UBP48_MOUSE
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 03-AUG-2022, entry version 139.
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. [Q3V0C5-5]
DR AlphaFoldDB; Q3V0C5; -.
DR SMR; Q3V0C5; -.
DR BioGRID; 228386; 4.
DR STRING; 10090.ENSMUSP00000055016; -.
DR MEROPS; C19.068; -.
DR iPTMnet; Q3V0C5; -.
DR PhosphoSitePlus; Q3V0C5; -.
DR EPD; Q3V0C5; -.
DR jPOST; Q3V0C5; -.
DR MaxQB; Q3V0C5; -.
DR PaxDb; Q3V0C5; -.
DR PeptideAtlas; Q3V0C5; -.
DR PRIDE; 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 Antibodypedia; 29995; 201 antibodies from 28 providers.
DR DNASU; 170707; -.
DR Ensembl; ENSMUST00000055131; ENSMUSP00000055016; ENSMUSG00000043411. [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 CTD; 84196; -.
DR MGI; MGI:2158502; Usp48.
DR VEuPathDB; HostDB:ENSMUSG00000043411; -.
DR eggNOG; KOG1863; Eukaryota.
DR GeneTree; ENSGT00940000156015; -.
DR InParanoid; Q3V0C5; -.
DR OrthoDB; 113272at2759; -.
DR PhylomeDB; Q3V0C5; -.
DR TreeFam; TF106280; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 170707; 0 hits in 58 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 265 other tissues.
DR ExpressionAtlas; Q3V0C5; baseline and differential.
DR Genevisible; Q3V0C5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; 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; 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..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
