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LOCUS       NP_006588                646 aa            linear   PRI 05-MAY-2012
DEFINITION  heat shock cognate 71 kDa protein isoform 1 [Homo sapiens].
ACCESSION   NP_006588
VERSION     NP_006588.1  GI:5729877
DBSOURCE    REFSEQ: accession NM_006597.4
KEYWORDS    RefSeq.
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   Kaufer,S., Coffey,C.M. and Parker,J.S.
  TITLE     The cellular chaperone hsc70 is specifically recruited to reovirus
            viral factories independently of its chaperone function
  JOURNAL   J. Virol. 86 (2), 1079-1089 (2012)
   PUBMED   22090113
  REMARK    GeneRIF: Hsc70 is recruited to reovirus viral factories
            independently of its chaperone function.
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Cho,H.J., Gee,H.Y., Baek,K.H., Ko,S.K., Park,J.M., Lee,H.,
            Kim,N.D., Lee,M.G. and Shin,I.
  TITLE     A small molecule that binds to an ATPase domain of Hsc70 promotes
            membrane trafficking of mutant cystic fibrosis transmembrane
            conductance regulator
  JOURNAL   J. Am. Chem. Soc. 133 (50), 20267-20276 (2011)
   PUBMED   22074182
  REMARK    GeneRIF: It is proposed that Az suppresses ubiquitination of
            DeltaF508-CFTR maybe by blocking interaction of the mutant with
            Hsc70 and CHIP, and, as a consequence, it enhances membrane
            trafficking of the mutant
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Patterson,K.R., Ward,S.M., Combs,B., Voss,K., Kanaan,N.M.,
            Morfini,G., Brady,S.T., Gamblin,T.C. and Binder,L.I.
  TITLE     Heat shock protein 70 prevents both tau aggregation and the
            inhibitory effects of preexisting tau aggregates on fast axonal
            transport
  JOURNAL   Biochemistry 50 (47), 10300-10310 (2011)
   PUBMED   22039833
  REMARK    GeneRIF: Addition of Hsp70 to a mixture of oligomeric and fibrillar
            tau aggregates prevents the toxic effect of these tau species on
            fast axonal transport.
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Meimaridou,E., Gooljar,S.B., Ramnarace,N., Anthonypillai,L.,
            Clark,A.J. and Chapple,J.P.
  TITLE     The cytosolic chaperone Hsc70 promotes traffic to the cell surface
            of intracellular retained melanocortin-4 receptor mutants
  JOURNAL   Mol. Endocrinol. 25 (9), 1650-1660 (2011)
   PUBMED   21719532
  REMARK    GeneRIF: The ability of the cytosolic cognate 70-kDa heat-shock
            protein (Hsc70) chaperone system to modulate cell surface
            expression of MC4R, was investigated.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Chen,K., Luo,Z., Tang,J. and Zheng,S.J.
  TITLE     A critical role of heat shock cognate protein 70 in Apoptin-induced
            phosphorylation of Akt
  JOURNAL   Biochem. Biophys. Res. Commun. 409 (2), 200-204 (2011)
   PUBMED   21565169
  REMARK    GeneRIF: Apoptin induced the translocation of endogenous Hsc70 from
            the cytoplasm to the nucleus, and both were co-localized in the
            nucleus.
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
            Vandekerckhove,J.
  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 AK310467.1, BC019816.2 and
            AK222628.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the heat shock protein 70
            family, which contains both heat-inducible and constitutively
            expressed members. This protein belongs to the latter group, which
            are also referred to as heat-shock cognate proteins. It functions
            as a chaperone, and 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. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.1"
     Protein         1..646
                     /product="heat shock cognate 71 kDa protein isoform 1"
                     /note="heat shock 70kd protein 10; constitutive heat shock
                     protein 70; lipopolysaccharide-associated protein 1;
                     LPS-associated protein 1; heat shock cognate protein 54;
                     heat shock cognate 71 kDa protein; 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"
     Site            2
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N-acetylserine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     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            15
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphotyrosine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     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            41
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphotyrosine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            88
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            107
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphotyrosine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            108
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            113
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine; propagated from UniProtKB/Swiss-Prot
                     (P11142.1)"
     Site            115
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphotyrosine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            120
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine; propagated from UniProtKB/Swiss-Prot
                     (P11142.1)"
     Site            121
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine; propagated from UniProtKB/Swiss-Prot
                     (P11142.1)"
     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"
                     /note="Phosphoserine; propagated from UniProtKB/Swiss-Prot
                     (P11142.1)"
     Site            153
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /citation=[6]
     Region          186..377
                     /region_name="Interaction with BAG1"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            246
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            319
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            348
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            477
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphothreonine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            477
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /citation=[7]
     Site            512
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            524
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            541
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine; propagated from UniProtKB/Swiss-Prot
                     (P11142.1)"
     Site            589
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            597
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            601
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            637
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine; propagated from UniProtKB/Swiss-Prot
                     (P11142.1)"
     Site            638
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine; propagated from UniProtKB/Swiss-Prot
                     (P11142.1)"
     CDS             1..646
                     /gene="HSPA8"
                     /gene_synonym="HSC54; HSC70; HSC71; HSP71; HSP73; HSPA10;
                     LAP1; NIP71"
                     /coded_by="NM_006597.4:136..2076"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8440.1"
                     /db_xref="GeneID:3312"
                     /db_xref="HGNC:HGNC:5241"
                     /db_xref="HPRD:07205"
                     /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
//