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LOCUS       NP_006588                646 aa            linear   PRI 17-APR-2013
DEFINITION  heat shock cognate 71 kDa protein isoform 1 [Homo sapiens].
VERSION     NP_006588.1  GI:5729877
DBSOURCE    REFSEQ: accession NM_006597.4
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   Cloutier,P., Lavallee-Adam,M., Faubert,D., Blanchette,M. and
  TITLE     A newly uncovered group of distantly related lysine
            methyltransferases preferentially interact with molecular
            chaperones to regulate their activity
  JOURNAL   PLoS Genet. 9 (1), E1003210 (2013)
   PUBMED   23349634
  REMARK    GeneRIF: Trimethylated at Lys-561 by METTL21A
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Zagouri,F., Sergentanis,T.N., Gazouli,M., Tsigginou,A.,
            Dimitrakakis,C., Papaspyrou,I., Eleutherakis-Papaiakovou,E.,
            Chrysikos,D., Theodoropoulos,G., Zografos,G.C., Antsaklis,A.,
            Dimopoulos,A.M. and Papadimitriou,C.A.
  TITLE     HSP90, HSPA8, HIF-1 alpha and HSP70-2 polymorphisms in breast
            cancer: a case-control study
  JOURNAL   Mol. Biol. Rep. 39 (12), 10873-10879 (2012)
   PUBMED   23065205
  REMARK    GeneRIF: This case control study aims to investigate the role of
            HSP90 Gln488His (C > G), HSP70-2 P1/P2, HIF-1 alpha C1772T and
            HSPA8 intronic 1541-1542delGT polymorphisms as potential risk
            factors and/or prognostic markers for breast cancer.
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Redeker,V., Pemberton,S., Bienvenut,W., Bousset,L. and Melki,R.
  TITLE     Identification of protein interfaces between alpha-synuclein, the
            principal component of Lewy bodies in Parkinson disease, and the
            molecular chaperones human Hsc70 and the yeast Ssa1p
  JOURNAL   J. Biol. Chem. 287 (39), 32630-32639 (2012)
   PUBMED   22843682
  REMARK    GeneRIF: the client binding domain of Hsc70 and Ssa1p binds two
            regions within alpha-Syn similar to a tweezer, with the first
            spanning residues 10-45 and the second spanning residues 97-102.
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Gong,X., Luo,T., Deng,P., Liu,Z., Xiu,J., Shi,H. and Jiang,Y.
  TITLE     Stress-induced interaction between p38 MAPK and HSP70
  JOURNAL   Biochem. Biophys. Res. Commun. 425 (2), 357-362 (2012)
   PUBMED   22842575
  REMARK    GeneRIF: thise preliminary result indicated that HSP70 was related
            to the phosphorylation of MK2, a specific nuclear downstream target
            of p38, suggesting HSP70 is a potential chaperone for the nuclear
            translocation of p38.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Qi,L., Zhang,X.D., Wu,J.C., Lin,F., Wang,J., DiFiglia,M. and
  TITLE     The role of chaperone-mediated autophagy in huntingtin degradation
  JOURNAL   PLoS ONE 7 (10), E46834 (2012)
   PUBMED   23071649
  REMARK    GeneRIF: Studies suggest that Hsc70 and lysosome-associated protein
            2A (LAMP-2A) through chaperone-mediated autophagy (CMA) play a role
            in the clearance of Htt and suggest a novel strategy to target the
            degradation of mutant huntingtin (Htt).
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 AK310467.1, BC019816.2 and
            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.
            Transcript exon combination :: BC016660.1, AK129885.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           ERS025084, ERS025088 [ECO:0000348]
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Homo sapiens"
     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"
     Region          1..613
                     /note="heat shock 70 kDa protein; Provisional"
     Site            2
                     /experiment="experimental evidence, no additional details
                     /note="N-acetylserine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Region          6..381
                     /note="Nucleotide-binding domain of HSPA1-A, -B, -L,
                     HSPA-2, -6, -7, -8, and similar proteins; cd10233"
     Site            order(10,12..15,71,147,175,199..204,206,230..231,268,
                     /note="nucleotide binding site [chemical binding]"
     Site            order(23,25,27,32..34,36,50,54,57,133..134,258,262,269,
                     /note="NEF/HSP70 interaction site [polypeptide binding]"
     Site            order(33,35,57,60..61,257..258,261..262,265..266,269,
                     /note="BAG/HSP70 interaction site [polypeptide binding]"
     Site            order(152,192,213,215..217,219..220,325)
                     /note="SBD interface [polypeptide binding]"
     Site            153
                     /experiment="experimental evidence, no additional details
                     /note="Phosphoserine; propagated from UniProtKB/Swiss-Prot
     Site            153
                     /experiment="experimental evidence, no additional details
     Region          186..377
                     /region_name="Interaction with BAG1"
                     /experiment="experimental evidence, no additional details
                     /note="propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            246
                     /experiment="experimental evidence, no additional details
                     /note="N6-acetyllysine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            319
                     /experiment="experimental evidence, no additional details
                     /note="N6-acetyllysine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            362
                     /experiment="experimental evidence, no additional details
                     /note="Phosphoserine; propagated from UniProtKB/Swiss-Prot
     Site            477
                     /experiment="experimental evidence, no additional details
     Site            589
                     /experiment="experimental evidence, no additional details
                     /note="N6-acetyllysine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            597
                     /experiment="experimental evidence, no additional details
                     /note="N6-acetyllysine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            601
                     /experiment="experimental evidence, no additional details
                     /note="N6-acetyllysine; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     CDS             1..646
                     /gene_synonym="HSC54; HSC70; HSC71; HSP71; HSP73; HSPA10;
                     LAP1; 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