RAB33B
entrez
83452
canonical
uniprot
Q9H082
canonical
ensembl
ENSG00000172007
resolver
ensp
ENSP00000306496
resolver
ensp
ENSP00000498778
resolver
ensp
ENSP00000543945
resolver
ensp
ENSP00000600432
resolver
enst
ENST00000305626
resolver
enst
ENST00000652268
resolver
enst
ENST00000873886
resolver
enst
ENST00000930373
resolver
genesymbol
RAB33B
resolver
hgnc
HGNC:16075
resolver
uniprot
A0A494C0Z5
resolver
uniprot
B2R987
resolver
uniprot
Q4W5B0
resolver
uniprot_entry
A0A494C0Z5_HUMAN
resolver
uniprot_entry
RB33B_HUMAN
resolver
uniprot_sec
B2R987
resolver
uniprot_sec
Q4W5B0
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP (Probable). Regulated by GTPase activating proteins (GAPs) such as SGSM2 which increase the GTP hydrolysis activity (PubMed:21808068). Inhibited by GDP dissociation inhibitors (GDIs) (Probable). {ECO:0000269|PubMed:21808068, ECO:0000305}.
uniprot
proteins
amino_acid_sequence
MAEEMESSLEASFSSSGAVSGASGFLPPARSRIFKIIVIGDSNVGKTCLTYRFCAGRFPDRTEATIGVDFRERAVEIDGERIKIQLWDTAGQERFRKSMVQHYYRNVHAVVFVYDMTNMASFHSLPSWIEECKQHLLANDIPRILVGNKCDLRSAIQVPTDLAQKFADTHSMPLFETSAKNPNDNDHVEAIFMTLAHKLKSHKPLMLSQPPDNGIILKPEPKPAMTCWC
uniprot
proteins
disease_involvement
DISEASE: Smith-McCort dysplasia 2 (SMC2) [MIM:615222]: A rare autosomal recessive osteochondrodysplasia with skeletal features identical to those of Dyggve-Melchior-Clausen syndrome, but with normal intelligence and no microcephaly. It is characterized by short limbs and trunk with barrel-shaped chest. The radiographic phenotype includes platyspondyly, generalized abnormalities of the epiphyses and metaphyses, and a distinctive lacy appearance of the iliac crest. {ECO:0000269|PubMed:22652534, ECO:0000269|PubMed:23042644}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (PubMed:20163571, PubMed:21808068). 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:18448665, PubMed:20163571, PubMed:21808068). RAB33B acts, in coordination with RAB6A, to regulate intra-Golgi retrograde trafficking (PubMed:20163571). Participates in autophagosome formation by recruiting the ATG12-ATG5-ATG16L1 complex to phagophores, probably in a nucleotide-independent manner (PubMed:18448665, PubMed:32960676). {ECO:0000269|PubMed:18448665, ECO:0000269|PubMed:20163571, ECO:0000269|PubMed:21808068, ECO:0000269|PubMed:32960676}.
uniprot
proteins
mass_dalton
25718
uniprot
proteins
mutagenesis
MUTAGEN 35; /note="K->A: Loss of interaction with ATG16L1. No change in prenylation activity. Loss of interaction with ATG12-ATG5-ATG16L1 complex and colocalization to phagophore; when associated with A-85."; /evidence="ECO:0000269|PubMed:32960676"; MUTAGEN 66; /note="I->A: Decreased binding affinity by 273-fold with ATG16L1. No change in prenylation activity. Loss of interaction with ATG16L1 and colocalization to phagophore; when associated with A-95."; /evidence="ECO:0000269|PubMed:32960676"; MUTAGEN 85; /note="Q->A: Loss of interaction with ATG16L1. No change in prenylation activity. Loss of interaction with ATG12-ATG5-ATG16L1 complex and colocalization to phagophore; when associated with A-35."; /evidence="ECO:0000269|PubMed:32960676"; MUTAGEN 95; /note="F->A: Decreased binding affinity by 179-fold with ATG16L1. No change in prenylation activity. Loss of interaction with ATG16L1 and colocalization to phagophore; when associated with A-66."; /evidence="ECO:0000269|PubMed:32960676
uniprot
proteins
post_translational_modification
PTM: Prenylated. {ECO:0000269|PubMed:32960676}.
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
18448665
uniprot
proteins
pubmed
20163571
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21808068
uniprot
proteins
pubmed
22652534
uniprot
proteins
pubmed
23042644
uniprot
proteins
pubmed
23091056
uniprot
proteins
pubmed
32960676
uniprot
proteins
sequence_length
229
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:32960676}; Lipid-anchor {ECO:0000305}. Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:18448665}. Preautophagosomal structure membrane {ECO:0000269|PubMed:32960676}. Note=Under starvation conditions punctate RAB33B-positive structures are often observed in the cytoplasm (By similarity). Under starved conditions RAB33B translocates from the Golgi to phagophores; this translocation is driven by interaction with ATG16L1 (PubMed:32960676). {ECO:0000250|UniProtKB:O35963, ECO:0000269|PubMed:32960676}.
uniprot
proteins