IED ID | IndEnz0002014595 |
Enzyme Type ID | protease014595 |
Protein Name |
CASP8-associated protein 2 FLICE-associated huge protein |
Gene Name | Casp8ap2 Flash |
Organism | Mus musculus (Mouse) |
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
Enzyme Sequence | MAADDDNGDGTGLFDVCPASPLKNNDEGSLDIYAGLDSAVSDSTARSCVSFRNCLDLYEEILTEEGTAKEATYNDLQIEYGKCQQQMKDLMKRFKEIQTQNLNLKNENQSLKKNISALIKTARVEINRKDEEINHLHQRLSEFPHFRNNHKTARTKDSQSTSPHLDDCSKTDHGVKSDVQKDVHPNTAQPNLEKEGKSHSEAQNPLHLSTGVEKHCANNVWSRSPYQVGEGNSNEDNRRGRSGTRHSQCSRGTDRTQKDLHSSCNDSEPRDKEANSRLQGHPEKHGNSEARTESKISESKSSTGMGYKSERSASSWEKETSRERPHTRVESQHDKNLEKQNERLQNMHRKELPSQDKTERKVDVKFKPAGEEQGHRGRVDRALPPHPKNDVKHYGFNKYHPEERRGREDCKRDRGMNSHGFQDRRCSSFLSSNRNSKYPHSKEVSVAHQWENTPFKAERHRTEDRRKRERENKEESRHVKSDKKSPPEHLQRTHKDTKKSTADGKRQTEPKHGKGAVSNSELSKGTDSKEGATKVESGPNEAKGKDLKLSFMEKLNLTLSPAKKQPACQDNPHQITGVPEPSGTCDSRSLETTGTVACLPSGSEHNREETKSELPEPKEALLATSQLRISIPENKMKEEKRLLFKSVENTVPCELLACGTEISLPAPVEIEQARCLLGSVEVEETCGGARTAASVVMHVLPEHASEDASQELDTKRHDGINACAISEGVKTKVILSPKAAAASESHLAPLVEEPSISLVNCSGDNNPKLEPSLEERPIVETKSCPLESCLPKETFVPSPQKTELIDHKIETGESNSVYQDDDNSVLSIDFNNLRPIPDPISPLNSPVRPVCKVVSMESSCAIPLYDSSHKDEFPSNSTLSTFKSQSDLNKENEKPVPKFDKCSEADSCKHLSLDELEEGEIRSDDEESVAQKRLEKSARPRVSAEVQPGKSSPGSRRSTVHVHKDNGRTAVKLPRDRLTWSKRSSESRPSNTERKSKTMSISSLEKILPLILVPSSLWEVMHMLRLLGKHVRKNYMKFKIKFSLTQFHRIIESAILSFTSLVKCLDLSKICKSVSTLQKSLCEVIESNLKQVKKNGIVDRLFEQQQTDMKKKLWKFVDEQLDYLFEKLKKILLKFCDSVNFENENSEGKLGKKYKERTQHSNCQKKKMDNKEIRREKVLKSENTVNFKSSLGCEKSEEKHQDQNKTNASIVKHDVKRTFSTCSDNTKNAECKEQFLEKSCPSTPRPGKDEGHTEEEAQAAQHASAKSERSFEILTEQQASSLTFNLVSDAQMGEIFKSLLQGSDLLDTSGTEKAEWELKTPEKQLLESLKCESAPACATEELVSEGASLCPKVISDDNWSLLSSEKGPSLSSGLSLPVHPDVLDENCMFEVSSNTALGKDNVYSSEKSKPCISSILLEDLAVSLTVPSPLKSDGHLSFLKPEVLSTSTPEEVISAHFSEDALLEEEDASEQDIHLALESDNSSSKSSCSSWTSRSVASGFQYHPNLPMHAVIMEKSNDHFIVKIRRATPSTSPGLKHGVVAEESLTSLPRTGKEAGVATEKEPNLFQSTVLKPVKDLENTDKNIDKSKLTHEEQNSIVQTQVPDIYEFLKDASNKVVHCDQVVDDCFKLHQVWEPKVSENLQELPSMEKIPHSLDNHLPDTHIDLTKDSATETKSLGELMEVTVLNVDHLECSQTNLDQDAEITCSSLQPDTIDAFIDLTHDASSESKNEGSEPVLAVEGMGCQVICIDEDTNKEGKMGRANSPLESIVEETCIDLTSESPGSCEIKRHNLKSEPPSKLDCLELPETLGNGHKKRKNSPGVSHSSQKKQRKDIDLSSEKTQRLSPNSDRNGDAHRKQASKKREPAVNETSLSSEASPEVKGSTAVLAASPASLSAKNVIKKKGEIIVSWTRNDDREILLECQKRMPSLKTFTYLAVKLNKNPNQVSERFQQLKKLFEKSKCR |
Enzyme Length | 1962 |
Uniprot Accession Number | Q9WUF3 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Participates in TNF-alpha-induced blockade of glucocorticoid receptor (GR) transactivation at the nuclear receptor coactivator level, upstream and independently of NF-kappa-B. Suppresses both NCOA2- and NCOA3-induced enhancement of GR transactivation (By similarity). Required for histone gene transcription and progression through S phase (By similarity). Required for histone gene transcription and S phase progression (By similarity). Involved in TNF-alpha-induced activation of NF-kappa-B via a TRAF2-dependent pathway. Acts as a downstream mediator for CASP8-induced activation of NF-kappa-B. Required for the activation of CASP8 in FAS-mediated apoptosis. {ECO:0000250, ECO:0000269|PubMed:11340079, ECO:0000269|PubMed:15592525}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Compositional bias (13); Initiator methionine (1); Modified residue (7); Motif (1); Region (10); Sequence conflict (3) |
Keywords | Acetylation;Activator;Apoptosis;Cell cycle;Cytoplasm;Mitochondrion;Nucleus;Phosphoprotein;Reference proteome;Repressor;Transcription;Transcription regulation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:17003125}. Nucleus, PML body {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Exported from the nucleus to the mitochondria upon FAS activation. {ECO:0000250}. |
Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:Q9UKL3; MOD_RES 20; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9UKL3; MOD_RES 560; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9UKL3; MOD_RES 798; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9UKL3; MOD_RES 858; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9UKL3; MOD_RES 923; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9UKL3; MOD_RES 1323; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:23806337 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10537104; 10725249; 11217851; 11591653; 12466851; 12520002; 12654726; 12904583; 14610273; 14621295; 15883645; 16615898; 18799693; 19546234; 21267068; 21338522; 21725362; 23673342; 25238250; 26208142; 27609454; 31084574; 32141129; |
Motif | MOTIF 1716..1720; /note=SUMO interaction motif 1 (SIM); mediates the binding to polysumoylated substrates; /evidence=ECO:0000250 |
Gene Encoded By | |
Mass | 219,091 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |