UBP54_MOUSE
ID UBP54_MOUSE Reviewed; 1588 AA.
AC Q8BL06; Q149D8; Q149D9; Q6NZE1; Q8BZ28; Q9D2I9;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Inactive ubiquitin carboxyl-terminal hydrolase 54;
DE AltName: Full=Inactive ubiquitin-specific peptidase 54;
GN Name=Usp54;
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 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1026-1588 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Corpus striatum, Testis, and Vagina;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 918-1588 (ISOFORM 1).
RC STRAIN=CD-1; TISSUE=Neural stem cell;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, 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).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-12, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Has no peptidase activity. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BL06-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BL06-2; Sequence=VSP_020488, VSP_035679, VSP_035680;
CC Name=3;
CC IsoId=Q8BL06-3; Sequence=VSP_035679, VSP_035680;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- CAUTION: Although the active site residues are conserved, lacks the
CC conserved His residue which is normally found 9 residues before the
CC catalytic His. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI17845.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI17846.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB31805.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK019588; BAB31805.1; ALT_INIT; mRNA.
DR EMBL; AK036864; BAC29609.1; -; mRNA.
DR EMBL; AK047620; BAC33102.1; -; mRNA.
DR EMBL; AC146594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC066166; AAH66166.1; -; mRNA.
DR EMBL; BC066175; AAH66175.1; -; mRNA.
DR EMBL; BC117844; AAI17845.1; ALT_INIT; mRNA.
DR EMBL; BC117845; AAI17846.1; ALT_INIT; mRNA.
DR CCDS; CCDS26847.2; -. [Q8BL06-1]
DR RefSeq; NP_084456.2; NM_030180.2. [Q8BL06-1]
DR RefSeq; XP_006519768.1; XM_006519705.3. [Q8BL06-1]
DR AlphaFoldDB; Q8BL06; -.
DR BioGRID; 219632; 2.
DR STRING; 10090.ENSMUSP00000036214; -.
DR MEROPS; C19.080; -.
DR iPTMnet; Q8BL06; -.
DR PhosphoSitePlus; Q8BL06; -.
DR MaxQB; Q8BL06; -.
DR PaxDb; Q8BL06; -.
DR PeptideAtlas; Q8BL06; -.
DR PRIDE; Q8BL06; -.
DR ProteomicsDB; 298367; -. [Q8BL06-1]
DR ProteomicsDB; 298368; -. [Q8BL06-2]
DR ProteomicsDB; 298369; -. [Q8BL06-3]
DR Antibodypedia; 54962; 80 antibodies from 17 providers.
DR DNASU; 78787; -.
DR Ensembl; ENSMUST00000022356; ENSMUSP00000022356; ENSMUSG00000034235. [Q8BL06-1]
DR Ensembl; ENSMUST00000035340; ENSMUSP00000036214; ENSMUSG00000034235. [Q8BL06-1]
DR GeneID; 78787; -.
DR KEGG; mmu:78787; -.
DR UCSC; uc007skb.1; mouse. [Q8BL06-1]
DR UCSC; uc007skc.1; mouse. [Q8BL06-3]
DR CTD; 159195; -.
DR MGI; MGI:1926037; Usp54.
DR VEuPathDB; HostDB:ENSMUSG00000034235; -.
DR eggNOG; KOG1887; Eukaryota.
DR GeneTree; ENSGT00940000155571; -.
DR HOGENOM; CLU_004234_0_0_1; -.
DR InParanoid; Q8BL06; -.
DR OMA; YGAENFH; -.
DR OrthoDB; 101145at2759; -.
DR PhylomeDB; Q8BL06; -.
DR TreeFam; TF336130; -.
DR BioGRID-ORCS; 78787; 8 hits in 72 CRISPR screens.
DR ChiTaRS; Usp54; mouse.
DR PRO; PR:Q8BL06; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BL06; protein.
DR Bgee; ENSMUSG00000034235; Expressed in lumbar subsegment of spinal cord and 196 other tissues.
DR ExpressionAtlas; Q8BL06; baseline and differential.
DR Genevisible; Q8BL06; MM.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR040142; USP54.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR22975:SF5; PTHR22975:SF5; 3.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1588
FT /note="Inactive ubiquitin carboxyl-terminal hydrolase 54"
FT /id="PRO_0000249531"
FT DOMAIN 31..352
FT /note="USP"
FT REGION 382..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1221..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1491..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 682..712
FT /evidence="ECO:0000255"
FT COMPBIAS 382..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1537..1561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IE24"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q70EL1"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IE24"
FT VAR_SEQ 1..69
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020488"
FT VAR_SEQ 383..402
FT /note="HLTDSECNQKHTSKKGSLVE -> EQPSSPTPPYSQMVGSHTQG (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035679"
FT VAR_SEQ 403..1588
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035680"
FT CONFLICT 925
FT /note="G -> D (in Ref. 3; AAH66166/AAH66175)"
FT /evidence="ECO:0000305"
FT CONFLICT 1288
FT /note="R -> G (in Ref. 3; AAI17845)"
FT /evidence="ECO:0000305"
FT CONFLICT 1476
FT /note="L -> V (in Ref. 1; BAB31805)"
FT /evidence="ECO:0000305"
FT CONFLICT 1574
FT /note="G -> E (in Ref. 3; AAH66166/AAH66175)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1588 AA; 176664 MW; 4F211ACF4502D584 CRC64;
MSWKRNYFSG SRGSVQGMFA PRSSMSIAPS KGLSNEPGQN SCFLNSALQV LWHLDIFRRS
FRQLTTHKCM GDSCIFCALK GIFNQFQCSS EKVLPSDTLR SALAKTFQDE QRFQLGIMDD
AAECFENLLM RIHFHIADET KEDICTAQHC ISHQKFAMTL FEQCVCSSCG ATSDPLPFIQ
MVHYISTTAL CNQAICMLEK REKPSPSMFG ELLQNASTMG DLRNCPSNCG ERIRIRRVLM
NAPQIITIGL VWDSEHSDLA EDVIHSLGTC LKLGDLFFRV TDDRAKQSEL YLVGMICYYG
KHYSTFFFQT KIRKWMYFDD AHVKEIGPKW KDVVTKCIKG HYQPLLLLYA DPQGTPVSAQ
DLPPHAQFLP YTKTCYDSED SGHLTDSECN QKHTSKKGSL VERRRSSGRV RRKGDEPQAS
GYHSEGETLK EKQAPRNASK SSSSSRLKDF KETVSNMIHS RPSLASQTSA GSPCVGRAGD
QLDKIPPRNF PLQARGWETE STSSEAKSSS SSKYRPTWRP KRESLNIDSI FSKDRRKHCG
YTQLRTFPED AAKEFTPDEV SKPTANDIKD GGSRSQHKLW GTARPGSHLL EQHPRLIQRM
ESGYESSERN SSSPVSLDAA PPDSVNVYRD QSTKRPVGFV PSWRHIPKSH SSSILEVDCT
APMTSWTKTQ PLSDGEVTSR SELDELQEEV VRRAQEQELR KKREKELEAA KGFNPHPSRY
MDLDELQNQG RSDGFERSLQ EANSIFEESL HLEQKGDCAA ALALCNEAIS KLRLTLHDAS
SSTHSRALVD KKLQISIRKA RSLQDRMQQQ ASSQQPVQPS ASLPSQGGAL PQPTSEQPIT
LQVLLNQEAQ LEPCKDTELG ATSSFFHSPA SCPELHSSLI PESPVSSVSQ HSPPGTSSLK
LLTSFEVDSV NRSAFHRQGL PKATGRTEMN SQHECLPLDA LEDRLQGHRE DNSCCSKFPP
REGRDIAQDQ LFEGKKNPAD ISMGMPWSYS TGEATSERVI YSLNSPSSSS AQPSIPPYSS
CHPITSAASS PVLHAADPMQ KLNQHVQAQS LQTSLTSKVV RSSEEPYRLE FPSTKGLVRS
LAEQFQKMQN TSTRDVIGSQ DRSLPNGVRK SSSPSDFMPP LSQGPGREHC RWVKQPRSPD
GRERPPCWED PAAHPPLSMG SGLPDGETSR TAQPRLAEPD MYQGKLPQVT DIRSKELGSS
VNLGTSLPLD SWVNVTRLCD SQVKPSAPGP GDKSSSHDSH PRATCLERSP ILLHPHWDQD
TEQETSELES LYQASLQASS HTAYSDWRSQ DVAWQPLSLA GSADGMGRRL HSAPGLDLSK
PLTAEMEHVL YEPSTVPVSQ DSSNVRKKTL ETGHHCSSSS SLPVIHDPPV FLLDPKLYPP
QPQFLSPDVL MPSMAGEPYR PPGTSRSVHQ FLAMCDRDET PQGVKYTGRT LNYRSLPHRS
RTDASWGPGS ETNQHIGARV LTMPACKPQL TYTATLPERH QGLQVPHAQS WGNLFHSPSH
PSAVHPGSPP SSNLHVPLRS TWNSGPVLGS RTPGPRRIDM PPDDDWRQSS YPSQDRHRSP
GEERIMFALS NAAGREQNRV RFLQHSRW
