RAB35
entrez
11021
canonical
uniprot
Q15286
canonical
ensembl
ENSG00000111737
resolver
ensp
ENSP00000229340
resolver
ensp
ENSP00000441883
resolver
genesymbol
RAB35
resolver
genesymbol_syn
RAB1C
resolver
genesymbol_syn
RAY
resolver
hgnc
HGNC:9774
resolver
uniprot
B2R6E0
resolver
uniprot
B4E390
resolver
uniprot_entry
RAB35_HUMAN
resolver
uniprot_sec
B2R6E0
resolver
uniprot_sec
B4E390
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors (GEFs) including DENND1A, DENND1B and DENND1C which promote the exchange of bound GDP for free GTP (PubMed:20154091). Regulated by GTPase activating proteins (GAPs) including TBC1D10 and TBC1D13 which increase GTP hydrolysis activity (PubMed:30905672). Inhibited by GDP dissociation inhibitors (GDIs) which prevent Rab-GDP dissociation (Probable). {ECO:0000269|PubMed:20154091, ECO:0000269|PubMed:30905672, ECO:0000305}.
uniprot
proteins
amino_acid_sequence
MARDYDHLFKLLIIGDSGVGKSSLLLRFADNTFSGSYITTIGVDFKIRTVEINGEKVKLQIWDTAGQERFRTITSTYYRGTHGVIVVYDVTSAESFVNVKRWLHEINQNCDDVCRILVGNKNDDPERKVVETEDAYKFAGQMGIQLFETSAKENVNVEEMFNCITELVLRAKKDNLAKQQQQQQNDVVKLTKNSKRKKRCC
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:30905672). RAB35 is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane (PubMed:21951725). During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge (PubMed:16950109). May indirectly regulate neurite outgrowth. Together with TBC1D13 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes (By similarity). {ECO:0000250|UniProtKB:Q6PHN9, ECO:0000269|PubMed:16950109, ECO:0000269|PubMed:21951725, ECO:0000269|PubMed:30905672}.
uniprot
proteins
mass_dalton
23025
uniprot
proteins
mutagenesis
MUTAGEN 4; /note="D->A: Decreased interaction with RUSC2. No change in interaction with ACAP2, OCRL and MICAL1."; /evidence="ECO:0000269|PubMed:30905672"; MUTAGEN 5; /note="Y->A: Decreased interaction with RUSC2."; /evidence="ECO:0000269|PubMed:30905672"; MUTAGEN 10; /note="K->A: Loss of interaction with RUSC2."; /evidence="ECO:0000269|PubMed:30905672"; MUTAGEN 22; /note="S->N: Destabilization of the intercellular bridge during cytokinesis. Strong reduction in fast recycling."; /evidence="ECO:0000269|PubMed:16950109"; MUTAGEN 45; /note="F->A: Decreased interaction with ACAP2 and RUSC2."; /evidence="ECO:0000269|PubMed:30905672"; MUTAGEN 58; /note="K->A: Loss of interaction with RUSC2."; /evidence="ECO:0000269|PubMed:30905672"; MUTAGEN 60; /note="Q->A: Decreased interaction with RUSC2."; /evidence="ECO:0000269|PubMed:30905672"; MUTAGEN 62; /note="W->A: Loss of interaction with ACAP2 and RUSC2."; /evidence="ECO:0000269|PubMed:30905672"; MUTAGEN 67; /note="Q->L: Loss of GTPase activity. Increased fast recycling."; /evidence="ECO:0000269|PubMed:16950109"; MUTAGEN 72; /note="T->A: Loss of phosphorylation. No effect on binding to GDI1 and GDI2. Loss of interaction with ACAP2. No change in interaction with RUSC2, OCRL and MICAL1."; /evidence="ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:30905672"; MUTAGEN 72; /note="T->D: Loss of interaction with ACAP2. No change in interaction with RUSC2."; /evidence="ECO:0000269|PubMed:30905672"; MUTAGEN 72; /note="T->E: Phosphomimetic mutant. Loss of binding to GDI1, GDI2, CHM and CHML. Loss of interaction with ACAP2. No change in the interaction with RUSC2, OCRL and MICAL1."; /evidence="ECO:0000269|PubMed:29125462"; MUTAGEN 76; /note="T->S: Decreased interaction with ACAP2."; /evidence="ECO:0000269|PubMed:30905672"; MUTAGEN 79; /note="R->E: Loss of interaction with ACAP2 and RUSC2."; /evidence="ECO:0000269|PubMed:30905672"; MUTAGEN 79; /note="R->Q: Decreased interaction with ACAP2 and RUSC2."; /evidence="ECO:0000269|PubMed:30905672"; MUTAGEN 79; /note="R->W: Decreased interaction with ACAP2 and RUSC2."; /evidence="ECO:0000269|PubMed:30905672
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-72 by LRRK2 prevents the association of regulatory proteins including CHM, CHML and GDP dissociation inhibitors GDI1 and GDI2. {ECO:0000269|PubMed:29125462}.; PTM: AMPylation at Tyr-77 by L.pneumophila DrrA occurs in the switch 2 region and leads to moderate inactivation of the GTPase activity. It appears to prolong the lifetime of the GTP state of RAB1B by restricting access of GTPase effectors to switch 2 and blocking effector-stimulated GTP hydrolysis, thereby rendering RAB35 constitutively active. {ECO:0000269|PubMed:21822290, ECO:0000269|PubMed:22307087}.; PTM: Phosphocholinated by L.pneumophila AnkX. Both GDP-bound and GTP-bound forms can be phosphocholinated. Phosphocholination inhibits the GEF activity of DENND1A.
uniprot
proteins
protein_family
Rab family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16950109
uniprot
proteins
pubmed
17081065
uniprot
proteins
pubmed
20154091
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21822290
uniprot
proteins
pubmed
21951725
uniprot
proteins
pubmed
22065758
uniprot
proteins
pubmed
22307087
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
29125462
uniprot
proteins
pubmed
30905672
uniprot
proteins
pubmed
7811277
uniprot
proteins
sequence_length
201
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16950109, ECO:0000269|PubMed:21951725, ECO:0000269|PubMed:30905672}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:16950109}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:16950109}. Endosome {ECO:0000269|PubMed:16950109, ECO:0000269|PubMed:21951725}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Present on sorting endosomes and recycling endosome tubules (PubMed:16950109). Tends to be enriched in PIP2-positive cell membrane domains (PubMed:16950109). During mitosis, associated with the plasma membrane and present at the ingressing furrow during early cytokinesis as well as at the intercellular bridge later during cytokinesis (PubMed:16950109). Identified in stage I to stage IV melanosomes (PubMed:17081065). Colocalizes with ACAP2 and RUSC2 at the membrane protrusions of HEK293T cells (PubMed:30905672). {ECO:0000269|PubMed:16950109, ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:30905672}.
uniprot
proteins