Detail Information for IndEnz0002014595
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