., Daito,T., Honda,T., Ikuta,K. and Tomonaga,K.
  TITLE     Heat shock cognate protein 70 controls Borna disease virus
            replication via interaction with the viral non-structural protein X
  JOURNAL   Microbes Infect. 11 (3), 394-402 (2009)
   PUBMED   19397879
  REMARK    GeneRIF: These data indicate that Hsc70 may be involved in viral
            replication by regulating the intracellular distribution of X.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Watanabe,K., Tachibana,M., Kim,S. and Watarai,M.
  TITLE     EEVD motif of heat shock cognate protein 70 contributes to
            bacterial uptake by trophoblast giant cells
  JOURNAL   J. Biomed. Sci. 16, 113 (2009)
   PUBMED   20003465
  REMARK    GeneRIF: surface located Hsc70 on trophoblast giant cells mediates
            the uptake of pathogenic bacteria and proteins containing the TPR
            domain inhibit the function of Hsc70 by binding to its EEVD motif
            GeneRIF: surface located Hsc70 on trophoblast giant cells mediates
            the uptake of pathogenic bacteria and proteins containing the TPR
            domain inhibit the function of Hsc70 by binding to its EEVD motif
            Publication Status: Online-Only
REFERENCE   6  (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   7  (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   8  (residues 1 to 646)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   9  (residues 1 to 646)
  AUTHORS   Hattori,H., Liu,Y.C., Tohnai,I., Ueda,M., Kaneda,T., Kobayashi,T.,
            Tanabe,K. and Ohtsuka,K.
  TITLE     Intracellular localization and partial amino acid sequence of a
            stress-inducible 40-kDa protein in HeLa cells
  JOURNAL   Cell Struct. Funct. 17 (1), 77-86 (1992)
   PUBMED   1586970
REFERENCE   10 (residues 1 to 646)
  AUTHORS   DeLuca-Flaherty,C., McKay,D.B., Parham,P. and Hill,B.L.
  TITLE     Uncoating protein (hsc70) binds a conformationally labile domain of
            clathrin light chain LCa to stimulate ATP hydrolysis
  JOURNAL   Cell 62 (5), 875-887 (1990)
   PUBMED   1975516
REFERENCE   11 (residues 1 to 646)
  AUTHORS   Lim,M.Y., Davis,N., Zhang,J.Y. and Bose,H.R. Jr.
  TITLE     The v-rel oncogene product is complexed with cellular proteins
            including its proto-oncogene product and heat shock protein 70
  JOURNAL   Virology 175 (1), 149-160 (1990)
   PUBMED   2155506
REFERENCE   12 (residues 1 to 646)
  AUTHORS   Welch,W.J. and Mizzen,L.A.
  TITLE     Characterization of the thermotolerant cell. II. Effects on the
            intracellular distribution of heat-shock protein 70, intermediate
            filaments, and small nuclear ribonucleoprotein complexes
  JOURNAL   J. Cell Biol. 106 (4), 1117-1130 (1988)
   PUBMED   2966179
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. [provided by RefSeq].
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform.
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the
            Entrez Gene record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Homo sapiens"
     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; N-myristoyltransferase inhibitor protein 71"
     Region          1..613
                     /note="Hsp70 protein; cl26953"
     Site            153
                     /experiment="experimental evidence, no additional details
     Site            477
                     /experiment="experimental evidence, no additional details
     CDS             1..646
                     /gene_synonym="HSC54; HSC70; HSC71; HSP71; HSP73; HSPA10;
                     LAP1; MGC131511; MGC29929; NIP71"
                     /note="isoform 1 is encoded by transcript variant 1"
        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