Full text data of PSMD14
PSMD14
(POH1)
[Confidence: high (present in two of the MS resources)]
26S proteasome non-ATPase regulatory subunit 14; 3.4.19.- (26S proteasome regulatory subunit RPN11; 26S proteasome-associated PAD1 homolog 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
26S proteasome non-ATPase regulatory subunit 14; 3.4.19.- (26S proteasome regulatory subunit RPN11; 26S proteasome-associated PAD1 homolog 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00024821
IPI00024821 26S proteasome non-ATPase regulatory subunit 14 Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00024821 26S proteasome non-ATPase regulatory subunit 14 Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
O00487
ID PSDE_HUMAN Reviewed; 310 AA.
AC O00487; B3KNW2; O00176;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1997, sequence version 1.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 14;
DE EC=3.4.19.-;
DE AltName: Full=26S proteasome regulatory subunit RPN11;
DE AltName: Full=26S proteasome-associated PAD1 homolog 1;
GN Name=PSMD14; Synonyms=POH1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=9374539; DOI=10.1074/jbc.272.48.30470;
RA Spataro V., Toda T., Craig R., Seeger M., Dubiel W., Harris A.L.,
RA Norbury C.;
RT "Resistance to diverse drugs and ultraviolet light conferred by
RT overexpression of a novel human 26 S proteasome subunit.";
RL J. Biol. Chem. 272:30470-30475(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 199-208, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate
RT reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT Wnt signal transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [8]
RP PROBABLE FUNCTION, AND IDENTIFICATION IN THE PROTEASOME.
RX PubMed=19214193; DOI=10.1038/emboj.2009.27;
RA Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M.,
RA Cohen R.E.;
RT "K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-
RT associated Brcc36 and proteasomal Poh1.";
RL EMBO J. 28:621-631(2009).
RN [9]
RP INTERACTION WITH TXNL1.
RX PubMed=19349277; DOI=10.1074/jbc.M900016200;
RA Andersen K.M., Madsen L., Prag S., Johnsen A.H., Semple C.A.,
RA Hendil K.B., Hartmann-Petersen R.;
RT "Thioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S
RT proteasome.";
RL J. Biol. Chem. 284:15246-15254(2009).
RN [10]
RP IDENTIFICATION BY 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 [11]
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.,
RA Buerckstuemmer T., 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 [12]
RP FUNCTION, IDENTIFICATION IN THE PROTEASOME, AND MUTAGENESIS OF
RP 113-HIS--HIS-115.
RX PubMed=22909820; DOI=10.1038/emboj.2012.232;
RA Butler L.R., Densham R.M., Jia J., Garvin A.J., Stone H.R., Shah V.,
RA Weekes D., Festy F., Beesley J., Morris J.R.;
RT "The proteasomal de-ubiquitinating enzyme POH1 promotes the double-
RT strand DNA break response.";
RL EMBO J. 31:3918-3934(2012).
CC -!- FUNCTION: Metalloprotease component of the 26S proteasome that
CC specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S
CC proteasome is involved in the ATP-dependent degradation of
CC ubiquitinated proteins. Plays a role in response to double-strand
CC breaks (DSBs): acts as a regulator of non-homologous end joining
CC (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby
CC promoting retention of JMJD2A/KDM4A on chromatin and restricting
CC TP53BP1 accumulation. Also involved in homologous recombination
CC repair by promoting RAD51 loading.
CC -!- SUBUNIT: Component of the lid subcomplex of the 19S proteasome
CC regulatory particle complex (also named PA700 complex). The 26S
CC proteasome consists of a 20S proteasome core and two 19S
CC regulatory subunits. Interacts with TXNL1.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest levels in heart and
CC skeletal muscle.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. PSMD14
CC subfamily.
CC -!- SIMILARITY: Contains 1 MPN (JAB/Mov34) domain.
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DR EMBL; U86782; AAC51866.1; -; mRNA.
DR EMBL; AK055128; BAG51474.1; -; mRNA.
DR EMBL; CH471058; EAX11370.1; -; Genomic_DNA.
DR EMBL; BC066336; AAH66336.1; -; mRNA.
DR RefSeq; NP_005796.1; NM_005805.5.
DR UniGene; Hs.740477; -.
DR ProteinModelPortal; O00487; -.
DR SMR; O00487; 26-310.
DR IntAct; O00487; 23.
DR MINT; MINT-5003743; -.
DR STRING; 9606.ENSP00000386541; -.
DR BindingDB; O00487; -.
DR ChEMBL; CHEMBL2007629; -.
DR MEROPS; M67.001; -.
DR PhosphoSite; O00487; -.
DR OGP; O00487; -.
DR REPRODUCTION-2DPAGE; IPI00024821; -.
DR PaxDb; O00487; -.
DR PeptideAtlas; O00487; -.
DR PRIDE; O00487; -.
DR Ensembl; ENST00000409682; ENSP00000386541; ENSG00000115233.
DR GeneID; 10213; -.
DR KEGG; hsa:10213; -.
DR UCSC; uc002ubu.3; human.
DR CTD; 10213; -.
DR GeneCards; GC02P162164; -.
DR HGNC; HGNC:16889; PSMD14.
DR HPA; HPA002114; -.
DR MIM; 607173; gene.
DR neXtProt; NX_O00487; -.
DR PharmGKB; PA134957776; -.
DR eggNOG; COG1310; -.
DR HOGENOM; HOG000183690; -.
DR HOVERGEN; HBG053742; -.
DR InParanoid; O00487; -.
DR KO; K03030; -.
DR OMA; QDPKKHL; -.
DR OrthoDB; EOG7T7GTF; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; PSMD14; -.
DR GenomeRNAi; 10213; -.
DR NextBio; 38668; -.
DR PRO; PR:O00487; -.
DR ArrayExpress; O00487; -.
DR Bgee; O00487; -.
DR CleanEx; HS_PSMD14; -.
DR Genevestigator; O00487; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IMP:UniProtKB.
DR GO; GO:0061133; F:endopeptidase activator activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; TAS:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
DR GO; GO:0004221; F:ubiquitin thiolesterase activity; IMP:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR000555; JAB_MPN_dom.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; DNA damage; DNA repair;
KW Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Proteasome; Reference proteome; Ubl conjugation pathway; Zinc.
FT CHAIN 1 310 26S proteasome non-ATPase regulatory
FT subunit 14.
FT /FTId=PRO_0000213952.
FT DOMAIN 26 139 MPN.
FT MOTIF 113 126 JAMM motif.
FT METAL 113 113 Zinc; catalytic (Probable).
FT METAL 115 115 Zinc; catalytic (Probable).
FT METAL 126 126 Zinc; catalytic (By similarity).
FT MOD_RES 150 150 Phosphoserine.
FT MOD_RES 224 224 Phosphoserine.
FT MUTAGEN 113 115 HSH->ASA: Abolishes ubiquitin
FT thiolesterase activity, leading to
FT prevent maintenance of JMJD2A/KDM4A on
FT chromatin.
SQ 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
//
ID PSDE_HUMAN Reviewed; 310 AA.
AC O00487; B3KNW2; O00176;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1997, sequence version 1.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 14;
DE EC=3.4.19.-;
DE AltName: Full=26S proteasome regulatory subunit RPN11;
DE AltName: Full=26S proteasome-associated PAD1 homolog 1;
GN Name=PSMD14; Synonyms=POH1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=9374539; DOI=10.1074/jbc.272.48.30470;
RA Spataro V., Toda T., Craig R., Seeger M., Dubiel W., Harris A.L.,
RA Norbury C.;
RT "Resistance to diverse drugs and ultraviolet light conferred by
RT overexpression of a novel human 26 S proteasome subunit.";
RL J. Biol. Chem. 272:30470-30475(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 199-208, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate
RT reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT Wnt signal transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [8]
RP PROBABLE FUNCTION, AND IDENTIFICATION IN THE PROTEASOME.
RX PubMed=19214193; DOI=10.1038/emboj.2009.27;
RA Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M.,
RA Cohen R.E.;
RT "K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-
RT associated Brcc36 and proteasomal Poh1.";
RL EMBO J. 28:621-631(2009).
RN [9]
RP INTERACTION WITH TXNL1.
RX PubMed=19349277; DOI=10.1074/jbc.M900016200;
RA Andersen K.M., Madsen L., Prag S., Johnsen A.H., Semple C.A.,
RA Hendil K.B., Hartmann-Petersen R.;
RT "Thioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S
RT proteasome.";
RL J. Biol. Chem. 284:15246-15254(2009).
RN [10]
RP IDENTIFICATION BY 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 [11]
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.,
RA Buerckstuemmer T., 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 [12]
RP FUNCTION, IDENTIFICATION IN THE PROTEASOME, AND MUTAGENESIS OF
RP 113-HIS--HIS-115.
RX PubMed=22909820; DOI=10.1038/emboj.2012.232;
RA Butler L.R., Densham R.M., Jia J., Garvin A.J., Stone H.R., Shah V.,
RA Weekes D., Festy F., Beesley J., Morris J.R.;
RT "The proteasomal de-ubiquitinating enzyme POH1 promotes the double-
RT strand DNA break response.";
RL EMBO J. 31:3918-3934(2012).
CC -!- FUNCTION: Metalloprotease component of the 26S proteasome that
CC specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S
CC proteasome is involved in the ATP-dependent degradation of
CC ubiquitinated proteins. Plays a role in response to double-strand
CC breaks (DSBs): acts as a regulator of non-homologous end joining
CC (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby
CC promoting retention of JMJD2A/KDM4A on chromatin and restricting
CC TP53BP1 accumulation. Also involved in homologous recombination
CC repair by promoting RAD51 loading.
CC -!- SUBUNIT: Component of the lid subcomplex of the 19S proteasome
CC regulatory particle complex (also named PA700 complex). The 26S
CC proteasome consists of a 20S proteasome core and two 19S
CC regulatory subunits. Interacts with TXNL1.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest levels in heart and
CC skeletal muscle.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. PSMD14
CC subfamily.
CC -!- SIMILARITY: Contains 1 MPN (JAB/Mov34) domain.
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DR EMBL; U86782; AAC51866.1; -; mRNA.
DR EMBL; AK055128; BAG51474.1; -; mRNA.
DR EMBL; CH471058; EAX11370.1; -; Genomic_DNA.
DR EMBL; BC066336; AAH66336.1; -; mRNA.
DR RefSeq; NP_005796.1; NM_005805.5.
DR UniGene; Hs.740477; -.
DR ProteinModelPortal; O00487; -.
DR SMR; O00487; 26-310.
DR IntAct; O00487; 23.
DR MINT; MINT-5003743; -.
DR STRING; 9606.ENSP00000386541; -.
DR BindingDB; O00487; -.
DR ChEMBL; CHEMBL2007629; -.
DR MEROPS; M67.001; -.
DR PhosphoSite; O00487; -.
DR OGP; O00487; -.
DR REPRODUCTION-2DPAGE; IPI00024821; -.
DR PaxDb; O00487; -.
DR PeptideAtlas; O00487; -.
DR PRIDE; O00487; -.
DR Ensembl; ENST00000409682; ENSP00000386541; ENSG00000115233.
DR GeneID; 10213; -.
DR KEGG; hsa:10213; -.
DR UCSC; uc002ubu.3; human.
DR CTD; 10213; -.
DR GeneCards; GC02P162164; -.
DR HGNC; HGNC:16889; PSMD14.
DR HPA; HPA002114; -.
DR MIM; 607173; gene.
DR neXtProt; NX_O00487; -.
DR PharmGKB; PA134957776; -.
DR eggNOG; COG1310; -.
DR HOGENOM; HOG000183690; -.
DR HOVERGEN; HBG053742; -.
DR InParanoid; O00487; -.
DR KO; K03030; -.
DR OMA; QDPKKHL; -.
DR OrthoDB; EOG7T7GTF; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; PSMD14; -.
DR GenomeRNAi; 10213; -.
DR NextBio; 38668; -.
DR PRO; PR:O00487; -.
DR ArrayExpress; O00487; -.
DR Bgee; O00487; -.
DR CleanEx; HS_PSMD14; -.
DR Genevestigator; O00487; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IMP:UniProtKB.
DR GO; GO:0061133; F:endopeptidase activator activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; TAS:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
DR GO; GO:0004221; F:ubiquitin thiolesterase activity; IMP:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR000555; JAB_MPN_dom.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; DNA damage; DNA repair;
KW Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Proteasome; Reference proteome; Ubl conjugation pathway; Zinc.
FT CHAIN 1 310 26S proteasome non-ATPase regulatory
FT subunit 14.
FT /FTId=PRO_0000213952.
FT DOMAIN 26 139 MPN.
FT MOTIF 113 126 JAMM motif.
FT METAL 113 113 Zinc; catalytic (Probable).
FT METAL 115 115 Zinc; catalytic (Probable).
FT METAL 126 126 Zinc; catalytic (By similarity).
FT MOD_RES 150 150 Phosphoserine.
FT MOD_RES 224 224 Phosphoserine.
FT MUTAGEN 113 115 HSH->ASA: Abolishes ubiquitin
FT thiolesterase activity, leading to
FT prevent maintenance of JMJD2A/KDM4A on
FT chromatin.
SQ 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
//
MIM
607173
*RECORD*
*FIELD* NO
607173
*FIELD* TI
*607173 PROTEASOME 26S SUBUNIT, NON-ATPase, 14; PSMD14
;;PAD1, YEAST, HOMOLOG OF;;
read more26S PROTEASOME-ASSOCIATED PAD1 HOMOLOG; POH1
*FIELD* TX
DESCRIPTION
PSMD14 is a component of the 26S proteasome, a multiprotein complex that
degrades proteins targeted for destruction by the ubiquitin pathway
(Spataro et al., 1997).
CLONING
Spataro et al. (1997) cloned POH1 from a Basinger human fibroblast cDNA
library. The predicted 310-amino acid POH1 protein shares 68% identity
with fission yeast Pad1 and is also related to JAB1 (604850) and the
S12/p40 component of the 26S proteasome regulatory subunit (PSMD7;
157970). Northern blot analysis detected a 1.7-kb POH1 transcript in a
wide variety of human tissues, with the highest levels in heart and
skeletal muscle. By immunoblot analysis, Spataro et al. (1997) showed
that POH1 is a component of the 19S regulatory cap of the 26S
proteasome.
GENE FUNCTION
By transfection experiments and immunoblot analysis, Spataro et al.
(1997) showed that POH1 can substitute fully for Pad1(+) and induce AP1
(see 165160)-dependent drug resistance in fission yeast. Further,
transient overproduction of POH1 in COS-1 cells induced a distinctive
pattern of multidrug resistance in mammalian cells and moderate
resistance to ultraviolet light.
Yao and Cohen (2002) reported that the POH1 subunit of the 19S complex
is responsible for substrate deubiquitination during proteasomal
degradation. The inability to remove ubiquitin can be rate-limiting for
degradation in vitro and is lethal to yeast. Unlike all other
deubiquitinating enzymes, which are cysteine proteases, POH1 appears to
be a zinc-dependent protease.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PSMD14
gene to chromosome 2 (TMAP stSG44142).
*FIELD* RF
1. 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. Yao, T.; Cohen, R. E.: A cryptic protease couples deubiquitination
and degradation by the proteasome. Nature 419: 403-407, 2002.
*FIELD* CN
Ada Hamosh - updated: 9/10/2002
*FIELD* CD
Joanna S. Amberger: 8/27/2002
*FIELD* ED
wwang: 10/17/2006
carol: 11/8/2002
alopez: 9/11/2002
tkritzer: 9/10/2002
mgross: 8/30/2002
joanna: 8/28/2002
*RECORD*
*FIELD* NO
607173
*FIELD* TI
*607173 PROTEASOME 26S SUBUNIT, NON-ATPase, 14; PSMD14
;;PAD1, YEAST, HOMOLOG OF;;
read more26S PROTEASOME-ASSOCIATED PAD1 HOMOLOG; POH1
*FIELD* TX
DESCRIPTION
PSMD14 is a component of the 26S proteasome, a multiprotein complex that
degrades proteins targeted for destruction by the ubiquitin pathway
(Spataro et al., 1997).
CLONING
Spataro et al. (1997) cloned POH1 from a Basinger human fibroblast cDNA
library. The predicted 310-amino acid POH1 protein shares 68% identity
with fission yeast Pad1 and is also related to JAB1 (604850) and the
S12/p40 component of the 26S proteasome regulatory subunit (PSMD7;
157970). Northern blot analysis detected a 1.7-kb POH1 transcript in a
wide variety of human tissues, with the highest levels in heart and
skeletal muscle. By immunoblot analysis, Spataro et al. (1997) showed
that POH1 is a component of the 19S regulatory cap of the 26S
proteasome.
GENE FUNCTION
By transfection experiments and immunoblot analysis, Spataro et al.
(1997) showed that POH1 can substitute fully for Pad1(+) and induce AP1
(see 165160)-dependent drug resistance in fission yeast. Further,
transient overproduction of POH1 in COS-1 cells induced a distinctive
pattern of multidrug resistance in mammalian cells and moderate
resistance to ultraviolet light.
Yao and Cohen (2002) reported that the POH1 subunit of the 19S complex
is responsible for substrate deubiquitination during proteasomal
degradation. The inability to remove ubiquitin can be rate-limiting for
degradation in vitro and is lethal to yeast. Unlike all other
deubiquitinating enzymes, which are cysteine proteases, POH1 appears to
be a zinc-dependent protease.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PSMD14
gene to chromosome 2 (TMAP stSG44142).
*FIELD* RF
1. 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. Yao, T.; Cohen, R. E.: A cryptic protease couples deubiquitination
and degradation by the proteasome. Nature 419: 403-407, 2002.
*FIELD* CN
Ada Hamosh - updated: 9/10/2002
*FIELD* CD
Joanna S. Amberger: 8/27/2002
*FIELD* ED
wwang: 10/17/2006
carol: 11/8/2002
alopez: 9/11/2002
tkritzer: 9/10/2002
mgross: 8/30/2002
joanna: 8/28/2002