| IED ID | IndEnz0002011923 |
| Enzyme Type ID | protease011923 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 44 EC 3.4.19.12 Deubiquitinating enzyme 44 Ubiquitin thioesterase 44 Ubiquitin-specific-processing protease 44 |
| Gene Name | USP44 |
| 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 | MLAMDTCKHVGQLQLAQDHSSLNPQKWHCVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVNEMYVFCYLCDDYVLNDNTTGDLKLLRRTLSAIKSQNYHCTTRSGRFLRSMGTGDDSYFLHDGAQSLLQSEDQLYTALWHRRRILMGKIFRTWFEQSPIGRKKQEEPFQEKIVVKREVKKRRQELEYQVKAELESMPPRKSLRLQGLAQSTIIEIVSVQVPAQTPASPAKDKVLSTSENEISQKVSDSSVKRRPIVTPGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAMTASEKTRSCKHPPVTDTVVYQMNECQEKDTGFVCSRQSSLSSGLSGGASKGRKMELIQPKEPTSQYISLCHELHTLFQVMWSGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTSLPALIPTSQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQCSGKDIASQPCLVTEMLAKFTETEALEGKIYVCDQCNSKRRRFSSKPVVLTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKIGVHVGFEEILNMEPYCCRETLKSLRPECFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYTQRVTENGHSKLLPPELLLGSQHPNEDADTSSNEILS |
| Enzyme Length | 712 |
| Uniprot Accession Number | Q9H0E7 |
| Absorption | |
| Active Site | ACT_SITE 282; /note="Nucleophile"; ACT_SITE 636; /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:14715245, ECO:0000269|PubMed:17443180, ECO:0000269|PubMed:20402667}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic checkpoint complex), thereby preventing premature activation of the APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint. Acts as a negative regulator of histone H2B (H2BK120ub1) ubiquitination. {ECO:0000269|PubMed:17443180, ECO:0000269|PubMed:22681888}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Metal binding (12); Modified residue (4); Mutagenesis (1); Natural variant (3); Region (1); Zinc finger (1) |
| Keywords | Cell cycle;Cell division;Hydrolase;Metal-binding;Mitosis;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger |
| Interact With | P41208; Q9BZS1 |
| Induction | INDUCTION: Transcriptionally regulated by POU5F1/OCT4 in embryonic stem cells and embryonal carcinoma cells. {ECO:0000269|PubMed:20505756}. |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20402667}. Note=Peaks in interphase, with relatively low levels maintained throughout mitosis. {ECO:0000250}. |
| Modified Residue | MOD_RES 169; /note=Phosphoserine; /evidence=ECO:0000305|PubMed:22692537; MOD_RES 239; /note=Phosphoserine; /evidence=ECO:0000305|PubMed:22692537; MOD_RES 269; /note=Phosphothreonine; /evidence=ECO:0000305|PubMed:22692537; MOD_RES 401; /note=Phosphoserine; /evidence=ECO:0000305|PubMed:22692537 |
| Post Translational Modification | PTM: Dephosphorylated by CTDP1.; PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination and is degraded by the proteasome. {ECO:0000269|PubMed:20402667}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 19615732; 23615962; 24837038; 26232424; 27880911; 28492742; 28520534; 28544703; 30622230; 31197957; 31968013; 32164618; 32285989; 32445925; 32644293; 32956592; 33647455; |
| Motif | |
| Gene Encoded By | |
| Mass | 81,185 |
| Kinetics | |
| Metal Binding | METAL 7; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 9; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 29; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 32; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 41; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 44; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 49; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 56; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 60; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 66; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 79; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 82; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502 |
| Rhea ID | |
| Cross Reference Brenda |