Search in Entrez for 
Search for Sequence Id(s) 
LOCUS       NP_006588                646 aa            linear   PRI 18-SEP-2017
DEFINITION  heat shock cognate 71 kDa protein isoform 1 [Homo sapiens].
ACCESSION   NP_006588
VERSION     NP_006588.1
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   Ganguly A, Han X, Das U, Wang L, Loi J, Sun J, Gitler D, Caillol G,
            Leterrier C, Yates JR 3rd and Roy S.
  TITLE     Hsc70 chaperone activity is required for the cytosolic slow axonal
            transport of synapsin
  JOURNAL   J. Cell Biol. 216 (7), 2059-2074 (2017)
   PUBMED   28559423
  REMARK    GeneRIF: Synapsin is part of a multiprotein complex enriched in
            chaperones/cochaperones including Hsc70. Hsc70 chaperone activity
            is required for the cytosolic slow axonal transport of synapsin.
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Dupzyk A, Williams JM, Bagchi P, Inoue T and Tsai B.
  TITLE     SGTA-Dependent Regulation of Hsc70 Promotes Cytosol Entry of Simian
            Virus 40 from the Endoplasmic Reticulum
  JOURNAL   J. Virol. 91 (12), e00232-17 (2017)
   PUBMED   28356524
  REMARK    GeneRIF: study demonstrates a critical role of Hsc70 in SV40
            endoplasmic reticulum-to-cytosol penetration and reveal how SGTA
            controls Hsc70 to impact this process
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Geng J, Li H, Huang C, Chai J, Zheng R, Li F and Jiang S.
  TITLE     Functional analysis of HSPA1A and HSPA8 in parturition
  JOURNAL   Biochem. Biophys. Res. Commun. 483 (1), 371-379 (2017)
   PUBMED   28025138
  REMARK    GeneRIF: HSPA1A and HSPA8 have roles in parturition through
            stimulating immune inflammatory and estrogen response
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Li K, Jiang Q, Bai X, Yang YF, Ruan MY and Cai SQ.
  TITLE     Tetrameric Assembly of K+ Channels Requires ER-Located Chaperone
            Proteins
  JOURNAL   Mol. Cell 65 (1), 52-65 (2017)
   PUBMED   27916661
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Seo JH, Park JH, Lee EJ, Vo TT, Choi H, Kim JY, Jang JK, Wee HJ,
            Lee HS, Jang SH, Park ZY, Jeong J, Lee KJ, Seok SH, Park JY, Lee
            BJ, Lee MN, Oh GT and Kim KW.
  TITLE     ARD1-mediated Hsp70 acetylation balances stress-induced protein
            refolding and degradation
  JOURNAL   Nat Commun 7, 12882 (2016)
   PUBMED   27708256
  REMARK    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 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   Chiang HL, Terlecky SR, Plant CP and Dice JF.
  TITLE     A role for a 70-kilodalton heat shock protein in lysosomal
            degradation of intracellular proteins
  JOURNAL   Science 246 (4928), 382-385 (1989)
   PUBMED   2799391
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 :: FJ224294.1, SRR1803612.77063.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437 [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; heat
                     shock 70kDa protein 8"
                     /calculated_mol_wt=70767
     Region          1..613
                     /region_name="HSP70"
                     /note="Hsp70 protein; cl26953"
                     /db_xref="CDD:331774"
     Region          2..386
                     /region_name="Nucleotide-binding domain (NBD).
                     {ECO:0000305|PubMed:27474739}"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            2
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N-acetylserine. {ECO:0000244|PubMed:19413330,
                     ECO:0000269|Ref.5, ECO:0000269|Ref.6}; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            108
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine. {ECO:0000250|UniProtKB:P63017};
                     propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            153
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:17525332};
                     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. {ECO:0000244|PubMed:19608861};
                     propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            319
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine, alternate.
                     {ECO:0000244|PubMed:19608861}; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            319
                     /site_type="modified"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-succinyllysine, alternate.
                     {ECO:0000250|UniProtKB:P63017}; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            328
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine. {ECO:0000250|UniProtKB:P63017};
                     propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            329
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:23186163};
                     propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            362
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:20068231};
                     propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Region          394..509
                     /region_name="Substrate-binding domain (SBD).
                     {ECO:0000305|PubMed:27474739}"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            469
                     /site_type="methylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Omega-N-methylarginine.
                     {ECO:0000244|PubMed:24129315}; 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, alternate.
                     {ECO:0000250|UniProtKB:P63017}; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            512
                     /site_type="modified"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-succinyllysine, alternate.
                     {ECO:0000250|UniProtKB:P63017}; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            524
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine. {ECO:0000250|UniProtKB:P63017};
                     propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            541
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:23186163};
                     propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            561
                     /site_type="methylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6,N6,N6-trimethyllysine, by METTL21A, alternate.
                     {ECO:0000269|PubMed:23349634,
                     ECO:0000269|PubMed:23921388}; N6,N6-dimethyllysine,
                     alternate. {ECO:0000244|PubMed:24129315}; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            589
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine. {ECO:0000244|PubMed:19608861};
                     propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            597
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine. {ECO:0000244|PubMed:19608861};
                     propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            601
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine. {ECO:0000244|PubMed:19608861};
                     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="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
//