UBP1_BOVIN
ID UBP1_BOVIN Reviewed; 783 AA.
AC Q29RP1;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 1;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:O94782};
DE AltName: Full=Deubiquitinating enzyme 1;
DE AltName: Full=Ubiquitin thioesterase 1;
DE AltName: Full=Ubiquitin-specific-processing protease 1;
DE Contains:
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment {ECO:0000250|UniProtKB:O94782};
GN Name=USP1 {ECO:0000250|UniProtKB:O94782};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI14088.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI14088.1};
RC TISSUE=Heart ventricle {ECO:0000312|EMBL:AAI14088.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Negative regulator of DNA damage repair which specifically
CC deubiquitinates monoubiquitinated FANCD2. Also involved in PCNA-
CC mediated translesion synthesis (TLS) by deubiquitinating
CC monoubiquitinated PCNA. Has almost no deubiquitinating activity by
CC itself and requires the interaction with WDR48 to have a high activity.
CC {ECO:0000250|UniProtKB:O94782}.
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; Evidence={ECO:0000250|UniProtKB:O94782};
CC -!- SUBUNIT: Interacts with FANCD2 and PCNA. Interacts with WDR48.
CC Interacts with ATAD5; the interaction regulates USP1-mediated PCNA
CC deubiquitination. {ECO:0000250|UniProtKB:O94782}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94782}.
CC -!- PTM: Autocatalytic cleavage of USP1 following UV irradiation
CC inactivates it leading to an increase in ubiquitinated PCNA,
CC recruitment of POLH and translesion synthesis.
CC {ECO:0000250|UniProtKB:O94782}.
CC -!- PTM: [Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment]:
CC Ubiquitinated by the CRL2(KLHDC2) complex following autocatalytic
CC cleavage, leading to its degradation: the CRL2(KLHDC2) complex
CC recognizes the diglycine (Gly-Gly) at the C-terminus.
CC {ECO:0000250|UniProtKB:O94782}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000255}.
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DR EMBL; BC114087; AAI14088.1; -; mRNA.
DR RefSeq; NP_001039689.1; NM_001046224.1.
DR AlphaFoldDB; Q29RP1; -.
DR SMR; Q29RP1; -.
DR STRING; 9913.ENSBTAP00000027254; -.
DR MEROPS; C19.019; -.
DR PaxDb; Q29RP1; -.
DR PRIDE; Q29RP1; -.
DR GeneID; 516328; -.
DR KEGG; bta:516328; -.
DR CTD; 7398; -.
DR eggNOG; KOG1864; Eukaryota.
DR InParanoid; Q29RP1; -.
DR OrthoDB; 439300at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02671; Peptidase_C19O; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033815; USP1.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 2.
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 Autocatalytic cleavage; DNA damage; DNA repair; Hydrolase; Nucleus;
KW Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..783
FT /note="Ubiquitin carboxyl-terminal hydrolase 1"
FT /id="PRO_0000306286"
FT CHAIN 1..669
FT /note="Ubiquitin carboxyl-terminal hydrolase 1, N-terminal
FT fragment"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT /id="PRO_0000453161"
FT DOMAIN 81..783
FT /note="USP"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 591
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT SITE 669..670
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJQ2"
SQ SEQUENCE 783 AA; 88459 MW; 7910D2FC5668E87C CRC64;
MPGVIPSESN GLSRGSPSKK NRLSLKFFQK KETKRALDFT DSQENEEKTS EYKGSEIDQV
VPAAQSSPIN CEKRENLLPF VGLNNLGNTC YLNSILQVLY FCPGFKSGVK HLFNIISRKK
EALKDEANQK DKGNCKEDSL ASYELICSLQ SLIISVEQLQ ASFLLNPEKY TDELATQPRR
LLNTLRELNP MYEGYLQHDA QEVLQCILGN IQETCQLLKK EEVKNVEDLS TKVEEYQKEE
MSDNNSMEMD NMRHSEDYKE KLSKGNGKRK SDAEFGNMKK KVKISKEHQS SEENQRQTRS
KRKAAGDTLE ISHKIIPKHI SENESTRPSQ RKSKVKINWL KSAAKQPSIL SKFCSMGKIA
TNQGSKGHCK ENEYDLEEDL GKYENDNTTN DCELESPGNN DMPVHVNEVK PINKGAEQIG
FELVEKLFQG QLVLRTRCLE CESLTERRED FQDISVPVQE DELSKVEENS EISPEPKTEM
KTLRWAISQF ASVERIVGED KYFCENCHHY TEAERSLLFD KMPEVITIHL KCFAASGLEF
DCYGGGLSKI NTPLLTPLKL SLEEWSTKPT NDSYGLFAVV MHSGITISSG HYTASVKVTD
LNSLELDKEN FVIDQTCEIG KPEPLNEEEV RGVVENYDNE EVSIRVSGNN QPSKVLNKKN
VEAIGLLGGQ KSKADYELYN KASNPDKVAS TALPENRNSE TNNTNGTDES DSNKESSDQT
GINISGFENK ISYVVQSLKE YEGKWLLFDD SEVKVTEEKD FLNSLSPSTS PTSTPYLLFY
KKL
