UBP42_MOUSE
ID UBP42_MOUSE Reviewed; 1324 AA.
AC B2RQC2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 42;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 42;
DE AltName: Full=Ubiquitin thioesterase 42;
DE AltName: Full=Ubiquitin-specific-processing protease 42;
GN Name=Usp42;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16904385; DOI=10.1016/j.modgep.2006.06.006;
RA Kim Y.K., Kim Y.S., Yoo K.J., Lee H.J., Lee D.R., Yeo C.Y., Baek K.H.;
RT "The expression of Usp42 during embryogenesis and spermatogenesis in
RT mouse.";
RL Gene Expr. Patterns 7:143-148(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-858; SER-910; SER-1227;
RP SER-1230 AND SER-1234, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=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: Deubiquitinating enzyme which may play an important role
CC during spermatogenesis. {ECO:0000269|PubMed:16904385}.
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 -!- TISSUE SPECIFICITY: Highest expression seen in the testis. Also
CC expressed in brain, lung and thymus. The expression level gradually
CC increases from 2 weeks after birth and then decreases from the
CC pachytene spermatocyte (PS) stage during spermatogenesis.
CC {ECO:0000269|PubMed:16904385}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the midbrain, forebrain, optic
CC vesicles and eyes of embryos at 10.5 dpc and a more pronounced
CC expression is seen at 12.5 dpc. {ECO:0000269|PubMed:16904385}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; CH466529; EDL19037.1; -; Genomic_DNA.
DR EMBL; BC137852; AAI37853.1; -; mRNA.
DR CCDS; CCDS39372.1; -.
DR RefSeq; NP_084025.2; NM_029749.2.
DR RefSeq; XP_006504817.1; XM_006504754.3.
DR AlphaFoldDB; B2RQC2; -.
DR SMR; B2RQC2; -.
DR BioGRID; 218324; 2.
DR IntAct; B2RQC2; 1.
DR MINT; B2RQC2; -.
DR STRING; 10090.ENSMUSP00000053955; -.
DR iPTMnet; B2RQC2; -.
DR PhosphoSitePlus; B2RQC2; -.
DR EPD; B2RQC2; -.
DR MaxQB; B2RQC2; -.
DR PaxDb; B2RQC2; -.
DR PeptideAtlas; B2RQC2; -.
DR PRIDE; B2RQC2; -.
DR ProteomicsDB; 297704; -.
DR Antibodypedia; 1719; 107 antibodies from 27 providers.
DR DNASU; 76800; -.
DR Ensembl; ENSMUST00000053287; ENSMUSP00000053955; ENSMUSG00000051306.
DR GeneID; 76800; -.
DR KEGG; mmu:76800; -.
DR UCSC; uc009akp.1; mouse.
DR CTD; 84132; -.
DR MGI; MGI:1924050; Usp42.
DR VEuPathDB; HostDB:ENSMUSG00000051306; -.
DR eggNOG; KOG1865; Eukaryota.
DR GeneTree; ENSGT00940000154596; -.
DR HOGENOM; CLU_005541_1_0_1; -.
DR InParanoid; B2RQC2; -.
DR OMA; HVEKKAW; -.
DR OrthoDB; 929408at2759; -.
DR PhylomeDB; B2RQC2; -.
DR TreeFam; TF315281; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 76800; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Usp42; mouse.
DR PRO; PR:B2RQC2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; B2RQC2; protein.
DR Bgee; ENSMUSG00000051306; Expressed in cumulus cell and 214 other tissues.
DR Genevisible; B2RQC2; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; TAS:UniProtKB.
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 1: Evidence at protein level;
KW Differentiation; Hydrolase; Phosphoprotein; Protease; Reference proteome;
KW Spermatogenesis; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1324
FT /note="Ubiquitin carboxyl-terminal hydrolase 42"
FT /id="PRO_0000404199"
FT DOMAIN 110..411
FT /note="USP"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1217
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1253
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 370
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9J4"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9J4"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9J4"
FT MOD_RES 858
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9J4"
FT MOD_RES 1227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9J4"
SQ SEQUENCE 1324 AA; 146223 MW; 5214E845D98C3288 CRC64;
MTIVDKTEPS DPSTCQNQPG SCEAVSPEDM DTGSASWGAV SSISDVSSHT LPLGPVPGAV
VYSNSSVPEK SKPSPPKDQV LGDGIAPPQK VLFPSEKICL KWQQSHRVGA GLQNLGNTCF
ANAALQCLTY TPPLANYMLS HEHSKTCHAE GFCMMCTMQT HITQALSNPG DVIKPMFVIN
EMRRIARHFR FGNQEDAHEF LQYTVDAMQK ACLNGSNKLD RHTQATTLVC QIFGGYLRSR
VKCLNCKGVS DTFDPYLDIT LEIKAAQSVT KALEQFVKPE QLDGENSYKC SKCKKMVPAS
KRFTIHRSSN VLTISLKRFA NFTGGKIAKD VKYPEYLDIR PYMSQPNGEP IIYVLYAVLV
HTGFNCHAGH YFCYIKASNG LWYQMNDSIV STSDIRAVLN QQAYVLFYIR SHDVKNGGES
AHPAHSPGQS SPRPGVSQRV VNNKQVAPGF IGPQLPSHVM KNTPHLNGTT PVKDTPSSSV
SSPNGNTSVN RASPATASTS VQNWSVTRPS VIPDHPKKQK ITISIHNKLP ARQGQAPLNN
SLHGPCLEAP SKAAPSSTIT NPSAIQSTSN VPTTSTSPSE ACPKPMVNGK AKVGASVLVP
YGAESSEESD EESKGLAKEN GVDMMAGTHS DRPEAAADDG AEASSHELQE PVLLNGANSA
DSDSQENSLA FDSASCQVQP ELHTENLFSK LNGLPGKVTP APLQSVPEDR ILETFKLTNQ
AKGPAGEESW TTTGGSSPKD PVSQLEPISD EPSPLEIPEA VTNGSTQTPS TTSPLEPTIS
CTKEDSSVVV SAEPVEGLPS VPALCNSTGT ILGDTPVPEL CDPGDLTANP SQPTEAVKGD
TAEKAQDSAM AEVVERLSPA PSVLTGDGCE QKLLLYLSAE GSEETEDSSR SSAVSADTMP
PKPDRTTTSS CEGAAEQAAG DRGDGGHVGP KAQEPSPAKE KMSSLRKVDR GHYRSRRERS
SSGEHVRDSR PRPEDHHHKK RHCYSRERPK QDRHPTNSYC NGGQHLGHGD RASPERRSLS
RYSHHHSRIR SGLEQDWSRY HHLENEHAWV RERFYQDKLR WDKCRYYHDR YTPLYTARDA
REWRPLHGRE HDRLVQSGRP YKDSYWGRKG WELQSRGKER PHFNSPREAP SLAVPLERHL
QEKAALSVQD SSHSLPERFH EHKSVKSRKR RYETLENNDG RLEKKVHKSL EKDTLEEPRV
KKHKKSKKKK KSKDKHRDRE SRHQQESDFS GAYSDADLHR HRKKKKKKKR HSRKSEDFIK
DVEMRLPKLS SYEAGGHFRR TEGSFLLADG LPVEDSGPFR EKTKHLRMES RPDRCRLSEY
GQGD
