HSP13_MOUSE
ID HSP13_MOUSE Reviewed; 471 AA.
AC Q8BM72; Q3TII6; Q9D1X5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Heat shock 70 kDa protein 13;
DE AltName: Full=Microsomal stress-70 protein ATPase core;
DE AltName: Full=Stress-70 protein chaperone microsome-associated 60 kDa protein;
DE Flags: Precursor;
GN Name=Hspa13; Synonyms=Stch;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Corpora quadrigemina, and Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, and Spleen;
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: Has peptide-independent ATPase activity. {ECO:0000250}.
CC -!- SUBUNIT: Binds UBQLN2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Microsome {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BM72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BM72-2; Sequence=VSP_013912, VSP_013913;
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE39860.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK021006; BAB32274.1; -; mRNA.
DR EMBL; AK034643; BAC28781.1; -; mRNA.
DR EMBL; AK167839; BAE39860.1; ALT_INIT; mRNA.
DR EMBL; BC085181; AAH85181.1; -; mRNA.
DR CCDS; CCDS28273.1; -. [Q8BM72-1]
DR RefSeq; NP_084477.1; NM_030201.3. [Q8BM72-1]
DR AlphaFoldDB; Q8BM72; -.
DR SMR; Q8BM72; -.
DR BioGRID; 226017; 9.
DR STRING; 10090.ENSMUSP00000048817; -.
DR GlyConnect; 2366; 4 N-Linked glycans (1 site).
DR GlyGen; Q8BM72; 1 site, 4 N-linked glycans (1 site).
DR PhosphoSitePlus; Q8BM72; -.
DR SwissPalm; Q8BM72; -.
DR EPD; Q8BM72; -.
DR jPOST; Q8BM72; -.
DR MaxQB; Q8BM72; -.
DR PaxDb; Q8BM72; -.
DR PeptideAtlas; Q8BM72; -.
DR PRIDE; Q8BM72; -.
DR ProteomicsDB; 273191; -. [Q8BM72-1]
DR ProteomicsDB; 273192; -. [Q8BM72-2]
DR Antibodypedia; 2522; 197 antibodies from 30 providers.
DR DNASU; 110920; -.
DR Ensembl; ENSMUST00000046283; ENSMUSP00000048817; ENSMUSG00000032932. [Q8BM72-1]
DR GeneID; 110920; -.
DR KEGG; mmu:110920; -.
DR UCSC; uc007zrp.2; mouse. [Q8BM72-1]
DR UCSC; uc007zrr.2; mouse. [Q8BM72-2]
DR CTD; 6782; -.
DR MGI; MGI:1309463; Hspa13.
DR VEuPathDB; HostDB:ENSMUSG00000032932; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00890000139503; -.
DR HOGENOM; CLU_005965_0_3_1; -.
DR InParanoid; Q8BM72; -.
DR OMA; LRKTNFN; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; Q8BM72; -.
DR TreeFam; TF105047; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR BioGRID-ORCS; 110920; 10 hits in 73 CRISPR screens.
DR ChiTaRS; Hspa13; mouse.
DR PRO; PR:Q8BM72; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BM72; protein.
DR Bgee; ENSMUSG00000032932; Expressed in manus and 228 other tissues.
DR ExpressionAtlas; Q8BM72; baseline and differential.
DR Genevisible; Q8BM72; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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 CDD; cd10237; HSPA13-like_NBD; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR InterPro; IPR042048; HSPA13.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 2.
DR SUPFAM; SSF53067; SSF53067; 2.
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 Alternative splicing; ATP-binding; Endoplasmic reticulum; Microsome;
KW Nucleotide-binding; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..471
FT /note="Heat shock 70 kDa protein 13"
FT /id="PRO_0000013559"
FT REGION 317..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 195..199
FT /note="LKILR -> NSTFD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013912"
FT VAR_SEQ 200..471
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013913"
FT CONFLICT 1
FT /note="M -> V (in Ref. 1; BAE39860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 51709 MW; F60982FF20A88D55 CRC64;
MAGEMTILGS AVLTLLLAGY LAQQYLPLPT PKVIGIDLGT TYCSVGVFFP GTGKVKVIPD
ENGHISIPSM VSFTDGDVYV GYESLELADS NPQNTIYDAK RFIGKIFTPE ELEAEVGRYP
FKVLHRNGMA EFSVTSNETI IVSPEFVGSR LLLKLKEMAE EYLGMPVANA VISVPAEFDL
QQRNSTIQAA NLAGLKILRV INEPTAAAMA YGLHKVDVFY VLVIDLGGGT LDVSLLNKQG
GMFLTRAMSG NNKLGGQDFN QRLLQHLYKE IYQTYGFLPS RKEEIHRLRQ AVEMVKLNLT
IHQSAQVSVL LTVEGKDSKE PQNGDSELPK DQLTPGDGHH VNRVFRPGLS ESKSGKSQVL
FETEVSRKLF DALNEDLFQK ILVPIQQVLK EGLLDKTEID EVVLVGGSTR IPRIRQVIQE
FFGKDPNTSV DPDLAVVTGV AIQAGIDGGS WPLQVSALEI PNKHLQKTNF N
