HSP74_MOUSE
ID HSP74_MOUSE Reviewed; 841 AA.
AC Q61316;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Heat shock 70 kDa protein 4;
DE AltName: Full=Heat shock 70-related protein APG-2;
GN Name=Hspa4; Synonyms=Apg2, Hsp110;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DDY/STD; TISSUE=Testis;
RX PubMed=9161406; DOI=10.1016/s0378-1119(96)00807-4;
RA Kaneko Y., Kimura T., Kishishita M., Noda Y., Fujita J.;
RT "Cloning of apg-2 encoding a novel member of heat shock protein 110
RT family.";
RL Gene 189:19-24(1997).
RN [2]
RP PROTEIN SEQUENCE OF 74-124; 155-169; 186-196; 220-234; 330-346; 361-374;
RP 391-405; 699-705 AND 719-734, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-336 AND TYR-661, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-336, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-415 AND THR-540, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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).
CC -!- SUBUNIT: Interacts with TJP1/ZO-1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; D85904; BAA12914.1; -; mRNA.
DR AlphaFoldDB; Q61316; -.
DR SMR; Q61316; -.
DR DIP; DIP-46965N; -.
DR IntAct; Q61316; 8.
DR MINT; Q61316; -.
DR STRING; 10090.ENSMUSP00000020630; -.
DR iPTMnet; Q61316; -.
DR PhosphoSitePlus; Q61316; -.
DR SwissPalm; Q61316; -.
DR REPRODUCTION-2DPAGE; Q61316; -.
DR CPTAC; non-CPTAC-3824; -.
DR EPD; Q61316; -.
DR jPOST; Q61316; -.
DR MaxQB; Q61316; -.
DR PaxDb; Q61316; -.
DR PeptideAtlas; Q61316; -.
DR PRIDE; Q61316; -.
DR ProteomicsDB; 273195; -.
DR MGI; MGI:1342292; Hspa4.
DR eggNOG; KOG0103; Eukaryota.
DR InParanoid; Q61316; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR ChiTaRS; Hspa4; mouse.
DR PRO; PR:Q61316; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61316; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0043392; P:negative regulation of DNA binding; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0009408; P:response to heat; ISO:MGI.
DR CDD; cd11737; HSPA4_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 2.
DR Gene3D; 2.60.34.10; -; 1.
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 InterPro; IPR042052; HSPA4_NBD.
DR Pfam; PF00012; HSP70; 2.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 2.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Methylation; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Stress response.
FT CHAIN 1..841
FT /note="Heat shock 70 kDa protein 4"
FT /id="PRO_0000078263"
FT REGION 500..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 89
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P34932"
FT MOD_RES 336
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660,
FT ECO:0007744|PubMed:18034455"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34932"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 430
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P34932"
FT MOD_RES 540
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34932"
FT MOD_RES 661
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 680
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P34932"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34932"
FT MOD_RES 774
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P34932"
SQ SEQUENCE 841 AA; 94133 MW; E7FF19F555C115ED CRC64;
MSVVGIDLGF QSCYVAVARA GGIETIANEY SDRCTPACVS FGPKNRSIGA AAKSQVISNA
KNTVQGFKRF HGRAFSDPFV EAEKSNLAYD IVQLPTGLTG IKVTYMEEER NFTTEQVTAM
LLSKLKETAE SVLKKPVVDC VVSVPSFYTD AERRSVMDAT QIAGLNCLRL MNETTAVALA
YGIYKQDLPA LEEKPRNVVF VDMGHSAYQV SVCAFNKGKL KVLATAFDTT LGGRKFDEVL
VNHFCEEFGK KYKLDIKSKI RALLRLSQEC EKLKKLMSAN ASDLPLSIEC FMNDIDVSGT
MNRGKFLEMC DDLLARVEPP LRSVLEQSKL KKEDIYAVEI VGGATRIPAV KEKISKFFGK
ELSTTLNADE AVTRGCALQC AILSPAFKVR EFSITDVVPY PISLRWNSPA EEGLSDCEVF
PKNHAAPFSK VLTFYRKEPF TLEAYYSSPQ DLPYPDPAIA QFSVQKVTPQ SDGSSSKVKV
KVRVNVHGIF SVSSAALVEV HKSEESEEPM ETDQNAKEEE KMQVDQEEPH TEEQQQQPQT
PAENKAESEE METSQAGSKD KKTDQPPQAK KAKVKTSTVD LPIEHTLWQL DREMLALYTE
NEGKMIMQDK LEKERNDAKN AVEEYVYEMR DKLSGEYEKF VSEDDRNTFT LKLEDTENWL
YEDGEDQPKQ VYVDKLAELK SLGQPIKTRF QESEERPKLF EELGKQIQQY MKVISSFKNK
EDQYEHLDAA DVTKVEKSTN EAMEWMNSKL NLQNKQSLTV DPVVKTKEIE AKIKELTSIC
SPIISKPKPK VEPPKEEPKH AEQNGPVDGQ GDNPGSQAAE HGADTAVPSD GDKKLPEMDI
D
