ID HS71L_HUMAN Reviewed; 641 AA. AC P34931; A6NNB0; B0UXW8; O75634; Q2HXR3; Q8NE72; Q96QC9; Q9UQM1; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2002, sequence version 2. DT 09-FEB-2010, entry version 92. 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 MEDLINE=91055806; 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 MEDLINE=98351992; 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 MEDLINE=22935763; 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 [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [9] RP VARIANT MET-493. RX MEDLINE=92406261; 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/"; 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; 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 IPI; IPI00939442; -. DR PIR; B45871; B45871. DR RefSeq; NP_005518.3; -. DR UniGene; Hs.690634; -. DR PDB; 3GDQ; X-ray; 1.80 A; A=1-386. DR PDBsum; 3GDQ; -. DR SMR; P34931; 4-555, 544-619. DR IntAct; P34931; 39. DR STRING; P34931; -. DR PhosphoSite; P34931; -. DR PRIDE; P34931; -. DR Ensembl; ENST00000375654; ENSP00000364805; ENSG00000204390; Homo sapiens. DR Ensembl; ENST00000417601; ENSP00000396486; ENSG00000234258; Homo sapiens. DR GeneID; 3305; -. DR KEGG; hsa:3305; -. DR UCSC; uc003nxh.1; human. DR CTD; 3305; -. DR GeneCards; GC06M031885; -. DR HGNC; HGNC:5234; HSPA1L. DR MIM; 140559; gene. DR PharmGKB; PA29500; -. DR HOVERGEN; P34931; -. DR InParanoid; P34931; -. DR OMA; DKAKIHD; -. DR OrthoDB; EOG9TQPV5; -. DR PhylomeDB; P34931; -. DR NextBio; 13111; -. DR CleanEx; HS_HSPA1L; -. DR Genevestigator; P34931; -. DR GermOnline; ENSG00000204390; Homo sapiens. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IDA:MGI. 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 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; ATP-binding; Complete proteome; Nucleotide-binding; KW Polymorphism. FT CHAIN 1 641 Heat shock 70 kDa protein 1-like. FT /FTId=PRO_0000078255. FT VARIANT 8 8 A -> P (in dbSNP:rs9469057). FT /FTId=VAR_025841. FT VARIANT 268 268 A -> T. FT /FTId=VAR_025842. FT VARIANT 294 294 D -> G. 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 17 19 FT STRAND 39 41 FT STRAND 44 46 FT HELIX 56 59 FT HELIX 60 63 FT HELIX 65 67 FT HELIX 72 75 FT HELIX 83 89 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 234 251 FT HELIX 255 258 FT HELIX 259 275 FT TURN 276 278 FT STRAND 279 286 FT STRAND 295 300 FT HELIX 301 307 FT HELIX 309 312 FT HELIX 316 325 FT HELIX 330 332 FT STRAND 335 339 FT HELIX 346 355 FT TURN 367 372 FT HELIX 376 382 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 //