Detail Information for IndEnz0005001251
IED ID IndEnz0005001251
Enzyme Type ID lipase001251
Protein Name Rab GDP dissociation inhibitor beta
Rab GDI beta
Guanosine diphosphate dissociation inhibitor 2
GDI-2
Gene Name GDI2 RABGDIB
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MNEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESASITPLEDLYKRFKIPGSPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVTEGSFVYKGGKIYKVPSTEAEALASSLMGLFEKRRFRKFLVYVANFDEKDPRTFEGIDPKKTTMRDVYKKFDLGQDVIDFTGHALALYRTDDYLDQPCYETINRIKLYSESLARYGKSPYLYPLYGLGELPQGFARLSAIYGGTYMLNKPIEEIIVQNGKVIGVKSEGEIARCKQLICDPSYVKDRVEKVGQVIRVICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISFAHNVAAQGKYIAIVSTTVETKEPEKEIRPALELLEPIEQKFVSISDLLVPKDLGTESQIFISRTYDATTHFETTCDDIKNIYKRMTGSEFDFEEMKRKKNDIYGED
Enzyme Length 445
Uniprot Accession Number P50395
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: GDP-dissociation inhibitor preventing the GDP to GTP exchange of most Rab proteins. By keeping these small GTPases in their inactive GDP-bound form regulates intracellular membrane trafficking (PubMed:25860027). Negatively regulates protein transport to the cilium and ciliogenesis through the inhibition of RAB8A (PubMed:25860027). {ECO:0000269|PubMed:25860027}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Chain (1); Modified residue (7); Sequence conflict (1)
Keywords Acetylation;Alternative splicing;Cytoplasm;GTPase activation;Membrane;Phosphoprotein;Reference proteome
Interact With P62820-1; Q8BMD2; Q8BMD2-1; P61027; P55258; P61007
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Modified Residue MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0007744|PubMed:19413330"; MOD_RES 57; /note="N6-succinyllysine"; /evidence="ECO:0000250|UniProtKB:Q61598"; MOD_RES 61; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"; MOD_RES 112; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 130; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P50399"; MOD_RES 269; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 382; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10818110; 10990452; 11038176; 11179213; 11516400; 11689439; 11703925; 11746448; 11771757; 11784320; 11917121; 12058051; 12221131; 12244319; 12364329; 12427552; 12475894; 12684051; 12944476; 12972505; 15096524; 15138286; 1516130; 15247254; 15388334; 15528189; 15561770; 15692570; 15878329; 15914536; 15958533; 16207721; 16373702; 16385451; 16410077; 16525024; 16525121; 16571673; 16641372; 16754960; 16880209; 16950109; 17043139; 17132146; 17189207; 17208202; 17239822; 17287728; 17353931; 17488286; 17507299; 17562788; 17574030; 17646400; 17671165; 17678623; 18076383; 18094055; 18354496; 18367545; 1845915; 18477474; 18559336; 18585354; 18664496; 18701652; 18779367; 18804435; 1900457; 19109890; 19135240; 19345684; 19403694; 19490898; 19570034; 19620288; 19656848; 19725050; 19729655; 19738201; 19745841; 20008558; 20154091; 20159109; 20159556; 20305638; 20308558; 20360068; 20404108; 20434987; 20562859; 20592283; 20711500; 20797862; 20851765; 20937701; 21041651; 2115402; 21183348; 21187289; 21216617; 21273506; 21330364; 21421921; 21445324; 21458671; 21532587; 21554507; 21565611; 21586568; 21683469; 21706022; 21718402; 21776405; 21951725; 21988832; 22013193; 22065758; 22072793; 22171327; 22252131; 22365832; 22433857; 22511774; 22581368; 22595670; 22622570; 22648168; 22653444; 22705394; 22762500; 22810585; 22908308; 22983554; 23084991; 23091056; 23176487; 23176493; 23220125; 23239882; 23247405; 23263280; 23333653; 23351085; 23357852; 23378591; 23416715; 23420520; 23444368; 23478338; 23645161; 23650620; 23678941; 23684622; 23713133; 23839779; 24284321; 24296415; 24366813; 24644286; 24694596; 24719330; 24891604; 24917561; 24967941; 25074980; 25277244; 25341920; 25343031; 25472813; 25609649; 25648148; 25713415; 25925668; 26177209; 26245486; 26434594; 26496610; 26538022; 26925400; 26936971; 27041585; 27044746; 27103185; 27246931; 27329675; 32945458; 34051575; 34556814; 7688123; 7911226; 8144603; 8408203; 8522602; 8692836; 8863739; 9020086; 9020161; 9030515; 9136770; 9323142; 9590177; 9733780;
Motif
Gene Encoded By
Mass 50,663
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda