UBP48_HUMAN
ID UBP48_HUMAN Reviewed; 1035 AA.
AC Q86UV5; B7ZKS7; Q2M3I4; Q5SZI4; Q5T3T5; Q6NX53; Q8N3F6; Q96F64; Q96IQ3;
AC Q9H5N3; Q9H5T7; Q9NUJ6; Q9NXR0;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 48;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 48;
DE AltName: Full=Ubiquitin thioesterase 48;
DE AltName: Full=Ubiquitin-specific peptidase 48;
DE AltName: Full=Ubiquitin-specific protease 48;
DE AltName: Full=Ubiquitin-specific-processing protease 48;
GN Name=USP48; Synonyms=USP31;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=15354349; DOI=10.1080/10855660310001638197;
RA Lockhart P.J., Hulihan M., Lincoln S., Hussey J., Skipper L., Bisceglio G.,
RA Wilkes K., Farrer M.J.;
RT "Identification of the human ubiquitin specific protease 31 (USP31) gene:
RT structure, sequence and expression analysis.";
RL DNA Seq. 15:9-14(2004).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 712-1035 (ISOFORM 1).
RC TISSUE=Colon, Hepatoma, and Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 8), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 399-1035 (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-636 (ISOFORMS 1/2).
RC TISSUE=Colon, Eye, Pancreas, Skin, and Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 691-1035 (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=14715245; DOI=10.1016/j.bbrc.2003.12.050;
RA Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S.,
RA Lopez-Otin C.;
RT "Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
RT proteases.";
RL Biochem. Biophys. Res. Commun. 314:54-62(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP ALTERNATIVE SPLICING (ISOFORM 7), ENZYME ACTIVITY, FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH RELA AND TRAF2.
RX PubMed=16214042; DOI=10.1016/j.cellsig.2005.03.017;
RA Tzimas C., Michailidou G., Arsenakis M., Kieff E., Mosialos G.,
RA Hatzivassiliou E.G.;
RT "Human ubiquitin specific protease 31 is a deubiquitinating enzyme
RT implicated in activation of nuclear factor-kappaB.";
RL Cell. Signal. 18:83-92(2006).
RN [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-956, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886; SER-887 AND SER-888, 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886 AND SER-888, 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal
CC Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC precursors as well as that of ubiquitinated proteins. May be involved
CC in the regulation of NF-kappa-B activation by TNF receptor superfamily
CC via its interactions with RELA and TRAF2. May also play a regulatory
CC role at postsynaptic sites. {ECO:0000269|PubMed:16214042}.
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; Evidence={ECO:0000269|PubMed:16214042};
CC -!- SUBUNIT: Interacts with TRAF2 and RELA. {ECO:0000269|PubMed:16214042}.
CC -!- INTERACTION:
CC Q86UV5; Q13148: TARDBP; NbExp=3; IntAct=EBI-2512161, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16214042}. Nucleus
CC {ECO:0000269|PubMed:16214042}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q86UV5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86UV5-2; Sequence=VSP_020480;
CC Name=3;
CC IsoId=Q86UV5-3; Sequence=VSP_020479;
CC Name=4;
CC IsoId=Q86UV5-4; Sequence=VSP_020473, VSP_020474;
CC Name=5;
CC IsoId=Q86UV5-5; Sequence=VSP_020472, VSP_020475, VSP_020478,
CC VSP_020480;
CC Name=6;
CC IsoId=Q86UV5-6; Sequence=VSP_020471, VSP_020481;
CC Name=7; Synonyms=USP31S1;
CC IsoId=Q86UV5-7; Sequence=VSP_020476, VSP_020477;
CC Name=8;
CC IsoId=Q86UV5-8; Sequence=VSP_054487, VSP_054488;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14715245,
CC ECO:0000269|PubMed:15354349, ECO:0000269|PubMed:16214042}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- CAUTION: Was termed (PubMed:15354349 and PubMed:17081983) USP31.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH13567.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH67261.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI03725.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA92128.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 5]:
CC Sequence=BAB15533.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF502942; AAP30832.1; -; mRNA.
DR EMBL; AL359815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK000110; BAA90950.1; -; mRNA.
DR EMBL; AK002190; BAA92128.1; ALT_INIT; mRNA.
DR EMBL; AK026707; BAB15533.1; ALT_FRAME; mRNA.
DR EMBL; AK026930; BAB15591.1; -; mRNA.
DR EMBL; BC007326; AAH07326.2; -; mRNA.
DR EMBL; BC013567; AAH13567.1; ALT_INIT; mRNA.
DR EMBL; BC067261; AAH67261.1; ALT_SEQ; mRNA.
DR EMBL; BC103724; AAI03725.1; ALT_SEQ; mRNA.
DR EMBL; BC104896; AAI04897.1; -; mRNA.
DR EMBL; BC143354; AAI43355.1; -; mRNA.
DR EMBL; AL834375; CAD39038.1; -; mRNA.
DR CCDS; CCDS30623.1; -. [Q86UV5-1]
DR CCDS; CCDS44084.1; -. [Q86UV5-7]
DR CCDS; CCDS81277.1; -. [Q86UV5-2]
DR RefSeq; NP_001027902.1; NM_001032730.1. [Q86UV5-7]
DR RefSeq; NP_001317323.1; NM_001330394.1. [Q86UV5-2]
DR RefSeq; NP_115612.4; NM_032236.6. [Q86UV5-1]
DR AlphaFoldDB; Q86UV5; -.
DR SMR; Q86UV5; -.
DR BioGRID; 123941; 65.
DR IntAct; Q86UV5; 20.
DR MINT; Q86UV5; -.
DR STRING; 9606.ENSP00000309262; -.
DR MEROPS; C19.068; -.
DR GlyGen; Q86UV5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86UV5; -.
DR PhosphoSitePlus; Q86UV5; -.
DR BioMuta; USP48; -.
DR DMDM; 74750436; -.
DR EPD; Q86UV5; -.
DR jPOST; Q86UV5; -.
DR MassIVE; Q86UV5; -.
DR MaxQB; Q86UV5; -.
DR PaxDb; Q86UV5; -.
DR PeptideAtlas; Q86UV5; -.
DR PRIDE; Q86UV5; -.
DR ProteomicsDB; 69905; -. [Q86UV5-1]
DR ProteomicsDB; 69906; -. [Q86UV5-2]
DR ProteomicsDB; 69907; -. [Q86UV5-3]
DR ProteomicsDB; 69908; -. [Q86UV5-4]
DR ProteomicsDB; 69909; -. [Q86UV5-5]
DR ProteomicsDB; 69910; -. [Q86UV5-6]
DR ProteomicsDB; 69911; -. [Q86UV5-7]
DR ProteomicsDB; 7191; -.
DR Antibodypedia; 29995; 201 antibodies from 28 providers.
DR DNASU; 84196; -.
DR Ensembl; ENST00000308271.14; ENSP00000309262.9; ENSG00000090686.16. [Q86UV5-1]
DR Ensembl; ENST00000400301.5; ENSP00000383157.1; ENSG00000090686.16. [Q86UV5-2]
DR Ensembl; ENST00000421625.6; ENSP00000406256.2; ENSG00000090686.16. [Q86UV5-7]
DR Ensembl; ENST00000529637.5; ENSP00000431949.1; ENSG00000090686.16. [Q86UV5-8]
DR GeneID; 84196; -.
DR KEGG; hsa:84196; -.
DR MANE-Select; ENST00000308271.14; ENSP00000309262.9; NM_032236.8; NP_115612.4.
DR UCSC; uc001bfb.4; human. [Q86UV5-1]
DR CTD; 84196; -.
DR DisGeNET; 84196; -.
DR GeneCards; USP48; -.
DR HGNC; HGNC:18533; USP48.
DR HPA; ENSG00000090686; Low tissue specificity.
DR MIM; 617445; gene.
DR neXtProt; NX_Q86UV5; -.
DR OpenTargets; ENSG00000090686; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR PharmGKB; PA134947522; -.
DR VEuPathDB; HostDB:ENSG00000090686; -.
DR eggNOG; KOG1863; Eukaryota.
DR GeneTree; ENSGT00940000156015; -.
DR HOGENOM; CLU_010287_0_0_1; -.
DR InParanoid; Q86UV5; -.
DR OMA; LGQEKWE; -.
DR OrthoDB; 113272at2759; -.
DR PhylomeDB; Q86UV5; -.
DR TreeFam; TF106280; -.
DR PathwayCommons; Q86UV5; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; Q86UV5; -.
DR BioGRID-ORCS; 84196; 34 hits in 1088 CRISPR screens.
DR ChiTaRS; USP48; human.
DR GeneWiki; USP48; -.
DR GenomeRNAi; 84196; -.
DR Pharos; Q86UV5; Tbio.
DR PRO; PR:Q86UV5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q86UV5; protein.
DR Bgee; ENSG00000090686; Expressed in calcaneal tendon and 195 other tissues.
DR ExpressionAtlas; Q86UV5; baseline and differential.
DR Genevisible; Q86UV5; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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 CDD; cd02668; Peptidase_C19L; 1.
DR CDD; cd01795; Ubl_USP48; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR044743; Ubl_USP48.
DR InterPro; IPR033841; USP48.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF143791; SSF143791; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS51283; DUSP; 3.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Hydrolase; Nucleus;
KW Phosphoprotein; Protease; Reference proteome; Repeat; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1035
FT /note="Ubiquitin carboxyl-terminal hydrolase 48"
FT /id="PRO_0000249523"
FT DOMAIN 89..421
FT /note="USP"
FT DOMAIN 460..554
FT /note="DUSP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 569..691
FT /note="DUSP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 711..824
FT /note="DUSP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 929..1009
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 612..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 353
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 956
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..875
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020471"
FT VAR_SEQ 1..469
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020472"
FT VAR_SEQ 369..392
FT /note="FNDEDIEKMEGKKLQLGIEEDLAE -> LILNTNYHLPPSPKPIKIKNYNKP
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020473"
FT VAR_SEQ 391
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054487"
FT VAR_SEQ 393..1035
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020474"
FT VAR_SEQ 470..483
FT /note="EEVKELYQRLPAGA -> MNLSLSQKTVKIHRLFPMLAFS (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020475"
FT VAR_SEQ 484..485
FT /note="EP -> GL (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_020476"
FT VAR_SEQ 486..1035
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_020477"
FT VAR_SEQ 589
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020478"
FT VAR_SEQ 654
FT /note="H -> HAVFFFSKYIFLNS (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054488"
FT VAR_SEQ 704..1035
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020479"
FT VAR_SEQ 909..960
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_020480"
FT VAR_SEQ 1020..1035
FT /note="VCMPEEGFKGTGLLGH -> GKDEFVLGIC (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020481"
FT VARIANT 125
FT /note="S -> C (in dbSNP:rs4253886)"
FT /id="VAR_027427"
FT VARIANT 135
FT /note="E -> K (in dbSNP:rs12097805)"
FT /id="VAR_027428"
SQ SEQUENCE 1035 AA; 119032 MW; 6F7DAF88527E2627 CRC64;
MAPRLQLEKA AWRWAETVRP EEVSQEHIET AYRIWLEPCI RGVCRRNCKG NPNCLVGIGE
HIWLGEIDEN SFHNIDDPNC ERRKKNSFVG LTNLGATCYV NTFLQVWFLN LELRQALYLC
PSTCSDYMLG DGIQEEKDYE PQTICEHLQY LFALLQNSNR RYIDPSGFVK ALGLDTGQQQ
DAQEFSKLFM SLLEDTLSKQ KNPDVRNIVQ QQFCGEYAYV TVCNQCGRES KLLSKFYELE
LNIQGHKQLT DCISEFLKEE KLEGDNRYFC ENCQSKQNAT RKIRLLSLPC TLNLQLMRFV
FDRQTGHKKK LNTYIGFSEI LDMEPYVEHK GGSYVYELSA VLIHRGVSAY SGHYIAHVKD
PQSGEWYKFN DEDIEKMEGK KLQLGIEEDL AEPSKSQTRK PKCGKGTHCS RNAYMLVYRL
QTQEKPNTTV QVPAFLQELV DRDNSKFEEW CIEMAEMRKQ SVDKGKAKHE EVKELYQRLP
AGAEPYEFVS LEWLQKWLDE STPTKPIDNH ACLCSHDKLH PDKISIMKRI SEYAADIFYS
RYGGGPRLTV KALCKECVVE RCRILRLKNQ LNEDYKTVNN LLKAAVKGSD GFWVGKSSLR
SWRQLALEQL DEQDGDAEQS NGKMNGSTLN KDESKEERKE EEELNFNEDI LCPHGELCIS
ENERRLVSKE AWSKLQQYFP KAPEFPSYKE CCSQCKILER EGEENEALHK MIANEQKTSL
PNLFQDKNRP CLSNWPEDTD VLYIVSQFFV EEWRKFVRKP TRCSPVSSVG NSALLCPHGG
LMFTFASMTK EDSKLIALIW PSEWQMIQKL FVVDHVIKIT RIEVGDVNPS ETQYISEPKL
CPECREGLLC QQQRDLREYT QATIYVHKVV DNKKVMKDSA PELNVSSSET EEDKEEAKPD
GEKDPDFNQS NGGTKRQKIS HQNYIAYQKQ VIRRSMRHRK VRGEKALLVS ANQTLKELKI
QIMHAFSVAP FDQNLSIDGK ILSDDCATLG TLGVIPESVI LLKADEPIAD YAAMDDVMQV
CMPEEGFKGT GLLGH
