UBP50_MOUSE
ID UBP50_MOUSE Reviewed; 390 AA.
AC Q6P8X6; Q9D558; Q9D9E7;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Putative ubiquitin carboxyl-terminal hydrolase 50;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 50;
DE AltName: Full=Ubiquitin thioesterase 50;
DE AltName: Full=Ubiquitin-specific-processing protease 50;
GN Name=Usp50;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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).
CC -!- FUNCTION: May recognize and hydrolyze the peptide bond at the C-
CC terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC precursors as well as that of ubiquitinated proteins (By similarity).
CC {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P8X6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P8X6-2; Sequence=VSP_020486, VSP_020487;
CC -!- MISCELLANEOUS: The human ortholog is inactive.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AK007018; BAB24831.1; -; mRNA.
DR EMBL; AK015766; BAB29966.1; -; mRNA.
DR EMBL; BC061020; AAH61020.1; -; mRNA.
DR CCDS; CCDS16688.1; -. [Q6P8X6-1]
DR RefSeq; NP_083439.2; NM_029163.3. [Q6P8X6-1]
DR AlphaFoldDB; Q6P8X6; -.
DR SMR; Q6P8X6; -.
DR STRING; 10090.ENSMUSP00000028842; -.
DR MEROPS; C19.058; -.
DR PhosphoSitePlus; Q6P8X6; -.
DR PaxDb; Q6P8X6; -.
DR PRIDE; Q6P8X6; -.
DR ProteomicsDB; 298463; -. [Q6P8X6-1]
DR ProteomicsDB; 298464; -. [Q6P8X6-2]
DR Antibodypedia; 24751; 129 antibodies from 25 providers.
DR DNASU; 75083; -.
DR Ensembl; ENSMUST00000028842; ENSMUSP00000028842; ENSMUSG00000027364. [Q6P8X6-1]
DR GeneID; 75083; -.
DR KEGG; mmu:75083; -.
DR UCSC; uc008mee.2; mouse. [Q6P8X6-1]
DR CTD; 373509; -.
DR MGI; MGI:1922333; Usp50.
DR VEuPathDB; HostDB:ENSMUSG00000027364; -.
DR eggNOG; KOG1868; Eukaryota.
DR GeneTree; ENSGT00940000160441; -.
DR HOGENOM; CLU_008279_1_3_1; -.
DR InParanoid; Q6P8X6; -.
DR OMA; ECTDHYD; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; Q6P8X6; -.
DR TreeFam; TF106277; -.
DR BioGRID-ORCS; 75083; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Usp50; mouse.
DR PRO; PR:Q6P8X6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q6P8X6; protein.
DR Bgee; ENSMUSG00000027364; Expressed in seminiferous tubule of testis and 63 other tissues.
DR ExpressionAtlas; Q6P8X6; baseline and differential.
DR Genevisible; Q6P8X6; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0031313; C:extrinsic component of endosome membrane; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0019783; F:ubiquitin-like protein peptidase activity; ISO:MGI.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0035063; P:nuclear speck organization; ISO:MGI.
DR GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; IMP:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:MGI.
DR GO; GO:0032741; P:positive regulation of interleukin-18 production; IMP:MGI.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IMP:MGI.
DR GO; GO:0016579; P:protein deubiquitination; ISO:MGI.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IBA:GO_Central.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..390
FT /note="Putative ubiquitin carboxyl-terminal hydrolase 50"
FT /id="PRO_0000249529"
FT DOMAIN 45..363
FT /note="USP"
FT ACT_SITE 54
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020486"
FT VAR_SEQ 220..232
FT /note="DCLQCFFQQDTLT -> VGSPQLLNIFSCF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020487"
FT CONFLICT 173
FT /note="T -> I (in Ref. 1; BAB29966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 44543 MW; 37D9FC61FF818E88 CRC64;
MCFIDMASHR PVPADDFGAY YNLAECADYD SLPESKTQPH FQGVTGLRNL GNTCYMNAIL
QCLCSVSPLV EYFLSGKYIT ALKKDCSEVT TAFAYLMTDM WLGDSDCVSP EIFLSAVGSL
YPAFLKKTQQ DAQEFLIYVL NELHEALKKH CRRRVNEKRT GQSCCRKVPA QETSIITRLF
EGQLSYSITC LKCESCTHKN EVFTILSLPI PSDYECSLQD CLQCFFQQDT LTWSNQIYCS
FCEIKQEAAV RTTISKVPKI IVFHFKRFDI QGTVKRKLRT DIHYPLTNLD LTPYICPVFR
KHPMYNLCAV VNHFGDLDGG HYTAFCKNSV TQAWYSFDDT RVSEIPDTSV QTATAYLLFY
SCQPFSIPAQ KRKSQDSTPD HCKQAIRKWP
