HS105_HUMAN
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 03-AUG-2022, entry version 218.
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="http://atlasgeneticsoncology.org/Genes/HSPH1ID40891ch13q12.html";
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; 232.
DR IntAct; Q92598; 86.
DR MINT; Q92598; -.
DR STRING; 9606.ENSP00000318687; -.
DR ChEMBL; CHEMBL3706560; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR GlyGen; Q92598; 2 sites, 1 O-linked glycan (2 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; Q92598; -.
DR PeptideAtlas; Q92598; -.
DR PRIDE; Q92598; -.
DR ProteomicsDB; 5525; -.
DR ProteomicsDB; 75344; -. [Q92598-1]
DR ProteomicsDB; 75345; -. [Q92598-2]
DR ProteomicsDB; 75346; -. [Q92598-3]
DR Antibodypedia; 22778; 534 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 CTD; 10808; -.
DR DisGeNET; 10808; -.
DR GeneCards; HSPH1; -.
DR HGNC; HGNC:16969; HSPH1.
DR HPA; ENSG00000120694; Group enriched (brain, choroid plexus).
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; NMLSHAY; -.
DR OrthoDB; 406172at2759; -.
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; 8 hits in 1084 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 bronchial epithelial cell and 200 other tissues.
DR ExpressionAtlas; Q92598; baseline and differential.
DR Genevisible; Q92598; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
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; 2.60.34.10; -; 1.
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 Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 2.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01036; HSP70_3; 1.
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
