ID   PSD11_HUMAN             Reviewed;         422 AA.
AC   O00231; O00495;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   07-JUL-2009, entry version 82.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 11;
DE   AltName: Full=26S proteasome regulatory subunit S9;
DE   AltName: Full=26S proteasome regulatory subunit p44.5;
GN   Name=PSMD11;
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], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=97227943; PubMed=9119060; DOI=10.1016/S0014-5793(97)00126-9;
RA   Hoffman L., Rechsteiner M.;
RT   "Molecular cloning and expression of subunit 9 of the 26S
RT   proteasome.";
RL   FEBS Lett. 404:179-184(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98086225; PubMed=9426256; DOI=10.1016/S0378-1119(97)00524-6;
RA   Saito A., Watanabe T.K., Shimada Y., Fujiwara T., Slaughter C.A.,
RA   DeMartino G.N., Tanahashi N., Tanaka K.;
RT   "cDNA cloning and functional analysis of p44.5 and p55, two regulatory
RT   subunits of the 26S proteasome.";
RL   Gene 203:241-250(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=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   [4]
RP   PROTEIN SEQUENCE OF 2-11.
RC   TISSUE=Platelet;
RX   MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-11, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V., Potts A., Brablan J., Quadroni M.;
RL   Submitted (JUL-2004) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-79,
RP   ACETYLATION AT ALA-2, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
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 26S proteasome which
CC       is involved in the ATP-dependent degradation of ubiquitinated
CC       proteins.
CC   -!- SUBUNIT: Component of the PA700 complex.
CC   -!- INTERACTION:
CC       Q9BRP4:PAAF1; NbExp=1; IntAct=EBI-357816, EBI-1056358;
CC       P43686:PSMC4; NbExp=1; IntAct=EBI-357816, EBI-743997;
CC       O75832:PSMD10; NbExp=1; IntAct=EBI-357816, EBI-752185;
CC       Q15008:PSMD6; NbExp=1; IntAct=EBI-357816, EBI-359701;
CC   -!- SIMILARITY: Belongs to the proteasome subunit S9 family.
CC   -!- SIMILARITY: Contains 1 PCI domain.
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DR   EMBL; AF001212; AAB58732.1; -; mRNA.
DR   EMBL; AB003102; BAA19748.1; -; mRNA.
DR   EMBL; BC000437; AAH00437.1; -; mRNA.
DR   EMBL; BC004430; AAH04430.1; -; mRNA.
DR   IPI; IPI00105598; -.
DR   PIR; JC6524; JC6524.
DR   RefSeq; NP_002806.2; -.
DR   UniGene; Hs.655396; -.
DR   IntAct; O00231; 32.
DR   PhosphoSite; O00231; -.
DR   OGP; O00231; -.
DR   PRIDE; O00231; -.
DR   Ensembl; ENSG00000108671; Homo sapiens.
DR   GeneID; 5717; -.
DR   KEGG; hsa:5717; -.
DR   UCSC; uc002hhm.1; human.
DR   GeneCards; GC17P027795; -.
DR   H-InvDB; HIX0013704; -.
DR   HGNC; HGNC:9556; PSMD11.
DR   MIM; 604449; gene.
DR   PharmGKB; PA33902; -.
DR   HOVERGEN; O00231; -.
DR   OMA; O00231; HAADERD.
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; 22212; -.
DR   ArrayExpress; O00231; -.
DR   Bgee; O00231; -.
DR   CleanEx; HS_PSMD11; -.
DR   GermOnline; ENSG00000108671; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-KW.
DR   GO; GO:0000502; C:proteasome complex; TAS:ProtInc.
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   InterPro; IPR013143; PAM.
DR   InterPro; IPR000717; PCI.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00753; PAM; 1.
DR   SMART; SM00088; PINT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Direct protein sequencing;
KW   Phosphoprotein; Proteasome.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    422       26S proteasome non-ATPase regulatory
FT                                subunit 11.
FT                                /FTId=PRO_0000173857.
FT   DOMAIN      222    389       PCI.
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES      14     14       Phosphoserine.
FT   MOD_RES      79     79       Phosphoserine.
FT   MOD_RES     272    272       Phosphoserine.
FT   CONFLICT    113    113       C -> S (in Ref. 1; AAB58732).
SQ   SEQUENCE   422 AA;  47464 MW;  CE113054CBEBDB05 CRC64;
     MAAAAVVEFQ RAQSLLSTDR EASIDILHSI VKRDIQENDE EAVQVKEQSI LELGSLLAKT
     GQAAELGGLL KYVRPFLNSI SKAKAARLVR SLLDLFLDME AATGQEVELC LECIEWAKSE
     KRTFLRQALE ARLVSLYFDT KRYQEALHLG SQLLRELKKM DDKALLVEVQ LLESKTYHAL
     SNLPKARAAL TSARTTANAI YCPPKLQATL DMQSGIIHAA EEKDWKTAYS YFYEAFEGYD
     SIDSPKAITS LKYMLLCKIM LNTPEDVQAL VSGKLALRYA GRQTEALKCV AQASKNRSLA
     DFEKALTDYR AELRDDPIIS THLAKLYDNL LEQNLIRVIE PFSRVQIEHI SSLIKLSKAD
     VERKLSQMIL DKKFHGILDQ GEGVLIIFDE PPVDKTYEAA LETIQNMSKV VDSLYNKAKK
     LT
//