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UniProtKB/Swiss-Prot entry P54652


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

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Entry information
Entry name HSP72_HUMAN
Primary accession number P54652
Secondary accession numbers Q15508 Q53XM3 Q9UE78
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 83)
Name and origin of the protein
Protein name Heat shock-related 70 kDa protein 2
Synonym Heat shock 70 kDa protein 2
Gene name
Name: HSPA2
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].
DOI=10.1006/geno.1994.1462; PubMed=7829106 [NCBI, ExPASy, EBI, Israel, Japan]
Bonnycastle L.L.C., Yu C.-E., Hunt C.R., Trask B.J., Clancy K.P., Weber J.L., Patterson D., Schellenberg G.D.;
"Cloning, sequencing, and mapping of the human chromosome 14 heat shock protein gene (HSPA2).";
Genomics 23:85-93(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Goralski T.J., Krensky A.M.;
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-191 AND GLU-496.
NIEHS SNPs program;
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Eye;
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-126.
DOI=10.1093/hmg/3.10.1819; PubMed=7849706 [NCBI, ExPASy, EBI, Israel, Japan]
Roux A.-F., Nguyen V.T.T., Squire J.A., Cox D.W.;
"A heat shock gene at 14q22: mapping and expression.";
Hum. Mol. Genet. 3:1819-1822(1994).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42 AND TYR-108, AND MASS SPECTROMETRY.
TISSUE=Lung;
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[8]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
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.
  • SUBUNIT: Interacts with ZNF541 (By similarity).
  • SIMILARITY: Belongs to the heat shock protein 70 family.
  • WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/hspa2/";.
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
L26336; AAA52698.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U56725; AAD11466.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT009815; AAP88817.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ489378; ABE96830.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001752; AAH01752.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC036107; AAH36107.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U10149; AAC50076.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00007702; -.
PIR A55719; A55719.
I37564; I37564.
RefSeq NP_068814.2; -.
UniGene Hs.432648
3D structure databases
HSSP P19120; 3HSC. [HSSP ENTRY / PDB]
SMR P54652; 3-557, 545-620.
ModBase P54652.
Protein-protein interaction databases
IntAct P54652; 8.
PTM databases
PhosphoSite P54652; -.
2D gel databases
REPRODUCTION-2DPAGE IPI00007702; -.
Organism-specific databases
GeneCards GC14P064072; -.
H-InvDB HIX0011736; -.
HGNC HGNC:5235; HSPA2.
GenAtlas HSPA2.
HPA HPA000798; -.
MIM 140560; gene. [NCBI / EBI]
PharmGKB PA29501; -.
Gene expression databases
ArrayExpress P54652; -.
Bgee P54652; -.
CleanEx HS_HSPA2; -.
GermOnline ENSG00000126803; Homo sapiens.
Ontologies
GO
GO:0009986; Cellular component: cell surface (inferred from direct assay from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051082; Molecular function: unfolded protein binding (traceable author statement from ProtInc).
GO:0007140; Biological process: male meiosis (traceable author statement from ProtInc).
GO:0006986; Biological process: response to unfolded protein (traceable author statement from ProtInc).
GO:0007286; Biological process: spermatid development (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
PeptideAtlas P54652; -.
PRIDE P54652; -.
Genome annotation databases
Ensembl ENSG00000126803; Homo sapiens. [Contig view]
GeneID 3306; -.
KEGG hsa:3306; -.
Phylogenomic databases
HOGENOM P54652; -.
HOVERGEN P54652; -.
OMA P54652; LESYTYN.
Other
NextBio 13115; -.
SOURCE HSPA2; Homo sapiens.
ProtoNet P54652.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein; Polymorphism; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   639  639     Heat shock-related 70 kDa protein 2. PRO_0000078258
MOD_RES   42    42        Phosphotyrosine. 
MOD_RES   108   108        Phosphotyrosine. 
VARIANT   191   191  1     C -> S. VAR_032706 [3D]
VARIANT   496   496  1     K -> E. VAR_032707 
CONFLICT   14    14        T -> P (in Ref. 5; AAH36107). 
CONFLICT   54    54        Missing (in Ref. 6; AAC50076). 
CONFLICT   80    80        E -> G (in Ref. 5; AAH36107). 
CONFLICT   266   266        L -> S (in Ref. 2; AAD11466). 
Sequence information
Length: 639 AA [This is the length of the unprocessed precursor] Molecular weight: 70021 Da [This is the MW of the unprocessed precursor] CRC64: 3851755494E7B729 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER LIGDAAKNQV 

        70         80         90        100        110        120 
AMNPTNTIFD AKRLIGRKFE DATVQSDMKH WPFRVVSEGG KPKVQVEYKG ETKTFFPEEI 

       130        140        150        160        170        180 
SSMVLTKMKE IAEAYLGGKV HSAVITVPAY FNDSQRQATK DAGTITGLNV LRIINEPTAA 

       190        200        210        220        230        240 
AIAYGLDKKG CAGGEKNVLI FDLGGGTFDV SILTIEDGIF EVKSTAGDTH LGGEDFDNRM 

       250        260        270        280        290        300 
VSHLAEEFKR KHKKDIGPNK RAVRRLRTAC ERAKRTLSSS TQASIEIDSL YEGVDFYTSI 

       310        320        330        340        350        360 
TRARFEELNA DLFRGTLEPV EKALRDAKLD KGQIQEIVLV GGSTRIPKIQ KLLQDFFNGK 

       370        380        390        400        410        420 
ELNKSINPDE AVAYGAAVQA AILIGDKSEN VQDLLLLDVT PLSLGIETAG GVMTPLIKRN 

       430        440        450        460        470        480 
TTIPTKQTQT FTTYSDNQSS VLVQVYEGER AMTKDNNLLG KFDLTGIPPA PRGVPQIEVT 

       490        500        510        520        530        540 
FDIDANGILN VTAADKSTGK ENKITITNDK GRLSKDDIDR MVQEAERYKS EDEANRDRVA 

       550        560        570        580        590        600 
AKNALESYTY NIKQTVEDEK LRGKISEQDK NKILDKCQEV INWLDRNQMA EKDEYEHKQK 

       610        620        630 
ELERVCNPII SKLYQGGPGG GSGGGGSGAS GGPTIEEVD 

P54652 in FASTA format

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