P61020 · RAB5B_HUMAN

  • Protein
    Ras-related protein Rab-5B
  • Gene
    RAB5B
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Protein transport. Probably involved in vesicular traffic.

Catalytic activity

Activity regulation

Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site27-35GTP (UniProtKB | ChEBI)
Binding site46-52GTP (UniProtKB | ChEBI)
Binding site75-79GTP (UniProtKB | ChEBI)
Binding site133-136GTP (UniProtKB | ChEBI)
Binding site163-165GTP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentearly endosome
Cellular Componentearly endosome membrane
Cellular Componentendocytic vesicle
Cellular Componentendomembrane system
Cellular Componentendosome
Cellular Componentextracellular exosome
Cellular Componentintracellular membrane-bounded organelle
Cellular Componentmelanosome
Cellular Componentmembrane
Cellular Componentplasma membrane
Cellular Componentsecretory granule membrane
Cellular Componentsynaptic vesicle membrane
Molecular FunctionG protein activity
Molecular FunctionGDP binding
Molecular FunctionGTP binding
Molecular FunctionGTP-dependent protein binding
Molecular FunctionGTPase activity
Biological Processantigen processing and presentation
Biological Processendocytosis
Biological Processendosome organization
Biological Processintracellular protein transport
Biological Processplasma membrane to endosome transport
Biological Processregulation of endocytosis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ras-related protein Rab-5B
  • EC number

Gene names

    • Name
      RAB5B

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    P61020
  • Secondary accessions
    • A8K982
    • B4DKD7
    • P35239
    • P35277
    • Q6PIK9

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis34Constitutively inactivated. Strongly reduces interaction with RIN2.
Mutagenesis79Constitutively active.
Mutagenesis84Loss of phosphorylation. No effect on GDI1, GDI2, CHML and CHM binding.
Mutagenesis84Phosphomimetic mutant. Loss of GDI1, GDI2, CHML and CHM binding.

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.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, modified residue (large scale data), lipidation.

TypeIDPosition(s)SourceDescription
Initiator methionine1UniProtRemoved
Modified residue2UniProtN-acetylthreonine
ChainPRO_00001211072-215UniProt
Modified residue (large scale data)29PRIDEPhosphoserine
Modified residue (large scale data)82PRIDEPhosphotyrosine
Modified residue84UniProtPhosphoserine; by LRRK2
Modified residue (large scale data)123PRIDEPhosphoserine
Modified residue (large scale data)205PRIDEPhosphoserine
Lipidation212UniProtS-geranylgeranyl cysteine
Lipidation213UniProtS-geranylgeranyl cysteine

Post-translational modification

Phosphorylation of Ser-84 in the switch II region by LRRK2 prevents the association of RAB regulatory proteins, including CHM, CHML and RAB GDP dissociation inhibitors GDI1 and GDI2.
(Microbial infection) Glycosylated on arginine residues by S.typhimurium protein Ssek3.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Binds EEA1 (PubMed:10491193).
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

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for motif, region, compositional bias.

TypeIDPosition(s)Description
Motif49-57Effector region
Region186-215Disordered
Compositional bias200-215Polar residues

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

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.

  • Length
    215
  • Mass (Da)
    23,707
  • Last updated
    2004-04-26 v1
  • Checksum
    D47AD834BCF8B591
MTSRSTARPNGQPQASKICQFKLVLLGESAVGKSSLVLRFVKGQFHEYQESTIGAAFLTQSVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNQETFARAKTWVKELQRQASPSIVIALAGNKADLANKRMVEYEEAQAYADDNSLLFMETSAKTAMNVNDLFLAIAKKLPKSEPQNLGGAAGRSRGVDLHEQSQQNKSQCCSN

P61020-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F8VWZ7F8VWZ7_HUMANRAB5B79
F8VVZ0F8VVZ0_HUMANRAB5B100
F8VUA5F8VUA5_HUMANRAB5B115
F8VPW9F8VPW9_HUMANRAB5B73

Sequence caution

The sequence AAH40143.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for alternative sequence, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_045301106-146in isoform 2
Compositional bias200-215Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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