UBP21_HUMAN
ID UBP21_HUMAN Reviewed; 565 AA.
AC Q9UK80; Q59H60; Q5BKT5; Q5VTW9; Q5VTX0; Q9BTV1; Q9HBS2; Q9NYN4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 21;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 21;
DE AltName: Full=Ubiquitin thioesterase 21;
DE AltName: Full=Ubiquitin-specific-processing protease 21;
GN Name=USP21; Synonyms=USP23; ORFNames=PP1490;
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).
RX PubMed=10786635; DOI=10.1016/s0167-4781(99)00233-x;
RA Smith T.S., Southan C.;
RT "Sequencing, tissue distribution and chromosomal assignment of a novel
RT ubiquitin-specific protease USP23.";
RL Biochim. Biophys. Acta 1490:184-188(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF CYS-221.
RC TISSUE=Placenta;
RX PubMed=10799498; DOI=10.1074/jbc.275.19.14212;
RA Gong L., Kamitani T., Millas S., Yeh E.T.H.;
RT "Identification of a novel isopeptidase with dual specificity for
RT ubiquitin- and NEDD8-conjugated proteins.";
RL J. Biol. Chem. 275:14212-14216(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, Lung, and Testis;
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 [9]
RP SUBCELLULAR LOCATION, AND NUCLEAR EXPORT SIGNAL.
RX PubMed=21888622; DOI=10.1042/bj20111300;
RA Garcia-Santisteban I., Banuelos S., Rodriguez J.A.;
RT "A global survey of CRM1-dependent nuclear export sequences in the human
RT deubiquitinase family.";
RL Biochem. J. 441:209-217(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [11]
RP FUNCTION, AND INTERACTION WITH BEND3 AND BAZ2A.
RX PubMed=26100909; DOI=10.1073/pnas.1424705112;
RA Khan A., Giri S., Wang Y., Chakraborty A., Ghosh A.K., Anantharaman A.,
RA Aggarwal V., Sathyan K.M., Ha T., Prasanth K.V., Prasanth S.G.;
RT "BEND3 represses rDNA transcription by stabilizing a NoRC component via
RT USP21 deubiquitinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:8338-8343(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-75 IN COMPLEX WITH USP21.
RX PubMed=21399617; DOI=10.1038/embor.2011.17;
RA Ye Y., Akutsu M., Reyes-Turcu F., Enchev R.I., Wilkinson K.D., Komander D.;
RT "Polyubiquitin binding and cross-reactivity in the USP domain
RT deubiquitinase USP21.";
RL EMBO Rep. 12:350-357(2011).
CC -!- FUNCTION: Deubiquitinates histone H2A, a specific tag for epigenetic
CC transcriptional repression, thereby acting as a coactivator.
CC Deubiquitination of histone H2A releaves the repression of di- and
CC trimethylation of histone H3 at 'Lys-4', resulting in regulation of
CC transcriptional initiation. Regulates gene expression via histone H2A
CC deubiquitination (By similarity). Also capable of removing NEDD8 from
CC NEDD8 conjugates but has no effect on Sentrin-1 conjugates
CC (PubMed:10799498). Deubiquitinates BAZ2A/TIP5 leading to its
CC stabilization (PubMed:26100909). {ECO:0000250|UniProtKB:Q9QZL6,
CC ECO:0000269|PubMed:10799498, ECO:0000269|PubMed:26100909}.
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 BEND3 and BAZ2A/TIP5.
CC {ECO:0000269|PubMed:26100909}.
CC -!- INTERACTION:
CC Q9UK80; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-373242, EBI-10173507;
CC Q9UK80; Q16630-2: CPSF6; NbExp=3; IntAct=EBI-373242, EBI-11088043;
CC Q9UK80; O95967: EFEMP2; NbExp=3; IntAct=EBI-373242, EBI-743414;
CC Q9UK80; Q9NYD6: HOXC10; NbExp=3; IntAct=EBI-373242, EBI-1188075;
CC Q9UK80; Q7L273: KCTD9; NbExp=3; IntAct=EBI-373242, EBI-4397613;
CC Q9UK80; Q6A162: KRT40; NbExp=3; IntAct=EBI-373242, EBI-10171697;
CC Q9UK80; P09936: UCHL1; NbExp=4; IntAct=EBI-373242, EBI-714860;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21888622}. Nucleus
CC {ECO:0000269|PubMed:21888622}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UK80-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UK80-2; Sequence=VSP_036717, VSP_036718;
CC Name=3;
CC IsoId=Q9UK80-3; Sequence=VSP_036719;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, pancreas and skeletal
CC muscle. Also expressed in brain, placenta, liver and kidney, and at
CC very low level in lung. {ECO:0000269|PubMed:10799498}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP21 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF61308.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAG17222.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD92136.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF177758; AAD54321.1; -; mRNA.
DR EMBL; AF233442; AAF61308.1; ALT_FRAME; mRNA.
DR EMBL; AK292319; BAF85008.1; -; mRNA.
DR EMBL; AF217979; AAG17222.1; ALT_FRAME; mRNA.
DR EMBL; AB208899; BAD92136.1; ALT_INIT; mRNA.
DR EMBL; AL590714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52644.1; -; Genomic_DNA.
DR EMBL; BC003130; AAH03130.2; -; mRNA.
DR EMBL; BC090946; AAH90946.1; -; mRNA.
DR EMBL; BC136291; AAI36292.1; -; mRNA.
DR CCDS; CCDS30920.1; -. [Q9UK80-1]
DR CCDS; CCDS81392.1; -. [Q9UK80-3]
DR RefSeq; NP_001014443.1; NM_001014443.2. [Q9UK80-1]
DR RefSeq; NP_001306777.1; NM_001319848.1. [Q9UK80-3]
DR RefSeq; NP_036607.3; NM_012475.4. [Q9UK80-1]
DR PDB; 2Y5B; X-ray; 2.70 A; A/E=196-565.
DR PDB; 3I3T; X-ray; 2.59 A; A/C/E/G=209-563.
DR PDB; 3MTN; X-ray; 2.70 A; A/C=209-562.
DR PDBsum; 2Y5B; -.
DR PDBsum; 3I3T; -.
DR PDBsum; 3MTN; -.
DR AlphaFoldDB; Q9UK80; -.
DR SMR; Q9UK80; -.
DR BioGRID; 117950; 150.
DR DIP; DIP-31255N; -.
DR IntAct; Q9UK80; 27.
DR MINT; Q9UK80; -.
DR STRING; 9606.ENSP00000356981; -.
DR BindingDB; Q9UK80; -.
DR ChEMBL; CHEMBL2157852; -.
DR MEROPS; C19.034; -.
DR iPTMnet; Q9UK80; -.
DR PhosphoSitePlus; Q9UK80; -.
DR BioMuta; USP21; -.
DR DMDM; 10720334; -.
DR jPOST; Q9UK80; -.
DR MassIVE; Q9UK80; -.
DR PaxDb; Q9UK80; -.
DR PeptideAtlas; Q9UK80; -.
DR PRIDE; Q9UK80; -.
DR ProteomicsDB; 84737; -. [Q9UK80-1]
DR ProteomicsDB; 84738; -. [Q9UK80-2]
DR ProteomicsDB; 84739; -. [Q9UK80-3]
DR Antibodypedia; 34297; 337 antibodies from 30 providers.
DR DNASU; 27005; -.
DR Ensembl; ENST00000289865.12; ENSP00000289865.8; ENSG00000143258.16. [Q9UK80-1]
DR Ensembl; ENST00000368001.1; ENSP00000356980.1; ENSG00000143258.16. [Q9UK80-3]
DR Ensembl; ENST00000368002.8; ENSP00000356981.3; ENSG00000143258.16. [Q9UK80-1]
DR GeneID; 27005; -.
DR KEGG; hsa:27005; -.
DR MANE-Select; ENST00000368002.8; ENSP00000356981.3; NM_001014443.3; NP_001014443.1.
DR UCSC; uc031vci.2; human. [Q9UK80-1]
DR CTD; 27005; -.
DR DisGeNET; 27005; -.
DR GeneCards; USP21; -.
DR HGNC; HGNC:12620; USP21.
DR HPA; ENSG00000143258; Low tissue specificity.
DR MIM; 604729; gene.
DR neXtProt; NX_Q9UK80; -.
DR OpenTargets; ENSG00000143258; -.
DR PharmGKB; PA37246; -.
DR VEuPathDB; HostDB:ENSG00000143258; -.
DR eggNOG; KOG1868; Eukaryota.
DR GeneTree; ENSGT00940000155545; -.
DR HOGENOM; CLU_035237_0_0_1; -.
DR InParanoid; Q9UK80; -.
DR OMA; ERRNPGP; -.
DR OrthoDB; 561804at2759; -.
DR PhylomeDB; Q9UK80; -.
DR TreeFam; TF106277; -.
DR BRENDA; 3.4.19.12; 2681.
DR PathwayCommons; Q9UK80; -.
DR Reactome; R-HSA-5357786; TNFR1-induced proapoptotic signaling.
DR Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; Q9UK80; -.
DR BioGRID-ORCS; 27005; 13 hits in 1121 CRISPR screens.
DR ChiTaRS; USP21; human.
DR EvolutionaryTrace; Q9UK80; -.
DR GenomeRNAi; 27005; -.
DR Pharos; Q9UK80; Tbio.
DR PRO; PR:Q9UK80; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UK80; protein.
DR Bgee; ENSG00000143258; Expressed in right uterine tube and 190 other tissues.
DR ExpressionAtlas; Q9UK80; baseline and differential.
DR Genevisible; Q9UK80; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IMP:UniProtKB.
DR GO; GO:0019784; F:deNEDDylase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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 Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Chromatin regulator;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleus; Protease; Reference proteome;
KW Thiol protease; Transcription; Transcription regulation;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..565
FT /note="Ubiquitin carboxyl-terminal hydrolase 21"
FT /id="PRO_0000080648"
FT DOMAIN 212..558
FT /note="USP"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 134..152
FT /note="Nuclear export signal"
FT COMPBIAS 57..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 221
FT /note="Nucleophile"
FT ACT_SITE 518
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT VAR_SEQ 372..382
FT /note="DLFVGQLKSCL -> GMEWGKAMREN (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_036717"
FT VAR_SEQ 383..565
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_036718"
FT VAR_SEQ 498..511
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_036719"
FT VARIANT 91
FT /note="P -> S (in dbSNP:rs34779722)"
FT /id="VAR_051531"
FT VARIANT 321
FT /note="G -> D (in dbSNP:rs17356051)"
FT /id="VAR_051532"
FT VARIANT 336
FT /note="P -> T (in dbSNP:rs1127525)"
FT /id="VAR_051533"
FT MUTAGEN 221
FT /note="C->A: Abolishes ubiquitin thioesterase activity."
FT /evidence="ECO:0000269|PubMed:10799498"
FT CONFLICT 42
FT /note="A -> G (in Ref. 8; AAH90946)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="P -> L (in Ref. 2; AAF61308)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="S -> F (in Ref. 2; AAF61308)"
FT /evidence="ECO:0000305"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3MTN"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:3I3T"
FT HELIX 234..242
FT /evidence="ECO:0007829|PDB:3I3T"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:3I3T"
FT HELIX 257..268
FT /evidence="ECO:0007829|PDB:3I3T"
FT HELIX 281..290
FT /evidence="ECO:0007829|PDB:3I3T"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3I3T"
FT HELIX 302..317
FT /evidence="ECO:0007829|PDB:3I3T"
FT HELIX 351..365
FT /evidence="ECO:0007829|PDB:3I3T"
FT HELIX 369..374
FT /evidence="ECO:0007829|PDB:3I3T"
FT STRAND 376..384
FT /evidence="ECO:0007829|PDB:3I3T"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:3I3T"
FT STRAND 390..402
FT /evidence="ECO:0007829|PDB:3I3T"
FT HELIX 416..424
FT /evidence="ECO:0007829|PDB:3I3T"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:3I3T"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:3I3T"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:3I3T"
FT STRAND 446..454
FT /evidence="ECO:0007829|PDB:3I3T"
FT STRAND 457..463
FT /evidence="ECO:0007829|PDB:3I3T"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:2Y5B"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:2Y5B"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:3I3T"
FT STRAND 501..513
FT /evidence="ECO:0007829|PDB:3I3T"
FT STRAND 516..525
FT /evidence="ECO:0007829|PDB:3I3T"
FT STRAND 528..533
FT /evidence="ECO:0007829|PDB:3I3T"
FT STRAND 536..540
FT /evidence="ECO:0007829|PDB:3I3T"
FT HELIX 542..546
FT /evidence="ECO:0007829|PDB:3I3T"
FT STRAND 551..557
FT /evidence="ECO:0007829|PDB:3I3T"
SQ SEQUENCE 565 AA; 62656 MW; 8A13ED34C03B2330 CRC64;
MPQASEHRLG RTREPPVNIQ PRVGSKLPFA PRARSKERRN PASGPNPMLR PLPPRPGLPD
ERLKKLELGR GRTSGPRPRG PLRADHGVPL PGSPPPTVAL PLPSRTNLAR SKSVSSGDLR
PMGIALGGHR GTGELGAALS RLALRPEPPT LRRSTSLRRL GGFPGPPTLF SIRTEPPASH
GSFHMISARS SEPFYSDDKM AHHTLLLGSG HVGLRNLGNT CFLNAVLQCL SSTRPLRDFC
LRRDFRQEVP GGGRAQELTE AFADVIGALW HPDSCEAVNP TRFRAVFQKY VPSFSGYSQQ
DAQEFLKLLM ERLHLEINRR GRRAPPILAN GPVPSPPRRG GALLEEPELS DDDRANLMWK
RYLEREDSKI VDLFVGQLKS CLKCQACGYR STTFEVFCDL SLPIPKKGFA GGKVSLRDCF
NLFTKEEELE SENAPVCDRC RQKTRSTKKL TVQRFPRILV LHLNRFSASR GSIKKSSVGV
DFPLQRLSLG DFASDKAGSP VYQLYALCNH SGSVHYGHYT ALCRCQTGWH VYNDSRVSPV
SENQVASSEG YVLFYQLMQE PPRCL
