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Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8)

 HSP7C_MOUSE             Reviewed;         646 AA.
P63017; P08109; P12225; Q3U6R0; Q3U764; Q3U7D7; Q3U7E2; Q3U9B4;
Q3U9G0; Q3UGM0; Q5FWJ6; Q62373; Q62374; Q62375; Q6NZD0;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
22-NOV-2017, entry version 145.
RecName: Full=Heat shock cognate 71 kDa protein;
AltName: Full=Heat shock 70 kDa protein 8;
Name=Hspa8; Synonyms=Hsc70, Hsc73;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3334718; DOI=10.1016/0012-1606(88)90073-5;
Giebel L.B., Dworniczak B.P., Bautz E.K.F.;
"Developmental regulation of a constitutively expressed mouse mRNA
encoding a 72-kDa heat shock-like protein.";
Dev. Biol. 125:200-207(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129; TISSUE=Mammary gland;
PubMed=8682318; DOI=10.1016/0378-1119(96)00169-2;
Soulier S., Vilotte J.-L., L'Huillier P.J., Mercier J.-C.;
"Developmental regulation of murine integrin beta 1 subunit- and
Hsc73-encoding genes in mammary gland: sequence of a new mouse Hsc73
cDNA.";
Gene 172:285-289(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129;
PubMed=10095055; DOI=10.1016/S0167-4781(98)00285-1;
Hunt C.R., Parsian A.J., Goswami P.C., Kozak C.A.;
"Characterization and expression of the mouse Hsc70 gene.";
Biochim. Biophys. Acta 1444:315-325(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and DBA/2J;
TISSUE=Amnion, Bone marrow, Heart, Kidney, Liver, Stomach, Thymus, and
Urinary bladder;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and FVB/N;
TISSUE=Brain, Embryo, Embryonic germ cell, Eye, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 4-49; 57-71; 77-102; 113-155; 160-188; 221-246;
300-319; 326-342; 349-357; 362-384; 424-447; 540-550 AND 584-597, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 333-383; 438-452 AND 580-587.
PubMed=2251119; DOI=10.1093/nar/18.22.6565;
Liu J., Maxwell E.S.;
"Mouse U14 snRNA is encoded in an intron of the mouse cognate hsc70
heat shock gene.";
Nucleic Acids Res. 18:6565-6571(1990).
[8]
INTERACTION WITH HSPH1.
PubMed=9675148; DOI=10.1006/bbrc.1998.8979;
Hatayama T., Yasuda K., Yasuda K.;
"Association of HSP105 with HSC70 in high molecular mass complexes in
mouse FM3A cells.";
Biochem. Biophys. Res. Commun. 248:395-401(1998).
[9]
INTERACTION WITH HSPH1.
PubMed=15292236; DOI=10.1074/jbc.M407947200;
Yamagishi N., Ishihara K., Hatayama T.;
"Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70
ATPase activity.";
J. Biol. Chem. 279:41727-41733(2004).
[10]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[11]
INTERACTION WITH IRAK1BP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17233114; DOI=10.1089/dna.2006.25.704;
Haag Breese E., Uversky V.N., Georgiadis M.M., Harrington M.A.;
"The disordered amino-terminus of SIMPL interacts with members of the
70-kDa heat-shock protein family.";
DNA Cell Biol. 25:704-714(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
METHYLATION AT LYS-561.
PubMed=23921388; DOI=10.1074/jbc.M113.483248;
Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S.,
Melki R., Falnes P.O.;
"Identification and characterization of a novel human
methyltransferase modulating Hsp70 function through lysine
methylation.";
J. Biol. Chem. 288:27752-27763(2013).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108; LYS-246; LYS-319;
LYS-328; LYS-512; LYS-524 AND LYS-601, SUCCINYLATION [LARGE SCALE
ANALYSIS] AT LYS-319 AND LYS-512, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast, and Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[15]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-469, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Molecular chaperone implicated in a wide variety of
cellular processes, including protection of the proteome from
stress, folding and transport of newly synthesized polypeptides,
activation of proteolysis of misfolded proteins and the formation
and dissociation of protein complexes. Plays a pivotal role in the
protein quality control system, ensuring the correct folding of
proteins, the re-folding of misfolded proteins and controlling the
targeting of proteins for subsequent degradation. This is achieved
through cycles of ATP binding, ATP hydrolysis and ADP release,
mediated by co-chaperones. The co-chaperones have been shown to
not only regulate different steps of the ATPase cycle of HSP70,
but they also have an individual specificity such that one co-
chaperone may promote folding of a substrate while another may
promote degradation. The affinity of HSP70 for polypeptides is
regulated by its nucleotide bound state. In the ATP-bound form, it
has a low affinity for substrate proteins. However, upon
hydrolysis of the ATP to ADP, it undergoes a conformational change
that increases its affinity for substrate proteins. HSP70 goes
through repeated cycles of ATP hydrolysis and nucleotide exchange,
which permits cycles of substrate binding and release. The HSP70-
associated co-chaperones are of three types: J-domain co-
chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the
nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate
conversion of HSP70 from the ADP-bound to the ATP-bound state
thereby promoting substrate release), and the TPR domain
chaperones such as HOPX and STUB1. Acts as a repressor of
transcriptional activation. Inhibits the transcriptional
coactivator activity of CITED1 on Smad-mediated transcription.
Component of the PRP19-CDC5L complex that forms an integral part
of the spliceosome and is required for activating pre-mRNA
splicing. May have a scaffolding role in the spliceosome assembly
as it contacts all other components of the core complex. Binds
bacterial lipopolysaccharide (LPS) and mediates LPS-induced
inflammatory response, including TNF secretion. Participates in
the ER-associated degradation (ERAD) quality control pathway in
conjunction with J domain-containing co-chaperones and the E3
ligase STUB1. {ECO:0000250|UniProtKB:P11142}.
-!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
containing untranslated mRNAs. Interacts with PACRG. Interacts
with DNAJC7. Interacts with DNAJB12 (via J domain). Interacts with
DNAJB14 (via J domain). Interacts (via C-terminus) with the E3
ligase STUB1 forming a 210 kDa complex of one STUB1 and two HSPA8
molecules. Interacts with CITED1 (via N-terminus); the interaction
suppresses the association of CITED1 to p300/CBP and Smad-mediated
transcription transactivation. Component of the PRP19-CDC5L
splicing complex composed of a core complex comprising a
homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three
less stably associated proteins CTNNBL1, CWC15 and HSPA8.
Interacts with IRAK1BP1 and HSPH1/HSP105 (PubMed:9675148,
PubMed:15292236, PubMed:17233114). Interacts with TRIM5. Part of a
complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2,
MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may
have a histone H3-specific methyltransferase activity. Following
LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1.
Interacts with PRKN. Interacts with FOXP3. Interacts with DNAJC9
(via J domain). Interacts with MLLT11. Interacts with RNF207.
Interacts with DNAJC21. Interacts with DNAJB2. Interacts with TTC1
(via TPR repeats). Interacts with SGTA (via TPR repeats).
Interacts with HSF1 (via transactivation domain). Interacts with
HOPX, STUB1, HSP40, HSP90, BAG2 and BAG3 (By similarity).
Interacts with DNAJC12 (By similarity).
{ECO:0000250|UniProtKB:P11142, ECO:0000250|UniProtKB:P63018,
ECO:0000269|PubMed:15292236, ECO:0000269|PubMed:17233114,
ECO:0000269|PubMed:9675148}.
-!- INTERACTION:
O41974:GAMMAHV.ORF73 (xeno); NbExp=3; IntAct=EBI-433443, EBI-6933128;
O88447:Klc1; NbExp=3; IntAct=EBI-433443, EBI-301550;
P43883:Plin2; NbExp=3; IntAct=EBI-433443, EBI-16156700;
Q9DBG5:Plin3; NbExp=2; IntAct=EBI-433443, EBI-643495;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
{ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cell membrane
{ECO:0000250}. Note=Localized in cytoplasmic mRNP granules
containing untranslated mRNAs. Translocates rapidly from the
cytoplasm to the nuclei, and especially to the nucleoli, upon heat
shock (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- INDUCTION: Constitutively synthesized.
-!- DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known
as the ATPase domain) is responsible for binding and hydrolyzing
ATP. The C-terminal substrate-binding domain (SBD) (also known as
peptide-binding domain) binds to the client/substrate proteins.
The two domains are allosterically coupled so that, when ATP is
bound to the NBD, the SBD binds relatively weakly to clients. When
ADP is bound in the NBD, a conformational change enhances the
affinity of the SBD for client proteins.
{ECO:0000250|UniProtKB:P11142}.
-!- PTM: Acetylated. {ECO:0000250|UniProtKB:P11142}.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- PTM: Trimethylation at Lys-561 reduces fibrillar SNCA binding.
{ECO:0000250|UniProtKB:P11142}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAE31508.1; Type=Frameshift; Positions=256, 269; Evidence={ECO:0000305};
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EMBL; M19141; AAA37869.1; -; mRNA.
EMBL; U27129; AAC52836.1; -; mRNA.
EMBL; U73744; AAB18391.1; -; Genomic_DNA.
EMBL; AK035286; BAC29016.1; -; mRNA.
EMBL; AK075935; BAC36065.1; -; mRNA.
EMBL; AK145579; BAE26523.1; -; mRNA.
EMBL; AK146708; BAE27374.1; -; mRNA.
EMBL; AK146985; BAE27588.1; -; mRNA.
EMBL; AK147864; BAE28187.1; -; mRNA.
EMBL; AK150474; BAE29591.1; -; mRNA.
EMBL; AK150498; BAE29612.1; -; mRNA.
EMBL; AK150701; BAE29780.1; -; mRNA.
EMBL; AK150958; BAE29990.1; -; mRNA.
EMBL; AK151065; BAE30081.1; -; mRNA.
EMBL; AK151127; BAE30135.1; -; mRNA.
EMBL; AK151287; BAE30272.1; -; mRNA.
EMBL; AK151435; BAE30398.1; -; mRNA.
EMBL; AK151516; BAE30465.1; -; mRNA.
EMBL; AK151537; BAE30484.1; -; mRNA.
EMBL; AK151775; BAE30681.1; -; mRNA.
EMBL; AK151808; BAE30707.1; -; mRNA.
EMBL; AK151865; BAE30753.1; -; mRNA.
EMBL; AK151892; BAE30776.1; -; mRNA.
EMBL; AK151948; BAE30822.1; -; mRNA.
EMBL; AK151997; BAE30861.1; -; mRNA.
EMBL; AK152598; BAE31346.1; -; mRNA.
EMBL; AK152697; BAE31427.1; -; mRNA.
EMBL; AK152703; BAE31432.1; -; mRNA.
EMBL; AK152803; BAE31508.1; ALT_FRAME; mRNA.
EMBL; AK153032; BAE31664.1; -; mRNA.
EMBL; AK153834; BAE32204.1; -; mRNA.
EMBL; AK159479; BAE35116.1; -; mRNA.
EMBL; AK164000; BAE37581.1; -; mRNA.
EMBL; AK166643; BAE38912.1; -; mRNA.
EMBL; AK166721; BAE38970.1; -; mRNA.
EMBL; AK166767; BAE39005.1; -; mRNA.
EMBL; AK166776; BAE39012.1; -; mRNA.
EMBL; AK166808; BAE39036.1; -; mRNA.
EMBL; AK166830; BAE39053.1; -; mRNA.
EMBL; AK166846; BAE39065.1; -; mRNA.
EMBL; AK166861; BAE39076.1; -; mRNA.
EMBL; AK166873; BAE39084.1; -; mRNA.
EMBL; AK166908; BAE39109.1; -; mRNA.
EMBL; AK166910; BAE39111.1; -; mRNA.
EMBL; AK166913; BAE39113.1; -; mRNA.
EMBL; AK166933; BAE39127.1; -; mRNA.
EMBL; AK167043; BAE39211.1; -; mRNA.
EMBL; AK167121; BAE39269.1; -; mRNA.
EMBL; AK167122; BAE39270.1; -; mRNA.
EMBL; AK167134; BAE39280.1; -; mRNA.
EMBL; AK167163; BAE39304.1; -; mRNA.
EMBL; AK167218; BAE39344.1; -; mRNA.
EMBL; AK167229; BAE39353.1; -; mRNA.
EMBL; AK167845; BAE39865.1; -; mRNA.
EMBL; AK167910; BAE39917.1; -; mRNA.
EMBL; AK168492; BAE40379.1; -; mRNA.
EMBL; AK168519; BAE40398.1; -; mRNA.
EMBL; AK168542; BAE40419.1; -; mRNA.
EMBL; AK168711; BAE40553.1; -; mRNA.
EMBL; AK168750; BAE40590.1; -; mRNA.
EMBL; AK168776; BAE40612.1; -; mRNA.
EMBL; AK168887; BAE40704.1; -; mRNA.
EMBL; AK168934; BAE40745.1; -; mRNA.
EMBL; AK169093; BAE40876.1; -; mRNA.
EMBL; AK169179; BAE40957.1; -; mRNA.
EMBL; AK169236; BAE41004.1; -; mRNA.
EMBL; AK169293; BAE41049.1; -; mRNA.
EMBL; BC006722; AAH06722.1; -; mRNA.
EMBL; BC066191; AAH66191.1; -; mRNA.
EMBL; BC085486; AAH85486.1; -; mRNA.
EMBL; BC089322; AAH89322.1; -; mRNA.
EMBL; BC089457; AAH89457.1; -; mRNA.
EMBL; BC106193; AAI06194.1; -; mRNA.
EMBL; X54401; CAA38267.1; -; Genomic_DNA.
EMBL; X54402; CAA38268.1; -; Genomic_DNA.
EMBL; X54403; CAA38269.1; -; Genomic_DNA.
CCDS; CCDS23083.1; -.
PIR; A45935; A45935.
PIR; JC4853; JC4853.
RefSeq; NP_112442.2; NM_031165.4.
UniGene; Mm.290774; -.
UniGene; Mm.336743; -.
UniGene; Mm.351377; -.
UniGene; Mm.412745; -.
UniGene; Mm.485345; -.
UniGene; Mm.486272; -.
PDB; 3CQX; X-ray; 2.30 A; A/B=1-381.
PDBsum; 3CQX; -.
ProteinModelPortal; P63017; -.
SMR; P63017; -.
BioGrid; 200428; 44.
CORUM; P63017; -.
DIP; DIP-32353N; -.
IntAct; P63017; 46.
MINT; MINT-189032; -.
STRING; 10090.ENSMUSP00000015800; -.
iPTMnet; P63017; -.
PhosphoSitePlus; P63017; -.
SwissPalm; P63017; -.
COMPLUYEAST-2DPAGE; P63017; -.
REPRODUCTION-2DPAGE; IPI00323357; -.
REPRODUCTION-2DPAGE; P63017; -.
REPRODUCTION-2DPAGE; Q6NZD0; -.
SWISS-2DPAGE; P63017; -.
UCD-2DPAGE; P63017; -.
EPD; P63017; -.
MaxQB; P63017; -.
PaxDb; P63017; -.
PeptideAtlas; P63017; -.
PRIDE; P63017; -.
Ensembl; ENSMUST00000015800; ENSMUSP00000015800; ENSMUSG00000015656.
GeneID; 15481; -.
KEGG; mmu:15481; -.
UCSC; uc009ozx.3; mouse.
CTD; 3312; -.
MGI; MGI:105384; Hspa8.
eggNOG; KOG0101; Eukaryota.
eggNOG; COG0443; LUCA.
GeneTree; ENSGT00900000140908; -.
HOVERGEN; HBG051845; -.
InParanoid; P63017; -.
KO; K03283; -.
OMA; AYTKNQD; -.
OrthoDB; EOG091G03SF; -.
PhylomeDB; P63017; -.
TreeFam; TF105042; -.
Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-MMU-3371568; Attenuation phase.
Reactome; R-MMU-3371571; HSF1-dependent transactivation.
Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
Reactome; R-MMU-8876725; Protein methylation.
Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation.
EvolutionaryTrace; P63017; -.
PRO; PR:P63017; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000015656; -.
CleanEx; MM_HSPA8; -.
ExpressionAtlas; P63017; baseline and differential.
Genevisible; P63017; MM.
GO; GO:0072562; C:blood microparticle; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; IDA:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0005770; C:late endosome; IDA:ParkinsonsUK-UCL.
GO; GO:1990836; C:lysosomal matrix; ISO:MGI.
GO; GO:0005765; C:lysosomal membrane; ISS:ParkinsonsUK-UCL.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0016887; F:ATPase activity; ISO:MGI.
GO; GO:0042623; F:ATPase activity, coupled; IDA:MGI.
GO; GO:0055131; F:C3HC4-type RING finger domain binding; ISO:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0001664; F:G-protein coupled receptor binding; ISO:MGI.
GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
GO; GO:0023026; F:MHC class II protein complex binding; ISO:MGI.
GO; GO:0001786; F:phosphatidylserine binding; IDA:ParkinsonsUK-UCL.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0051082; F:unfolded protein binding; IPI:MGI.
GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
GO; GO:0043624; P:cellular protein complex disassembly; ISO:MGI.
GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IGI:MGI.
GO; GO:0061684; P:chaperone-mediated autophagy; ISS:ParkinsonsUK-UCL.
GO; GO:1904764; P:chaperone-mediated autophagy translocation complex disassembly; ISS:ParkinsonsUK-UCL.
GO; GO:0061741; P:chaperone-mediated protein transport involved in chaperone-mediated autophagy; ISO:MGI.
GO; GO:0072318; P:clathrin coat disassembly; IGI:MGI.
GO; GO:0061738; P:late endosomal microautophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0044788; P:modulation by host of viral process; IMP:AgBase.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:1902904; P:negative regulation of supramolecular fiber organization; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0044829; P:positive regulation by host of viral genome replication; IMP:AgBase.
GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:MGI.
GO; GO:0006457; P:protein folding; IDA:MGI.
GO; GO:0042026; P:protein refolding; ISS:ParkinsonsUK-UCL.
GO; GO:0061740; P:protein targeting to lysosome involved in chaperone-mediated autophagy; ISO:MGI.
GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
GO; GO:0061635; P:regulation of protein complex stability; ISS:ParkinsonsUK-UCL.
GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell membrane; Chaperone;
Complete proteome; Cytoplasm; Direct protein sequencing;
Isopeptide bond; Membrane; Methylation; mRNA processing;
mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Spliceosome; Stress response;
Transcription; Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P11142}.
CHAIN 2 646 Heat shock cognate 71 kDa protein.
/FTId=PRO_0000078271.
NP_BIND 12 15 ATP. {ECO:0000250}.
NP_BIND 202 204 ATP. {ECO:0000250}.
NP_BIND 268 275 ATP. {ECO:0000250}.
NP_BIND 339 342 ATP. {ECO:0000250}.
REGION 2 386 Nucleotide-binding domain (NBD).
{ECO:0000250|UniProtKB:P11142}.
REGION 186 377 Interaction with BAG1. {ECO:0000250}.
REGION 394 509 Substrate-binding domain (SBD).
{ECO:0000250|UniProtKB:P11142}.
BINDING 71 71 ATP. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 108 108 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 153 153 Phosphoserine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 246 246 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 319 319 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 319 319 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 328 328 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 469 469 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 512 512 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 512 512 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 524 524 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 541 541 Phosphoserine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 561 561 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:23921388}.
MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A;
alternate. {ECO:0000250}.
MOD_RES 561 561 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 589 589 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 597 597 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 601 601 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
CROSSLNK 512 512 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P11142}.
CROSSLNK 512 512 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P11142}.
CONFLICT 9 9 I -> V (in Ref. 4; BAE28187).
{ECO:0000305}.
CONFLICT 35 35 N -> K (in Ref. 4; BAE30081/BAE30861/
BAE30753). {ECO:0000305}.
CONFLICT 268 268 E -> G (in Ref. 4; BAE31432/BAE31346).
{ECO:0000305}.
CONFLICT 269 269 R -> G (in Ref. 4; BAE31508).
{ECO:0000305}.
CONFLICT 353 353 F -> C (in Ref. 4; BAE31664).
{ECO:0000305}.
CONFLICT 428 428 F -> L (in Ref. 1; AAA37869 and 3;
AAB18391). {ECO:0000305}.
CONFLICT 432 432 S -> Y (in Ref. 4; BAE30707).
{ECO:0000305}.
CONFLICT 589 589 K -> E (in Ref. 5; AAH66191).
{ECO:0000305}.
CONFLICT 645 645 V -> M (in Ref. 4; BAE30272/BAE31427).
{ECO:0000305}.
STRAND 7 11 {ECO:0000244|PDB:3CQX}.
STRAND 13 22 {ECO:0000244|PDB:3CQX}.
STRAND 25 28 {ECO:0000244|PDB:3CQX}.
STRAND 36 39 {ECO:0000244|PDB:3CQX}.
STRAND 42 44 {ECO:0000244|PDB:3CQX}.
STRAND 49 51 {ECO:0000244|PDB:3CQX}.
HELIX 53 57 {ECO:0000244|PDB:3CQX}.
TURN 58 61 {ECO:0000244|PDB:3CQX}.
HELIX 63 65 {ECO:0000244|PDB:3CQX}.
HELIX 70 72 {ECO:0000244|PDB:3CQX}.
TURN 73 75 {ECO:0000244|PDB:3CQX}.
HELIX 81 86 {ECO:0000244|PDB:3CQX}.
TURN 87 89 {ECO:0000244|PDB:3CQX}.
STRAND 91 97 {ECO:0000244|PDB:3CQX}.
STRAND 100 107 {ECO:0000244|PDB:3CQX}.
STRAND 110 114 {ECO:0000244|PDB:3CQX}.
HELIX 116 135 {ECO:0000244|PDB:3CQX}.
STRAND 141 146 {ECO:0000244|PDB:3CQX}.
HELIX 152 164 {ECO:0000244|PDB:3CQX}.
STRAND 168 174 {ECO:0000244|PDB:3CQX}.
HELIX 175 182 {ECO:0000244|PDB:3CQX}.
TURN 183 186 {ECO:0000244|PDB:3CQX}.
STRAND 187 200 {ECO:0000244|PDB:3CQX}.
STRAND 205 213 {ECO:0000244|PDB:3CQX}.
STRAND 216 225 {ECO:0000244|PDB:3CQX}.
HELIX 230 249 {ECO:0000244|PDB:3CQX}.
HELIX 257 273 {ECO:0000244|PDB:3CQX}.
TURN 274 276 {ECO:0000244|PDB:3CQX}.
STRAND 278 288 {ECO:0000244|PDB:3CQX}.
STRAND 291 298 {ECO:0000244|PDB:3CQX}.
HELIX 299 312 {ECO:0000244|PDB:3CQX}.
HELIX 314 324 {ECO:0000244|PDB:3CQX}.
HELIX 328 330 {ECO:0000244|PDB:3CQX}.
STRAND 333 338 {ECO:0000244|PDB:3CQX}.
HELIX 339 342 {ECO:0000244|PDB:3CQX}.
HELIX 344 353 {ECO:0000244|PDB:3CQX}.
TURN 354 356 {ECO:0000244|PDB:3CQX}.
TURN 365 367 {ECO:0000244|PDB:3CQX}.
HELIX 368 380 {ECO:0000244|PDB:3CQX}.
SEQUENCE 646 AA; 70871 MW; 03A27B30E6C076ED CRC64;
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS
SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA
IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH
FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN
KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI
DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN
SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIISW LDKNQTAEKE EFEHQQKELE
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD


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