A0A7P0T917 · A0A7P0T917_HUMAN
- ProteinEndoplasmin
- GeneHSP90B1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids719 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 19 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 23 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 65 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 70 | ATP (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 78 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 84 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 85-86 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SG | ||||||
Binding site | 110-115 | ATP (UniProtKB | ChEBI) | ||||
Sequence: QFGVGF | ||||||
Binding site | 161 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 364 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | melanosome | |
Cellular Component | sarcoplasmic reticulum lumen | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent protein folding chaperone | |
Molecular Function | unfolded protein binding |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameEndoplasmin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A7P0T917
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 499 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 22 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 71 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 88 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 222 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 319 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 355 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 363 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 417 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 420 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 593 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 641 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 702 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 713 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-171 | Histidine kinase/HSP90-like ATPase | ||||
Sequence: NKEIFLRELISNASDALDKIRLISLTDENALSGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEA | ||||||
Region | 204-239 | Disordered | ||||
Sequence: TVEEPMEEEEAAKEEKEESDDEAAVEEEEEEKKPKT | ||||||
Compositional bias | 206-230 | Acidic residues | ||||
Sequence: EEPMEEEEAAKEEKEESDDEAAVEE | ||||||
Region | 666-719 | Disordered | ||||
Sequence: DPDAKVEEEPEEEPEETAEDTTEDTEQDEDEEMDVGTDEEEETAKESTAEKDEL | ||||||
Compositional bias | 670-706 | Acidic residues | ||||
Sequence: KVEEEPEEEPEETAEDTTEDTEQDEDEEMDVGTDEEE |
Sequence similarities
Belongs to the heat shock protein 90 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length719
- Mass (Da)83,014
- Last updated2021-06-02 v1
- ChecksumA3F9AC8F50F762DA
Computationally mapped potential isoform sequences
There are 16 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
P14625 | ENPL_HUMAN | HSP90B1 | 803 | ||
H0YIV0 | H0YIV0_HUMAN | HSP90B1 | 796 | ||
A0A7P0T8C8 | A0A7P0T8C8_HUMAN | HSP90B1 | 59 | ||
A0A7P0T8R3 | A0A7P0T8R3_HUMAN | HSP90B1 | 251 | ||
A0A7P0T823 | A0A7P0T823_HUMAN | HSP90B1 | 813 | ||
A0A7P0T885 | A0A7P0T885_HUMAN | HSP90B1 | 274 | ||
F8W026 | F8W026_HUMAN | HSP90B1 | 48 | ||
A0A7P0TAT8 | A0A7P0TAT8_HUMAN | HSP90B1 | 814 | ||
A0A7P0TAY2 | A0A7P0TAY2_HUMAN | HSP90B1 | 661 | ||
A0A7P0TBC2 | A0A7P0TBC2_HUMAN | HSP90B1 | 465 | ||
A0A7P0TAC2 | A0A7P0TAC2_HUMAN | HSP90B1 | 55 | ||
A0A7P0TAE1 | A0A7P0TAE1_HUMAN | HSP90B1 | 789 | ||
A0A7P0TAG4 | A0A7P0TAG4_HUMAN | HSP90B1 | 53 | ||
A0A7P0Z405 | A0A7P0Z405_HUMAN | HSP90B1 | 163 | ||
A0A7P0Z4B4 | A0A7P0Z4B4_HUMAN | HSP90B1 | 68 | ||
A0A087WT78 | A0A087WT78_HUMAN | HSP90B1 | 751 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 206-230 | Acidic residues | ||||
Sequence: EEPMEEEEAAKEEKEESDDEAAVEE | ||||||
Compositional bias | 670-706 | Acidic residues | ||||
Sequence: KVEEEPEEEPEETAEDTTEDTEQDEDEEMDVGTDEEE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC078819 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |