{ "uniprot_canonical_ac": "D6R9N7-1", "uniprot_ac": "D6R9N7", "uniprot_id": "U17LI_HUMAN", "mass": { "chemical_mass": 59657.0, "monoisotopic_mass": 59657.0 }, "refseq": { "ac": "NP_001243788", "name": "ubiquitin carboxyl-terminal hydrolase 17-like protein 18", "summary": "", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001243788" }, "gene_names": [ { "name": "USP17L18", "resource": "UniProtKB", "type": "recommended", "url": "https://www.uniprot.org/uniprot/D6R9N7", "id": "D6R9N7" }, { "name": "USP17L18", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001243788", "id": "NP_001243788" } ], "protein_names": [ { "name": "Ubiquitin carboxyl-terminal hydrolase 17-like protein 18", "resource": "UniProtKB", "type": "recommended", "url": "", "id": "D6R9N7" }, { "name": "3.4.19.12", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "D6R9N7" }, { "name": "ubiquitin carboxyl-terminal hydrolase 17-like protein 18", "resource": "RefSeq", 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"resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "lung neoplasm", "description": "" }, { "id": "MIM:211980", "resource": "MIM", "url": "https://www.omim.org/entry/211980", "name": "Lung cancer", "description": "Lung cancer" } ] }, { "disease_id": "DOID:2531", "recommended_name": { "id": "DOID:2531", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2531", "name": "hematologic cancer", "description": "An organ system cancer located in the hematological system that is characterized by uncontrolled cellular proliferation in blood, bone marrow and lymph nodes." }, "synonyms": [ { "id": "DOID:2531", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2531", "name": "Hematologic malignancy", "description": "" }, { "id": "DOID:2531", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2531", "name": "Hematologic neoplasm", "description": "" }, { "id": "DOID:2531", 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"Protein Classification" ] }, { "id": "IPR006861", "url": "https://www.ebi.ac.uk/interpro/entry/IPR006861", "database": "InterPro", "categories": [ "Protein Classification" ] }, { "id": "IPR018200", "url": "https://www.ebi.ac.uk/interpro/entry/IPR018200", "database": "InterPro", "categories": [ "Protein Classification" ] }, { "id": "IPR028889", "url": "https://www.ebi.ac.uk/interpro/entry/IPR028889", "database": "InterPro", "categories": [ "Protein Classification" ] }, { "id": "IPR038765", "url": "https://www.ebi.ac.uk/interpro/entry/IPR038765", "database": "InterPro", "categories": [ "Protein Classification" ] }, { "id": "hsa:100287364", "url": "https://www.genome.jp/dbget-bin/get_linkdb?-t+pathway+hsa:100287364", "database": "KEGG Pathway", "categories": [ "Enzyme and Pathway" ] }, { "id": "NX_D6R9N7", "url": "https://www.nextprot.org/entry/NX_D6R9N7", "database": "neXtProt", "categories": [ "Protein", "Organism-specific" ] }, { "id": "CLDMQHY", "url": 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"MEDDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSCETRVDLCDDLAPVARQLAPREKLPLSSRRPAAVGAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQTNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRAKQGELKRDHPCLQAPELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVRKVEGTLPPDVLVIHQSKYKCGMKNHHPEQQSSLLNLSSTTPTHQESMNTGTLASLRGRARRSKGKNKHSKRALLVCQ", "length": 530, "header": "sp|D6R9N7-1|U17LI_HUMAN Isoform 1 of Ubiquitin carboxyl-terminal hydrolase 17-like protein 18 OS=Homo sapiens OX=9606 GN=USP17L18 PE=3 SV=1 CANONICAL=D6R9N7-1" }, "locus": { "chromosome": "4", "start_pos": 9250219, "end_pos": 9248630, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000504209.1", "url": "https://www.ensembl.org/id/ENST00000504209.1" }, { "database": "Ensembl Peptide", "id": 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"2000", "authors": "Kato M, Miyazawa K, Kitamura N", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "10982817", "url": "https://glygen.org/publication/PubMed/10982817" } ] }, { "title": "A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14.", "journal": "The EMBO journal", "date": "2001", "authors": "Borodovsky A, Kessler BM, Casagrande R, Overkleeft HS, Wilkinson KD, Ploegh HL", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "11566882", "url": "https://glygen.org/publication/PubMed/11566882" } ] }, { "title": "Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization.", "journal": "Nature", "date": "2002", "authors": "Li M, Chen D, Shiloh A, Luo J, Nikolaev AY, Qin J, Gu W", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "11923872", "url": "https://glygen.org/publication/PubMed/11923872" } ] }, { "title": "CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members.", "journal": "Nature", "date": "2003", "authors": "Trompouki E, Hatzivassiliou E, Tsichritzis T, Farmer H, Ashworth A, Mosialos G", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "12917689", "url": "https://glygen.org/publication/PubMed/12917689" } ] }, { "title": "The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination.", "journal": "Nature", "date": "2003", "authors": "Kovalenko A, Chable-Bessia C, Cantarella G, Israel A, Wallach D, Courtois G", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "12917691", "url": "https://glygen.org/publication/PubMed/12917691" } ] }, { "title": "Two isoforms of otubain 1 regulate T cell anergy via GRAIL.", "journal": "Nature immunology", "date": "2004", "authors": "Soares L, Seroogy C, Skrenta H, Anandasabapathy N, Lovelace P, Chung CD, Engleman E, Fathman CG", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "14661020", "url": "https://glygen.org/publication/PubMed/14661020" } ] }, { "title": "A dynamic role of HAUSP in the p53-Mdm2 pathway.", "journal": "Molecular cell", "date": "2004", "authors": "Li M, Brooks CL, Kon N, Gu W", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "15053880", "url": "https://glygen.org/publication/PubMed/15053880" } ] }, { "title": "Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2.", "journal": "Molecular cell", "date": "2005", "authors": "Meulmeester E, Maurice MM, Boutell C, Teunisse AF, Ovaa H, Abraham TE, Dirks RW, Jochemsen AG", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "15916963", "url": "https://glygen.org/publication/PubMed/15916963" } ] }, { "title": "Human ubiquitin specific protease 31 is a deubiquitinating enzyme implicated in activation of nuclear factor-kappaB.", "journal": "Cellular signalling", "date": "2006", "authors": "Tzimas C, Michailidou G, Arsenakis M, Kieff E, Mosialos G, Hatzivassiliou EG", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "16214042", "url": "https://glygen.org/publication/PubMed/16214042" } ] }, { "title": "A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response.", "journal": "Cell", "date": "2006", "authors": "Zhang D, Zaugg K, Mak TW, Elledge SJ", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "16901786", "url": "https://glygen.org/publication/PubMed/16901786" } ] }, { "title": "FOXO4 transcriptional activity is regulated by monoubiquitination and USP7/HAUSP.", "journal": "Nature cell biology", "date": "2006", "authors": "van der Horst A, de Vries-Smits AM, Brenkman AB, van Triest MH, van den Broek N, Colland F, Maurice MM, Burgering BM", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "16964248", "url": "https://glygen.org/publication/PubMed/16964248" } ] }, { "title": "The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2.", "journal": "The EMBO journal", "date": "2007", "authors": "Stevenson LF, Sparks A, Allende-Vega N, Xirodimas DP, Lane DP, Saville MK", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "17290220", "url": "https://glygen.org/publication/PubMed/17290220" } ] }, { "title": "Anaphase initiation is regulated by antagonistic ubiquitination and deubiquitination activities.", "journal": "Nature", "date": "2007", "authors": "Stegmeier F, Rape M, Draviam VM, Nalepa G, Sowa ME, Ang XL, McDonald ER 3rd, Li MZ, Hannon GJ, Sorger PK, Kirschner MW, Harper JW, Elledge SJ", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "17443180", "url": "https://glygen.org/publication/PubMed/17443180" } ] }, { "title": "Fbw7 and Usp28 regulate myc protein stability in response to DNA damage.", "journal": "Cell cycle (Georgetown, Tex.)", "date": "2007", "authors": "Popov N, Herold S, Llamazares M, Schulein C, Eilers M", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "17873522", "url": "https://glygen.org/publication/PubMed/17873522" } ] }, { "title": "Human USP3 is a chromatin modifier required for S phase progression and genome stability.", "journal": "Current biology : CB", "date": "2007", "authors": "Nicassio F, Corrado N, Vissers JH, Areces LB, Bergink S, Marteijn JA, Geverts B, Houtsmuller AB, Vermeulen W, Di Fiore PP, Citterio E", "evidence": [ { 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Matsuyama T, Ikura T, Muramatsu M, Ito T", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "18172164", "url": "https://glygen.org/publication/PubMed/18172164" } ] }, { "title": "Regulation of IkappaB kinase-related kinases and antiviral responses by tumor suppressor CYLD.", "journal": "The Journal of biological chemistry", "date": "2008", "authors": "Zhang M, Wu X, Lee AJ, Jin W, Chang M, Wright A, Imaizumi T, Sun SC", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "18467330", "url": "https://glygen.org/publication/PubMed/18467330" } ] }, { "title": "Vasopressin-inducible ubiquitin-specific protease 10 increases ENaC cell surface expression by deubiquitylating and stabilizing sorting nexin 3.", "journal": "American journal of physiology. Renal physiology", "date": "2008", "authors": "Boulkroun S, Ruffieux-Daidie D, Vitagliano JJ, Poirot O, Charles RP, Lagnaz D, Firsov D, Kellenberger S, Staub O", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "18632802", "url": "https://glygen.org/publication/PubMed/18632802" } ] }, { "title": "The tumour suppressor CYLD is a negative regulator of RIG-I-mediated antiviral response.", "journal": "EMBO reports", "date": "2008", "authors": "Friedman CS, O'Donnell MA, Legarda-Addison D, Ng A, Cardenas WB, Yount JS, Moran TM, Basler CF, Komuro A, Horvath CM, Xavier R, Ting AT", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "18636086", "url": "https://glygen.org/publication/PubMed/18636086" } ] }, { "title": "USP19 deubiquitinating enzyme supports cell proliferation by stabilizing KPC1, a ubiquitin ligase for p27Kip1.", "journal": "Molecular and cellular biology", "date": "2009", "authors": "Lu Y, Adegoke OA, Nepveu A, Nakayama KI, Bedard N, Cheng D, Peng J, Wing SS", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "19015242", "url": "https://glygen.org/publication/PubMed/19015242" } ] }, { "title": "FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling, controls Smad4 monoubiquitination.", "journal": "Cell", "date": "2009", "authors": "Dupont S, Mamidi A, Cordenonsi M, Montagner M, Zacchigna L, Adorno M, Martello G, Stinchfield MJ, Soligo S, Morsut L, Inui M, Moro S, Modena N, Argenton F, Newfeld SJ, Piccolo S", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "19135894", "url": "https://glygen.org/publication/PubMed/19135894" } ] }, { "title": "USP17 regulates Ras activation and cell proliferation by blocking RCE1 activity.", "journal": "The Journal of biological chemistry", "date": "2009", "authors": "Burrows JF, Kelvin AA, McFarlane C, Burden RE, McGrattan MJ, De la Vega M, Govender U, Quinn DJ, Dib K, Gadina M, Scott CJ, Johnston JA", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "19188362", "url": "https://glygen.org/publication/PubMed/19188362" } ] }, { "title": "Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2.", "journal": "Proceedings of the National Academy of Sciences of the United States of America", "date": "2009", "authors": "Shenoy SK, Modi AS, Shukla AK, Xiao K, Berthouze M, Ahn S, Wilkinson KD, Miller WE, Lefkowitz RJ", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "19363159", "url": "https://glygen.org/publication/PubMed/19363159" } ] }, { "title": "The deubiquitinating enzyme USP10 regulates the post-endocytic sorting of cystic fibrosis transmembrane conductance regulator in airway epithelial cells.", "journal": "The Journal of biological chemistry", "date": "2009", "authors": "Bomberger JM, Barnaby RL, Stanton BA", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "19398555", "url": "https://glygen.org/publication/PubMed/19398555" } ] }, { "title": "The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic receptor recycling and resensitization.", "journal": "The EMBO journal", "date": "2009", "authors": "Berthouze M, Venkataramanan V, Li Y, Shenoy SK", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "19424180", "url": "https://glygen.org/publication/PubMed/19424180" } ] }, { "title": "MdmX is a substrate for the deubiquitinating enzyme USP2a.", "journal": "Oncogene", "date": "2010", "authors": "Allende-Vega N, Sparks A, Lane DP, Saville MK", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "19838211", "url": "https://glygen.org/publication/PubMed/19838211" } ] }, { "title": "USP11 negatively regulates TNFalpha-induced NF-kappaB activation by targeting on IkappaBalpha.", "journal": "Cellular signalling", "date": "2010", "authors": "Sun W, Tan X, Shi Y, Xu G, Mao R, Gu X, Fan Y, Yu Y, Burlingame S, Zhang H, Rednam SP, Lu X, Zhang T, Fu S, Cao G, Qin J, Yang J", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "19874889", "url": "https://glygen.org/publication/PubMed/19874889" } ] }, { "title": "Ubiquitin-specific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kappaB activation via binding to and deubiquitinating receptor-interacting protein 1.", "journal": "The Journal of biological chemistry", "date": "2010", "authors": "Xu G, Tan X, Wang H, Sun W, Shi Y, Burlingame S, Gu X, Cao G, Zhang T, Qin J, Yang J", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "19910467", "url": "https://glygen.org/publication/PubMed/19910467" } ] }, { "title": "USP10 regulates p53 localization and stability by deubiquitinating p53.", "journal": "Cell", "date": "2010", "authors": "Yuan J, Luo K, Zhang L, Cheville JC, Lou Z", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "20096447", "url": "https://glygen.org/publication/PubMed/20096447" } ] }, { "title": "Ubiquitin hydrolase Dub3 promotes oncogenic transformation by stabilizing Cdc25A.", "journal": "Nature cell biology", "date": "2010", "authors": "Pereg Y, Liu BY, O'Rourke KM, Sagolla M, Dey A, Komuves L, French DM, Dixit VM", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "20228808", "url": "https://glygen.org/publication/PubMed/20228808" } ] }, { "title": "The ubiquitin-specific protease 17 is involved in virus-triggered type I IFN signaling.", "journal": "Cell research", "date": "2010", "authors": "Chen R, Zhang L, Zhong B, Tan B, Liu Y, Shu HB", "evidence": [ { 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Journal of biological chemistry", "date": "2013", "authors": "Burska UL, Harle VJ, Coffey K, Darby S, Ramsey H, O'Neill D, Logan IR, Gaughan L, Robson CN", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "24056413", "url": "https://glygen.org/publication/PubMed/24056413" } ] }, { "title": "Ubiquitin-specific proteases 25 negatively regulates virus-induced type I interferon signaling.", "journal": "PloS one", "date": "2013", "authors": "Zhong H, Wang D, Fang L, Zhang H, Luo R, Shang M, Ouyang C, Ouyang H, Chen H, Xiao S", "evidence": [ { "database": "Reactome", "id": "R-HSA-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5689880" } ], "reference": [ { "type": "PubMed", "id": "24260525", "url": "https://glygen.org/publication/PubMed/24260525" } ] }, { "title": "USP21 negatively regulates antiviral response by acting as a RIG-I deubiquitinase.", 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"http://www.informatics.jax.org/homology/45936787", "database": "MGI" } ], "common_name": "Human" }, { "uniprot_canonical_ac": "C9JVI0-1", "protein_name": "Ubiquitin carboxyl-terminal hydrolase 17-like protein 11", "gene_name": "USP17L11", "tax_id": 9606, "organism": "Homo sapiens", "sequence": { "sequence": "MEDDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSCETRVDLCDDLAPVARQLAPREKLPLSSRRPAAVGAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQTNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRATQGELKRDHPCLQAPELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVRKVEGTLPPDVLVIHQSKYKCGMKNHHPEQQSSLLNLSSTTPTHQESMNTGTLASLRGRARRSKGKNKHSKRALLVCQ", "length": 530 }, "evidence": [ { "id": "45936788", "url": "http://www.informatics.jax.org/homology/45936788", "database": "MGI" }, { "id": "45936789", "url": "http://www.informatics.jax.org/homology/45936789", "database": "MGI" }, { "id": "45936785", "url": "http://www.informatics.jax.org/homology/45936785", "database": "MGI" }, { "id": "45936786", "url": "http://www.informatics.jax.org/homology/45936786", "database": "MGI" }, { "id": "45936787", "url": "http://www.informatics.jax.org/homology/45936787", "database": "MGI" } ], "common_name": "Human" }, { "uniprot_canonical_ac": "D6R901-1", "protein_name": "Ubiquitin carboxyl-terminal hydrolase 17-like protein 21", "gene_name": "USP17L21", "tax_id": 9606, "organism": "Homo sapiens", "sequence": { "sequence": "MEEDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSCETRVDLCDDLAPVARQLAPREKLPLSNRRPAAVGAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKMLTLLTSAKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQPNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRATQGELKRDHPCLQAPELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVRKVEGTLPPDVLVIHQSKYKCGMKNHHPEQQSSLLNLSSSTPTHQESMNTGTLASLRGRARRSKGKNKHSKRALLVCQ", "length": 530 }, "evidence": [ { "id": "45936788", "url": "http://www.informatics.jax.org/homology/45936788", "database": "MGI" }, { "id": "45936789", "url": "http://www.informatics.jax.org/homology/45936789", "database": "MGI" }, { "id": "45936785", "url": "http://www.informatics.jax.org/homology/45936785", "database": "MGI" }, { "id": "45936786", "url": "http://www.informatics.jax.org/homology/45936786", "database": "MGI" }, { "id": "45936787", "url": "http://www.informatics.jax.org/homology/45936787", "database": "MGI" } ], "common_name": "Human" }, { "uniprot_canonical_ac": "D6RA61-1", "protein_name": "Ubiquitin carboxyl-terminal hydrolase 17-like protein 22", "gene_name": "USP17L22", "tax_id": 9606, "organism": "Homo sapiens", "sequence": { "sequence": "MEDDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSCETRVDLCDDLAPVARQLAPREKLPLSSRRPAAVGAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRATQGELKRDHPCLQAPELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVRKVEGTLPPDVLVIHQSKYKCGMKNHHPEQQSSLLKLSSTTPTHQESMNTGTLASLRGRARRSKGKNKHSKRALLVCQ", "length": 530 }, "evidence": [ { "id": "45936788", "url": "http://www.informatics.jax.org/homology/45936788", "database": "MGI" }, { "id": "45936789", "url": "http://www.informatics.jax.org/homology/45936789", "database": "MGI" }, { "id": "45936785", "url": "http://www.informatics.jax.org/homology/45936785", "database": "MGI" }, { "id": "45936786", "url": "http://www.informatics.jax.org/homology/45936786", "database": "MGI" }, { "id": "45936787", "url": "http://www.informatics.jax.org/homology/45936787", "database": "MGI" } ], "common_name": "Human" }, { "uniprot_canonical_ac": "D6RBQ6-1", "protein_name": "Ubiquitin carboxyl-terminal hydrolase 17-like protein 17", "gene_name": "USP17L17", "tax_id": 9606, "organism": "Homo sapiens", "sequence": { "sequence": "MEDDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSCETRVDLCDDLAPVARQLAPREKLPLSSRRPAAVGAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTAASITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRATQGELKRDHPCLQAPELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVRKVEGTLPPDVLVIHQSKYKCGMKNHHPEQQSSLLNLSSSTPTHQESMNTGTLASLRGRARRSKGKNKHSKRALLVCQ", "length": 530 }, "evidence": [ { "id": "45936788", "url": "http://www.informatics.jax.org/homology/45936788", "database": "MGI" }, { "id": "45936789", "url": "http://www.informatics.jax.org/homology/45936789", "database": "MGI" }, { "id": "45936785", "url": "http://www.informatics.jax.org/homology/45936785", "database": "MGI" }, { "id": "45936786", "url": "http://www.informatics.jax.org/homology/45936786", "database": "MGI" }, { "id": "45936787", "url": "http://www.informatics.jax.org/homology/45936787", "database": "MGI" } ], "common_name": "Human" }, { "uniprot_canonical_ac": "D6RCP7-1", "protein_name": "Ubiquitin carboxyl-terminal hydrolase 17-like protein 19", "gene_name": "USP17L19", "tax_id": 9606, "organism": "Homo sapiens", "sequence": { "sequence": "MEEDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSCETRVDLCDDLAPVARQLAPREKLPLSSRRPAAVGAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQTNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRATQGELKRDHPCLQAPELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVRKVEGTLPPDVLVIHQSKYKCGMKNHHPEQQSSLLKLSSTTPTHQESMNTGTLASLRGRARRSKGKNKHSKRALLVCQ", "length": 530 }, "evidence": [ { "id": "45936788", "url": "http://www.informatics.jax.org/homology/45936788", "database": "MGI" }, { "id": "45936789", "url": "http://www.informatics.jax.org/homology/45936789", "database": "MGI" }, { "id": "45936785", "url": "http://www.informatics.jax.org/homology/45936785", "database": "MGI" }, { "id": "45936786", "url": "http://www.informatics.jax.org/homology/45936786", "database": "MGI" }, { "id": "45936787", "url": "http://www.informatics.jax.org/homology/45936787", "database": "MGI" } ], "common_name": "Human" }, { "uniprot_canonical_ac": "D6RJB6-1", "protein_name": "Ubiquitin carboxyl-terminal hydrolase 17-like protein 20", "gene_name": "USP17L20", "tax_id": 9606, "organism": "Homo sapiens", "sequence": { "sequence": "MEDDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSCETRVDLCDDLAPVARQLAPREKLPLSSRRPAAVGAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQPNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRATQGELKRDHPCLQAPELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVRKVEGTLPPDVLVIHQSKYKCGMKNHHPEQQSSLLNLSSTTPTHQESMNTGTLASLRGRARRSKGKNKHSKRALLVCQ", "length": 530 }, "evidence": [ { "id": "45936788", "url": "http://www.informatics.jax.org/homology/45936788", "database": "MGI" }, { "id": "45936789", "url": "http://www.informatics.jax.org/homology/45936789", "database": "MGI" }, { "id": "45936785", "url": "http://www.informatics.jax.org/homology/45936785", "database": "MGI" }, { "id": "45936786", "url": "http://www.informatics.jax.org/homology/45936786", "database": "MGI" }, { "id": "45936787", "url": "http://www.informatics.jax.org/homology/45936787", "database": "MGI" } ], "common_name": "Human" }, { "uniprot_canonical_ac": "E9Q9U0-1", "protein_name": "Ubiquitin carboxyl-terminal hydrolase 17-like protein B", "gene_name": "Usp17lb", "tax_id": 10090, "organism": "Mus musculus", "sequence": { "sequence": "MVVALSFPEADPAMSPPSAPELHQDEAQVVEELAANGKHSLSWESPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCKMCAMEAHVTQSLLHTHSGDVMKPSQNLTSAFHKRKQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGWWRSQIKCHHCQGTSYSYDPFLDIPLDISSVQSVKQALQDTEKAEELCGENSYYCGRCRQKKPASKTLKLYSAPKVLMLVLKRFSGSMGKKLDRKVSYPEFLDLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFCCVKAGHGKWYKMDDTKVTSCDVTSVLNENAYVLFYVQQNDLKKGSINMPEGRIHEVLDAKYQLKKSGEKKHNKSPCTEDAGEPCENREKRSSKETSLGEGKVLQEQDHQKAGQKQENTKLTPQEQNHEKGGQNLRNTEGELDRLSGAIVVYQPICTAN", "length": 468 }, "evidence": [ { "id": "45936789", "url": "http://www.informatics.jax.org/homology/45936789", "database": "MGI" } ], "common_name": "Mouse" }, { "uniprot_canonical_ac": "G5E8G2-1", "protein_name": "Ubiquitin carboxyl-terminal hydrolase 17-like protein D", "gene_name": "Usp17ld", "tax_id": 10090, "organism": "Mus musculus", "sequence": { "sequence": "MVVSLSFPEADPALSSPGAQQLHQDEAQVVVELTANDKPSLSWECPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCKMCAMEAHVTQSLLHSHSGDVMKPSQILTSAFHKHQQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSAQSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSAFMGNKLDRKVSYPEFLDLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFSYVKAGHGKWYKMDDTKVTSCDVTSVLNENAYVLFYVQQTDLKEVSIDMPEGRIHEVLDPEYQLKKSRRKKHKKKSPCTEDVGEPSKNREKKATKETSLGEGKVLQEKNHKKAGQKHENTKLVPQEQNHQKLGQKHRNNEILPQEQNHQKTGQSLRNTEGELDLPADAIVIHLPRSIANWGRDTPDKVNQPWHNADRLLTSQDLVNTGQLCRQEGRRRSKKGKNKNKQGQKLLLVR", "length": 545 }, "evidence": [ { "id": "45936787", "url": "http://www.informatics.jax.org/homology/45936787", "database": "MGI" } ], "common_name": "Mouse" }, { "uniprot_canonical_ac": "G5E8I7-1", "protein_name": "Ubiquitin carboxyl-terminal hydrolase 17-like protein C", "gene_name": "Usp17lc", "tax_id": 10090, "organism": "Mus musculus", "sequence": { "sequence": "MVVSLSFPEADPALSSPGAQQLHQDEAQVVVELTANDKPSLSWECPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCKMCAMEAHVTQSLLHSHSGDVMKPSQILTSAFHKHQQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSAQSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSAFMGNKLDRKVSYPEFLDLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFSYVKARHGAWYKMDDTKVTSCDVTSVLNENAYVLFYVQQTDLKQVSIDMPEGRVHEVLDPEYQLKKSRRKKHKKKSPCTEDAGEPCKNREKRATKETSLGEGKVLQEKNHKKAGQKHENTKLVPQEQNHQKLGQKHRINEILPQEQNHQKAGQSLRNTEGELDLPADAIVIHLLRSTENWGRDAPDKENQPWHNADRLLTSQDPVNTGQLCRQEGRRRSKKGKNKNKQGQRLLLVC", "length": 545 }, "evidence": [ { "id": "45936786", "url": "http://www.informatics.jax.org/homology/45936786", "database": "MGI" } ], "common_name": "Mouse" }, { "uniprot_canonical_ac": "P0C7H9-1", "protein_name": "Inactive ubiquitin carboxyl-terminal hydrolase 17-like protein 7", "gene_name": "USP17L7", "tax_id": 9606, "organism": "Homo sapiens", "sequence": { "sequence": "MEDDSLYLGGDWQFNHFSKLTSSRLDAAFAEIQRTSLSEKSPLSSETRFDLCDDLAPVARQLAPREKLPLSSRRPAAVGAGLQKIGNTFYVNVSLQCLTYTLPLSNYMLSREDSQTCHLHKCCMFCTMQAHITWALHSPGHVIQPSQVLAAGFHRGEQEDAHEFLMFTVDAMKKACLPGHKQLDHHSKDTTLIHQIFGAYWRSQIKYLHCHGVSDTFDPYLDIALDIQAAQSVKQALEQLVKPKELNGENAYHCGLCLQKAPASKTLTLPTSAKVLILVLKRFSDVTGNKLAKNVQYPKCRDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASGITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRPATQGELKRDHPCLQVPELDEHLVERATQESTLDHWKFPQEQNKTKPEFNVRKVEGTLPPNVLVIHQSKYKCGMKNHHPEQQSSLLNLSSTKPTDQESMNTGTLASLQGSTRRSKGNNKHSKRSLLVCQ", "length": 530 }, "evidence": [ { "id": "45936788", "url": "http://www.informatics.jax.org/homology/45936788", "database": "MGI" }, { "id": "45936789", "url": "http://www.informatics.jax.org/homology/45936789", "database": "MGI" }, { "id": "45936785", "url": "http://www.informatics.jax.org/homology/45936785", "database": "MGI" }, { "id": "45936786", "url": "http://www.informatics.jax.org/homology/45936786", "database": "MGI" }, { "id": "45936787", "url": "http://www.informatics.jax.org/homology/45936787", "database": "MGI" } ], "common_name": "Human" }, { "uniprot_canonical_ac": "P0C7I0-1", "protein_name": "Inactive ubiquitin carboxyl-terminal hydrolase 17-like protein 8", "gene_name": "USP17L8", "tax_id": 9606, "organism": "Homo sapiens", "sequence": { "sequence": "MEDDSLYLGGEWQFNHFSKLTSPRPDAAFAEIQRTSLPEKSPLSSETRVDLCDDLAPVARQLAPREKLPLSSRRPAAVGAGLQNMGNTCYLNASLQCLTYTPPLANYMLSREHSQTCQRPKCCMLCTMQAHITWALHSPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVKQALEQLVKPEELNGENAYPCGLCLQRAPASNTLTLHTSAKVLILVLKRFCDVTGNKLAKNVQYPECLDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHNGYYFSYVKAQEGQWYKMDDAEVTACSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRPATQGELKRDHPCLQVPELDEHLVERATEESTLDHWKFPQEQNKMKPEFNVRKVEGTLPPNVLVIHQSKYKCGMKNHHPEQQSSLLNLSSMNSTDQESMNTGTLASLQGRTRRSKGKNKHSKRSLLVCQ", "length": 530 }, "evidence": [ { "id": "45936788", "url": "http://www.informatics.jax.org/homology/45936788", "database": "MGI" }, { "id": "45936789", "url": "http://www.informatics.jax.org/homology/45936789", "database": "MGI" }, { "id": "45936785", "url": "http://www.informatics.jax.org/homology/45936785", "database": "MGI" }, { "id": "45936786", "url": "http://www.informatics.jax.org/homology/45936786", "database": "MGI" }, { "id": "45936787", "url": "http://www.informatics.jax.org/homology/45936787", "database": "MGI" } ], "common_name": "Human" }, { "uniprot_canonical_ac": "Q0WX57-1", "protein_name": "Ubiquitin carboxyl-terminal hydrolase 17-like protein 24", "gene_name": "USP17L30", "tax_id": 9606, "organism": "Homo sapiens", "sequence": { "sequence": "MEDDSLYLRGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSCETRVDLCDDLAPVARQLAPREKLPLSSRRPAAVGAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQPNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRATQGELKRDHPCLQAPELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVRKVEGTLPPDVLVIHQSKYKCGMKNHHPEQQSSLLNLSSSTPTHQESMNTGTLASLRGRARRSKGKNKHSKRALLVCQ", "length": 530 }, "evidence": [ { "id": "45936788", "url": "http://www.informatics.jax.org/homology/45936788", "database": "MGI" }, { "id": "45936789", "url": "http://www.informatics.jax.org/homology/45936789", "database": "MGI" }, { "id": "45936785", "url": "http://www.informatics.jax.org/homology/45936785", "database": "MGI" }, { "id": "45936786", "url": "http://www.informatics.jax.org/homology/45936786", "database": "MGI" }, { "id": "45936787", "url": "http://www.informatics.jax.org/homology/45936787", "database": "MGI" } ], "common_name": "Human" }, { "uniprot_canonical_ac": "Q61068-1", "protein_name": "Ubiquitin carboxyl-terminal hydrolase 17-like protein A", "gene_name": "Usp17la", "tax_id": 10090, "organism": "Mus musculus", "sequence": { "sequence": "MVVALSFPEADPALSSPDAPELHQDEAQVVEELTVNGKHSLSWESPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCKLCAMEALVTQSLLHSHSGDVMKPSHILTSAFHKHQQEDAHEFLMFTLETMHESCLQVHRQSKPTSEDSSPIHDIFGGWWRSQIKCLLCQGTSDTYDRFLDIPLDISSAQSVKQALWDTEKSEELCGDNAYYCGKCRQKMPASKTLHVHIAPKVLMVVLNRFSAFTGNKLDRKVSYPEFLDLKPYLSEPTGGPLPYALYAVLVHDGATSHSGHYFCCVKAGHGKWYKMDDTKVTRCDVTSVLNENAYVLFYVQQANLKQVSIDMPEGRINEVLDPEYQLKKSRRKKHKKKSPFTEDLGEPCENRDKRAIKETSLGKGKVLQEVNHKKAGQKHGNTKLMPQKQNHQKAGQNLRNTEVELDLPADAIVIHQPRSTANWGRDSPDKENQPLHNADRLLTSQGPVNTWQLCRQEGRRRSKKGQNKNKQGQRLLLVC", "length": 526 }, "evidence": [ { "id": "45936788", "url": "http://www.informatics.jax.org/homology/45936788", "database": "MGI" } ], "common_name": "Mouse" }, { "uniprot_canonical_ac": "Q6R6M4-1", "protein_name": "Ubiquitin carboxyl-terminal hydrolase 17", "gene_name": "USP17L2", "tax_id": 9606, "organism": "Homo sapiens", "sequence": { "sequence": "MEDDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSSEARVDLCDDLAPVARQLAPRKKLPLSSRRPAAVGAGLQNMGNTCYENASLQCLTYTPPLANYMLSREHSQTCQRPKCCMLCTMQAHITWALHSPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVKQALEQLVKPEELNGENAYHCGLCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKLAKNVQYPECLDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHDGHYFSYVKAQEGQWYKMDDAKVTACSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRATQGELKRDHPCLQAPELDERLVERATQESTLDHWKFPQEQNKTKPEFNVRKVEGTLPPNVLVIHQSKYKCGMKNHHPEQQSSLLNLSSTTRTDQESVNTGTLASLQGRTRRSKGKNKHSKRALLVCQ", "length": 530 }, "evidence": [ { "id": "45936788", "url": "http://www.informatics.jax.org/homology/45936788", "database": "MGI" }, { "id": "45936789", "url": "http://www.informatics.jax.org/homology/45936789", "database": "MGI" }, { "id": "45936785", "url": "http://www.informatics.jax.org/homology/45936785", "database": "MGI" }, { "id": "45936786", "url": "http://www.informatics.jax.org/homology/45936786", "database": "MGI" }, { "id": "45936787", "url": "http://www.informatics.jax.org/homology/45936787", "database": "MGI" } ], "common_name": "Human" }, { "uniprot_canonical_ac": "Q7M764-1", "protein_name": "Ubiquitin carboxyl-terminal hydrolase 17-like protein E", "gene_name": "Usp17le", "tax_id": 10090, "organism": "Mus musculus", "sequence": { "sequence": "MVVSLSFPEETGGENLPSAPLEDSSKFFEEVFGDMVFARSFPEADPALSSPDAPELHQDEAQVVEELTTNGKHSLSWESPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCKMCAMEAHVTQSLLHSHSGDVMKPSQILTSAFHKHQQEDAHEFLMFTLETMHESCLQVHRQSDPTPQDTSPIHDIFGGWWRSQIKCLHCQGTSHTFDPFLDVPLDISSAQSVNQALWDTGKSEELLGENAYYCGRCRQKMPASKTLHVHIAPKVLLLVLKRFSAFTGNKLDRKVSYPEFLDLKPYLSEPTGGPLPYALYAVLVHDGATSNSGHYFCCVKAGHGKWYKMDDTKVTRCDVTSVLNENAYVLFYVQQTDLKQVSIDMPEGRVHEVLDPKYQLKKSRRKKRKKQCHCTDDAGEACENREKRAKKETSLGEGKVPQEVNHEKAGQKHGNTKLVPQEQNHQRAGQNLRNTEVELDLPVDAIVIHQPRSTANWGTDAPDKENQPWHNGDRLLTSQGLMSPGQLCSQGGR", "length": 540 }, "evidence": [ { "id": "45936785", "url": "http://www.informatics.jax.org/homology/45936785", "database": "MGI" } ], "common_name": "Mouse" }, { "uniprot_canonical_ac": "Q7RTZ2-1", "protein_name": "Ubiquitin carboxyl-terminal hydrolase 17-like protein 1", "gene_name": "USP17L1", "tax_id": 9606, "organism": "Homo sapiens", "sequence": { "sequence": "MGDDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSSETRVDLCDDLAPVARQLAPREKLPLSSRRPAAVGAGLQNMGNTCYENASLQCLTYTLPLANYMLSREHSQTCQRPKCCMLCTMQAHITWALHSPGHVIQPSQALAAGFHRGKQEDVHEFLMFTVDAMKKACLPGHKQVDHHCKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVKQALEQLVKPEELNGENAYHCGLCLQRAPASNTLTLHTSAKVLILVLKRFSDVAGNKLAKNVQYPECLDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHDGHYFSYVKAQEVQWYKMDDAEVTVCSIISVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRAKQGELKRDHPCLQAPELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVGKVEGTLPPNALVIHQSKYKCGMKNHHPEQQSSLLNLSSTTRTDQESMNTGTLASLQGRTRRAKGKNKHSKRALLVCQ", "length": 530 }, "evidence": [ { "id": "45936788", "url": "http://www.informatics.jax.org/homology/45936788", "database": "MGI" }, { "id": "45936789", "url": "http://www.informatics.jax.org/homology/45936789", "database": "MGI" }, { "id": "45936785", "url": "http://www.informatics.jax.org/homology/45936785", "database": "MGI" }, { "id": "45936786", "url": "http://www.informatics.jax.org/homology/45936786", "database": "MGI" }, { "id": "45936787", "url": "http://www.informatics.jax.org/homology/45936787", "database": "MGI" } ], "common_name": "Human" } ], "go_annotation": { "categories": [ { "name": "Cellular Component", "total": 3, "go_terms": [ { "name": "nucleus", "id": "GO:0005634", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005634", "evidence": [ { "database": "UniProtKB", "id": "D6R9N7", "url": "https://www.uniprot.org/uniprot/D6R9N7" } ], "pmid": "" }, { "name": "endoplasmic reticulum", "id": "GO:0005783", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005783", "evidence": [ { "database": "UniProtKB", "id": "D6R9N7", "url": "https://www.uniprot.org/uniprot/D6R9N7" } ], "pmid": "" }, { "name": "cytosol", "id": "GO:0005829", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005829", "evidence": [ { "database": "UniProtKB", "id": "D6R9N7", "url": "https://www.uniprot.org/uniprot/D6R9N7" } ], "pmid": "" } ] }, { "name": "Biological Process", "total": 2, "go_terms": [ { "name": "proteolysis", "id": "GO:0006508", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006508", "evidence": [ { "database": "UniProtKB", "id": "D6R9N7", "url": "https://www.uniprot.org/uniprot/D6R9N7" } ], "pmid": "" }, { "name": "regulation of apoptotic process", "id": "GO:0042981", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042981", "evidence": [ { "database": "UniProtKB", "id": "D6R9N7", "url": "https://www.uniprot.org/uniprot/D6R9N7" } ], "pmid": "" } ] }, { "name": "Molecular Function", "total": 1, "go_terms": [ { "name": "cysteine-type deubiquitinase activity", "id": "GO:0004843", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004843", "evidence": [ { "database": "UniProtKB", "id": "D6R9N7", "url": "https://www.uniprot.org/uniprot/D6R9N7" } ], "pmid": "" } ] } ] }, "pro_annotation": [], "site_annotation": [ { "start_pos": 444, "end_pos": 446, "annotation": "n_glycosylation_sequon" }, { "start_pos": 488, "end_pos": 490, "annotation": "n_glycosylation_sequon" }, { "start_pos": 92, "end_pos": 94, "annotation": "n_glycosylation_sequon" } ], "ptm_annotation": [], "interactions": [], "reactions": [ { "id": "R-HSA-5696600", "name": "USP17 deubiquitinates RCE1, CDC25A, DDX58, IFIH1", "equation": "", "summary": "USP17 regulates cell proliferation by deubiquitinating and inhibiting RCE1, which influences the localization and activation of the small GTPases NRAS and HRAS (Burrows et al. 2009). In addition, USP17 mediates deubiquitination of CDC25A, which prevents CDC25A degradation by the proteasome during the G1/S and G2/M phases, promoting cell-cycle progression (Pereq et al. 2010). USP17 cleaves Lys-48 and Lys-63-linked polyubiquitin chains from the cytoplasmic innate immune receptors DDX58 (RIG-I) and IFIH1 (MDA5), which increases activation of the IFN-beta promoter, part of the cellular response to viral infection (Chen et al. 2010). USP17 expression is upregulated by interleukin-4 and interleukin-6 (Burrows et al. 2004).", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q9Y256-1", "P30304-1", "Q9BYX4-1", "Q6R6M4-1", "Q7RTZ2-1", "C9JPN9-1", "O95786-1", "C9JJH3-1", "A6NCW0-1", "A8MUK1-1", "C9J2P7-1", "C9JLJ4-1", "C9JVI0-1", "D6R9N7-1", "D6RA61-1", "D6RBQ6-1", "D6RCP7-1", "D6RJB6-1", "D6R901-1", "Q0WX57-1" ], "evidence": [ { "id": "R-HSA-5696600", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5696600" } ] }, { "id": "R-HSA-6782820", "name": "USP17 deubiquitinates SUDS3", "equation": "", "summary": "USP17 removes Lys-63-linked ubiquitin chains from SDS3, a key component of the histone deacetylase (HDAC)-dependent Sin3A co-repressor complex, serving to maintain its HDAC activity (Ramakrishna et al. 2011).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q6R6M4-1", "Q7RTZ2-1", "C9JPN9-1", "C9JJH3-1", "A6NCW0-1", "A8MUK1-1", "C9J2P7-1", "C9JLJ4-1", "C9JVI0-1", "D6R9N7-1", "D6RA61-1", "D6RBQ6-1", "D6RCP7-1", "D6RJB6-1", "D6R901-1", "Q0WX57-1" ], "evidence": [ { "id": "R-HSA-6782820", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6782820" } ] } ], "reaction_participants": [], "reaction_enzymes": [ { "uniprot_ac": "A6NCW0", "gene_name": "USP17L3", "activity": [ { "ec_number": "3.4.19.12", "activity": "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).", "evidence": [ { "id": "A6NCW0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/A6NCW0" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "A6NCW0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/A6NCW0" } ] } ] }, { "uniprot_ac": "A8MUK1", "gene_name": "USP17L5", "activity": [ { "ec_number": "3.4.19.12", "activity": "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).", "evidence": [ { "id": "A8MUK1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/A8MUK1" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "A8MUK1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/A8MUK1" } ] } ] }, { "uniprot_ac": "C9J2P7", "gene_name": "USP17L15", "activity": [ { "ec_number": "3.4.19.12", "activity": "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).", "evidence": [ { "id": "C9J2P7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/C9J2P7" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "C9J2P7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/C9J2P7" } ] } ] }, { "uniprot_ac": "C9JJH3", "gene_name": "USP17L10", "activity": [ { "ec_number": "3.4.19.12", "activity": "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).", "evidence": [ { "id": "C9JJH3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/C9JJH3" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "C9JJH3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/C9JJH3" } ] } ] }, { "uniprot_ac": "C9JLJ4", "gene_name": "USP17L13", "activity": [ { "ec_number": "3.4.19.12", "activity": "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).", "evidence": [ { "id": "C9JLJ4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/C9JLJ4" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "C9JLJ4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/C9JLJ4" } ] } ] }, { "uniprot_ac": "C9JPN9", "gene_name": "USP17L12", "activity": [ { "ec_number": "3.4.19.12", "activity": "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).", "evidence": [ { "id": "C9JPN9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/C9JPN9" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "C9JPN9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/C9JPN9" } ] } ] }, { "uniprot_ac": "C9JVI0", "gene_name": "USP17L11", "activity": [ { "ec_number": "3.4.19.12", "activity": "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).", "evidence": [ { "id": "C9JVI0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/C9JVI0" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "C9JVI0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/C9JVI0" } ] } ] }, { "uniprot_ac": "D6R901", "gene_name": "USP17L21", "activity": [ { "ec_number": "3.4.19.12", "activity": "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).", "evidence": [ { "id": "D6R901", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6R901" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "D6R901", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6R901" } ] } ] }, { "uniprot_ac": "D6R9N7", "gene_name": "USP17L18", "activity": [ { "ec_number": "3.4.19.12", "activity": "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).", "evidence": [ { "id": "D6R9N7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6R9N7" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "D6R9N7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6R9N7" } ] } ] }, { "uniprot_ac": "D6RA61", "gene_name": "USP17L22", "activity": [ { "ec_number": "3.4.19.12", "activity": "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).", "evidence": [ { "id": "D6RA61", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RA61" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "D6RA61", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RA61" } ] } ] }, { "uniprot_ac": "D6RBQ6", "gene_name": "USP17L17", "activity": [ { "ec_number": "3.4.19.12", "activity": "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).", "evidence": [ { "id": "D6RBQ6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RBQ6" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "D6RBQ6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RBQ6" } ] } ] }, { "uniprot_ac": "D6RCP7", "gene_name": "USP17L19", "activity": [ { "ec_number": "3.4.19.12", "activity": "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).", "evidence": [ { "id": "D6RCP7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RCP7" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "D6RCP7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RCP7" } ] } ] }, { "uniprot_ac": "D6RJB6", "gene_name": "USP17L20", "activity": [ { "ec_number": "3.4.19.12", "activity": "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).", "evidence": [ { "id": "D6RJB6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RJB6" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "D6RJB6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RJB6" } ] } ] }, { "uniprot_ac": "O95786", "gene_name": "RIGI", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O95786", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O95786" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "O95786", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O95786" } ] } ] }, { "uniprot_ac": "P30304", "gene_name": "CDC25A", "activity": [ { "ec_number": "3.1.3.48", "activity": "H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate.", "evidence": [ { "id": "P30304", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P30304" } ] }, { "ec_number": "3.1.3.48", "activity": "", "evidence": [ { "id": "P30304", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P30304" } ] } ] }, { "uniprot_ac": "Q0WX57", "gene_name": "USP17L30", "activity": [ { "ec_number": "3.4.19.12", "activity": "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).", "evidence": [ { "id": "Q0WX57", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q0WX57" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "Q0WX57", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q0WX57" } ] } ] }, { "uniprot_ac": "Q6R6M4", "gene_name": "USP17L2", "activity": [ { "ec_number": "3.4.19.12", "activity": "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).", "evidence": [ { "id": "Q6R6M4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q6R6M4" } ] }, { "ec_number": "3.4.19.12", "activity": "", 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