U17L3_HUMAN
ID U17L3_HUMAN Reviewed; 530 AA.
AC A6NCW0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 17-like protein 3;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 17-like protein 3;
DE AltName: Full=Ubiquitin thioesterase 17-like protein 3;
DE AltName: Full=Ubiquitin-specific-processing protease 17-like protein 3;
GN Name=USP17L3; Synonyms=USP17B, USP17F;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [2]
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 [3]
RP NOMENCLATURE.
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).
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:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000250}.
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; AC130365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS78301.1; -.
DR RefSeq; NP_001243800.1; NM_001256871.1.
DR AlphaFoldDB; A6NCW0; -.
DR SMR; A6NCW0; -.
DR BioGRID; 570781; 1.
DR IntAct; A6NCW0; 1.
DR STRING; 9606.ENSP00000485323; -.
DR MEROPS; C19.A82; -.
DR MEROPS; C19.A85; -.
DR iPTMnet; A6NCW0; -.
DR PhosphoSitePlus; A6NCW0; -.
DR BioMuta; USP17L3; -.
DR EPD; A6NCW0; -.
DR jPOST; A6NCW0; -.
DR PeptideAtlas; A6NCW0; -.
DR PRIDE; A6NCW0; -.
DR Antibodypedia; 74875; 18 antibodies from 9 providers.
DR DNASU; 645836; -.
DR Ensembl; ENST00000530484.1; ENSP00000485323.1; ENSG00000225327.3.
DR GeneID; 645836; -.
DR KEGG; hsa:645836; -.
DR MANE-Select; ENST00000530484.1; ENSP00000485323.1; NM_001256871.1; NP_001243800.1.
DR UCSC; uc031taf.1; human.
DR CTD; 645836; -.
DR GeneCards; USP17L3; -.
DR HGNC; HGNC:37175; USP17L3.
DR HPA; ENSG00000225327; Not detected.
DR neXtProt; NX_A6NCW0; -.
DR VEuPathDB; HostDB:ENSG00000225327; -.
DR eggNOG; KOG1865; Eukaryota.
DR GeneTree; ENSGT00940000161948; -.
DR HOGENOM; CLU_008279_10_0_1; -.
DR InParanoid; A6NCW0; -.
DR OMA; HEYLLHT; -.
DR OrthoDB; 561804at2759; -.
DR PhylomeDB; A6NCW0; -.
DR PathwayCommons; A6NCW0; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 645836; 12 hits in 174 CRISPR screens.
DR GenomeRNAi; 645836; -.
DR Pharos; A6NCW0; Tdark.
DR PRO; PR:A6NCW0; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; A6NCW0; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
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 3"
FT /id="PRO_0000331645"
FT DOMAIN 80..375
FT /note="USP"
FT REGION 382..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 89
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 334
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 530 AA; 59536 MW; E7452B190523A0F3 CRC64;
MGDDSLYLGG EWQFNHFSKL TSSRPDAAFA EIQRTSLPEK SPLSSETRVD LCDDLAPVAR
QLAPREKLPL SSRRPAAVGA GLQNMGNTCY ENASLQCLTY TLPLANYMLS REHSQTCQRP
KCCMLCTMQA HITWALHSPG HVIQPSQALA SGFHRGKQED VHEFLMFTVD AMKKACLPGH
KQVDHHSKDT TLIHQIFGGC WRSQIKCLHC HGISDTFDPY LDIALDIQAA QSVKQALEQL
VKPEELNGEN AYHCGLCLQR APASNTLTLH TSAKVLILVL KRFSDVAGNK LAKNVQYPEC
LDMQPYMSQQ NTGPLVYVLY AVLVHAGWSC HDGHYFSYVK AQEGQWYKMD DAEVTVCSIT
SVLSQQAYVL FYIQKSEWER HSESVSRGRE PRALGAEDTD RRAKQGELKR DHPCLQAPEL
DEHLVERATQ ESTLDHWKFL QEQNKTKPEF NVGKVEGTLP PNALVIHQSK YKCGMKNHHP
EQQSSLLNLS STTRTDQESM NTGTLASLQG RTRRAKGKNK HSKRALLVCQ
