Full text data of PSMD3
PSMD3
[Confidence: high (present in two of the MS resources)]
26S proteasome non-ATPase regulatory subunit 3 (26S proteasome regulatory subunit RPN3; 26S proteasome regulatory subunit S3; Proteasome subunit p58)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
26S proteasome non-ATPase regulatory subunit 3 (26S proteasome regulatory subunit RPN3; 26S proteasome regulatory subunit S3; Proteasome subunit p58)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00011603
IPI00011603 26S proteasome non-ATPase regulatory subunit 3 Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins 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
IPI00011603 26S proteasome non-ATPase regulatory subunit 3 Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins 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
O43242
ID PSMD3_HUMAN Reviewed; 534 AA.
AC O43242; B3KMW9; Q96EI2; Q9BQA4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 3;
DE AltName: Full=26S proteasome regulatory subunit RPN3;
DE AltName: Full=26S proteasome regulatory subunit S3;
DE AltName: Full=Proteasome subunit p58;
GN Name=PSMD3;
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].
RC TISSUE=Hepatoblastoma;
RX PubMed=9017604; DOI=10.1091/mbc.8.1.171;
RA Kominami K., Okura N., Kawamura M., Demartino G.N., Slaughter C.A.,
RA Shimbara N., Chung C.H., Fujimuro M., Yokosawa H., Shimizu Y.,
RA Tanahashi N., Tanaka K., Toh-e A.;
RT "Yeast counterparts of subunits S5a and p58 (S3) of the human 26S
RT proteasome are encoded by two multicopy suppressors of nin1-1.";
RL Mol. Biol. Cell 8:171-187(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, Lung, Pancreas, and Skin;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which
CC is involved in the ATP-dependent degradation of ubiquitinated
CC proteins.
CC -!- SUBUNIT: The 26S proteasome is composed of a core protease, known
CC as the 20S proteasome, capped at one or both ends by the 19S
CC regulatory complex (RC). The RC is composed of at least 18
CC different subunits in two subcomplexes, the base and the lid,
CC which form the portions proximal and distal to the 20S proteolytic
CC core, respectively.
CC -!- SIMILARITY: Belongs to the proteasome subunit S3 family.
CC -!- SIMILARITY: Contains 1 PCI 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; D67025; BAA23651.1; -; mRNA.
DR EMBL; BT007217; AAP35881.1; -; mRNA.
DR EMBL; AK022896; BAG51131.1; -; mRNA.
DR EMBL; CH471152; EAW60625.1; -; Genomic_DNA.
DR EMBL; BC000074; AAH00074.1; -; mRNA.
DR EMBL; BC004859; AAH04859.1; -; mRNA.
DR EMBL; BC012302; AAH12302.1; -; mRNA.
DR EMBL; BC020518; AAH20518.1; -; mRNA.
DR EMBL; BC025686; AAH25686.1; -; mRNA.
DR RefSeq; NP_002800.2; NM_002809.3.
DR UniGene; Hs.12970; -.
DR ProteinModelPortal; O43242; -.
DR SMR; O43242; 226-467.
DR DIP; DIP-27571N; -.
DR IntAct; O43242; 17.
DR MINT; MINT-5003834; -.
DR STRING; 9606.ENSP00000264639; -.
DR PhosphoSite; O43242; -.
DR PaxDb; O43242; -.
DR PeptideAtlas; O43242; -.
DR PRIDE; O43242; -.
DR DNASU; 5709; -.
DR Ensembl; ENST00000264639; ENSP00000264639; ENSG00000108344.
DR GeneID; 5709; -.
DR KEGG; hsa:5709; -.
DR UCSC; uc002htn.2; human.
DR CTD; 5709; -.
DR GeneCards; GC17P038137; -.
DR HGNC; HGNC:9560; PSMD3.
DR HPA; CAB017038; -.
DR neXtProt; NX_O43242; -.
DR PharmGKB; PA38123; -.
DR eggNOG; NOG251646; -.
DR HOGENOM; HOG000193909; -.
DR HOVERGEN; HBG000703; -.
DR InParanoid; O43242; -.
DR KO; K03033; -.
DR OMA; NQVARFL; -.
DR OrthoDB; EOG7JQBNM; -.
DR PhylomeDB; O43242; -.
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; PSMD3; human.
DR GeneWiki; PSMD3; -.
DR GenomeRNAi; 5709; -.
DR NextBio; 22182; -.
DR PRO; PR:O43242; -.
DR ArrayExpress; O43242; -.
DR Bgee; O43242; -.
DR CleanEx; HS_PSMD3; -.
DR Genevestigator; O43242; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
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: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:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR013586; 26S_Psome_reg_C.
DR InterPro; IPR013143; PAM.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF08375; Rpn3_C; 1.
DR SMART; SM00753; PAM; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Proteasome; Reference proteome.
FT CHAIN 1 534 26S proteasome non-ATPase regulatory
FT subunit 3.
FT /FTId=PRO_0000173816.
FT DOMAIN 358 462 PCI.
FT COMPBIAS 26 32 Poly-Pro.
FT CONFLICT 60 60 A -> V (in Ref. 1; BAA23651).
FT CONFLICT 157 158 TP -> NT (in Ref. 5; AAH12302).
FT CONFLICT 304 304 E -> V (in Ref. 5; AAH12302).
SQ SEQUENCE 534 AA; 60978 MW; 3B3FB5593542C078 CRC64;
MKQEGSARRR GADKAKPPPG GGEQEPPPPP APQDVEMKEE AATGGGSTGE ADGKTAAAAA
EHSQRELDTV TLEDIKEHVK QLEKAVSGKE PRFVLRALRM LPSTSRRLNH YVLYKAVQGF
FTSNNATRDF LLPFLEEPMD TEADLQFRPR TGKAASTPLL PEVEAYLQLL VVIFMMNSKR
YKEAQKISDD LMQKISTQNR RALDLVAAKC YYYHARVYEF LDKLDVVRSF LHARLRTATL
RHDADGQATL LNLLLRNYLH YSLYDQAEKL VSKSVFPEQA NNNEWARYLY YTGRIKAIQL
EYSEARRTMT NALRKAPQHT AVGFKQTVHK LLIVVELLLG EIPDRLQFRQ PSLKRSLMPY
FLLTQAVRTG NLAKFNQVLD QFGEKFQADG TYTLIIRLRH NVIKTGVRMI SLSYSRISLA
DIAQKLQLDS PEDAEFIVAK AIRDGVIEAS INHEKGYVQS KEMIDIYSTR EPQLAFHQRI
SFCLDIHNMS VKAMRFPPKS YNKDLESAEE RREREQQDLE FAKEMAEDDD DSFP
//
ID PSMD3_HUMAN Reviewed; 534 AA.
AC O43242; B3KMW9; Q96EI2; Q9BQA4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 3;
DE AltName: Full=26S proteasome regulatory subunit RPN3;
DE AltName: Full=26S proteasome regulatory subunit S3;
DE AltName: Full=Proteasome subunit p58;
GN Name=PSMD3;
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].
RC TISSUE=Hepatoblastoma;
RX PubMed=9017604; DOI=10.1091/mbc.8.1.171;
RA Kominami K., Okura N., Kawamura M., Demartino G.N., Slaughter C.A.,
RA Shimbara N., Chung C.H., Fujimuro M., Yokosawa H., Shimizu Y.,
RA Tanahashi N., Tanaka K., Toh-e A.;
RT "Yeast counterparts of subunits S5a and p58 (S3) of the human 26S
RT proteasome are encoded by two multicopy suppressors of nin1-1.";
RL Mol. Biol. Cell 8:171-187(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, Lung, Pancreas, and Skin;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which
CC is involved in the ATP-dependent degradation of ubiquitinated
CC proteins.
CC -!- SUBUNIT: The 26S proteasome is composed of a core protease, known
CC as the 20S proteasome, capped at one or both ends by the 19S
CC regulatory complex (RC). The RC is composed of at least 18
CC different subunits in two subcomplexes, the base and the lid,
CC which form the portions proximal and distal to the 20S proteolytic
CC core, respectively.
CC -!- SIMILARITY: Belongs to the proteasome subunit S3 family.
CC -!- SIMILARITY: Contains 1 PCI 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; D67025; BAA23651.1; -; mRNA.
DR EMBL; BT007217; AAP35881.1; -; mRNA.
DR EMBL; AK022896; BAG51131.1; -; mRNA.
DR EMBL; CH471152; EAW60625.1; -; Genomic_DNA.
DR EMBL; BC000074; AAH00074.1; -; mRNA.
DR EMBL; BC004859; AAH04859.1; -; mRNA.
DR EMBL; BC012302; AAH12302.1; -; mRNA.
DR EMBL; BC020518; AAH20518.1; -; mRNA.
DR EMBL; BC025686; AAH25686.1; -; mRNA.
DR RefSeq; NP_002800.2; NM_002809.3.
DR UniGene; Hs.12970; -.
DR ProteinModelPortal; O43242; -.
DR SMR; O43242; 226-467.
DR DIP; DIP-27571N; -.
DR IntAct; O43242; 17.
DR MINT; MINT-5003834; -.
DR STRING; 9606.ENSP00000264639; -.
DR PhosphoSite; O43242; -.
DR PaxDb; O43242; -.
DR PeptideAtlas; O43242; -.
DR PRIDE; O43242; -.
DR DNASU; 5709; -.
DR Ensembl; ENST00000264639; ENSP00000264639; ENSG00000108344.
DR GeneID; 5709; -.
DR KEGG; hsa:5709; -.
DR UCSC; uc002htn.2; human.
DR CTD; 5709; -.
DR GeneCards; GC17P038137; -.
DR HGNC; HGNC:9560; PSMD3.
DR HPA; CAB017038; -.
DR neXtProt; NX_O43242; -.
DR PharmGKB; PA38123; -.
DR eggNOG; NOG251646; -.
DR HOGENOM; HOG000193909; -.
DR HOVERGEN; HBG000703; -.
DR InParanoid; O43242; -.
DR KO; K03033; -.
DR OMA; NQVARFL; -.
DR OrthoDB; EOG7JQBNM; -.
DR PhylomeDB; O43242; -.
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; PSMD3; human.
DR GeneWiki; PSMD3; -.
DR GenomeRNAi; 5709; -.
DR NextBio; 22182; -.
DR PRO; PR:O43242; -.
DR ArrayExpress; O43242; -.
DR Bgee; O43242; -.
DR CleanEx; HS_PSMD3; -.
DR Genevestigator; O43242; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
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: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:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR013586; 26S_Psome_reg_C.
DR InterPro; IPR013143; PAM.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF08375; Rpn3_C; 1.
DR SMART; SM00753; PAM; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Proteasome; Reference proteome.
FT CHAIN 1 534 26S proteasome non-ATPase regulatory
FT subunit 3.
FT /FTId=PRO_0000173816.
FT DOMAIN 358 462 PCI.
FT COMPBIAS 26 32 Poly-Pro.
FT CONFLICT 60 60 A -> V (in Ref. 1; BAA23651).
FT CONFLICT 157 158 TP -> NT (in Ref. 5; AAH12302).
FT CONFLICT 304 304 E -> V (in Ref. 5; AAH12302).
SQ SEQUENCE 534 AA; 60978 MW; 3B3FB5593542C078 CRC64;
MKQEGSARRR GADKAKPPPG GGEQEPPPPP APQDVEMKEE AATGGGSTGE ADGKTAAAAA
EHSQRELDTV TLEDIKEHVK QLEKAVSGKE PRFVLRALRM LPSTSRRLNH YVLYKAVQGF
FTSNNATRDF LLPFLEEPMD TEADLQFRPR TGKAASTPLL PEVEAYLQLL VVIFMMNSKR
YKEAQKISDD LMQKISTQNR RALDLVAAKC YYYHARVYEF LDKLDVVRSF LHARLRTATL
RHDADGQATL LNLLLRNYLH YSLYDQAEKL VSKSVFPEQA NNNEWARYLY YTGRIKAIQL
EYSEARRTMT NALRKAPQHT AVGFKQTVHK LLIVVELLLG EIPDRLQFRQ PSLKRSLMPY
FLLTQAVRTG NLAKFNQVLD QFGEKFQADG TYTLIIRLRH NVIKTGVRMI SLSYSRISLA
DIAQKLQLDS PEDAEFIVAK AIRDGVIEAS INHEKGYVQS KEMIDIYSTR EPQLAFHQRI
SFCLDIHNMS VKAMRFPPKS YNKDLESAEE RREREQQDLE FAKEMAEDDD DSFP
//