Gene Symbol | HSP90AA1 |
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Entrez Gene | 3320 |
Alt Symbol | EL52, HSP86, HSP89A, HSP90A, HSP90N, HSPC1, HSPCA, HSPCAL1, HSPCAL4, HSPN, Hsp89, Hsp90, LAP-2, LAP2 |
Species | Human |
Gene Type | protein-coding |
Description | heat shock protein 90kDa alpha (cytosolic), class A member 1 |
Other Description | HSP 86|LPS-associated protein 2|epididymis luminal secretory protein 52|heat shock 86 kDa|heat shock 90kD protein 1, alpha|heat shock 90kD protein 1, alpha-like 4|heat shock 90kD protein, alpha-like 4|heat shock 90kDa protein 1, alpha|heat shock protein HSP 90-alpha|lipopolysaccharide-associated protein 2|renal carcinoma antigen NY-REN-38 |
Swissprots | Q5CAQ7 Q5CAQ6 B3KPJ9 A8K500 Q9BVQ5 Q2PP14 P07900 |
Accessions | AAA36023 AAA63194 ABC40730 EAW81765 EAW81766 EAW81767 EAW81768 P07900 AF028832 AAC25497 AI250920 AJ890082 CAI64495 AJ890083 CAI64496 AK056446 BAG51711 AK129557 AK291115 BAF83804 AK291607 BAF84296 AK300126 BAG61917 AK310595 BC000987 AAH00987 BC001695 BC007989 AAH07989 BC017233 BC023006 AAH23006 BC108695 AAI08696 BC121062 AAI21063 BX247955 CAD62296 BX248761 CAD66568 DA237149 DC303876 GQ149083 ADD71695 X07270 CAA30255 X15183 CAA33259 XM_011536718 XP_011535020 NM_001017963 NP_001017963 NM_005348 NP_005339 |
Function | Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. {ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:15937123}. |
Subcellular Location | Cytoplasm. Melanosome. Cell membrane. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. |
Top Pathways | Progesterone-mediated oocyte maturation, Prostate cancer, NOD-like receptor signaling pathway, Protein processing in endoplasmic reticulum, PI3K-Akt signaling pathway |
HSP 90α CRISPR/Cas9 KO Plasmid (h) - sc-400088 from Santa Cruz Biotechnology
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HSP 90α HDR Plasmid (h) - sc-400088-HDR from Santa Cruz Biotechnology
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HSP 90α Double Nickase Plasmid (h) - sc-400088-NIC from Santa Cruz Biotechnology
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HSP 90α Double Nickase Plasmid (h2) - sc-400088-NIC-2 from Santa Cruz Biotechnology
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HSP 90α CRISPR Activation Plasmid (h) - sc-400088-ACT from Santa Cruz Biotechnology
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HSP 90α CRISPR Activation Plasmid (h2) - sc-400088-ACT-2 from Santa Cruz Biotechnology
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HSP 90α Lentiviral Activation Particles (h) - sc-400088-LAC from Santa Cruz Biotechnology
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HSP 90α Lentiviral Activation Particles (h2) - sc-400088-LAC-2 from Santa Cruz Biotechnology
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HSP 90α siRNA (h) - sc-29353 from Santa Cruz Biotechnology
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HSP 90α shRNA Plasmid (h) - sc-29353-SH from Santa Cruz Biotechnology
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HSP 90α shRNA (h) Lentiviral Particles - sc-29353-V from Santa Cruz Biotechnology
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HSP 90α/β siRNA (h) - sc-35608 from Santa Cruz Biotechnology
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HSP 90α/β shRNA Plasmid (h) - sc-35608-SH from Santa Cruz Biotechnology
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HSP 90α/&beta shRNA (h) Lentiviral Particles - sc-35608-V from Santa Cruz Biotechnology
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MISSION® esiRNA - EHU114671 from Sigma-Aldrich
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MISSION® esiRNA - EHU108501 from Sigma-Aldrich
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CompoZr® Knockout ZFN Kit - CKOZFN1870 from Sigma-Aldrich
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CompoZr® Knockout ZFN Kit, ZFN plasmid only - CKOZFND1870 from Sigma-Aldrich
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MISSION® 3′UTR Lenti GoClone™ - HUTR13079 from Sigma-Aldrich
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HSP90AA1 siRNA (Human) - CRH2269 from Cohesion Biosciences
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HSP90AA1 - MBS8218565 from MyBioSource
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shRNA set against Human HSP90AA1 (NM_001017963.2) - SHH315461 from Creative biogene
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shRNA set against Human HSP90AA1(NM_001017963.2) - SHH133643 from Creative biogene
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shRNA set against Human HSP90AA1(NM_005348.3) - SHH133661 from Creative biogene
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Human HSP90AA1 siRNA - orb262771 from Biorbyt
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