| IED ID | IndEnz0002011425 |
| Enzyme Type ID | protease011425 |
| Protein Name |
Probable ubiquitin carboxyl-terminal hydrolase FAF-X EC 3.4.19.12 Deubiquitinating enzyme FAF-X Fat facets homolog Fat facets protein-related, X-linked Ubiquitin carboxyl-terminal hydrolase FAM Ubiquitin thioesterase FAF-X Ubiquitin-specific protease 9, X chromosome Ubiquitin-specific-processing protease FAF-X |
| Gene Name | Usp9x Fafl Fam |
| 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 | MTATTRGSPVGGNDNQGQAPDGQSQPPLQQNQTSSPDSSNENSPATPPDEQGQGDAPPQIEDEEPAFPHTDLAKLDDMINRPRWVVPVLPKGELEVLLEAAIDLSKKGLDVKSEACQRFFRDGLTISFTKILTDEAVSGWKFEIHRCIINNTHRLVELCVAKLAQDWFPLLELLAMALNPHCKFHIYNGTRPCESVSSSVQLPEDELFARSPDPRSPKGWLVDLLNKFGTLNGFQILHDRFINGSALNVQIIAALIKPFGQCYEFLTLHTVKKYFLPIIEMVPQFLENLTDEELKKEAKNEAKNDALSMIIKSLKNLASRVPGQEETVKNLEIFRLKMILRLLQISSFNGKMNALNEVNKVISSVSYYTHRHGSSEDEEWLTAERMAEWIQQNNILSIVLRDSLHQPQYVEKLEKILRFVIKEKALTLQDLDNIWAAQAGKHEAIVKNVHDLLAKLAWDFSPEQLDHLFDCFKASWTNASKKQREKLLELIRRLAEDDKDGVMAHKVLNLLWNLAHSDDVPVDIMDLALSAHIKILDYSCSQDRDTQKIQWIDRFIEELRTNDKWVIPALKQIREICSLFGEAPQNLSQSQRSPHVFYRHDLINQLQHNHALVTLVAENLATYMESMRMYGRDNEDYDPQTVRLGSRYSHVQEVQERLNFLRFLLKDGQLWLCAPQAKQIWKCLAENAVYLCDREACFKWYSKLMGDEPDLDPDINKDFFESNVLQLDPSLLTENGMKCFERFFKAVNCREGKLVAKRRAYMMDDLELIGLDYLWRVVIQSNDDIACRAIDLLKEIYTNLGPRLQVNQVVIHEDFIQSCFDRLKASYDTLCVLDGDKDSINCARQEAVRMVRVLTVLREYINECDSDYHEERTILPMSRAFRGKHLSFIVRFPNQGRQVDDLEVWSHTNDTIGSVRRCILNRIKANVAHTKIELFVGGELIDPGDDRKLIGQLNLKDKSLITAKLTQISSNMPSSPDSSSDSSTGSPGNHGNHYSDGPNPEVESCLPGVIMSLHPRYISFLWQVADLGSSLNMPPLRDGARVLMKLMPPDSTTIEKLRAICLDHAKLGESSLSPSLDSLFFGPSASQVLYLTEVVYALLMPAGAPLTDDSSDFQFHFLKSGGLPLVLSMLTRNNFLPNADMETRRGAYLNALKIAKLLLTAIGYGHVRAVAEACQPGVEGVNPMTSVNQVTHDQAVVLQSALQSIPNPSSECMLRNVSVRLAQQISDEASRYMPDICVIRAIQKIIWTSGCGGLQLVFSPNEEVTKIYEKTNAGNEPDLEDEQVCCEALEVMTLCFALIPTALDALSKEKAWQTFIIDLLLHCHSKTVRQVAQEQFFLMCTRCCMGHRPLLFFITLLFTVLGSTARERAKHSGDYFTLLRHLLNYAYNSNINVPNAEVLLNNEIDWLKRIRDDVKRTGETGVEETILEGHLGVTKELLAFQTPEKKFHIGCEKGGANLIKELIDDFIFPASNVYLQYMRNGELPAEQAIPVCGSPATINAGFELLVALAVGCVRNLKQIVDSLTEMYYIGTAITTCEALTEWEYLPPVGPRPPKGFVGLKNAGATCYMNSVIQQLYMIPSIRNGILAIEGTGSDVDDDMSGDEKQDNESNVDPRDDVFGYPQQFEDKPPLSKTEDRKEYNIGVLRHLQVIFGHLAASRLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAMLSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYVKGDLLEGANAYHCEKCNKKVDTVKRLLIKKLPPVLAIQLKRFDYDWERECAIKFNDYFEFPRELDMEPYTVAGVAKLEGDNVNPESQLIQQNEQSESEKAGSTKYRLVGVLVHSGQASGGHYYSYIIQRNGGDGEKNRWYKFDDGDVTECKMDDDEEMKNQCFGGEYMGEVFDHMMKRMSYRRQKRWWNAYILFYERMDTIGHDDEVIRYISEIAITTRPHQIVMPSAIERSVRKQNVQFMHNRMQYSLEYFQFMKKLLTCNGVYLNPPPGQDHLSPEAEEITMISIQLAARFLFTTGFHTKKIVRGSASDWYDALCILLRHSKNVRFWFAHNVLFNVSNRFSEYLLECPSAEVRGAFAKLIVFIAHFSLQDGPCPSPFASPGPSSQAYDNLSLSDHLLRAVLNLLRREVSEHGRHLQQYFNLFVMYANLGVAEKTQLLKLSVPATFMLVSLDEGPGPPIKYQYAELGKLYSVVSQLIRCCNVSSRMQSSINGNPSLPNPFGDPNLSQPIMPIQQNVVDILFVRTSYVKKIIEDCSNSDETVKLLRFCCWENPQFSSTVLSELLWQVAYSYTYELRPYLDLLLQILLIEDSWQTHRIHNALKGIPDDRDGLFDTIQRSKNHYQKRAYQCIKCMVALFSSCPVAYQILQGNGDLKRKWTWAVEWLGDELERRPYTGNPQYTYNNWSPPVQSNETSNGYFLERSHSARMTLAKACELCPEEEPDDQDAPDEHESPPPEDAPLYPHSPGSQYQQNNHVHGQPYTGPAAHHMNNPQRTGQRAQENYEGGEEVSPPQTKGSVKCTY |
| Enzyme Length | 2559 |
| Uniprot Accession Number | P70398 |
| Absorption | |
| Active Site | ACT_SITE 1566; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093, ECO:0000305|PubMed:30951545"; ACT_SITE 1879; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:29626158, ECO:0000269|PubMed:30951545}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Deubiquitinase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins (PubMed:29626158, PubMed:30951545). May therefore play an important regulatory role at the level of protein turnover by preventing degradation of proteins through the removal of conjugated ubiquitin (PubMed:29626158, PubMed:30951545). Specifically hydrolyzes 'Lys-48'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitins chains (By similarity). Essential component of TGF-beta/BMP signaling cascade (By similarity). Specifically deubiquitinates monoubiquitinated SMAD4, opposing the activity of E3 ubiquitin-protein ligase TRIM33 (By similarity). Deubiquitinates alkylation repair enzyme ALKBH3 (By similarity). OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions (By similarity). Regulates chromosome alignment and segregation in mitosis by regulating the localization of BIRC5/survivin to mitotic centromeres (By similarity). Involved in axonal growth and neuronal cell migration (PubMed:24607389). Regulates cellular clock function by enhancing the protein stability and transcriptional activity of the core circadian protein ARNTL/BMAL1 via its deubiquitinating activity (PubMed:29626158). Deubiquitinates PEG10 (PubMed:30951545). {ECO:0000250|UniProtKB:Q93008, ECO:0000269|PubMed:24607389, ECO:0000269|PubMed:29626158, ECO:0000269|PubMed:30951545}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (4); Domain (1); Modified residue (8); Mutagenesis (1); Region (4); Sequence conflict (13) |
| Keywords | Biological rhythms;Cell cycle;Cell division;Cell projection;Chromosome partition;Cytoplasm;Hydrolase;Mitosis;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | A5PKW4; Q13485 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q93008}. Cell projection, growth cone {ECO:0000269|PubMed:24607389}. |
| Modified Residue | MOD_RES 374; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 375; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 588; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q93008"; MOD_RES 1600; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 2443; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 2540; /note="Phosphotyrosine"; /evidence="ECO:0007744|PubMed:17947660"; MOD_RES 2547; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q93008"; MOD_RES 2551; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:Q93008" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10704870; 11217851; 12023983; 12466851; 12520002; 12617843; 12904583; 12925892; 14516667; 14610273; 14762062; 15509704; 15741177; 15978012; 16023255; 16141072; 16602821; 16615898; 17500595; 18410486; 18799693; 19135894; 19176755; 19334288; 20339350; 20362541; 20548051; 21173155; 21267068; 22544753; 22653443; 22699621; 23690623; 23861879; 23979718; 24591637; 25200027; 25763846; 26811477; 26936881; 27181636; 28341829; 28559472; 28808228; 28877990; 29346117; 30970248; 31216195; 31813652; 33323119; 33378666; 33767158; 33857489; 9384609; 9817915; |
| Motif | |
| Gene Encoded By | |
| Mass | 290,711 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |