Search in Entrez for 
Search for Sequence Id(s) 
LOCUS       NP_006588                646 aa            linear   PRI 12-MAR-2011
DEFINITION  heat shock cognate 71 kDa protein isoform 1 [Homo sapiens].
ACCESSION   NP_006588
VERSION     NP_006588.1  GI:5729877
DBSOURCE    REFSEQ: accession NM_006597.3
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   Hirschhausen,N., Schlesier,T., Schmidt,M.A., Gotz,F., Peters,G. and
            Heilmann,C.
  TITLE     A novel staphylococcal internalization mechanism involves the major
            autolysin Atl and heat shock cognate protein Hsc70 as host cell
            receptor
  JOURNAL   Cell. Microbiol. 12 (12), 1746-1764 (2010)
   PUBMED   20642807
  REMARK    GeneRIF: The importance of Hsc70 in AtlE adhesin-mediated
            internalization was demonstrated by the inhibition of
            Staphylococcus aureus internalization with anti-Hsc70 antibodies.
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Clapp,K.M., Peng,H.M., Morishima,Y., Lau,M., Walker,V.J.,
            Pratt,W.B. and Osawa,Y.
  TITLE     C331A mutant of neuronal nitric-oxide synthase is labilized for
            Hsp70/CHIP (C terminus of HSC70-interacting protein)-dependent
            ubiquitination
  JOURNAL   J. Biol. Chem. 285 (44), 33642-33651 (2010)
   PUBMED   20729196
  REMARK    GeneRIF: the C331A mutant of neuronal nitric-oxide synthase is
            labilized for Hsp70/CHIP (C terminus of HSC70-interacting
            protein)-dependent ubiquitination
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Guinez,C., Mir,A.M., Martin,N., Leprince,D., Michalski,J.C.,
            Vergoten,G. and Lefebvre,T.
  TITLE     Arginine 469 is a pivotal residue for the Hsc70-GlcNAc-binding
            property
  JOURNAL   Biochem. Biophys. Res. Commun. 400 (4), 537-542 (2010)
   PUBMED   20804732
  REMARK    GeneRIF: This is the first work reporting the localization of the
            GlcNAc-binding domain of a member of the HSP70 family.
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Shiota,M., Saiwai,H., Mun,S., Harada,A., Okada,S., Odawara,J.,
            Tanaka,M., Iwao,H. and Ohkawa,Y.
  TITLE     Generation of a rat monoclonal antibody specific for heat shock
            cognate protein 70
  JOURNAL   Hybridoma (Larchmt) 29 (5), 453-456 (2010)
   PUBMED   21050049
  REMARK    GeneRIF: Immunocytochemical staining using this newly established
            antibody revealed that Hsc70 localizes predominantly in the
            cytoplasm in unstressed cells, whereas oxidative stress produced by
            H2O2 induces Hsc70 to translocate into the nucleus.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Ebrahimi,M., Mohammadi,P., Daryadel,A. and Baharvand,H.
  TITLE     Assessment of heat shock protein (HSP60, HSP72, HSP90, and HSC70)
            expression in cultured limbal stem cells following air lifting
  JOURNAL   Mol. Vis. 16, 1680-1688 (2010)
   PUBMED   20806039
  REMARK    GeneRIF: The aim of this study is to examine the expression of
            HSP60, HSP72, and HSP90, and heat-shock cognate 70 (HCS70) at the
            mRNA and protein level in differentiating corneal cells from limbal
            stem cells following air exposure.
            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
            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 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 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 cognate protein, 71-kDa; heat shock 70kD
                     protein 8; 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; MGC131511; MGC29929; NIP71"
                     /coded_by="NM_006597.3:79..2019"
                     /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
//