UCHL5_HUMAN
ID UCHL5_HUMAN Reviewed; 329 AA.
AC Q9Y5K5; Q5LJA6; Q5LJA7; Q8TBS4; Q96BJ9; Q9H1W5; Q9P0I3; Q9UQN2;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L5;
DE Short=UCH-L5;
DE EC=3.4.19.12;
DE AltName: Full=Ubiquitin C-terminal hydrolase UCH37;
DE AltName: Full=Ubiquitin thioesterase L5;
GN Name=UCHL5; Synonyms=UCH37; ORFNames=AD-019, CGI-70;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ACTIVITY REGULATION,
RP MUTAGENESIS OF CYS-88, AND INTERACTION WITH ADRM1.
RX PubMed=16906146; DOI=10.1038/ncb1460;
RA Yao T., Song L., Xu W., DeMartino G.N., Florens L., Swanson S.K.,
RA Washburn M.P., Conaway R.C., Conaway J.W., Cohen R.E.;
RT "Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme
RT by Adrm1.";
RL Nat. Cell Biol. 8:994-1002(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PHE-197.
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PHE-197.
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Lung, and Uterus;
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 [7]
RP INTERACTION WITH ADRM1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16990800; DOI=10.1038/sj.emboj.7601338;
RA Hamazaki J., Iemura S., Natsume T., Yashiroda H., Tanaka K., Murata S.;
RT "A novel proteasome-interacting protein recruits the deubiquitinating
RT enzyme UCH37 to 26S proteasomes.";
RL EMBO J. 25:4524-4536(2006).
RN [8]
RP INTERACTION WITH ADRM1, ACTIVITY REGULATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=17139257; DOI=10.1038/sj.emboj.7601450;
RA Qiu X.-B., Ouyang S.-Y., Li C.-J., Miao S., Wang L., Goldberg A.L.;
RT "hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the
RT deubiquitinating enzyme, UCH37.";
RL EMBO J. 25:5742-5753(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human 26S
RT proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION IN THE INO80
RP COMPLEX, INTERACTION WITH NFRKB AND ADRM1, AND ACTIVITY REGULATION.
RX PubMed=18922472; DOI=10.1016/j.molcel.2008.08.027;
RA Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P.,
RA Florens L., Conaway R.C., Cohen R.E., Conaway J.W.;
RT "Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the
RT proteasome and in the Ino80 chromatin-remodeling complex.";
RL Mol. Cell 31:909-917(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-158, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION IN THE INO80 COMPLEX.
RX PubMed=21303910; DOI=10.1074/jbc.m111.222505;
RA Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P.,
RA Conaway J.W., Conaway R.C.;
RT "Subunit organization of the human INO80 chromatin remodeling complex: An
RT evolutionarily conserved core complex catalyzes ATP-dependent nucleosome
RT remodeling.";
RL J. Biol. Chem. 286:11283-11289(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-228.
RX PubMed=19836345; DOI=10.1016/j.bbrc.2009.10.062;
RA Nishio K., Kim S.W., Kawai K., Mizushima T., Yamane T., Hamazaki J.,
RA Murata S., Tanaka K., Morimoto Y.;
RT "Crystal structure of the de-ubiquitinating enzyme UCH37 (human UCH-L5)
RT catalytic domain.";
RL Biochem. Biophys. Res. Commun. 390:855-860(2009).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 2-328.
RG Center for eukaryotic structural genomics (CESG);
RT "Crystal structure of UCH37.";
RL Submitted (AUG-2009) to the PDB data bank.
CC -!- FUNCTION: Protease that specifically cleaves 'Lys-48'-linked
CC polyubiquitin chains. Deubiquitinating enzyme associated with the 19S
CC regulatory subunit of the 26S proteasome. Putative regulatory component
CC of the INO80 complex; however is inactive in the INO80 complex and is
CC activated by a transient interaction of the INO80 complex with the
CC proteasome via ADRM1. {ECO:0000269|PubMed:16906146,
CC ECO:0000269|PubMed:18922472}.
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 -!- ACTIVITY REGULATION: Activated by ADRM1. Inhibited by interaction with
CC NFRKB. {ECO:0000269|PubMed:16906146, ECO:0000269|PubMed:17139257,
CC ECO:0000269|PubMed:18922472}.
CC -!- SUBUNIT: Component of the 19S (PA700) regulatory complex of the 26S
CC proteasome. Interacts with ADRM1 and NFRKB; in vitro ADRM1 and NFRKB
CC compete for interaction with UCHL5. Component of the INO80 complex;
CC specifically part of a complex module associated with N-terminus of
CC INO80. {ECO:0000269|PubMed:16906146, ECO:0000269|PubMed:16990800,
CC ECO:0000269|PubMed:17139257, ECO:0000269|PubMed:18922472,
CC ECO:0000269|PubMed:21303910}.
CC -!- INTERACTION:
CC Q9Y5K5; Q9H981: ACTR8; NbExp=3; IntAct=EBI-1051183, EBI-769597;
CC Q9Y5K5; Q16186: ADRM1; NbExp=21; IntAct=EBI-1051183, EBI-954387;
CC Q9Y5K5; Q8NBZ0: INO80E; NbExp=7; IntAct=EBI-1051183, EBI-769401;
CC Q9Y5K5; Q6P4R8: NFRKB; NbExp=12; IntAct=EBI-1051183, EBI-2511210;
CC Q9Y5K5; P60900: PSMA6; NbExp=4; IntAct=EBI-1051183, EBI-357793;
CC Q9Y5K5; Q13200: PSMD2; NbExp=5; IntAct=EBI-1051183, EBI-357648;
CC Q9Y5K5; P55036: PSMD4; NbExp=5; IntAct=EBI-1051183, EBI-359318;
CC Q9Y5K5; P0C1Z6: TFPT; NbExp=3; IntAct=EBI-1051183, EBI-1245626;
CC Q9Y5K5; O96006: ZBED1; NbExp=3; IntAct=EBI-1051183, EBI-740037;
CC Q9Y5K5-3; Q16186: ADRM1; NbExp=5; IntAct=EBI-11749875, EBI-954387;
CC Q9Y5K5-3; Q6P4R8: NFRKB; NbExp=3; IntAct=EBI-11749875, EBI-2511210;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18922472}. Nucleus
CC {ECO:0000269|PubMed:18922472}. Note=Associates with the proteasome 19S
CC subunit in the cytoplasm. Associates with the INO80 complex in the
CC nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q9Y5K5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y5K5-2; Sequence=VSP_005253, VSP_005254;
CC Name=3;
CC IsoId=Q9Y5K5-3; Sequence=VSP_005253;
CC Name=4;
CC IsoId=Q9Y5K5-4; Sequence=VSP_005253, VSP_017062;
CC -!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
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DR EMBL; AF147717; AAD31528.1; -; mRNA.
DR EMBL; AF151828; AAD34065.1; -; mRNA.
DR EMBL; AF157320; AAF67486.1; -; mRNA.
DR EMBL; BT006790; AAP35436.1; -; mRNA.
DR EMBL; AL136370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015521; AAH15521.1; -; mRNA.
DR EMBL; BC025369; AAH25369.1; -; mRNA.
DR CCDS; CCDS1378.1; -. [Q9Y5K5-1]
DR CCDS; CCDS55668.1; -. [Q9Y5K5-3]
DR CCDS; CCDS55669.1; -. [Q9Y5K5-2]
DR CCDS; CCDS55670.1; -. [Q9Y5K5-4]
DR RefSeq; NP_001186190.1; NM_001199261.1. [Q9Y5K5-3]
DR RefSeq; NP_001186191.1; NM_001199262.1. [Q9Y5K5-4]
DR RefSeq; NP_001186192.1; NM_001199263.1. [Q9Y5K5-2]
DR RefSeq; NP_057068.1; NM_015984.3. [Q9Y5K5-1]
DR PDB; 3A7S; X-ray; 2.20 A; A=1-228.
DR PDB; 3IHR; X-ray; 2.95 A; A=1-329.
DR PDB; 3RII; X-ray; 2.00 A; A/B=1-228.
DR PDB; 3RIS; X-ray; 2.40 A; A/B/C/D=1-240.
DR PDB; 3TB3; X-ray; 2.30 A; A/B=1-227.
DR PDB; 4UEL; X-ray; 2.30 A; A=1-329.
DR PDB; 4UEM; X-ray; 2.82 A; A=1-329.
DR PDB; 4UF5; X-ray; 3.70 A; A=1-329.
DR PDB; 4UF6; X-ray; 3.69 A; A/D/G/J=1-329.
DR PDB; 4WLP; X-ray; 3.10 A; A=5-322.
DR PDBsum; 3A7S; -.
DR PDBsum; 3IHR; -.
DR PDBsum; 3RII; -.
DR PDBsum; 3RIS; -.
DR PDBsum; 3TB3; -.
DR PDBsum; 4UEL; -.
DR PDBsum; 4UEM; -.
DR PDBsum; 4UF5; -.
DR PDBsum; 4UF6; -.
DR PDBsum; 4WLP; -.
DR AlphaFoldDB; Q9Y5K5; -.
DR SMR; Q9Y5K5; -.
DR BioGRID; 119509; 255.
DR ComplexPortal; CPX-846; INO80 chromatin remodeling complex.
DR DIP; DIP-42671N; -.
DR IntAct; Q9Y5K5; 79.
DR MINT; Q9Y5K5; -.
DR STRING; 9606.ENSP00000356425; -.
DR BindingDB; Q9Y5K5; -.
DR ChEMBL; CHEMBL3407316; -.
DR MEROPS; C12.005; -.
DR iPTMnet; Q9Y5K5; -.
DR MetOSite; Q9Y5K5; -.
DR PhosphoSitePlus; Q9Y5K5; -.
DR SwissPalm; Q9Y5K5; -.
DR BioMuta; UCHL5; -.
DR DMDM; 108936023; -.
DR EPD; Q9Y5K5; -.
DR jPOST; Q9Y5K5; -.
DR MassIVE; Q9Y5K5; -.
DR MaxQB; Q9Y5K5; -.
DR PaxDb; Q9Y5K5; -.
DR PeptideAtlas; Q9Y5K5; -.
DR PRIDE; Q9Y5K5; -.
DR ProteomicsDB; 86430; -. [Q9Y5K5-1]
DR ProteomicsDB; 86431; -. [Q9Y5K5-2]
DR ProteomicsDB; 86432; -. [Q9Y5K5-3]
DR ProteomicsDB; 86433; -. [Q9Y5K5-4]
DR Antibodypedia; 1573; 333 antibodies from 30 providers.
DR DNASU; 51377; -.
DR Ensembl; ENST00000367448.5; ENSP00000356418.1; ENSG00000116750.14. [Q9Y5K5-4]
DR Ensembl; ENST00000367449.5; ENSP00000356419.1; ENSG00000116750.14. [Q9Y5K5-2]
DR Ensembl; ENST00000367454.6; ENSP00000356424.1; ENSG00000116750.14. [Q9Y5K5-3]
DR Ensembl; ENST00000367455.8; ENSP00000356425.3; ENSG00000116750.14. [Q9Y5K5-1]
DR GeneID; 51377; -.
DR KEGG; hsa:51377; -.
DR MANE-Select; ENST00000367454.6; ENSP00000356424.1; NM_001199261.3; NP_001186190.1. [Q9Y5K5-3]
DR UCSC; uc001gsm.4; human. [Q9Y5K5-1]
DR CTD; 51377; -.
DR DisGeNET; 51377; -.
DR GeneCards; UCHL5; -.
DR HGNC; HGNC:19678; UCHL5.
DR HPA; ENSG00000116750; Low tissue specificity.
DR MIM; 610667; gene.
DR neXtProt; NX_Q9Y5K5; -.
DR OpenTargets; ENSG00000116750; -.
DR PharmGKB; PA134916228; -.
DR VEuPathDB; HostDB:ENSG00000116750; -.
DR eggNOG; KOG2778; Eukaryota.
DR GeneTree; ENSGT00940000155195; -.
DR HOGENOM; CLU_018316_0_0_1; -.
DR InParanoid; Q9Y5K5; -.
DR OMA; DGAGNWC; -.
DR OrthoDB; 1363547at2759; -.
DR PhylomeDB; Q9Y5K5; -.
DR TreeFam; TF313976; -.
DR BRENDA; 3.4.19.12; 2681.
DR PathwayCommons; Q9Y5K5; -.
DR Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR SignaLink; Q9Y5K5; -.
DR SIGNOR; Q9Y5K5; -.
DR BioGRID-ORCS; 51377; 206 hits in 1106 CRISPR screens.
DR ChiTaRS; UCHL5; human.
DR EvolutionaryTrace; Q9Y5K5; -.
DR GeneWiki; Ubiquitin_carboxyl-terminal_hydrolase_L5; -.
DR GenomeRNAi; 51377; -.
DR Pharos; Q9Y5K5; Tbio.
DR PRO; PR:Q9Y5K5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y5K5; protein.
DR Bgee; ENSG00000116750; Expressed in cortical plate and 188 other tissues.
DR ExpressionAtlas; Q9Y5K5; baseline and differential.
DR Genevisible; Q9Y5K5; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031597; C:cytosolic proteasome complex; IEA:Ensembl.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IMP:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0048853; P:forebrain morphogenesis; IEA:Ensembl.
DR GO; GO:0021670; P:lateral ventricle development; IEA:Ensembl.
DR GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; IEA:Ensembl.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0033044; P:regulation of chromosome organization; IMP:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:0060382; P:regulation of DNA strand elongation; IMP:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02255; Peptidase_C12; 1.
DR Gene3D; 3.40.532.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR InterPro; IPR017390; Ubiquitinyl_hydrolase_UCH37.
DR InterPro; IPR033837; UCH37.
DR InterPro; IPR041507; UCH_C.
DR PANTHER; PTHR10589; PTHR10589; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR Pfam; PF18031; UCH_C; 1.
DR PIRSF; PIRSF038120; Ubiquitinyl_hydrolase_UCH37; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; Hydrolase; Nucleus; Protease; Proteasome;
KW Reference proteome; Thiol protease; Transcription;
KW Transcription regulation; Ubl conjugation pathway.
FT CHAIN 1..329
FT /note="Ubiquitin carboxyl-terminal hydrolase isozyme L5"
FT /id="PRO_0000211066"
FT REGION 313..329
FT /note="Interaction with ADRM1"
FT ACT_SITE 88
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 164
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT SITE 179
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250"
FT MOD_RES 47
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUP7"
FT MOD_RES 158
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 289
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUP7"
FT VAR_SEQ 246
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10810093,
FT ECO:0000303|PubMed:10931946, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.4"
FT /id="VSP_005253"
FT VAR_SEQ 316..329
FT /note="AKEKQNAKKAQETK -> GK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10810093,
FT ECO:0000303|PubMed:10931946"
FT /id="VSP_005254"
FT VAR_SEQ 316..329
FT /note="AKEKQNAKKAQETK -> FEKHFEKTLLGK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017062"
FT VARIANT 197
FT /note="I -> F"
FT /evidence="ECO:0000269|PubMed:10810093,
FT ECO:0000269|PubMed:10931946"
FT /id="VAR_011613"
FT MUTAGEN 88
FT /note="C->A: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:16906146"
FT CONFLICT 6
FT /note="G -> V (in Ref. 2; AAD34065)"
FT /evidence="ECO:0000305"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:3RII"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:3RII"
FT TURN 40..46
FT /evidence="ECO:0007829|PDB:3RII"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:3RII"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3RII"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:3RII"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3RII"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:3RII"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:3RII"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:3RII"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:3RII"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:3RII"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:3RII"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:3RII"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3RII"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:3RII"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3RII"
FT HELIX 197..213
FT /evidence="ECO:0007829|PDB:3RII"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:3RII"
FT HELIX 227..244
FT /evidence="ECO:0007829|PDB:4UEL"
FT HELIX 255..289
FT /evidence="ECO:0007829|PDB:4UEL"
FT HELIX 293..305
FT /evidence="ECO:0007829|PDB:4UEL"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:4UEL"
SQ SEQUENCE 329 AA; 37607 MW; DF307347D48C9D0F CRC64;
MTGNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ENFEKLKPVH GLIFLFKWQP
GEEPAGSVVQ DSRLDTIFFA KQVINNACAT QAIVSVLLNC THQDVHLGET LSEFKEFSQS
FDAAMKGLAL SNSDVIRQVH NSFARQQMFE FDTKTSAKEE DAFHFVSYVP VNGRLYELDG
LREGPIDLGA CNQDDWISAV RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR
QLAEEEPMDT DQGNSMLSAI QSEVAKNQML IEEEVQKLKR YKIENIRRKH NYLPFIMELL
KTLAEHQQLI PLVEKAKEKQ NAKKAQETK
