USC-OGP 2-DE database Two-dimensional polyacrylamide gel electrophoresis database

USC-OGP 2-DE database  Search by                Maps             Select Remote Interfaces [All Interfaces] SWISS-2DPAGE World-2DPAGE Portal World-2DPAGE Repository Exclude local DBs has only effect if a remote interface is selected

Searching in 'USC-OGP 2-DE database' for entry matching: P07900 USC-OGP 2-DE database:  P07900 P07900 General information about the entry View entry in simple text format Entry name HS90A_HUMAN Primary accession number P07900 integrated into USC-OGP 2-DE database on  January 17, 2017 (release 1) 2D Annotations were last modified on January 17, 2017 (version 1) General Annotations were last modified on  April 5, 2017 (version 2) Name and origin of the protein Description RecName: Full=Heat shock protein HSP 90-alpha; AltName: Full=Heat shock 86 kDa; Short=HSP 86; Short=HSP86; AltName: Full=Lipopolysaccharide-associated protein 2; Short=LAP-2; Short=LPS-associated protein 2; AltName: Full=Renal carcinoma antigen NY-REN-38;. Gene name Name=HSP90AA1 Synonyms=HSP90A, HSPC1, HSPCA Annotated species Homo sapiens (Human) [TaxID: 9606] Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. References [1]   2D GEL CHARACTERIZATION Author 1., Author 2. Submitted (Mar-2011) to Current 2D PAGE maps for identified proteins How to interpret a protein PLATELET_4-5 {PLATELET 4-5} Homo sapiens (Human)   map experimental info   PLATELET_4-5 MAP LOCATIONS: SPOT OGP-0017: pI=4.97; Mw=96951 UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10} Homo sapiens (Human)   map experimental info   UVEAL_MELANOMA_3-10 MAP LOCATIONS: SPOT OGP-1111: pI=5.20; Mw=104418 Cross-references UniProtKB/Swiss-Prot P07900; HS90A_HUMAN. 2D PAGE maps for identified proteins How to interpret a protein map You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw. Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly. Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed. External data extracted from UniProtKB/Swiss-Prot Extracted from UniProtKB/Swiss-Prot, release: 0.0 Entry name HS90A_HUMAN Primary accession number P07900 Secondary accession number(s) A8K500 B3KPJ9 Q2PP14 Q5CAQ6 Q5CAQ7 Q9BVQ5 Sequence was last modified on  January 23, 2007 (version 5) Annotations were last modified on  March 15, 2017 (version 223) Name and origin of the protein Description RecName: Full=Heat shock protein HSP 90-alpha; AltName: Full=Heat shock 86 kDa; Short=HSP 86; Short=HSP86; AltName: Full=Lipopolysaccharide-associated protein 2; Short=LAP-2; Short=LPS-associated protein 2; AltName: Full=Renal carcinoma antigen NY-REN-38; Gene name Name=HSP90AA1 Synonyms=HSP90A, HSPC1, HSPCA Encoded on Name=HSP90AA1; Synonyms=HSP90A, HSPC1, HSPCA Keywords 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell membrane; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; S-nitrosylation; Stress response; Ubl conjugation. Copyright Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL X15183; CAA33259.1; -; mRNA EMBL M27024; AAA63194.1; -; Genomic_DNA EMBL AJ890082; CAI64495.1; -; mRNA EMBL AJ890083; CAI64496.1; -; mRNA EMBL DQ314871; ABC40730.1; -; Genomic_DNA EMBL AK056446; BAG51711.1; -; mRNA EMBL AK291115; BAF83804.1; -; mRNA EMBL AK291607; BAF84296.1; -; mRNA EMBL AL133223; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL CH471061; EAW81765.1; -; Genomic_DNA EMBL X07270; CAA30255.1; -; mRNA EMBL M30626; AAA36023.1; -; Genomic_DNA EMBL BC000987; AAH00987.1; -; mRNA EMBL BC121062; AAI21063.1; -; mRNA EMBL D87666; BAA13430.1; -; mRNA EMBL D87666; BAA13431.1; -; mRNA CCDS CCDS32160.1; -. [P07900-2]; . CCDS CCDS9967.1; -. [P07900-1]; . PIR A32319; HHHU86; . RefSeq NP_001017963.2; NM_001017963.2. [P07900-2]; . RefSeq NP_005339.3; NM_005348.3. [P07900-1]; . UniGene Hs.525600; -; . PDB 1BYQ; X-ray; 1.50 A; A=9-236 PDB 1OSF; X-ray; 1.75 A; A=9-223 PDB 1UY6; X-ray; 1.90 A; A=2-236 PDB 1UY7; X-ray; 1.90 A; A=2-236 PDB 1UY8; X-ray; 1.98 A; A=2-236 PDB 1UY9; X-ray; 2.00 A; A=2-236 PDB 1UYC; X-ray; 2.00 A; A=2-236 PDB 1UYD; X-ray; 2.20 A; A=2-236 PDB 1UYE; X-ray; 2.00 A; A=2-236 PDB 1UYF; X-ray; 2.00 A; A=2-236 PDB 1UYG; X-ray; 2.00 A; A=2-236 PDB 1UYH; X-ray; 2.20 A; A=2-236 PDB 1UYI; X-ray; 2.20 A; A=2-236 PDB 1UYK; X-ray; 2.20 A; A=2-236 PDB 1UYL; X-ray; 1.40 A; A=2-236 PDB 1YC1; X-ray; 1.70 A; A=9-236 PDB 1YC3; X-ray; 2.12 A; A=9-236 PDB 1YC4; X-ray; 1.81 A; A=9-236 PDB 1YER; X-ray; 1.65 A; A=9-236 PDB 1YES; X-ray; 2.20 A; A=9-236 PDB 1YET; X-ray; 1.90 A; A=9-236 PDB 2BSM; X-ray; 2.05 A; A=2-236 PDB 2BT0; X-ray; 1.90 A; A/B=2-236 PDB 2BUG; NMR; -; B=728-732 PDB 2BYH; X-ray; 1.90 A; A=11-236 PDB 2BYI; X-ray; 1.60 A; A=11-236 PDB 2BZ5; X-ray; 1.90 A; A/B=2-236 PDB 2C2L; X-ray; 3.30 A; E/F/G/H=724-732 PDB 2CCS; X-ray; 1.79 A; A=1-236 PDB 2CCT; X-ray; 2.30 A; A=1-236 PDB 2CCU; X-ray; 2.70 A; A=1-236 PDB 2FWY; X-ray; 2.10 A; A=1-236 PDB 2FWZ; X-ray; 2.10 A; A=1-236 PDB 2H55; X-ray; 2.00 A; A=1-236 PDB 2JJC; X-ray; 1.95 A; A=9-223 PDB 2K5B; NMR; -; A=14-223 PDB 2QF6; X-ray; 3.10 A; A/B/C/D=17-223 PDB 2QFO; X-ray; 1.68 A; A/B=17-223 PDB 2QG0; X-ray; 1.85 A; A/B=17-223 PDB 2QG2; X-ray; 1.80 A; A=17-223 PDB 2UWD; X-ray; 1.90 A; A=2-236 PDB 2VCI; X-ray; 2.00 A; A=1-236 PDB 2VCJ; X-ray; 2.50 A; A=1-236 PDB 2WI1; X-ray; 2.30 A; A=1-236 PDB 2WI2; X-ray; 2.09 A; A/B=1-236 PDB 2WI3; X-ray; 1.90 A; A=1-236 PDB 2WI4; X-ray; 2.40 A; A=1-236 PDB 2WI5; X-ray; 2.10 A; A=1-236 PDB 2WI6; X-ray; 2.18 A; A=1-236 PDB 2WI7; X-ray; 2.50 A; A=1-236 PDB 2XAB; X-ray; 1.90 A; A/B=9-236 PDB 2XDK; X-ray; 1.97 A; A=9-236 PDB 2XDL; X-ray; 1.98 A; A=9-236 PDB 2XDS; X-ray; 1.97 A; A=9-236 PDB 2XDU; X-ray; 1.74 A; A=14-224 PDB 2XDX; X-ray; 2.42 A; A=9-236 PDB 2XHR; X-ray; 2.20 A; A=9-236 PDB 2XHT; X-ray; 2.27 A; A=9-236 PDB 2XHX; X-ray; 2.80 A; A=9-236 PDB 2XJG; X-ray; 2.25 A; A=9-236 PDB 2XJJ; X-ray; 1.90 A; A/B=9-236 PDB 2XJX; X-ray; 1.66 A; A=9-236 PDB 2XK2; X-ray; 1.95 A; A=9-236 PDB 2YE2; X-ray; 1.90 A; A=9-236 PDB 2YE3; X-ray; 1.95 A; A=9-236 PDB 2YE4; X-ray; 2.30 A; A=9-236 PDB 2YE5; X-ray; 1.73 A; A=9-236 PDB 2YE6; X-ray; 2.56 A; A=9-236 PDB 2YE7; X-ray; 2.20 A; A=9-236 PDB 2YE8; X-ray; 2.30 A; A=9-236 PDB 2YE9; X-ray; 2.20 A; A=9-236 PDB 2YEA; X-ray; 1.73 A; A=9-236 PDB 2YEB; X-ray; 2.40 A; A=9-236 PDB 2YEC; X-ray; 2.10 A; A=9-236 PDB 2YED; X-ray; 2.10 A; A=9-236 PDB 2YEE; X-ray; 2.30 A; A=9-236 PDB 2YEF; X-ray; 1.55 A; A=9-236 PDB 2YEG; X-ray; 2.50 A; A/B=9-236 PDB 2YEH; X-ray; 2.10 A; A=9-236 PDB 2YEI; X-ray; 2.20 A; A=9-236 PDB 2YEJ; X-ray; 2.20 A; A=9-236 PDB 2YI0; X-ray; 1.60 A; A=1-229 PDB 2YI5; X-ray; 2.50 A; A=1-229 PDB 2YI6; X-ray; 1.80 A; A=1-229 PDB 2YI7; X-ray; 1.40 A; A=1-229 PDB 2YJW; X-ray; 1.61 A; A=18-223 PDB 2YJX; X-ray; 1.83 A; A=18-223 PDB 2YK2; X-ray; 1.74 A; A=18-223 PDB 2YK9; X-ray; 1.32 A; A=18-223 PDB 2YKB; X-ray; 1.93 A; A=18-223 PDB 2YKC; X-ray; 1.67 A; A=18-223 PDB 2YKE; X-ray; 1.43 A; A=18-223 PDB 2YKI; X-ray; 1.67 A; A=18-223 PDB 2YKJ; X-ray; 1.46 A; A=18-223 PDB 3B24; X-ray; 1.70 A; A/B=9-236 PDB 3B25; X-ray; 1.75 A; A=9-236 PDB 3B26; X-ray; 2.10 A; A/B=9-236 PDB 3B27; X-ray; 1.50 A; A=9-236 PDB 3B28; X-ray; 1.35 A; A/B=9-236 PDB 3BM9; X-ray; 1.60 A; A=14-236 PDB 3BMY; X-ray; 1.60 A; A=14-236 PDB 3D0B; X-ray; 1.74 A; A=1-232 PDB 3EKO; X-ray; 1.55 A; A/B=9-225 PDB 3EKR; X-ray; 2.00 A; A/B=9-225 PDB 3FT5; X-ray; 1.90 A; A=9-236 PDB 3FT8; X-ray; 2.00 A; A=9-236 PDB 3HEK; X-ray; 1.95 A; A/B=9-225 PDB 3HHU; X-ray; 1.59 A; A/B=1-224 PDB 3HYY; X-ray; 1.90 A; A=9-236 PDB 3HYZ; X-ray; 2.30 A; A/B=9-236 PDB 3HZ1; X-ray; 2.30 A; A=9-236 PDB 3HZ5; X-ray; 1.90 A; A=9-236 PDB 3INW; X-ray; 1.95 A; A=10-236 PDB 3INX; X-ray; 1.75 A; A=10-236 PDB 3K97; X-ray; 1.95 A; A=9-236 PDB 3K98; X-ray; 2.40 A; A/B=9-225 PDB 3K99; X-ray; 2.10 A; A/B/C/D=9-225 PDB 3MNR; X-ray; 1.90 A; P=1-232 PDB 3O0I; X-ray; 1.47 A; A=1-236 PDB 3OW6; X-ray; 1.80 A; A=17-223 PDB 3OWB; X-ray; 2.05 A; A=17-223 PDB 3OWD; X-ray; 1.63 A; A=17-223 PDB 3Q6M; X-ray; 3.00 A; A/B/C=293-732 PDB 3Q6N; X-ray; 3.05 A; A/B/C/D/E/F=293-732 PDB 3QDD; X-ray; 1.79 A; A=1-236 PDB 3QTF; X-ray; 1.57 A; A=14-236 PDB 3R4M; X-ray; 1.70 A; A=9-236 PDB 3R4N; X-ray; 2.00 A; A/B=9-225 PDB 3R4O; X-ray; 2.65 A; A/B=9-225 PDB 3R4P; X-ray; 1.70 A; A/B=9-225 PDB 3R91; X-ray; 1.58 A; A=14-236 PDB 3R92; X-ray; 1.58 A; A=14-236 PDB 3RKZ; X-ray; 1.57 A; A=14-236 PDB 3RLP; X-ray; 1.70 A; A/B=9-225 PDB 3RLQ; X-ray; 1.90 A; A/B=9-225 PDB 3RLR; X-ray; 1.70 A; A/B=9-225 PDB 3T0H; X-ray; 1.20 A; A=9-236 PDB 3T0Z; X-ray; 2.19 A; A=9-236 PDB 3T10; X-ray; 1.24 A; A=9-236 PDB 3T1K; X-ray; 1.50 A; A/B=9-236 PDB 3T2S; X-ray; 1.50 A; A/B=9-236 PDB 3TUH; X-ray; 1.80 A; A/B=16-224 PDB 3VHA; X-ray; 1.39 A; A=9-236 PDB 3VHC; X-ray; 1.41 A; A=9-236 PDB 3VHD; X-ray; 1.52 A; A/B=9-236 PDB 3WHA; X-ray; 1.30 A; A/B=9-236 PDB 3WQ9; X-ray; 1.80 A; A=1-236 PDB 4AIF; X-ray; 2.01 A; D/E=726-732 PDB 4AWO; X-ray; 1.70 A; A/B=9-236 PDB 4AWP; X-ray; 1.82 A; A/B=9-236 PDB 4AWQ; X-ray; 1.60 A; A/B=9-236 PDB 4B7P; X-ray; 1.70 A; A=9-236 PDB 4BQG; X-ray; 1.90 A; A=9-236 PDB 4BQJ; X-ray; 2.00 A; A=9-236 PDB 4CGQ; X-ray; 2.00 A; Q=726-732 PDB 4CGU; X-ray; 2.11 A; C=726-732 PDB 4CGV; X-ray; 2.54 A; E/F=726-732 PDB 4CGW; X-ray; 3.00 A; C/D=726-732 PDB 4CWF; X-ray; 2.00 A; A=9-236 PDB 4CWN; X-ray; 1.80 A; A=9-236 PDB 4CWO; X-ray; 2.31 A; A=9-236 PDB 4CWP; X-ray; 1.95 A; A=9-236 PDB 4CWQ; X-ray; 2.00 A; A=9-236 PDB 4CWR; X-ray; 2.00 A; A=9-236 PDB 4CWS; X-ray; 2.30 A; A=9-236 PDB 4CWT; X-ray; 1.90 A; A=9-236 PDB 4EEH; X-ray; 1.60 A; A=9-236 PDB 4EFT; X-ray; 2.12 A; A=9-236 PDB 4EFU; X-ray; 2.00 A; A=9-236 PDB 4EGH; X-ray; 1.60 A; A=9-236 PDB 4EGI; X-ray; 1.79 A; A=9-236 PDB 4EGK; X-ray; 1.69 A; A=9-236 PDB 4FCP; X-ray; 2.00 A; A/B=1-236 PDB 4FCQ; X-ray; 2.15 A; A=1-236 PDB 4FCR; X-ray; 1.70 A; A=1-236 PDB 4HY6; X-ray; 1.65 A; A=9-236 PDB 4JQL; X-ray; 1.72 A; A=9-236 PDB 4L8Z; X-ray; 1.70 A; A=9-236 PDB 4L90; X-ray; 2.00 A; A=9-236 PDB 4L91; X-ray; 1.75 A; A=9-236 PDB 4L93; X-ray; 1.84 A; A/B=9-236 PDB 4L94; X-ray; 1.65 A; A=9-236 PDB 4LWE; X-ray; 1.50 A; A=17-224 PDB 4LWF; X-ray; 1.75 A; A=17-224 PDB 4LWG; X-ray; 1.60 A; A=17-224 PDB 4LWH; X-ray; 1.70 A; A=16-224 PDB 4LWI; X-ray; 1.70 A; A=17-224 PDB 4NH7; X-ray; 2.00 A; A/B=9-236 PDB 4NH8; X-ray; 1.65 A; A=9-236 PDB 4O04; X-ray; 1.82 A; A=9-236 PDB 4O05; X-ray; 1.79 A; A=9-236 PDB 4O07; X-ray; 1.86 A; A=9-236 PDB 4O09; X-ray; 1.96 A; A=9-236 PDB 4O0B; X-ray; 1.93 A; A=9-236 PDB 4R3M; X-ray; 1.80 A; A=16-224 PDB 4U93; X-ray; 1.55 A; A=1-236 PDB 4W7T; X-ray; 1.80 A; A=1-236 PDB 4XIP; X-ray; 1.70 A; A=9-236 PDB 4XIQ; X-ray; 1.84 A; A=9-236 PDB 4XIR; X-ray; 1.70 A; A=9-236 PDB 4XIT; X-ray; 1.86 A; A=9-236 PDB 4YKQ; X-ray; 1.91 A; A=2-236 PDB 4YKR; X-ray; 1.61 A; A=2-236 PDB 4YKT; X-ray; 1.85 A; A=2-236 PDB 4YKU; X-ray; 1.70 A; A=2-236 PDB 4YKW; X-ray; 1.85 A; A/B=2-236 PDB 4YKX; X-ray; 1.80 A; A=2-236 PDB 4YKY; X-ray; 1.78 A; A=2-236 PDB 4YKZ; X-ray; 1.85 A; A=2-236 PDB 5CF0; X-ray; 1.80 A; A=9-236 PDB 5FNC; X-ray; 2.20 A; A=1-236 PDB 5FND; X-ray; 2.00 A; A=1-236 PDB 5FNF; X-ray; 2.10 A; A=1-236 PDBsum 1BYQ; -; . PDBsum 1OSF; -; . PDBsum 1UY6; -; . PDBsum 1UY7; -; . PDBsum 1UY8; -; . PDBsum 1UY9; -; . PDBsum 1UYC; -; . PDBsum 1UYD; -; . PDBsum 1UYE; -; . PDBsum 1UYF; -; . PDBsum 1UYG; -; . PDBsum 1UYH; -; . PDBsum 1UYI; -; . PDBsum 1UYK; -; . PDBsum 1UYL; -; . PDBsum 1YC1; -; . PDBsum 1YC3; -; . PDBsum 1YC4; -; . PDBsum 1YER; -; . PDBsum 1YES; -; . PDBsum 1YET; -; . PDBsum 2BSM; -; . PDBsum 2BT0; -; . PDBsum 2BUG; -; . PDBsum 2BYH; -; . PDBsum 2BYI; -; . PDBsum 2BZ5; -; . PDBsum 2C2L; -; . PDBsum 2CCS; -; . PDBsum 2CCT; -; . PDBsum 2CCU; -; . PDBsum 2FWY; -; . PDBsum 2FWZ; -; . PDBsum 2H55; -; . PDBsum 2JJC; -; . PDBsum 2K5B; -; . PDBsum 2QF6; -; . PDBsum 2QFO; -; . PDBsum 2QG0; -; . PDBsum 2QG2; -; . PDBsum 2UWD; -; . PDBsum 2VCI; -; . PDBsum 2VCJ; -; . PDBsum 2WI1; -; . PDBsum 2WI2; -; . PDBsum 2WI3; -; . PDBsum 2WI4; -; . PDBsum 2WI5; -; . PDBsum 2WI6; -; . PDBsum 2WI7; -; . PDBsum 2XAB; -; . PDBsum 2XDK; -; . PDBsum 2XDL; -; . PDBsum 2XDS; -; . PDBsum 2XDU; -; . PDBsum 2XDX; -; . PDBsum 2XHR; -; . PDBsum 2XHT; -; . PDBsum 2XHX; -; . PDBsum 2XJG; -; . PDBsum 2XJJ; -; . PDBsum 2XJX; -; . PDBsum 2XK2; -; . PDBsum 2YE2; -; . PDBsum 2YE3; -; . PDBsum 2YE4; -; . PDBsum 2YE5; -; . PDBsum 2YE6; -; . PDBsum 2YE7; -; . PDBsum 2YE8; -; . PDBsum 2YE9; -; . PDBsum 2YEA; -; . PDBsum 2YEB; -; . PDBsum 2YEC; -; . PDBsum 2YED; -; . PDBsum 2YEE; -; . PDBsum 2YEF; -; . PDBsum 2YEG; -; . PDBsum 2YEH; -; . PDBsum 2YEI; -; . PDBsum 2YEJ; -; . PDBsum 2YI0; -; . PDBsum 2YI5; -; . PDBsum 2YI6; -; . PDBsum 2YI7; -; . PDBsum 2YJW; -; . PDBsum 2YJX; -; . PDBsum 2YK2; -; . PDBsum 2YK9; -; . PDBsum 2YKB; -; . PDBsum 2YKC; -; . PDBsum 2YKE; -; . PDBsum 2YKI; -; . PDBsum 2YKJ; -; . PDBsum 3B24; -; . PDBsum 3B25; -; . PDBsum 3B26; -; . PDBsum 3B27; -; . PDBsum 3B28; -; . PDBsum 3BM9; -; . PDBsum 3BMY; -; . PDBsum 3D0B; -; . PDBsum 3EKO; -; . PDBsum 3EKR; -; . PDBsum 3FT5; -; . PDBsum 3FT8; -; . PDBsum 3HEK; -; . PDBsum 3HHU; -; . PDBsum 3HYY; -; . PDBsum 3HYZ; -; . PDBsum 3HZ1; -; . PDBsum 3HZ5; -; . PDBsum 3INW; -; . PDBsum 3INX; -; . PDBsum 3K97; -; . PDBsum 3K98; -; . PDBsum 3K99; -; . PDBsum 3MNR; -; . PDBsum 3O0I; -; . PDBsum 3OW6; -; . PDBsum 3OWB; -; . PDBsum 3OWD; -; . PDBsum 3Q6M; -; . PDBsum 3Q6N; -; . PDBsum 3QDD; -; . PDBsum 3QTF; -; . PDBsum 3R4M; -; . PDBsum 3R4N; -; . PDBsum 3R4O; -; . PDBsum 3R4P; -; . PDBsum 3R91; -; . PDBsum 3R92; -; . PDBsum 3RKZ; -; . PDBsum 3RLP; -; . PDBsum 3RLQ; -; . PDBsum 3RLR; -; . PDBsum 3T0H; -; . PDBsum 3T0Z; -; . PDBsum 3T10; -; . PDBsum 3T1K; -; . PDBsum 3T2S; -; . PDBsum 3TUH; -; . PDBsum 3VHA; -; . PDBsum 3VHC; -; . PDBsum 3VHD; -; . PDBsum 3WHA; -; . PDBsum 3WQ9; -; . PDBsum 4AIF; -; . PDBsum 4AWO; -; . PDBsum 4AWP; -; . PDBsum 4AWQ; -; . PDBsum 4B7P; -; . PDBsum 4BQG; -; . PDBsum 4BQJ; -; . PDBsum 4CGQ; -; . PDBsum 4CGU; -; . PDBsum 4CGV; -; . PDBsum 4CGW; -; . PDBsum 4CWF; -; . PDBsum 4CWN; -; . PDBsum 4CWO; -; . PDBsum 4CWP; -; . PDBsum 4CWQ; -; . PDBsum 4CWR; -; . PDBsum 4CWS; -; . PDBsum 4CWT; -; . PDBsum 4EEH; -; . PDBsum 4EFT; -; . PDBsum 4EFU; -; . PDBsum 4EGH; -; . PDBsum 4EGI; -; . PDBsum 4EGK; -; . PDBsum 4FCP; -; . PDBsum 4FCQ; -; . PDBsum 4FCR; -; . PDBsum 4HY6; -; . PDBsum 4JQL; -; . PDBsum 4L8Z; -; . PDBsum 4L90; -; . PDBsum 4L91; -; . PDBsum 4L93; -; . PDBsum 4L94; -; . PDBsum 4LWE; -; . PDBsum 4LWF; -; . PDBsum 4LWG; -; . PDBsum 4LWH; -; . PDBsum 4LWI; -; . PDBsum 4NH7; -; . PDBsum 4NH8; -; . PDBsum 4O04; -; . PDBsum 4O05; -; . PDBsum 4O07; -; . PDBsum 4O09; -; . PDBsum 4O0B; -; . PDBsum 4R3M; -; . PDBsum 4U93; -; . PDBsum 4W7T; -; . PDBsum 4XIP; -; . PDBsum 4XIQ; -; . PDBsum 4XIR; -; . PDBsum 4XIT; -; . PDBsum 4YKQ; -; . PDBsum 4YKR; -; . PDBsum 4YKT; -; . PDBsum 4YKU; -; . PDBsum 4YKW; -; . PDBsum 4YKX; -; . PDBsum 4YKY; -; . PDBsum 4YKZ; -; . PDBsum 5CF0; -; . PDBsum 5FNC; -; . PDBsum 5FND; -; . PDBsum 5FNF; -; . ProteinModelPortal P07900; -; . SMR P07900; -; . BioGrid 109552; 803; . DIP DIP-27595N; -; . IntAct P07900; 225; . MINT MINT-132070; -; . STRING 9606.ENSP00000335153; -; . BindingDB P07900; -; . ChEMBL CHEMBL3880; -; . DrugBank DB07317; (3E)-3-[(phenylamino)methylidene]dihydrofuran-2(3H)-one; . DrugBank DB03080; 17-Dmag; . DrugBank DB08786; 4-(2-methoxyethoxy)-6-methylpyrimidin-2-amine; . DrugBank DB03809; 9-Butyl-8-(3-Methoxybenzyl)-9h-Purin-6-Amine; . DrugBank DB03899; 9-Butyl-8-(4-Methoxybenzyl)-9h-Purin-6-Amine; . DrugBank DB05134; CNF1010; . DrugBank DB02424; Geldanamycin; . DrugBank DB07325; N-[(2-AMINO-6-METHYLPYRIMIDIN-4-YL)METHYL]-3-{[(E)-(2-OXODIHYDROFURAN-3(2H)-YLIDENE)METHYL]AMINO}BENZENESULFONAMIDE; . DrugBank DB00716; Nedocromil; . DrugBank DB00615; Rifabutin; . DrugBank DB06070; SNX-5422; . GuidetoPHARMACOLOGY 2905; -; . iPTMnet P07900; -; . PhosphoSitePlus P07900; -; . SwissPalm P07900; -; . BioMuta HSP90AA1; -; . DMDM 92090606; -; . OGP P07900; -; . REPRODUCTION-2DPAGE IPI00784295; -; . EPD P07900; -; . MaxQB P07900; -; . PaxDb P07900; -; . PeptideAtlas P07900; -; . PRIDE P07900; -; . TopDownProteomics P07900-1; -. [P07900-1]; . Ensembl ENST00000216281; ENSP00000216281; ENSG00000080824. [P07900-1]; . Ensembl ENST00000334701; ENSP00000335153; ENSG00000080824. [P07900-2]; . GeneID 3320; -; . KEGG hsa:3320; -; . UCSC uc001yku.5; human. [P07900-1]; . CTD 3320; -; . DisGeNET 3320; -; . GeneCards HSP90AA1; -; . HGNC HGNC:5253; HSP90AA1; . HPA CAB002058; -; . MIM 140571; gene; . neXtProt NX_P07900; -; . OpenTargets ENSG00000080824; -; . PharmGKB PA29519; -; . eggNOG KOG0019; Eukaryota; . eggNOG KOG0020; Eukaryota; . eggNOG COG0326; LUCA; . GeneTree ENSGT00840000129758; -; . HOVERGEN HBG007374; -; . InParanoid P07900; -; . KO K04079; -; . OMA CERPAIS; -; . OrthoDB EOG091G0270; -; . PhylomeDB P07900; -; . TreeFam TF300686; -; . Reactome R-HSA-1227986; Signaling by ERBB2; . Reactome R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants; . Reactome R-HSA-1474151; Tetrahydrobiopterin (BH4) synthesis; recycling; salvage and regulation Reactome R-HSA-192905; vRNP Assembly; . Reactome R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation; . Reactome R-HSA-203615; eNOS activation; . Reactome R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition; . Reactome R-HSA-3000484; Scavenging by Class F Receptors; . Reactome R-HSA-3371511; HSF1 activation; . Reactome R-HSA-3371568; Attenuation phase; . Reactome R-HSA-3371571; HSF1-dependent transactivation; . Reactome R-HSA-380259; Loss of Nlp from mitotic centrosomes; . Reactome R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes; . Reactome R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome; . Reactome R-HSA-3928663; EPHA-mediated growth cone collapse; . Reactome R-HSA-399954; Sema3A PAK dependent Axon repulsion; . Reactome R-HSA-4420097; VEGFA-VEGFR2 Pathway; . Reactome R-HSA-5218920; VEGFR2 mediated vascular permeability; . Reactome R-HSA-5336415; Uptake and function of diphtheria toxin; . Reactome R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis; . Reactome R-HSA-5620912; Anchoring of the basal body to the plasma membrane; . Reactome R-HSA-5637810; Constitutive Signaling by EGFRvIII; . Reactome R-HSA-6785807; Interleukin-4 and 13 signaling; . Reactome R-HSA-6798695; Neutrophil degranulation; . Reactome R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint; . Reactome R-HSA-8854518; AURKA Activation by TPX2; . Reactome R-HSA-8863795; Downregulation of ERBB2 signaling; . SIGNOR P07900; -; . ChiTaRS HSP90AA1; human; . EvolutionaryTrace P07900; -; . GenomeRNAi 3320; -; . PMAP-CutDB P07900; -; . PRO PR:P07900; -; . Proteomes UP000005640; Chromosome 14; . Bgee ENSG00000080824; -; . CleanEx HS_HSP90AA1; -; . ExpressionAtlas P07900; baseline and differential; . Genevisible P07900; HS; . GO GO:0005737; C:cytoplasm; ISS:AgBase; . GO GO:0005829; C:cytosol; NAS:UniProtKB; . GO GO:0071682; C:endocytic vesicle lumen; TAS:Reactome; . GO GO:0070062; C:extracellular exosome; IDA:UniProtKB; . GO GO:0005576; C:extracellular region; TAS:Reactome; . GO GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome; . GO GO:0043202; C:lysosomal lumen; TAS:ParkinsonsUK-UCL; . GO GO:0042470; C:melanosome; IEA:UniProtKB-SubCell; . GO GO:0016020; C:membrane; IDA:UniProtKB; . GO GO:0043209; C:myelin sheath; IEA:Ensembl; . GO GO:0005654; C:nucleoplasm; TAS:Reactome; . GO GO:0005634; C:nucleus; IDA:UniProtKB; . GO GO:0005886; C:plasma membrane; TAS:Reactome; . GO GO:0032587; C:ruffle membrane; IEA:Ensembl; . GO GO:0034774; C:secretory granule lumen; TAS:Reactome; . GO GO:0005524; F:ATP binding; IDA:UniProtKB; . GO GO:0016887; F:ATPase activity; IDA:UniProtKB; . GO GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL; . GO GO:0051020; F:GTPase binding; IPI:UniProtKB; . GO GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL; . GO GO:0042802; F:identical protein binding; IPI:IntAct; . GO GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB; . GO GO:0030235; F:nitric-oxide synthase regulator activity; IDA:UniProtKB; . GO GO:0000166; F:nucleotide binding; TAS:UniProtKB; . GO GO:0042803; F:protein homodimerization activity; TAS:UniProtKB; . GO GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome; . GO GO:1990782; F:protein tyrosine kinase binding; IPI:UniProtKB; . GO GO:0003723; F:RNA binding; IDA:UniProtKB; . GO GO:0030911; F:TPR domain binding; IDA:UniProtKB; . GO GO:0061684; P:chaperone-mediated autophagy; TAS:ParkinsonsUK-UCL; . GO GO:0051131; P:chaperone-mediated protein complex assembly; IDA:BHF-UCL; . GO GO:0097711; P:ciliary basal body docking; TAS:Reactome; . GO GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome; . GO GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome; . GO GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome; . GO GO:0006839; P:mitochondrial transport; TAS:UniProtKB; . GO GO:0043312; P:neutrophil degranulation; TAS:Reactome; . GO GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB; . GO GO:0051973; P:positive regulation of telomerase activity; IDA:BHF-UCL; . GO GO:0045040; P:protein import into mitochondrial outer membrane; IDA:BHF-UCL; . GO GO:0042026; P:protein refolding; TAS:UniProtKB; . GO GO:0050821; P:protein stabilization; IMP:UniProtKB; . GO GO:0043335; P:protein unfolding; NAS:ParkinsonsUK-UCL; . GO GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome; . GO GO:1900034; P:regulation of cellular response to heat; TAS:Reactome; . GO GO:0050999; P:regulation of nitric-oxide synthase activity; TAS:Reactome; . GO GO:0043254; P:regulation of protein complex assembly; NAS:ParkinsonsUK-UCL; . GO GO:0031396; P:regulation of protein ubiquitination; IDA:BHF-UCL; . GO GO:0046677; P:response to antibiotic; ISS:AgBase; . GO GO:0009409; P:response to cold; ISS:AgBase; . GO GO:0009408; P:response to heat; ISS:AgBase; . GO GO:0006986; P:response to unfolded protein; NAS:UniProtKB; . GO GO:0007165; P:signal transduction; NAS:UniProtKB; . GO GO:1905323; P:telomerase holoenzyme complex assembly; IDA:BHF-UCL; . GO GO:0007004; P:telomere maintenance via telomerase; IDA:BHF-UCL; . GO GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome; . Gene3D 3.30.565.10; -; 2; . HAMAP MF_00505; HSP90; 1; . InterPro IPR003594; HATPase_C; . InterPro IPR019805; Heat_shock_protein_90_CS; . InterPro IPR001404; Hsp90_fam; . InterPro IPR020575; Hsp90_N; . InterPro IPR020568; Ribosomal_S5_D2-typ_fold; . PANTHER PTHR11528; PTHR11528; 1; . Pfam PF02518; HATPase_c; 1; . Pfam PF00183; HSP90; 1; . PIRSF PIRSF002583; Hsp90; 1; . PRINTS PR00775; HEATSHOCK90; . SMART SM00387; HATPase_c; 1; . SUPFAM SSF54211; SSF54211; 1; . SUPFAM SSF55874; SSF55874; 1; . PROSITE PS00298; HSP90; 1; .

Gateways to other related servers

• The World-2DPAGE Constellation - Entry point to the world-wide 2-DPAGE resources.
• World-2DPAGE Repository - A public repository for gel-based proteomics data linked to protein identification published in the literature.
• World-2DPAGE Portal - A dynamic portal to query simultaneously world-wide gel-based proteomics databases.
• SWISS-2DPAGE - The Geneva Two-dimensional polyacrylamide gel electrophoresis database.
• ExPASy - The resources web server of the Swiss Institute of Bioinformatics

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