MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Heat shock protein 105 kDa; AltName: Full=42 degrees C-HSP; AltName: Full=Heat shock 110 kDa protein; AltName: Full=Heat shock-related 100 kDa protein E7I; Short=HSP-E7I; |
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| MyHits synonyms | HS105_MOUSE , Q61699 , Q3TNS2 , Q3UIY8 , Q62578 , Q62579 , Q6A0A5 , Q8C430 , Q8VCW6 , 0576A4C2C4715032 |
 Legends: 1, INIT_MET Removed. {ECO:0000250|UniProtKB:Q92598}; 2, N-acetylserine. {ECO:0000250|UniProtKB:Q92598}; 3, N6-acetyllysine. {ECO:0000244|PubMed:23806337}; 4, Phosphoserine. {ECO:0000244|PubMed:21183079, ECO:0000269|PubMed:12558502}; 5, Phosphoserine. {ECO:0000244|PubMed:21183079}; 6, Phosphoserine. {ECO:0000244|PubMed:15345747}; 7, Phosphothreonine. {ECO:0000250|UniProtKB:Q92598}; 8, Phosphoserine. {ECO:0000244|PubMed:19131326, ECO:0000244|PubMed:19144319}; 9, CONFLICT S -> L (in Ref. 4; BAC38797). {ECO:0000305}; 10, CONFLICT D -> N (in Ref. 4; BAC38797). {ECO:0000305}; 11, CONFLICT S -> R (in Ref. 4; BAC38797). {ECO:0000305}; 12, CONFLICT E -> D (in Ref. 4; BAC38797). {ECO:0000305}; 13, CONFLICT A -> R (in Ref. 1; AAA99485 and 2; BAA11036). {ECO:0000305}; 14, CONFLICT C -> S (in Ref. 4; BAE38016). {ECO:0000305}; 15, CONFLICT P -> L (in Ref. 2; BAA11036). {ECO:0000305}; 16, CONFLICT A -> R (in Ref. 1; AAA99485). {ECO:0000305}; 17, CONFLICT P -> FQ (in Ref. 1; AAA99485). {ECO:0000305}; 18, CONFLICT I -> R (in Ref. 4; BAE27367). {ECO:0000305}; 19, CONFLICT I -> N (in Ref. 1; AAA99485). {ECO:0000305}; 20, VAR_SEQ Missing (in isoform HSP105-beta). {ECO:0000303|PubMed:8530361}; 21, CONFLICT DV -> EL (in Ref. 1; AAA99485). {ECO:0000305}; 22, CONFLICT AVAR -> VGEG (in Ref. 4; BAC38797). {ECO:0000305}; 23, CONFLICT NE -> KD (in Ref. 4; BAC38797). {ECO:0000305}; 24, ipat:HSP70_3 [T].
| |
ID HS105_MOUSE Reviewed; 858 AA.
AC Q61699; Q3TNS2; Q3UIY8; Q62578; Q62579; Q6A0A5; Q8C430; Q8VCW6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 02-NOV-2016, entry version 160.
DE RecName: Full=Heat shock protein 105 kDa;
DE AltName: Full=42 degrees C-HSP;
DE AltName: Full=Heat shock 110 kDa protein;
DE AltName: Full=Heat shock-related 100 kDa protein E7I;
DE Short=HSP-E7I;
GN Name=Hsph1; Synonyms=Hsp105, Hsp110, Kiaa0201;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HSP105-ALPHA).
RX PubMed=7556594; DOI=10.1016/0014-5793(95)00884-C;
RA Morozov A., Subjeck J., Raychaudhuri P.;
RT "HPV16 E7 oncoprotein induces expression of a 110 kDa heat shock
RT protein.";
RL FEBS Lett. 371:214-218(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HSP105-ALPHA AND HSP105-BETA).
RX PubMed=8530361; DOI=10.1074/jbc.270.50.29718;
RA Yasuda K., Nakai A., Hatayama T., Nagata K.;
RT "Cloning and expression of murine high molecular mass heat shock
RT proteins, HSP105.";
RL J. Biol. Chem. 270:29718-29723(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
RP HSP105-ALPHA).
RC STRAIN=BALB/cJ;
RX PubMed=10066425; DOI=10.1006/bbrc.1999.0283;
RA Yasuda K., Ishihara K., Nakashima K., Hatayama T.;
RT "Genomic cloning and promoter analysis of the mouse 105-kDa heat shock
RT protein (HSP105) gene.";
RL Biochem. Biophys. Res. Commun. 256:75-80(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HSP105-ALPHA).
RC STRAIN=C57BL/6J; TISSUE=Eye, Hippocampus, and Liver;
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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HSP105-ALPHA).
RC STRAIN=NMRI; TISSUE=Mammary gland;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 54-68; 74-82; 361-374 AND 462-471, AND
RP 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-858.
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT cDNAs identified by screening of terminal sequences of cDNA clones
RT randomly sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [8]
RP INTERACTION WITH HSPA8.
RX PubMed=9675148; DOI=10.1006/bbrc.1998.8979;
RA Hatayama T., Yasuda K., Yasuda K.;
RT "Association of HSP105 with HSC70 in high molecular mass complexes in
RT mouse FM3A cells.";
RL Biochem. Biophys. Res. Commun. 248:395-401(1998).
RN [9]
RP PHOSPHORYLATION.
RX PubMed=10772927; DOI=10.1006/bbrc.2000.2541;
RA Ishihara K., Yasuda K., Hatayama T.;
RT "Phosphorylation of the 105-kDa heat shock proteins, HSP105alpha and
RT HSP105beta, by casein kinase II.";
RL Biochem. Biophys. Res. Commun. 270:927-931(2000).
RN [10]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=10865058; DOI=10.1016/S0006-8993(00)02346-5;
RA Hylander B.L., Chen X., Graf P.C.F., Subjeck J.R.;
RT "The distribution and localization of hsp110 in brain.";
RL Brain Res. 869:49-55(2000).
RN [11]
RP PHOSPHORYLATION AT SER-509.
RX PubMed=12558502; DOI=10.1042/BJ20021331;
RA Ishihara K., Yamagishi N., Hatayama T.;
RT "Protein kinase CK2 phosphorylates Hsp105 alpha at Ser509 and
RT modulates its function.";
RL Biochem. J. 371:917-925(2003).
RN [12]
RP FUNCTION.
RX PubMed=14644449; DOI=10.1016/S0014-5793(03)01292-4;
RA Yamagishi N., Ishihara K., Saito Y., Hatayama T.;
RT "Hsp105 but not Hsp70 family proteins suppress the aggregation of
RT heat-denatured protein in the presence of ADP.";
RL FEBS Lett. 555:390-396(2003).
RN [13]
RP INTERACTION WITH HSPA8, AND FUNCTION.
RX PubMed=15292236; DOI=10.1074/jbc.M407947200;
RA Yamagishi N., Ishihara K., Hatayama T.;
RT "Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70
RT ATPase activity.";
RL J. Biol. Chem. 279:41727-41733(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
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 [15]
RP TISSUE SPECIFICITY.
RX PubMed=16232202; DOI=10.1111/j.1349-7006.2005.00093.x;
RA Miyazaki M., Nakatsura T., Yokomine K., Senju S., Monji M., Hosaka S.,
RA Komori H., Yoshitake Y., Motomura Y., Minohara M., Kubo T.,
RA Ishihara K., Hatayama T., Ogawa M., Nishimura Y.;
RT "DNA vaccination of HSP105 leads to tumor rejection of colorectal
RT cancer and melanoma in mice through activation of both CD4 T cells and
RT CD8 T cells.";
RL Cancer Sci. 96:695-705(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, AND IDENTIFICATION
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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
RT electron capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509 AND SER-510, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC Pancreas, 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
RT expression.";
RL Cell 143:1174-1189(2010).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-471, AND IDENTIFICATION BY
RP MASS 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.,
RA Zhang Y., 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 -!- FUNCTION: Prevents the aggregation of denatured proteins in cells
CC under severe stress, on which the ATP levels decrease markedly.
CC Inhibits HSPA8/HSC70 ATPase and chaperone activities.
CC {ECO:0000269|PubMed:14644449, ECO:0000269|PubMed:15292236}.
CC -!- SUBUNIT: Interacts with HSPA8/HSC70. {ECO:0000269|PubMed:15292236,
CC ECO:0000269|PubMed:9675148}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10865058}.
CC Nucleus {ECO:0000269|PubMed:10865058}. Note=Strictly cytoplasmic
CC in neurons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=HSP105-alpha;
CC IsoId=Q61699-1; Sequence=Displayed;
CC Name=HSP105-beta;
CC IsoId=Q61699-2; Sequence=VSP_002429;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Present at lower
CC levels in most brain regions, except cerebellum. Within the brain,
CC expression is restricted to neurons (at protein level).
CC Overexpressed in cancer cells. {ECO:0000269|PubMed:10865058,
CC ECO:0000269|PubMed:16232202}.
CC -!- INDUCTION: By heat shock. Hsp105-alpha also induced by other
CC stresses.
CC -!- PTM: Phosphorylation on Ser-509 may be important for regulation of
CC the HSPA8/HSC70 chaperone activity. {ECO:0000269|PubMed:10772927,
CC ECO:0000269|PubMed:12558502}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000305}.
DR EMBL; L40406; AAA99485.1; -; mRNA.
DR EMBL; D67016; BAA11035.1; -; mRNA.
DR EMBL; D67017; BAA11036.1; -; mRNA.
DR EMBL; AB005282; BAA74540.1; -; Genomic_DNA.
DR EMBL; AK083179; BAC38797.1; -; mRNA.
DR EMBL; AK146697; BAE27367.1; -; mRNA.
DR EMBL; AK165046; BAE38016.1; -; mRNA.
DR EMBL; BC018378; AAH18378.1; -; mRNA.
DR EMBL; AK172913; BAD32191.1; -; mRNA.
DR CCDS; CCDS19885.1; -. [Q61699-1]
DR PIR; S66666; S66666.
DR RefSeq; NP_038587.2; NM_013559.2. [Q61699-1]
DR RefSeq; XP_006504977.1; XM_006504914.2. [Q61699-2]
DR UniGene; Mm.270681; -.
DR ProteinModelPortal; Q61699; -.
DR SMR; Q61699; -.
DR BioGrid; 200448; 22.
DR DIP; DIP-32354N; -.
DR IntAct; Q61699; 24.
DR MINT; MINT-4097981; -.
DR STRING; 10090.ENSMUSP00000074392; -.
DR iPTMnet; Q61699; -.
DR PhosphoSitePlus; Q61699; -.
DR SwissPalm; Q61699; -.
DR EPD; Q61699; -.
DR PaxDb; Q61699; -.
DR PeptideAtlas; Q61699; -.
DR PRIDE; Q61699; -.
DR Ensembl; ENSMUST00000074846; ENSMUSP00000074392; ENSMUSG00000029657. [Q61699-2]
DR Ensembl; ENSMUST00000201452; ENSMUSP00000144654; ENSMUSG00000029657. [Q61699-1]
DR Ensembl; ENSMUST00000202361; ENSMUSP00000144413; ENSMUSG00000029657. [Q61699-1]
DR GeneID; 15505; -.
DR KEGG; mmu:15505; -.
DR UCSC; uc009apy.1; mouse. [Q61699-1]
DR UCSC; uc009apz.1; mouse. [Q61699-2]
DR CTD; 10808; -.
DR MGI; MGI:105053; Hsph1.
DR eggNOG; KOG0103; Eukaryota.
DR eggNOG; COG0443; LUCA.
DR GeneTree; ENSGT00390000016919; -.
DR HOVERGEN; HBG047955; -.
DR InParanoid; Q61699; -.
DR KO; K09485; -.
DR OMA; VVRTHEI; -.
DR OrthoDB; EOG091G04Y6; -.
DR PhylomeDB; Q61699; -.
DR TreeFam; TF105043; -.
DR Reactome; R-MMU-3000484; Scavenging by Class F Receptors.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR PRO; PR:Q61699; -.
DR Proteomes; UP000000589; Chromosome 5.
DR Bgee; ENSMUSG00000029657; -.
DR CleanEx; MM_HSPH1; -.
DR ExpressionAtlas; Q61699; baseline and differential.
DR Genevisible; Q61699; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IDA:MGI.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI.
DR GO; GO:1903748; P:negative regulation of establishment of protein localization to mitochondrion; IMP:MGI.
DR GO; GO:1903751; P:negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; TAS:BHF-UCL.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; IGI:MGI.
DR GO; GO:0045345; P:positive regulation of MHC class I biosynthetic process; TAS:BHF-UCL.
DR GO; GO:0051135; P:positive regulation of NK T cell activation; TAS:BHF-UCL.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; NAS:BHF-UCL.
DR GO; GO:0006986; P:response to unfolded protein; TAS:BHF-UCL.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 2.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C.
DR InterPro; IPR029047; HSP70_peptide-bd.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF100920; SSF100920; 2.
DR SUPFAM; SSF100934; SSF100934; 2.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Stress response.
FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q92598}.
FT CHAIN 2 858 Heat shock protein 105 kDa.
FT /FTId=PRO_0000078285.
FT MOD_RES 2 2 N-acetylserine.
FT {ECO:0000250|UniProtKB:Q92598}.
FT MOD_RES 471 471 N6-acetyllysine.
FT {ECO:0000244|PubMed:23806337}.
FT MOD_RES 509 509 Phosphoserine.
FT {ECO:0000244|PubMed:21183079,
FT ECO:0000269|PubMed:12558502}.
FT MOD_RES 510 510 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 558 558 Phosphoserine.
FT {ECO:0000244|PubMed:15345747}.
FT MOD_RES 562 562 Phosphothreonine.
FT {ECO:0000250|UniProtKB:Q92598}.
FT MOD_RES 810 810 Phosphoserine.
FT {ECO:0000244|PubMed:19131326,
FT ECO:0000244|PubMed:19144319}.
FT MOD_RES 816 816 Phosphothreonine.
FT {ECO:0000250|UniProtKB:Q92598}.
FT VAR_SEQ 530 573 Missing (in isoform HSP105-beta).
FT {ECO:0000303|PubMed:8530361}.
FT /FTId=VSP_002429.
FT CONFLICT 2 2 S -> L (in Ref. 4; BAC38797).
FT {ECO:0000305}.
FT CONFLICT 7 8 DV -> EL (in Ref. 1; AAA99485).
FT {ECO:0000305}.
FT CONFLICT 7 7 D -> N (in Ref. 4; BAC38797).
FT {ECO:0000305}.
FT CONFLICT 12 12 S -> R (in Ref. 4; BAC38797).
FT {ECO:0000305}.
FT CONFLICT 16 19 AVAR -> VGEG (in Ref. 4; BAC38797).
FT {ECO:0000305}.
FT CONFLICT 24 24 E -> D (in Ref. 4; BAC38797).
FT {ECO:0000305}.
FT CONFLICT 28 29 NE -> KD (in Ref. 4; BAC38797).
FT {ECO:0000305}.
FT CONFLICT 159 159 A -> R (in Ref. 1; AAA99485 and 2;
FT BAA11036). {ECO:0000305}.
FT CONFLICT 310 310 C -> S (in Ref. 4; BAE38016).
FT {ECO:0000305}.
FT CONFLICT 320 320 P -> L (in Ref. 2; BAA11036).
FT {ECO:0000305}.
FT CONFLICT 373 373 A -> R (in Ref. 1; AAA99485).
FT {ECO:0000305}.
FT CONFLICT 518 518 P -> FQ (in Ref. 1; AAA99485).
FT {ECO:0000305}.
FT CONFLICT 658 658 I -> R (in Ref. 4; BAE27367).
FT {ECO:0000305}.
FT CONFLICT 744 744 I -> N (in Ref. 1; AAA99485).
FT {ECO:0000305}.
FT CONFLICT 838 838 A -> R (in Ref. 1; AAA99485).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 3 705 ipfam:HSP70 [T]
FT MYHIT 338 352 ipat:HSP70_3 [T]
SQ SEQUENCE 858 AA; 96407 MW; 0576A4C2C4715032 CRC64;
MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGSKNRTIGV AAKNQQITHA
NNTVSSFKRF HGRAFNDPFI QKEKENLSYD LVPMKNGGVG IKVMYMDEEH FFSVEQITAM
LLTKLKETAE NNLKKPVTDC VISVPSFFTD AERRSVLDAA QIVGLNCLRL MNDMTAVALN
YGIYKQDLPN AEEKPRVVVF VDMGHSSFQV SACAFNKGKL KVLGTAFDPF LGGKNFDEKL
VEHFCAEFKT KYKLDAKSKI RALLRLHQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSGK
MNRSQFEELC AELLQKIEVP LHSLMAQTQL KAEDVSAIEI VGGATRIPAV KERIAKFFGK
DVSTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF PISLVWNHDS EETEGVHEVF
SRNHAAPFSK VLTFLRRGPF ELEAFYSDPQ GVPYPEAKIG RFVVQNVSAQ KDGEKSRVKV
KVRVNTHGIF TISTASMVEK VPTEEEDGSS LEADMECPNQ RPTESSDVDK NIQQDNSEAG
TQPQVQTDGQ QTSQSPPSPE LTSEESKTPD ADKANEKKVD QPPEAKKPKI KVVNVELPVE
ANLVWQLGRD LLNMYIETEG KMIMQDKLEK ERNDAKNAVE ECVYEFRDKL CGPYEKFICE
QEHEKFLRLL TETEDWLYEE GEDQAKQAYI DKLEELMKMG TPVKVRFQEA EERPKVLEEL
GQRLQHYAKI AADFRGKDEK YNHIDESEMK KVEKSVNEVM EWMNNVMNAQ AKRSLDQDPV
VRTHEIRAKV KELNNVCEPV VTQPKPKIES PKLERTPNGP NIDKKEDLEG KNNLGAEAPH
QNGECHPNEK GSVNMDLD
//
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