HSP7E_MOUSE
ID HSP7E_MOUSE Reviewed; 509 AA.
AC Q99M31; A2AJH7; Q3U5W7; Q60637;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Heat shock 70 kDa protein 14;
DE AltName: Full=NST-1;
DE AltName: Full=hsr.1;
GN Name=Hspa14; Synonyms=Hsp70-4;
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] (ISOFORM 1).
RC TISSUE=Brain;
RA Yang C.;
RT "The molecular cloning and characterization of NST-1 (hsr.1), a novel
RT member of the Hsp70 superfamily.";
RL Thesis (1994), Rockefeller University, United States.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, 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).
CC -!- FUNCTION: Component of the ribosome-associated complex (RAC), a complex
CC involved in folding or maintaining nascent polypeptides in a folding-
CC competent state. In the RAC complex, binds to the nascent polypeptide
CC chain, while DNAJC2 stimulates its ATPase activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of ribosome-associated complex (RAC), a heterodimer
CC composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type
CC chaperone DNAJC2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99M31-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99M31-2; Sequence=VSP_026032;
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; U08215; AAA17724.1; -; mRNA.
DR EMBL; AK145937; BAE26767.1; -; mRNA.
DR EMBL; AK153397; BAE31959.1; -; mRNA.
DR EMBL; AL732620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002056; AAH02056.1; -; mRNA.
DR CCDS; CCDS15653.1; -. [Q99M31-1]
DR RefSeq; NP_056580.2; NM_015765.2. [Q99M31-1]
DR AlphaFoldDB; Q99M31; -.
DR SMR; Q99M31; -.
DR BioGRID; 206043; 8.
DR IntAct; Q99M31; 10.
DR MINT; Q99M31; -.
DR STRING; 10090.ENSMUSP00000027961; -.
DR iPTMnet; Q99M31; -.
DR PhosphoSitePlus; Q99M31; -.
DR EPD; Q99M31; -.
DR MaxQB; Q99M31; -.
DR PaxDb; Q99M31; -.
DR PeptideAtlas; Q99M31; -.
DR PRIDE; Q99M31; -.
DR ProteomicsDB; 267068; -. [Q99M31-1]
DR ProteomicsDB; 267069; -. [Q99M31-2]
DR Antibodypedia; 37843; 146 antibodies from 28 providers.
DR DNASU; 50497; -.
DR Ensembl; ENSMUST00000027961; ENSMUSP00000027961; ENSMUSG00000109865. [Q99M31-1]
DR GeneID; 50497; -.
DR KEGG; mmu:50497; -.
DR UCSC; uc008ief.1; mouse. [Q99M31-1]
DR UCSC; uc008ieg.1; mouse. [Q99M31-2]
DR CTD; 51182; -.
DR MGI; MGI:1354164; Hspa14.
DR VEuPathDB; HostDB:ENSMUSG00000109865; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00940000156380; -.
DR HOGENOM; CLU_005965_0_3_1; -.
DR InParanoid; Q99M31; -.
DR OMA; TSVFHYR; -.
DR OrthoDB; 646813at2759; -.
DR PhylomeDB; Q99M31; -.
DR TreeFam; TF105045; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR BioGRID-ORCS; 50497; 20 hits in 75 CRISPR screens.
DR PRO; PR:Q99M31; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99M31; protein.
DR Bgee; ENSMUSG00000109865; Expressed in ectoplacental cone and 261 other tissues.
DR Genevisible; Q99M31; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005840; C:ribosome; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd10238; HSPA14-like_NBD; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR InterPro; IPR042049; HSPA14_NBD.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chaperone; Cytoplasm;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..509
FT /note="Heat shock 70 kDa protein 14"
FT /id="PRO_0000289947"
FT VAR_SEQ 485..509
FT /note="DGSLQVTCTDQDTGKCEAITVEVAS -> YKMKCFQYYEDSLKLGPFGAWLN
FT YHSRQILC (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026032"
FT CONFLICT 229
FT /note="A -> G (in Ref. 1; AAA17724)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="Q -> R (in Ref. 3; AAH02056)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="C -> WHE (in Ref. 1; AAA17724)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 54650 MW; D27133C677373DB0 CRC64;
MAAIGVHLGC TSACVAVYKD GRADVVANDA GDRVTPAIVA YSEREQVVGL AAKQSRIRHV
SSTVVKVKQI LGRSSADPQA QKYISESKCL VIEKNGKLRY EIDTGEETKL VNPEDVARLI
FSKMKETAHS VLGSDANDVV VTVPFDFGEK QKSALGEAAG AAGFNVLRLI HEPSAALLAY
GIGQDHPTGK SNVLVFKLGG TSLSLSVMEV NSGMYRVLST NTSDNIGGAH FTDTLAQYLA
SEFQRLFKHD VRGNARAMMK LMNSAEVAKH SLSTLGSANC FVDSLYEGQD FDCNVSRARF
ELLCSPLFNK CTEAIRELLR QTGFTADDIN KVVLCGGSSR IPKLQQLIKD LFPAVDLLNS
IPPDEVIPIG AAIEAGILVG KESTSGDDSV MIECSAKDIL VKGVDESGAD RFTVLFPSGT
PLPARRQHTL QAPGRVSSVC LELYESEGKN SAKEEAKFAQ VVLQDLDKKE NGLRDILAVL
TMKRDGSLQV TCTDQDTGKC EAITVEVAS
