ID HS105_HUMAN Reviewed; 858 AA. AC Q92598; B4DYH1; O95739; Q5TBM6; Q5TBM7; Q5TBM8; Q9UPC4; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 227. DE RecName: Full=Heat shock protein 105 kDa; DE AltName: Full=Antigen NY-CO-25; DE AltName: Full=Heat shock 110 kDa protein; GN Name=HSPH1; Synonyms=HSP105, HSP110, KIAA0201; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), AND SUBCELLULAR RP LOCATION. RX PubMed=9931472; DOI=10.1016/s0167-4781(98)00254-1; RA Ishihara K., Yasuda K., Hatayama T.; RT "Molecular cloning, expression and localization of human 105 kDa heat shock RT protein, hsp105."; RL Biochim. Biophys. Acta 1444:138-142(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA). RC TISSUE=Colon carcinoma; RX PubMed=9610721; RX DOI=10.1002/(sici)1097-0215(19980529)76:5<652::aid-ijc7>3.0.co;2-p; RA Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E., RA Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.; RT "Characterization of human colon cancer antigens recognized by autologous RT antibodies."; RL Int. J. Cancer 76:652-658(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA). RC TISSUE=Bone marrow; RX PubMed=9039502; DOI=10.1093/dnares/3.5.321; RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., RA Tanaka A., Kotani H., Miyajima N., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. VI. The RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of RT cDNA clones from cell line KG-1 and brain."; RL DNA Res. 3:321-329(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA). RC TISSUE=Testis; 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 [8] RP PROTEIN SEQUENCE OF 332-346 AND 375-388, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP TISSUE SPECIFICITY. 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [11] 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., Ishihara K., RA Hatayama T., Ogawa M., Nishimura Y.; RT "DNA vaccination of HSP105 leads to tumor rejection of colorectal cancer RT and melanoma in mice through activation of both CD4 T cells and CD8 T RT cells."; RL Cancer Sci. 96:695-705(2005). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557; SER-809 AND THR-815, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557 AND SER-809, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809 AND THR-815, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [21] RP FUNCTION, AND INTERACTION WITH HSPA1A AND HSPA1B. RX PubMed=24318877; DOI=10.1074/jbc.m113.521997; RA Rauch J.N., Gestwicki J.E.; RT "Binding of human nucleotide exchange factors to heat shock protein 70 RT (Hsp70) generates functionally distinct complexes in vitro."; RL J. Biol. Chem. 289:1402-1414(2014). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-561, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Acts as a nucleotide-exchange factor (NEF) for chaperone CC proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B CC thereby triggering client/substrate protein release (PubMed:24318877). CC Prevents the aggregation of denatured proteins in cells under severe CC stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 CC ATPase and chaperone activities (By similarity). CC {ECO:0000250|UniProtKB:Q60446, ECO:0000250|UniProtKB:Q61699, CC ECO:0000269|PubMed:24318877}. CC -!- SUBUNIT: Interacts with HSPA8/HSC70 (By similarity). Interacts with CC HSPA1A (via NBD) and HSPA1B (via NBD) (PubMed:24318877). CC {ECO:0000250|UniProtKB:Q61699, ECO:0000269|PubMed:24318877}. CC -!- INTERACTION: CC Q92598; Q96BE0; NbExp=3; IntAct=EBI-356829, EBI-9356686; CC Q92598; Q62392: Phlda1; Xeno; NbExp=2; IntAct=EBI-356829, EBI-309727; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9931472}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=Alpha; CC IsoId=Q92598-1; Sequence=Displayed; CC Name=Beta; CC IsoId=Q92598-2; Sequence=VSP_002428; CC Name=3; CC IsoId=Q92598-3; Sequence=VSP_035428; CC Name=4; CC IsoId=Q92598-4; Sequence=VSP_054883; CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Present at lower levels CC in most brain regions, except cerebellum. Overexpressed in cancer CC cells. {ECO:0000269|PubMed:10865058, ECO:0000269|PubMed:16232202}. CC -!- PTM: Phosphorylation on Ser-509 may be important for regulation of the CC HSPA8/HSC70 chaperone activity. {ECO:0000250|UniProtKB:Q61699}. CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC18044.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAA13192.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40891/HSPH1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB003333; BAA34779.1; -; mRNA. DR EMBL; AB003334; BAA34780.1; -; mRNA. DR EMBL; AF039695; AAC18044.1; ALT_INIT; mRNA. DR EMBL; D86956; BAA13192.2; ALT_INIT; mRNA. DR EMBL; AK302430; BAG63733.1; -; mRNA. DR EMBL; AL137142; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471075; EAX08479.1; -; Genomic_DNA. DR EMBL; CH471075; EAX08482.1; -; Genomic_DNA. DR EMBL; BC037553; AAH37553.1; -; mRNA. DR CCDS; CCDS66525.1; -. [Q92598-2] DR CCDS; CCDS66526.1; -. [Q92598-4] DR CCDS; CCDS9340.1; -. [Q92598-1] DR RefSeq; NP_001273432.1; NM_001286503.1. [Q92598-2] DR RefSeq; NP_001273433.1; NM_001286504.1. [Q92598-4] DR RefSeq; NP_001273434.1; NM_001286505.1. DR RefSeq; NP_006635.2; NM_006644.3. [Q92598-1] DR PDB; 6GFA; X-ray; 2.00 A; A=1-380. DR PDBsum; 6GFA; -. DR AlphaFoldDB; Q92598; -. DR SMR; Q92598; -. DR BioGRID; 116022; 410. DR IntAct; Q92598; 101. DR MINT; Q92598; -. DR STRING; 9606.ENSP00000487365; -. DR ChEMBL; CHEMBL3706560; -. DR DrugBank; DB12695; Phenethyl Isothiocyanate. DR GlyCosmos; Q92598; 2 sites, 1 glycan. DR GlyGen; Q92598; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q92598; -. DR MetOSite; Q92598; -. DR PhosphoSitePlus; Q92598; -. DR SwissPalm; Q92598; -. DR BioMuta; HSPH1; -. DR DMDM; 2495344; -. DR REPRODUCTION-2DPAGE; Q92598; -. DR CPTAC; CPTAC-526; -. DR CPTAC; CPTAC-527; -. DR EPD; Q92598; -. DR jPOST; Q92598; -. DR MassIVE; Q92598; -. DR MaxQB; Q92598; -. DR PaxDb; 9606-ENSP00000318687; -. DR PeptideAtlas; Q92598; -. DR ProteomicsDB; 5525; -. DR ProteomicsDB; 75344; -. [Q92598-1] DR ProteomicsDB; 75345; -. [Q92598-2] DR ProteomicsDB; 75346; -. [Q92598-3] DR Pumba; Q92598; -. DR Antibodypedia; 22778; 580 antibodies from 39 providers. DR DNASU; 10808; -. DR Ensembl; ENST00000320027.10; ENSP00000318687.5; ENSG00000120694.20. [Q92598-1] DR Ensembl; ENST00000380405.7; ENSP00000369768.4; ENSG00000120694.20. [Q92598-2] DR Ensembl; ENST00000630972.2; ENSP00000487365.1; ENSG00000120694.20. [Q92598-4] DR GeneID; 10808; -. DR KEGG; hsa:10808; -. DR MANE-Select; ENST00000320027.10; ENSP00000318687.5; NM_006644.4; NP_006635.2. DR UCSC; uc001utj.5; human. [Q92598-1] DR AGR; HGNC:16969; -. DR CTD; 10808; -. DR DisGeNET; 10808; -. DR GeneCards; HSPH1; -. DR HGNC; HGNC:16969; HSPH1. DR HPA; ENSG00000120694; Low tissue specificity. DR MIM; 610703; gene. DR neXtProt; NX_Q92598; -. DR OpenTargets; ENSG00000120694; -. DR PharmGKB; PA134869917; -. DR VEuPathDB; HostDB:ENSG00000120694; -. DR eggNOG; KOG0103; Eukaryota. DR GeneTree; ENSGT00940000159635; -. DR HOGENOM; CLU_005965_5_1_1; -. DR InParanoid; Q92598; -. DR OMA; NEFTDRC; -. DR OrthoDB; 276440at2759; -. DR PhylomeDB; Q92598; -. DR TreeFam; TF105043; -. DR PathwayCommons; Q92598; -. DR Reactome; R-HSA-3000484; Scavenging by Class F Receptors. DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response. DR SignaLink; Q92598; -. DR SIGNOR; Q92598; -. DR BioGRID-ORCS; 10808; 10 hits in 1162 CRISPR screens. DR ChiTaRS; HSPH1; human. DR GeneWiki; HSPH1; -. DR GenomeRNAi; 10808; -. DR Pharos; Q92598; Tbio. DR PRO; PR:Q92598; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q92598; Protein. DR Bgee; ENSG00000120694; Expressed in primordial germ cell in gonad and 202 other cell types or tissues. DR ExpressionAtlas; Q92598; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:BHF-UCL. DR GO; GO:0005874; C:microtubule; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:UniProtKB. DR GO; GO:0043014; F:alpha-tubulin binding; IEA:Ensembl. 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:0051085; P:chaperone cofactor-dependent protein refolding; IEA:Ensembl. 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:0006457; P:protein folding; IBA:GO_Central. DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc. DR CDD; cd11739; HSPH1_NBD; 1. DR Gene3D; 1.20.1270.10; -; 2. DR Gene3D; 3.30.30.30; -; 1. DR Gene3D; 3.30.420.40; -; 2. 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; IPR042053; HSPH1_NBD. DR PANTHER; PTHR45639:SF2; HEAT SHOCK PROTEIN 105 KDA; 1. DR PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 2. DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1. DR PROSITE; PS01036; HSP70_3; 1. DR Genevisible; Q92598; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm; KW Direct protein sequencing; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Stress response. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..858 FT /note="Heat shock protein 105 kDa" FT /id="PRO_0000078284" FT REGION 500..584 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 796..858 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 523..561 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 564..584 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 807..834 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22223895" FT MOD_RES 471 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q61699" FT MOD_RES 509 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61699" FT MOD_RES 510 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61699" FT MOD_RES 557 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 561 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 809 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 815 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..36 FT /note="MSVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTP -> MATAAVLRGPAA FT HWVESFQKAREEGSGSGTWRGRWRRR (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054883" FT VAR_SEQ 104..144 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_035428" FT VAR_SEQ 529..572 FT /note="Missing (in isoform Beta)" FT /evidence="ECO:0000303|PubMed:9931472" FT /id="VSP_002428" FT STRAND 4..8 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 10..18 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 20..25 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 35..41 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 46..49 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 50..54 FT /evidence="ECO:0007829|PDB:6GFA" FT TURN 55..59 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 60..62 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 63..66 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 68..70 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 78..84 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 88..93 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 97..104 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 106..113 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 114..133 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 139..144 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 150..163 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 166..172 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 173..184 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 196..203 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 208..216 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 219..228 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 233..252 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 256..258 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 260..276 FT /evidence="ECO:0007829|PDB:6GFA" FT TURN 277..279 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 284..292 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 295..301 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 303..309 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 311..316 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 318..328 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 332..334 FT /evidence="ECO:0007829|PDB:6GFA" FT STRAND 337..343 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 344..346 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 348..358 FT /evidence="ECO:0007829|PDB:6GFA" FT TURN 368..370 FT /evidence="ECO:0007829|PDB:6GFA" FT HELIX 371..379 FT /evidence="ECO:0007829|PDB:6GFA" SQ SEQUENCE 858 AA; 96865 MW; D0E757970E340B56 CRC64; MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGSKNRTIGV AAKNQQITHA NNTVSNFKRF HGRAFNDPFI QKEKENLSYD LVPLKNGGVG IKVMYMGEEH LFSVEQITAM LLTKLKETAE NSLKKPVTDC VISVPSFFTD AERRSVLDAA QIVGLNCLRL MNDMTAVALN YGIYKQDLPS LDEKPRIVVF VDMGHSAFQV SACAFNKGKL KVLGTAFDPF LGGKNFDEKL VEHFCAEFKT KYKLDAKSKI RALLRLYQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSGK MNRSQFEELC AELLQKIEVP LYSLLEQTHL KVEDVSAVEI VGGATRIPAV KERIAKFFGK DISTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF PISLIWNHDS EDTEGVHEVF SRNHAAPFSK VLTFLRRGPF ELEAFYSDPQ GVPYPEAKIG RFVVQNVSAQ KDGEKSRVKV KVRVNTHGIF TISTASMVEK VPTEENEMSS EADMECLNQR PPENPDTDKN VQQDNSEAGT QPQVQTDAQQ TSQSPPSPEL TSEENKIPDA DKANEKKVDQ PPEAKKPKIK VVNVELPIEA NLVWQLGKDL LNMYIETEGK MIMQDKLEKE RNDAKNAVEE YVYEFRDKLC GPYEKFICEQ DHQNFLRLLT ETEDWLYEEG EDQAKQAYVD KLEELMKIGT PVKVRFQEAE ERPKMFEELG QRLQHYAKIA ADFRNKDEKY NHIDESEMKK VEKSVNEVME WMNNVMNAQA KKSLDQDPVV RAQEIKTKIK ELNNTCEPVV TQPKPKIESP KLERTPNGPN IDKKEEDLED KNNFGAEPPH QNGECYPNEK NSVNMDLD //