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   16-JUN-2009, entry version 25.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 1;
DE            EC=3.1.2.15;
DE   AltName: Full=Ubiquitin thioesterase 1;
DE   AltName: Full=Ubiquitin-specific-processing protease 1;
DE   AltName: Full=Deubiquitinating enzyme 1;
GN   Name=USP1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
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. Autocatalytic
CC       cleavage of USP1 leads to an increase in ubiquitinated PCNA,
CC       recruitment of POLH and translesion synthesis following DNA
CC       damage. Regulates ubiquitination of FANCD2 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Ubiquitin C-terminal thioester + H(2)O =
CC       ubiquitin + a thiol.
CC   -!- SUBUNIT: Interacts with FANCD2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- PTM: Ubiquitinated; leading to its subsequent proteasomal
CC       degradation (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
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DR   EMBL; BC114087; AAI14088.1; -; mRNA.
DR   IPI; IPI00708651; -.
DR   RefSeq; NP_001039689.1; -.
DR   UniGene; Bt.40485; -.
DR   MEROPS; C19.019; -.
DR   Ensembl; ENSBTAG00000020451; Bos taurus.
DR   GeneID; 516328; -.
DR   KEGG; bta:516328; -.
DR   HOVERGEN; Q29RP1; -.
DR   BRENDA; 3.1.2.15; 251.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   Pfam; PF00443; UCH; 1.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   2: Evidence at transcript level;
KW   Autocatalytic cleavage; DNA damage; DNA repair; Hydrolase; Nucleus;
KW   Phosphoprotein; Protease; Thiol protease; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN         1    783       Ubiquitin carboxyl-terminal hydrolase 1.
FT                                /FTId=PRO_0000306286.
FT   ACT_SITE     90     90       By similarity.
FT   ACT_SITE    582    582       By similarity.
FT   ACT_SITE    591    591       By similarity.
FT   SITE        669    670       Cleavage; by autolysis (By similarity).
FT   MOD_RES      13     13       Phosphoserine (By similarity).
FT   MOD_RES      42     42       Phosphoserine (By similarity).
FT   MOD_RES      67     67       Phosphoserine (By similarity).
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
//