UBP24_HUMAN
ID UBP24_HUMAN Reviewed; 2620 AA.
AC Q9UPU5; Q6ZSY2; Q8N2Y4; Q9NXD1;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 24;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 24;
DE AltName: Full=Ubiquitin thioesterase 24;
DE AltName: Full=Ubiquitin-specific-processing protease 24;
GN Name=USP24; Synonyms=KIAA1057;
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 751-2082 AND 2256-2620, AND
RP VARIANT ALA-2468.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2233-2620, AND VARIANT ALA-2468.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1483-2620.
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-1141; SER-2047;
RP THR-2565 AND SER-2604, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2561, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047 AND THR-2565, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047 AND THR-2565, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP FUNCTION.
RX PubMed=23159851; DOI=10.4161/cc.22688;
RA Zhang L., Lubin A., Chen H., Sun Z., Gong F.;
RT "The deubiquitinating protein USP24 interacts with DDB2 and regulates DDB2
RT stability.";
RL Cell Cycle 11:4378-4384(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1141; SER-1285; SER-2047;
RP SER-2561 AND SER-2604, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-2047, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP FUNCTION, AND INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL38
RP (MICROBIAL INFECTION).
RX PubMed=29695420; DOI=10.1128/jvi.00191-18;
RA Sun Y., Bao Q., Xuan B., Xu W., Pan D., Li Q., Qian Z.;
RT "Human Cytomegalovirus Protein pUL38 Prevents Premature Cell Death by
RT Binding to Ubiquitin-specific Protease 24 and Regulating Iron Metabolism.";
RL J. Virol. 0:0-0(2018).
CC -!- FUNCTION: Ubiquitin-specific protease that regulates cell survival in
CC various contexts through modulating the protein stability of some of
CC its substrates including DDB2, MCL1 or TP53. Plays a positive role on
CC ferritinophagy where ferritin is degraded in lysosomes and releases
CC free iron. {ECO:0000269|PubMed:23159851, ECO:0000269|PubMed:29695420}.
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 -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC protein UL38. {ECO:0000269|PubMed:29695420}.
CC -!- INTERACTION:
CC Q9UPU5; P42858: HTT; NbExp=21; IntAct=EBI-1642365, EBI-466029;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29660.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA91084.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC091609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK000321; BAA91084.1; ALT_INIT; mRNA.
DR EMBL; AK127075; BAC86814.1; -; mRNA.
DR EMBL; AB028980; BAA83009.1; -; mRNA.
DR EMBL; BC029660; AAH29660.1; ALT_INIT; mRNA.
DR CCDS; CCDS44154.2; -.
DR RefSeq; NP_056121.2; NM_015306.2.
DR AlphaFoldDB; Q9UPU5; -.
DR SMR; Q9UPU5; -.
DR BioGRID; 116939; 81.
DR IntAct; Q9UPU5; 30.
DR MINT; Q9UPU5; -.
DR STRING; 9606.ENSP00000294383; -.
DR MEROPS; C19.047; -.
DR GlyGen; Q9UPU5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UPU5; -.
DR PhosphoSitePlus; Q9UPU5; -.
DR BioMuta; USP24; -.
DR DMDM; 212276491; -.
DR EPD; Q9UPU5; -.
DR jPOST; Q9UPU5; -.
DR MassIVE; Q9UPU5; -.
DR MaxQB; Q9UPU5; -.
DR PaxDb; Q9UPU5; -.
DR PeptideAtlas; Q9UPU5; -.
DR PRIDE; Q9UPU5; -.
DR ProteomicsDB; 85446; -.
DR Antibodypedia; 33232; 177 antibodies from 26 providers.
DR DNASU; 23358; -.
DR Ensembl; ENST00000294383.7; ENSP00000294383.5; ENSG00000162402.14.
DR GeneID; 23358; -.
DR KEGG; hsa:23358; -.
DR MANE-Select; ENST00000294383.7; ENSP00000294383.5; NM_015306.3; NP_056121.2.
DR UCSC; uc021onw.2; human.
DR CTD; 23358; -.
DR DisGeNET; 23358; -.
DR GeneCards; USP24; -.
DR HGNC; HGNC:12623; USP24.
DR HPA; ENSG00000162402; Low tissue specificity.
DR MIM; 610569; gene.
DR neXtProt; NX_Q9UPU5; -.
DR OpenTargets; ENSG00000162402; -.
DR PharmGKB; PA37248; -.
DR VEuPathDB; HostDB:ENSG00000162402; -.
DR eggNOG; KOG1866; Eukaryota.
DR GeneTree; ENSGT00940000159474; -.
DR HOGENOM; CLU_000331_1_0_1; -.
DR InParanoid; Q9UPU5; -.
DR OMA; GRNTDQG; -.
DR OrthoDB; 625455at2759; -.
DR PhylomeDB; Q9UPU5; -.
DR TreeFam; TF323966; -.
DR PathwayCommons; Q9UPU5; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; Q9UPU5; -.
DR SIGNOR; Q9UPU5; -.
DR BioGRID-ORCS; 23358; 21 hits in 1119 CRISPR screens.
DR ChiTaRS; USP24; human.
DR GeneWiki; USP24; -.
DR GenomeRNAi; 23358; -.
DR Pharos; Q9UPU5; Tbio.
DR PRO; PR:Q9UPU5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UPU5; protein.
DR Bgee; ENSG00000162402; Expressed in sural nerve and 201 other tissues.
DR ExpressionAtlas; Q9UPU5; baseline and differential.
DR Genevisible; Q9UPU5; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021905; DUF3517.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR033382; USP24.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006:SF729; PTHR24006:SF729; 1.
DR Pfam; PF12030; DUF3517; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50030; UBA; 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 Host-virus interaction; Hydrolase; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..2620
FT /note="Ubiquitin carboxyl-terminal hydrolase 24"
FT /id="PRO_0000080652"
FT DOMAIN 3..44
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 1689..2042
FT /note="USP"
FT REGION 45..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1921..1945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2063..2090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2575..2620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2575..2600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1698
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 1970
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 942
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:B1AY13"
FT MOD_RES 1141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1943
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AY13"
FT MOD_RES 2047
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 2077
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AY13"
FT MOD_RES 2561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2565
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 2604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 226
FT /note="T -> I (in dbSNP:rs1165222)"
FT /id="VAR_047154"
FT VARIANT 1940
FT /note="G -> S (in dbSNP:rs2274540)"
FT /id="VAR_047155"
FT VARIANT 2134
FT /note="Y -> S (in dbSNP:rs12753590)"
FT /id="VAR_047156"
FT VARIANT 2468
FT /note="V -> A (in dbSNP:rs487230)"
FT /evidence="ECO:0000269|PubMed:10470851,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_047157"
FT CONFLICT 840
FT /note="N -> S (in Ref. 2; BAC86814)"
FT /evidence="ECO:0000305"
FT CONFLICT 990
FT /note="I -> L (in Ref. 2; BAC86814)"
FT /evidence="ECO:0000305"
FT CONFLICT 1253
FT /note="P -> S (in Ref. 2; BAC86814)"
FT /evidence="ECO:0000305"
FT CONFLICT 1776
FT /note="E -> G (in Ref. 2; BAC86814)"
FT /evidence="ECO:0000305"
FT CONFLICT 2576
FT /note="K -> R (in Ref. 2; BAA91084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2620 AA; 294365 MW; 2773B7857A8B6633 CRC64;
MESEEEQHMT TLLCMGFSDP ATIRKALRLA KNDINEAVAL LTNERPGLDY GGYEPMDSGG
GPSPGPGGGP RGDGGGDGGG GGPSRGGSTG GGGGFDPPPA YHEVVDAEKN DENGNCSGEG
IEFPTTNLYE LESRVLTDHW SIPYKREESL GKCLLASTYL ARLGLSESDE NCRRFMDRCM
PEAFKKLLTS SAVHKWGTEI HEGIYNMLML LIELVAERIK QDPIPTGLLG VLTMAFNPDN
EYHFKNRMKV SQRNWAEVFG EGNMFAVSPV STFQKEPHGW VVDLVNKFGE LGGFAAIQAK
LHSEDIELGA VSALIQPLGV CAEYLNSSVV QPMLDPVILT TIQDVRSVEE KDLKDKRLVS
IPELLSAVKL LCMRFQPDLV TIVDDLRLDI LLRMLKSPHF SAKMNSLKEV TKLIEDSTLS
KSVKNAIDTD RLLDWLVENS VLSIALEGNI DQAQYCDRIK GIIELLGSKL SLDELTKIWK
IQSGQSSTVI ENIHTIIAAA AVKFNSDQLN HLFVLIQKSW ETESDRVRQK LLSLIGRIGR
EARFETTSGK VLDVLWELAH LPTLPSSLIQ QALEEHLTIL SDAYAVKEAI KRSYIIKCIE
DIKRPGEWSG LEKNKKDGFK SSQLNNPQFV WVVPALRQLH EITRSFIKQT YQKQDKSIIQ
DLKKNFEIVK LVTGSLIACH RLAAAVAGPG GLSGSTLVDG RYTYREYLEA HLKFLAFFLQ
EATLYLGWNR AKEIWECLVT GQDVCELDRE MCFEWFTKGQ HDLESDVQQQ LFKEKILKLE
SYEITMNGFN LFKTFFENVN LCDHRLKRQG AQLYVEKLEL IGMDFIWKIA MESPDEEIAN
EAIQLIINYS YINLNPRLKK DSVSLHKKFI ADCYTRLEAA SSALGGPTLT HAVTRATKML
TATAMPTVAT SVQSPYRSTK LVIIERLLLL AERYVITIED FYSVPRTILP HGASFHGHLL
TLNVTYESTK DTFTVEAHSN ETIGSVRWKI AKQLCSPVDN IQIFTNDSLL TVNKDQKLLH
QLGFSDEQIL TVKTSGSGTP SGSSADSSTS SSSSSSGVFS SSYAMEQEKS LPGVVMALVC
NVFDMLYQLA NLEEPRITLR VRKLLLLIPT DPAIQEALDQ LDSLGRKKTL LSESSSQSSK
SPSLSSKQQH QPSASSILES LFRSFAPGMS TFRVLYNLEV LSSKLMPTAD DDMARSCAKS
FCENFLKAGG LSLVVNVMQR DSIPSEVDYE TRQGVYSICL QLARFLLVGQ TMPTLLDEDL
TKDGIEALSS RPFRNVSRQT SRQMSLCGTP EKSSYRQLSV SDRSSIRVEE IIPAARVAIQ
TMEVSDFTST VACFMRLSWA AAAGRLDLVG SSQPIKESNS LCPAGIRNRL SSSGSNCSSG
SEGEPVALHA GICVRQQSVS TKDSLIAGEA LSLLVTCLQL RSQQLASFYN LPCVADFIID
ILLGSPSAEI RRVACDQLYT LSQTDTSAHP DVQKPNQFLL GVILTAQLPL WSPTSIMRGV
NQRLLSQCME YFDLRCQLLD DLTTSEMEQL RISPATMLED EITWLDNFEP NRTAECETSE
ADNILLAGHL RLIKTLLSLC GAEKEMLGSS LIKPLLDDFL FRASRIILNS HSPAGSAAIS
QQDFHPKCST ANSRLAAYEV LVMLADSSPS NLQIIIKELL SMHHQPDPAL TKEFDYLPPV
DSRSSSGFVG LRNGGATCYM NAVFQQLYMQ PGLPESLLSV DDDTDNPDDS VFYQVQSLFG
HLMESKLQYY VPENFWKIFK MWNKELYVRE QQDAYEFFTS LIDQMDEYLK KMGRDQIFKN
TFQGIYSDQK ICKDCPHRYE REEAFMALNL GVTSCQSLEI SLDQFVRGEV LEGSNAYYCE
KCKEKRITVK RTCIKSLPSV LVIHLMRFGF DWESGRSIKY DEQIRFPWML NMEPYTVSGM
ARQDSSSEVG ENGRSVDQGG GGSPRKKVAL TENYELVGVI VHSGQAHAGH YYSFIKDRRG
CGKGKWYKFN DTVIEEFDLN DETLEYECFG GEYRPKVYDQ TNPYTDVRRR YWNAYMLFYQ
RVSDQNSPVL PKKSRVSVVR QEAEDLSLSA PSSPEISPQS SPRPHRPNND RLSILTKLVK
KGEKKGLFVE KMPARIYQMV RDENLKFMKN RDVYSSDYFS FVLSLASLNA TKLKHPYYPC
MAKVSLQLAI QFLFQTYLRT KKKLRVDTEE WIATIEALLS KSFDACQWLV EYFISSEGRE
LIKIFLLECN VREVRVAVAT ILEKTLDSAL FYQDKLKSLH QLLEVLLALL DKDVPENCKN
CAQYFFLFNT FVQKQGIRAG DLLLRHSALR HMISFLLGAS RQNNQIRRWS SAQAREFGNL
HNTVALLVLH SDVSSQRNVA PGIFKQRPPI SIAPSSPLLP LHEEVEALLF MSEGKPYLLE
VMFALRELTG SLLALIEMVV YCCFCNEHFS FTMLHFIKNQ LETAPPHELK NTFQLLHEIL
VIEDPIQVER VKFVFETENG LLALMHHSNH VDSSRCYQCV KFLVTLAQKC PAAKEYFKEN
SHHWSWAVQW LQKKMSEHYW TPQSNVSNET STGKTFQRTI SAQDTLAYAT ALLNEKEQSG
SSNGSESSPA NENGDRHLQQ GSESPMMIGE LRSDLDDVDP
