ID HSP76_HUMAN Reviewed; 643 AA. AC P17066; Q1HBA8; Q8IYK7; Q9BT95; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2003, sequence version 2. DT 25-JAN-2012, entry version 111. 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 MEDLINE=90226304; 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 MEDLINE=92128997; 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 MEDLINE=89037198; 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-321 AND LYS-502, AND MASS RP SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). 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 IPI; IPI00339269; -. 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; 15. DR MINT; MINT-1139180; -. DR STRING; P17066; -. DR PhosphoSite; P17066; -. DR DMDM; 34978357; -. DR UCD-2DPAGE; P17066; -. DR PRIDE; P17066; -. DR Ensembl; ENST00000309758; ENSP00000310219; ENSG00000173110. DR GeneID; 3310; -. DR KEGG; hsa:3310; -. DR UCSC; uc001gap.1; 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; maNOG16200; -. DR HOGENOM; HBG334976; -. DR HOVERGEN; HBG051845; -. DR InParanoid; P17066; -. DR OMA; IQRNATI; -. DR OrthoDB; EOG4Q58P1; -. DR PhylomeDB; P17066; -. DR NextBio; 13127; -. DR ArrayExpress; P17066; -. DR Bgee; P17066; -. DR CleanEx; HS_HSPA6; -. DR Genevestigator; P17066; -. DR GermOnline; ENSG00000173110; Homo sapiens. 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; IPR001023; Hsp70. DR InterPro; IPR013126; Hsp_70. DR KO; K03283; -. DR PANTHER; PTHR19375; Hsp70; 1. 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; Acetylation; ATP-binding; Complete proteome; KW Nucleotide-binding; Polymorphism; Reference proteome; Stress response. FT CHAIN 1 643 Heat shock 70 kDa protein 6. FT /FTId=PRO_0000078264. FT MOD_RES 321 321 N6-acetyllysine. FT MOD_RES 502 502 N6-acetyllysine. 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 CONFLICT 106 108 RVC -> PVS (in Ref. 1 and 3). FT CONFLICT 263 263 R -> G (in Ref. 1; CAA36061). FT STRAND 17 19 FT STRAND 39 41 FT STRAND 44 46 FT HELIX 56 59 FT TURN 60 63 FT HELIX 65 67 FT HELIX 72 74 FT HELIX 83 90 FT STRAND 93 98 FT STRAND 103 108 FT STRAND 113 116 FT HELIX 118 136 FT STRAND 143 148 FT HELIX 154 162 FT STRAND 170 176 FT HELIX 177 184 FT STRAND 195 202 FT STRAND 208 214 FT STRAND 219 225 FT HELIX 234 250 FT HELIX 259 275 FT TURN 276 278 FT STRAND 280 286 FT STRAND 295 300 FT HELIX 301 314 FT HELIX 316 326 FT HELIX 330 332 FT STRAND 334 339 FT HELIX 346 355 FT TURN 367 372 FT HELIX 376 382 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 //