UBP14_HUMAN
ID UBP14_HUMAN Reviewed; 494 AA.
AC P54578; B7Z4N8; J3QRZ5; Q53XY5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 14;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 14;
DE AltName: Full=Ubiquitin thioesterase 14;
DE AltName: Full=Ubiquitin-specific-processing protease 14;
GN Name=USP14; Synonyms=TGT;
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).
RC TISSUE=Placenta;
RA Deshpande K.L., Katze J.R.;
RT "tRNA-guanine transglycosylase cDNA from human placenta.";
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [LARGE SCALE MRNA] OF 1-308 (ISOFORM 2).
RC TISSUE=T-cell;
RA Heil O., Ebert L., Hennig S., Henze S., Radelof U., Schneider D., Korn B.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH FANCC.
RX PubMed=14499622; DOI=10.1016/s0014-4827(03)00261-1;
RA Reuter T.Y., Medhurst A.L., Waisfisz Q., Zhi Y., Herterich S., Hoehn H.,
RA Gross H.J., Joenje H., Hoatlin M.E., Mathew C.G., Huber P.A.;
RT "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in
RT transcription regulation, cell signaling, oxidative metabolism, and
RT cellular transport.";
RL Exp. Cell Res. 289:211-221(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [9]
RP ASSOCIATION WITH THE 26S PROTEASOME, AND FUNCTION.
RX PubMed=18162577; DOI=10.1091/mbc.e07-10-1040;
RA Koulich E., Li X., DeMartino G.N.;
RT "Relative structural and functional roles of multiple deubiquitylating
RT proteins associated with mammalian 26S proteasome.";
RL Mol. Biol. Cell 19:1072-1082(2008).
RN [10]
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 [11]
RP FUNCTION, AND INTERACTION WITH ERN1.
RX PubMed=19135427; DOI=10.1016/j.bbrc.2008.12.182;
RA Nagai A., Kadowaki H., Maruyama T., Takeda K., Nishitoh H., Ichijo H.;
RT "USP14 inhibits ER-associated degradation via interaction with IRE1alpha.";
RL Biochem. Biophys. Res. Commun. 379:995-1000(2009).
RN [12]
RP INTERACTION WITH CXCR4, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19106094; DOI=10.1074/jbc.m808507200;
RA Mines M.A., Goodwin J.S., Limbird L.E., Cui F.F., Fan G.H.;
RT "Deubiquitination of CXCR4 by USP14 is critical for both CXCL12-induced
RT CXCR4 degradation and chemotaxis but not ERK activation.";
RL J. Biol. Chem. 284:5742-5752(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-449, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND THR-235, AND
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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY
RP 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-52; SER-143; SER-237; SER-302
RP AND SER-432, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND THR-235, 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 [20]
RP FUNCTION, AND INTERACTION WITH TRIM14.
RX PubMed=27666593; DOI=10.1016/j.molcel.2016.08.025;
RA Chen M., Meng Q., Qin Y., Liang P., Tan P., He L., Zhou Y., Chen Y.,
RA Huang J., Wang R.F., Cui J.;
RT "TRIM14 inhibits cGAS degradation mediated by selective autophagy receptor
RT p62 to promote innate immune responses.";
RL Mol. Cell 64:105-119(2016).
RN [21]
RP FUNCTION.
RX PubMed=28396413; DOI=10.1073/pnas.1701734114;
RA Kuo C.L., Goldberg A.L.;
RT "Ubiquitinated proteins promote the association of proteasomes with the
RT deubiquitinating enzyme Usp14 and the ubiquitin ligase Ube3c.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E3404-E3413(2017).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 91-494, CATALYTIC ACTIVITY, AND
RP ACTIVE SITE.
RX PubMed=16211010; DOI=10.1038/sj.emboj.7600832;
RA Hu M., Li P., Song L., Jeffrey P.D., Chenova T.A., Wilkinson K.D.,
RA Cohen R.E., Shi Y.;
RT "Structure and mechanisms of the proteasome-associated deubiquitinating
RT enzyme USP14.";
RL EMBO J. 24:3747-3756(2005).
CC -!- FUNCTION: Proteasome-associated deubiquitinase which releases ubiquitin
CC from the proteasome targeted ubiquitinated proteins. Ensures the
CC regeneration of ubiquitin at the proteasome (PubMed:18162577,
CC PubMed:28396413). Is a reversibly associated subunit of the proteasome
CC and a large fraction of proteasome-free protein exists within the cell
CC (PubMed:18162577). Required for the degradation of the chemokine
CC receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis
CC (PubMed:19106094). Serves also as a physiological inhibitor of
CC endoplasmic reticulum-associated degradation (ERAD) under the non-
CC stressed condition by inhibiting the degradation of unfolded
CC endoplasmic reticulum proteins via interaction with ERN1
CC (PubMed:19135427). Indispensable for synaptic development and function
CC at neuromuscular junctions (NMJs) (By similarity). Plays a role in the
CC innate immune defense against viruses by stabilizing the viral DNA
CC sensor CGAS and thus inhibiting its autophagic degradation
CC (PubMed:27666593). {ECO:0000250|UniProtKB:Q9JMA1,
CC ECO:0000269|PubMed:18162577, ECO:0000269|PubMed:19106094,
CC ECO:0000269|PubMed:19135427, ECO:0000269|PubMed:27666593,
CC ECO:0000269|PubMed:28396413}.
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:16211010};
CC -!- SUBUNIT: Homodimer (Potential). Associates with the 26S proteasome.
CC Interacts with FANCC, CXCR4 and ERN1. Interacts with TRIM14; this
CC interaction recruits USP14 to cleave ubiquitin chains of CGAS.
CC {ECO:0000269|PubMed:14499622, ECO:0000269|PubMed:19106094,
CC ECO:0000269|PubMed:19135427, ECO:0000269|PubMed:27666593, ECO:0000305}.
CC -!- INTERACTION:
CC P54578; Q08209: PPP3CA; NbExp=3; IntAct=EBI-1048016, EBI-352922;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19106094}. Cell
CC membrane {ECO:0000269|PubMed:19106094}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19106094}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P54578-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P54578-2; Sequence=VSP_047343;
CC Name=3;
CC IsoId=P54578-3; Sequence=VSP_057292;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP14/UBP6 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a guanine tRNA-
CC ribosyltransferase. {ECO:0000305, ECO:0000305|Ref.1}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CR976282; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U30888; AAB60365.1; -; mRNA.
DR EMBL; BT007183; AAP35847.1; -; mRNA.
DR EMBL; AK297605; BAH12624.1; -; mRNA.
DR EMBL; AP000845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003556; AAH03556.1; -; mRNA.
DR EMBL; CR976282; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS32780.1; -. [P54578-1]
DR CCDS; CCDS32781.1; -. [P54578-2]
DR PIR; G01932; G01932.
DR RefSeq; NP_001032411.1; NM_001037334.1. [P54578-2]
DR RefSeq; NP_005142.1; NM_005151.3. [P54578-1]
DR PDB; 2AYN; X-ray; 3.20 A; A/B/C=91-494.
DR PDB; 2AYO; X-ray; 3.50 A; A=91-494.
DR PDB; 5GJQ; EM; 4.50 A; x=1-494.
DR PDB; 6IIK; X-ray; 1.97 A; A/B=96-494.
DR PDB; 6IIL; X-ray; 2.20 A; A/B=96-494.
DR PDB; 6IIM; X-ray; 2.21 A; A/B=96-494.
DR PDB; 6IIN; X-ray; 2.53 A; A/B=101-485.
DR PDB; 6LVS; X-ray; 2.73 A; A/B/C/D/E/F=92-494.
DR PDBsum; 2AYN; -.
DR PDBsum; 2AYO; -.
DR PDBsum; 5GJQ; -.
DR PDBsum; 6IIK; -.
DR PDBsum; 6IIL; -.
DR PDBsum; 6IIM; -.
DR PDBsum; 6IIN; -.
DR PDBsum; 6LVS; -.
DR AlphaFoldDB; P54578; -.
DR BMRB; P54578; -.
DR SMR; P54578; -.
DR BioGRID; 114551; 471.
DR IntAct; P54578; 49.
DR MINT; P54578; -.
DR STRING; 9606.ENSP00000261601; -.
DR BindingDB; P54578; -.
DR ChEMBL; CHEMBL1293295; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR GuidetoPHARMACOLOGY; 2429; -.
DR MEROPS; C19.015; -.
DR GlyGen; P54578; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P54578; -.
DR MetOSite; P54578; -.
DR PhosphoSitePlus; P54578; -.
DR SwissPalm; P54578; -.
DR BioMuta; USP14; -.
DR DMDM; 1729927; -.
DR OGP; P54578; -.
DR EPD; P54578; -.
DR jPOST; P54578; -.
DR MassIVE; P54578; -.
DR MaxQB; P54578; -.
DR PaxDb; P54578; -.
DR PeptideAtlas; P54578; -.
DR PRIDE; P54578; -.
DR ProteomicsDB; 56687; -. [P54578-1]
DR ProteomicsDB; 6620; -.
DR Antibodypedia; 676; 320 antibodies from 35 providers.
DR DNASU; 9097; -.
DR Ensembl; ENST00000261601.8; ENSP00000261601.6; ENSG00000101557.15. [P54578-1]
DR Ensembl; ENST00000400266.7; ENSP00000383125.3; ENSG00000101557.15. [P54578-3]
DR Ensembl; ENST00000582707.5; ENSP00000464447.1; ENSG00000101557.15. [P54578-2]
DR GeneID; 9097; -.
DR KEGG; hsa:9097; -.
DR MANE-Select; ENST00000261601.8; ENSP00000261601.6; NM_005151.4; NP_005142.1.
DR UCSC; uc002kkf.2; human. [P54578-1]
DR CTD; 9097; -.
DR DisGeNET; 9097; -.
DR GeneCards; USP14; -.
DR HGNC; HGNC:12612; USP14.
DR HPA; ENSG00000101557; Low tissue specificity.
DR MIM; 607274; gene.
DR neXtProt; NX_P54578; -.
DR OpenTargets; ENSG00000101557; -.
DR PharmGKB; PA37238; -.
DR VEuPathDB; HostDB:ENSG00000101557; -.
DR eggNOG; KOG1872; Eukaryota.
DR GeneTree; ENSGT00390000009615; -.
DR InParanoid; P54578; -.
DR OMA; MCKGGIL; -.
DR OrthoDB; 600543at2759; -.
DR PhylomeDB; P54578; -.
DR TreeFam; TF314494; -.
DR PathwayCommons; P54578; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; P54578; -.
DR SIGNOR; P54578; -.
DR BioGRID-ORCS; 9097; 96 hits in 1084 CRISPR screens.
DR ChiTaRS; USP14; human.
DR EvolutionaryTrace; P54578; -.
DR GeneWiki; USP14; -.
DR GenomeRNAi; 9097; -.
DR Pharos; P54578; Tchem.
DR PRO; PR:P54578; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P54578; protein.
DR Bgee; ENSG00000101557; Expressed in secondary oocyte and 219 other tissues.
DR ExpressionAtlas; P54578; baseline and differential.
DR Genevisible; P54578; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IMP:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1903070; P:negative regulation of ER-associated ubiquitin-dependent protein catabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
DR GO; GO:0050920; P:regulation of chemotaxis; IMP:UniProtKB.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IMP:UniProtKB.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR044635; UBP14-like.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR43982; PTHR43982; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 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; Acetylation; Alternative splicing; Cell membrane; Cytoplasm;
KW Hydrolase; Immunity; Innate immunity; Membrane; Phosphoprotein; Protease;
KW Proteasome; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..494
FT /note="Ubiquitin carboxyl-terminal hydrolase 14"
FT /id="PRO_0000080636"
FT DOMAIN 4..80
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 105..483
FT /note="USP"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:16211010"
FT ACT_SITE 435
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 52
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMA1"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 449
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 55..65
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057292"
FT VAR_SEQ 66..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_047343"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:6IIL"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:6IIK"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6LVS"
FT HELIX 147..165
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:6IIK"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:6IIK"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:6LVS"
FT HELIX 200..214
FT /evidence="ECO:0007829|PDB:6IIK"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 249..259
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:2AYN"
FT HELIX 286..293
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:6IIK"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 307..319
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 321..329
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:6LVS"
FT TURN 335..338
FT /evidence="ECO:0007829|PDB:6LVS"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:6LVS"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:6IIK"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:6IIK"
FT HELIX 361..376
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:6LVS"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:2AYN"
FT STRAND 414..429
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 435..443
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:6IIK"
FT HELIX 460..464
FT /evidence="ECO:0007829|PDB:6IIK"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:6IIK"
FT STRAND 474..482
FT /evidence="ECO:0007829|PDB:6IIK"
SQ SEQUENCE 494 AA; 56069 MW; E6D4679A86E9DF00 CRC64;
MPLYSVTVKW GKEKFEGVEL NTDEPPMVFK AQLFALTGVQ PARQKVMVKG GTLKDDDWGN
IKIKNGMTLL MMGSADALPE EPSAKTVFVE DMTEEQLASA MELPCGLTNL GNTCYMNATV
QCIRSVPELK DALKRYAGAL RASGEMASAQ YITAALRDLF DSMDKTSSSI PPIILLQFLH
MAFPQFAEKG EQGQYLQQDA NECWIQMMRV LQQKLEAIED DSVKETDSSS ASAATPSKKK
SLIDQFFGVE FETTMKCTES EEEEVTKGKE NQLQLSCFIN QEVKYLFTGL KLRLQEEITK
QSPTLQRNAL YIKSSKISRL PAYLTIQMVR FFYKEKESVN AKVLKDVKFP LMLDMYELCT
PELQEKMVSF RSKFKDLEDK KVNQQPNTSD KKSSPQKEVK YEPFSFADDI GSNNCGYYDL
QAVLTHQGRS SSSGHYVSWV KRKQDEWIKF DDDKVSIVTP EDILRLSGGG DWHIAYVLLY
GPRRVEIMEE ESEQ
