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UniProtKB/Swiss-Prot entry Q92598


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HS105_HUMAN
Primary accession number Q92598
Secondary accession numbers O95739 Q5TBM6 Q5TBM7 Q5TBM8 Q9UPC4
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on February 1, 1997 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 100)
Name and origin of the protein
Protein name Heat shock protein 105 kDa
Synonyms Heat shock 110 kDa protein
Antigen NY-CO-25
Gene name
Name: HSPH1
Synonyms: HSP105, HSP110, KIAA0201
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), AND SUBCELLULAR LOCATION.
DOI=10.1016/S0167-4781(98)00254-1; PubMed=9931472 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
TISSUE=Colon carcinoma;
DOI=10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P; PubMed=9610721 [NCBI, ExPASy, EBI, Israel, Japan]
Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E., Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
"Characterization of human colon cancer antigens recognized by autologous antibodies.";
Int. J. Cancer 76:652-658(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Bone marrow;
DOI=10.1093/dnares/3.5.321; PubMed=9039502 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02379; PubMed=15057823 [NCBI, ExPASy, EBI, Israel, Japan]
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 332-346 AND 375-388, AND MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[8]
TISSUE SPECIFICITY.
DOI=10.1016/S0006-8993(00)02346-5; PubMed=10865058 [NCBI, ExPASy, EBI, Israel, Japan]
Hylander B.L., Chen X., Graf P.C.F., Subjeck J.R.;
"The distribution and localization of hsp110 in brain.";
Brain Res. 869:49-55(2000).
[9]
TISSUE SPECIFICITY.
DOI=10.1111/j.1349-7006.2005.00093.x; PubMed=16232202 [NCBI, ExPASy, EBI, Israel, Japan]
Miyazaki M., Nakatsura T., Yokomine K., Senju S., Monji M., Hosaka S., Komori H., Yoshitake Y., Motomura Y., Minohara M., Kubo T., Ishihara K., Hatayama T., Ogawa M., Nishimura Y.;
"DNA vaccination of HSP105 leads to tumor rejection of colorectal cancer and melanoma in mice through activation of both CD4 T cells and CD8 T cells.";
Cancer Sci. 96:695-705(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND MASS SPECTROMETRY.
DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-E., Tannenbaum S.R., White F.M.;
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
J. Proteome Res. 4:1339-1346(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 AND THR-815, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557 AND SER-809, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-809, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-700; SER-809 AND THR-815, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB003333; BAA34779.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB003334; BAA34780.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039695; AAC18044.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D86956; BAA13192.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL137142; CAI12428.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL137142; CAI12429.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL137142; CAI12430.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471075; EAX08482.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC037553; AAH37553.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00218993; -.
IPI00513743; -.
IPI00514983; -.
RefSeq NP_006635.2; -.
UniGene Hs.36927
3D structure databases
HSSP P19120; 1BUP. [HSSP ENTRY / PDB]
ModBase Q92598.
Protein-protein interaction databases
IntAct Q92598; 5.
PTM databases
PhosphoSite Q92598; -.
2D gel databases
REPRODUCTION-2DPAGE Q92598; -.
Organism-specific databases
GeneCards GC13M030608; -.
H-InvDB HIX0011215; -.
HGNC HGNC:16969; HSPH1.
GenAtlas HSPH1.
HPA CAB002060; -.
MIM 610703; gene. [NCBI / EBI]
PharmGKB PA134869917; -.
HUGE KIAA0201.
Gene expression databases
ArrayExpress Q92598; -.
Bgee Q92598; -.
CleanEx HS_HSPH1; -.
GermOnline ENSG00000120694; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from ProtInc).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006986; Biological process: response to unfolded protein (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR018181; Heat_shock_70_CS.
IPR001023; Hsp70.
IPR013126; Hsp_70.
Graphical view of domain structure.
PANTHER PTHR19375; Hsp70; 1.
Pfam PF00012; HSP70; 1.
Pfam graphical view of domain structure.
PRINTS PR00301; HEATSHOCK70.
ProDom PD000089; Hsp70; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00297; HSP70_1; FALSE_NEG.
PS00329; HSP70_2; FALSE_NEG.
PS01036; HSP70_3; 1.
Proteomic databases
PRIDE Q92598; -.
Genome annotation databases
Ensembl ENSG00000120694; Homo sapiens. [Contig view]
GeneID 10808; -.
KEGG hsa:10808; -.
Phylogenomic databases
HOGENOM Q92598; -.
HOVERGEN Q92598; -.
OMA Q92598; LMEQTQL.
Other
NextBio 41059; -.
PMAP-CutDB Q92598; -.
SOURCE HSPH1; Homo sapiens.
ProtoNet Q92598.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ATP-binding; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   858  858     Heat shock protein 105 kDa. PRO_0000078284
MOD_RES   31    31        Phosphoserine. 
MOD_RES   384   384        Phosphoserine. 
MOD_RES   509   509        Phosphoserine (By similarity). 
MOD_RES   557   557        Phosphoserine. 
MOD_RES   700   700        Phosphothreonine. 
MOD_RES   809   809        Phosphoserine. 
MOD_RES   815   815        Phosphothreonine. 
VAR_SEQ   104   144        Missing (in isoform 3). VSP_035428
VAR_SEQ   529   572        Missing (in isoform Beta). VSP_002428
Sequence information
Length: 858 AA [This is the length of the unprocessed precursor] Molecular weight: 96865 Da [This is the MW of the unprocessed precursor] CRC64: D0E757970E340B56 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGSKNRTIGV AAKNQQITHA 

        70         80         90        100        110        120 
NNTVSNFKRF HGRAFNDPFI QKEKENLSYD LVPLKNGGVG IKVMYMGEEH LFSVEQITAM 

       130        140        150        160        170        180 
LLTKLKETAE NSLKKPVTDC VISVPSFFTD AERRSVLDAA QIVGLNCLRL MNDMTAVALN 

       190        200        210        220        230        240 
YGIYKQDLPS LDEKPRIVVF VDMGHSAFQV SACAFNKGKL KVLGTAFDPF LGGKNFDEKL 

       250        260        270        280        290        300 
VEHFCAEFKT KYKLDAKSKI RALLRLYQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSGK 

       310        320        330        340        350        360 
MNRSQFEELC AELLQKIEVP LYSLLEQTHL KVEDVSAVEI VGGATRIPAV KERIAKFFGK 

       370        380        390        400        410        420 
DISTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF PISLIWNHDS EDTEGVHEVF 

       430        440        450        460        470        480 
SRNHAAPFSK VLTFLRRGPF ELEAFYSDPQ GVPYPEAKIG RFVVQNVSAQ KDGEKSRVKV 

       490        500        510        520        530        540 
KVRVNTHGIF TISTASMVEK VPTEENEMSS EADMECLNQR PPENPDTDKN VQQDNSEAGT 

       550        560        570        580        590        600 
QPQVQTDAQQ TSQSPPSPEL TSEENKIPDA DKANEKKVDQ PPEAKKPKIK VVNVELPIEA 

       610        620        630        640        650        660 
NLVWQLGKDL LNMYIETEGK MIMQDKLEKE RNDAKNAVEE YVYEFRDKLC GPYEKFICEQ 

       670        680        690        700        710        720 
DHQNFLRLLT ETEDWLYEEG EDQAKQAYVD KLEELMKIGT PVKVRFQEAE ERPKMFEELG 

       730        740        750        760        770        780 
QRLQHYAKIA ADFRNKDEKY NHIDESEMKK VEKSVNEVME WMNNVMNAQA KKSLDQDPVV 

       790        800        810        820        830        840 
RAQEIKTKIK ELNNTCEPVV TQPKPKIESP KLERTPNGPN IDKKEEDLED KNNFGAEPPH 

       850 
QNGECYPNEK NSVNMDLD 

Q92598 in FASTA format

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