ID E9Q0U7_MOUSE Unreviewed; 817 AA.
AC E9Q0U7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Heat shock 105kDa/110kDa protein 1 {ECO:0000313|Ensembl:ENSMUSP00000144297.2};
GN Name=Hsph1 {ECO:0000313|Ensembl:ENSMUSP00000144297.2,
GN ECO:0000313|MGI:MGI:105053};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000144297.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:15345747}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [2] {ECO:0007829|PubMed:19144319}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [3] {ECO:0007829|PubMed:19131326}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [4] {ECO:0000313|Ensembl:ENSMUSP00000144297.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000144297.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6] {ECO:0007829|PubMed:23806337}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7] {ECO:0000313|Ensembl:ENSMUSP00000144297.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000144297.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
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DR AlphaFoldDB; E9Q0U7; -.
DR SMR; E9Q0U7; -.
DR SwissPalm; E9Q0U7; -.
DR jPOST; E9Q0U7; -.
DR MaxQB; E9Q0U7; -.
DR PeptideAtlas; E9Q0U7; -.
DR ProteomicsDB; 363647; -.
DR Antibodypedia; 22778; 580 antibodies from 39 providers.
DR Ensembl; ENSMUST00000202089.4; ENSMUSP00000144297.2; ENSMUSG00000029657.16.
DR AGR; MGI:105053; -.
DR MGI; MGI:105053; Hsph1.
DR VEuPathDB; HostDB:ENSMUSG00000029657; -.
DR GeneTree; ENSGT00940000159635; -.
DR ChiTaRS; Hsph1; mouse.
DR Proteomes; UP000000589; Chromosome 5.
DR Bgee; ENSMUSG00000029657; Expressed in embryonic post-anal tail and 266 other cell types or tissues.
DR ExpressionAtlas; E9Q0U7; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR Gene3D; 1.20.1270.10; -; 2.
DR Gene3D; 3.30.420.40; -; 3.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR45639:SF2; HEAT SHOCK PROTEIN 105 KDA; 1.
DR PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 2.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proteomics identification {ECO:0007829|EPD:E9Q0U7,
KW ECO:0007829|MaxQB:E9Q0U7};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT REGION 459..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 817 AA; 91678 MW; 1F0ABBEF3295F53F CRC64;
MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGSKNRTIGV AAKNQQITHA
NNTVSSFKRF HGRAFNDPFI QKEKENLSYD LVPMKNGGVG IKVPSFFTDA ERRSVLDAAQ
IVGLNCLRLM NDMTAVALNY GIYKQDLPNA EEKPRVVVFV DMGHSSFQVS ACAFNKGKLK
VLGTAFDPFL GGKNFDEKLV EHFCAEFKTK YKLDAKSKIR ALLRLHQECE KLKKLMSSNS
TDLPLNIECF MNDKDVSGKM NRSQFEELCA ELLQKIEVPL HSLMAQTQLK AEDVSAIEIV
GGATRIPAVK ERIAKFFGKD VSTTLNADEA VARGCALQCA ILSPAFKVRE FSVTDAVPFP
ISLVWNHDSE ETEGVHEVFS RNHAAPFSKV LTFLRRGPFE LEAFYSDPQG VPYPEAKIGR
FVVQNVSAQK DGEKSRVKVK VRVNTHGIFT ISTASMVEKV PTEEEDGSSL EADMECPNQR
PTESSDVDKN IQQDNSEAGT QPQVQTDGQQ TSQSPPSPEL TSEESKTPDA DKANEKKVDQ
PPEAKKPKIK VVNVELPVEA NLVWQLGRDL LNMYIETEGK MIMQDKLEKE RNDAKNAVEE
CVYEFRDKLC GPYEKFICEQ EHEKFLRLLT ETEDWLYEEG EDQAKQAYID KLEELMKMGT
PVKVRFQEAE ERPKVLEELG QRLQHYAKIA ADFRGKDEKY NHIDESEMKK VEKSVNEVME
WMNNVMNAQA KRSLDQDPVV RTHEIRAKVK ELNNVCEPVV TQPKPKIESP KLERTPNGPN
IDKKEDLEGK NNLGAEAPHQ NGECHPNEKG SVNMDLD
//
