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UniProtKB/Swiss-Prot entry O00231


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PSD11_HUMAN
Primary accession number O00231
Secondary accession number O00495
Integrated into Swiss-Prot on May 15, 2002
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    December 16, 2008 (Entry version 76)
Name and origin of the protein
Protein name 26S proteasome non-ATPase regulatory subunit 11
Synonyms 26S proteasome regulatory subunit S9
26S proteasome regulatory subunit p44.5
Gene name
Name: PSMD11
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
DOI=10.1016/S0014-5793(97)00126-9; PubMed=9119060 [NCBI, ExPASy, EBI, Israel, Japan]
Hoffman L., Rechsteiner M.;
"Molecular cloning and expression of subunit 9 of the 26S proteasome.";
FEBS Lett. 404:179-184(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0378-1119(97)00524-6; PubMed=9426256 [NCBI, ExPASy, EBI, Israel, Japan]
Saito A., Watanabe T.K., Shimada Y., Fujiwara T., Slaughter C.A., DeMartino G.N., Tanahashi N., Tanaka K.;
"cDNA cloning and functional analysis of p44.5 and p55, two regulatory subunits of the 26S proteasome.";
Gene 203:241-250(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 2-11.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[5]
PROTEIN SEQUENCE OF 2-11, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V., Potts A., Brablan J., Quadroni M.;
Submitted (JUL-2004) to UniProtKB.
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-79, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
DOI=10.1021/bi061994u; PubMed=17323924 [NCBI, ExPASy, EBI, Israel, Japan]
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF001212; AAB58732.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB003102; BAA19748.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000437; AAH00437.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004430; AAH04430.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC6524; JC6524.
RefSeq NP_002806.2; -.
UniGene Hs.655396
3D structure databases
ModBase O00231.
Protein-protein interaction databases
IntAct O00231; 32.
PTM databases
PhosphoSite O00231; -.
Enzyme and pathway databases
Reactome REACT_11045; Signaling by Wnt.
REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
REACT_383; DNA Replication.
REACT_6185; HIV Infection.
REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_9035; APC/C:Cdh1-mediated degradation of Skp2.
2D gel databases
OGP O00231; -.
Organism-specific databases
GeneCards GC17P027795; -.
H-InvDB HIX0013704; -.
HGNC HGNC:9556; PSMD11.
GenAtlas PSMD11.
MIM 604449; gene. [NCBI / EBI]
PharmGKB PA33902; -.
GeneCards O00231.
Gene expression databases
ArrayExpress O00231; -.
CleanEx HS_PSMD11; -.
GermOnline ENSG00000108671; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from electronic annotation from UniProtKB-KW).
GO:0000502; Cellular component: proteasome complex (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0031145; Biological process: anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from experiment from Reactome).
GO:0051436; Biological process: negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
GO:0051437; Biological process: positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR013143; PAM.
IPR000717; PCI.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.
Gene3D G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
Pfam PF01399; PCI; 1.
Pfam graphical view of domain structure.
SMART SM00753; PAM; 1.
SM00088; PINT; 1.
SMART graphical view of domain structure.
Proteomics databases
PRIDE O00231; -.
Genome annotation databases
Ensembl ENSG00000108671; Homo sapiens. [Contig view]
GeneID 5717; -.
KEGG hsa:5717; -.
Phylogenomic databases
HOVERGEN O00231; -.
Other
NextBio 22212; -.
SOURCE PSMD11; Homo sapiens.
ProtoNet O00231.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; Phosphoprotein; Proteasome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   422  421     26S proteasome non-ATPase regulatory subunit 11. PRO_0000173857
DOMAIN   222   389  168     PCI. 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   14    14        Phosphoserine. 
MOD_RES   79    79        Phosphoserine. 
MOD_RES   272   272        Phosphoserine. 
CONFLICT   113   113        C -> S (in Ref. 1; AAB58732). 
Sequence information
Length: 422 AA [This is the length of the unprocessed precursor] Molecular weight: 47464 Da [This is the MW of the unprocessed precursor] CRC64: CE113054CBEBDB05 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAAAVVEFQ RAQSLLSTDR EASIDILHSI VKRDIQENDE EAVQVKEQSI LELGSLLAKT 

        70         80         90        100        110        120 
GQAAELGGLL KYVRPFLNSI SKAKAARLVR SLLDLFLDME AATGQEVELC LECIEWAKSE 

       130        140        150        160        170        180 
KRTFLRQALE ARLVSLYFDT KRYQEALHLG SQLLRELKKM DDKALLVEVQ LLESKTYHAL 

       190        200        210        220        230        240 
SNLPKARAAL TSARTTANAI YCPPKLQATL DMQSGIIHAA EEKDWKTAYS YFYEAFEGYD 

       250        260        270        280        290        300 
SIDSPKAITS LKYMLLCKIM LNTPEDVQAL VSGKLALRYA GRQTEALKCV AQASKNRSLA 

       310        320        330        340        350        360 
DFEKALTDYR AELRDDPIIS THLAKLYDNL LEQNLIRVIE PFSRVQIEHI SSLIKLSKAD 

       370        380        390        400        410        420 
VERKLSQMIL DKKFHGILDQ GEGVLIIFDE PPVDKTYEAA LETIQNMSKV VDSLYNKAKK 


LT 

O00231 in FASTA format

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