{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P51159","secondaryAccessions":["O00195","Q6FI40","Q9UIR9","Q9Y5U3"],"uniProtkbId":"RB27A_HUMAN","entryAudit":{"firstPublicDate":"1996-10-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2006-10-17","entryVersion":231,"sequenceVersion":3},"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-27A"},"shortNames":[{"value":"Rab-27"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12531900"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15548590"}],"value":"3.6.5.2"}]},"alternativeNames":[{"fullName":{"value":"GTP-binding protein Ram"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:9766"}],"value":"RAB27A"},"synonyms":[{"value":"RAB27"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18812475"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30771381"}],"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:30771381). RAB27A regulates homeostasis of late endocytic pathway, including endosomal positioning, maturation and secretion (PubMed:30771381). Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse (PubMed:18812475)"}],"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:0000305","source":"PubMed","id":"12531900"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15548590"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:19670"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12531900"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15548590"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35308027"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"30771381"}],"value":"Regulated by guanine nucleotide exchange factors (GEFs) including DENND10, which promote the exchange of bound GDP for free GTP (Probable). Regulated by GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity. Inhibited by GDP dissociation inhibitors (GDIs) (Probable)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9ERI2"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12062444"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15548590"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17237785"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18812475"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20048159"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30771381"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35308027"}],"value":"Binds SYTL1, SLAC2B, MYRIP, SYTL3, SYTL4 and SYTL5. Interacts with RPH3A and RPH3A (By similarity). Interacts with MLPH (PubMed:12062444). Interacts with SYTL2 (PubMed:18812475, PubMed:35308027). Interacts with UNC13D (PubMed:15548590, PubMed:17237785). Does not interact with the BLOC-3 complex (heterodimer of HPS1 and HPS4) (PubMed:20048159). Interacts (GDP-bound form preferentially) with DENND10 (PubMed:30771381). Interacts with FBXO28; this interaction promotes RAB27A ubiquitination and proteasomal degradation (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P51159","intActId":"EBI-716881"},"interactantTwo":{"uniProtKBAccession":"Q9BV36","geneName":"MLPH","intActId":"EBI-7042162"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P51159","intActId":"EBI-716881"},"interactantTwo":{"uniProtKBAccession":"Q8NFW9","geneName":"MYRIP","intActId":"EBI-1759414"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P51159","intActId":"EBI-716881"},"interactantTwo":{"uniProtKBAccession":"Q8IYJ3","geneName":"SYTL1","intActId":"EBI-2802861"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P51159","intActId":"EBI-716881"},"interactantTwo":{"uniProtKBAccession":"Q4VX76","geneName":"SYTL3","intActId":"EBI-2840607"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P51159","intActId":"EBI-716881"},"interactantTwo":{"uniProtKBAccession":"Q96C24","geneName":"SYTL4","intActId":"EBI-747142"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P51159","intActId":"EBI-716881"},"interactantTwo":{"uniProtKBAccession":"Q8TDW5-2","geneName":"SYTL5","intActId":"EBI-12243980"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P51159","intActId":"EBI-716881"},"interactantTwo":{"uniProtKBAccession":"Q70J99","geneName":"UNC13D","intActId":"EBI-11479429"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P51159-1","intActId":"EBI-15528760"},"interactantTwo":{"uniProtKBAccession":"Q9BV36","geneName":"MLPH","intActId":"EBI-7042162"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12643545"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17081065"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17237785"}],"value":"Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:12643545, PubMed:17081065). 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Low expression was found in thymus, kidney, muscle and placenta. Detected in melanocytes, and in most tumor cell lines examined. Expressed in cytotoxic T-lymphocytes (CTL) and mast cells"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P62820"}],"value":"Switch I, switch II 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 drive interaction with specific sets of effector proteins, with most effectors only binding to GTP-bound Rab"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9ERI2"}],"value":"Ubiquitinated in a FBXO28-dependent manner; leading to proteasomal degradation"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Griscelli syndrome 2","diseaseAccession":"DI-01687","acronym":"GS2","description":"Rare autosomal recessive disorder that results in pigmentary dilution of the skin and hair, the presence of large clumps of pigment in hair shafts, and an accumulation of melanosomes in melanocytes. GS2 patients also develop an uncontrolled T-lymphocyte and macrophage activation syndrome, known as hemophagocytic syndrome, leading to death in the absence of bone marrow transplantation. 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