Primary Information |
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BoMiProt ID | Bomi10223 |
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Protein Name | Ubiquitin carboxyl-terminal hydrolase 42/Deubiquitinating enzyme 42/Ubiquitin thioesterase 42/Ubiquitin-specific-processing protease 42 |
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Organism | Bos taurus |
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Uniprot ID | E1B9W9 |
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Milk Fraction | Whey |
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Aminoacid Length | 1333 |
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Molecular Weight | 146748 |
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FASTA Sequence |
Download |
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Gene Name | USP42 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | Deubiquitinating enzyme.Regulating transcription by deubiquitylating histones. which has important role during spermatogenesis.drives nuclear speckle phase separation dependent on its de-ubiquitinating activity, thus governing mRNA splicing events.USP42 inhibits Wnt signalling by deubiquitinating ZNRF3.USP42 is crucial for tumour supressors( ZNRF3/RNF43 ) stabilisation at the cell surface. |
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Biochemical Properties | Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin. |
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PTMs | Phosphorylation on Ser |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|E1B9W9|UBP42_BOVIN Ubiquitin carboxyl-terminal hydrolase 42 OS=Bos taurus OX=9913 GN=USP42 PE=3 SV=1
MTIVDKASESSDPSTYQNQPGSSEAVSPGDMDAGSASWGAVSSLNDVSNHTLSLGPVPGA
VVYSSSSVPEKSKPS*75PQKDQALGDGIAPPQKVLFPSEKICLKWQQTHRVGAGLQNLGNTC
FANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMQAHITQALSNPGDVIKPMFVI
NEMRRIARHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRS
RVKCLNCKGVSDTFDPYLDITLEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPA
SKRFTIHRSSNVLTLSLKRFANFTGGKIAKDVKYPEYLDIRPYMSQPNGEPIIYVLYAVL
VHTGFNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYIRSHDVKNGGE
LTHSAHSPGQSSPRPVISQRVVNSKQAASGFIGPQLPSHMMKNPPHLNGTGPLKETPSSP
MSGPSGNSSVSRTGPVSASPSVQNWSVNRPSVIPEHPKKQKITISIHNKLPVRQGQSQSN
LHSNSLEHPNKPAPSSTITTSSAIQSTSSAPTPPASSKVPKQMAPREACSRPMMNGRPRL
SAGVLVPYGAESSEESDEEAKGLGQENGRGLTESACSPALDAEDGDASPHELQEPVALNG
ATGLDSDPTENGLPSDGAPCPGQPALHSEHPFPKANGLPGKLMPAPLPPLPEDKILETFK
LGSKAKGSAEETRTPGSEERPLEHPEAELEAGRS*754PPGDARDNLESVSNLSSKFKKASPPS
DPSIKPTKEEVSERVSAEPEEAVPSASTFCNPDKDALGDDQLLAPCDPGNLTDDQSKPSP
DVGGTLPERPQDPVAAEAAGRLS*863PGPSVPSEGDHEPEPLGHSGRDRGSDAEGPSKSMGVS
TDEAPSAQLDTITENRPEGPPERSSSERGEDSKAGQKAPEPCLVQEKVSSLRKVDRGHYR
SRRDRSSSGEHARESRSRTEVQHRRKRPHREHERPRPERPRPEPCALAPQPPCPSSLARS
GHHHSRSRGAPDQEWGRYHHAEGDHAWTREKYYPDRLRWERCRYHHDRSPLYPSREPRDW
RPFHAEREYERAGPYGGRPYKDHYRGRKGYELVAKERDRHRFSSPRAGMAHAPPPHPAAK
YTHDRLSFGAEDGSCDLAARFHEHDNIKSRKRRYDSLENESHVEKKAWRS*1190LQKDPVEEPK
VKKHKKSKKKKKSKDKHRDRDSRHQQDS*1228DLS*1231VAHS*1235DADLHRHKKKKKKKK
RHSRKS*1256EDFGRDSEPRLPKAASCETVDHFRKAEGAFPLADGLPLEGAAPFCEKTKHFRMESREVRCRLSQ
CDQGKGARWESGS
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Predicted Disorder Regions | 1-34,67-74, 610-659, 780-834, 863-870, 913-925, |
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DisProt Annotation | |
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TM Helix Prediction | no TM helices |
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Bibliography | 1.Giebel N, de Jaime-Soguero A, García Del Arco A, Landry JJM, Tietje M, Villacorta L, Benes V, Fernández-Sáiz V, Acebrón SP. USP42 protects ZNRF3/RNF43 from R-spondin-dependent clearance and inhibits Wnt signalling. EMBO Rep. 2021 May 5;22(5):e51415. doi: 10.15252/embr.202051415. Epub 2021 Mar 30. PMID: 33786993; PMCID: PMC8097334. 2.Hock AK, Vigneron AM, Vousden KH. Ubiquitin-specific peptidase 42 (USP42) functions to deubiquitylate histones and regulate transcriptional activity. J Biol Chem. 2014 Dec 12;289(50):34862-70. doi: 10.1074/jbc.M114.589267. Epub 2014 Oct 21. PMID: 25336640; PMCID: PMC4263885. |