HSP90AA1

HSP90AA1
Strwythurau PDB Human UniProt search: PDBe RCSB Rhestr o ddynodwyr PDB 1BYQ, 1OSF, 1UY6, 1UY7, 1UY8, 1UY9, 1UYC, 1UYD, 1UYE, 1UYF, 1UYG, 1UYH, 1UYI, 1UYK, 1UYL, 1YC1, 1YC3, 1YC4, 1YER, 1YES, 1YET, 2BSM, 2BT0, 2BYH, 2BYI, 2BZ5, 2C2L, 2CCS, 2CCT, 2CCU, 2FWY, 2FWZ, 2JJC, 2K5B, 2QF6, 2QFO, 2QG0, 2QG2, 2UWD, 2VCI, 2VCJ, 2WI1, 2WI2, 2WI3, 2WI4, 2WI5, 2WI6, 2WI7, 2XAB, 2XDK, 2XDS, 2XDU, 2XDX, 2XHR, 2XHT, 2XHX, 2XJG, 2XJJ, 2XJX, 2XK2, 2YE2, 2YE3, 2YE4, 2YE5, 2YE6, 2YE7, 2YE8, 2YE9, 2YEA, 2YEB, 2YEC, 2YED, 2YEE, 2YEF, 2YEG, 2YEH, 2YEI, 2YEJ, 2YI0, 2YI5, 2YI6, 2YI7, 2YJW, 2YJX, 2YK2, 2YK9, 2YKB, 2YKC, 2YKE, 2YKI, 2YKJ, 3B24, 3B25, 3B26, 3B27, 3B28, 3BM9, 3BMY, 3D0B, 3EKO, 3EKR, 3FT5, 3FT8, 3HEK, 3HHU, 3HYY, 3HYZ, 3HZ1, 3HZ5, 3INW, 3INX, 3K97, 3K98, 3K99, 3MNR, 3O0I, 3OW6, 3OWB, 3OWD, 3Q6M, 3Q6N, 3QDD, 3QTF, 3R4M, 3R4N, 3R4O, 3R4P, 3R91, 3R92, 3RKZ, 3RLP, 3RLQ, 3RLR, 3T0H, 3T0Z, 3T10, 3T1K, 3T2S, 3TUH, 3VHA, 3VHC, 3VHD, 3WHA, 3WQ9, 4AIF, 4AWO, 4AWP, 4AWQ, 4B7P, 4BQJ, 4CGQ, 4CGU, 4CGV, 4CGW, 4CWF, 4CWN, 4CWO, 4CWP, 4CWQ, 4CWR, 4CWS, 4CWT, 4EEH, 4EFT, 4EFU, 4EGH, 4EGI, 4EGK, 4FCP, 4FCQ, 4FCR, 4HY6, 4JQL, 4L8Z, 4L90, 4L91, 4L93, 4L94, 4LWE, 4LWF, 4LWG, 4LWH, 4LWI, 4NH7, 4NH8, 4O04, 4O05, 4O07, 4O0B, 4R3M, 4U93, 4W7T, 4XIP, 4XIQ, 4XIR, 4XIT, 4YKT, 4YKW, 4YKU, 4YKQ, 4YKY, 4YKR, 4YKX, 4YKZ, 2BUG, 5CF0, 2H55, 4BQG
Dynodwyr
Cyfenwau	HSP90AA1, EL52, HSP86, HSP89A, HSP90A, HSP90N, HSPC1, HSPCA, HSPCAL1, HSPCAL4, HSPN, Hsp89, Hsp90, LAP-2, LAP2, HEL-S-65p, Heat shock protein 90kDa alpha, heat shock protein 90kDa alpha family class A member 1, heat shock protein 90 alpha family class A member 1, Hsp103
Dynodwyr allanol	OMIM: 140571 HomoloGene: 68464 GeneCards: HSP90AA1
Patrwm RNA pattern Rhagor o gyfeiriadau
Ontoleg y genyn Gweithrediad moleciwlaidd • nucleotide binding • protein homodimerization activity • unfolded protein binding • histone deacetylase binding • nitric-oxide synthase regulator activity • ATPase activity • GO:0001948, GO:0016582 protein binding • MHC class II protein complex binding • identical protein binding • GTPase binding • TPR domain binding • protein tyrosine kinase activity • RNA binding • ATP binding • DNA polymerase binding • protein tyrosine kinase binding • disordered domain specific binding • ubiquitin protein ligase binding • tau protein binding • scaffold protein binding Cydrannau o'r gell • cytosol • endocytic vesicle lumen • bilen • melanosome • myelin sheath • Cellbilen • intracellular anatomical structure • ruffle membrane • extracellular region • lysosomal lumen • extracellular exosome • cnewyllyn cell • nucleoplasm • secretory granule lumen • ficolin-1-rich granule lumen • cytoplasm • cell surface • GO:0009327 protein-containing complex • neuronal cell body • dendritic growth cone • axonal growth cone • perinuclear region of cytoplasm Prosesau biolegol • chaperone-mediated autophagy • protein insertion into mitochondrial outer membrane • chaperone-mediated protein complex assembly • Fc-gamma receptor signaling pathway involved in phagocytosis • GO:1904576 response to antibiotic • positive regulation of nitric oxide biosynthetic process • regulation of protein ubiquitination • regulation of nitric-oxide synthase activity • response to stress • mitochondrial transport • receptor-mediated endocytosis • response to unfolded protein • vascular endothelial growth factor receptor signaling pathway • G2/M transition of mitotic cell cycle • protein folding • protein refolding • protein unfolding • regulation of cellular response to heat • response to cold • GO:0106159 regulation of protein-containing complex assembly • GO:0072468 signal transduction • peptidyl-tyrosine phosphorylation • ERBB2 signaling pathway • telomere maintenance via telomerase • response to heat • neutrophil degranulation • protein stabilization • positive regulation of telomerase activity • ciliary basal body-plasma membrane docking • telomerase holoenzyme complex assembly • regulation of G2/M transition of mitotic cell cycle • positive regulation of protein phosphorylation • cytokine-mediated signaling pathway • central nervous system neuron axonogenesis • establishment of cell polarity • positive regulation of protein polymerization • positive regulation of peptidyl-serine phosphorylation • cellular response to heat • axon extension • positive regulation of protein kinase B signaling • positive regulation of tau-protein kinase activity Sources:Amigo / QuickGO
Orthologau
Species	Bod dynol	Llygoden
Entrez	3320	n/a
Ensembl	ENSG00000080824	n/a
UniProt	P07900	n/a
RefSeq (mRNA)	NM_001017963 NM_005348	n/a
RefSeq (protein)	NP_001017963 NP_005339	n/a
Lleoliad (UCSC)	n/a	n/a
PubMed search		n/a
Wicidata
Gweld/Golygu Bod dynol

Protein sy'n cael ei godio yn y corff dynol gan y genyn HSP90AA1 yw HSP90AA1 a elwir hefyd yn Heat shock protein HSP 90-alpha (Saesneg). Segment o DNA yw'r genyn, sy'n amgodio ffwythiant arbennig. Mae'r genyn yma wedi ei leoli ar yr edefyn ôl o gromosom dynol 14, band 14q32.31.

Cyfystyron

Yn aml mae gan enynnau lawer o gyfystyron. Mae hyn oherwydd eu bod yn aml yn cael eu darganfod gan nifer o bobl mewn cyd-destunau gwahanol heb wybod mai'r un genynnau oeddyn nhw. Hefyd mae gan wahanol gymunedau gwyddonol safonau gwahanol ar gyfer enwi genynnau. Dyma restr o gyfystyron ar gyfer y genyn HSP90AA1.

• EL52
• HSPN
• LAP2
• HSP86
• HSPC1
• HSPCA
• Hsp89
• Hsp90
• LAP-2
• HSP89A
• HSP90A
• HSP90N
• Hsp103
• HSPCAL1
• HSPCAL4
• HEL-S-65p

Llyfryddiaeth

• "HSP90 inhibition enhances cancer immunotherapy by upregulating interferon response genes. ". Nat Commun. 2017. PMID 28878208.
• "HSP90 promotes Burkitt lymphoma cell survival by maintaining tonic B-cell receptor signaling. ". Blood. 2017. PMID 28064214.
• "Ratio of proliferation markers and HSP90 gene expression as a predictor of pathological complete response in breast cancer neoadjuvant chemotherapy. ". Folia Histochem Cytobiol. 2016. PMID 28051275.
• "Secreted heat shock protein 90 promotes prostate cancer stem cell heterogeneity. ". Oncotarget. 2017. PMID 28038472.
• "Extensive Citrullination Promotes Immunogenicity of HSP90 through Protein Unfolding and Exposure of Cryptic Epitopes.". J Immunol. 2016. PMID 27448590.