Full text data of HSPH1
HSPH1
(HSP105, HSP110, KIAA0201)
[Confidence: low (only semi-automatic identification from reviews)]
Heat shock protein 105 kDa (Antigen NY-CO-25; Heat shock 110 kDa protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Heat shock protein 105 kDa (Antigen NY-CO-25; Heat shock 110 kDa protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q92598
ID HS105_HUMAN Reviewed; 858 AA.
AC Q92598; O95739; Q5TBM6; Q5TBM7; Q5TBM8; Q9UPC4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1997, sequence version 1.
DT 22-JAN-2014, entry version 146.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT shock 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
RT autologous 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.
RT The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
RT analysis of cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [4]
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.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA 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.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA 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.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 332-346 AND 375-388, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
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 [12]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND MASS
RP SPECTROMETRY.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557; SER-809 AND
RP THR-815, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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.,
RA Buerckstuemmer T., 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557 AND SER-809, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
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 (By
CC similarity).
CC -!- SUBUNIT: Interacts with HSPA8/HSC70 (By similarity).
CC -!- INTERACTION:
CC Q62392:Phlda1 (xeno); NbExp=2; IntAct=EBI-356829, EBI-309727;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Present at lower
CC levels in most brain regions, except cerebellum. Overexpressed in
CC cancer cells.
CC -!- PTM: Phosphorylation on Ser-509 may be important for regulation of
CC the HSPA8/HSC70 chaperone activity (By similarity).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18044.1; Type=Erroneous initiation;
CC Sequence=BAA13192.2; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/HSPH1ID40891ch13q12.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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; AL137142; CAI12428.1; -; Genomic_DNA.
DR EMBL; AL137142; CAI12429.1; -; Genomic_DNA.
DR EMBL; AL137142; CAI12430.1; -; Genomic_DNA.
DR EMBL; CH471075; EAX08482.1; -; Genomic_DNA.
DR EMBL; BC037553; AAH37553.1; -; mRNA.
DR RefSeq; NP_001273432.1; NM_001286503.1.
DR RefSeq; NP_001273433.1; NM_001286504.1.
DR RefSeq; NP_001273434.1; NM_001286505.1.
DR RefSeq; NP_006635.2; NM_006644.3.
DR UniGene; Hs.743267; -.
DR ProteinModelPortal; Q92598; -.
DR SMR; Q92598; 5-714.
DR IntAct; Q92598; 19.
DR MINT; MINT-1374987; -.
DR STRING; 9606.ENSP00000318687; -.
DR PhosphoSite; Q92598; -.
DR DMDM; 2495344; -.
DR REPRODUCTION-2DPAGE; Q92598; -.
DR PaxDb; Q92598; -.
DR PRIDE; Q92598; -.
DR DNASU; 10808; -.
DR Ensembl; ENST00000320027; ENSP00000318687; ENSG00000120694.
DR Ensembl; ENST00000380405; ENSP00000369768; ENSG00000120694.
DR Ensembl; ENST00000380406; ENSP00000369769; ENSG00000120694.
DR GeneID; 10808; -.
DR KEGG; hsa:10808; -.
DR UCSC; uc001utj.3; human.
DR CTD; 10808; -.
DR GeneCards; GC13M031710; -.
DR HGNC; HGNC:16969; HSPH1.
DR HPA; CAB002060; -.
DR HPA; HPA028675; -.
DR MIM; 610703; gene.
DR neXtProt; NX_Q92598; -.
DR PharmGKB; PA134869917; -.
DR eggNOG; COG0443; -.
DR HOGENOM; HOG000228138; -.
DR HOVERGEN; HBG047955; -.
DR InParanoid; Q92598; -.
DR KO; K09485; -.
DR OrthoDB; EOG77M8N0; -.
DR PhylomeDB; Q92598; -.
DR Reactome; REACT_160300; Binding and Uptake of Ligands by Scavenger Receptors.
DR ChiTaRS; HSPH1; human.
DR GeneWiki; HSPH1; -.
DR GenomeRNAi; 10808; -.
DR NextBio; 41059; -.
DR PMAP-CutDB; Q92598; -.
DR PRO; PR:Q92598; -.
DR ArrayExpress; Q92598; -.
DR Bgee; Q92598; -.
DR CleanEx; HS_HSPH1; -.
DR Genevestigator; Q92598; -.
DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:BHF-UCL.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; 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:0006986; P:response to unfolded protein; TAS:ProtInc.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR PROSITE; PS00297; HSP70_1; FALSE_NEG.
DR PROSITE; PS00329; HSP70_2; FALSE_NEG.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1 858 Heat shock protein 105 kDa.
FT /FTId=PRO_0000078284.
FT MOD_RES 509 509 Phosphoserine (By similarity).
FT MOD_RES 557 557 Phosphoserine.
FT MOD_RES 809 809 Phosphoserine.
FT MOD_RES 815 815 Phosphothreonine.
FT VAR_SEQ 104 144 Missing (in isoform 3).
FT /FTId=VSP_035428.
FT VAR_SEQ 529 572 Missing (in isoform Beta).
FT /FTId=VSP_002428.
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
//
ID HS105_HUMAN Reviewed; 858 AA.
AC Q92598; O95739; Q5TBM6; Q5TBM7; Q5TBM8; Q9UPC4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1997, sequence version 1.
DT 22-JAN-2014, entry version 146.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT shock 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
RT autologous 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.
RT The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
RT analysis of cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [4]
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.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA 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.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA 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.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 332-346 AND 375-388, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
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 [12]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND MASS
RP SPECTROMETRY.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557; SER-809 AND
RP THR-815, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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.,
RA Buerckstuemmer T., 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557 AND SER-809, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
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 (By
CC similarity).
CC -!- SUBUNIT: Interacts with HSPA8/HSC70 (By similarity).
CC -!- INTERACTION:
CC Q62392:Phlda1 (xeno); NbExp=2; IntAct=EBI-356829, EBI-309727;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Present at lower
CC levels in most brain regions, except cerebellum. Overexpressed in
CC cancer cells.
CC -!- PTM: Phosphorylation on Ser-509 may be important for regulation of
CC the HSPA8/HSC70 chaperone activity (By similarity).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18044.1; Type=Erroneous initiation;
CC Sequence=BAA13192.2; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/HSPH1ID40891ch13q12.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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; AL137142; CAI12428.1; -; Genomic_DNA.
DR EMBL; AL137142; CAI12429.1; -; Genomic_DNA.
DR EMBL; AL137142; CAI12430.1; -; Genomic_DNA.
DR EMBL; CH471075; EAX08482.1; -; Genomic_DNA.
DR EMBL; BC037553; AAH37553.1; -; mRNA.
DR RefSeq; NP_001273432.1; NM_001286503.1.
DR RefSeq; NP_001273433.1; NM_001286504.1.
DR RefSeq; NP_001273434.1; NM_001286505.1.
DR RefSeq; NP_006635.2; NM_006644.3.
DR UniGene; Hs.743267; -.
DR ProteinModelPortal; Q92598; -.
DR SMR; Q92598; 5-714.
DR IntAct; Q92598; 19.
DR MINT; MINT-1374987; -.
DR STRING; 9606.ENSP00000318687; -.
DR PhosphoSite; Q92598; -.
DR DMDM; 2495344; -.
DR REPRODUCTION-2DPAGE; Q92598; -.
DR PaxDb; Q92598; -.
DR PRIDE; Q92598; -.
DR DNASU; 10808; -.
DR Ensembl; ENST00000320027; ENSP00000318687; ENSG00000120694.
DR Ensembl; ENST00000380405; ENSP00000369768; ENSG00000120694.
DR Ensembl; ENST00000380406; ENSP00000369769; ENSG00000120694.
DR GeneID; 10808; -.
DR KEGG; hsa:10808; -.
DR UCSC; uc001utj.3; human.
DR CTD; 10808; -.
DR GeneCards; GC13M031710; -.
DR HGNC; HGNC:16969; HSPH1.
DR HPA; CAB002060; -.
DR HPA; HPA028675; -.
DR MIM; 610703; gene.
DR neXtProt; NX_Q92598; -.
DR PharmGKB; PA134869917; -.
DR eggNOG; COG0443; -.
DR HOGENOM; HOG000228138; -.
DR HOVERGEN; HBG047955; -.
DR InParanoid; Q92598; -.
DR KO; K09485; -.
DR OrthoDB; EOG77M8N0; -.
DR PhylomeDB; Q92598; -.
DR Reactome; REACT_160300; Binding and Uptake of Ligands by Scavenger Receptors.
DR ChiTaRS; HSPH1; human.
DR GeneWiki; HSPH1; -.
DR GenomeRNAi; 10808; -.
DR NextBio; 41059; -.
DR PMAP-CutDB; Q92598; -.
DR PRO; PR:Q92598; -.
DR ArrayExpress; Q92598; -.
DR Bgee; Q92598; -.
DR CleanEx; HS_HSPH1; -.
DR Genevestigator; Q92598; -.
DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:BHF-UCL.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; 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:0006986; P:response to unfolded protein; TAS:ProtInc.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR PROSITE; PS00297; HSP70_1; FALSE_NEG.
DR PROSITE; PS00329; HSP70_2; FALSE_NEG.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1 858 Heat shock protein 105 kDa.
FT /FTId=PRO_0000078284.
FT MOD_RES 509 509 Phosphoserine (By similarity).
FT MOD_RES 557 557 Phosphoserine.
FT MOD_RES 809 809 Phosphoserine.
FT MOD_RES 815 815 Phosphothreonine.
FT VAR_SEQ 104 144 Missing (in isoform 3).
FT /FTId=VSP_035428.
FT VAR_SEQ 529 572 Missing (in isoform Beta).
FT /FTId=VSP_002428.
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
//
MIM
610703
*RECORD*
*FIELD* NO
610703
*FIELD* TI
*610703 HEAT-SHOCK 105/110-KD PROTEIN 1; HSPH1
;;HEAT-SHOCK PROTEIN, 105-KD; HSP105;;
read moreHEAT-SHOCK PROTEIN, 110-KD; HSP110;;
KIAA0201
*FIELD* TX
CLONING
By sequencing clones obtained from an immature myeloid leukemia cell
line cDNA library, Nagase et al. (1996) cloned HSPH1, which they
designated KIAA0201. The deduced 858-amino acid protein contains an
HSP70 (see HSPA1A; 140550)-like motif and shares 93.4% identity with
mouse Hsph1-alpha. Northern blot analysis detected highest expression in
brain, lung, and testis. Expression was lower in heart, skeletal muscle,
kidney, pancreas, spleen, ovary, small intestine, colon, and peripheral
blood leukocytes, and weak in liver. No expression was detected in
thymus and prostate.
Using mouse Hsph1 to screen a cDNA library derived from heat-shocked
HeLa cells, Ishihara et al. (1999) cloned 2 splice variants of HSPH1,
which they called HSP105-alpha and HSP105-beta. The HSP105-alpha and
HSP105-beta proteins contain 858 and 814 amino acids, respectively, and
both have an N-terminal ATP-binding domain. Northern blot analysis
detected a 4-kb HSP105 transcript in HeLa cells. Immunohistochemical
analysis localized HSP105 mainly in the cytoplasm. Database analysis
indicated that both HSP105 isoforms are highly conserved during
evolution.
GENE FUNCTION
Using Northern blot analysis, Ishihara et al. (1999) found that both
HSP105-alpha and HSP105-beta were upregulated in HeLa cells exposed to
heat shock. HSP105-alpha, but not HSP105-beta, was also upregulated in
response to other cell stresses. Following heat shock, HSP105
relocalized from a cytoplasmic to perinuclear position.
MOLECULAR GENETICS
Dorard et al. (2011) identified a mutant of HSP110, which they called
HSP110-delta-E9, in colorectal cancer (114500) showing microsatellite
instability (MSI CRC), generated from an aberrantly spliced mRNA and
lacking the HSP110 substrate-binding domain. This mutant was expressed
at variable levels in almost all MSI CRC cell lines and primary tumors
tested. HSP110-delta-E9 impaired both the normal cellular localization
of HSP110 and its interaction with other HSPs, thus abrogating the
chaperone activity and antiapoptotic function of HSP110 in a
dominant-negative manner. HSP110-delta-E9 overexpression caused the
sensitization of cells to anticancer agents such as oxaliplatin and
5-fluorouracil, which are routinely prescribed in the adjuvant treatment
of people with colorectal cancer. The survival and response to
chemotherapy of subjects with colorectal cancer showing microsatellite
instability was associated with the tumor expression level of
HSP110-delta-E9. Dorard et al. (2011) concluded that HSP110 may thus
constitute a major determinant for both prognosis and treatment response
in colorectal cancer.
MAPPING
By analysis of radiation hybrids and human/rodent hybrid cell lines,
Nagase et al. (1996) mapped the HSPH1 gene to chromosome 13.
*FIELD* RF
1. Dorard, C.; de Thonel, A.; Collura, A.; Marisa, L.; Svrcek, M.;
Lagrange, A.; Jego, G.; Wanherdrick, K.; Joly, A. L.; Buhard, O.;
Gobbo, J.; Penard-Lacronique, V.; and 16 others: Expression of
a mutant HSP110 sensitizes colorectal cancer cells to chemotherapy
and improves disease prognosis. Nature Med. 17: 1283-1289, 2011.
2. Ishihara, K.; Yasuda, K.; Hatayama, T.: Molecular cloning, expression
and localization of human 105 kDa heat shock protein, hsp105. Biochim.
Biophys. Acta 1444: 138-142, 1999.
3. Nagase, T.; Seki, N.; Ishikawa, K.; Ohira, M.; Kawarabayasi, Y.;
Ohara, O.; Tanaka, A.; Kotani, H.; Miyajima, N.; Nomura, N.: Prediction
of the coding sequences of unidentified human genes. VI. The coding
sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis
of cDNA clones from cell line KG-1 and brain. DNA Res. 3: 321-329,
1996.
*FIELD* CN
Ada Hamosh - updated: 12/12/2011
*FIELD* CD
Patricia A. Hartz: 1/16/2007
*FIELD* ED
alopez: 12/19/2011
terry: 12/12/2011
mgross: 1/16/2007
*RECORD*
*FIELD* NO
610703
*FIELD* TI
*610703 HEAT-SHOCK 105/110-KD PROTEIN 1; HSPH1
;;HEAT-SHOCK PROTEIN, 105-KD; HSP105;;
read moreHEAT-SHOCK PROTEIN, 110-KD; HSP110;;
KIAA0201
*FIELD* TX
CLONING
By sequencing clones obtained from an immature myeloid leukemia cell
line cDNA library, Nagase et al. (1996) cloned HSPH1, which they
designated KIAA0201. The deduced 858-amino acid protein contains an
HSP70 (see HSPA1A; 140550)-like motif and shares 93.4% identity with
mouse Hsph1-alpha. Northern blot analysis detected highest expression in
brain, lung, and testis. Expression was lower in heart, skeletal muscle,
kidney, pancreas, spleen, ovary, small intestine, colon, and peripheral
blood leukocytes, and weak in liver. No expression was detected in
thymus and prostate.
Using mouse Hsph1 to screen a cDNA library derived from heat-shocked
HeLa cells, Ishihara et al. (1999) cloned 2 splice variants of HSPH1,
which they called HSP105-alpha and HSP105-beta. The HSP105-alpha and
HSP105-beta proteins contain 858 and 814 amino acids, respectively, and
both have an N-terminal ATP-binding domain. Northern blot analysis
detected a 4-kb HSP105 transcript in HeLa cells. Immunohistochemical
analysis localized HSP105 mainly in the cytoplasm. Database analysis
indicated that both HSP105 isoforms are highly conserved during
evolution.
GENE FUNCTION
Using Northern blot analysis, Ishihara et al. (1999) found that both
HSP105-alpha and HSP105-beta were upregulated in HeLa cells exposed to
heat shock. HSP105-alpha, but not HSP105-beta, was also upregulated in
response to other cell stresses. Following heat shock, HSP105
relocalized from a cytoplasmic to perinuclear position.
MOLECULAR GENETICS
Dorard et al. (2011) identified a mutant of HSP110, which they called
HSP110-delta-E9, in colorectal cancer (114500) showing microsatellite
instability (MSI CRC), generated from an aberrantly spliced mRNA and
lacking the HSP110 substrate-binding domain. This mutant was expressed
at variable levels in almost all MSI CRC cell lines and primary tumors
tested. HSP110-delta-E9 impaired both the normal cellular localization
of HSP110 and its interaction with other HSPs, thus abrogating the
chaperone activity and antiapoptotic function of HSP110 in a
dominant-negative manner. HSP110-delta-E9 overexpression caused the
sensitization of cells to anticancer agents such as oxaliplatin and
5-fluorouracil, which are routinely prescribed in the adjuvant treatment
of people with colorectal cancer. The survival and response to
chemotherapy of subjects with colorectal cancer showing microsatellite
instability was associated with the tumor expression level of
HSP110-delta-E9. Dorard et al. (2011) concluded that HSP110 may thus
constitute a major determinant for both prognosis and treatment response
in colorectal cancer.
MAPPING
By analysis of radiation hybrids and human/rodent hybrid cell lines,
Nagase et al. (1996) mapped the HSPH1 gene to chromosome 13.
*FIELD* RF
1. Dorard, C.; de Thonel, A.; Collura, A.; Marisa, L.; Svrcek, M.;
Lagrange, A.; Jego, G.; Wanherdrick, K.; Joly, A. L.; Buhard, O.;
Gobbo, J.; Penard-Lacronique, V.; and 16 others: Expression of
a mutant HSP110 sensitizes colorectal cancer cells to chemotherapy
and improves disease prognosis. Nature Med. 17: 1283-1289, 2011.
2. Ishihara, K.; Yasuda, K.; Hatayama, T.: Molecular cloning, expression
and localization of human 105 kDa heat shock protein, hsp105. Biochim.
Biophys. Acta 1444: 138-142, 1999.
3. Nagase, T.; Seki, N.; Ishikawa, K.; Ohira, M.; Kawarabayasi, Y.;
Ohara, O.; Tanaka, A.; Kotani, H.; Miyajima, N.; Nomura, N.: Prediction
of the coding sequences of unidentified human genes. VI. The coding
sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis
of cDNA clones from cell line KG-1 and brain. DNA Res. 3: 321-329,
1996.
*FIELD* CN
Ada Hamosh - updated: 12/12/2011
*FIELD* CD
Patricia A. Hartz: 1/16/2007
*FIELD* ED
alopez: 12/19/2011
terry: 12/12/2011
mgross: 1/16/2007