Full text data of PSMD13
PSMD13
[Confidence: low (only semi-automatic identification from reviews)]
26S proteasome non-ATPase regulatory subunit 13 (26S proteasome regulatory subunit RPN9; 26S proteasome regulatory subunit S11; 26S proteasome regulatory subunit p40.5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
26S proteasome non-ATPase regulatory subunit 13 (26S proteasome regulatory subunit RPN9; 26S proteasome regulatory subunit S11; 26S proteasome regulatory subunit p40.5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UNM6
ID PSD13_HUMAN Reviewed; 376 AA.
AC Q9UNM6; B3KT15; O75831; Q53XU2; Q9UNV3;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 2.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 13;
DE AltName: Full=26S proteasome regulatory subunit RPN9;
DE AltName: Full=26S proteasome regulatory subunit S11;
DE AltName: Full=26S proteasome regulatory subunit p40.5;
GN Name=PSMD13;
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] (ISOFORM 1).
RX PubMed=9714768; DOI=10.1016/S0378-1119(98)00309-6;
RA Hori T., Kato S., Saeki M., DeMartino G.N., Slaughter C.A.,
RA Takeuchi J., Toh-e A., Tanaka K.;
RT "cDNA cloning and functional analysis of p28 (Nas6p) and p40.5
RT (Nas7p), two novel regulatory subunits of the 26S proteasome.";
RL Gene 216:113-122(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-13.
RC TISSUE=Liver;
RA Ting M.C., Chang L.Y.;
RT "Cloning of the human 26S proteasome subunit p40.5.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-13.
RX PubMed=10225435; DOI=10.1016/S0014-5793(99)00403-2;
RA Hoffman L., Gorbea C., Rechsteiner M.;
RT "Identification, molecular cloning, and characterization of subunit 11
RT of the human 26S proteasome.";
RL FEBS Lett. 449:88-92(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP SER-13.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-13.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-13.
RC TISSUE=Kidney, and Lung;
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-298, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [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).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] SER-13, AND MASS 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).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which
CC is involved in the ATP-dependent degradation of ubiquitinated
CC proteins.
CC -!- SUBUNIT: Component of the PA700 complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UNM6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UNM6-2; Sequence=VSP_041067;
CC -!- SIMILARITY: Belongs to the proteasome subunit S11 family.
CC -!- SIMILARITY: Contains 1 PCI domain.
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DR EMBL; AB009398; BAA33214.1; -; mRNA.
DR EMBL; AF107837; AAD43442.1; -; mRNA.
DR EMBL; AF086708; AAC64104.1; -; mRNA.
DR EMBL; BT007307; AAP35971.1; -; mRNA.
DR EMBL; AK094775; BAG52927.1; -; mRNA.
DR EMBL; AC136475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471278; EAW61234.1; -; Genomic_DNA.
DR EMBL; BC001100; AAH01100.1; -; mRNA.
DR EMBL; BC001747; AAH01747.1; -; mRNA.
DR RefSeq; NP_002808.3; NM_002817.3.
DR RefSeq; NP_787128.2; NM_175932.2.
DR UniGene; Hs.134688; -.
DR ProteinModelPortal; Q9UNM6; -.
DR SMR; Q9UNM6; 16-331.
DR DIP; DIP-27576N; -.
DR IntAct; Q9UNM6; 11.
DR MINT; MINT-1161305; -.
DR STRING; 9606.ENSP00000396937; -.
DR PhosphoSite; Q9UNM6; -.
DR DMDM; 20978558; -.
DR PaxDb; Q9UNM6; -.
DR PRIDE; Q9UNM6; -.
DR DNASU; 5719; -.
DR Ensembl; ENST00000431206; ENSP00000396937; ENSG00000185627.
DR Ensembl; ENST00000532097; ENSP00000436186; ENSG00000185627.
DR GeneID; 5719; -.
DR KEGG; hsa:5719; -.
DR UCSC; uc001lol.2; human.
DR CTD; 5719; -.
DR GeneCards; GC11P000226; -.
DR H-InvDB; HIX0009340; -.
DR HGNC; HGNC:9558; PSMD13.
DR HPA; HPA038692; -.
DR MIM; 603481; gene.
DR neXtProt; NX_Q9UNM6; -.
DR PharmGKB; PA33904; -.
DR eggNOG; NOG272621; -.
DR HOGENOM; HOG000216633; -.
DR HOVERGEN; HBG053740; -.
DR InParanoid; Q9UNM6; -.
DR KO; K03039; -.
DR OMA; EQEQHAF; -.
DR OrthoDB; EOG7C5M8X; -.
DR PhylomeDB; Q9UNM6; -.
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 ChiTaRS; PSMD13; human.
DR GeneWiki; PSMD13; -.
DR GenomeRNAi; 5719; -.
DR NextBio; 22226; -.
DR PRO; PR:Q9UNM6; -.
DR ArrayExpress; Q9UNM6; -.
DR Bgee; Q9UNM6; -.
DR CleanEx; HS_PSMD13; -.
DR Genevestigator; Q9UNM6; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005838; C:proteasome regulatory particle; TAS:ProtInc.
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:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0007127; P:meiosis I; IEA:Ensembl.
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:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR000717; PCI_dom.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Polymorphism;
KW Proteasome; Reference proteome.
FT CHAIN 1 376 26S proteasome non-ATPase regulatory
FT subunit 13.
FT /FTId=PRO_0000173867.
FT DOMAIN 239 335 PCI.
FT MOD_RES 298 298 N6-acetyllysine.
FT VAR_SEQ 32 69 KLWHQLTLQVLDFVQDPCFAQGDGLIKLYENFISEFEH ->
FT NFMKTLSVNLNTGKSLSSVFHFENECIDARRCSKAGGFYF
FT (in isoform 2).
FT /FTId=VSP_041067.
FT VARIANT 13 13 N -> S (in dbSNP:rs1045288).
FT /FTId=VAR_024591.
FT VARIANT 150 150 S -> L (in dbSNP:rs28927679).
FT /FTId=VAR_057050.
FT VARIANT 204 204 G -> E (in dbSNP:rs1794108).
FT /FTId=VAR_031094.
FT VARIANT 205 205 L -> F (in dbSNP:rs1794109).
FT /FTId=VAR_031095.
FT CONFLICT 253 253 T -> I (in Ref. 3; AAC64104).
SQ SEQUENCE 376 AA; 42945 MW; E96C99A49CAC5ED3 CRC64;
MKDVPGFLQQ SQNSGPGQPA VWHRLEELYT KKLWHQLTLQ VLDFVQDPCF AQGDGLIKLY
ENFISEFEHR VNPLSLVEII LHVVRQMTDP NVALTFLEKT REKVKSSDEA VILCKTAIGA
LKLNIGDLQV TKETIEDVEE MLNNLPGVTS VHSRFYDLSS KYYQTIGNHA SYYKDALRFL
GCVDIKDLPV SEQQERAFTL GLAGLLGEGV FNFGELLMHP VLESLRNTDR QWLIDTLYAF
NSGNVERFQT LKTAWGQQPD LAANEAQLLR KIQLLCLMEM TFTRPANHRQ LTFEEIAKSA
KITVNEVELL VMKALSVGLV KGSIDEVDKR VHMTWVQPRV LDLQQIKGMK DRLEFWCTDV
KSMEMLVEHQ AHDILT
//
ID PSD13_HUMAN Reviewed; 376 AA.
AC Q9UNM6; B3KT15; O75831; Q53XU2; Q9UNV3;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 2.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 13;
DE AltName: Full=26S proteasome regulatory subunit RPN9;
DE AltName: Full=26S proteasome regulatory subunit S11;
DE AltName: Full=26S proteasome regulatory subunit p40.5;
GN Name=PSMD13;
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] (ISOFORM 1).
RX PubMed=9714768; DOI=10.1016/S0378-1119(98)00309-6;
RA Hori T., Kato S., Saeki M., DeMartino G.N., Slaughter C.A.,
RA Takeuchi J., Toh-e A., Tanaka K.;
RT "cDNA cloning and functional analysis of p28 (Nas6p) and p40.5
RT (Nas7p), two novel regulatory subunits of the 26S proteasome.";
RL Gene 216:113-122(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-13.
RC TISSUE=Liver;
RA Ting M.C., Chang L.Y.;
RT "Cloning of the human 26S proteasome subunit p40.5.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-13.
RX PubMed=10225435; DOI=10.1016/S0014-5793(99)00403-2;
RA Hoffman L., Gorbea C., Rechsteiner M.;
RT "Identification, molecular cloning, and characterization of subunit 11
RT of the human 26S proteasome.";
RL FEBS Lett. 449:88-92(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP SER-13.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-13.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-13.
RC TISSUE=Kidney, and Lung;
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-298, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [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).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] SER-13, AND MASS 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).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which
CC is involved in the ATP-dependent degradation of ubiquitinated
CC proteins.
CC -!- SUBUNIT: Component of the PA700 complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UNM6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UNM6-2; Sequence=VSP_041067;
CC -!- SIMILARITY: Belongs to the proteasome subunit S11 family.
CC -!- SIMILARITY: Contains 1 PCI domain.
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DR EMBL; AB009398; BAA33214.1; -; mRNA.
DR EMBL; AF107837; AAD43442.1; -; mRNA.
DR EMBL; AF086708; AAC64104.1; -; mRNA.
DR EMBL; BT007307; AAP35971.1; -; mRNA.
DR EMBL; AK094775; BAG52927.1; -; mRNA.
DR EMBL; AC136475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471278; EAW61234.1; -; Genomic_DNA.
DR EMBL; BC001100; AAH01100.1; -; mRNA.
DR EMBL; BC001747; AAH01747.1; -; mRNA.
DR RefSeq; NP_002808.3; NM_002817.3.
DR RefSeq; NP_787128.2; NM_175932.2.
DR UniGene; Hs.134688; -.
DR ProteinModelPortal; Q9UNM6; -.
DR SMR; Q9UNM6; 16-331.
DR DIP; DIP-27576N; -.
DR IntAct; Q9UNM6; 11.
DR MINT; MINT-1161305; -.
DR STRING; 9606.ENSP00000396937; -.
DR PhosphoSite; Q9UNM6; -.
DR DMDM; 20978558; -.
DR PaxDb; Q9UNM6; -.
DR PRIDE; Q9UNM6; -.
DR DNASU; 5719; -.
DR Ensembl; ENST00000431206; ENSP00000396937; ENSG00000185627.
DR Ensembl; ENST00000532097; ENSP00000436186; ENSG00000185627.
DR GeneID; 5719; -.
DR KEGG; hsa:5719; -.
DR UCSC; uc001lol.2; human.
DR CTD; 5719; -.
DR GeneCards; GC11P000226; -.
DR H-InvDB; HIX0009340; -.
DR HGNC; HGNC:9558; PSMD13.
DR HPA; HPA038692; -.
DR MIM; 603481; gene.
DR neXtProt; NX_Q9UNM6; -.
DR PharmGKB; PA33904; -.
DR eggNOG; NOG272621; -.
DR HOGENOM; HOG000216633; -.
DR HOVERGEN; HBG053740; -.
DR InParanoid; Q9UNM6; -.
DR KO; K03039; -.
DR OMA; EQEQHAF; -.
DR OrthoDB; EOG7C5M8X; -.
DR PhylomeDB; Q9UNM6; -.
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 ChiTaRS; PSMD13; human.
DR GeneWiki; PSMD13; -.
DR GenomeRNAi; 5719; -.
DR NextBio; 22226; -.
DR PRO; PR:Q9UNM6; -.
DR ArrayExpress; Q9UNM6; -.
DR Bgee; Q9UNM6; -.
DR CleanEx; HS_PSMD13; -.
DR Genevestigator; Q9UNM6; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005838; C:proteasome regulatory particle; TAS:ProtInc.
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:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0007127; P:meiosis I; IEA:Ensembl.
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:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR000717; PCI_dom.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Polymorphism;
KW Proteasome; Reference proteome.
FT CHAIN 1 376 26S proteasome non-ATPase regulatory
FT subunit 13.
FT /FTId=PRO_0000173867.
FT DOMAIN 239 335 PCI.
FT MOD_RES 298 298 N6-acetyllysine.
FT VAR_SEQ 32 69 KLWHQLTLQVLDFVQDPCFAQGDGLIKLYENFISEFEH ->
FT NFMKTLSVNLNTGKSLSSVFHFENECIDARRCSKAGGFYF
FT (in isoform 2).
FT /FTId=VSP_041067.
FT VARIANT 13 13 N -> S (in dbSNP:rs1045288).
FT /FTId=VAR_024591.
FT VARIANT 150 150 S -> L (in dbSNP:rs28927679).
FT /FTId=VAR_057050.
FT VARIANT 204 204 G -> E (in dbSNP:rs1794108).
FT /FTId=VAR_031094.
FT VARIANT 205 205 L -> F (in dbSNP:rs1794109).
FT /FTId=VAR_031095.
FT CONFLICT 253 253 T -> I (in Ref. 3; AAC64104).
SQ SEQUENCE 376 AA; 42945 MW; E96C99A49CAC5ED3 CRC64;
MKDVPGFLQQ SQNSGPGQPA VWHRLEELYT KKLWHQLTLQ VLDFVQDPCF AQGDGLIKLY
ENFISEFEHR VNPLSLVEII LHVVRQMTDP NVALTFLEKT REKVKSSDEA VILCKTAIGA
LKLNIGDLQV TKETIEDVEE MLNNLPGVTS VHSRFYDLSS KYYQTIGNHA SYYKDALRFL
GCVDIKDLPV SEQQERAFTL GLAGLLGEGV FNFGELLMHP VLESLRNTDR QWLIDTLYAF
NSGNVERFQT LKTAWGQQPD LAANEAQLLR KIQLLCLMEM TFTRPANHRQ LTFEEIAKSA
KITVNEVELL VMKALSVGLV KGSIDEVDKR VHMTWVQPRV LDLQQIKGMK DRLEFWCTDV
KSMEMLVEHQ AHDILT
//
MIM
603481
*RECORD*
*FIELD* NO
603481
*FIELD* TI
*603481 PROTEASOME 26S SUBUNIT, NON-ATPase, 13; PSMD13
;;p40.5;;
PROTEASE 26S, SUBUNIT 11; S11
read more*FIELD* TX
Ubiquitinated proteins are degraded by a 26S ATP-dependent protease. The
protease is composed of a 20S catalytic proteasome and PA700, a 700-kD
regulatory complex (see PSMC1; 602706).
Hori et al. (1998) determined the partial protein sequences of bovine
p28 (PSMD10; 603480) and p40.5, 2 components of PA700. By searching a
sequence database, they identified cDNAs encoding the human p28 and
p40.5 homologs. The predicted human p40.5 protein contains 376 amino
acids and has a molecular mass of 43 kD. Using computerized homology
searches, Hori et al. (1998) identified Nas7, an S. cerevisiae gene
encoding a protein with 31% identity to p40.5. They disrupted the Nas7
gene and found that Nas7-deficient yeast cells were sensitive to heat
stress. Northern blot analysis revealed that p40.5 was expressed as a
1.3-kb mRNA in all human tissues tested.
By sequencing peptides obtained from purified 26S proteasome subunits,
followed by database analysis and PCR of human myeloblast cell line RNA,
Hoffman et al. (1999) cloned the PSMD13 gene, which they called subunit
11 (S11). The deduced 376-amino acid protein has a calculated molecular
mass of 42.9 kD, and it shares 97% identity with mouse S11. Western blot
analysis detected S11 at about 43 kD.
By Far Western blot analysis, Hoffman et al. (1999) determined that S11
bound the 26S proteasome and the 19S regulatory complex, but not the 20S
proteasome.
The International Radiation Hybrid Mapping Consortium mapped the PSMD13
gene to chromosome 11 (TMAP STS-T99644).
*FIELD* RF
1. Hoffman, L.; Gorbea, C.; Rechsteiner, M.: Identification, molecular
cloning, and characterization of subunit 11 of the human 26S proteasome. FEBS
Lett. 449: 88-92, 1999.
2. Hori, T.; Kato, S.; Saeki, M.; DeMartino, G. N.; Slaughter, C.
A.; Takeuchi, J.; Toh-e, A.; Tanaka, K.: cDNA cloning and functional
analysis of p28 (Nas6p) and p40.5 (Nas7p), two novel regulatory subunits
of the 26S proteasome. Gene 216: 113-122, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 2/8/2006
*FIELD* CD
Rebekah S. Rasooly: 2/3/1999
*FIELD* ED
carol: 05/19/2008
wwang: 3/3/2006
wwang: 2/14/2006
terry: 2/8/2006
alopez: 2/3/1999
*RECORD*
*FIELD* NO
603481
*FIELD* TI
*603481 PROTEASOME 26S SUBUNIT, NON-ATPase, 13; PSMD13
;;p40.5;;
PROTEASE 26S, SUBUNIT 11; S11
read more*FIELD* TX
Ubiquitinated proteins are degraded by a 26S ATP-dependent protease. The
protease is composed of a 20S catalytic proteasome and PA700, a 700-kD
regulatory complex (see PSMC1; 602706).
Hori et al. (1998) determined the partial protein sequences of bovine
p28 (PSMD10; 603480) and p40.5, 2 components of PA700. By searching a
sequence database, they identified cDNAs encoding the human p28 and
p40.5 homologs. The predicted human p40.5 protein contains 376 amino
acids and has a molecular mass of 43 kD. Using computerized homology
searches, Hori et al. (1998) identified Nas7, an S. cerevisiae gene
encoding a protein with 31% identity to p40.5. They disrupted the Nas7
gene and found that Nas7-deficient yeast cells were sensitive to heat
stress. Northern blot analysis revealed that p40.5 was expressed as a
1.3-kb mRNA in all human tissues tested.
By sequencing peptides obtained from purified 26S proteasome subunits,
followed by database analysis and PCR of human myeloblast cell line RNA,
Hoffman et al. (1999) cloned the PSMD13 gene, which they called subunit
11 (S11). The deduced 376-amino acid protein has a calculated molecular
mass of 42.9 kD, and it shares 97% identity with mouse S11. Western blot
analysis detected S11 at about 43 kD.
By Far Western blot analysis, Hoffman et al. (1999) determined that S11
bound the 26S proteasome and the 19S regulatory complex, but not the 20S
proteasome.
The International Radiation Hybrid Mapping Consortium mapped the PSMD13
gene to chromosome 11 (TMAP STS-T99644).
*FIELD* RF
1. Hoffman, L.; Gorbea, C.; Rechsteiner, M.: Identification, molecular
cloning, and characterization of subunit 11 of the human 26S proteasome. FEBS
Lett. 449: 88-92, 1999.
2. Hori, T.; Kato, S.; Saeki, M.; DeMartino, G. N.; Slaughter, C.
A.; Takeuchi, J.; Toh-e, A.; Tanaka, K.: cDNA cloning and functional
analysis of p28 (Nas6p) and p40.5 (Nas7p), two novel regulatory subunits
of the 26S proteasome. Gene 216: 113-122, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 2/8/2006
*FIELD* CD
Rebekah S. Rasooly: 2/3/1999
*FIELD* ED
carol: 05/19/2008
wwang: 3/3/2006
wwang: 2/14/2006
terry: 2/8/2006
alopez: 2/3/1999