ID H0YMI4_HUMAN Unreviewed; 503 AA. AC H0YMI4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 16-JAN-2019, entry version 61. DE RecName: Full=Ubiquitinyl hydrolase 1 {ECO:0000256|SAAS:SAAS01044305}; DE EC=3.4.19.12 {ECO:0000256|SAAS:SAAS01044305}; GN Name=USP3 {ECO:0000313|Ensembl:ENSP00000453619}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000453619, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000453619, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., RA Sneddon K.M., Stewart S., Sougnez C., Stone S.M., Topham K., RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., RA Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human RT chromosome 15."; RL Nature 440:671-675(2006). RN [2] {ECO:0000313|Ensembl:ENSP00000453619} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, CC peptide and isopeptide bonds formed by the C-terminal Gly of CC ubiquitin (a 76-residue protein attached to proteins as an CC intracellular targeting signal).; EC=3.4.19.12; CC Evidence={ECO:0000256|SAAS:SAAS01117307}; CC -!- SIMILARITY: Belongs to the peptidase C19 family. CC {ECO:0000256|SAAS:SAAS01045498}. 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; AC007950; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC118274; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H0YMI4; -. DR EPD; H0YMI4; -. DR jPOST; H0YMI4; -. DR MaxQB; H0YMI4; -. DR PeptideAtlas; H0YMI4; -. DR PRIDE; H0YMI4; -. DR Ensembl; ENST00000558285; ENSP00000453619; ENSG00000140455. DR UCSC; uc010bgs.5; human. DR EuPathDB; HostDB:ENSG00000140455.16; -. DR HGNC; HGNC:12626; USP3. DR OpenTargets; ENSG00000140455; -. DR eggNOG; KOG1867; Eukaryota. DR eggNOG; ENOG410XQQ0; LUCA. DR GeneTree; ENSGT00940000157850; -. DR ChiTaRS; USP3; human. DR Proteomes; UP000005640; Chromosome 15. DR Bgee; ENSG00000140455; Expressed in 219 organ(s), highest expression level in blood. DR ExpressionAtlas; H0YMI4; baseline and differential. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA. DR GO; GO:0090543; C:Flemming body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro. 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; IPR018200; USP_CS. DR InterPro; IPR028889; USP_dom. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR001607; Znf_UBP. DR Pfam; PF00443; UCH; 1. DR Pfam; PF02148; zf-UBP; 1. DR SMART; SM00290; ZnF_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 Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Hydrolase {ECO:0000256|SAAS:SAAS01044269}; KW Metal-binding {ECO:0000256|SAAS:SAAS01044352}; KW Protease {ECO:0000256|SAAS:SAAS01044269}; KW Proteomics identification {ECO:0000213|EPD:H0YMI4, KW ECO:0000213|MaxQB:H0YMI4, ECO:0000213|PeptideAtlas:H0YMI4}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Thiol protease {ECO:0000256|SAAS:SAAS01044269}; KW Ubl conjugation pathway {ECO:0000256|SAAS:SAAS01044331}; KW Zinc {ECO:0000256|SAAS:SAAS01044352}; KW Zinc-finger {ECO:0000256|SAAS:SAAS01044352}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 503 Ubiquitinyl hydrolase 1. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003546754. FT DOMAIN 5 87 UBP-type. {ECO:0000259|PROSITE:PS50271}. FT DOMAIN 142 494 USP. {ECO:0000259|PROSITE:PS50235}. FT ZN_FING 5 87 UBP-type. {ECO:0000256|PROSITE- FT ProRule:PRU00502}. SQ SEQUENCE 503 AA; 57423 MW; 34D6253FDE1511EC CRC64; MMQLVYCVFF FLLVCRSNKS PWVCLTCSSV HCGRYVNGHA KKHYEDAQVP LTNHKKSEKQ DKVQHTVCMD CSSYSTYCYR CDDFVVNDTK LGLVQKVREH LQNLENSAFT ADRHKKRKLL ENSTLNSKLL KVNGSTTAIC ATGLRNLGNT CFMNAILQSL SNIEQFCCYF KELPAVELRN GKTAGRRTYH TRSQGDNNVS LVEEFRKTLC ALWQGSQTAF SPESLFYVVW KIMPNFRGYQ QQDAHEFMRY LLDHLHLELQ GGFNGVSRSA ILQENSTLSA SNKCCINGAS TVVTAIFGGI LQNEVNCLIC GTESRKFDPF LDLSLDIPSQ FRSKRSKNQE NGPVCSLRDC LRSFTDLEEL DETELYMCHK CKKKQKSTKK FWIQKLPKVL CLHLKRFHWT AYLRNKVDTY VEFPLRGLDM KCYLLEPENS GPESCLYDLA AVVVHHGSGV GSGHYTAYAT HEGRWFHFND STVTLTDEET VVKAKAYILF YVEHQAKAGS DKL //