ID   PSDE_HUMAN              Reviewed;         310 AA.
AC   O00487; B3KNW2; O00176;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-JAN-2012, entry version 99.
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   MEDLINE=98043754; 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 TYR-32, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [7]
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   [8]
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   [9]
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   [10]
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).
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. The function of the 'Lys-63'-specific
CC       deubiquitination of the proteasome is unclear.
CC   -!- SUBUNIT: Component of the 19S regulatory cap of the 26S
CC       proteasome.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   IPI; IPI00024821; -.
DR   RefSeq; NP_005796.1; NM_005805.4.
DR   UniGene; Hs.567410; -.
DR   ProteinModelPortal; O00487; -.
DR   SMR; O00487; 31-165.
DR   IntAct; O00487; 21.
DR   STRING; O00487; -.
DR   MEROPS; M67.001; -.
DR   PhosphoSite; O00487; -.
DR   OGP; O00487; -.
DR   REPRODUCTION-2DPAGE; IPI00024821; -.
DR   PeptideAtlas; O00487; -.
DR   PRIDE; O00487; -.
DR   Ensembl; ENST00000409682; ENSP00000386541; ENSG00000115233.
DR   GeneID; 10213; -.
DR   KEGG; hsa:10213; -.
DR   UCSC; uc002ubu.1; human.
DR   CTD; 10213; -.
DR   GeneCards; GC02P162164; -.
DR   H-InvDB; HIX0002542; -.
DR   HGNC; HGNC:16889; PSMD14.
DR   HPA; HPA002114; -.
DR   MIM; 607173; gene.
DR   neXtProt; NX_O00487; -.
DR   PharmGKB; PA134957776; -.
DR   eggNOG; prNOG05900; -.
DR   HOGENOM; HBG499867; -.
DR   HOVERGEN; HBG053742; -.
DR   InParanoid; O00487; -.
DR   OMA; QDPKKHL; -.
DR   OrthoDB; EOG4R23V7; -.
DR   PhylomeDB; O00487; -.
DR   Reactome; REACT_111102; Signal Transduction.
DR   Reactome; REACT_111217; Metabolism.
DR   Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR   Reactome; REACT_152; Cell Cycle, Mitotic.
DR   Reactome; REACT_1538; Cell Cycle Checkpoints.
DR   Reactome; REACT_383; DNA Replication.
DR   Reactome; REACT_578; Apoptosis.
DR   Reactome; REACT_6185; HIV Infection.
DR   Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; REACT_6900; Immune System.
DR   NextBio; 38668; -.
DR   ArrayExpress; O00487; -.
DR   Bgee; O00487; -.
DR   CleanEx; HS_PSMD14; -.
DR   Genevestigator; O00487; -.
DR   GermOnline; ENSG00000115233; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0000502; C:proteasome complex; TAS: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; TAS:UniProtKB.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; 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:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0000216; P:M/G1 transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0016071; P:mRNA metabolic 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; TAS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR   GO; GO:0042981; P:regulation of apoptotic process; 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:0000084; P:S phase of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0016032; P:viral reproduction; TAS:Reactome.
DR   InterPro; IPR000555; Mov34_MPN_PAD1.
DR   KO; K03030; -.
DR   Pfam; PF01398; Mov34; 1.
DR   SMART; SM00232; JAB_MPN; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Hydrolase;
KW   Metal-binding; Metalloprotease; Phosphoprotein; Protease; Proteasome;
KW   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      32     32       Phosphotyrosine.
FT   MOD_RES     150    150       Phosphoserine.
FT   MOD_RES     224    224       Phosphoserine.
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
//