U17L5_HUMAN
ID U17L5_HUMAN Reviewed; 530 AA.
AC A8MUK1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 17-like protein 5;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 17-like protein 5;
DE AltName: Full=Ubiquitin thioesterase 17-like protein 5;
DE AltName: Full=Ubiquitin-specific-processing protease 17-like protein 5;
GN Name=USP17L5;
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).
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; AC116655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS59467.1; -.
DR RefSeq; NP_001229258.1; NM_001242329.1.
DR AlphaFoldDB; A8MUK1; -.
DR SMR; A8MUK1; -.
DR BioGRID; 608813; 1.
DR IntAct; A8MUK1; 1.
DR STRING; 9606.ENSP00000425955; -.
DR MEROPS; C19.078; -.
DR MEROPS; C19.A86; -.
DR iPTMnet; A8MUK1; -.
DR PhosphoSitePlus; A8MUK1; -.
DR BioMuta; USP17L5; -.
DR jPOST; A8MUK1; -.
DR PaxDb; A8MUK1; -.
DR PeptideAtlas; A8MUK1; -.
DR PRIDE; A8MUK1; -.
DR Antibodypedia; 61294; 12 antibodies from 7 providers.
DR DNASU; 728386; -.
DR Ensembl; ENST00000507227.1; ENSP00000425955.1; ENSG00000227140.3.
DR GeneID; 728386; -.
DR KEGG; hsa:728386; -.
DR MANE-Select; ENST00000507227.1; ENSP00000425955.1; NM_001242329.1; NP_001229258.1.
DR UCSC; uc021xlo.1; human.
DR CTD; 728386; -.
DR GeneCards; USP17L5; -.
DR HGNC; HGNC:37177; USP17L5.
DR HPA; ENSG00000227140; Not detected.
DR neXtProt; NX_A8MUK1; -.
DR PharmGKB; PA165664776; -.
DR VEuPathDB; HostDB:ENSG00000227140; -.
DR eggNOG; KOG1865; Eukaryota.
DR GeneTree; ENSGT00940000161948; -.
DR HOGENOM; CLU_008279_10_0_1; -.
DR InParanoid; A8MUK1; -.
DR OrthoDB; 561804at2759; -.
DR PhylomeDB; A8MUK1; -.
DR TreeFam; TF315281; -.
DR PathwayCommons; A8MUK1; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; A8MUK1; -.
DR BioGRID-ORCS; 728386; 406 hits in 879 CRISPR screens.
DR GenomeRNAi; 728386; -.
DR Pharos; A8MUK1; Tdark.
DR PRO; PR:A8MUK1; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; A8MUK1; protein.
DR Bgee; ENSG00000227140; Expressed in blood.
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; 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 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 5"
FT /id="PRO_0000331647"
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; 59683 MW; 625A1B0A52EFE2FC 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
AKPEELNGEN 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
