Full text data of HSPA6
HSPA6
(HSP70B')
[Confidence: low (only semi-automatic identification from reviews)]
Heat shock 70 kDa protein 6 (Heat shock 70 kDa protein B')
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Heat shock 70 kDa protein 6 (Heat shock 70 kDa protein B')
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P17066
ID HSP76_HUMAN Reviewed; 643 AA.
AC P17066; Q1HBA8; Q8IYK7; Q9BT95;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-SEP-2003, sequence version 2.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Heat shock 70 kDa protein 6;
DE AltName: Full=Heat shock 70 kDa protein B';
GN Name=HSPA6; Synonyms=HSP70B';
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Lung;
RX PubMed=2327978;
RA Leung T.K.C., Rajendran M.Y., Monfries C., Hall C., Lim L.;
RT "The human heat-shock protein family. Expression of a novel heat-
RT inducible HSP70 (HSP70B') and isolation of its cDNA and genomic DNA.";
RL Biochem. J. 267:125-132(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-65; GLN-95;
RP THR-150; SER-153; ASN-154; VAL-159; LYS-170; PRO-173; ALA-178;
RP LYS-194; PHE-198; LYS-297; ILE-464; HIS-471; GLU-528; GLU-562; GLN-577
RP AND ALA-626.
RG NIEHS SNPs program;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-250.
RX PubMed=1346391; DOI=10.1016/0888-7543(92)90409-L;
RA Leung T.K.C., Hall C., Rajendran M., Spurr N.K., Lim L.;
RT "The human heat-shock genes HSPA6 and HSPA7 are both expressed and
RT localize to chromosome 1.";
RL Genomics 12:74-79(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX PubMed=3184191; DOI=10.1016/0022-2836(88)90094-0;
RA Schiller P., Amin J., Ananthan J., Brown M.E., Scott W.A., Voellmy R.;
RT "Cis-acting elements involved in the regulated expression of a human
RT HSP70 gene.";
RL J. Mol. Biol. 203:97-105(1988).
RN [7]
RP METHYLATION AT LYS-563, AND MUTAGENESIS OF LYS-563.
RX PubMed=23921388; DOI=10.1074/jbc.M113.483248;
RA Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S.,
RA Melki R., Falnes P.O.;
RT "Identification and characterization of a novel human
RT methyltransferase modulating Hsp70 function through lysine
RT methylation.";
RL J. Biol. Chem. 288:27752-27763(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 6-385 IN COMPLEX WITH ADP
RP AND PHOSPHATE.
RX PubMed=20072699; DOI=10.1371/journal.pone.0008625;
RA Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T.,
RA Moche M., Schuler H.;
RT "Crystal structures of the ATPase domains of four human Hsp70
RT isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and
RT HSPA5/BiP/GRP78.";
RL PLoS ONE 5:E8625-E8625(2010).
CC -!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
CC preexistent proteins against aggregation and mediate the folding
CC of newly translated polypeptides in the cytosol as well as within
CC organelles. These chaperones participate in all these processes
CC through their ability to recognize nonnative conformations of
CC other proteins. They bind extended peptide segments with a net
CC hydrophobic character exposed by polypeptides during translation
CC and membrane translocation, or following stress-induced damage (By
CC similarity).
CC -!- INDUCTION: Only at higher temperatures, and no basal expression.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hspa6/";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X51757; CAA36061.1; -; Genomic_DNA.
DR EMBL; X51758; CAA36062.1; -; mRNA.
DR EMBL; DQ521571; ABF47108.1; -; Genomic_DNA.
DR EMBL; AL590385; CAI16120.1; -; Genomic_DNA.
DR EMBL; BC004279; AAH04279.1; -; mRNA.
DR EMBL; BC035665; AAH35665.1; -; mRNA.
DR EMBL; S78631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S09036; S09036.
DR RefSeq; NP_002146.2; NM_002155.3.
DR UniGene; Hs.654614; -.
DR PDB; 3FE1; X-ray; 2.20 A; A/B/C=6-385.
DR PDBsum; 3FE1; -.
DR ProteinModelPortal; P17066; -.
DR SMR; P17066; 6-615.
DR IntAct; P17066; 23.
DR MINT; MINT-1139180; -.
DR STRING; 9606.ENSP00000310219; -.
DR PhosphoSite; P17066; -.
DR DMDM; 34978357; -.
DR UCD-2DPAGE; P17066; -.
DR PaxDb; P17066; -.
DR PRIDE; P17066; -.
DR DNASU; 3310; -.
DR Ensembl; ENST00000309758; ENSP00000310219; ENSG00000173110.
DR GeneID; 3310; -.
DR KEGG; hsa:3310; -.
DR UCSC; uc001gaq.3; human.
DR CTD; 3310; -.
DR GeneCards; GC01P161495; -.
DR HGNC; HGNC:5239; HSPA6.
DR HPA; CAB017452; -.
DR HPA; HPA028549; -.
DR MIM; 140555; gene.
DR neXtProt; NX_P17066; -.
DR PharmGKB; PA29505; -.
DR eggNOG; COG0443; -.
DR HOGENOM; HOG000228135; -.
DR HOVERGEN; HBG051845; -.
DR InParanoid; P17066; -.
DR KO; K03283; -.
DR OMA; LEAYVFH; -.
DR OrthoDB; EOG7PCJGF; -.
DR PhylomeDB; P17066; -.
DR EvolutionaryTrace; P17066; -.
DR GeneWiki; HSPA6; -.
DR GenomeRNAi; 3310; -.
DR NextBio; 13127; -.
DR PRO; PR:P17066; -.
DR Bgee; P17066; -.
DR CleanEx; HS_HSPA6; -.
DR Genevestigator; P17066; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Complete proteome; Methylation;
KW Nucleotide-binding; Polymorphism; Reference proteome; Stress response.
FT CHAIN 1 643 Heat shock 70 kDa protein 6.
FT /FTId=PRO_0000078264.
FT NP_BIND 14 17 ATP.
FT NP_BIND 204 206 ATP.
FT NP_BIND 270 277 ATP.
FT NP_BIND 341 344 ATP.
FT BINDING 73 73 ATP.
FT MOD_RES 563 563 N6,N6,N6-trimethyllysine; by METTL21A; in
FT vitro.
FT VARIANT 65 65 P -> T.
FT /FTId=VAR_060718.
FT VARIANT 95 95 R -> Q.
FT /FTId=VAR_060719.
FT VARIANT 150 150 A -> T (in dbSNP:rs10919224).
FT /FTId=VAR_049605.
FT VARIANT 153 153 N -> S (in dbSNP:rs10919225).
FT /FTId=VAR_049606.
FT VARIANT 154 154 D -> N (in dbSNP:rs10919226).
FT /FTId=VAR_049607.
FT VARIANT 159 159 A -> V.
FT /FTId=VAR_060720.
FT VARIANT 170 170 N -> K (in dbSNP:rs41297704).
FT /FTId=VAR_049608.
FT VARIANT 173 173 R -> P (in dbSNP:rs41297708).
FT /FTId=VAR_049609.
FT VARIANT 178 178 P -> A (in dbSNP:rs41297710).
FT /FTId=VAR_049610.
FT VARIANT 194 194 E -> K (in dbSNP:rs41297714).
FT /FTId=VAR_049611.
FT VARIANT 198 198 L -> F (in dbSNP:rs1079109).
FT /FTId=VAR_024182.
FT VARIANT 260 260 R -> H (in dbSNP:rs41299256).
FT /FTId=VAR_049612.
FT VARIANT 297 297 T -> K.
FT /FTId=VAR_060721.
FT VARIANT 336 336 V -> F (in dbSNP:rs417707).
FT /FTId=VAR_059360.
FT VARIANT 464 464 S -> I (in dbSNP:rs388218).
FT /FTId=VAR_049613.
FT VARIANT 471 471 R -> H (in dbSNP:rs41299256).
FT /FTId=VAR_049614.
FT VARIANT 528 528 K -> E (in dbSNP:rs570189).
FT /FTId=VAR_049615.
FT VARIANT 528 528 K -> R (in dbSNP:rs570167).
FT /FTId=VAR_059361.
FT VARIANT 562 562 D -> E (in dbSNP:rs753856).
FT /FTId=VAR_024183.
FT VARIANT 572 572 M -> V (in dbSNP:rs452004).
FT /FTId=VAR_049616.
FT VARIANT 577 577 R -> Q (in dbSNP:rs368844).
FT /FTId=VAR_049617.
FT VARIANT 626 626 T -> A (in dbSNP:rs41299260).
FT /FTId=VAR_049618.
FT MUTAGEN 563 563 K->R: Complete loss of in vitro
FT methylation by METTL21A.
FT CONFLICT 106 108 RVC -> PVS (in Ref. 1; CAA36061).
FT CONFLICT 263 263 R -> G (in Ref. 1; CAA36061).
FT STRAND 9 12
FT STRAND 15 24
FT STRAND 27 30
FT STRAND 38 41
FT STRAND 44 46
FT STRAND 51 53
FT HELIX 55 59
FT TURN 60 63
FT HELIX 65 67
FT HELIX 72 74
FT TURN 75 77
FT HELIX 83 90
FT STRAND 93 99
FT STRAND 102 109
FT STRAND 112 116
FT HELIX 118 137
FT STRAND 143 148
FT HELIX 154 166
FT STRAND 170 176
FT HELIX 177 184
FT TURN 185 188
FT STRAND 195 202
FT STRAND 207 215
FT STRAND 218 227
FT HELIX 232 251
FT HELIX 259 275
FT TURN 276 278
FT STRAND 280 290
FT STRAND 293 300
FT HELIX 301 314
FT HELIX 316 326
FT HELIX 330 332
FT STRAND 334 340
FT HELIX 341 344
FT HELIX 346 355
FT TURN 356 358
FT TURN 367 369
FT HELIX 370 383
SQ SEQUENCE 643 AA; 71028 MW; BCE348F0226DB70B CRC64;
MQAPRELAVG IDLGTTYSCV GVFQQGRVEI LANDQGNRTT PSYVAFTDTE RLVGDAAKSQ
AALNPHNTVF DAKRLIGRKF ADTTVQSDMK HWPFRVVSEG GKPKVRVCYR GEDKTFYPEE
ISSMVLSKMK ETAEAYLGQP VKHAVITVPA YFNDSQRQAT KDAGAIAGLN VLRIINEPTA
AAIAYGLDRR GAGERNVLIF DLGGGTFDVS VLSIDAGVFE VKATAGDTHL GGEDFDNRLV
NHFMEEFRRK HGKDLSGNKR ALRRLRTACE RAKRTLSSST QATLEIDSLF EGVDFYTSIT
RARFEELCSD LFRSTLEPVE KALRDAKLDK AQIHDVVLVG GSTRIPKVQK LLQDFFNGKE
LNKSINPDEA VAYGAAVQAA VLMGDKCEKV QDLLLLDVAP LSLGLETAGG VMTTLIQRNA
TIPTKQTQTF TTYSDNQPGV FIQVYEGERA MTKDNNLLGR FELSGIPPAP RGVPQIEVTF
DIDANGILSV TATDRSTGKA NKITITNDKG RLSKEEVERM VHEAEQYKAE DEAQRDRVAA
KNSLEAHVFH VKGSLQEESL RDKIPEEDRR KMQDKCREVL AWLEHNQLAE KEEYEHQKRE
LEQICRPIFS RLYGGPGVPG GSSCGTQARQ GDPSTGPIIE EVD
//
ID HSP76_HUMAN Reviewed; 643 AA.
AC P17066; Q1HBA8; Q8IYK7; Q9BT95;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-SEP-2003, sequence version 2.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Heat shock 70 kDa protein 6;
DE AltName: Full=Heat shock 70 kDa protein B';
GN Name=HSPA6; Synonyms=HSP70B';
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Lung;
RX PubMed=2327978;
RA Leung T.K.C., Rajendran M.Y., Monfries C., Hall C., Lim L.;
RT "The human heat-shock protein family. Expression of a novel heat-
RT inducible HSP70 (HSP70B') and isolation of its cDNA and genomic DNA.";
RL Biochem. J. 267:125-132(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-65; GLN-95;
RP THR-150; SER-153; ASN-154; VAL-159; LYS-170; PRO-173; ALA-178;
RP LYS-194; PHE-198; LYS-297; ILE-464; HIS-471; GLU-528; GLU-562; GLN-577
RP AND ALA-626.
RG NIEHS SNPs program;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-250.
RX PubMed=1346391; DOI=10.1016/0888-7543(92)90409-L;
RA Leung T.K.C., Hall C., Rajendran M., Spurr N.K., Lim L.;
RT "The human heat-shock genes HSPA6 and HSPA7 are both expressed and
RT localize to chromosome 1.";
RL Genomics 12:74-79(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX PubMed=3184191; DOI=10.1016/0022-2836(88)90094-0;
RA Schiller P., Amin J., Ananthan J., Brown M.E., Scott W.A., Voellmy R.;
RT "Cis-acting elements involved in the regulated expression of a human
RT HSP70 gene.";
RL J. Mol. Biol. 203:97-105(1988).
RN [7]
RP METHYLATION AT LYS-563, AND MUTAGENESIS OF LYS-563.
RX PubMed=23921388; DOI=10.1074/jbc.M113.483248;
RA Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S.,
RA Melki R., Falnes P.O.;
RT "Identification and characterization of a novel human
RT methyltransferase modulating Hsp70 function through lysine
RT methylation.";
RL J. Biol. Chem. 288:27752-27763(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 6-385 IN COMPLEX WITH ADP
RP AND PHOSPHATE.
RX PubMed=20072699; DOI=10.1371/journal.pone.0008625;
RA Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T.,
RA Moche M., Schuler H.;
RT "Crystal structures of the ATPase domains of four human Hsp70
RT isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and
RT HSPA5/BiP/GRP78.";
RL PLoS ONE 5:E8625-E8625(2010).
CC -!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
CC preexistent proteins against aggregation and mediate the folding
CC of newly translated polypeptides in the cytosol as well as within
CC organelles. These chaperones participate in all these processes
CC through their ability to recognize nonnative conformations of
CC other proteins. They bind extended peptide segments with a net
CC hydrophobic character exposed by polypeptides during translation
CC and membrane translocation, or following stress-induced damage (By
CC similarity).
CC -!- INDUCTION: Only at higher temperatures, and no basal expression.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hspa6/";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X51757; CAA36061.1; -; Genomic_DNA.
DR EMBL; X51758; CAA36062.1; -; mRNA.
DR EMBL; DQ521571; ABF47108.1; -; Genomic_DNA.
DR EMBL; AL590385; CAI16120.1; -; Genomic_DNA.
DR EMBL; BC004279; AAH04279.1; -; mRNA.
DR EMBL; BC035665; AAH35665.1; -; mRNA.
DR EMBL; S78631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S09036; S09036.
DR RefSeq; NP_002146.2; NM_002155.3.
DR UniGene; Hs.654614; -.
DR PDB; 3FE1; X-ray; 2.20 A; A/B/C=6-385.
DR PDBsum; 3FE1; -.
DR ProteinModelPortal; P17066; -.
DR SMR; P17066; 6-615.
DR IntAct; P17066; 23.
DR MINT; MINT-1139180; -.
DR STRING; 9606.ENSP00000310219; -.
DR PhosphoSite; P17066; -.
DR DMDM; 34978357; -.
DR UCD-2DPAGE; P17066; -.
DR PaxDb; P17066; -.
DR PRIDE; P17066; -.
DR DNASU; 3310; -.
DR Ensembl; ENST00000309758; ENSP00000310219; ENSG00000173110.
DR GeneID; 3310; -.
DR KEGG; hsa:3310; -.
DR UCSC; uc001gaq.3; human.
DR CTD; 3310; -.
DR GeneCards; GC01P161495; -.
DR HGNC; HGNC:5239; HSPA6.
DR HPA; CAB017452; -.
DR HPA; HPA028549; -.
DR MIM; 140555; gene.
DR neXtProt; NX_P17066; -.
DR PharmGKB; PA29505; -.
DR eggNOG; COG0443; -.
DR HOGENOM; HOG000228135; -.
DR HOVERGEN; HBG051845; -.
DR InParanoid; P17066; -.
DR KO; K03283; -.
DR OMA; LEAYVFH; -.
DR OrthoDB; EOG7PCJGF; -.
DR PhylomeDB; P17066; -.
DR EvolutionaryTrace; P17066; -.
DR GeneWiki; HSPA6; -.
DR GenomeRNAi; 3310; -.
DR NextBio; 13127; -.
DR PRO; PR:P17066; -.
DR Bgee; P17066; -.
DR CleanEx; HS_HSPA6; -.
DR Genevestigator; P17066; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Complete proteome; Methylation;
KW Nucleotide-binding; Polymorphism; Reference proteome; Stress response.
FT CHAIN 1 643 Heat shock 70 kDa protein 6.
FT /FTId=PRO_0000078264.
FT NP_BIND 14 17 ATP.
FT NP_BIND 204 206 ATP.
FT NP_BIND 270 277 ATP.
FT NP_BIND 341 344 ATP.
FT BINDING 73 73 ATP.
FT MOD_RES 563 563 N6,N6,N6-trimethyllysine; by METTL21A; in
FT vitro.
FT VARIANT 65 65 P -> T.
FT /FTId=VAR_060718.
FT VARIANT 95 95 R -> Q.
FT /FTId=VAR_060719.
FT VARIANT 150 150 A -> T (in dbSNP:rs10919224).
FT /FTId=VAR_049605.
FT VARIANT 153 153 N -> S (in dbSNP:rs10919225).
FT /FTId=VAR_049606.
FT VARIANT 154 154 D -> N (in dbSNP:rs10919226).
FT /FTId=VAR_049607.
FT VARIANT 159 159 A -> V.
FT /FTId=VAR_060720.
FT VARIANT 170 170 N -> K (in dbSNP:rs41297704).
FT /FTId=VAR_049608.
FT VARIANT 173 173 R -> P (in dbSNP:rs41297708).
FT /FTId=VAR_049609.
FT VARIANT 178 178 P -> A (in dbSNP:rs41297710).
FT /FTId=VAR_049610.
FT VARIANT 194 194 E -> K (in dbSNP:rs41297714).
FT /FTId=VAR_049611.
FT VARIANT 198 198 L -> F (in dbSNP:rs1079109).
FT /FTId=VAR_024182.
FT VARIANT 260 260 R -> H (in dbSNP:rs41299256).
FT /FTId=VAR_049612.
FT VARIANT 297 297 T -> K.
FT /FTId=VAR_060721.
FT VARIANT 336 336 V -> F (in dbSNP:rs417707).
FT /FTId=VAR_059360.
FT VARIANT 464 464 S -> I (in dbSNP:rs388218).
FT /FTId=VAR_049613.
FT VARIANT 471 471 R -> H (in dbSNP:rs41299256).
FT /FTId=VAR_049614.
FT VARIANT 528 528 K -> E (in dbSNP:rs570189).
FT /FTId=VAR_049615.
FT VARIANT 528 528 K -> R (in dbSNP:rs570167).
FT /FTId=VAR_059361.
FT VARIANT 562 562 D -> E (in dbSNP:rs753856).
FT /FTId=VAR_024183.
FT VARIANT 572 572 M -> V (in dbSNP:rs452004).
FT /FTId=VAR_049616.
FT VARIANT 577 577 R -> Q (in dbSNP:rs368844).
FT /FTId=VAR_049617.
FT VARIANT 626 626 T -> A (in dbSNP:rs41299260).
FT /FTId=VAR_049618.
FT MUTAGEN 563 563 K->R: Complete loss of in vitro
FT methylation by METTL21A.
FT CONFLICT 106 108 RVC -> PVS (in Ref. 1; CAA36061).
FT CONFLICT 263 263 R -> G (in Ref. 1; CAA36061).
FT STRAND 9 12
FT STRAND 15 24
FT STRAND 27 30
FT STRAND 38 41
FT STRAND 44 46
FT STRAND 51 53
FT HELIX 55 59
FT TURN 60 63
FT HELIX 65 67
FT HELIX 72 74
FT TURN 75 77
FT HELIX 83 90
FT STRAND 93 99
FT STRAND 102 109
FT STRAND 112 116
FT HELIX 118 137
FT STRAND 143 148
FT HELIX 154 166
FT STRAND 170 176
FT HELIX 177 184
FT TURN 185 188
FT STRAND 195 202
FT STRAND 207 215
FT STRAND 218 227
FT HELIX 232 251
FT HELIX 259 275
FT TURN 276 278
FT STRAND 280 290
FT STRAND 293 300
FT HELIX 301 314
FT HELIX 316 326
FT HELIX 330 332
FT STRAND 334 340
FT HELIX 341 344
FT HELIX 346 355
FT TURN 356 358
FT TURN 367 369
FT HELIX 370 383
SQ SEQUENCE 643 AA; 71028 MW; BCE348F0226DB70B CRC64;
MQAPRELAVG IDLGTTYSCV GVFQQGRVEI LANDQGNRTT PSYVAFTDTE RLVGDAAKSQ
AALNPHNTVF DAKRLIGRKF ADTTVQSDMK HWPFRVVSEG GKPKVRVCYR GEDKTFYPEE
ISSMVLSKMK ETAEAYLGQP VKHAVITVPA YFNDSQRQAT KDAGAIAGLN VLRIINEPTA
AAIAYGLDRR GAGERNVLIF DLGGGTFDVS VLSIDAGVFE VKATAGDTHL GGEDFDNRLV
NHFMEEFRRK HGKDLSGNKR ALRRLRTACE RAKRTLSSST QATLEIDSLF EGVDFYTSIT
RARFEELCSD LFRSTLEPVE KALRDAKLDK AQIHDVVLVG GSTRIPKVQK LLQDFFNGKE
LNKSINPDEA VAYGAAVQAA VLMGDKCEKV QDLLLLDVAP LSLGLETAGG VMTTLIQRNA
TIPTKQTQTF TTYSDNQPGV FIQVYEGERA MTKDNNLLGR FELSGIPPAP RGVPQIEVTF
DIDANGILSV TATDRSTGKA NKITITNDKG RLSKEEVERM VHEAEQYKAE DEAQRDRVAA
KNSLEAHVFH VKGSLQEESL RDKIPEEDRR KMQDKCREVL AWLEHNQLAE KEEYEHQKRE
LEQICRPIFS RLYGGPGVPG GSSCGTQARQ GDPSTGPIIE EVD
//
MIM
140555
*RECORD*
*FIELD* NO
140555
*FIELD* TI
*140555 HEAT-SHOCK 70-KD PROTEIN 6; HSPA6
;;HSP70B-PRIME
*FIELD* TX
CLONING
HSPA6 (HPS70B-prime) is a stress-induced heat-shock gene encoding a
read morebasic 70-kD protein. It is a close homolog of HSPA7 (140556), formerly
designated HSP70B (Leung et al., 1990).
Leung et al. (1992) stated that both HSPA6 and HSPA7 represent
functional genes, as determined by analyses of mRNA from heat-shocked
human cells using sequence-specific oligonucleotides. After heat shock
at 45 degrees C, HSPA6 mRNA was detected in fibroblast, HeLa, and Daudi
cells, whereas HSPA7 mRNA was detected only in fibroblasts.
Parsian et al. (2000) found that HSPA6 and HSPA7 share 98% nucleotide
identity through their putative coding regions. However, HSPA7 was
predicted to lack protein-coding potential. Orthologs of HSPA6 and HSPA7
were not detected in mouse by Southern blot analysis.
GENE FUNCTION
Using RT-PCR, Parsian et al. (2000) detected the expression of HSPA6 and
HSPA7 only after heat shock in human W138 and HeLa cells. HSPA6 was more
strongly expressed following heat shock.
MAPPING
By hybridization analyses of a somatic cell hybrid DNA panel, Leung et
al. (1992) found that HSPA6 and HSPA7 localize to 1q. A BamHI
polymorphism in the HSPA7 gene was present in a predominantly Asian
population.
Grosz et al. (1992) concluded that bovine HSP70-4 is homologous to HSPA6
or HSPA7 because it is syntenic with amylase-1 (104700) and PGM1
(171900), both of which are on human chromosome 1.
Using FISH, Parsian et al. (2000) mapped the HSPA6 and HSPA7 genes to
within 5 to 10 Mb of each other on chromosome 1q23.1.
Brzustowicz et al. (2002) stated that the HSPA6 and HSPA7 genes are
located on chromosome 1q22, according to sequence data provided by the
Human Genome Project, and are in close proximity to a susceptibility
locus for schizophrenia (604906).
*FIELD* RF
1. Brzustowicz, L. M.; Hayter, J. E.; Hodgkinson, K. A.; Chow, E.
W. C.; Bassett, A. S.: Fine mapping of the schizophrenia susceptibility
locus on chromosome 1q22. Hum. Hered. 54: 199-209, 2002.
2. Grosz, M. D.; Womack, J. E.; Skow, L. C.: Syntenic conservation
of HSP70 genes in cattle and humans. Genomics 14: 863-868, 1992.
3. Leung, T. K. C.; Hall, C.; Rajendran, M.; Spurr, N. K.; Lim, L.
: The human heat-shock genes HSPA6 and HSPA7 are both expressed and
localize to chromosome 1. Genomics 12: 74-79, 1992.
4. Leung, T. K. C.; Rajendran, M. Y.; Monfries, C.; Hall, C.; Lim,
L.: The human heat-shock protein family: expression of a novel heat-inducible
HSP70 (HSP70B-prime) and isolation of its cDNA and genomic DNA. Biochem.
J. 267: 125-132, 1990.
5. Parsian, A. J.; Sheren, J. E.; Tao, T. Y.; Goswami, P. C.; Malyapa,
R.; Van Rheeden, R.; Watson, M. S.; Hunt, C. R.: The human Hsp70B
gene at the HSPA7 locus of chromosome 1 is transcribed but non-functional. Biochim.
Biophys. Acta 1494: 201-205, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 11/12/2010
Victor A. McKusick - updated: 9/15/2003
*FIELD* CD
Victor A. McKusick: 11/6/1991
*FIELD* ED
carol: 11/12/2010
tkritzer: 9/17/2003
tkritzer: 9/15/2003
terry: 7/24/1998
carol: 1/14/1993
carol: 11/30/1992
supermim: 3/16/1992
carol: 1/6/1992
carol: 11/13/1991
carol: 11/6/1991
*RECORD*
*FIELD* NO
140555
*FIELD* TI
*140555 HEAT-SHOCK 70-KD PROTEIN 6; HSPA6
;;HSP70B-PRIME
*FIELD* TX
CLONING
HSPA6 (HPS70B-prime) is a stress-induced heat-shock gene encoding a
read morebasic 70-kD protein. It is a close homolog of HSPA7 (140556), formerly
designated HSP70B (Leung et al., 1990).
Leung et al. (1992) stated that both HSPA6 and HSPA7 represent
functional genes, as determined by analyses of mRNA from heat-shocked
human cells using sequence-specific oligonucleotides. After heat shock
at 45 degrees C, HSPA6 mRNA was detected in fibroblast, HeLa, and Daudi
cells, whereas HSPA7 mRNA was detected only in fibroblasts.
Parsian et al. (2000) found that HSPA6 and HSPA7 share 98% nucleotide
identity through their putative coding regions. However, HSPA7 was
predicted to lack protein-coding potential. Orthologs of HSPA6 and HSPA7
were not detected in mouse by Southern blot analysis.
GENE FUNCTION
Using RT-PCR, Parsian et al. (2000) detected the expression of HSPA6 and
HSPA7 only after heat shock in human W138 and HeLa cells. HSPA6 was more
strongly expressed following heat shock.
MAPPING
By hybridization analyses of a somatic cell hybrid DNA panel, Leung et
al. (1992) found that HSPA6 and HSPA7 localize to 1q. A BamHI
polymorphism in the HSPA7 gene was present in a predominantly Asian
population.
Grosz et al. (1992) concluded that bovine HSP70-4 is homologous to HSPA6
or HSPA7 because it is syntenic with amylase-1 (104700) and PGM1
(171900), both of which are on human chromosome 1.
Using FISH, Parsian et al. (2000) mapped the HSPA6 and HSPA7 genes to
within 5 to 10 Mb of each other on chromosome 1q23.1.
Brzustowicz et al. (2002) stated that the HSPA6 and HSPA7 genes are
located on chromosome 1q22, according to sequence data provided by the
Human Genome Project, and are in close proximity to a susceptibility
locus for schizophrenia (604906).
*FIELD* RF
1. Brzustowicz, L. M.; Hayter, J. E.; Hodgkinson, K. A.; Chow, E.
W. C.; Bassett, A. S.: Fine mapping of the schizophrenia susceptibility
locus on chromosome 1q22. Hum. Hered. 54: 199-209, 2002.
2. Grosz, M. D.; Womack, J. E.; Skow, L. C.: Syntenic conservation
of HSP70 genes in cattle and humans. Genomics 14: 863-868, 1992.
3. Leung, T. K. C.; Hall, C.; Rajendran, M.; Spurr, N. K.; Lim, L.
: The human heat-shock genes HSPA6 and HSPA7 are both expressed and
localize to chromosome 1. Genomics 12: 74-79, 1992.
4. Leung, T. K. C.; Rajendran, M. Y.; Monfries, C.; Hall, C.; Lim,
L.: The human heat-shock protein family: expression of a novel heat-inducible
HSP70 (HSP70B-prime) and isolation of its cDNA and genomic DNA. Biochem.
J. 267: 125-132, 1990.
5. Parsian, A. J.; Sheren, J. E.; Tao, T. Y.; Goswami, P. C.; Malyapa,
R.; Van Rheeden, R.; Watson, M. S.; Hunt, C. R.: The human Hsp70B
gene at the HSPA7 locus of chromosome 1 is transcribed but non-functional. Biochim.
Biophys. Acta 1494: 201-205, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 11/12/2010
Victor A. McKusick - updated: 9/15/2003
*FIELD* CD
Victor A. McKusick: 11/6/1991
*FIELD* ED
carol: 11/12/2010
tkritzer: 9/17/2003
tkritzer: 9/15/2003
terry: 7/24/1998
carol: 1/14/1993
carol: 11/30/1992
supermim: 3/16/1992
carol: 1/6/1992
carol: 11/13/1991
carol: 11/6/1991