Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P34931 (HS71L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat shock 70 kDa protein 1-like

Short name=Heat shock 70 kDa protein 1L
Alternative name(s):
Heat shock 70 kDa protein 1-Hom
Short name=HSP70-Hom
Gene names
Name:HSPA1L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length641 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. Ref.2

Induction

Not induced by heat shock. Ref.1

Sequence similarities

Belongs to the heat shock protein 70 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 641641Heat shock 70 kDa protein 1-like
PRO_0000078255

Regions

Nucleotide binding14 – 174ATP
Nucleotide binding204 – 2063ATP
Nucleotide binding270 – 2778ATP
Nucleotide binding341 – 3444ATP

Sites

Binding site731ATP

Natural variations

Natural variant81A → P. Ref.5
Corresponds to variant rs9469057 [ dbSNP | Ensembl ].
VAR_025841
Natural variant2681A → T. Ref.5
Corresponds to variant rs34620296 [ dbSNP | Ensembl ].
VAR_025842
Natural variant2941D → G. Ref.5
Corresponds to variant rs34360259 [ dbSNP | Ensembl ].
VAR_025843
Natural variant4791T → M. Ref.5
Corresponds to variant rs482145 [ dbSNP | Ensembl ].
VAR_025844
Natural variant4931T → M. Ref.5 Ref.6 Ref.7 Ref.10
Corresponds to variant rs2227956 [ dbSNP | Ensembl ].
VAR_003820
Natural variant5581E → A. Ref.5
Corresponds to variant rs2227955 [ dbSNP | Ensembl ].
VAR_025845
Natural variant6021E → K. Ref.5
Corresponds to variant rs2075800 [ dbSNP | Ensembl ].
VAR_025846

Experimental info

Sequence conflict4081A → V in AAA63228. Ref.1
Sequence conflict4161I → M in AAH34483. Ref.7
Sequence conflict4241T → P in AAA63228. Ref.1
Sequence conflict5061T → A in AAH34483. Ref.7
Sequence conflict6271V → M in BAA32521. Ref.2

Secondary structure

...................................................................... 641
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P34931 [UniParc].

Last modified October 10, 2002. Version 2.
Checksum: A9339D7657166FF7

FASTA64170,375
        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 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression of the three MHC-linked HSP70 genes."
Milner C.M., Campbell R.D.
Immunogenetics 32:242-251(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
[2]"Genomic structure of the spermatid-specific HSP70 homolog gene located in the class III region of the major histocompatibility complex of mouse and man."
Ito Y., Ando A., Ando H., Ando J., Saijoh Y., Inoko H., Fujimoto H.
J. Biochem. 124:347-353(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
Tissue: Testis.
[3]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
Shiina S., Tamiya G., Oka A., Inoko H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]NIEHS SNPs program
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-8; THR-268; GLY-294; MET-479; MET-493; ALA-558 AND LYS-602.
[6]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT MET-493.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-493.
Tissue: Testis.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78."
Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T., Moche M., Schuler H.
PLoS ONE 5:E8625-E8625(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-386 IN COMPLEX WITH ADP AND PHOSPHATE.
[10]"Polymorphic analysis of the three MHC-linked HSP70 genes."
Milner C.M., Campbell R.D.
Immunogenetics 36:357-362(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MET-493.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59829 Genomic DNA. Translation: AAA63228.1.
D85730 mRNA. Translation: BAA32521.1.
AF134726 Genomic DNA. Translation: AAD21817.1.
BA000025 Genomic DNA. Translation: BAB63301.1.
DQ383515 Genomic DNA. Translation: ABC88476.1.
AL662834 Genomic DNA. Translation: CAI17736.1.
AL671762 Genomic DNA. Translation: CAI18215.1.
AL929592 Genomic DNA. Translation: CAI18463.1.
CR388202 Genomic DNA. Translation: CAQ09503.1.
BC034483 mRNA. Translation: AAH34483.1.
PIRB45871.
RefSeqNP_005518.3. NM_005527.3.
XP_005249128.1. XM_005249071.1.
XP_005249130.1. XM_005249073.1.
XP_005272873.1. XM_005272816.1.
XP_005272874.1. XM_005272817.1.
XP_005275030.1. XM_005274973.1.
XP_005275031.1. XM_005274974.1.
XP_005275458.1. XM_005275401.1.
XP_005275459.1. XM_005275402.1.
UniGeneHs.690634.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GDQX-ray1.80A1-386[»]
ProteinModelPortalP34931.
SMRP34931. Positions 4-612.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109537. 92 interactions.
IntActP34931. 32 interactions.
MINTMINT-1136903.
STRING9606.ENSP00000396486.

PTM databases

PhosphoSiteP34931.

Polymorphism databases

DMDM23831140.

2D gel databases

UCD-2DPAGEP34931.

Proteomic databases

PaxDbP34931.
PRIDEP34931.

Protocols and materials databases

DNASU3305.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375654; ENSP00000364805; ENSG00000204390.
ENST00000383390; ENSP00000372881; ENSG00000206383.
ENST00000417199; ENSP00000387691; ENSG00000204390.
ENST00000417601; ENSP00000396486; ENSG00000234258.
ENST00000456772; ENSP00000408347; ENSG00000236251.
GeneID3305.
KEGGhsa:3305.
UCSCuc003nxh.3. human.

Organism-specific databases

CTD3305.
GeneCardsGC06M031777.
GC06Mj31764.
GC06Mk31759.
GC06Mn31767.
H-InvDBHIX0165969.
HIX0166127.
HIX0166446.
HIX0167182.
HIX0184230.
HGNCHGNC:5234. HSPA1L.
HPAHPA043285.
MIM140559. gene.
neXtProtNX_P34931.
PharmGKBPA29500.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0443.
HOVERGENHBG051845.
InParanoidP34931.
KOK03283.
OMAIESAIQW.
OrthoDBEOG7PCJGF.
PhylomeDBP34931.
TreeFamTF105042.

Gene expression databases

BgeeP34931.
CleanExHS_HSPA1L.
GenevestigatorP34931.

Family and domain databases

InterProIPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
PROSITEPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP34931.
GeneWikiHSPA1L.
GenomeRNAi3305.
NextBio13111.
PROP34931.
SOURCESearch...

Entry information

Entry nameHS71L_HUMAN
AccessionPrimary (citable) accession number: P34931
Secondary accession number(s): A6NNB0 expand/collapse secondary AC list , B0UXW8, O75634, Q2HXR3, Q8NE72, Q96QC9, Q9UQM1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 10, 2002
Last modified: April 16, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM