Full text data of HSPA1L
HSPA1L
[Confidence: low (only semi-automatic identification from reviews)]
Heat shock 70 kDa protein 1-like; Heat shock 70 kDa protein 1L (Heat shock 70 kDa protein 1-Hom; HSP70-Hom)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Heat shock 70 kDa protein 1-like; Heat shock 70 kDa protein 1L (Heat shock 70 kDa protein 1-Hom; HSP70-Hom)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P34931
ID HS71L_HUMAN Reviewed; 641 AA.
AC P34931; A6NNB0; B0UXW8; O75634; Q2HXR3; Q8NE72; Q96QC9; Q9UQM1;
read moreDT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Heat shock 70 kDa protein 1-like;
DE Short=Heat shock 70 kDa protein 1L;
DE AltName: Full=Heat shock 70 kDa protein 1-Hom;
DE Short=HSP70-Hom;
GN Name=HSPA1L;
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], AND INDUCTION.
RX PubMed=1700760; DOI=10.1007/BF00187095;
RA Milner C.M., Campbell R.D.;
RT "Structure and expression of the three MHC-linked HSP70 genes.";
RL Immunogenetics 32:242-251(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=9685725;
RA Ito Y., Ando A., Ando H., Ando J., Saijoh Y., Inoko H., Fujimoto H.;
RT "Genomic structure of the spermatid-specific HSP70 homolog gene
RT located in the class III region of the major histocompatibility
RT complex of mouse and man.";
RL J. Biochem. 124:347-353(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA Campbell R.D., Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-8; THR-268;
RP GLY-294; MET-479; MET-493; ALA-558 AND LYS-602.
RG NIEHS SNPs program;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-493.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-493.
RC TISSUE=Testis;
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 [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).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-386 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).
RN [10]
RP VARIANT MET-493.
RX PubMed=1356099; DOI=10.1007/BF00218042;
RA Milner C.M., Campbell R.D.;
RT "Polymorphic analysis of the three MHC-linked HSP70 genes.";
RL Immunogenetics 36:357-362(1992).
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 -!- TISSUE SPECIFICITY: Expressed in spermatids.
CC -!- INDUCTION: Not induced by heat shock.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hspa1l/";
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DR EMBL; M59829; AAA63228.1; -; Genomic_DNA.
DR EMBL; D85730; BAA32521.1; -; mRNA.
DR EMBL; AF134726; AAD21817.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63301.1; -; Genomic_DNA.
DR EMBL; DQ383515; ABC88476.1; -; Genomic_DNA.
DR EMBL; AL662834; CAI17736.1; -; Genomic_DNA.
DR EMBL; AL671762; CAI18215.1; -; Genomic_DNA.
DR EMBL; AL929592; CAI18463.1; -; Genomic_DNA.
DR EMBL; CR388202; CAQ09503.1; -; Genomic_DNA.
DR EMBL; BC034483; AAH34483.1; -; mRNA.
DR PIR; B45871; B45871.
DR RefSeq; NP_005518.3; NM_005527.3.
DR RefSeq; XP_005249128.1; XM_005249071.1.
DR RefSeq; XP_005249129.1; XM_005249072.1.
DR RefSeq; XP_005249130.1; XM_005249073.1.
DR RefSeq; XP_005249131.1; XM_005249074.1.
DR RefSeq; XP_005272871.1; XM_005272814.1.
DR RefSeq; XP_005272872.1; XM_005272815.1.
DR RefSeq; XP_005272873.1; XM_005272816.1.
DR RefSeq; XP_005272874.1; XM_005272817.1.
DR RefSeq; XP_005275028.1; XM_005274971.1.
DR RefSeq; XP_005275029.1; XM_005274972.1.
DR RefSeq; XP_005275030.1; XM_005274973.1.
DR RefSeq; XP_005275031.1; XM_005274974.1.
DR RefSeq; XP_005275455.1; XM_005275398.1.
DR RefSeq; XP_005275457.1; XM_005275400.1.
DR RefSeq; XP_005275458.1; XM_005275401.1.
DR RefSeq; XP_005275459.1; XM_005275402.1.
DR UniGene; Hs.690634; -.
DR PDB; 3GDQ; X-ray; 1.80 A; A=1-386.
DR PDBsum; 3GDQ; -.
DR ProteinModelPortal; P34931; -.
DR SMR; P34931; 4-612.
DR IntAct; P34931; 32.
DR MINT; MINT-1136903; -.
DR STRING; 9606.ENSP00000396486; -.
DR PhosphoSite; P34931; -.
DR DMDM; 23831140; -.
DR UCD-2DPAGE; P34931; -.
DR PaxDb; P34931; -.
DR PRIDE; P34931; -.
DR DNASU; 3305; -.
DR Ensembl; ENST00000375654; ENSP00000364805; ENSG00000204390.
DR Ensembl; ENST00000383390; ENSP00000372881; ENSG00000206383.
DR Ensembl; ENST00000417199; ENSP00000387691; ENSG00000204390.
DR Ensembl; ENST00000417601; ENSP00000396486; ENSG00000234258.
DR Ensembl; ENST00000456772; ENSP00000408347; ENSG00000236251.
DR GeneID; 3305; -.
DR KEGG; hsa:3305; -.
DR UCSC; uc003nxh.3; human.
DR CTD; 3305; -.
DR GeneCards; GC06M031777; -.
DR GeneCards; GC06Mj31764; -.
DR GeneCards; GC06Mk31759; -.
DR GeneCards; GC06Mn31767; -.
DR H-InvDB; HIX0165969; -.
DR H-InvDB; HIX0166127; -.
DR H-InvDB; HIX0166446; -.
DR H-InvDB; HIX0167182; -.
DR H-InvDB; HIX0184230; -.
DR HGNC; HGNC:5234; HSPA1L.
DR HPA; HPA043285; -.
DR MIM; 140559; gene.
DR neXtProt; NX_P34931; -.
DR PharmGKB; PA29500; -.
DR eggNOG; COG0443; -.
DR HOVERGEN; HBG051845; -.
DR InParanoid; P34931; -.
DR KO; K03283; -.
DR OMA; IESAIQW; -.
DR OrthoDB; EOG7PCJGF; -.
DR EvolutionaryTrace; P34931; -.
DR GeneWiki; HSPA1L; -.
DR GenomeRNAi; 3305; -.
DR NextBio; 13111; -.
DR PRO; PR:P34931; -.
DR Bgee; P34931; -.
DR CleanEx; HS_HSPA1L; -.
DR Genevestigator; P34931; -.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
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; Nucleotide-binding;
KW Polymorphism; Reference proteome.
FT CHAIN 1 641 Heat shock 70 kDa protein 1-like.
FT /FTId=PRO_0000078255.
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 VARIANT 8 8 A -> P (in dbSNP:rs9469057).
FT /FTId=VAR_025841.
FT VARIANT 268 268 A -> T (in dbSNP:rs34620296).
FT /FTId=VAR_025842.
FT VARIANT 294 294 D -> G (in dbSNP:rs34360259).
FT /FTId=VAR_025843.
FT VARIANT 479 479 T -> M (in dbSNP:rs482145).
FT /FTId=VAR_025844.
FT VARIANT 493 493 T -> M (in dbSNP:rs2227956).
FT /FTId=VAR_003820.
FT VARIANT 558 558 E -> A (in dbSNP:rs2227955).
FT /FTId=VAR_025845.
FT VARIANT 602 602 E -> K (in dbSNP:rs2075800).
FT /FTId=VAR_025846.
FT CONFLICT 408 408 A -> V (in Ref. 1; AAA63228).
FT CONFLICT 416 416 I -> M (in Ref. 7; AAH34483).
FT CONFLICT 424 424 T -> P (in Ref. 1; AAA63228).
FT CONFLICT 506 506 T -> A (in Ref. 7; AAH34483).
FT CONFLICT 627 627 V -> M (in Ref. 2; BAA32521).
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 HELIX 60 63
FT HELIX 65 67
FT HELIX 72 75
FT HELIX 83 89
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 255 257
FT HELIX 259 275
FT TURN 276 278
FT STRAND 279 290
FT STRAND 293 300
FT HELIX 301 307
FT HELIX 309 314
FT HELIX 316 325
FT HELIX 330 332
FT STRAND 335 340
FT HELIX 341 344
FT HELIX 346 355
FT TURN 356 358
FT TURN 367 369
FT HELIX 370 383
SQ SEQUENCE 641 AA; 70375 MW; A9339D7657166FF7 CRC64;
MATAKGIAIG IDLGTTYSCV GVFQHGKVEI IANDQGNRTT PSYVAFTDTE RLIGDAAKNQ
VAMNPQNTVF DAKRLIGRKF NDPVVQADMK LWPFQVINEG GKPKVLVSYK GENKAFYPEE
ISSMVLTKLK ETAEAFLGHP VTNAVITVPA YFNDSQRQAT KDAGVIAGLN VLRIINEPTA
AAIAYGLDKG GQGERHVLIF DLGGGTFDVS ILTIDDGIFE VKATAGDTHL GGEDFDNRLV
SHFVEEFKRK HKKDISQNKR AVRRLRTACE RAKRTLSSST QANLEIDSLY EGIDFYTSIT
RARFEELCAD LFRGTLEPVE KALRDAKMDK AKIHDIVLVG GSTRIPKVQR LLQDYFNGRD
LNKSINPDEA VAYGAAVQAA ILMGDKSEKV QDLLLLDVAP LSLGLETAGG VMTALIKRNS
TIPTKQTQIF TTYSDNQPGV LIQVYEGERA MTKDNNLLGR FDLTGIPPAP RGVPQIEVTF
DIDANGILNV TATDKSTGKV NKITITNDKG RLSKEEIERM VLDAEKYKAE DEVQREKIAA
KNALESYAFN MKSVVSDEGL KGKISESDKN KILDKCNELL SWLEVNQLAE KDEFDHKRKE
LEQMCNPIIT KLYQGGCTGP ACGTGYVPGR PATGPTIEEV D
//
ID HS71L_HUMAN Reviewed; 641 AA.
AC P34931; A6NNB0; B0UXW8; O75634; Q2HXR3; Q8NE72; Q96QC9; Q9UQM1;
read moreDT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Heat shock 70 kDa protein 1-like;
DE Short=Heat shock 70 kDa protein 1L;
DE AltName: Full=Heat shock 70 kDa protein 1-Hom;
DE Short=HSP70-Hom;
GN Name=HSPA1L;
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], AND INDUCTION.
RX PubMed=1700760; DOI=10.1007/BF00187095;
RA Milner C.M., Campbell R.D.;
RT "Structure and expression of the three MHC-linked HSP70 genes.";
RL Immunogenetics 32:242-251(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=9685725;
RA Ito Y., Ando A., Ando H., Ando J., Saijoh Y., Inoko H., Fujimoto H.;
RT "Genomic structure of the spermatid-specific HSP70 homolog gene
RT located in the class III region of the major histocompatibility
RT complex of mouse and man.";
RL J. Biochem. 124:347-353(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA Campbell R.D., Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-8; THR-268;
RP GLY-294; MET-479; MET-493; ALA-558 AND LYS-602.
RG NIEHS SNPs program;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-493.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-493.
RC TISSUE=Testis;
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 [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).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-386 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).
RN [10]
RP VARIANT MET-493.
RX PubMed=1356099; DOI=10.1007/BF00218042;
RA Milner C.M., Campbell R.D.;
RT "Polymorphic analysis of the three MHC-linked HSP70 genes.";
RL Immunogenetics 36:357-362(1992).
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 -!- TISSUE SPECIFICITY: Expressed in spermatids.
CC -!- INDUCTION: Not induced by heat shock.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hspa1l/";
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DR EMBL; M59829; AAA63228.1; -; Genomic_DNA.
DR EMBL; D85730; BAA32521.1; -; mRNA.
DR EMBL; AF134726; AAD21817.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63301.1; -; Genomic_DNA.
DR EMBL; DQ383515; ABC88476.1; -; Genomic_DNA.
DR EMBL; AL662834; CAI17736.1; -; Genomic_DNA.
DR EMBL; AL671762; CAI18215.1; -; Genomic_DNA.
DR EMBL; AL929592; CAI18463.1; -; Genomic_DNA.
DR EMBL; CR388202; CAQ09503.1; -; Genomic_DNA.
DR EMBL; BC034483; AAH34483.1; -; mRNA.
DR PIR; B45871; B45871.
DR RefSeq; NP_005518.3; NM_005527.3.
DR RefSeq; XP_005249128.1; XM_005249071.1.
DR RefSeq; XP_005249129.1; XM_005249072.1.
DR RefSeq; XP_005249130.1; XM_005249073.1.
DR RefSeq; XP_005249131.1; XM_005249074.1.
DR RefSeq; XP_005272871.1; XM_005272814.1.
DR RefSeq; XP_005272872.1; XM_005272815.1.
DR RefSeq; XP_005272873.1; XM_005272816.1.
DR RefSeq; XP_005272874.1; XM_005272817.1.
DR RefSeq; XP_005275028.1; XM_005274971.1.
DR RefSeq; XP_005275029.1; XM_005274972.1.
DR RefSeq; XP_005275030.1; XM_005274973.1.
DR RefSeq; XP_005275031.1; XM_005274974.1.
DR RefSeq; XP_005275455.1; XM_005275398.1.
DR RefSeq; XP_005275457.1; XM_005275400.1.
DR RefSeq; XP_005275458.1; XM_005275401.1.
DR RefSeq; XP_005275459.1; XM_005275402.1.
DR UniGene; Hs.690634; -.
DR PDB; 3GDQ; X-ray; 1.80 A; A=1-386.
DR PDBsum; 3GDQ; -.
DR ProteinModelPortal; P34931; -.
DR SMR; P34931; 4-612.
DR IntAct; P34931; 32.
DR MINT; MINT-1136903; -.
DR STRING; 9606.ENSP00000396486; -.
DR PhosphoSite; P34931; -.
DR DMDM; 23831140; -.
DR UCD-2DPAGE; P34931; -.
DR PaxDb; P34931; -.
DR PRIDE; P34931; -.
DR DNASU; 3305; -.
DR Ensembl; ENST00000375654; ENSP00000364805; ENSG00000204390.
DR Ensembl; ENST00000383390; ENSP00000372881; ENSG00000206383.
DR Ensembl; ENST00000417199; ENSP00000387691; ENSG00000204390.
DR Ensembl; ENST00000417601; ENSP00000396486; ENSG00000234258.
DR Ensembl; ENST00000456772; ENSP00000408347; ENSG00000236251.
DR GeneID; 3305; -.
DR KEGG; hsa:3305; -.
DR UCSC; uc003nxh.3; human.
DR CTD; 3305; -.
DR GeneCards; GC06M031777; -.
DR GeneCards; GC06Mj31764; -.
DR GeneCards; GC06Mk31759; -.
DR GeneCards; GC06Mn31767; -.
DR H-InvDB; HIX0165969; -.
DR H-InvDB; HIX0166127; -.
DR H-InvDB; HIX0166446; -.
DR H-InvDB; HIX0167182; -.
DR H-InvDB; HIX0184230; -.
DR HGNC; HGNC:5234; HSPA1L.
DR HPA; HPA043285; -.
DR MIM; 140559; gene.
DR neXtProt; NX_P34931; -.
DR PharmGKB; PA29500; -.
DR eggNOG; COG0443; -.
DR HOVERGEN; HBG051845; -.
DR InParanoid; P34931; -.
DR KO; K03283; -.
DR OMA; IESAIQW; -.
DR OrthoDB; EOG7PCJGF; -.
DR EvolutionaryTrace; P34931; -.
DR GeneWiki; HSPA1L; -.
DR GenomeRNAi; 3305; -.
DR NextBio; 13111; -.
DR PRO; PR:P34931; -.
DR Bgee; P34931; -.
DR CleanEx; HS_HSPA1L; -.
DR Genevestigator; P34931; -.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
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; Nucleotide-binding;
KW Polymorphism; Reference proteome.
FT CHAIN 1 641 Heat shock 70 kDa protein 1-like.
FT /FTId=PRO_0000078255.
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 VARIANT 8 8 A -> P (in dbSNP:rs9469057).
FT /FTId=VAR_025841.
FT VARIANT 268 268 A -> T (in dbSNP:rs34620296).
FT /FTId=VAR_025842.
FT VARIANT 294 294 D -> G (in dbSNP:rs34360259).
FT /FTId=VAR_025843.
FT VARIANT 479 479 T -> M (in dbSNP:rs482145).
FT /FTId=VAR_025844.
FT VARIANT 493 493 T -> M (in dbSNP:rs2227956).
FT /FTId=VAR_003820.
FT VARIANT 558 558 E -> A (in dbSNP:rs2227955).
FT /FTId=VAR_025845.
FT VARIANT 602 602 E -> K (in dbSNP:rs2075800).
FT /FTId=VAR_025846.
FT CONFLICT 408 408 A -> V (in Ref. 1; AAA63228).
FT CONFLICT 416 416 I -> M (in Ref. 7; AAH34483).
FT CONFLICT 424 424 T -> P (in Ref. 1; AAA63228).
FT CONFLICT 506 506 T -> A (in Ref. 7; AAH34483).
FT CONFLICT 627 627 V -> M (in Ref. 2; BAA32521).
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 HELIX 60 63
FT HELIX 65 67
FT HELIX 72 75
FT HELIX 83 89
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 255 257
FT HELIX 259 275
FT TURN 276 278
FT STRAND 279 290
FT STRAND 293 300
FT HELIX 301 307
FT HELIX 309 314
FT HELIX 316 325
FT HELIX 330 332
FT STRAND 335 340
FT HELIX 341 344
FT HELIX 346 355
FT TURN 356 358
FT TURN 367 369
FT HELIX 370 383
SQ SEQUENCE 641 AA; 70375 MW; A9339D7657166FF7 CRC64;
MATAKGIAIG IDLGTTYSCV GVFQHGKVEI IANDQGNRTT PSYVAFTDTE RLIGDAAKNQ
VAMNPQNTVF DAKRLIGRKF NDPVVQADMK LWPFQVINEG GKPKVLVSYK GENKAFYPEE
ISSMVLTKLK ETAEAFLGHP VTNAVITVPA YFNDSQRQAT KDAGVIAGLN VLRIINEPTA
AAIAYGLDKG GQGERHVLIF DLGGGTFDVS ILTIDDGIFE VKATAGDTHL GGEDFDNRLV
SHFVEEFKRK HKKDISQNKR AVRRLRTACE RAKRTLSSST QANLEIDSLY EGIDFYTSIT
RARFEELCAD LFRGTLEPVE KALRDAKMDK AKIHDIVLVG GSTRIPKVQR LLQDYFNGRD
LNKSINPDEA VAYGAAVQAA ILMGDKSEKV QDLLLLDVAP LSLGLETAGG VMTALIKRNS
TIPTKQTQIF TTYSDNQPGV LIQVYEGERA MTKDNNLLGR FDLTGIPPAP RGVPQIEVTF
DIDANGILNV TATDKSTGKV NKITITNDKG RLSKEEIERM VLDAEKYKAE DEVQREKIAA
KNALESYAFN MKSVVSDEGL KGKISESDKN KILDKCNELL SWLEVNQLAE KDEFDHKRKE
LEQMCNPIIT KLYQGGCTGP ACGTGYVPGR PATGPTIEEV D
//
MIM
140559
*RECORD*
*FIELD* NO
140559
*FIELD* TI
*140559 HEAT-SHOCK 70-KD PROTEIN-LIKE 1; HSPA1L
;;HEAT-SHOCK PROTEIN, 70-KD, HOMOLOGOUS;;
read moreHSP70-HOM;;
HSP70-1L;;
HSP70T
*FIELD* TX
CLONING
The human HSP70, or HSPA, multigene family encodes several highly
conserved 70-kD heat-shock proteins that vary in their inducibility in
response to metabolic stress. Sargent et al. (1989) identified the
HSP70-HOM gene as a region with similarity to HSP70-1 (HSPA1A; 140550)
that was located approximately 4 kb telomeric to HSP70-1 in the class
III region of the major histocompatibility complex on 6p21.3. Milner and
Campbell (1990) defined this homologous region as a gene of the HSP70
family. They found that the HSP70-HOM gene lacks introns. The predicted
641-amino acid HSP70-HOM protein is 90%, 84%, and 79% identical to the
HSP70-1, HSC70 (HSPA8; 600816), and HSP70B-prime (HSPA6; 140555)
proteins, respectively; the sequences differ most in the C-terminal 100
amino acids. Northern blot analysis of HeLa cell RNA detected an
approximately 3-kb HSP70-HOM transcript that was expressed
constitutively at a low level but was not induced by heat shock.
GENE FUNCTION
Hasson et al. (2013) elucidated regulators that have an impact on parkin
(PARK2; 602544) translocation to damaged mitochondria with genomewide
small interfering RNA (siRNA) screens coupled to high-content
microscopy. Screening yielded gene candidates involved in diverse
cellular processes that were subsequently validated in low-throughput
assays. This led to characterization of TOMM7 (607980) as essential for
stabilizing PINK1 (608309) on the outer mitochondrial membrane following
mitochondrial damage. Hasson et al. (2013) also discovered that HSPA1L
and BAG4 (603884) have mutually opposing roles in the regulation of
parkin translocation. The screens revealed that SIAH3 (615609), found to
localize to mitochondria, inhibits PINK1 accumulation after
mitochondrial insult, reducing parkin translocation.
MOLECULAR GENETICS
Milner and Campbell (1992) investigated the presence of sequence
variation in the HSP70-HOM gene among different HLA haplotypes. They
identified a T-to-C transition in a number of haplotypes that results in
a met-to-thr substitution at position 493 (M493T), which is located
within the proposed peptide-binding site of HSP70 proteins.
Abacavir is a commonly used nucleoside analog with potent antiviral
activity against HIV-1. Approximately 5 to 9% of patients treated with
abacavir develop a hypersensitivity reaction characterized by
multisystem involvement that can be fatal in rare cases (Mallal et al.,
2002; Hetherington et al., 2002). Martin et al. (2004) reported that the
combination of HLA-B*5701 (see 142830) and a haplotypic M493T
polymorphism of HSP70-HOM is highly predictive of abacavir
hypersensitivity.
Spagnolo et al. (2007) found a strong association between the HSP70-HOM
dbSNP rs2075800 G allele and uveitis in patients with sarcoidosis
(181000). Their study included 270 white patients with sarcoidosis,
including 88 with sarcoid-related uveitis; 347 matched control subjects;
and 181 patients with idiopathic interior or intermediate uveitis. The
HSPA1L dbSNP rs2075800 G allele frequency was higher in the
sarcoid-uveitis group than in both the sarcoid-nonuveitis and control
groups (83% vs 71%, OR, 2.00, P(c) = 0.01; and 83% vs 66%, OR, 2.45,
P(c) = 0.00005, respectively). Similar results were observed when
considering the carriage frequency of the associated haplotype (HSP70
haplotype 2) across the 3 study groups. In addition, the association was
specific sarcoidosis, as the carriage of the G allele discriminated
between sarcoid-related and idiopathic forms of uveitis.
For a discussion of a possible association between variation in the
HSPA2 gene and noise-induced hearing loss, see 613035.
*FIELD* RF
1. Hasson, S. A.; Kane, L. A.; Yamano, K.; Huang, C.-H.; Sliter, D.
A.; Buehler, E.; Wang, C.; Heman-Ackah, S. M.; Hessa, T.; Guha, R.;
Martin, S. E.; Youle, R. J.: High-content genome-wide RNAi screens
identify regulators of parkin upstream of mitophagy. Nature 504:
291-295, 2013.
2. Hetherington, S.; Hughes, A. R.; Mosteller, M.; Shortino, D.; Baker,
K. L.; Spreen, W.; Lai, E.; Davies, K.; Handley, A.; Dow, D. J.; Fling,
M. E.; Stocum, M.; Bowman, C.; Thurmond, L. M.; Roses, A. D.: Genetic
variations in HLA-B region and hypersensitivity reactions to abacavir. Lancet 359:
1121-1122, 2002.
3. Mallal, S.; Nolan, D.; Witt, C.; Masel, G.; Martin, A. M.; Moore,
C.; Sayer, D.; Castley, A.; Mamotte, C.; Maxwell, D.; James, I.; Christiansen,
F. T.: Association between presence of HLA-B*5701, HLA-DR7, and HLA-DQ3
and hypersensitivity to HIV-1 reverse-transcriptase inhibitor abacavir. Lancet 359:
727-732, 2002.
4. Martin, A. M.; Nolan, D.; Gaudieri, S.; Almeida, C. A.; Nolan,
R.; James, I.; Carvalho, F.; Phillips, E.; Christiansen, F. T.; Purcell,
A. W.; McCluskey, J.; Mallal, S.: Predisposition to abacavir hypersensitivity
conferred by HLA-B*5701 and a haplotypic Hsp70-Hom variant. Proc.
Nat. Acad. Sci. 101: 4180-4185, 2004.
5. Milner, C. M.; Campbell, R. D.: Structure and expression of the
three MHC-linked HSP70 genes. Immunogenetics 32: 242-251, 1990.
6. Milner, C. M.; Campbell, R. D.: Polymorphic analysis of the three
MHC-linked HSP70 genes. Immunogenetics 36: 357-362, 1992.
7. Sargent, C. A.; Dunham, I.; Trowsdale, J.; Campbell, R. D.: Human
major histocompatibility complex contains genes for the major heat
shock protein HSP70. Proc. Nat. Acad. Sci. 86: 1968-1972, 1989.
8. Spagnolo, P.; Sato, H.; Marshall, S. E.; Antoniou, K. M.; Ahmad,
T.; Wells, A. U.; Ahad, M. A.; Lightman, S.; du Bois, R. M.; Welsh,
K. I.: Association between heat shock protein 70/Hom genetic polymorphisms
and uveitis in patients with sarcoidosis. Invest. Ophthal. Vis. Sci. 48:
3019-3025, 2007.
*FIELD* CN
Ada Hamosh - updated: 1/13/2014
Jane Kelly - updated: 4/21/2008
Patti M. Sherman: 9/1/1998
*FIELD* CD
Victor A. McKusick: 11/13/1991
*FIELD* ED
mgross: 01/22/2014
alopez: 1/13/2014
wwang: 10/14/2009
ckniffin: 9/25/2009
carol: 4/21/2008
mgross: 10/6/2005
carol: 1/14/2005
tkritzer: 5/5/2004
cwells: 2/5/2001
cwells: 1/31/2001
carol: 10/26/1999
psherman: 9/8/1999
alopez: 9/21/1998
terry: 7/24/1998
supermim: 3/16/1992
carol: 2/19/1992
carol: 11/13/1991
*RECORD*
*FIELD* NO
140559
*FIELD* TI
*140559 HEAT-SHOCK 70-KD PROTEIN-LIKE 1; HSPA1L
;;HEAT-SHOCK PROTEIN, 70-KD, HOMOLOGOUS;;
read moreHSP70-HOM;;
HSP70-1L;;
HSP70T
*FIELD* TX
CLONING
The human HSP70, or HSPA, multigene family encodes several highly
conserved 70-kD heat-shock proteins that vary in their inducibility in
response to metabolic stress. Sargent et al. (1989) identified the
HSP70-HOM gene as a region with similarity to HSP70-1 (HSPA1A; 140550)
that was located approximately 4 kb telomeric to HSP70-1 in the class
III region of the major histocompatibility complex on 6p21.3. Milner and
Campbell (1990) defined this homologous region as a gene of the HSP70
family. They found that the HSP70-HOM gene lacks introns. The predicted
641-amino acid HSP70-HOM protein is 90%, 84%, and 79% identical to the
HSP70-1, HSC70 (HSPA8; 600816), and HSP70B-prime (HSPA6; 140555)
proteins, respectively; the sequences differ most in the C-terminal 100
amino acids. Northern blot analysis of HeLa cell RNA detected an
approximately 3-kb HSP70-HOM transcript that was expressed
constitutively at a low level but was not induced by heat shock.
GENE FUNCTION
Hasson et al. (2013) elucidated regulators that have an impact on parkin
(PARK2; 602544) translocation to damaged mitochondria with genomewide
small interfering RNA (siRNA) screens coupled to high-content
microscopy. Screening yielded gene candidates involved in diverse
cellular processes that were subsequently validated in low-throughput
assays. This led to characterization of TOMM7 (607980) as essential for
stabilizing PINK1 (608309) on the outer mitochondrial membrane following
mitochondrial damage. Hasson et al. (2013) also discovered that HSPA1L
and BAG4 (603884) have mutually opposing roles in the regulation of
parkin translocation. The screens revealed that SIAH3 (615609), found to
localize to mitochondria, inhibits PINK1 accumulation after
mitochondrial insult, reducing parkin translocation.
MOLECULAR GENETICS
Milner and Campbell (1992) investigated the presence of sequence
variation in the HSP70-HOM gene among different HLA haplotypes. They
identified a T-to-C transition in a number of haplotypes that results in
a met-to-thr substitution at position 493 (M493T), which is located
within the proposed peptide-binding site of HSP70 proteins.
Abacavir is a commonly used nucleoside analog with potent antiviral
activity against HIV-1. Approximately 5 to 9% of patients treated with
abacavir develop a hypersensitivity reaction characterized by
multisystem involvement that can be fatal in rare cases (Mallal et al.,
2002; Hetherington et al., 2002). Martin et al. (2004) reported that the
combination of HLA-B*5701 (see 142830) and a haplotypic M493T
polymorphism of HSP70-HOM is highly predictive of abacavir
hypersensitivity.
Spagnolo et al. (2007) found a strong association between the HSP70-HOM
dbSNP rs2075800 G allele and uveitis in patients with sarcoidosis
(181000). Their study included 270 white patients with sarcoidosis,
including 88 with sarcoid-related uveitis; 347 matched control subjects;
and 181 patients with idiopathic interior or intermediate uveitis. The
HSPA1L dbSNP rs2075800 G allele frequency was higher in the
sarcoid-uveitis group than in both the sarcoid-nonuveitis and control
groups (83% vs 71%, OR, 2.00, P(c) = 0.01; and 83% vs 66%, OR, 2.45,
P(c) = 0.00005, respectively). Similar results were observed when
considering the carriage frequency of the associated haplotype (HSP70
haplotype 2) across the 3 study groups. In addition, the association was
specific sarcoidosis, as the carriage of the G allele discriminated
between sarcoid-related and idiopathic forms of uveitis.
For a discussion of a possible association between variation in the
HSPA2 gene and noise-induced hearing loss, see 613035.
*FIELD* RF
1. Hasson, S. A.; Kane, L. A.; Yamano, K.; Huang, C.-H.; Sliter, D.
A.; Buehler, E.; Wang, C.; Heman-Ackah, S. M.; Hessa, T.; Guha, R.;
Martin, S. E.; Youle, R. J.: High-content genome-wide RNAi screens
identify regulators of parkin upstream of mitophagy. Nature 504:
291-295, 2013.
2. Hetherington, S.; Hughes, A. R.; Mosteller, M.; Shortino, D.; Baker,
K. L.; Spreen, W.; Lai, E.; Davies, K.; Handley, A.; Dow, D. J.; Fling,
M. E.; Stocum, M.; Bowman, C.; Thurmond, L. M.; Roses, A. D.: Genetic
variations in HLA-B region and hypersensitivity reactions to abacavir. Lancet 359:
1121-1122, 2002.
3. Mallal, S.; Nolan, D.; Witt, C.; Masel, G.; Martin, A. M.; Moore,
C.; Sayer, D.; Castley, A.; Mamotte, C.; Maxwell, D.; James, I.; Christiansen,
F. T.: Association between presence of HLA-B*5701, HLA-DR7, and HLA-DQ3
and hypersensitivity to HIV-1 reverse-transcriptase inhibitor abacavir. Lancet 359:
727-732, 2002.
4. Martin, A. M.; Nolan, D.; Gaudieri, S.; Almeida, C. A.; Nolan,
R.; James, I.; Carvalho, F.; Phillips, E.; Christiansen, F. T.; Purcell,
A. W.; McCluskey, J.; Mallal, S.: Predisposition to abacavir hypersensitivity
conferred by HLA-B*5701 and a haplotypic Hsp70-Hom variant. Proc.
Nat. Acad. Sci. 101: 4180-4185, 2004.
5. Milner, C. M.; Campbell, R. D.: Structure and expression of the
three MHC-linked HSP70 genes. Immunogenetics 32: 242-251, 1990.
6. Milner, C. M.; Campbell, R. D.: Polymorphic analysis of the three
MHC-linked HSP70 genes. Immunogenetics 36: 357-362, 1992.
7. Sargent, C. A.; Dunham, I.; Trowsdale, J.; Campbell, R. D.: Human
major histocompatibility complex contains genes for the major heat
shock protein HSP70. Proc. Nat. Acad. Sci. 86: 1968-1972, 1989.
8. Spagnolo, P.; Sato, H.; Marshall, S. E.; Antoniou, K. M.; Ahmad,
T.; Wells, A. U.; Ahad, M. A.; Lightman, S.; du Bois, R. M.; Welsh,
K. I.: Association between heat shock protein 70/Hom genetic polymorphisms
and uveitis in patients with sarcoidosis. Invest. Ophthal. Vis. Sci. 48:
3019-3025, 2007.
*FIELD* CN
Ada Hamosh - updated: 1/13/2014
Jane Kelly - updated: 4/21/2008
Patti M. Sherman: 9/1/1998
*FIELD* CD
Victor A. McKusick: 11/13/1991
*FIELD* ED
mgross: 01/22/2014
alopez: 1/13/2014
wwang: 10/14/2009
ckniffin: 9/25/2009
carol: 4/21/2008
mgross: 10/6/2005
carol: 1/14/2005
tkritzer: 5/5/2004
cwells: 2/5/2001
cwells: 1/31/2001
carol: 10/26/1999
psherman: 9/8/1999
alopez: 9/21/1998
terry: 7/24/1998
supermim: 3/16/1992
carol: 2/19/1992
carol: 11/13/1991