UL17C_HUMAN
ID UL17C_HUMAN Reviewed; 530 AA.
AC C9JPN9;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 17-like protein 12;
DE EC=3.4.19.12;
GN Name=USP17L12;
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}.
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; AC108519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS59456.1; -.
DR RefSeq; NP_001243782.1; NM_001256853.1.
DR AlphaFoldDB; C9JPN9; -.
DR SMR; C9JPN9; -.
DR BioGRID; 938867; 3.
DR IntAct; C9JPN9; 1.
DR STRING; 9606.ENSP00000389443; -.
DR MEROPS; C19.A82; -.
DR MEROPS; C19.A89; -.
DR iPTMnet; C9JPN9; -.
DR PhosphoSitePlus; C9JPN9; -.
DR BioMuta; USP17L12; -.
DR jPOST; C9JPN9; -.
DR PaxDb; C9JPN9; -.
DR PeptideAtlas; C9JPN9; -.
DR PRIDE; C9JPN9; -.
DR Antibodypedia; 71846; 1 antibodies from 1 providers.
DR DNASU; 100287205; -.
DR Ensembl; ENST00000415041.1; ENSP00000389443.1; ENSG00000227551.1.
DR GeneID; 100287205; -.
DR KEGG; hsa:100287205; -.
DR MANE-Select; ENST00000415041.1; ENSP00000389443.1; NM_001256853.1; NP_001243782.1.
DR UCSC; uc031sdi.1; human.
DR CTD; 100287205; -.
DR GeneCards; USP17L12; -.
DR HGNC; HGNC:44440; USP17L12.
DR HPA; ENSG00000227551; Not detected.
DR neXtProt; NX_C9JPN9; -.
DR VEuPathDB; HostDB:ENSG00000227551; -.
DR eggNOG; KOG1865; Eukaryota.
DR GeneTree; ENSGT00940000161948; -.
DR HOGENOM; CLU_008279_10_0_1; -.
DR InParanoid; C9JPN9; -.
DR OrthoDB; 561804at2759; -.
DR PhylomeDB; C9JPN9; -.
DR TreeFam; TF315281; -.
DR PathwayCommons; C9JPN9; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 100287205; 46 hits in 531 CRISPR screens.
DR GenomeRNAi; 100287205; -.
DR Pharos; C9JPN9; Tdark.
DR PRO; PR:C9JPN9; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; C9JPN9; 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; 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 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 12"
FT /id="PRO_0000421088"
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; 59687 MW; DF0C87A781245DC7 CRC64;
MEEDSLYLGG EWQFNHFSKL TSSRPDAAFA EIQRTSLPEK SPLSCETRVD LCDDLAPVAR
QLAPREKLPL SNRRPAAVGA GLQNMGNTCY VNASLQCLTY TPPLANYMLS REHSQTCHRH
KGCMLCTMQA HITRALHNPG HVIQPSQALA AGFHRGKQED AHEFLMFTVD AMKKACLPGH
KQVDHHSKDT TLIHQIFGGY WRSQIKCLHC HGISDTFDPY LDIALDIQAA QSVQQALEQL
VKPEELNGEN AYHCGVCLQR APASKMLTLL TSAKVLILVL KRFSDVTGNK IAKNVQYPEC
LDMQPYMSQP NTGPLVYVLY AVLVHAGWSC HNGHYFSYVK AQEGQWYKMD DAEVTASSIT
SVLSQQAYVL FYIQKSEWER HSESVSRGRE PRALGAEDTD RRATQGELKR DHPCLQAPEL
DEHLVERATQ ESTLDHWKFL QEQNKTKPEF NVRKVEGTLP PDVLVIHQSK YKCGMKNHHP
EQQSSLLKLS STTPTHQESM NTGTLASLRG RARRSKGKNK HSKRALLVCQ
