Details for: AHSA1
Associated with
Other Information
Genular Protein ID: 2274597723
Symbol: AHSA1_HUMAN
Name: Activator of 90 kDa heat shock protein ATPase homolog 1
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 10931946
Title: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning.
PubMed ID: 10931946
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 12508121
Title: The DNA sequence and analysis of human chromosome 14.
PubMed ID: 12508121
DOI: 10.1038/nature01348
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 11042152
Title: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells.
PubMed ID: 11042152
DOI: 10.1101/gr.140200
PubMed ID: 11554768
Title: p38: a novel protein that associates with the vesicular stomatitis virus glycoprotein.
PubMed ID: 11554768
PubMed ID: 12504007
Title: Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1.
PubMed ID: 12504007
PubMed ID: 12604615
Title: Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone.
PubMed ID: 12604615
PubMed ID: 16696853
Title: A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein interactions.
PubMed ID: 16696853
PubMed ID: 19240134
Title: Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones.
PubMed ID: 19240134
DOI: 10.1101/gad.1752109
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 25114211
Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
PubMed ID: 25114211
PubMed ID: 27353360
Title: The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.
PubMed ID: 27353360
DOI: 10.1038/ncomms12037
PubMed ID: 29127155
Title: Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients.
PubMed ID: 29127155
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
Sequence Information:
- Length: 338
- Mass: 38274
- Checksum: E6B686DDD8D7D729
- Sequence:
MAKWGEGDPR WIVEERADAT NVNNWHWTER DASNWSTDKL KTLFLAVQVQ NEEGKCEVTE VSKLDGEASI NNRKGKLIFF YEWSVKLNWT GTSKSGVQYK GHVEIPNLSD ENSVDEVEIS VSLAKDEPDT NLVALMKEEG VKLLREAMGI YISTLKTEFT QGMILPTMNG ESVDPVGQPA LKTEERKAKP APSKTQARPV GVKIPTCKIT LKETFLTSPE ELYRVFTTQE LVQAFTHAPA TLEADRGGKF HMVDGNVSGE FTDLVPEKHI VMKWRFKSWP EGHFATITLT FIDKNGETEL CMEGRGIPAP EEERTRQGWQ RYYFEGIKQT FGYGARLF
Genular Protein ID: 1679556106
Symbol: G3V438_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 12508121
Title: The DNA sequence and analysis of human chromosome 14.
PubMed ID: 12508121
DOI: 10.1038/nature01348
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 25114211
Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
PubMed ID: 25114211
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
Sequence Information:
- Length: 203
- Mass: 22978
- Checksum: 566E1B355CCC7C9A
- Sequence:
MKEEGVKLLR EAMGIYISTL KTEFTQGMIL PTMNGESVDP VGQPALKTEE RKAKPAPSKT QARPVGVKIP TCKITLKETF LTSPEELYRV FTTQELVQAF THAPATLEAD RGGKFHMVDG NVSGEFTDLV PEKHIVMKWR FKSWPEGHFA TITLTFIDKN GETELCMEGR GIPAPEEERT RQGWQRYYFE GIKQTFGYGA RLF
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.