ID   PSMD3_HUMAN             Reviewed;         534 AA.
AC   O43242; Q96EI2; Q9BQA4;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2002, sequence version 2.
DT   07-JUL-2009, entry version 84.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 3;
DE            Short=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   MEDLINE=97170075; PubMed=9017604;
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].
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   [4]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
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   [5]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
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   -!- INTERACTION:
CC       Q9BUV8:C20orf24; NbExp=1; IntAct=EBI-357622, EBI-1050079;
CC       Q9BRP4:PAAF1; NbExp=1; IntAct=EBI-357622, EBI-1056358;
CC       O75832:PSMD10; NbExp=1; IntAct=EBI-357622, EBI-752185;
CC       Q15008:PSMD6; NbExp=1; IntAct=EBI-357622, EBI-359701;
CC       O75365:PTP4A3; NbExp=1; IntAct=EBI-357622, EBI-1043866;
CC       Q9P2S5:WDR8; NbExp=1; IntAct=EBI-357622, EBI-1054904;
CC   -!- SIMILARITY: Belongs to the proteasome subunit S3 family.
CC   -!- SIMILARITY: Contains 1 PCI domain.
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DR   EMBL; D67025; BAA23651.1; -; mRNA.
DR   EMBL; BT007217; AAP35881.1; -; mRNA.
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   IPI; IPI00011603; -.
DR   RefSeq; NP_002800.2; -.
DR   UniGene; Hs.12970; -.
DR   DIP; DIP:27571N; -.
DR   IntAct; O43242; 16.
DR   PhosphoSite; O43242; -.
DR   PeptideAtlas; O43242; -.
DR   PRIDE; O43242; -.
DR   Ensembl; ENSG00000108344; Homo sapiens.
DR   GeneID; 5709; -.
DR   KEGG; hsa:5709; -.
DR   NMPDR; fig|9606.3.peg.13656; -.
DR   UCSC; uc002htn.1; human.
DR   GeneCards; GC17P035390; -.
DR   H-InvDB; HIX0013776; -.
DR   HGNC; HGNC:9560; PSMD3.
DR   HPA; CAB017038; -.
DR   PharmGKB; PA33906; -.
DR   HOVERGEN; O43242; -.
DR   OMA; O43242; LMVIFLM.
DR   Reactome; REACT_11045; Signaling by Wnt.
DR   Reactome; REACT_13; Metabolism of amino acids.
DR   Reactome; REACT_13635; Regulation of activated PAK-2p34 by proteasome mediated degradation.
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_9035; APC/C:Cdh1-mediated degradation of Skp2.
DR   NextBio; 22182; -.
DR   ArrayExpress; O43242; -.
DR   Bgee; O43242; -.
DR   CleanEx; HS_PSMD3; -.
DR   GermOnline; ENSG00000108344; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-KW.
DR   GO; GO:0000502; C:proteasome complex; TAS:ProtInc.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent protea...; EXP:Reactome.
DR   GO; GO:0051436; P:negative regulation of ubiquitin-protein li...; EXP:Reactome.
DR   GO; GO:0051437; P:positive regulation of ubiquitin-protein li...; EXP:Reactome.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR   InterPro; IPR013586; 26S_Psome_reg_C.
DR   InterPro; IPR013143; PAM.
DR   InterPro; IPR000717; PCI.
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.
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. 3; AAH12302).
FT   CONFLICT    304    304       E -> V (in Ref. 3; 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
//