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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.
23-FEB-2022, entry version 193.
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:
O00487; Q9C005: DPY30; NbExp=6; IntAct=EBI-722193, EBI-744973;
O00487; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-722193, EBI-10175124;
O00487; P42858: HTT; NbExp=7; IntAct=EBI-722193, EBI-466029;
O00487; P50222: MEOX2; NbExp=3; IntAct=EBI-722193, EBI-748397;
O00487; P51665: PSMD7; NbExp=14; 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.
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; 5VFP; EM; 4.20 A; c=24-310.
PDB; 5VFQ; EM; 4.20 A; c=24-310.
PDB; 5VFR; EM; 4.90 A; c=24-310.
PDB; 5VFS; EM; 3.60 A; c=2-310.
PDB; 5VFT; EM; 7.00 A; c=24-310.
PDB; 5VFU; EM; 5.80 A; c=24-310.
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.
PDB; 6MSB; EM; 3.00 A; c=2-310.
PDB; 6MSD; EM; 3.20 A; c=2-310.
PDB; 6MSE; EM; 3.30 A; c=2-310.
PDB; 6MSG; EM; 3.50 A; c=2-310.
PDB; 6MSH; EM; 3.60 A; c=2-310.
PDB; 6MSJ; EM; 3.30 A; c=2-310.
PDB; 6MSK; EM; 3.20 A; c=2-310.
PDB; 6WJD; EM; 4.80 A; c=2-310.
PDB; 6WJN; EM; 5.70 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; 5VFP; -.
PDBsum; 5VFQ; -.
PDBsum; 5VFR; -.
PDBsum; 5VFS; -.
PDBsum; 5VFT; -.
PDBsum; 5VFU; -.
PDBsum; 5VGZ; -.
PDBsum; 5VHF; -.
PDBsum; 5VHH; -.
PDBsum; 5VHI; -.
PDBsum; 5VHS; -.
PDBsum; 6MSB; -.
PDBsum; 6MSD; -.
PDBsum; 6MSE; -.
PDBsum; 6MSG; -.
PDBsum; 6MSH; -.
PDBsum; 6MSJ; -.
PDBsum; 6MSK; -.
PDBsum; 6WJD; -.
PDBsum; 6WJN; -.
SMR; O00487; -.
BioGRID; 115508; 437.
ComplexPortal; CPX-5993; 26S Proteasome complex.
CORUM; O00487; -.
IntAct; O00487; 87.
MINT; O00487; -.
STRING; 9606.ENSP00000386541; -.
BindingDB; O00487; -.
ChEMBL; CHEMBL2007629; -.
MEROPS; M67.A10; -.
GlyGen; O00487; 1 site, 2 O-linked glycans (1 site).
iPTMnet; O00487; -.
MetOSite; O00487; -.
PhosphoSitePlus; O00487; -.
SwissPalm; O00487; -.
BioMuta; PSMD14; -.
OGP; O00487; -.
REPRODUCTION-2DPAGE; IPI00024821; -.
EPD; O00487; -.
jPOST; O00487; -.
MassIVE; O00487; -.
MaxQB; O00487; -.
PaxDb; O00487; -.
PeptideAtlas; O00487; -.
PRIDE; O00487; -.
ProteomicsDB; 47932; -.
TopDownProteomics; O00487; -.
Antibodypedia; 1047; 256 antibodies from 34 providers.
DNASU; 10213; -.
Ensembl; ENST00000409682; ENSP00000386541; ENSG00000115233.
GeneID; 10213; -.
KEGG; hsa:10213; -.
MANE-Select; ENST00000409682.8; ENSP00000386541.3; NM_005805.6; NP_005796.1.
UCSC; uc002ubu.4; human.
CTD; 10213; -.
DisGeNET; 10213; -.
GeneCards; PSMD14; -.
HGNC; HGNC:16889; PSMD14.
HPA; ENSG00000115233; Low tissue specificity.
MIM; 607173; gene.
neXtProt; NX_O00487; -.
OpenTargets; ENSG00000115233; -.
PharmGKB; PA134957776; -.
VEuPathDB; HostDB:ENSG00000115233; -.
eggNOG; KOG1555; Eukaryota.
GeneTree; ENSGT00730000111116; -.
HOGENOM; CLU_052991_0_1_1; -.
InParanoid; O00487; -.
OMA; VFQTRMM; -.
OrthoDB; 1031881at2759; -.
PhylomeDB; O00487; -.
TreeFam; TF105748; -.
PathwayCommons; O00487; -.
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-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 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-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
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-8932339; ROS sensing by NFE2L2.
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-9020702; Interleukin-1 signaling.
Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; O00487; -.
SIGNOR; O00487; -.
BioGRID-ORCS; 10213; 784 hits in 1053 CRISPR screens.
ChiTaRS; PSMD14; human.
GeneWiki; PSMD14; -.
GenomeRNAi; 10213; -.
Pharos; O00487; Tbio.
PRO; PR:O00487; -.
Proteomes; UP000005640; Chromosome 2.
RNAct; O00487; protein.
Bgee; ENSG00000115233; Expressed in deltoid and 249 other tissues.
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: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; HDA: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:0070122; F:isopeptidase activity; IEA:InterPro.
GO; GO:0061578; F:Lys63-specific deubiquitinase activity; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0140492; F:metal-dependent deubiquitinase activity; IMP:UniProtKB.
GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
GO; GO:0004843; F:thiol-dependent deubiquitinase; IBA:GO_Central.
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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
GO; GO:0070536; P:protein K63-linked deubiquitination; IMP:UniProtKB.
GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IMP:UniProtKB.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:UniProtKB.
InterPro; IPR000555; JAMM/MPN+_dom.
InterPro; IPR037518; MPN.
InterPro; IPR035299; PSMD14.
InterPro; IPR024969; Rpn11/EIF3F_C.
PANTHER; PTHR10410:SF22; PTHR10410:SF22; 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; Direct protein sequencing; DNA damage; DNA repair; Hydrolase;
Metal-binding; Metalloprotease; Phosphoprotein; Protease; Proteasome;
Reference proteome; Ubl conjugation pathway; Zinc.
CHAIN 1..310
/note="26S proteasome non-ATPase regulatory subunit 14"
/id="PRO_0000213952"
DOMAIN 31..166
/note="MPN"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
MOTIF 113..126
/note="JAMM motif"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
METAL 113
/note="Zinc; catalytic"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
METAL 115
/note="Zinc; catalytic"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
METAL 126
/note="Zinc; catalytic"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
MOD_RES 150
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17693683,
ECO:0007744|PubMed:24275569"
MOD_RES 224
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17323924"
MOD_RES 266
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:23186163"
MUTAGEN 113..115
/note="HSH->ASA: Abolishes ubiquitin thioesterase activity,
leading to prevent maintenance of JMJD2A/KDM4A on
chromatin."
/evidence="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


Related products :

Catalog number Product name Quantity
EIAAB32809 26S proteasome non-ATPase regulatory subunit 14,26S proteasome regulatory subunit RPN11,26S proteasome-associated PAD1 homolog 1,Homo sapiens,Human,POH1,PSMD14
18-003-42215 26S proteasome non-ATPase regulatory subunit 14 - 26S proteasome regulatory subunit rpn11; 26S proteasome-associated PAD1 homolog 1 Polyclonal 0.05 mg Aff Pur
18-003-42216 26S proteasome non-ATPase regulatory subunit 14 - 26S proteasome regulatory subunit rpn11; 26S proteasome-associated PAD1 homolog 1 Polyclonal 0.1 mg Protein A
EIAAB32810 26S proteasome non-ATPase regulatory subunit 14,26S proteasome regulatory subunit RPN11,MAD1,Mouse,Mus musculus,Pad1,Psmd14
EIAAB32808 26S proteasome non-ATPase regulatory subunit 7,26S proteasome regulatory subunit RPN8,26S proteasome regulatory subunit S12,Homo sapiens,Human,Mov34 protein homolog,MOV34L,Proteasome subunit p40,PSMD7
EIAAB32847 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Bos taurus,Bovine,PSMD2,TRAP2,Tumor necrosis facto
EIAAB32846 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Homo sapiens,Human,Protein 55.11,PSMD2,TRAP2,Tumor
EIAAB32850 26S proteasome non-ATPase regulatory subunit 3,26S proteasome regulatory subunit RPN3,26S proteasome regulatory subunit S3,Mouse,Mus musculus,P91a,Proteasome subunit p58,Psmd3,Transplantation antigen
EIAAB32842 26S proteasome non-ATPase regulatory subunit 1,26S proteasome regulatory subunit RPN2,26S proteasome regulatory subunit S1,26S proteasome subunit p112,Homo sapiens,Human,PSMD1
EIAAB32789 26S proteasome non-ATPase regulatory subunit 11,26S proteasome regulatory subunit p44.5,26S proteasome regulatory subunit RPN6,26S proteasome regulatory subunit S9,Homo sapiens,Human,PSMD11
EIAAB32798 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Homo sapiens,Human,PSMD13
EIAAB32848 26S proteasome non-ATPase regulatory subunit 3,26S proteasome regulatory subunit RPN3,26S proteasome regulatory subunit S3,Homo sapiens,Human,Proteasome subunit p58,PSMD3
EIAAB32841 26S proteasome non-ATPase regulatory subunit 1,26S proteasome regulatory subunit RPN2,26S proteasome regulatory subunit S1,26S proteasome subunit p112,Psmd1,Rat,Rattus norvegicus
EIAAB32858 26S proteasome non-ATPase regulatory subunit 6,26S proteasome regulatory subunit RPN7,26S proteasome regulatory subunit S10,Breast cancer-associated protein SGA-113M,Homo sapiens,Human,KIAA0107,p42A,P
EIAAB32799 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Bos taurus,Bovine,PSMD13
EIAAB32797 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Mouse,Mus musculus,Psmd13
EIAAB32791 26S proteasome non-ATPase regulatory subunit 11,26S proteasome regulatory subunit p44.5,26S proteasome regulatory subunit RPN6,26S proteasome regulatory subunit S9,Mouse,Mus musculus,Psmd11
EIAAB32796 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Psmd13,Rat,Rattus norvegicus
EIAAB32852 26S proteasome non-ATPase regulatory subunit 4,26S proteasome regulatory subunit RPN10,26S proteasome regulatory subunit S5A,Mcb1,Mouse,Multiubiquitin chain-binding protein,Mus musculus,Psmd4
EIAAB32851 26S proteasome non-ATPase regulatory subunit 4,26S proteasome regulatory subunit RPN10,26S proteasome regulatory subunit S5A,AF,Antisecretory factor 1,ASF,Homo sapiens,Human,MCB1,Multiubiquitin chain-
EIAAB32844 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Mouse,Mus musculus,Psmd2
EIAAB32669 26S protease regulatory subunit 8,26S proteasome AAA-ATPase subunit RPT6,p45_SUG,Pig,Proteasome 26S subunit ATPase 5,Proteasome subunit p45,PSMC5,Sus scrofa,Tat-binding protein homolog 10,TBP10
EIAAB32807 26S proteasome non-ATPase regulatory subunit 7,26S proteasome regulatory subunit RPN8,26S proteasome regulatory subunit S12,Mouse,Mov34,Mov-34,Mov34 protein,Mus musculus,Proteasome subunit p40,Psmd7
EIAAB32862 26S proteasome non-ATPase regulatory subunit 8,26S proteasome regulatory subunit RPN12,26S proteasome regulatory subunit S14,Homo sapiens,Human,p31,PSMD8
EIAAB32793 26S proteasome non-ATPase regulatory subunit 12,26S proteasome regulatory subunit p55,26S proteasome regulatory subunit RPN5,Homo sapiens,Human,PSMD12
Pathways :
WP1691: Proteasome
WP470: Proteasome Degradation
WP1079: Proteasome Degradation
WP302: Proteasome Degradation
WP1240: Proteasome Degradation
WP519: Proteasome Degradation
WP158: Proteasome Degradation
WP960: Proteasome Degradation
WP281: Proteasome Degradation
WP1196: Proteasome Degradation
WP841: Proteasome Degradation
WP183: Proteasome Degradation
WP267: Proteasome Degradation
WP1693: Purine metabolism
WP1718: Vitamin B6 metabolism
WP1493: Carbon assimilation C4 pathway
WP731: Sterol regulatory element binding protein related
WP1614: 1- and 2-Methylnaphthalene degradation
WP1909: Signal regulatory protein (SIRP) family interactions
WP2272: Pathogenic Escherichia coli infection
WP1644: DNA replication
WP1671: Methane metabolism
WP1711: Trinitrotoluene degradation
WP1901: Regulatory RNA pathways
WP1634: Butanoate metabolism

Related Genes :
[PSMD14 POH1] 26S proteasome non-ATPase regulatory subunit 14 (EC 3.4.19.-) (26S proteasome regulatory subunit RPN11) (26S proteasome-associated PAD1 homolog 1)
[Psmd14 Pad1] 26S proteasome non-ATPase regulatory subunit 14 (EC 3.4.19.-) (26S proteasome regulatory subunit RPN11) (MAD1)
[rpn11 bfr2 pad1 sks1 SPAC31G5.13] 26S proteasome regulatory subunit rpn11 (Protein pad1)
[RPN11 At5g23540 MQM1.19] 26S proteasome non-ATPase regulatory subunit 14 homolog (EC 3.4.19.-) (26S proteasome regulatory subunit RPN11) (AtRPN11)
[PSMD7 MOV34L] 26S proteasome non-ATPase regulatory subunit 7 (26S proteasome regulatory subunit RPN8) (26S proteasome regulatory subunit S12) (Mov34 protein homolog) (Proteasome subunit p40)
[RPN12A At1g64520 F1N19.9] 26S proteasome non-ATPase regulatory subunit 8 homolog A (26S proteasome regulatory subunit RPN12a) (AtRPN12a) (26S proteasome regulatory subunit S14 homolog A)
[RPT2A HLR At4g29040 F19B15.70 F25O24.6] 26S proteasome regulatory subunit 4 homolog A (26S proteasome AAA-ATPase subunit RPT2a) (26S proteasome subunit 4 homolog A) (Protein HALTED ROOT) (Regulatory particle triple-A ATPase subunit 2a)
[RPN10 MBP1 MCB1 At4g38630 F20M13.190 T9A14.7] 26S proteasome non-ATPase regulatory subunit 4 homolog (26S proteasome regulatory subunit RPN10) (AtRPN10) (26S proteasome regulatory subunit S5A homolog) (Multiubiquitin chain-binding protein 1) (AtMCB1)
[RPT5B TBP1 At1g09100 F7G19.2] 26S proteasome regulatory subunit 6A homolog B (26S proteasome AAA-ATPase subunit RPT5b) (Proteasome 26S subunit 6A homolog B) (Regulatory particle triple-A ATPase subunit 5b) (Tat-binding protein 1 homolog B) (TBP-1 homolog B)
[RPT5A ATS6A.2 TBP1 At3g05530 F22F7.1] 26S proteasome regulatory subunit 6A homolog A (26S proteasome AAA-ATPase subunit RPT5a) (Proteasome 26S subunit 6A homolog A) (Regulatory particle triple-A ATPase subunit 5a) (Tat-binding protein 1 homolog A) (TBP-1 homolog A)
[RPT2B At2g20140 T2G17.6] 26S proteasome regulatory subunit 4 homolog B (26S proteasome AAA-ATPase subunit RPT2b) (26S proteasome subunit 4 homolog B) (Regulatory particle triple-A ATPase subunit 2b)
[RPN8A AE3 MOV34 At5g05780 MJJ3.19] 26S proteasome non-ATPase regulatory subunit 7 homolog A (26S proteasome regulatory subunit RPN8a) (AtRPN8a) (Protein ASYMMETRIC LEAVES ENHANCER 3) (Protein MOV34) (AtMOV34)
[RPN1A At2g20580 F23N11.10] 26S proteasome non-ATPase regulatory subunit 2 homolog A (26S proteasome regulatory subunit RPN1a) (AtRPN1a) (26S proteasome regulatory subunit S2 homolog A)
[RPT3 YNT1 YTA2 YDR394W D9509.14] 26S proteasome regulatory subunit 6B homolog (Protein YNT1) (Tat-binding homolog 2)
[PSMD1] 26S proteasome non-ATPase regulatory subunit 1 (26S proteasome regulatory subunit RPN2) (26S proteasome regulatory subunit S1) (26S proteasome subunit p112)
[PSMC5 SUG1] 26S proteasome regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6) (Proteasome 26S subunit ATPase 5) (Proteasome subunit p45) (Thyroid hormone receptor-interacting protein 1) (TRIP1) (p45/SUG)
[RPT6 CIM3 CRL3 SUG1 TBPY TBY1 YGL048C] 26S proteasome regulatory subunit 8 homolog (Protein CIM3) (Protein SUG1) (Tat-binding protein TBY1)
[RPT1 CIM5 YTA3 YKL145W] 26S proteasome regulatory subunit 7 homolog (Protein CIM5) (Tat-binding homolog 3)
[PSMD4 MCB1] 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Antisecretory factor 1) (AF) (ASF) (Multiubiquitin chain-binding protein)
[PSMC1] 26S proteasome regulatory subunit 4 (P26s4) (26S proteasome AAA-ATPase subunit RPT2) (Proteasome 26S subunit ATPase 1)
[PSMD6 KIAA0107 PFAAP4] 26S proteasome non-ATPase regulatory subunit 6 (26S proteasome regulatory subunit RPN7) (26S proteasome regulatory subunit S10) (Breast cancer-associated protein SGA-113M) (Phosphonoformate immuno-associated protein 4) (Proteasome regulatory particle subunit p44S10) (p42A)
[PSMC3 TBP1] 26S proteasome regulatory subunit 6A (26S proteasome AAA-ATPase subunit RPT5) (Proteasome 26S subunit ATPase 3) (Proteasome subunit P50) (Tat-binding protein 1) (TBP-1)
[PSMD2 TRAP2] 26S proteasome non-ATPase regulatory subunit 2 (26S proteasome regulatory subunit RPN1) (26S proteasome regulatory subunit S2) (26S proteasome subunit p97) (Protein 55.11) (Tumor necrosis factor type 1 receptor-associated protein 2)
[PSMC4 MIP224 TBP7] 26S proteasome regulatory subunit 6B (26S proteasome AAA-ATPase subunit RPT3) (MB67-interacting protein) (MIP224) (Proteasome 26S subunit ATPase 4) (Tat-binding protein 7) (TBP-7)
[Psmc1] 26S proteasome regulatory subunit 4 (P26s4) (26S proteasome AAA-ATPase subunit RPT2) (Proteasome 26S subunit ATPase 1)
[PSMD3] 26S proteasome non-ATPase regulatory subunit 3 (26S proteasome regulatory subunit RPN3) (26S proteasome regulatory subunit S3) (Proteasome subunit p58)
[Psmc5 Sug1] 26S proteasome regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6) (Proteasome 26S subunit ATPase 5) (Proteasome subunit p45) (p45/SUG) (mSUG1)
[PSMD11] 26S proteasome non-ATPase regulatory subunit 11 (26S proteasome regulatory subunit RPN6) (26S proteasome regulatory subunit S9) (26S proteasome regulatory subunit p44.5)
[PSMD13] 26S proteasome non-ATPase regulatory subunit 13 (26S proteasome regulatory subunit RPN9) (26S proteasome regulatory subunit S11) (26S proteasome regulatory subunit p40.5)
[RPT2 YHS4 YTA5 YDL007W D2920] 26S proteasome regulatory subunit 4 homolog (Tat-binding homolog 5)

Bibliography :