Rab33b
entrez
19338
canonical
uniprot
O35963
canonical
ensembl
ENSMUSG00000027739
resolver
ensp
ENSMUSP00000063054
resolver
enst
ENSMUST00000054387
resolver
genesymbol
Rab33b
resolver
genesymbol_syn
Rab33B
resolver
uniprot
Q0PD21
resolver
uniprot
Q3TWI8
resolver
uniprot_entry
Q0PD21_MOUSE
resolver
uniprot_entry
RB33B_MOUSE
resolver
uniprot_sec
Q3TWI8
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) such as SGSM2 which increase the GTP hydrolysis activity. Inhibited by GDP dissociation inhibitors (GDIs). {ECO:0000250|UniProtKB:Q9H082}.
uniprot
proteins
amino_acid_sequence
MTSEMESSLEVSFSSSCAVSGASGCLPPARSRIFKIIVIGDSNVGKTCLTYRFCAGRFPDRTEATIGVDFRERAVDIDGERIKIQLWDTAGQERFRKSMVQHYYRNVHAVVFVYDMTNMASFHSLPAWIEECKQHLLANDIPRILVGNKCDLRSAIQVPTDLAQKFADTHSMPLFETSAKNPNDNDHVEAIFMTLAHKLKSHKPLMLSQLPDNRISLKPETKPAVTCWC
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 sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:16855591). RAB33B acts, in coordination with RAB6A, to regulate intra-Golgi retrograde trafficking (By similarity). Participates in autophagosome formation by recruiting the ATG12-ATG5-ATG16L1 complex to phagophores, probably in a nucleotide-independent manner (PubMed:18448665). {ECO:0000250|UniProtKB:Q9H082, ECO:0000269|PubMed:16855591, ECO:0000269|PubMed:18448665}.
uniprot
proteins
mass_dalton
25767
uniprot
proteins
mutagenesis
MUTAGEN 47; /note="T->N: Affects interaction with ATG16L1."; /evidence="ECO:0000269|PubMed:18448665"; MUTAGEN 92; /note="Q->A: Decreased GTPase catalytic efficiency."; /evidence="ECO:0000269|PubMed:16855591"; MUTAGEN 92; /note="Q->L: Does not affect interaction with ATG16L1. Induces lipidation of LC3. Decreased GTPase catalytic efficiency."; /evidence="ECO:0000269|PubMed:16855591, ECO:0000269|PubMed:18448665
uniprot
proteins
post_translational_modification
PTM: Prenylated. {ECO:0000250|UniProtKB:Q9H082}.
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16034420
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16855591
uniprot
proteins
pubmed
18448665
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22082872
uniprot
proteins
pubmed
9512502
uniprot
proteins
sequence_length
229
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:18448665, ECO:0000269|PubMed:9512502}; Lipid-anchor {ECO:0000305}. Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:18448665}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q9H082}. Note=Under starvation conditions punctate RAB33B-positive structures are often observed in the cytoplasm (PubMed:9512502). Under starved conditions RAB33B translocates from the Golgi to phagophores; this translocation is driven by interaction with ATG16L1 (By similarity). {ECO:0000250|UniProtKB:Q9H082, ECO:0000269|PubMed:9512502}.
uniprot
proteins