ID   U17LD_HUMAN             Reviewed;         530 AA.
AC   C9JLJ4;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 17-like protein 13;
DE            EC=3.4.19.12;
GN   Name=USP17L13;
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=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).
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 on chromosome 4 and
CC       chromosome 8. The high similarity between the UPS17-like genes makes it
CC       impossible to specifically assign data to a particular gene of the
CC       family. Oligonucleotides designed in RNAi experiments are for instance
CC       not specific for a given UPS17-like gene. {ECO:0000305}.
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DR   EMBL; AC108519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS59457.1; -.
DR   RefSeq; NP_001243784.1; NM_001256855.1.
DR   AlphaFoldDB; C9JLJ4; -.
DR   SMR; C9JLJ4; -.
DR   IntAct; C9JLJ4; 1.
DR   STRING; 9606.ENSP00000414392; -.
DR   MEROPS; C19.A82; -.
DR   MEROPS; C19.A90; -.
DR   BioMuta; USP17L13; -.
DR   jPOST; C9JLJ4; -.
DR   PaxDb; C9JLJ4; -.
DR   PeptideAtlas; C9JLJ4; -.
DR   PRIDE; C9JLJ4; -.
DR   DNASU; 100287238; -.
DR   Ensembl; ENST00000429667.1; ENSP00000414392.1; ENSG00000232399.4.
DR   GeneID; 100287238; -.
DR   KEGG; hsa:100287238; -.
DR   MANE-Select; ENST00000429667.1; ENSP00000414392.1; NM_001256855.1; NP_001243784.1.
DR   UCSC; uc031sdj.1; human.
DR   CTD; 100287238; -.
DR   GeneCards; USP17L13; -.
DR   HGNC; HGNC:44441; USP17L13.
DR   HPA; ENSG00000232399; Not detected.
DR   neXtProt; NX_C9JLJ4; -.
DR   VEuPathDB; HostDB:ENSG00000232399; -.
DR   eggNOG; KOG1865; Eukaryota.
DR   GeneTree; ENSGT00940000161948; -.
DR   InParanoid; C9JLJ4; -.
DR   OMA; DRWKFLQ; -.
DR   OrthoDB; 561804at2759; -.
DR   PhylomeDB; C9JLJ4; -.
DR   PathwayCommons; C9JLJ4; -.
DR   Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR   BioGRID-ORCS; 100287238; 22 hits in 976 CRISPR screens.
DR   GenomeRNAi; 100287238; -.
DR   Pharos; C9JLJ4; Tdark.
DR   PRO; PR:C9JLJ4; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; C9JLJ4; 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: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; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Hydrolase; Nucleus; Protease; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..530
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 17-like
FT                   protein 13"
FT                   /id="PRO_0000421089"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        334
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
SQ   SEQUENCE   530 AA;  59694 MW;  AEBDA146AE398F75 CRC64;
     MEEDSLYLGG EWQFNHFSKL TSSRLDAAFA EIQRTSLPEK SPLSCETRVD LCDDLVPEAR
     QLAPREKLPL SSRRPAAVGA GLQNMGNTCY VNASLQCLTY TPPLANYMLS REHSQTCHRH
     KGCMLCTMQA HITRALHNPG HVIQPSQALA AGFHRGKQED AHEFLMFTVD AMKKACLPGH
     KQVDHPSKDT TLIHQIFGGY WRSQIKCLHC HGISDTFDPY LDIALDIQAA QSVQQALEQL
     VKPEELNGEN AYHCGVCLQR APASKTLTLH TSAKVLILVL KRFSDVTGNK IAKNVQYPEC
     LDMQPYMSQQ NTGPLVYVLY AVLVHAGWSC HNGHYFSYVK AQEGQWYKMD DAEVTAASIT
     SVLSQQAYVL FYIQKSEWER HSESVSRGRE PRALGAEDTD RRATQGELKR DHPCLQAPEL
     DEHLVERATQ ESTLDRWKFL QEQNKTKPEF NVRKVEGTLP PDVLVIHQSK YKCGMKNHHP
     EQQSSLLNLS SSTPTHQESM NTGTLASLRG RARRSKGKNK HSKRALLVCQ