ID   HSP72_HUMAN             Reviewed;         639 AA.
AC   P54652; Q15508; Q53XM3; Q9UE78;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-NOV-2009, entry version 89.
DE   RecName: Full=Heat shock-related 70 kDa protein 2;
DE            Short=Heat shock 70 kDa protein 2;
GN   Name=HSPA2;
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].
RX   MEDLINE=95130116; PubMed=7829106; DOI=10.1006/geno.1994.1462;
RA   Bonnycastle L.L.C., Yu C.-E., Hunt C.R., Trask B.J., Clancy K.P.,
RA   Weber J.L., Patterson D., Schellenberg G.D.;
RT   "Cloning, sequencing, and mapping of the human chromosome 14 heat
RT   shock protein gene (HSPA2).";
RL   Genomics 23:85-93(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Goralski T.J., Krensky A.M.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-191 AND GLU-496.
RG   NIEHS SNPs program;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Eye;
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-126.
RX   MEDLINE=95152505; PubMed=7849706; DOI=10.1093/hmg/3.10.1819;
RA   Roux A.-F., Nguyen V.T.T., Squire J.A., Cox D.W.;
RT   "A heat shock gene at 14q22: mapping and expression.";
RL   Hum. Mol. Genet. 3:1819-1822(1994).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42 AND TYR-108, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Lung;
RX   PubMed=18083107; DOI=10.1016/j.cell.2007.11.025;
RA   Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,
RA   Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,
RA   Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,
RA   Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,
RA   Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
RT   "Global survey of phosphotyrosine signaling identifies oncogenic
RT   kinases in lung cancer.";
RL   Cell 131:1190-1203(2007).
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.
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.
CC   -!- SUBUNIT: Interacts with ZNF541 (By similarity).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/hspa2/";
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DR   EMBL; L26336; AAA52698.1; -; Genomic_DNA.
DR   EMBL; U56725; AAD11466.1; -; mRNA.
DR   EMBL; BT009815; AAP88817.1; -; mRNA.
DR   EMBL; DQ489378; ABE96830.1; -; Genomic_DNA.
DR   EMBL; BC001752; AAH01752.1; -; mRNA.
DR   EMBL; BC036107; AAH36107.1; -; mRNA.
DR   EMBL; U10149; AAC50076.1; -; Genomic_DNA.
DR   IPI; IPI00007702; -.
DR   PIR; A55719; A55719.
DR   PIR; I37564; I37564.
DR   RefSeq; NP_068814.2; -.
DR   UniGene; Hs.432648; -.
DR   PDB; 3I33; X-ray; 1.30 A; A=6-386.
DR   PDBsum; 3I33; -.
DR   SMR; P54652; 3-557, 545-620.
DR   IntAct; P54652; 8.
DR   STRING; P54652; -.
DR   PhosphoSite; P54652; -.
DR   REPRODUCTION-2DPAGE; IPI00007702; -.
DR   PeptideAtlas; P54652; -.
DR   PRIDE; P54652; -.
DR   Ensembl; ENST00000247207; ENSP00000247207; ENSG00000126803; Homo sapiens.
DR   Ensembl; ENST00000394709; ENSP00000378199; ENSG00000126803; Homo sapiens.
DR   GeneID; 3306; -.
DR   KEGG; hsa:3306; -.
DR   UCSC; uc001xhj.2; human.
DR   CTD; 3306; -.
DR   GeneCards; GC14P064072; -.
DR   H-InvDB; HIX0011736; -.
DR   HGNC; HGNC:5235; HSPA2.
DR   HPA; HPA000798; -.
DR   MIM; 140560; gene.
DR   PharmGKB; PA29501; -.
DR   HOGENOM; P54652; -.
DR   HOVERGEN; P54652; -.
DR   OMA; LESYTYN; -.
DR   NextBio; 13115; -.
DR   ArrayExpress; P54652; -.
DR   Bgee; P54652; -.
DR   CleanEx; HS_HSPA2; -.
DR   Genevestigator; P54652; -.
DR   GermOnline; ENSG00000126803; Homo sapiens.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
DR   GO; GO:0007140; P:male meiosis; TAS:ProtInc.
DR   GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR   GO; GO:0007286; P:spermatid development; 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   ProDom; PD000089; Hsp70; 1.
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; Chaperone; Complete proteome;
KW   Nucleotide-binding; Phosphoprotein; Polymorphism; Stress response.
FT   CHAIN         1    639       Heat shock-related 70 kDa protein 2.
FT                                /FTId=PRO_0000078258.
FT   MOD_RES      42     42       Phosphotyrosine.
FT   MOD_RES     108    108       Phosphotyrosine.
FT   VARIANT     191    191       C -> S.
FT                                /FTId=VAR_032706.
FT   VARIANT     496    496       K -> E.
FT                                /FTId=VAR_032707.
FT   CONFLICT     14     14       T -> P (in Ref. 5; AAH36107).
FT   CONFLICT     54     54       Missing (in Ref. 6; AAC50076).
FT   CONFLICT     80     80       E -> G (in Ref. 5; AAH36107).
FT   CONFLICT    266    266       L -> S (in Ref. 2; AAD11466).
SQ   SEQUENCE   639 AA;  70021 MW;  3851755494E7B729 CRC64;
     MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER LIGDAAKNQV
     AMNPTNTIFD AKRLIGRKFE DATVQSDMKH WPFRVVSEGG KPKVQVEYKG ETKTFFPEEI
     SSMVLTKMKE IAEAYLGGKV HSAVITVPAY FNDSQRQATK DAGTITGLNV LRIINEPTAA
     AIAYGLDKKG CAGGEKNVLI FDLGGGTFDV SILTIEDGIF EVKSTAGDTH LGGEDFDNRM
     VSHLAEEFKR KHKKDIGPNK RAVRRLRTAC ERAKRTLSSS TQASIEIDSL YEGVDFYTSI
     TRARFEELNA DLFRGTLEPV EKALRDAKLD KGQIQEIVLV GGSTRIPKIQ KLLQDFFNGK
     ELNKSINPDE AVAYGAAVQA AILIGDKSEN VQDLLLLDVT PLSLGIETAG GVMTPLIKRN
     TTIPTKQTQT FTTYSDNQSS VLVQVYEGER AMTKDNNLLG KFDLTGIPPA PRGVPQIEVT
     FDIDANGILN VTAADKSTGK ENKITITNDK GRLSKDDIDR MVQEAERYKS EDEANRDRVA
     AKNALESYTY NIKQTVEDEK LRGKISEQDK NKILDKCQEV INWLDRNQMA EKDEYEHKQK
     ELERVCNPII SKLYQGGPGG GSGGGGSGAS GGPTIEEVD
//