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26S proteasome non-ATPase regulatory subunit 14 (EC 3.4.19.-) (26S proteasome regulatory subunit RPN11) (26S proteasome-associated PAD1 homolog 1)

 PSDE_HUMAN              Reviewed;         310 AA.
O00487; B3KNW2; O00176;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
22-NOV-2017, entry version 163.
RecName: Full=26S proteasome non-ATPase regulatory subunit 14;
EC=3.4.19.-;
AltName: Full=26S proteasome regulatory subunit RPN11;
AltName: Full=26S proteasome-associated PAD1 homolog 1;
Name=PSMD14; Synonyms=POH1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Lung;
PubMed=9374539; DOI=10.1074/jbc.272.48.30470;
Spataro V., Toda T., Craig R., Seeger M., Dubiel W., Harris A.L.,
Norbury C.;
"Resistance to diverse drugs and ultraviolet light conferred by
overexpression of a novel human 26 S proteasome subunit.";
J. Biol. Chem. 272:30470-30475(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 199-208, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[6]
FUNCTION.
PubMed=1317798; DOI=10.1111/j.1432-1033.1992.tb16961.x;
Kanayama H.O., Tamura T., Ugai S., Kagawa S., Tanahashi N.,
Yoshimura T., Tanaka K., Ichihara A.;
"Demonstration that a human 26S proteolytic complex consists of a
proteasome and multiple associated protein components and hydrolyzes
ATP and ubiquitin-ligated proteins by closely linked mechanisms.";
Eur. J. Biochem. 206:567-578(1992).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human
26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
network: indicating the involvement of ribonucleoside-diphosphate
reductase M2 subunit phosphorylation at residue serine 20 in canonical
Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[9]
PROBABLE FUNCTION, AND IDENTIFICATION IN THE PROTEASOME.
PubMed=19214193; DOI=10.1038/emboj.2009.27;
Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M.,
Cohen R.E.;
"K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-
associated Brcc36 and proteasomal Poh1.";
EMBO J. 28:621-631(2009).
[10]
INTERACTION WITH TXNL1.
PubMed=19349277; DOI=10.1074/jbc.M900016200;
Andersen K.M., Madsen L., Prag S., Johnsen A.H., Semple C.A.,
Hendil K.B., Hartmann-Petersen R.;
"Thioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S
proteasome.";
J. Biol. Chem. 284:15246-15254(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
FUNCTION, IDENTIFICATION IN THE PROTEASOME, AND MUTAGENESIS OF
113-HIS--HIS-115.
PubMed=22909820; DOI=10.1038/emboj.2012.232;
Butler L.R., Densham R.M., Jia J., Garvin A.J., Stone H.R., Shah V.,
Weekes D., Festy F., Beesley J., Morris J.R.;
"The proteasomal de-ubiquitinating enzyme POH1 promotes the double-
strand DNA break response.";
EMBO J. 31:3918-3934(2012).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
PubMed=27428775; DOI=10.1038/nsmb.3273;
Huang X., Luan B., Wu J., Shi Y.;
"An atomic structure of the human 26S proteasome.";
Nat. Struct. Mol. Biol. 23:778-785(2016).
[17]
STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), AND SUBUNIT.
PubMed=27342858; DOI=10.1073/pnas.1608050113;
Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
"Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
-!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
involved in the ATP-dependent degradation of ubiquitinated
proteins. This complex plays a key role in the maintenance of
protein homeostasis by removing misfolded or damaged proteins,
which could impair cellular functions, and by removing proteins
whose functions are no longer required. Therefore, the proteasome
participates in numerous cellular processes, including cell cycle
progression, apoptosis, or DNA damage repair. The PSMD14 subunit
is a metalloprotease that specifically cleaves 'Lys-63'-linked
polyubiquitin chains within the complex. Plays a role in response
to double-strand breaks (DSBs): acts as a regulator of non-
homologous end joining (NHEJ) by cleaving 'Lys-63'-linked
polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on
chromatin and restricting TP53BP1 accumulation. Also involved in
homologous recombination repair by promoting RAD51 loading.
{ECO:0000269|PubMed:1317798, ECO:0000269|PubMed:22909820,
ECO:0000269|PubMed:9374539}.
-!- SUBUNIT: Component of the 19S proteasome regulatory particle
complex. The 26S proteasome consists of a 20S core particle (CP)
and two 19S regulatory subunits (RP). The regulatory particle is
made of a lid composed of 9 subunits including PSMD4, a base
containing 6 ATPases and few additional components
(PubMed:27428775, PubMed:27342858). Within the complex, PSMD4
interacts with subunit PSMD7 through their respective MPN domain.
Interacts with TXNL1 (PubMed:19349277).
{ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:19349277,
ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775}.
-!- INTERACTION:
Q9C005:DPY30; NbExp=5; IntAct=EBI-722193, EBI-744973;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-722193, EBI-10175124;
P50222:MEOX2; NbExp=3; IntAct=EBI-722193, EBI-748397;
P51665:PSMD7; NbExp=8; IntAct=EBI-722193, EBI-357659;
-!- TISSUE SPECIFICITY: Widely expressed. Highest levels in heart and
skeletal muscle. {ECO:0000269|PubMed:9374539}.
-!- SIMILARITY: Belongs to the peptidase M67A family. PSMD14
subfamily. {ECO:0000305}.
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EMBL; U86782; AAC51866.1; -; mRNA.
EMBL; AK055128; BAG51474.1; -; mRNA.
EMBL; CH471058; EAX11370.1; -; Genomic_DNA.
EMBL; BC066336; AAH66336.1; -; mRNA.
CCDS; CCDS46437.1; -.
RefSeq; NP_005796.1; NM_005805.5.
UniGene; Hs.740477; -.
PDB; 5GJQ; EM; 4.50 A; V=1-310.
PDB; 5GJR; EM; 3.50 A; 9/V=1-310.
PDB; 5L4K; EM; 4.50 A; V=1-310.
PDB; 5LN3; EM; 6.80 A; V=1-310.
PDB; 5M32; EM; 3.80 A; q=1-310.
PDB; 5T0C; EM; 3.80 A; Ac/Bc=1-310.
PDB; 5T0G; EM; 4.40 A; c=2-310.
PDB; 5T0H; EM; 6.80 A; c=2-310.
PDB; 5T0I; EM; 8.00 A; c=2-310.
PDB; 5T0J; EM; 8.00 A; c=2-310.
PDB; 5VGZ; EM; 3.70 A; c=24-310.
PDB; 5VHF; EM; 5.70 A; c=24-310.
PDB; 5VHH; EM; 6.10 A; c=24-310.
PDB; 5VHI; EM; 6.80 A; c=24-310.
PDB; 5VHS; EM; 8.80 A; c=24-310.
PDBsum; 5GJQ; -.
PDBsum; 5GJR; -.
PDBsum; 5L4K; -.
PDBsum; 5LN3; -.
PDBsum; 5M32; -.
PDBsum; 5T0C; -.
PDBsum; 5T0G; -.
PDBsum; 5T0H; -.
PDBsum; 5T0I; -.
PDBsum; 5T0J; -.
PDBsum; 5VGZ; -.
PDBsum; 5VHF; -.
PDBsum; 5VHH; -.
PDBsum; 5VHI; -.
PDBsum; 5VHS; -.
ProteinModelPortal; O00487; -.
SMR; O00487; -.
BioGrid; 115508; 113.
CORUM; O00487; -.
IntAct; O00487; 67.
MINT; MINT-5003743; -.
STRING; 9606.ENSP00000386541; -.
BindingDB; O00487; -.
ChEMBL; CHEMBL2007629; -.
iPTMnet; O00487; -.
PhosphoSitePlus; O00487; -.
SwissPalm; O00487; -.
BioMuta; PSMD14; -.
OGP; O00487; -.
REPRODUCTION-2DPAGE; IPI00024821; -.
EPD; O00487; -.
MaxQB; O00487; -.
PaxDb; O00487; -.
PeptideAtlas; O00487; -.
PRIDE; O00487; -.
TopDownProteomics; O00487; -.
Ensembl; ENST00000409682; ENSP00000386541; ENSG00000115233.
GeneID; 10213; -.
KEGG; hsa:10213; -.
UCSC; uc002ubu.4; human.
CTD; 10213; -.
DisGeNET; 10213; -.
EuPathDB; HostDB:ENSG00000115233.11; -.
GeneCards; PSMD14; -.
HGNC; HGNC:16889; PSMD14.
HPA; HPA002114; -.
HPA; HPA003828; -.
MIM; 607173; gene.
neXtProt; NX_O00487; -.
OpenTargets; ENSG00000115233; -.
PharmGKB; PA134957776; -.
eggNOG; KOG1555; Eukaryota.
eggNOG; COG1310; LUCA.
GeneTree; ENSGT00730000111116; -.
HOGENOM; HOG000183690; -.
HOVERGEN; HBG053742; -.
InParanoid; O00487; -.
KO; K03030; -.
OMA; QTGRPET; -.
OrthoDB; EOG091G0CMC; -.
PhylomeDB; O00487; -.
TreeFam; TF105748; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-5689901; Metalloprotease DUBs.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; PSMD14; human.
GeneWiki; PSMD14; -.
GenomeRNAi; 10213; -.
PRO; PR:O00487; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115233; -.
CleanEx; HS_PSMD14; -.
ExpressionAtlas; O00487; baseline and differential.
Genevisible; O00487; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031597; C:cytosolic proteasome complex; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IMP:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0061133; F:endopeptidase activator activity; IMP:UniProtKB.
GO; GO:0061578; F:Lys63-specific deubiquitinase activity; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; TAS:UniProtKB.
GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IMP:UniProtKB.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0070536; P:protein K63-linked deubiquitination; IMP:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IMP:UniProtKB.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:UniProtKB.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
InterPro; IPR000555; JAMM/MPN+_dom.
InterPro; IPR035299; PSMD14.
InterPro; IPR024969; Rpn11/EIF3F_C.
PANTHER; PTHR10410:SF13; PTHR10410:SF13; 1.
Pfam; PF01398; JAB; 1.
Pfam; PF13012; MitMem_reg; 1.
SMART; SM00232; JAB_MPN; 1.
PROSITE; PS50249; MPN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
DNA damage; DNA repair; Hydrolase; Metal-binding; Metalloprotease;
Phosphoprotein; Protease; Proteasome; Reference proteome;
Ubl conjugation pathway; Zinc.
CHAIN 1 310 26S proteasome non-ATPase regulatory
subunit 14.
/FTId=PRO_0000213952.
DOMAIN 31 166 MPN. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
MOTIF 113 126 JAMM motif. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 113 113 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 115 115 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 126 126 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000244|PubMed:17693683,
ECO:0000244|PubMed:24275569}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:17323924}.
MOD_RES 266 266 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MUTAGEN 113 115 HSH->ASA: Abolishes ubiquitin
thioesterase activity, leading to prevent
maintenance of JMJD2A/KDM4A on chromatin.
{ECO:0000269|PubMed:22909820}.
SEQUENCE 310 AA; 34577 MW; 18ACE876C7682039 CRC64;
MDRLLRLGGG MPGLGQGPPT DAPAVDTAEQ VYISSLALLK MLKHGRAGVP MEVMGLMLGE
FVDDYTVRVI DVFAMPQSGT GVSVEAVDPV FQAKMLDMLK QTGRPEMVVG WYHSHPGFGC
WLSGVDINTQ QSFEALSERA VAVVVDPIQS VKGKVVIDAF RLINANMMVL GHEPRQTTSN
LGHLNKPSIQ ALIHGLNRHY YSITINYRKN ELEQKMLLNL HKKSWMEGLT LQDYSEHCKH
NESVVKEMLE LAKNYNKAVE EEDKMTPEQL AIKNVGKQDP KRHLEEHVDV LMTSNIVQCL
AAMLDTVVFK


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