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   25-JAN-2012, entry version 110.
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 carcinoma;
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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
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   -!- INTERACTION:
CC       Q9NZL4:HSPBP1; NbExp=3; IntAct=EBI-356991, EBI-356763;
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/";
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; 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; NM_021979.3.
DR   UniGene; Hs.728938; -.
DR   PDB; 3I33; X-ray; 1.30 A; A=6-386.
DR   PDBsum; 3I33; -.
DR   ProteinModelPortal; P54652; -.
DR   SMR; P54652; 3-616.
DR   IntAct; P54652; 5.
DR   MINT; MINT-1146083; -.
DR   STRING; P54652; -.
DR   PhosphoSite; P54652; -.
DR   DMDM; 1708307; -.
DR   REPRODUCTION-2DPAGE; IPI00007702; -.
DR   PeptideAtlas; P54652; -.
DR   PRIDE; P54652; -.
DR   Ensembl; ENST00000247207; ENSP00000247207; ENSG00000126803.
DR   Ensembl; ENST00000394709; ENSP00000378199; ENSG00000126803.
DR   GeneID; 3306; -.
DR   KEGG; hsa:3306; -.
DR   UCSC; uc001xhj.2; human.
DR   CTD; 3306; -.
DR   GeneCards; GC14P065002; -.
DR   H-InvDB; HIX0011736; -.
DR   HGNC; HGNC:5235; HSPA2.
DR   HPA; HPA000798; -.
DR   MIM; 140560; gene.
DR   neXtProt; NX_P54652; -.
DR   PharmGKB; PA29501; -.
DR   eggNOG; maNOG09073; -.
DR   GeneTree; ENSGT00550000074467; -.
DR   HOGENOM; HBG334976; -.
DR   HOVERGEN; HBG051845; -.
DR   InParanoid; P54652; -.
DR   OMA; LESYTYN; -.
DR   OrthoDB; EOG4W6NVK; -.
DR   PhylomeDB; P54652; -.
DR   Reactome; REACT_111183; Meiosis.
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: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   KO; K03283; -.
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; Chaperone; Complete proteome;
KW   Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW   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).
FT   STRAND       16     18
FT   STRAND       38     40
FT   STRAND       43     45
FT   HELIX        55     58
FT   TURN         59     62
FT   HELIX        71     73
FT   HELIX        82     88
FT   STRAND       92     97
FT   STRAND      102    107
FT   STRAND      112    115
FT   HELIX       117    135
FT   STRAND      142    147
FT   HELIX       153    161
FT   STRAND      169    175
FT   HELIX       176    183
FT   STRAND      197    203
FT   STRAND      209    215
FT   STRAND      220    226
FT   HELIX       235    252
FT   HELIX       260    276
FT   TURN        277    279
FT   STRAND      280    287
FT   STRAND      296    301
FT   HELIX       302    308
FT   HELIX       310    313
FT   HELIX       317    327
FT   STRAND      336    340
FT   HELIX       347    356
FT   TURN        368    373
FT   HELIX       377    383
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
//