IED ID | IndEnz0005000404 |
Enzyme Type ID | lipase000404 |
Protein Name |
FAS-associated factor 2 Protein ETEA UBX domain-containing protein 3B UBX domain-containing protein 8 |
Gene Name | FAF2 ETEA KIAA0887 UBXD8 UBXN3B |
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 | MAAPEERDLTQEQTEKLLQFQDLTGIESMDQCRHTLEQHNWNIEAAVQDRLNEQEGVPSVFNPPPSRPLQVNTADHRIYSYVVSRPQPRGLLGWGYYLIMLPFRFTYYTILDIFRFALRFIRPDPRSRVTDPVGDIVSFMHSFEEKYGRAHPVFYQGTYSQALNDAKRELRFLLVYLHGDDHQDSDEFCRNTLCAPEVISLINTRMLFWACSTNKPEGYRVSQALRENTYPFLAMIMLKDRRMTVVGRLEGLIQPDDLINQLTFIMDANQTYLVSERLEREERNQTQVLRQQQDEAYLASLRADQEKERKKREERERKRRKEEEVQQQKLAEERRRQNLQEEKERKLECLPPEPSPDDPESVKIIFKLPNDSRVERRFHFSQSLTVIHDFLFSLKESPEKFQIEANFPRRVLPCIPSEEWPNPPTLQEAGLSHTEVLFVQDLTDE |
Enzyme Length | 445 |
Uniprot Accession Number | Q96CS3 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Plays an important role in endoplasmic reticulum-associated degradation (ERAD) that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed:18711132, PubMed:24215460). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333). Involved in inhibition of lipid droplet degradation by binding to phospholipase PNPL2 and inhibiting its activity by promoting dissociation of PNPL2 from its endogenous activator, ABHD5 which inhibits the rate of triacylglycerol hydrolysis (PubMed:23297223). {ECO:0000269|PubMed:18711132, ECO:0000269|PubMed:23297223, ECO:0000269|PubMed:24215460, ECO:0000269|PubMed:26692333}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Coiled coil (1); Compositional bias (1); Domain (2); Helix (3); Initiator methionine (1); Modified residue (2); Region (1) |
Keywords | 3D-structure;Acetylation;Coiled coil;Cytoplasm;Endoplasmic reticulum;Lipid droplet;Reference proteome;Unfolded protein response |
Interact With | Q8NBM4; P55072 |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12372427}. Lipid droplet {ECO:0000269|PubMed:19773358, ECO:0000269|PubMed:23297223}. Endoplasmic reticulum {ECO:0000269|PubMed:18711132, ECO:0000269|PubMed:23297223}. |
Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0007744|PubMed:19413330; MOD_RES 167; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | NMR spectroscopy (1) |
Cross Reference PDB | 2DAM; |
Mapped Pubmed ID | 10037681; 10490598; 10619026; 10873388; 12221077; 15866170; 16630611; 17353931; 18158243; 18218625; 18775313; 18829452; 19615732; 20030946; 20101212; 20160012; 20562859; 20591975; 20660154; 21115839; 21150319; 21351730; 21699497; 21911578; 22238364; 22454508; 22593156; 22992742; 23606334; 23720822; 24128008; 24378746; 25260751; 26496610; 26638075; 27295553; 28882874; 29146911; 29899553; 31105010; 31871319; 34739333; 8543060; 8571126; 8617235; 8662891; 8692836; 8756646; 8816443; 9013646; 9111050; 9418861; 9535835; 9792683; 9829970; |
Motif | |
Gene Encoded By | |
Mass | 52,623 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |