{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q15286","secondaryAccessions":["B2R6E0","B4E390"],"uniProtkbId":"RAB35_HUMAN","entryAudit":{"firstPublicDate":"1998-07-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-11-01","entryVersion":224,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Ras-related protein Rab-35"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30905672"}],"value":"3.6.5.2"}]},"alternativeNames":[{"fullName":{"value":"GTP-binding protein RAY"}},{"fullName":{"value":"Ras-related protein Rab-1C"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:9774"}],"value":"RAB35"},"synonyms":[{"value":"RAB1C"},{"value":"RAY"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6PHN9"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16950109"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21951725"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30905672"}],"value":"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)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + H2O = GDP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19669"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58189"}],"ecNumber":"3.6.5.2","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30905672"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:19670"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"30905672"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30905672"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20154091"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30905672"},{"evidenceCode":"ECO:0000305"}],"value":"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)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q6PHN9"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20154091"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21951725"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22065758"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29125462"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30905672"}],"value":"Interacts with DENND1A and DENND1B; in a nucleotide-dependent manner (PubMed:20154091, PubMed:22065758). Interacts with DENND1C; weak interaction which is nucleotide-independent (PubMed:20154091). Interacts (GTP-bound form) with ACAP2, RUSC2, OCRL MICAL1 and MICALL1; the interaction is direct and probably recruits these effectors to membranes (PubMed:21951725, PubMed:30905672). Interacts with EHD1; the interaction is indirect through MICALL1 and probably recruits EHD1 to membranes (By similarity). Interacts with GDI1, GDI2, CHM and CHML; phosphorylation at Thr-72 by LRRK2 disrupts these interactions (PubMed:29125462)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q15286","intActId":"EBI-722275"},"interactantTwo":{"uniProtKBAccession":"P50570-2","geneName":"DNM2","intActId":"EBI-10968534"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q15286","intActId":"EBI-722275"},"interactantTwo":{"uniProtKBAccession":"P42858","geneName":"HTT","intActId":"EBI-466029"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q15286","intActId":"EBI-722275"},"interactantTwo":{"uniProtKBAccession":"Q8WXH2","geneName":"JPH3","intActId":"EBI-1055254"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q15286","intActId":"EBI-722275"},"interactantTwo":{"uniProtKBAccession":"Q8N3F8","geneName":"MICALL1","intActId":"EBI-1056885"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16950109"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17081065"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30905672"}],"value":"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)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16950109"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21951725"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30905672"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Lipid-anchor","id":"SL-9901"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16950109"}],"value":"Membrane, clathrin-coated pit","id":"SL-0069"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16950109"}],"value":"Cytoplasmic vesicle, clathrin-coated vesicle","id":"SL-0070"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16950109"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21951725"}],"value":"Endosome","id":"SL-0101"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17081065"}],"value":"Melanosome","id":"SL-0161"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q15286-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q15286-2"],"sequenceIds":["VSP_042918"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30905672"}],"value":"Switch 1, switch 2 and the interswitch regions are characteristic of Rab GTPases and mediate the interactions with Rab downstream effectors. The switch regions undergo conformational changes upon nucleotide binding which drives interaction with specific sets of effector proteins, with most effectors only binding to GTP-bound Rab"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29125462"}],"value":"Phosphorylation at Thr-72 by LRRK2 prevents the association of regulatory proteins including CHM, CHML and GDP dissociation inhibitors GDI1 and GDI2"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21822290"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22307087"}],"value":"AMPylation at Tyr-77 by L.pneumophila DrrA occurs in the switch 2 region and leads to moderate inactivation of the GTPase activity. 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