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LOCUS       NP_006588                646 aa            linear   PRI 26-MAY-2014
DEFINITION  heat shock cognate 71 kDa protein isoform 1 [Homo sapiens].
ACCESSION   NP_006588
VERSION     NP_006588.1  GI:5729877
DBSOURCE    REFSEQ: accession NM_006597.5
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   Bozidis P, Hyphantis T, Mantas C, Sotiropoulou M, Antypa N,
            Andreoulakis E, Serretti A, Mavreas V and Antoniou K.
  TITLE     HSP70 polymorphisms in first psychotic episode drug-naive
            schizophrenic patients
  JOURNAL   Life Sci. 100 (2), 133-137 (2014)
   PUBMED   24548631
  REMARK    GeneRIF: HSP8A polymorphism is associated with drug-naive
            schizophrenia.
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Connarn JN, Assimon VA, Reed RA, Tse E, Southworth DR, Zuiderweg
            ER, Gestwicki JE and Sun D.
  TITLE     The molecular chaperone Hsp70 activates protein phosphatase 5 (PP5)
            by binding the tetratricopeptide repeat (TPR) domain
  JOURNAL   J. Biol. Chem. 289 (5), 2908-2917 (2014)
   PUBMED   24327656
  REMARK    GeneRIF: These results demonstrate that Hsp70 recruits PP5 and
            activates its phosphatase activity which suggests dual roles for
            PP5 that might link chaperone systems with signaling pathways in
            cancer and development.
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Matsumura Y, Sakai J and Skach WR.
  TITLE     Endoplasmic reticulum protein quality control is determined by
            cooperative interactions between Hsp/c70 protein and the CHIP E3
            ligase
  JOURNAL   J. Biol. Chem. 288 (43), 31069-31079 (2013)
   PUBMED   23990462
  REMARK    GeneRIF: the U-box mutation stimulated CHIP binding to Hsc70 while
            promoting CHIP oligomerization. CHIP binding to Hsc70 binding was
            also stimulated by the presence of an Hsc70 client with a
            preference for the ADP-bound state.
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Ferreira JV, Fofo H, Bejarano E, Bento CF, Ramalho JS, Girao H and
            Pereira P.
  TITLE     STUB1/CHIP is required for HIF1A degradation by chaperone-mediated
            autophagy
  JOURNAL   Autophagy 9 (9), 1349-1366 (2013)
   PUBMED   23880665
  REMARK    GeneRIF: the ubiquitin ligase STUB1 is required for degradation of
            HIF1A in the lysosome by chaperone-mediated autophagy.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Hatakeyama T, Dai P, Harada Y, Hino H, Tsukahara F, Maru Y, Otsuji
            E and Takamatsu T.
  TITLE     Connexin43 functions as a novel interacting partner of heat shock
            cognate protein 70
  JOURNAL   Sci Rep 3, 2719 (2013)
   PUBMED   24056538
  REMARK    GeneRIF: Cx43-Hsc70 interaction probably plays a critical role
            during G1/S progression.
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 HH, van Damme J, Puype M, Gesser B, Celis JE 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 YC, 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 DB, Parham P and Hill BL.
  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 MY, Davis N, Zhang JY and Bose HR 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 WJ and Mizzen LA.
  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 DC312904.1, DC395565.1,
            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.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC016660.1, AK129885.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           ERS025087, ERS025093 [ECO:0000348]
            ##Evidence-Data-END##
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; epididymis luminal protein 33;
                     epididymis secretory sperm binding protein Li 72p"
                     /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            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"
                     /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, alternate; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            362
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine; propagated from UniProtKB/Swiss-Prot
                     (P11142.1)"
     Site            477
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /citation=[7]
     Site            561
                     /site_type="methylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6,N6,N6-trimethyllysine, by METTL21A; 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)"
     CDS             1..646
                     /gene="HSPA8"
                     /gene_synonym="HEL-33; HEL-S-72p; HSC54; HSC70; HSC71;
                     HSP71; HSP73; HSPA10; LAP-1; LAP1; NIP71"
                     /coded_by="NM_006597.5:278..2218"
                     /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
//