ID U17LO_HUMAN Reviewed; 530 AA. AC Q0WX57; A8MRA9; Q0WX56; Q3BEM1; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 2. DT 27-MAR-2024, entry version 129. DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 17-like protein 24; DE EC=3.4.19.12; DE AltName: Full=Deubiquitinating enzyme 17; DE AltName: Full=Ubiquitin thioesterase 17; DE AltName: Full=Ubiquitin-specific-processing protease 17; GN Name=USP17L24; GN Synonyms=USP17, USP17H, USP17I, USP17J, USP17K, USP17L, USP17M; GN and GN Name=USP17L25; GN and GN Name=USP17L26; GN and GN Name=USP17L27; GN and GN Name=USP17L28; GN and GN Name=USP17L29; GN and GN Name=USP17L30; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE RP SPECIFICITY, AND MUTAGENESIS OF CYS-89. RX PubMed=10936051; DOI=10.1006/geno.2000.6261; RA Saitoh Y., Miyamoto N., Okada T., Gondo Y., Showguchi-Miyata J., Hadano S., RA Ikeda J.-E.; RT "The RS447 human megasatellite tandem repetitive sequence encodes a novel RT deubiquitinating enzyme with a functional promoter."; RL Genomics 67:291-300(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], NOMENCLATURE, SUBCELLULAR LOCATION, CATALYTIC RP ACTIVITY, AND MUTAGENESIS OF CYS-89. RX PubMed=17109758; DOI=10.1186/1471-2164-7-292; RA Shin J.-M., Yoo K.-J., Kim M.-S., Kim D., Baek K.-H.; RT "Hyaluronan- and RNA-binding deubiquitinating enzymes of USP17 family RT members associated with cell viability."; RL BMC Genomics 7:292-292(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] RP IDENTIFICATION. RX PubMed=11941478; DOI=10.1007/s00439-002-0698-2; RA Okada T., Gondo Y., Goto J., Kanazawa I., Hadano S., Ikeda J.E.; RT "Unstable transmission of the RS447 human megasatellite tandem repetitive RT sequence that contains the USP17 deubiquitinating enzyme gene."; RL Hum. Genet. 110:302-313(2002). RN [5] RP IDENTIFICATION, AND NOMENCLATURE. RX PubMed=15780755; DOI=10.1016/j.ygeno.2004.11.013; RA Burrows J.F., McGrattan M.J., Johnston J.A.; RT "The DUB/USP17 deubiquitinating enzymes, a multigene family within a RT tandemly repeated sequence."; RL Genomics 85:524-529(2005). RN [6] RP IDENTIFICATION. RX PubMed=20403174; DOI=10.1186/1471-2164-11-250; RA Burrows J.F., Scott C.J., Johnston J.A.; RT "The DUB/USP17 deubiquitinating enzymes: a gene family within a tandemly RT repeated sequence, is also embedded within the copy number variable beta- RT defensin cluster."; RL BMC Genomics 11:250-250(2010). CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin CC from specific proteins to regulate different cellular processes that CC may include cell proliferation, progression through the cell cycle, CC apoptosis, cell migration, and the cellular response to viral CC infection. {ECO:0000269|PubMed:10936051}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- CC residue protein attached to proteins as an intracellular targeting CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:10936051, CC ECO:0000269|PubMed:17109758}; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17109758}. CC Endoplasmic reticulum {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, liver and skeletal CC muscle. {ECO:0000269|PubMed:10936051}. CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP17 subfamily. CC {ECO:0000305}. CC -!- CAUTION: The RS447 megasatellite DNA is a highly polymorphic conserved CC tandem repetitive sequence which contains a copy of the USP17 gene. It CC is present with an interindividual variation in copy number, ranging CC from 20 to 103, and can be found in the genome both on chromosome 4 and CC chromosome 8. The high similarity between the UPS17-like genes makes CC impossible to clearly assign data to one of the genes of the family. CC Oligonucleotides designed in RNAi experiments are for instance not CC specific of a given UPS17-like gene. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF544011; AAQ11741.1; -; mRNA. DR EMBL; AF544012; AAQ11742.1; -; mRNA. DR EMBL; AY188990; AAO38845.1; -; mRNA. DR EMBL; AC116655; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS59464.1; -. DR RefSeq; NP_001229255.1; NM_001242326.1. DR RefSeq; NP_001229256.1; NM_001242327.1. DR RefSeq; NP_001229257.1; NM_001242328.1. DR RefSeq; NP_001229259.1; NM_001242330.1. DR RefSeq; NP_001229260.1; NM_001242331.1. DR RefSeq; NP_001229261.1; NM_001242332.1. DR RefSeq; NP_001243796.1; NM_001256867.1. DR AlphaFoldDB; Q0WX57; -. DR SMR; Q0WX57; -. DR BioGRID; 608797; 1. DR BioGRID; 608820; 2. DR BioGRID; 608827; 1. DR BioGRID; 608832; 2. DR IntAct; Q0WX57; 7. DR STRING; 9606.ENSP00000422097; -. DR ChEMBL; CHEMBL4523281; -. DR MEROPS; C19.023; -. DR MEROPS; C19.078; -. DR iPTMnet; Q0WX57; -. DR PhosphoSitePlus; Q0WX57; -. DR BioMuta; USP17L25; -. DR DMDM; 187663978; -. DR jPOST; Q0WX57; -. DR MassIVE; Q0WX57; -. DR PaxDb; 9606-ENSP00000422097; -. DR PeptideAtlas; Q0WX57; -. DR Antibodypedia; 64154; 44 antibodies from 10 providers. DR Antibodypedia; 76737; 1 antibodies from 1 providers. DR Antibodypedia; 76742; 2 antibodies from 1 providers. DR DNASU; 728419; -. DR Ensembl; ENST00000504104.1; ENSP00000422887.1; ENSG00000228856.3. DR Ensembl; ENST00000504481.1; ENSP00000425375.1; ENSG00000232264.5. DR Ensembl; ENST00000504543.1; ENSP00000423777.1; ENSG00000231051.3. DR Ensembl; ENST00000509271.1; ENSP00000422097.1; ENSG00000230430.5. DR Ensembl; ENST00000509660.1; ENSP00000427366.1; ENSG00000229579.5. DR Ensembl; ENST00000511681.1; ENSP00000422969.1; ENSG00000231637.3. DR Ensembl; ENST00000515574.1; ENSP00000423211.1; ENSG00000235780.3. DR GeneID; 728369; -. DR GeneID; 728373; -. DR GeneID; 728379; -. DR GeneID; 728393; -. DR GeneID; 728400; -. DR GeneID; 728405; -. DR GeneID; 728419; -. DR KEGG; hsa:728369; -. DR KEGG; hsa:728373; -. DR KEGG; hsa:728379; -. DR KEGG; hsa:728393; -. DR KEGG; hsa:728400; -. DR KEGG; hsa:728405; -. DR KEGG; hsa:728419; -. DR MANE-Select; ENST00000504104.1; ENSP00000422887.1; NM_001256867.1; NP_001243796.1. DR MANE-Select; ENST00000504481.1; ENSP00000425375.1; NM_001242327.1; NP_001229256.1. DR MANE-Select; ENST00000504543.1; ENSP00000423777.1; NM_001242331.1; NP_001229260.1. DR MANE-Select; ENST00000509271.1; ENSP00000422097.1; NM_001242326.1; NP_001229255.1. DR MANE-Select; ENST00000509660.1; ENSP00000427366.1; NM_001242328.1; NP_001229257.1. DR MANE-Select; ENST00000511681.1; ENSP00000422969.1; NM_001242332.1; NP_001229261.1. DR MANE-Select; ENST00000515574.1; ENSP00000423211.1; NM_001242330.1; NP_001229259.1. DR UCSC; uc021xll.1; human. DR AGR; HGNC:44452; -. DR AGR; HGNC:44453; -. DR AGR; HGNC:44454; -. DR AGR; HGNC:44455; -. DR AGR; HGNC:44456; -. DR AGR; HGNC:44457; -. DR AGR; HGNC:44458; -. DR CTD; 728369; -. DR CTD; 728373; -. DR CTD; 728379; -. DR CTD; 728393; -. DR CTD; 728400; -. DR CTD; 728405; -. DR CTD; 728419; -. DR DisGeNET; 728369; -. DR DisGeNET; 728373; -. DR DisGeNET; 728379; -. DR DisGeNET; 728393; -. DR DisGeNET; 728400; -. DR DisGeNET; 728405; -. DR DisGeNET; 728419; -. DR GeneCards; USP17L24; -. DR GeneCards; USP17L25; -. DR GeneCards; USP17L26; -. DR GeneCards; USP17L27; -. DR GeneCards; USP17L28; -. DR GeneCards; USP17L29; -. DR GeneCards; USP17L30; -. DR HGNC; HGNC:44453; USP17L24. DR HGNC; HGNC:44452; USP17L25. DR HGNC; HGNC:44454; USP17L26. DR HGNC; HGNC:44455; USP17L27. DR HGNC; HGNC:44456; USP17L28. DR HGNC; HGNC:44457; USP17L29. DR HGNC; HGNC:44458; USP17L30. DR HPA; ENSG00000228856; Not detected. DR HPA; ENSG00000229579; Not detected. DR HPA; ENSG00000230430; Not detected. DR HPA; ENSG00000231051; Not detected. DR HPA; ENSG00000231637; Not detected. DR HPA; ENSG00000232264; Not detected. DR HPA; ENSG00000235780; Not detected. DR MIM; 607011; gene. DR neXtProt; NX_Q0WX57; -. DR OpenTargets; ENSG00000228856; -. DR VEuPathDB; HostDB:ENSG00000228856; -. DR VEuPathDB; HostDB:ENSG00000229579; -. DR VEuPathDB; HostDB:ENSG00000230430; -. DR VEuPathDB; HostDB:ENSG00000231051; -. DR VEuPathDB; HostDB:ENSG00000231637; -. DR VEuPathDB; HostDB:ENSG00000232264; -. DR VEuPathDB; HostDB:ENSG00000235780; -. DR eggNOG; KOG1865; Eukaryota. DR GeneTree; ENSGT00940000161948; -. DR HOGENOM; CLU_008279_10_0_1; -. DR InParanoid; Q0WX57; -. DR OMA; HAGWICH; -. DR OrthoDB; 227085at2759; -. DR PhylomeDB; Q0WX57; -. DR PathwayCommons; Q0WX57; -. DR Reactome; R-HSA-5689880; Ub-specific processing proteases. DR SignaLink; Q0WX57; -. DR BioGRID-ORCS; 728369; 10 hits in 182 CRISPR screens. DR BioGRID-ORCS; 728373; 17 hits in 153 CRISPR screens. DR BioGRID-ORCS; 728379; 12 hits in 169 CRISPR screens. DR BioGRID-ORCS; 728393; 13 hits in 133 CRISPR screens. DR BioGRID-ORCS; 728400; 14 hits in 478 CRISPR screens. DR BioGRID-ORCS; 728405; 17 hits in 175 CRISPR screens. DR BioGRID-ORCS; 728419; 10 hits in 131 CRISPR screens. DR Pharos; Q0WX57; Tbio. DR PRO; PR:Q0WX57; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q0WX57; Protein. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IMP:UniProtKB. DR GO; GO:0005540; F:hyaluronic acid binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:1904037; P:positive regulation of epithelial cell apoptotic process; IMP:UniProtKB. DR GO; GO:0071947; P:protein deubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central. DR CDD; cd02661; Peptidase_C19E; 1. DR Gene3D; 3.90.70.10; Cysteine proteinases; 1. DR InterPro; IPR006861; HABP4_PAIRBP1-bd. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR InterPro; IPR001394; Peptidase_C19_UCH. DR InterPro; IPR018200; USP_CS. DR InterPro; IPR028889; USP_dom. DR PANTHER; PTHR24006:SF651; INACTIVE UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 17-LIKE PROTEIN 4-RELATED; 1. DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1. DR Pfam; PF04774; HABP4_PAI-RBP1; 1. DR Pfam; PF00443; UCH; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR PROSITE; PS00972; USP_1; 1. DR PROSITE; PS00973; USP_2; 1. DR PROSITE; PS50235; USP_3; 1. PE 1: Evidence at protein level; KW Apoptosis; Endoplasmic reticulum; Hydrolase; Nucleus; Protease; KW Reference proteome; Thiol protease; Ubl conjugation pathway. FT CHAIN 1..530 FT /note="Ubiquitin carboxyl-terminal hydrolase 17-like FT protein 24" FT /id="PRO_0000331643" FT DOMAIN 80..375 FT /note="USP" FT REGION 382..412 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 477..530 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 478..508 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 89 FT /note="Nucleophile" FT ACT_SITE 334 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, FT ECO:0000255|PROSITE-ProRule:PRU10093" FT MUTAGEN 89 FT /note="C->S: Abolishes enzymatic activity. Loss of the FT pro-apoptotic function." FT /evidence="ECO:0000269|PubMed:10936051, FT ECO:0000269|PubMed:17109758" FT CONFLICT 9 FT /note="R -> G (in Ref. 2; AAO38845/AAQ11741/AAQ11742)" FT /evidence="ECO:0000305" FT CONFLICT 23 FT /note="S -> P (in Ref. 2; AAQ11742)" FT /evidence="ECO:0000305" FT CONFLICT 262 FT /note="P -> S (in Ref. 2; AAQ11741)" FT /evidence="ECO:0000305" FT CONFLICT 310 FT /note="P -> Q (in Ref. 2; AAQ11741/AAQ11742)" FT /evidence="ECO:0000305" FT CONFLICT 360 FT /note="T -> I (in Ref. 2; AAO38845)" FT /evidence="ECO:0000305" FT CONFLICT 361 FT /note="S -> P (in Ref. 2; AAQ11742)" FT /evidence="ECO:0000305" FT CONFLICT 364 FT /note="S -> T (in Ref. 2; AAQ11742)" FT /evidence="ECO:0000305" FT CONFLICT 392 FT /note="R -> S (in Ref. 2; AAO38845)" FT /evidence="ECO:0000305" FT CONFLICT 398 FT /note="D -> A (in Ref. 2; AAQ11742)" FT /evidence="ECO:0000305" FT CONFLICT 430 FT /note="Q -> H (in Ref. 2; AAQ11742)" FT /evidence="ECO:0000305" FT CONFLICT 492 FT /note="S -> T (in Ref. 2; AAO38845/AAQ11741/AAQ11742)" FT /evidence="ECO:0000305" FT CONFLICT 511 FT /note="R -> G (in Ref. 2; AAQ11742)" FT /evidence="ECO:0000305" SQ SEQUENCE 530 AA; 59711 MW; 5B0DC65280B2A098 CRC64; MEDDSLYLRG EWQFNHFSKL TSSRPDAAFA EIQRTSLPEK SPLSCETRVD LCDDLAPVAR QLAPREKLPL SSRRPAAVGA GLQNMGNTCY VNASLQCLTY TPPLANYMLS REHSQTCHRH KGCMLCTMQA HITRALHNPG HVIQPSQALA AGFHRGKQED AHEFLMFTVD AMKKACLPGH KQVDHHSKDT TLIHQIFGGY WRSQIKCLHC HGISDTFDPY LDIALDIQAA QSVQQALEQL VKPEELNGEN AYHCGVCLQR APASKTLTLH TSAKVLILVL KRFSDVTGNK IAKNVQYPEC LDMQPYMSQP NTGPLVYVLY AVLVHAGWSC HNGHYFSYVK AQEGQWYKMD DAEVTASSIT SVLSQQAYVL FYIQKSEWER HSESVSRGRE PRALGAEDTD RRATQGELKR DHPCLQAPEL DEHLVERATQ ESTLDHWKFL QEQNKTKPEF NVRKVEGTLP PDVLVIHQSK YKCGMKNHHP EQQSSLLNLS SSTPTHQESM NTGTLASLRG RARRSKGKNK HSKRALLVCQ //