UBP51_MOUSE
ID UBP51_MOUSE Reviewed; 661 AA.
AC B1AY15;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 51 {ECO:0000303|PubMed:27083998};
DE EC=3.4.19.12 {ECO:0000269|PubMed:27083998};
DE AltName: Full=Deubiquitinating enzyme 51;
GN Name=Usp51 {ECO:0000312|MGI:MGI:3588217};
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].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP FUNCTION, ACTIVE SITE, MUTAGENESIS OF CYS-329 AND HIS-615, AND CATALYTIC
RP ACTIVITY.
RX PubMed=27083998; DOI=10.1101/gad.271841.115;
RA Wang Z., Zhang H., Liu J., Cheruiyot A., Lee J.H., Ordog T., Lou Z.,
RA You Z., Zhang Z.;
RT "USP51 deubiquitylates H2AK13,15ub and regulates DNA damage response.";
RL Genes Dev. 30:946-959(2016).
CC -!- FUNCTION: Deubiquitinates histone H2A at 'Lys-13' and 'Lys-15' and
CC regulates DNA damage response. USP51 is recruited to chromatin after
CC DNA damage and regulates the dynamic assembly/disassembly of TP53BP1
CC and BRCA1 foci. {ECO:0000269|PubMed:27083998}.
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:0000269|PubMed:27083998};
CC -!- SUBUNIT: Interacts with H2A. {ECO:0000250|UniProtKB:Q70EK9}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q70EK9}.
CC Note=Dissociates from chromatin immediately after DNA damage and
CC reassociates with chromatin following DNA repair.
CC {ECO:0000250|UniProtKB:Q70EK9}.
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; AL840632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS53226.1; -.
DR RefSeq; NP_001131019.1; NM_001137547.1.
DR AlphaFoldDB; B1AY15; -.
DR SMR; B1AY15; -.
DR STRING; 10090.ENSMUSP00000093427; -.
DR MEROPS; C19.065; -.
DR PhosphoSitePlus; B1AY15; -.
DR PaxDb; B1AY15; -.
DR PRIDE; B1AY15; -.
DR Antibodypedia; 52206; 37 antibodies from 20 providers.
DR Ensembl; ENSMUST00000095755; ENSMUSP00000093427; ENSMUSG00000067215.
DR GeneID; 635253; -.
DR KEGG; mmu:635253; -.
DR UCSC; uc009uqp.2; mouse.
DR CTD; 158880; -.
DR MGI; MGI:3588217; Usp51.
DR VEuPathDB; HostDB:ENSMUSG00000067215; -.
DR eggNOG; KOG1867; Eukaryota.
DR GeneTree; ENSGT00940000163664; -.
DR HOGENOM; CLU_008279_11_0_1; -.
DR InParanoid; B1AY15; -.
DR OMA; KQRKCDK; -.
DR OrthoDB; 929408at2759; -.
DR PhylomeDB; B1AY15; -.
DR TreeFam; TF323554; -.
DR BioGRID-ORCS; 635253; 4 hits in 72 CRISPR screens.
DR PRO; PR:B1AY15; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; B1AY15; protein.
DR Bgee; ENSMUSG00000067215; Expressed in yolk sac and 39 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISO:MGI.
DR GO; GO:0010564; P:regulation of cell cycle process; ISO:MGI.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; ISO:MGI.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033383; USP51.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646:SF38; PTHR21646:SF38; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA damage; DNA repair; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..661
FT /note="Ubiquitin carboxyl-terminal hydrolase 51"
FT /id="PRO_0000441892"
FT DOMAIN 320..656
FT /note="USP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT ZN_FING 149..267
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 1..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..98
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 329
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035,
FT ECO:0000269|PubMed:27083998"
FT ACT_SITE 615
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035,
FT ECO:0000269|PubMed:27083998"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT MUTAGEN 329
FT /note="C->S: Abolishes ability to deubiquitinate histone
FT H2A; when associated with R-615."
FT /evidence="ECO:0000269|PubMed:27083998"
FT MUTAGEN 615
FT /note="H->R: Abolishes ability to deubiquitinate histone
FT H2A; when associated with S-329."
FT /evidence="ECO:0000269|PubMed:27083998"
SQ SEQUENCE 661 AA; 74783 MW; 835F5340AC471579 CRC64;
MRGTQGAQEM KPELWPEPKP TSENLTSRGS GSYEKVLPSI PAACHTSSSS VCPRRKPRPR
PQPRSRSRGG RGLKAPPPPP AKPPPPPPAP PPPPLPKQRS VAWRNSRRRS RPGPRPQTRK
SYSSDHGSSR DSDGSENSLL EVGSNKGPTG CCHVESFKVA KNWQRNLRMI YQRFIWSGTP
ETRKRKAKSC ICQICSTHKN RLHSCLSCVF FGCFTDKHIH IHAETTQHNL AVDLCHGVIY
CFMCRDYVYD KDIEKIAKET KEKILGLLSS PTGDASYQQL MASEVEENQL TCESKDQETS
LVKPKKKRRK KTMYYTVGFR GLINLGNTCF MNCIVQVLTH IPLLKEFFLS NKHKCMMTSP
SLCLVCEMSL LFQAMYSGNQ SPHIPYKLLH LIWIHAEHLA GYRQQDAQEF LIAILDVLHR
HSRDDGIDQE GNSNCCNCII DHIFTGSLQS DLTCQVCHGV STTIDPCWDI SLDLPGPYTP
GRASSSTSSR DGQKPRVISL TDCLKWFTRP EDLGSSAKIK CSQCQSYQES TKQLTMKKLP
IVACFHLKRF EHLGKQRRKI NSFISFPLEL DMTPFLASTK ESIMKGQPLT ECVPSENKYS
LFAVINHHGT LESGHYTSFV RQEKDQWFSC DDAVVTKATM EELLNSEGYL LFYHRQDIEK
E
