ID   UBP48_MOUSE             Reviewed;        1052 AA.
AC   Q3V0C5; Q3TM39; Q571J9; Q8VDJ1;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   24-JAN-2024, entry version 146.
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-processing protease 48;
GN   Name=Usp48; Synonyms=Kiaa4202;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Embryonic tail;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-633 (ISOFORM 5).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Liver, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 (By similarity). {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   -!- SUBUNIT: Interacts with TRAF2 and RELA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q3V0C5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3V0C5-2; Sequence=VSP_020482;
CC       Name=3;
CC         IsoId=Q3V0C5-3; Sequence=VSP_020483, VSP_020484, VSP_020485;
CC       Name=4;
CC         IsoId=Q3V0C5-4; Sequence=VSP_020484, VSP_020485;
CC       Name=5;
CC         IsoId=Q3V0C5-5; Sequence=VSP_020483;
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21769.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAD90375.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK220190; BAD90375.1; ALT_INIT; mRNA.
DR   EMBL; AK133251; BAE21579.1; -; mRNA.
DR   EMBL; AK166158; BAE38603.1; -; mRNA.
DR   EMBL; BC021769; AAH21769.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS38924.1; -. [Q3V0C5-1]
DR   RefSeq; NP_570949.2; NM_130879.2. [Q3V0C5-1]
DR   RefSeq; XP_017175495.1; XM_017320006.1.
DR   AlphaFoldDB; Q3V0C5; -.
DR   SMR; Q3V0C5; -.
DR   BioGRID; 228386; 540.
DR   STRING; 10090.ENSMUSP00000055016; -.
DR   MEROPS; C19.068; -.
DR   iPTMnet; Q3V0C5; -.
DR   PhosphoSitePlus; Q3V0C5; -.
DR   SwissPalm; Q3V0C5; -.
DR   EPD; Q3V0C5; -.
DR   jPOST; Q3V0C5; -.
DR   MaxQB; Q3V0C5; -.
DR   PaxDb; 10090-ENSMUSP00000055016; -.
DR   PeptideAtlas; Q3V0C5; -.
DR   ProteomicsDB; 298107; -. [Q3V0C5-1]
DR   ProteomicsDB; 298108; -. [Q3V0C5-2]
DR   ProteomicsDB; 298109; -. [Q3V0C5-3]
DR   ProteomicsDB; 298110; -. [Q3V0C5-4]
DR   ProteomicsDB; 298111; -. [Q3V0C5-5]
DR   Pumba; Q3V0C5; -.
DR   Antibodypedia; 29995; 220 antibodies from 28 providers.
DR   DNASU; 170707; -.
DR   Ensembl; ENSMUST00000055131.13; ENSMUSP00000055016.7; ENSMUSG00000043411.16. [Q3V0C5-1]
DR   GeneID; 170707; -.
DR   KEGG; mmu:170707; -.
DR   UCSC; uc008vjh.1; mouse. [Q3V0C5-2]
DR   UCSC; uc008vji.1; mouse. [Q3V0C5-3]
DR   UCSC; uc008vjj.1; mouse. [Q3V0C5-4]
DR   UCSC; uc008vjl.1; mouse. [Q3V0C5-1]
DR   AGR; MGI:2158502; -.
DR   CTD; 84196; -.
DR   MGI; MGI:2158502; Usp48.
DR   VEuPathDB; HostDB:ENSMUSG00000043411; -.
DR   eggNOG; KOG1863; Eukaryota.
DR   GeneTree; ENSGT00940000156015; -.
DR   InParanoid; Q3V0C5; -.
DR   OrthoDB; 307371at2759; -.
DR   PhylomeDB; Q3V0C5; -.
DR   TreeFam; TF106280; -.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   BioGRID-ORCS; 170707; 0 hits in 61 CRISPR screens.
DR   ChiTaRS; Usp48; mouse.
DR   PRO; PR:Q3V0C5; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q3V0C5; Protein.
DR   Bgee; ENSMUSG00000043411; Expressed in retinal neural layer and 268 other cell types or tissues.
DR   ExpressionAtlas; Q3V0C5; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0101005; F:deubiquitinase activity; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02668; Peptidase_C19L; 1.
DR   CDD; cd01795; Ubl_USP48; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 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   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF722; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 48; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS51283; DUSP; 3.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   Genevisible; Q3V0C5; MM.
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..1052
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 48"
FT                   /id="PRO_0000249524"
FT   DOMAIN          89..420
FT                   /note="USP"
FT   DOMAIN          459..553
FT                   /note="DUSP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT   DOMAIN          568..691
FT                   /note="DUSP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT   DOMAIN          710..841
FT                   /note="DUSP 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT   DOMAIN          946..1026
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   REGION          609..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          896..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..922
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        923..940
FT                   /note="Polar 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         903
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UV5"
FT   MOD_RES         904
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UV5"
FT   MOD_RES         905
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UV5"
FT   MOD_RES         973
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UV5"
FT   VAR_SEQ         1
FT                   /note="M -> MVGPCPFGRRRRRRRRPPGSASATSVKAM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020482"
FT   VAR_SEQ         390
FT                   /note="L -> LA (in isoform 3 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020483"
FT   VAR_SEQ         483..484
FT                   /note="EP -> GL (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT                   /id="VSP_020484"
FT   VAR_SEQ         485..1052
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT                   /id="VSP_020485"
SQ   SEQUENCE   1052 AA;  120631 MW;  347520CB80F34303 CRC64;
     MAPRLQLEKA AWRWAETVRP EEVSQEHIET AYRIWLEPCI RGVCRRNCRG NPNCLVGIGE
     HIWLGEIDEN SFHSIDDPNC ERRKKNSFVG LTNLGATCYV NTFLQVWFLN LELRQALYLC
     PSTCSDYTKG DGIHGGKDYE PQTICEHLQY LFALLQNSNR RYIDPSGFVK ALGLDTGQQQ
     DAQEFSKLFM SLLEDTLSKQ KNPDVRNVVQ QQFCGEYAYV TVCNQCGRES KLVSKFYELE
     LNIQGHKQLT DCISEFLKEE RLEGDNRYFC ENCQSKQNAT RKIRLLSLPC TLNLQLMRFV
     FDRQTGHKKK LNAYIGFSES LDMEPYVEHK GGSFVYELSA VLIHRGVSAY SGHYIAHVKD
     PQSGEWYKFN DEDIEKMEGK KLQLGIEEDL EPSKSQTRKP KCGKGTHCSR NAYMLVYRLQ
     AQEKNHTMVQ VPAFLQELVD RDNSKFEEWC VEMAEMRKQS VDKGKAKHEE VKELYQRLPA
     GAEPYEFVSL EWLQKWLDES TPTKPIDNNA CLCSHDKLHP DKISIMKRIS EYAANIFYSR
     YGGGPRLTVK ALCKDCVVER CRVLRLKNQL NEDYKAVNNL LKSTMKGDGF WVGKSSLRSW
     RQLALEQLDE QDGEAEQSNG KINGSTFNKD ESKEEKKEEE EELNFNEDIL CPHGELSISE
     NERRLVSQEA WSKLQQYFPK APEFPSYREC CSQCKILERE GEENEALHKM IANEQKTSLP
     NLFQDKNRPC LSNWPEDTDA LYIVSHFFLD EWRKFVRKPA RSAPVSSIGN AALLCPHGGL
     MFTFPSLTKE DSKLCQPLER REGGWPTAAH NNIALIWPSE WQMIQKLFVV DKVIKITRIE
     VGDVNPSQTQ YISEPSLCPD CREGLLCQQQ RDLREYTQAT IYVHKVVDNK KVMKDSAPEL
     NVSSSETEED KEEAKPDGEK DPDFNQSNGS TKRQKTSQQG YVAYQKQVIR RSTRHRKVRG
     EKALLVSANQ TLKELKIQIM HAFSVAPFDQ NLSIDGKILN DDCATLGTLG VIPESVILLK
     ADEPIADYAA MDDVMQVCMP EEGFKGTGLL GH
//