ID UBP20_HUMAN Reviewed; 914 AA.
AC Q9Y2K6; Q541F1; Q8IXQ1; Q96LG5; Q9UQN8; Q9UQP0;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 27-MAR-2024, entry version 203.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 20;
DE EC=3.4.19.12 {ECO:0000269|PubMed:26839314, ECO:0000269|PubMed:27801882, ECO:0000269|PubMed:29487085, ECO:0000269|PubMed:32354117, ECO:0000269|PubMed:35063767};
DE AltName: Full=Deubiquitinating enzyme 20;
DE AltName: Full=Ubiquitin thioesterase 20;
DE AltName: Full=Ubiquitin-specific-processing protease 20;
DE AltName: Full=VHL-interacting deubiquitinating enzyme 2;
DE Short=hVDU2;
GN Name=USP20; Synonyms=KIAA1003, LSFR3A, VDU2;
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], FUNCTION, UBIQUITINATION, AND INTERACTION WITH
RP VHL.
RX PubMed=12056827; DOI=10.1016/s0006-291x(02)00534-x;
RA Li Z., Wang D., Na X., Schoen S.R., Messing E.M., Wu G.;
RT "Identification of a deubiquitinating enzyme subfamily as substrates of the
RT von Hippel-Lindau tumor suppressor.";
RL Biochem. Biophys. Res. Commun. 294:700-709(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 581-803 AND 839-914.
RX PubMed=10369878; DOI=10.1093/hmg/8.7.1313;
RA Gilley J., Fried M.;
RT "Extensive gene order differences within regions of conserved synteny
RT between the Fugu and human genomes: implications for chromosomal evolution
RT and the cloning of disease genes.";
RL Hum. Mol. Genet. 8:1313-1320(1999).
RN [7]
RP FUNCTION, INTERACTION WITH DIO2, AND SUBCELLULAR LOCATION.
RX PubMed=12865408; DOI=10.1172/jci18348;
RA Curcio-Morelli C., Zavacki A.M., Christofollete M., Gereben B.,
RA de Freitas B.C., Harney J.W., Li Z., Wu G., Bianco A.C.;
RT "Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau
RT protein-interacting deubiquitinating enzymes regulates thyroid hormone
RT activation.";
RL J. Clin. Invest. 112:189-196(2003).
RN [8]
RP FUNCTION, AND INTERACTION WITH HIF1A.
RX PubMed=15776016; DOI=10.1038/sj.embor.7400377;
RA Li Z., Wang D., Messing E.M., Wu G.;
RT "VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and
RT stabilizes HIF-1alpha.";
RL EMBO Rep. 6:373-378(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-134, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-377 AND SER-413, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP FUNCTION, INTERACTION WITH ADRB2, AND MUTAGENESIS OF CYS-154 AND HIS-643.
RX PubMed=19424180; DOI=10.1038/emboj.2009.128;
RA Berthouze M., Venkataramanan V., Li Y., Shenoy S.K.;
RT "The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic receptor
RT recycling and resensitization.";
RL EMBO J. 28:1684-1696(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-134, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP INTERACTION WITH ADRB2.
RX PubMed=23166351; DOI=10.1083/jcb.201208192;
RA Han S.O., Xiao K., Kim J., Wu J.H., Wisler J.W., Nakamura N.,
RA Freedman N.J., Shenoy S.K.;
RT "MARCH2 promotes endocytosis and lysosomal sorting of carvedilol-bound
RT beta(2)-adrenergic receptors.";
RL J. Cell Biol. 199:817-830(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-132; SER-134;
RP SER-305; THR-377; SER-408 AND SER-413, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CCP110.
RX PubMed=23486064; DOI=10.1038/nature11941;
RA Li J., D'Angiolella V., Seeley E.S., Kim S., Kobayashi T., Fu W.,
RA Campos E.I., Pagano M., Dynlacht B.D.;
RT "USP33 regulates centrosome biogenesis via deubiquitination of the
RT centriolar protein CP110.";
RL Nature 495:255-259(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-134, AND
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 [18]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26839314; DOI=10.1074/jbc.m115.687129;
RA Jean-Charles P.Y., Zhang L., Wu J.H., Han S.O., Brian L., Freedman N.J.,
RA Shenoy S.K.;
RT "Ubiquitin-specific Protease 20 Regulates the Reciprocal Functions of beta-
RT Arrestin2 in Toll-like Receptor 4-promoted Nuclear Factor kappaB (NFkappaB)
RT Activation.";
RL J. Biol. Chem. 291:7450-7464(2016).
RN [19]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH USP18.
RX PubMed=27801882; DOI=10.1038/cr.2016.125;
RA Zhang M., Zhang M.X., Zhang Q., Zhu G.F., Yuan L., Zhang D.E., Zhu Q.,
RA Yao J., Shu H.B., Zhong B.;
RT "USP18 recruits USP20 to promote innate antiviral response through
RT deubiquitinating STING/MITA.";
RL Cell Res. 26:1302-1319(2016).
RN [20]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-154 AND HIS-643.
RX PubMed=29487085; DOI=10.15252/embr.201744378;
RA Kim J.H., Seo D., Kim S.J., Choi D.W., Park J.S., Ha J., Choi J., Lee J.H.,
RA Jung S.M., Seo K.W., Lee E.W., Lee Y.S., Cheong H., Choi C.Y., Park S.H.;
RT "The deubiquitinating enzyme USP20 stabilizes ULK1 and promotes autophagy
RT initiation.";
RL EMBO Rep. 19:0-0(2018).
RN [21]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32354117; DOI=10.3390/ijms21093116;
RA Ha J., Kim M., Seo D., Park J.S., Lee J., Lee J., Park S.H.;
RT "The Deubiquitinating Enzyme USP20 Regulates the TNFalpha-Induced NF-kappaB
RT Signaling Pathway through Stabilization of p62.";
RL Int. J. Mol. Sci. 21:0-0(2020).
RN [22]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=33792613; DOI=10.1083/jcb.202004086;
RA Culver J.A., Mariappan M.;
RT "Deubiquitinases USP20/33 promote the biogenesis of tail-anchored membrane
RT proteins.";
RL J. Cell Biol. 220:0-0(2021).
RN [23]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-154.
RX PubMed=35063767; DOI=10.1016/j.bbrc.2022.01.019;
RA Feng J., Liu P., Li X., Zhang D., Lin H., Hou Z., Guo C., Niu Y., Dai B.,
RA Wang O., Qi M., Wang H., Zhou H.;
RT "The deubiquitinating enzyme USP20 regulates the stability of the MCL1
RT protein.";
RL Biochem. Biophys. Res. Commun. 593:122-128(2022).
CC -!- FUNCTION: Deubiquitinating enzyme that plays a role in many cellular
CC processes including autophagy, cellular antiviral response or membrane
CC protein biogenesis (PubMed:27801882, PubMed:29487085). Attenuates TLR4-
CC mediated NF-kappa-B signaling by cooperating with beta-arrestin-2/ARRB2
CC and inhibiting TRAF6 autoubiquitination (PubMed:26839314). Promotes
CC cellular antiviral responses by deconjugating 'Lys-33' and 'Lys-48'-
CC linked ubiquitination of STING1 leading to its stabilization
CC (PubMed:27801882). Plays an essential role in autophagy induction by
CC regulating the ULK1 stability through deubiquitination of ULK1
CC (PubMed:29487085). Acts as a positive regulator for NF-kappa-B
CC activation by TNF-alpha through deubiquitinating 'Lys-48'-linked
CC polyubiquitination of SQSTM1, leading to its increased stability
CC (PubMed:32354117). Acts as a regulator of G-protein coupled receptor
CC (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic
CC receptor (ADRB2)(PubMed:19424180). Plays a central role in ADRB2
CC recycling and resensitization after prolonged agonist stimulation by
CC constitutively binding ADRB2, mediating deubiquitination of ADRB2 and
CC inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is
CC probably transferred to the translocated beta-arrestins, possibly
CC leading to beta-arrestins deubiquitination and disengagement from ADRB2
CC (PubMed:19424180). This suggests the existence of a dynamic exchange
CC between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby
CC regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading
CC to stabilize HIF1A and enhance HIF1A-mediated activity
CC (PubMed:15776016). Deubiquitinates MCL1, a pivotal member of the anti-
CC apoptotic Bcl-2 protein family to regulate its stability
CC (PubMed:35063767). Within the endoplasmic reticulum, participates with
CC USP33 in the rescue of post-translationally targeted membrane proteins
CC that are inappropriately ubiquitinated by the cytosolic protein quality
CC control in the cytosol (PubMed:33792613). {ECO:0000269|PubMed:12056827,
CC ECO:0000269|PubMed:12865408, ECO:0000269|PubMed:15776016,
CC ECO:0000269|PubMed:19424180, ECO:0000269|PubMed:26839314,
CC ECO:0000269|PubMed:27801882, ECO:0000269|PubMed:29487085,
CC ECO:0000269|PubMed:32354117, ECO:0000269|PubMed:33792613,
CC ECO:0000269|PubMed:35063767}.
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:26839314,
CC ECO:0000269|PubMed:27801882, ECO:0000269|PubMed:29487085,
CC ECO:0000269|PubMed:32354117, ECO:0000269|PubMed:35063767};
CC -!- SUBUNIT: Interacts with VHL, leading to its ubiquitination and
CC subsequent degradation (PubMed:12056827). Interacts with CCP110
CC (PubMed:23486064). Interacts with DIO2 (PubMed:12865408). Interacts
CC with HIF1A (PubMed:15776016). Interacts with ADRB2 (PubMed:19424180,
CC PubMed:23166351). Interacts with USP18 (PubMed:27801882).
CC {ECO:0000269|PubMed:12056827, ECO:0000269|PubMed:12865408,
CC ECO:0000269|PubMed:15776016, ECO:0000269|PubMed:19424180,
CC ECO:0000269|PubMed:23166351, ECO:0000269|PubMed:23486064,
CC ECO:0000269|PubMed:27801882}.
CC -!- INTERACTION:
CC Q9Y2K6; P13196: ALAS1; NbExp=3; IntAct=EBI-2511991, EBI-3905054;
CC Q9Y2K6; Q7L4P6: BEND5; NbExp=3; IntAct=EBI-2511991, EBI-724373;
CC Q9Y2K6; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-2511991, EBI-10181188;
CC Q9Y2K6; Q969F0: FATE1; NbExp=3; IntAct=EBI-2511991, EBI-743099;
CC Q9Y2K6; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-2511991, EBI-8638439;
CC Q9Y2K6; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-2511991, EBI-10178634;
CC Q9Y2K6; Q99750: MDFI; NbExp=3; IntAct=EBI-2511991, EBI-724076;
CC Q9Y2K6; O43597: SPRY2; NbExp=3; IntAct=EBI-2511991, EBI-742487;
CC Q9Y2K6; P36406: TRIM23; NbExp=3; IntAct=EBI-2511991, EBI-740098;
CC Q9Y2K6; O95292: VAPB; NbExp=3; IntAct=EBI-2511991, EBI-1188298;
CC Q9Y2K6; Q53XM7: VAPB; NbExp=3; IntAct=EBI-2511991, EBI-10178947;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8C6M1}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:12865408,
CC ECO:0000269|PubMed:33792613}. Cytoplasm, perinuclear region
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000269|PubMed:23486064}.
CC -!- DOMAIN: The UBP-type zinc finger binds 3 zinc ions. However, it does
CC not bind ubiquitin, probably because the conserved Arg in position 55
CC is replaced by a Glu residue (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated via a VHL-dependent pathway for proteasomal
CC degradation. {ECO:0000269|PubMed:12056827}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76847.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY074877; AAL79676.1; -; mRNA.
DR EMBL; AB023220; BAA76847.2; ALT_INIT; mRNA.
DR EMBL; AL158207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87914.1; -; Genomic_DNA.
DR EMBL; BC039593; AAH39593.1; -; mRNA.
DR EMBL; Y17457; CAB44350.1; -; Genomic_DNA.
DR EMBL; Y17459; CAB44352.1; -; Genomic_DNA.
DR CCDS; CCDS43892.1; -.
DR RefSeq; NP_001008563.2; NM_001008563.4.
DR RefSeq; NP_001103773.2; NM_001110303.3.
DR RefSeq; NP_006667.3; NM_006676.7.
DR RefSeq; XP_005251722.1; XM_005251665.3.
DR RefSeq; XP_011516463.1; XM_011518161.2.
DR RefSeq; XP_011516464.1; XM_011518162.2.
DR PDB; 6KCZ; NMR; -; A=1-99.
DR PDBsum; 6KCZ; -.
DR AlphaFoldDB; Q9Y2K6; -.
DR SMR; Q9Y2K6; -.
DR BioGRID; 116077; 146.
DR IntAct; Q9Y2K6; 56.
DR MINT; Q9Y2K6; -.
DR STRING; 9606.ENSP00000313811; -.
DR BindingDB; Q9Y2K6; -.
DR ChEMBL; CHEMBL3232682; -.
DR MEROPS; C19.025; -.
DR iPTMnet; Q9Y2K6; -.
DR PhosphoSitePlus; Q9Y2K6; -.
DR SwissPalm; Q9Y2K6; -.
DR BioMuta; USP20; -.
DR DMDM; 116242837; -.
DR EPD; Q9Y2K6; -.
DR jPOST; Q9Y2K6; -.
DR MassIVE; Q9Y2K6; -.
DR MaxQB; Q9Y2K6; -.
DR PaxDb; 9606-ENSP00000313811; -.
DR PeptideAtlas; Q9Y2K6; -.
DR ProteomicsDB; 85826; -.
DR Pumba; Q9Y2K6; -.
DR Antibodypedia; 1730; 350 antibodies from 32 providers.
DR DNASU; 10868; -.
DR Ensembl; ENST00000315480.9; ENSP00000313811.4; ENSG00000136878.14.
DR Ensembl; ENST00000358355.5; ENSP00000351122.1; ENSG00000136878.14.
DR Ensembl; ENST00000372429.8; ENSP00000361506.3; ENSG00000136878.14.
DR GeneID; 10868; -.
DR KEGG; hsa:10868; -.
DR MANE-Select; ENST00000372429.8; ENSP00000361506.3; NM_001110303.4; NP_001103773.2.
DR UCSC; uc004byr.4; human.
DR AGR; HGNC:12619; -.
DR CTD; 10868; -.
DR DisGeNET; 10868; -.
DR GeneCards; USP20; -.
DR HGNC; HGNC:12619; USP20.
DR HPA; ENSG00000136878; Low tissue specificity.
DR MIM; 615143; gene.
DR neXtProt; NX_Q9Y2K6; -.
DR OpenTargets; ENSG00000136878; -.
DR PharmGKB; PA37245; -.
DR VEuPathDB; HostDB:ENSG00000136878; -.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000158829; -.
DR HOGENOM; CLU_004896_0_0_1; -.
DR InParanoid; Q9Y2K6; -.
DR OMA; IDQDDEC; -.
DR OrthoDB; 227085at2759; -.
DR PhylomeDB; Q9Y2K6; -.
DR TreeFam; TF352179; -.
DR PathwayCommons; Q9Y2K6; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; Q9Y2K6; -.
DR SIGNOR; Q9Y2K6; -.
DR BioGRID-ORCS; 10868; 11 hits in 1195 CRISPR screens.
DR ChiTaRS; USP20; human.
DR GeneWiki; USP20; -.
DR GenomeRNAi; 10868; -.
DR Pharos; Q9Y2K6; Tbio.
DR PRO; PR:Q9Y2K6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9Y2K6; Protein.
DR Bgee; ENSG00000136878; Expressed in granulocyte and 145 other cell types or tissues.
DR Genevisible; Q9Y2K6; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IC:UniProt.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0140374; P:antiviral innate immune response; IDA:UniProt.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IDA:UniProt.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:UniProt.
DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
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 PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF13; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 20; 1.
DR Pfam; PF06337; DUSP; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00695; DUSP; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51283; DUSP; 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 3D-structure; Cytoplasm; Cytoskeleton; Endocytosis; Endoplasmic reticulum;
KW Hydrolase; Metal-binding; Phosphoprotein; Protease; Reference proteome;
KW Repeat; Thiol protease; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..914
FT /note="Ubiquitin carboxyl-terminal hydrolase 20"
FT /id="PRO_0000080647"
FT DOMAIN 145..685
FT /note="USP"
FT DOMAIN 687..780
FT /note="DUSP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 789..892
FT /note="DUSP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT ZN_FING 6..111
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 257..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /note="Nucleophile"
FT ACT_SITE 643
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 258
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C6M1"
FT MOD_RES 377
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 103
FT /note="S -> Y (in dbSNP:rs36086252)"
FT /id="VAR_051529"
FT VARIANT 444
FT /note="V -> I (in dbSNP:rs36055332)"
FT /id="VAR_051530"
FT MUTAGEN 154
FT /note="C->S: Abolishes deubiquitinating activity. Does not
FT inhibit lysosomal trafficking of ADRB2; when associated
FT with Q-643."
FT /evidence="ECO:0000269|PubMed:19424180,
FT ECO:0000269|PubMed:29487085, ECO:0000269|PubMed:35063767"
FT MUTAGEN 643
FT /note="H->Q: Abolishes deubiquitinating activity. Does not
FT inhibit lysosomal trafficking of ADRB2; when associated
FT with S-154."
FT /evidence="ECO:0000269|PubMed:19424180,
FT ECO:0000269|PubMed:29487085"
FT CONFLICT 320
FT /note="A -> V (in Ref. 1; AAL79676 and 2; BAA76847)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="Missing (in Ref. 1; AAL79676, 2; BAA76847, 4;
FT EAW87914 and 5; AAH39593)"
FT /evidence="ECO:0000305"
FT CONFLICT 776
FT /note="H -> Q (in Ref. 6; CAB44350)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="R -> M (in Ref. 6; CAB44350)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:6KCZ"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:6KCZ"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:6KCZ"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:6KCZ"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6KCZ"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:6KCZ"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:6KCZ"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6KCZ"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:6KCZ"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6KCZ"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:6KCZ"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6KCZ"
SQ SEQUENCE 914 AA; 102003 MW; DC094570A396D20E CRC64;
MGDSRDLCPH LDSIGEVTKE DLLLKSKGTC QSCGVTGPNL WACLQVACPY VGCGESFADH
STIHAQAKKH NLTVNLTTFR LWCYACEKEV FLEQRLAAPL LGSSSKFSEQ DSPPPSHPLK
AVPIAVADEG ESESEDDDLK PRGLTGMKNL GNSCYMNAAL QALSNCPPLT QFFLECGGLV
RTDKKPALCK SYQKLVSEVW HKKRPSYVVP TSLSHGIKLV NPMFRGYAQQ DTQEFLRCLM
DQLHEELKEP VVATVALTEA RDSDSSDTDE KREGDRSPSE DEFLSCDSSS DRGEGDGQGR
GGGSSQAETE LLIPDEAGRA ISEKERMKDR KFSWGQQRTN SEQVDEDADV DTAMAALDDQ
PAEAQPPSPR SSSPCRTPEP DNDAHLRSSS RPCSPVHHHE GHAKLSSSPP RASPVRMAPS
YVLKKAQVLS AGSRRRKEQR YRSVISDIFD GSILSLVQCL TCDRVSTTVE TFQDLSLPIP
GKEDLAKLHS AIYQNVPAKP GACGDSYAAQ GWLAFIVEYI RRFVVSCTPS WFWGPVVTLE
DCLAAFFAAD ELKGDNMYSC ERCKKLRNGV KYCKVLRLPE ILCIHLKRFR HEVMYSFKIN
SHVSFPLEGL DLRPFLAKEC TSQITTYDLL SVICHHGTAG SGHYIAYCQN VINGQWYEFD
DQYVTEVHET VVQNAEGYVL FYRKSSEEAM RERQQVVSLA AMREPSLLRF YVSREWLNKF
NTFAEPGPIT NQTFLCSHGG IPPHKYHYID DLVVILPQNV WEHLYNRFGG GPAVNHLYVC
SICQVEIEAL AKRRRIEIDT FIKLNKAFQA EESPGVIYCI SMQWFREWEA FVKGKDNEPP
GPIDNSRIAQ VKGSGHVQLK QGADYGQISE ETWTYLNSLY GGGPEIAIRQ SVAQPLGPEN
LHGEQKIEAE TRAV
//
