U17LO_HUMAN
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 03-AUG-2022, entry version 120.
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}.
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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 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 PaxDb; Q0WX57; -.
DR PeptideAtlas; Q0WX57; -.
DR PRIDE; Q0WX57; -.
DR Antibodypedia; 64154; 20 antibodies from 8 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 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; HDSKDTT; -.
DR OrthoDB; 561804at2759; -.
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 143 CRISPR screens.
DR BioGRID-ORCS; 728373; 13 hits in 123 CRISPR screens.
DR BioGRID-ORCS; 728379; 12 hits in 138 CRISPR screens.
DR BioGRID-ORCS; 728393; 9 hits in 103 CRISPR screens.
DR BioGRID-ORCS; 728400; 9 hits in 445 CRISPR screens.
DR BioGRID-ORCS; 728405; 14 hits in 143 CRISPR screens.
DR BioGRID-ORCS; 728419; 7 hits in 101 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:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
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:0016579; P:protein deubiquitination; IBA:GO_Central.
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 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 Pfam; PF04774; HABP4_PAI-RBP1; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 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 pro-
FT 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
