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 24-JAN-2024, entry version 103. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SwissPalm; B2RQC2; -. DR EPD; B2RQC2; -. DR MaxQB; B2RQC2; -. DR PaxDb; 10090-ENSMUSP00000053955; -. DR PeptideAtlas; B2RQC2; -. DR ProteomicsDB; 297704; -. DR Pumba; B2RQC2; -. DR Antibodypedia; 1719; 119 antibodies from 27 providers. DR DNASU; 76800; -. DR Ensembl; ENSMUST00000053287.6; ENSMUSP00000053955.6; ENSMUSG00000051306.8. DR GeneID; 76800; -. DR KEGG; mmu:76800; -. DR UCSC; uc009akp.1; mouse. DR AGR; MGI:1924050; -. 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; YGGRPYK; -. DR OrthoDB; 227085at2759; -. DR PhylomeDB; B2RQC2; -. DR TreeFam; TF315281; -. DR Reactome; R-MMU-5689880; Ub-specific processing proteases. DR BioGRID-ORCS; 76800; 1 hit in 75 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 217 other cell types or tissues. 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:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central. DR GO; GO:0007283; P:spermatogenesis; TAS:UniProtKB. DR CDD; cd02661; Peptidase_C19E; 1. DR Gene3D; 3.90.70.10; Cysteine proteinases; 1. 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 PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1. DR PANTHER; PTHR24006:SF727; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 42; 1. DR Pfam; PF00443; UCH; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR PROSITE; PS00972; USP_1; 1. DR PROSITE; PS00973; USP_2; 1. DR PROSITE; PS50235; USP_3; 1. DR Genevisible; B2RQC2; MM. 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 //