P62820 · RAB1A_HUMAN
- ProteinRas-related protein Rab-1A
- GeneRAB1A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids205 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
Catalytic activity
- GTP + H2O = GDP + H+ + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 18-26 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GDSGVGKSC | ||||||
Binding site | 36-43 | GTP (UniProtKB | ChEBI) | ||||
Sequence: YTESYIST | ||||||
Binding site | 66-70 | GTP (UniProtKB | ChEBI) | ||||
Sequence: DTAGQ | ||||||
Binding site | 124-127 | GTP (UniProtKB | ChEBI) | ||||
Sequence: NKCD | ||||||
Binding site | 154-156 | GTP (UniProtKB | ChEBI) | ||||
Sequence: SAK |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRas-related protein Rab-1A
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP62820
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 49 | Promotes TLRs trafficking and TLRs-mediated signaling; when associated with A-61. | ||||
Sequence: K → R | ||||||
Mutagenesis | 61 | Promotes TLRs trafficking and TLRs-mediated signaling; when associated with A-49. | ||||
Sequence: K → R | ||||||
Mutagenesis | 72-74 | Abolished arginine GlcNAcylation; when associated with A-82 and A-111. | ||||
Sequence: RFR → AFA | ||||||
Mutagenesis | 74 | Abolished arginine GlcNAcylation; when associated with A-82 and A-111. | ||||
Sequence: R → A | ||||||
Mutagenesis | 82 | Abolished arginine GlcNAcylation; when associated with A-74 and A-111. Abolished arginine GlcNAcylation; when associated with 72-A--A-74 and A-111. | ||||
Sequence: R → A | ||||||
Mutagenesis | 111 | Abolished arginine GlcNAcylation; when associated with A-74 and A-82. Abolished arginine GlcNAcylation; when associated with 72-A--A-74 and A-82. | ||||
Sequence: R → A | ||||||
Mutagenesis | 124 | Dominant negative mutant. Strongly reduces the levels of CASR present at the cell-surface. | ||||
Sequence: N → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 108 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, modified residue (large scale data), chain, cross-link, glycosylation, lipidation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000121056 | 2-205 | UniProt | Ras-related protein Rab-1A | |||
Sequence: SSMNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESFNNVKQWLQEIDRYASENVNKLLVGNKCDLTTKKVVDYTTAKEFADSLGIPFLETSAKNATNVEQSFMTMAAEIKKRMGPGATAGGAEKSNVKIQSTPVKQSGGGCC | |||||||
Modified residue (large scale data) | 3 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Cross-link | 49 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 61 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Glycosylation | 72 | UniProt | (Microbial infection) N-beta-linked (GlcNAc) arginine | ||||
Sequence: R | |||||||
Glycosylation | 74 | UniProt | (Microbial infection) N-beta-linked (GlcNAc) arginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 75 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 77 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 78 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 79 | UniProt | (Microbial infection) O-(2-cholinephosphoryl)serine | ||||
Sequence: S | |||||||
Glycosylation | 82 | UniProt | (Microbial infection) N-beta-linked (GlcNAc) arginine | ||||
Sequence: R | |||||||
Glycosylation | 111 | UniProt | (Microbial infection) N-beta-linked (GlcNAc) arginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 114 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 188 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 194 | UniProt | Phosphoserine; by CDK1 | ||||
Sequence: S | |||||||
Lipidation | 204 | UniProt | S-geranylgeranyl cysteine | ||||
Sequence: C | |||||||
Lipidation | 205 | UniProt | S-geranylgeranyl cysteine | ||||
Sequence: C |
Post-translational modification
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).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with C9orf72; the interaction mediates recruitment of RAB1A to the ATG1/ULK1 kinase complex (PubMed:27334615).
Interacts with GDI1; this promotes dissociation from membranes (PubMed:20176951, PubMed:23815289).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P62820 | C9orf72 Q96LT7-1 | 5 | EBI-716845, EBI-16693635 | |
BINARY | P62820 | C9orf72 Q96LT7-2 | 4 | EBI-716845, EBI-16693673 | |
XENO | P62820 | drrA Q29ST3 | 2 | EBI-716845, EBI-15838677 | |
XENO | P62820 | drrA Q5ZSQ3 | 7 | EBI-716845, EBI-7632432 | |
BINARY | P62820 | GDI1 P31150 | 7 | EBI-716845, EBI-946999 | |
BINARY | P62820 | MTOR P42345 | 4 | EBI-716845, EBI-359260 | |
BINARY | P62820 | OCRL Q01968 | 8 | EBI-716845, EBI-6148898 | |
BINARY | P62820 | RABIF P47224 | 5 | EBI-716845, EBI-713992 | |
BINARY | P62820 | RPTOR Q8N122 | 4 | EBI-716845, EBI-1567928 | |
XENO | P62820 | setA Q5ZU30 | 3 | EBI-716845, EBI-40253342 | |
XENO | P62820-1 | drrA Q29ST3 | 3 | EBI-15666813, EBI-15838677 | |
BINARY | P62820-1 | GDI2 P50395 | 2 | EBI-15666813, EBI-1049143 | |
XENO | P62820-1 | lepB Q6X1Y7 | 2 | EBI-15666813, EBI-15666803 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 40-48 | Effector region | ||||
Sequence: YISTIGVDF | ||||||
Region | 178-205 | Disordered | ||||
Sequence: PGATAGGAEKSNVKIQSTPVKQSGGGCC | ||||||
Compositional bias | 187-205 | Polar residues | ||||
Sequence: KSNVKIQSTPVKQSGGGCC |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P62820-1
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.
- Name1
- Length205
- Mass (Da)22,678
- Last updated2007-01-23 v3
- ChecksumB2A8F4E3B0FB17D6
P62820-2
- Name2
- Differences from canonical
- 33-96: Missing
P62820-3
- Name3
- Differences from canonical
- 65-140: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E7END7 | E7END7_HUMAN | RAB1A | 173 |
Features
Showing features for alternative sequence, compositional bias.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M28209 EMBL· GenBank· DDBJ | AAA60240.1 EMBL· GenBank· DDBJ | mRNA | ||
AL050268 EMBL· GenBank· DDBJ | CAB43369.1 EMBL· GenBank· DDBJ | mRNA | ||
BX571747 EMBL· GenBank· DDBJ | CAE11872.1 EMBL· GenBank· DDBJ | mRNA | ||
AK055927 EMBL· GenBank· DDBJ | BAB71048.1 EMBL· GenBank· DDBJ | mRNA | ||
AF498929 EMBL· GenBank· DDBJ | AAM21077.1 EMBL· GenBank· DDBJ | mRNA | ||
CR533479 EMBL· GenBank· DDBJ | CAG38510.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471053 EMBL· GenBank· DDBJ | EAW99921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000905 EMBL· GenBank· DDBJ | AAH00905.1 EMBL· GenBank· DDBJ | mRNA |