UBP19_HUMAN
ID UBP19_HUMAN Reviewed; 1318 AA.
AC O94966; A5PKX8; A6H8U2; B4DGT3; B4DTZ0; E7EN22; E7ETS0; E9PEG8; Q3KQW4;
AC Q641Q9; Q6NZY8; Q86XV9;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 19;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 19;
DE AltName: Full=Ubiquitin thioesterase 19;
DE AltName: Full=Ubiquitin-specific-processing protease 19;
DE AltName: Full=Zinc finger MYND domain-containing protein 9;
GN Name=USP19; Synonyms=KIAA0891, ZMYND9;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
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. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 6), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 846-1318 (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 90-1318 (ISOFORM 4).
RC TISSUE=Skin, 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 [5]
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 [6]
RP FUNCTION, TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=19465887; DOI=10.1038/embor.2009.69;
RA Hassink G.C., Zhao B., Sompallae R., Altun M., Gastaldello S., Zinin N.V.,
RA Masucci M.G., Lindsten K.;
RT "The ER-resident ubiquitin-specific protease 19 participates in the UPR and
RT rescues ERAD substrates.";
RL EMBO Rep. 10:755-761(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
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 [9]
RP FUNCTION, AND INTERACTION WITH BIRC2/C-IAP1; BIRC3/C-IAP2 AND XIAP/BIRC4.
RX PubMed=21849505; DOI=10.1074/jbc.m111.282020;
RA Mei Y., Hahn A.A., Hu S., Yang X.;
RT "The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2.";
RL J. Biol. Chem. 286:35380-35387(2011).
RN [10]
RP FUNCTION, AND LINKAGE SPECIFICITY.
RX PubMed=22689415; DOI=10.1002/cbic.201200261;
RA Iphofer A., Kummer A., Nimtz M., Ritter A., Arnold T., Frank R.,
RA van den Heuvel J., Kessler B.M., Jansch L., Franke R.;
RT "Profiling ubiquitin linkage specificities of deubiquitinating enzymes with
RT branched ubiquitin isopeptide probes.";
RL ChemBioChem 13:1416-1420(2012).
RN [11]
RP FUNCTION, AND INTERACTION WITH HIF1A.
RX PubMed=22128162; DOI=10.1074/jbc.m111.305615;
RA Altun M., Zhao B., Velasco K., Liu H., Hassink G., Paschke J., Pereira T.,
RA Lindsten K.;
RT "Ubiquitin-specific protease 19 (USP19) regulates hypoxia-inducible factor
RT 1alpha (HIF-1alpha) during hypoxia.";
RL J. Biol. Chem. 287:1962-1969(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP MASS 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 [13]
RP STRUCTURE BY NMR OF 273-393.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CS domain of human USP19.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Deubiquitinating enzyme that regulates the degradation of
CC various proteins. Deubiquitinates and prevents proteasomal degradation
CC of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent
CC degradation thereby playing a role in cell proliferation. Involved in
CC decreased protein synthesis in atrophying skeletal muscle. Modulates
CC transcription of major myofibrillar proteins. Also involved in turnover
CC of endoplasmic-reticulum-associated degradation (ERAD) substrates.
CC Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing
CC their ubiquitination. Required for cells to mount an appropriate
CC response to hypoxia and rescues HIF1A from degradation in a non-
CC catalytic manner. Plays an important role in 17 beta-estradiol (E2)-
CC inhibited myogenesis. Decreases the levels of ubiquitinated proteins
CC during skeletal muscle formation and acts to repress myogenesis.
CC Exhibits a preference towards 'Lys-63'-linked ubiquitin chains.
CC {ECO:0000269|PubMed:19465887, ECO:0000269|PubMed:21849505,
CC ECO:0000269|PubMed:22128162, ECO:0000269|PubMed:22689415}.
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 RNF123 (By similarity). Interacts with BIRC2/c-
CC IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Interacts with HIF1A (via N-
CC terminus). {ECO:0000250, ECO:0000269|PubMed:21849505,
CC ECO:0000269|PubMed:22128162}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19465887}; Single-pass membrane protein
CC {ECO:0000269|PubMed:19465887}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=O94966-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94966-2; Sequence=VSP_026708, VSP_026709, VSP_026710,
CC VSP_026711;
CC Name=3;
CC IsoId=O94966-3; Sequence=VSP_026712, VSP_026713;
CC Name=4;
CC IsoId=O94966-4; Sequence=VSP_026708, VSP_045891, VSP_026712,
CC VSP_026713;
CC Name=5;
CC IsoId=O94966-5; Sequence=VSP_026709;
CC Name=6;
CC IsoId=O94966-6; Sequence=VSP_026709, VSP_045891, VSP_026712,
CC VSP_026713;
CC Name=7;
CC IsoId=O94966-7; Sequence=VSP_047057, VSP_026712, VSP_026713;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI06030.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI06030.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAI42661.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA74914.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB020698; BAA74914.1; ALT_INIT; mRNA.
DR EMBL; AK294756; BAG57894.1; -; mRNA.
DR EMBL; AK300425; BAG62152.1; -; mRNA.
DR EMBL; AC135506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048269; AAH48269.1; -; mRNA.
DR EMBL; BC065909; AAH65909.1; -; mRNA.
DR EMBL; BC082241; AAH82241.1; -; mRNA.
DR EMBL; BC106029; AAI06030.1; ALT_SEQ; mRNA.
DR EMBL; BC142660; AAI42661.1; ALT_INIT; mRNA.
DR EMBL; BC146752; AAI46753.1; -; mRNA.
DR CCDS; CCDS43090.1; -. [O94966-1]
DR CCDS; CCDS56254.1; -. [O94966-5]
DR CCDS; CCDS56255.1; -. [O94966-6]
DR CCDS; CCDS56256.1; -. [O94966-7]
DR RefSeq; NP_001186089.1; NM_001199160.1. [O94966-5]
DR RefSeq; NP_001186090.1; NM_001199161.1. [O94966-6]
DR RefSeq; NP_001186091.1; NM_001199162.1. [O94966-7]
DR RefSeq; NP_006668.1; NM_006677.2. [O94966-1]
DR RefSeq; XP_005264888.1; XM_005264831.2.
DR RefSeq; XP_016861115.1; XM_017005626.1. [O94966-1]
DR RefSeq; XP_016861122.1; XM_017005633.1. [O94966-3]
DR PDB; 1WH0; NMR; -; A=273-393.
DR PDB; 4X3G; X-ray; 2.34 A; C/D=461-474.
DR PDB; 6K7W; NMR; -; A=113-204.
DR PDB; 6KHV; NMR; -; A=273-386.
DR PDB; 6KQV; NMR; -; A=679-766.
DR PDBsum; 1WH0; -.
DR PDBsum; 4X3G; -.
DR PDBsum; 6K7W; -.
DR PDBsum; 6KHV; -.
DR PDBsum; 6KQV; -.
DR AlphaFoldDB; O94966; -.
DR SMR; O94966; -.
DR BioGRID; 116078; 135.
DR IntAct; O94966; 57.
DR MINT; O94966; -.
DR STRING; 9606.ENSP00000401197; -.
DR BindingDB; O94966; -.
DR ChEMBL; CHEMBL4523156; -.
DR MEROPS; C19.024; -.
DR GlyGen; O94966; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O94966; -.
DR PhosphoSitePlus; O94966; -.
DR BioMuta; USP19; -.
DR EPD; O94966; -.
DR jPOST; O94966; -.
DR MassIVE; O94966; -.
DR MaxQB; O94966; -.
DR PaxDb; O94966; -.
DR PeptideAtlas; O94966; -.
DR PRIDE; O94966; -.
DR ProteomicsDB; 17063; -.
DR ProteomicsDB; 18276; -.
DR ProteomicsDB; 19884; -.
DR ProteomicsDB; 50583; -. [O94966-1]
DR ProteomicsDB; 50584; -. [O94966-2]
DR ProteomicsDB; 50585; -. [O94966-3]
DR ProteomicsDB; 50586; -. [O94966-4]
DR Antibodypedia; 30419; 184 antibodies from 32 providers.
DR DNASU; 10869; -.
DR Ensembl; ENST00000398888.6; ENSP00000381863.2; ENSG00000172046.20. [O94966-1]
DR Ensembl; ENST00000398896.6; ENSP00000381870.3; ENSG00000172046.20. [O94966-4]
DR Ensembl; ENST00000417901.6; ENSP00000395260.1; ENSG00000172046.20. [O94966-6]
DR Ensembl; ENST00000434032.6; ENSP00000401197.2; ENSG00000172046.20. [O94966-5]
DR Ensembl; ENST00000453664.5; ENSP00000400090.1; ENSG00000172046.20. [O94966-7]
DR GeneID; 10869; -.
DR KEGG; hsa:10869; -.
DR MANE-Select; ENST00000417901.6; ENSP00000395260.1; NM_001199161.2; NP_001186090.1. [O94966-6]
DR UCSC; uc003cvz.5; human. [O94966-1]
DR CTD; 10869; -.
DR DisGeNET; 10869; -.
DR GeneCards; USP19; -.
DR HGNC; HGNC:12617; USP19.
DR HPA; ENSG00000172046; Low tissue specificity.
DR MIM; 614471; gene.
DR neXtProt; NX_O94966; -.
DR OpenTargets; ENSG00000172046; -.
DR PharmGKB; PA37243; -.
DR VEuPathDB; HostDB:ENSG00000172046; -.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000159085; -.
DR InParanoid; O94966; -.
DR OMA; SVPCWRI; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; O94966; -.
DR TreeFam; TF106276; -.
DR PathwayCommons; O94966; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; O94966; -.
DR BioGRID-ORCS; 10869; 67 hits in 1092 CRISPR screens.
DR ChiTaRS; USP19; human.
DR EvolutionaryTrace; O94966; -.
DR GenomeRNAi; 10869; -.
DR Pharos; O94966; Tbio.
DR PRO; PR:O94966; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O94966; protein.
DR Bgee; ENSG00000172046; Expressed in gastrocnemius and 181 other tissues.
DR ExpressionAtlas; O94966; baseline and differential.
DR Genevisible; O94966; HS.
DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IEA:Ensembl.
DR GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; ISS:UniProtKB.
DR GO; GO:0090068; P:positive regulation of cell cycle process; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IMP:ParkinsonsUK-UCL.
DR GO; GO:0050821; P:protein stabilization; IMP:ParkinsonsUK-UCL.
DR GO; GO:1900037; P:regulation of cellular response to hypoxia; IMP:UniProtKB.
DR GO; GO:1904292; P:regulation of ERAD pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
DR Gene3D; 2.60.40.790; -; 2.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
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; IPR002893; Znf_MYND.
DR Pfam; PF04969; CS; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SUPFAM; SSF49764; SSF49764; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51203; CS; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endoplasmic reticulum; Hydrolase;
KW Membrane; Metal-binding; Phosphoprotein; Protease; Reference proteome;
KW Repeat; Thiol protease; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1318
FT /note="Ubiquitin carboxyl-terminal hydrolase 19"
FT /id="PRO_0000080646"
FT TOPO_DOM 1..1291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1292..1312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1313..1318
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 113..202
FT /note="CS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT DOMAIN 282..384
FT /note="CS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT DOMAIN 497..1214
FT /note="USP"
FT ZN_FING 791..833
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 506
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 1165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 791
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 794
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 808
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 811
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 817
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 821
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 829
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 833
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 100..114
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026708"
FT VAR_SEQ 193..202
FT /note="VPMLTWPSLL -> KKPLGTQELVPGLRCQENGQELSPIALEPGPEPHRAKQ
FT EARNQKRAQGRGEVGAGAGPGAQAGPSAKRAVHLCRGPEGDGSRDDPGPRGDAPPFVAD
FT PATQ (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047057"
FT VAR_SEQ 202
FT /note="L -> LKKPLGTQELVPGLRCQENGQELSPIALEPGPEPHRAKQEARNQKRA
FT QGRGEVGAGAGPGAQAGPSAKRAVHLCRGPEGDGSRDDPGPRGDAPPFVADPATQ (in
FT isoform 2, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_026709"
FT VAR_SEQ 389
FT /note="R -> RGA (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045891"
FT VAR_SEQ 573..574
FT /note="IV -> RL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026710"
FT VAR_SEQ 575..1318
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026711"
FT VAR_SEQ 1244..1298
FT /note="ASRIWQELEAEEEPVPEGSGPLGPWGPQDWVGPLPRGPTTPDEGCLRYFVLG
FT TVA -> GLGPGQAPEVAPTRTAPERFAPPVDRPAPTYSNMEEVD (in isoform
FT 3, isoform 4, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_026712"
FT VAR_SEQ 1299..1318
FT /note="Missing (in isoform 3, isoform 4, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_026713"
FT VARIANT 36
FT /note="D -> H (in dbSNP:rs11552724)"
FT /id="VAR_051528"
FT CONFLICT 942
FT /note="S -> C (in Ref. 2; BAG57894)"
FT /evidence="ECO:0000305"
FT CONFLICT 1041
FT /note="E -> G (in Ref. 2; BAG62152)"
FT /evidence="ECO:0000305"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6K7W"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:6K7W"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:6K7W"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:6K7W"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:6K7W"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:6K7W"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:6K7W"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:6K7W"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:6K7W"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6K7W"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:6K7W"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:6K7W"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:6K7W"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:1WH0"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:1WH0"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:1WH0"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:1WH0"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:1WH0"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:6KHV"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:1WH0"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:1WH0"
FT HELIX 329..334
FT /evidence="ECO:0007829|PDB:1WH0"
FT TURN 336..341
FT /evidence="ECO:0007829|PDB:6KHV"
FT STRAND 344..352
FT /evidence="ECO:0007829|PDB:1WH0"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:1WH0"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:1WH0"
FT STRAND 365..377
FT /evidence="ECO:0007829|PDB:1WH0"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:4X3G"
FT STRAND 682..687
FT /evidence="ECO:0007829|PDB:6KQV"
FT STRAND 691..693
FT /evidence="ECO:0007829|PDB:6KQV"
FT STRAND 697..702
FT /evidence="ECO:0007829|PDB:6KQV"
FT HELIX 711..720
FT /evidence="ECO:0007829|PDB:6KQV"
FT HELIX 725..727
FT /evidence="ECO:0007829|PDB:6KQV"
FT STRAND 731..733
FT /evidence="ECO:0007829|PDB:6KQV"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:6KQV"
FT CONFLICT O94966-4:1251
FT /note="A -> T (in Ref. 4; AAH82241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1318 AA; 145651 MW; EA9F318D03304AA1 CRC64;
MSGGASATGP RRGPPGLEDT TSKKKQKDRA NQESKDGDPR KETGSRYVAQ AGLEPLASGD
PSASASHAAG ITGSRHRTRL FFPSSSGSAS TPQEEQTKEG ACEDPHDLLA TPTPELLLDW
RQSAEEVIVK LRVGVGPLQL EDVDAAFTDT DCVVRFAGGQ QWGGVFYAEI KSSCAKVQTR
KGSLLHLTLP KKVPMLTWPS LLVEADEQLC IPPLNSQTCL LGSEENLAPL AGEKAVPPGN
DPVSPAMVRS RNPGKDDCAK EEMAVAADAA TLVDEPESMV NLAFVKNDSY EKGPDSVVVH
VYVKEICRDT SRVLFREQDF TLIFQTRDGN FLRLHPGCGP HTTFRWQVKL RNLIEPEQCT
FCFTASRIDI CLRKRQSQRW GGLEAPAARV GGAKVAVPTG PTPLDSTPPG GAPHPLTGQE
EARAVEKDKS KARSEDTGLD SVATRTPMEH VTPKPETHLA SPKPTCMVPP MPHSPVSGDS
VEEEEEEEKK VCLPGFTGLV NLGNTCFMNS VIQSLSNTRE LRDFFHDRSF EAEINYNNPL
GTGGRLAIGF AVLLRALWKG THHAFQPSKL KAIVASKASQ FTGYAQHDAQ EFMAFLLDGL
HEDLNRIQNK PYTETVDSDG RPDEVVAEEA WQRHKMRNDS FIVDLFQGQY KSKLVCPVCA
KVSITFDPFL YLPVPLPQKQ KVLPVFYFAR EPHSKPIKFL VSVSKENSTA SEVLDSLSQS
VHVKPENLRL AEVIKNRFHR VFLPSHSLDT VSPSDTLLCF ELLSSELAKE RVVVLEVQQR
PQVPSVPISK CAACQRKQQS EDEKLKRCTR CYRVGYCNQL CQKTHWPDHK GLCRPENIGY
PFLVSVPASR LTYARLAQLL EGYARYSVSV FQPPFQPGRM ALESQSPGCT TLLSTGSLEA
GDSERDPIQP PELQLVTPMA EGDTGLPRVW AAPDRGPVPS TSGISSEMLA SGPIEVGSLP
AGERVSRPEA AVPGYQHPSE AMNAHTPQFF IYKIDSSNRE QRLEDKGDTP LELGDDCSLA
LVWRNNERLQ EFVLVASKEL ECAEDPGSAG EAARAGHFTL DQCLNLFTRP EVLAPEEAWY
CPQCKQHREA SKQLLLWRLP NVLIVQLKRF SFRSFIWRDK INDLVEFPVR NLDLSKFCIG
QKEEQLPSYD LYAVINHYGG MIGGHYTACA RLPNDRSSQR SDVGWRLFDD STVTTVDESQ
VVTRYAYVLF YRRRNSPVER PPRAGHSEHH PDLGPAAEAA ASQASRIWQE LEAEEEPVPE
GSGPLGPWGP QDWVGPLPRG PTTPDEGCLR YFVLGTVAAL VALVLNVFYP LVSQSRWR
