Detail Information for IndEnz0005000075
IED ID IndEnz0005000075
Enzyme Type ID lipase000075
Protein Name Ras-related protein Rab-6A
Rab-6
Gene Name RAB6A RAB6
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 MSTGGDFGNPLRKFKLVFLGEQSVGKTSLITRFMYDSFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSTVAVVVYDITNVNSFQQTTKWIDDVRTERGSDVIIMLVGNKTDLADKRQVSIEEGERKAKELNVMFIETSAKAGYNVKQLFRRVAAALPGMESTQDRSREDMIDIKLEKPQEQPVSEGGCSC
Enzyme Length 208
Uniprot Accession Number P20340
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Has a low GTPase activity. Involved in COPI-independent retrograde transport from the Golgi to the ER (PubMed:25962623). {ECO:0000269|PubMed:25962623}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 20..28; /note="GTP"; /evidence="ECO:0000269|PubMed:16332443, ECO:0000269|PubMed:18243103, ECO:0000269|PubMed:19141279"; NP_BIND 68..72; /note="GTP"; /evidence="ECO:0000269|PubMed:16332443, ECO:0000269|PubMed:18243103, ECO:0000269|PubMed:19141279"; NP_BIND 126..129; /note="GTP"; /evidence="ECO:0000269|PubMed:16332443, ECO:0000269|PubMed:18243103, ECO:0000269|PubMed:19141279"; NP_BIND 156..158; /note="GTP"; /evidence="ECO:0000269|PubMed:16332443, ECO:0000269|PubMed:18243103, ECO:0000269|PubMed:19141279"
Features Alternative sequence (3); Beta strand (6); Chain (1); Helix (9); Initiator methionine (1); Lipidation (2); Modified residue (4); Motif (1); Mutagenesis (3); Nucleotide binding (4); Sequence conflict (1); Turn (1)
Keywords 3D-structure;Acetylation;Alternative splicing;Direct protein sequencing;ER-Golgi transport;GTP-binding;Golgi apparatus;Host-virus interaction;Lipoprotein;Membrane;Methylation;Nucleotide-binding;Phosphoprotein;Prenylation;Protein transport;Reference proteome;Transport
Interact With Q8TD16; Q8IWJ2; Q01968; Q92871; Q02410-2; Q6PAL8; Q5ZWZ3; P05067; Q9NP61; P20042; Q92871; Q16560-2
Induction
Subcellular Location SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:23091056, ECO:0000269|PubMed:25962623}; Lipid-anchor {ECO:0000269|PubMed:25962623}. Note=BICD2 facilitates its targeting to Golgi apparatus membrane. {ECO:0000269|PubMed:25962623}.; SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus membrane {ECO:0000269|PubMed:11071909}; Lipid-anchor {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus membrane {ECO:0000269|PubMed:11071909}; Lipid-anchor {ECO:0000305}.
Modified Residue MOD_RES 2; /note="N-acetylserine"; /evidence="ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"; MOD_RES 82; /note="O-AMP-tyrosine; by Legionella DrrA"; /evidence="ECO:0000269|PubMed:21822290"; MOD_RES 184; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P35279"; MOD_RES 208; /note="Cysteine methyl ester"; /evidence="ECO:0000250"
Post Translational Modification PTM: Prenylated. {ECO:0000269|PubMed:25962623}.
Signal Peptide
Structure 3D X-ray crystallography (6)
Cross Reference PDB 1YZQ; 2GIL; 3BBP; 3CWZ; 4DKX; 5LEF;
Mapped Pubmed ID 10359595; 10459009; 10545110; 10559986; 10562278; 10637310; 10865125; 10990452; 11141079; 11389151; 11483508; 11675392; 11689439; 11839770; 12377769; 12401177; 12738866; 1295745; 15029241; 15269279; 15377662; 15483056; 15654769; 15747776; 15758030; 15870108; 16189514; 16314391; 16395330; 1648736; 16536738; 16571679; 16683916; 16885419; 16902405; 17114793; 17353931; 17411337; 17451557; 17488291; 17562788; 17573808; 1764995; 17681140; 17684057; 17699596; 17716866; 17827179; 18195106; 18256213; 18367545; 18532927; 18664496; 18946081; 19109890; 19463016; 19603039; 19620288; 19632984; 19635840; 19703403; 20170518; 20197277; 20360680; 20562865; 20685960; 21183348; 21378754; 21421921; 21436057; 21543860; 21596566; 21807881; 21911578; 22124028; 22335553; 22581368; 22593156; 22607032; 22750005; 22909819; 23333653; 23416715; 23437303; 23569112; 23650620; 23783758; 24006491; 24023390; 24794632; 24891604; 25233431; 25341920; 25416956; 25453831; 25821985; 26000619; 26638075; 27246931; 27550519; 28448737; 29093437; 29144562; 29440364; 31142554; 33012781; 33247182; 7918097; 7957092; 7991565; 8164745; 8293978; 8349690; 8375503; 8513495; 8631982; 8662963; 8681805; 8836150; 9050864; 9244302; 9671731;
Motif MOTIF 42..50; /note=Effector region; /evidence=ECO:0000250
Gene Encoded By
Mass 23,593
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda