RAB1A
entrez
5861
canonical
uniprot
P62820
canonical
ensembl
ENSG00000138069
resolver
ensp
ENSP00000381540
resolver
ensp
ENSP00000387286
resolver
ensp
ENSP00000557683
resolver
genesymbol
RAB1A
resolver
genesymbol_syn
RAB1
resolver
hgnc
HGNC:9758
resolver
uniprot
B7Z8M7
resolver
uniprot
D6W5F3
resolver
uniprot
P11476
resolver
uniprot
Q5U0I6
resolver
uniprot
Q6FIE7
resolver
uniprot
Q96N61
resolver
uniprot
Q9Y3T2
resolver
uniprot_entry
B7Z8M7_HUMAN
resolver
uniprot_entry
Q5U0I6_HUMAN
resolver
uniprot_entry
RAB1A_HUMAN
resolver
uniprot_sec
D6W5F3
resolver
uniprot_sec
P11476
resolver
uniprot_sec
Q6FIE7
resolver
uniprot_sec
Q96N61
resolver
uniprot_sec
Q9Y3T2
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 (Probable). Inhibited by GDP dissociation inhibitors (GDIs) (Probable). {ECO:0000305}.
uniprot
proteins
amino_acid_sequence
MSSMNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESFNNVKQWLQEIDRYASENVNKLLVGNKCDLTTKKVVDYTTAKEFADSLGIPFLETSAKNATNVEQSFMTMAAEIKKRMGPGATAGGAEKSNVKIQSTPVKQSGGGCC
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:20639577, PubMed:20861236, PubMed:21303926, PubMed:22939626). 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:20639577, PubMed:20861236, PubMed:21303926, PubMed:22939626). RAB1A regulates vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment and on to the cell surface, and plays a role in IL-8 and growth hormone secretion (PubMed:21303926). Required to modulate the compacted morphology of the Golgi (PubMed:26209634). Regulates the level of CASR present at the cell membrane (PubMed:20861236). Plays a role in cell adhesion and cell migration, via its role in protein trafficking (PubMed:20639577). Plays a role in autophagosome assembly and cellular defense reactions against pathogenic bacteria (PubMed:22939626). Plays a role in microtubule-dependent protein transport by early endosomes and in anterograde melanosome transport (By similarity). {ECO:0000250|UniProtKB:P62821, ECO:0000269|PubMed:20639577, ECO:0000269|PubMed:20861236, ECO:0000269|PubMed:21303926, ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:26209634}.
uniprot
proteins
mass_dalton
22678
uniprot
proteins
mutagenesis
MUTAGEN 49; /note="K->R: Promotes TLRs trafficking and TLRs-mediated signaling; when associated with A-61."; /evidence="ECO:0000269|PubMed:35343654"; MUTAGEN 61; /note="K->R: Promotes TLRs trafficking and TLRs-mediated signaling; when associated with A-49."; /evidence="ECO:0000269|PubMed:35343654"; MUTAGEN 72..74; /note="RFR->AFA: Abolished arginine GlcNAcylation; when associated with A-82 and A-111."; /evidence="ECO:0000269|PubMed:32504010"; MUTAGEN 74; /note="R->A: Abolished arginine GlcNAcylation; when associated with A-82 and A-111."; /evidence="ECO:0000269|PubMed:32974215"; MUTAGEN 82; /note="R->A: Abolished arginine GlcNAcylation; when associated with A-74 and A-111. Abolished arginine GlcNAcylation; when associated with 72-A--A-74 and A-111."; /evidence="ECO:0000269|PubMed:32504010, ECO:0000269|PubMed:32974215"; MUTAGEN 111; /note="R->A: Abolished arginine GlcNAcylation; when associated with A-74 and A-82. Abolished arginine GlcNAcylation; when associated with 72-A--A-74 and A-82."; /evidence="ECO:0000269|PubMed:32504010, ECO:0000269|PubMed:32974215"; MUTAGEN 124; /note="N->I: Dominant negative mutant. Strongly reduces the levels of CASR present at the cell-surface."; /evidence="ECO:0000269|PubMed:20861236
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by CDK1 kinase during mitosis. {ECO:0000269|PubMed:1902553, ECO:0000269|PubMed:21822290, ECO:0000269|PubMed:22158903}.; PTM: (Microbial infection) Phosphocholinated at Ser-79 by L.pneumophila AnkX, leading to displace GDP dissociation inhibitors (GDI) (PubMed:21822290). Both GDP-bound and GTP-bound forms can be phosphocholinated. Dephosphocholinated by L.pneumophila Lem3, restoring accessibility to L.pneumophila GTPase effector LepB (PubMed:22158903). {ECO:0000269|PubMed:21822290, ECO:0000269|PubMed:22158903}.; PTM: (Microbial infection) Glycosylated by S.typhimurium protein Ssek3: arginine GlcNAcylation prevents GTPase activity, thereby disrupting vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment. {ECO:0000269|PubMed:32504010, ECO:0000269|PubMed:32974215}.; PTM: Ubiquitinated via 'Lys-11'-linked ubiquitination on Lys-49 and Lys-61; impairing the recruitment of guanosine diphosphate (GDP) dissociation inhibitor 1/GDI1. {ECO:0000250|UniProtKB:P51153}.
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
17974005
uniprot
proteins
pubmed
1902553
uniprot
proteins
pubmed
19603039
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19942850
uniprot
proteins
pubmed
20176951
uniprot
proteins
pubmed
20639577
uniprot
proteins
pubmed
20861236
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21303926
uniprot
proteins
pubmed
21822290
uniprot
proteins
pubmed
22158903
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22416225
uniprot
proteins
pubmed
22939626
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23588383
uniprot
proteins
pubmed
23815289
uniprot
proteins
pubmed
23821544
uniprot
proteins
pubmed
2501306
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26209634
uniprot
proteins
pubmed
27334615
uniprot
proteins
pubmed
32504010
uniprot
proteins
pubmed
32974215
uniprot
proteins
pubmed
35343654
uniprot
proteins
pubmed
7991565
uniprot
proteins
sequence_length
205
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:22939626}. Endoplasmic reticulum {ECO:0000269|PubMed:22939626}. Early endosome {ECO:0000269|PubMed:21303926}. Cytoplasm, cytosol {ECO:0000305|PubMed:19942850}. Membrane {ECO:0000269|PubMed:19942850, ECO:0000269|PubMed:23815289}. Melanosome {ECO:0000250|UniProtKB:P62821}. Note=Alternates between membrane-associated and cytosolic forms. {ECO:0000305|PubMed:19942850}.
uniprot
proteins