RAB26
entrez
25837
canonical
uniprot
Q9ULW5
canonical
ensembl
ENSG00000167964
resolver
ensp
ENSP00000210187
resolver
ensp
ENSP00000441580
resolver
genesymbol
RAB26
resolver
hgnc
HGNC:14259
resolver
uniprot
B2RAA6
resolver
uniprot
Q3L6K5
resolver
uniprot
Q6NXS7
resolver
uniprot_entry
RAB26_HUMAN
resolver
uniprot_sec
B2RAA6
resolver
uniprot_sec
Q3L6K5
resolver
uniprot_sec
Q6NXS7
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP. Regulated by GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity. Inhibited by GDP dissociation inhibitors (GDIs). {ECO:0000305}.
uniprot
proteins
amino_acid_sequence
MSRKKTPKSKGASTPAASTLPTANGARPARSGTALSGPDAPPNGPLQPGRPSLGGGVDFYDVAFKVMLVGDSGVGKTCLLVRFKDGAFLAGTFISTVGIDFRNKVLDVDGVKVKLQMWDTAGQERFRSVTHAYYRDAHALLLLYDVTNKASFDNIQAWLTEIHEYAQHDVALMLLGNKVDSAHERVVKREDGEKLAKEYGLPFMETSAKTGLNVDLAFTAIAKELKQRSMKAPSEPRFRLHDYVKREGRGASCCRP
uniprot
proteins
ec_number
3.6.5.2
uniprot
proteins
function
FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). RAB26 mediates transport of ADRA2A and ADRA2B from the Golgi to the cell membrane (PubMed:23105096). Plays a role in the maturation of zymogenic granules and in pepsinogen secretion in the stomach (PubMed:20038531). Plays a role in the secretion of amylase from acinar granules in the parotid gland (By similarity). {ECO:0000250|UniProtKB:P51156, ECO:0000250|UniProtKB:P61006, ECO:0000269|PubMed:20038531, ECO:0000269|PubMed:23105096}.
uniprot
proteins
mass_dalton
27900
uniprot
proteins
mutagenesis
MUTAGEN 77; /note="T->N: Inactive, constitutively GDP-bound. Abolishes location at Golgi membranes. Impairs transport of ADRA2A and ADRA2B from the Golgi to the cell membrane."; /evidence="ECO:0000269|PubMed:20038531, ECO:0000269|PubMed:23105096"; MUTAGEN 123; /note="Q->L: Constitutively activated."; /evidence="ECO:0000269|PubMed:23105096"; MUTAGEN 177; /note="N->I: Inactive, due to loss of GNP binding. Abolishes location at Golgi membranes. Impairs transport of ADRA2A and ADRA2B from the Golgi to the cell membrane."; /evidence="ECO:0000269|PubMed:23105096
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
11043516
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
20038531
uniprot
proteins
pubmed
23105096
uniprot
proteins
sequence_length
256
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:23105096}; Lipid-anchor {ECO:0000269|PubMed:23105096}; Cytoplasmic side {ECO:0000269|PubMed:23105096}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000305|PubMed:23105096}; Lipid-anchor {ECO:0000305|PubMed:23105096}; Cytoplasmic side {ECO:0000305|PubMed:23105096}. Note=Not localized at the plasma membrane (By similarity). Inhibition of S-geranylgeranyl cysteine formation abolishes membrane location. {ECO:0000250|UniProtKB:P51156}.
uniprot
proteins