Detail Information for IndEnz0001000041
IED ID IndEnz0001000041
Enzyme Type ID amylase000041
Protein Name Ras-related protein Rab-26
Gene Name RAB26
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 MSRKKTPKSKGASTPAASTLPTANGARPARSGTALSGPDAPPNGPLQPGRPSLGGGVDFYDVAFKVMLVGDSGVGKTCLLVRFKDGAFLAGTFISTVGIDFRNKVLDVDGVKVKLQMWDTAGQERFRSVTHAYYRDAHALLLLYDVTNKASFDNIQAWLTEIHEYAQHDVALMLLGNKVDSAHERVVKREDGEKLAKEYGLPFMETSAKTGLNVDLAFTAIAKELKQRSMKAPSEPRFRLHDYVKREGRGASCCRP
Enzyme Length 256
Uniprot Accession Number Q9ULW5
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: 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 set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Mediates transport of ADRA2A and ADRA2B from the Golgi to the cell membrane. Plays a role in the maturation of zymogenic granules and in pepsinogen secretion in the stomach. Plays a role in the secretion of amylase from acinar granules in the parotid gland. {ECO:0000269|PubMed:20038531, ECO:0000269|PubMed:23105096}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 70..78; /note=GTP; /evidence=ECO:0000269|Ref.10; NP_BIND 119..123; /note=GTP; /evidence=ECO:0000269|Ref.10; NP_BIND 177..180; /note=GTP; /evidence=ECO:0000269|Ref.10; NP_BIND 207..209; /note=GTP; /evidence=ECO:0000269|Ref.10
Features Alternative sequence (1); Beta strand (6); Chain (1); Compositional bias (1); Erroneous initiation (1); Helix (6); Lipidation (2); Motif (1); Mutagenesis (3); Nucleotide binding (4); Region (1); Sequence conflict (1); Turn (1)
Keywords 3D-structure;Alternative splicing;Cytoplasmic vesicle;GTP-binding;Golgi apparatus;Lipoprotein;Membrane;Nucleotide-binding;Prenylation;Protein transport;Reference proteome;Transport
Interact With P18089; Q5TD97; Q14525; O43482; Q9H9P5-5
Induction
Subcellular Location SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:23105096}; Lipid-anchor {ECO:0000269|PubMed:23105096}; Cytoplasmic side {ECO:0000269|PubMed:23105096}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000305|PubMed:23105096}; Lipid-anchor {ECO:0000305|PubMed:23105096}; Cytoplasmic side {ECO:0000305|PubMed:23105096}. Note=Not localized at the plasma membrane (By similarity). Inhibition of S-geranylgeranyl cysteine formation abolishes membrane location. {ECO:0000250|UniProtKB:P51156}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 2G6B;
Mapped Pubmed ID 11141079; 11389151; 11675392; 1648736; 16696853; 17114793; 17411337; 18532927; 19603039; 19913121; 20628086; 24023390; 24413166; 25341920; 25643395; 26496610; 33731709; 7957092; 7991565; 8164745; 8349690; 8375503; 8513495; 8631982; 8662963; 8836150;
Motif MOTIF 93..101; /note=Effector region; /evidence=ECO:0000250
Gene Encoded By
Mass 27,900
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda