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UniProtKB/Swiss-Prot entry P34931


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HS71L_HUMAN
Primary accession number P34931
Secondary accession numbers A6NNB0 B0UXW8 O75634 Q2HXR3 Q8NE72 Q96QC9 Q9UQM1
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on October 10, 2002 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 82)
Name and origin of the protein
Protein name Heat shock 70 kDa protein 1L
Synonyms Heat shock 70 kDa protein 1-like
Heat shock 70 kDa protein 1-Hom
HSP70-Hom
Gene name
Name: HSPA1L
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
DOI=10.1007/BF00187095; PubMed=1700760 [NCBI, ExPASy, EBI, Israel, Japan]
Milner C.M., Campbell R.D.;
"Structure and expression of the three MHC-linked HSP70 genes.";
Immunogenetics 32:242-251(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=9685725 [NCBI, ExPASy, EBI, Israel, Japan]
Ito Y., Ando A., Ando H., Ando J., Saijoh Y., Inoko H., Fujimoto H.;
"Genomic structure of the spermatid-specific HSP70 homolog gene located in the class III region of the major histocompatibility complex of mouse and man.";
J. Biochem. 124:347-353(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1101/gr.1736803; PubMed=14656967 [NCBI, ExPASy, EBI, Israel, Japan]
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Shiina S., Tamiya G., Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-8; THR-268; GLY-294; MET-479; MET-493; ALA-558 AND LYS-602.
NIEHS SNPs program;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-493.
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-493.
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[9]
VARIANT MET-493.
DOI=10.1007/BF00218042; PubMed=1356099 [NCBI, ExPASy, EBI, Israel, Japan]
Milner C.M., Campbell R.D.;
"Polymorphic analysis of the three MHC-linked HSP70 genes.";
Immunogenetics 36:357-362(1992).
Comments
  • FUNCTION: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity).
  • TISSUE SPECIFICITY: Expressed in spermatids.
  • INDUCTION: Not induced by heat shock.
  • SIMILARITY: Belongs to the heat shock protein 70 family.
  • WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/hspa1l/";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M59829; AAA63228.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D85730; BAA32521.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF134726; AAD21817.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000025; BAB63301.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ383515; ABC88476.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL662834; CAI17736.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL671762; CAI18215.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL929592; CAI18463.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR388202; CAQ09503.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC034483; AAH34483.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00301277; -.
PIR B45871; B45871.
RefSeq NP_005518.3; -.
UniGene Hs.690634
3D structure databases
PDB
3GDQ; X-ray; 1.80 A; A=1-386.[ExPASy / RCSB / EBI]
PDBsum 3GDQ; -.
SMR P34931; 4-555.
ModBase P34931.
Protein-protein interaction databases
IntAct P34931; 37.
PTM databases
PhosphoSite P34931; -.
Organism-specific databases
GeneCards GC06M031885; -.
HGNC HGNC:5234; HSPA1L.
GenAtlas HSPA1L.
MIM 140559; gene. [NCBI / EBI]
PharmGKB PA29500; -.
Gene expression databases
ArrayExpress P34931; -.
Bgee P34931; -.
CleanEx HS_HSPA1L; -.
GermOnline ENSG00000204390; Homo sapiens.
Ontologies
GO
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006986; Biological process: response to unfolded protein (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR018181; Heat_shock_70_CS.
IPR001023; Hsp70.
IPR013126; Hsp_70.
Graphical view of domain structure.
PANTHER PTHR19375; Hsp70; 1.
Pfam PF00012; HSP70; 1.
Pfam graphical view of domain structure.
PRINTS PR00301; HEATSHOCK70.
ProDom PD000089; Hsp70; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00297; HSP70_1; 1.
PS00329; HSP70_2; 1.
PS01036; HSP70_3; 1.
Proteomic databases
PRIDE P34931; -.
Genome annotation databases
Ensembl ENSG00000204390; Homo sapiens. [Contig view]
GeneID 3305; -.
KEGG hsa:3305; -.
Phylogenomic databases
HOGENOM P34931; -.
HOVERGEN P34931; -.
OMA P34931; AKIHDIV.
Other
NextBio 13111; -.
SOURCE HSPA1L; Homo sapiens.
ProtoNet P34931.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Methylation; Nucleotide-binding; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   641  641     Heat shock 70 kDa protein 1L. PRO_0000078255
MOD_RES   471   471        Omega-N-methylarginine (By similarity). 
VARIANT   8     8  1     A -> P (in dbSNP:rs9469057 [NCBI]). VAR_025841 [3D]
VARIANT   268   268  1     A -> T. VAR_025842 [3D]
VARIANT   294   294  1     D -> G. VAR_025843 [3D]
VARIANT   479   479  1     T -> M (in dbSNP:rs482145 [NCBI]). VAR_025844 
VARIANT   493   493  1     T -> M (in dbSNP:rs2227956 [NCBI]). VAR_003820 
VARIANT   558   558  1     E -> A (in dbSNP:rs2227955 [NCBI]). VAR_025845 
VARIANT   602   602  1     E -> K (in dbSNP:rs2075800 [NCBI]). VAR_025846 
CONFLICT   408   408        A -> V (in Ref. 1; AAA63228). 
CONFLICT   416   416        I -> M (in Ref. 7; AAH34483). 
CONFLICT   424   424        T -> P (in Ref. 1; AAA63228). 
CONFLICT   506   506        T -> A (in Ref. 7; AAH34483). 
CONFLICT   627   627        V -> M (in Ref. 2; BAA32521). 
Sequence information
Length: 641 AA [This is the length of the unprocessed precursor] Molecular weight: 70375 Da [This is the MW of the unprocessed precursor] CRC64: A9339D7657166FF7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATAKGIAIG IDLGTTYSCV GVFQHGKVEI IANDQGNRTT PSYVAFTDTE RLIGDAAKNQ 

        70         80         90        100        110        120 
VAMNPQNTVF DAKRLIGRKF NDPVVQADMK LWPFQVINEG GKPKVLVSYK GENKAFYPEE 

       130        140        150        160        170        180 
ISSMVLTKLK ETAEAFLGHP VTNAVITVPA YFNDSQRQAT KDAGVIAGLN VLRIINEPTA 

       190        200        210        220        230        240 
AAIAYGLDKG GQGERHVLIF DLGGGTFDVS ILTIDDGIFE VKATAGDTHL GGEDFDNRLV 

       250        260        270        280        290        300 
SHFVEEFKRK HKKDISQNKR AVRRLRTACE RAKRTLSSST QANLEIDSLY EGIDFYTSIT 

       310        320        330        340        350        360 
RARFEELCAD LFRGTLEPVE KALRDAKMDK AKIHDIVLVG GSTRIPKVQR LLQDYFNGRD 

       370        380        390        400        410        420 
LNKSINPDEA VAYGAAVQAA ILMGDKSEKV QDLLLLDVAP LSLGLETAGG VMTALIKRNS 

       430        440        450        460        470        480 
TIPTKQTQIF TTYSDNQPGV LIQVYEGERA MTKDNNLLGR FDLTGIPPAP RGVPQIEVTF 

       490        500        510        520        530        540 
DIDANGILNV TATDKSTGKV NKITITNDKG RLSKEEIERM VLDAEKYKAE DEVQREKIAA 

       550        560        570        580        590        600 
KNALESYAFN MKSVVSDEGL KGKISESDKN KILDKCNELL SWLEVNQLAE KDEFDHKRKE 

       610        620        630        640 
LEQMCNPIIT KLYQGGCTGP ACGTGYVPGR PATGPTIEEV D 

P34931 in FASTA format

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