!!This displayer contains script commands. You should enable JavaScripting within your browser preferences, or use another browser!
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:
HS90A_HUMAN
USC-OGP 2-DE database
:
HS90A_HUMAN
HS90A_HUMAN
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
Database constructed and maintained by
Angel Garcia
, using the
Make2D-DB II
package (
ver. 3.10.2
) from the
World-2DPAGE Constellation
of the
ExPASy web server
[
Home
]