UBP48_RAT
ID UBP48_RAT Reviewed; 1036 AA.
AC Q76LT8;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 48;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 48;
DE AltName: Full=Synaptic ubiquitin-specific protease;
DE Short=synUSP;
DE AltName: Full=Ubiquitin thioesterase 48;
DE AltName: Full=Ubiquitin-specific-processing protease 48;
GN Name=Usp48;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14535949; DOI=10.1046/j.1471-4159.2003.02024.x;
RA Tian Q.B., Okano A., Nakayama K., Miyazawa S., Endo S., Suzuki T.;
RT "A novel ubiquitin-specific protease, synUSP, is localized at the post-
RT synaptic density and post-synaptic lipid raft.";
RL J. Neurochem. 87:665-675(2003).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-887; SER-888 AND SER-889, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:14535949}.
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:14535949};
CC -!- SUBUNIT: Interacts with TRAF2 and RELA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=In neuronal cells, it localizes to dendrites, as well as somas.
CC {ECO:0000269|PubMed:14535949}.
CC -!- TISSUE SPECIFICITY: Present in the brain, in particular in the
CC postsynaptic density and the dendritic lipid raft fractions (at protein
CC level). {ECO:0000269|PubMed:14535949}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AB073880; BAD00009.1; -; mRNA.
DR RefSeq; NP_942080.1; NM_198785.1.
DR AlphaFoldDB; Q76LT8; -.
DR SMR; Q76LT8; -.
DR BioGRID; 263601; 1.
DR STRING; 10116.ENSRNOP00000030008; -.
DR MEROPS; C19.068; -.
DR iPTMnet; Q76LT8; -.
DR PhosphoSitePlus; Q76LT8; -.
DR PaxDb; Q76LT8; -.
DR GeneID; 362636; -.
DR KEGG; rno:362636; -.
DR UCSC; RGD:735213; rat.
DR CTD; 84196; -.
DR RGD; 735213; Usp48.
DR eggNOG; KOG1863; Eukaryota.
DR InParanoid; Q76LT8; -.
DR OrthoDB; 113272at2759; -.
DR PhylomeDB; Q76LT8; -.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR PRO; PR:Q76LT8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
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; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Repeat; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1036
FT /note="Ubiquitin carboxyl-terminal hydrolase 48"
FT /id="PRO_0000249525"
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..692
FT /note="DUSP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 712..825
FT /note="DUSP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 930..1010
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 611..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..924
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 887
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 889
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 957
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q86UV5"
SQ SEQUENCE 1036 AA; 118787 MW; EEC407C21D4BC539 CRC64;
MAPRLQLEKA AWRWAETVRP EEVSQEHIET AYRIWLEPCI RGVCRRNCRG NPNCLVGIGE
HIWLGEIDEN SFHNIDDPNC ERRKKNSFVG LTNLGASCYV NTFLQVWFLN LELRQALYLC
PSTCSDYTKG DGIRGGKDYE PQTICEHLQY LFALLQNSNR RYIDPSGFVK ALGLDTGQQQ
DAQESSKLFM SLLEDTLSKQ KNPDVRNVVQ QQFCGEYAYV TVCSQCGRES KLVSKFYELE
LNIQGHKQLT DCISEFLKEE RLEGDNRYFC ENCQSKQNAT RKIRLLSLPC TLNLQLMRFV
FDRQTGHKKK LNAYIGFSES LDMEPYVEHK GGSFVYELSA VLIHRGVSAY SGHYIAHVKD
PQSGDWYKFN DEDIEKMEGK KLQLGIEEDL TEPSKSQTRK PKCGKGTHCS RNAYMLVYRL
QTQEKNHTMV QVPAFLQELV DRDNSKFEEW CVEMAEMRRQ SVDKGRAKHE EVKELYQRLP
AGAEPYEFVS LEWLQKWLDE STPTKPIDNN ACLCSHDKLH PDKISIMKRI SEYAADIFYS
RYGGGPRLTV KALCKDCVVE RCRILRLKNQ LNEDYKTVNN LLKATMKGSD GFWVGKSSLR
SWRQLALEQL DEQDGEAEQS NGKINGSPFS KDESKEEKKE EEEELNFNED ILCPHGELSI
SENERRLVSQ EAWSKLQQYF PKAPEFPSYK ECCSQCKILE REGEENEALH KMIAKEQKTS
LPNLFQDKNR PCLSNWPEDT DALYIVSHFF LDEWRKFVRK PARSTPVSSV GNAALLCPHG
GLMFTFPSLT KEDSKLIALI WPSEWQMIQK LFVVDKVIKI TRIEVGDVNP SQTQYISEPN
LCPDCREGLL CQQQKDLREY TQATIYVHKV VDNKKVMKDS APELNVSSSE TEEDKEEAKP
DGEKDPDFNQ SNGGTKRQKT SQQGYVAYQK QVIRRSTRHR KVRGEKALLV SANQTLKELK
IQIMHAFSVA PFDQNLSIDG KILNDDCATL GTLGVIPESV ILLKADEPIA DYAAMDDVMQ
VCMPEEGFKG TGLLGH
