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 |