UBP5_MOUSE
ID UBP5_MOUSE Reviewed; 858 AA.
AC P56399;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 5;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 5;
DE AltName: Full=Isopeptidase T;
DE AltName: Full=Ubiquitin thioesterase 5;
DE AltName: Full=Ubiquitin-specific-processing protease 5;
GN Name=Usp5; Synonyms=Isot;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-623, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP INTERACTION WITH TRIML1.
RX PubMed=19156909; DOI=10.1002/mrd.20997;
RA Tian L., Wu X., Lin Y., Liu Z., Xiong F., Han Z., Zhou Y., Zeng Q.,
RA Wang Y., Deng J., Chen H.;
RT "Characterization and potential function of a novel pre-implantation
RT embryo-specific RING finger protein: TRIML1.";
RL Mol. Reprod. Dev. 76:656-664(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-623; SER-779 AND SER-783, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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: Cleaves linear and branched multiubiquitin polymers with a
CC marked preference for branched polymers. Involved in unanchored 'Lys-
CC 48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked
CC polyubiquitin with a lower affinity (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Interacts with TRIML1. {ECO:0000269|PubMed:19156909}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AC002397; AAC36015.1; -; Genomic_DNA.
DR EMBL; BC066993; AAH66993.1; -; mRNA.
DR CCDS; CCDS20531.1; -.
DR RefSeq; NP_001313523.1; NM_001326594.1.
DR RefSeq; NP_038728.1; NM_013700.2.
DR AlphaFoldDB; P56399; -.
DR SMR; P56399; -.
DR BioGRID; 204425; 23.
DR IntAct; P56399; 1.
DR MINT; P56399; -.
DR STRING; 10090.ENSMUSP00000041299; -.
DR MEROPS; C19.001; -.
DR iPTMnet; P56399; -.
DR PhosphoSitePlus; P56399; -.
DR SwissPalm; P56399; -.
DR EPD; P56399; -.
DR jPOST; P56399; -.
DR MaxQB; P56399; -.
DR PaxDb; P56399; -.
DR PeptideAtlas; P56399; -.
DR PRIDE; P56399; -.
DR ProteomicsDB; 297710; -.
DR Antibodypedia; 1723; 396 antibodies from 31 providers.
DR DNASU; 22225; -.
DR Ensembl; ENSMUST00000047510; ENSMUSP00000041299; ENSMUSG00000038429.
DR GeneID; 22225; -.
DR KEGG; mmu:22225; -.
DR UCSC; uc009dsa.1; mouse.
DR CTD; 8078; -.
DR MGI; MGI:1347343; Usp5.
DR VEuPathDB; HostDB:ENSMUSG00000038429; -.
DR eggNOG; KOG0944; Eukaryota.
DR GeneTree; ENSGT00940000156036; -.
DR InParanoid; P56399; -.
DR OMA; FDERQAV; -.
DR OrthoDB; 556111at2759; -.
DR PhylomeDB; P56399; -.
DR TreeFam; TF300576; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR BioGRID-ORCS; 22225; 24 hits in 73 CRISPR screens.
DR ChiTaRS; Usp5; mouse.
DR PRO; PR:P56399; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P56399; protein.
DR Bgee; ENSMUSG00000038429; Expressed in spermatocyte and 253 other tissues.
DR ExpressionAtlas; P56399; baseline and differential.
DR Genevisible; P56399; MM.
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; ISO:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0016579; P:protein deubiquitination; ISO:MGI.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISO:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd14383; UBA1_UBP5; 1.
DR Gene3D; 3.30.40.10; -; 3.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR InterPro; IPR041432; UBP13_Znf-UBP_var.
DR InterPro; IPR041812; UBP5_UBA1.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR Pfam; PF17807; zf-UBP_var; 1.
DR PIRSF; PIRSF016308; UBP; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50030; UBA; 2.
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 Acetylation; Disulfide bond; Hydrolase; Metal-binding; Phosphoprotein;
KW Protease; Reference proteome; Repeat; Thiol protease;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P45974"
FT CHAIN 2..858
FT /note="Ubiquitin carboxyl-terminal hydrolase 5"
FT /id="PRO_0000080624"
FT DOMAIN 326..856
FT /note="USP"
FT DOMAIN 654..695
FT /note="UBA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 722..762
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT ZN_FING 175..283
FT /note="UBP-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 73..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 335
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 818
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 221..224
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P45974"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P45974"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P45974"
FT MOD_RES 623
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P45974"
FT DISULFID 195..816
FT /evidence="ECO:0000250"
SQ SEQUENCE 858 AA; 95833 MW; E1F31A0C92687CA8 CRC64;
MAELSEEALL SVLPTIRVPK AGDRVHKDEC AFSFDTPESE GGLYICMNTF LGFGKQYVER
HFNKTGQRVY LHLRRTRRPK EEDTSAGTGD PPRKKPTRLA IGVEGGFDLT EDKFEFDEDV
KIVILPDYLE IARDGLGGLP DIVRDRVTSA VEALLSADSA SRKQEVQAWD GEVRQVSKHA
FNLKQLDNPA RIPPCGWKCS KCDMRENLWL NLTDGSILCG RRYFDGSGGN NHAVEHYRET
GYPLAVKLGT ITPDGADVYS YDEDDMVLDP SLAEHLSHFG IDMLKMQKTD KTMTELEIDM
NQRIGEWELI QESGVPLKPL FGPGYTGIRN LGNSCYLNSV VQVLFSIPDF QRKYVDKLEK
IFQNAPTDPT QDFSTQVAKL GHGLLSGEYS KPALESGDGE QVPEQKEVQD GIAPRMFKAL
IGKGHPEFST NRQQDAQEFF LHLINMVERN CRSSENPNEV FRFLVEEKIK CLATEKVKYT
QRVDYIMQLP VPMDAALNKE ELLEYEEKKR QAEEEKVPLP ELVRAQVPFS SCLEAYGAPE
QVDDFWSTAL QAKSVAVKTT RFASFPDYLV IQIKKFTFGL DWVPKKLDVS IEMPEELDIS
QLRGTGLQPG EEELPDIAPP LVTPDEPKGS LGFYGNEDED SFCSPHFSSP TSPMLDESVI
IQLVEMGFPM DACRKAVYYT GNSGAEAAMN WVMSHMDDPD FANPLILPGS SGPGSTSAAA
DPPPEDCVTT IVSMGFSRDQ ALKALRATNN SLERAVDWIF SHIDDLDAEA AMDISEGRSA
AESISESVPV GPKVRDGPGK YQLFAFISHM GTSTMCGHYV CHIKKEGRWV IYNDQKVCAS
EKPPKDLGYI YFYQRVVS
