P61020 · RAB5B_HUMAN
- ProteinRas-related protein Rab-5B
- GeneRAB5B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids215 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic activity
- GTP + H2O = GDP + H+ + phosphateThis reaction proceeds in the forward direction.
Activity regulation
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 27-35 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GESAVGKSS | ||||||
Binding site | 46-52 | GTP (UniProtKB | ChEBI) | ||||
Sequence: HEYQEST | ||||||
Binding site | 75-79 | GTP (UniProtKB | ChEBI) | ||||
Sequence: DTAGQ | ||||||
Binding site | 133-136 | GTP (UniProtKB | ChEBI) | ||||
Sequence: NKAD | ||||||
Binding site | 163-165 | GTP (UniProtKB | ChEBI) | ||||
Sequence: SAK |
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 | early endosome | |
Cellular Component | early endosome membrane | |
Cellular Component | endocytic vesicle | |
Cellular Component | endomembrane system | |
Cellular Component | endosome | |
Cellular Component | extracellular exosome | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | melanosome | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Cellular Component | secretory granule membrane | |
Cellular Component | synaptic vesicle membrane | |
Molecular Function | G protein activity | |
Molecular Function | GDP binding | |
Molecular Function | GTP binding | |
Molecular Function | GTP-dependent protein binding | |
Molecular Function | GTPase activity | |
Biological Process | antigen processing and presentation | |
Biological Process | endocytosis | |
Biological Process | endosome organization | |
Biological Process | intracellular protein transport | |
Biological Process | plasma membrane to endosome transport | |
Biological Process | regulation of endocytosis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRas-related protein Rab-5B
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP61020
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 34 | Constitutively inactivated. Strongly reduces interaction with RIN2. | ||||
Sequence: S → N | ||||||
Mutagenesis | 79 | Constitutively active. | ||||
Sequence: Q → L | ||||||
Mutagenesis | 84 | Loss of phosphorylation. No effect on GDI1, GDI2, CHML and CHM binding. | ||||
Sequence: S → A | ||||||
Mutagenesis | 84 | Phosphomimetic mutant. Loss of GDI1, GDI2, CHML and CHM binding. | ||||
Sequence: S → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 219 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data), lipidation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylthreonine | ||||
Sequence: T | |||||||
Chain | PRO_0000121107 | 2-215 | UniProt | Ras-related protein Rab-5B | |||
Sequence: TSRSTARPNGQPQASKICQFKLVLLGESAVGKSSLVLRFVKGQFHEYQESTIGAAFLTQSVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNQETFARAKTWVKELQRQASPSIVIALAGNKADLANKRMVEYEEAQAYADDNSLLFMETSAKTAMNVNDLFLAIAKKLPKSEPQNLGGAAGRSRGVDLHEQSQQNKSQCCSN | |||||||
Modified residue (large scale data) | 29 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 82 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 84 | UniProt | Phosphoserine; by LRRK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 123 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 205 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Lipidation | 212 | UniProt | S-geranylgeranyl cysteine | ||||
Sequence: C | |||||||
Lipidation | 213 | UniProt | S-geranylgeranyl cysteine | ||||
Sequence: C |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with RIN2 and RIN3, which probably regulate its pathway, possibly by acting as GEFs (PubMed:11733506).
Interacts with GDI1, GDI2, CHML and CHM; phosphorylation at Ser-84 disrupts this interaction (PubMed:29125462).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P61020 | EEA1 Q15075 | 3 | EBI-399401, EBI-298113 | |
BINARY | P61020 | FHIP1B Q8N612 | 4 | EBI-399401, EBI-742137 | |
BINARY | P61020 | HTT P42858 | 3 | EBI-399401, EBI-466029 | |
BINARY | P61020 | LRRK2 Q5S007 | 9 | EBI-399401, EBI-5323863 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 49-57 | Effector region | ||||
Sequence: QESTIGAAF | ||||||
Region | 186-215 | Disordered | ||||
Sequence: PQNLGGAAGRSRGVDLHEQSQQNKSQCCSN | ||||||
Compositional bias | 200-215 | Polar residues | ||||
Sequence: DLHEQSQQNKSQCCSN |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P61020-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length215
- Mass (Da)23,707
- Last updated2004-04-26 v1
- ChecksumD47AD834BCF8B591
P61020-2
- Name2
- Differences from canonical
- 106-146: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_045301 | 106-146 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 200-215 | Polar residues | ||||
Sequence: DLHEQSQQNKSQCCSN |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X54871 EMBL· GenBank· DDBJ | CAA38653.1 EMBL· GenBank· DDBJ | mRNA | ||
AF498937 EMBL· GenBank· DDBJ | AAM21085.1 EMBL· GenBank· DDBJ | mRNA | ||
AK292597 EMBL· GenBank· DDBJ | BAF85286.1 EMBL· GenBank· DDBJ | mRNA | ||
AK296517 EMBL· GenBank· DDBJ | BAG59149.1 EMBL· GenBank· DDBJ | mRNA | ||
BX537408 EMBL· GenBank· DDBJ | CAD97650.1 EMBL· GenBank· DDBJ | mRNA | ||
AC034102 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471054 EMBL· GenBank· DDBJ | EAW96862.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471054 EMBL· GenBank· DDBJ | EAW96864.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC032740 EMBL· GenBank· DDBJ | AAH32740.1 EMBL· GenBank· DDBJ | mRNA | ||
BC040143 EMBL· GenBank· DDBJ | AAH40143.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC050558 EMBL· GenBank· DDBJ | AAH50558.2 EMBL· GenBank· DDBJ | mRNA | ||
BC056422 EMBL· GenBank· DDBJ | AAH56422.2 EMBL· GenBank· DDBJ | mRNA | ||
BC065298 EMBL· GenBank· DDBJ | AAH65298.2 EMBL· GenBank· DDBJ | mRNA |