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UniProtKB/Swiss-Prot entry O00232


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

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Entry information
Entry name PSD12_HUMAN
Primary accession number O00232
Secondary accession numbers Q53HA2 Q6P053
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 69)
Name and origin of the protein
Protein name 26S proteasome non-ATPase regulatory subunit 12
Synonym 26S proteasome regulatory subunit p55
Gene name
Name: PSMD12
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].
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle, and Testis;
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 2-12, AND ACETYLATION AT ALA-2.
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]
IDENTIFICATION [LARGE SCALE ANALYSIS], 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).
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
AB003103; BAA19749.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK222679; BAD96399.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019062; AAH19062.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC065826; AAH65826.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR PC6501; JC6523.
RefSeq NP_002807.1; -.
UniGene Hs.646575
3D structure databases
ModBase O00232.
Protein-protein interaction databases
DIP DIP:27549N; -.
IntAct O00232; 9.
PTM databases
PhosphoSite O00232; -.
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.
Organism-specific databases
GeneCards GC17M062764; -.
H-InvDB HIX0014093; -.
HGNC HGNC:9557; PSMD12.
GenAtlas PSMD12.
MIM 604450; gene. [NCBI / EBI]
PharmGKB PA33903; -.
GeneCards O00232.
Gene expression databases
ArrayExpress O00232; -.
CleanEx HS_PSMD12; -.
GermOnline ENSG00000197170; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from electronic annotation from UniProtKB-KW).
GO:0005838; Cellular component: proteasome regulatory particle (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 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 SM00088; PINT; 1.
SMART graphical view of domain structure.
Proteomic databases
PeptideAtlas O00232; -.
Proteomics databases
PRIDE O00232; -.
Genome annotation databases
Ensembl ENSG00000197170; Homo sapiens. [Contig view]
GeneID 5718; -.
KEGG hsa:5718; -.
Phylogenomic databases
HOGENOM O00232; -.
HOVERGEN O00232; -.
Other
LinkHub O00232; -.
NextBio 22216; -.
SOURCE PSMD12; Homo sapiens.
ProtoNet O00232.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; Polymorphism; Proteasome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   456  455     26S proteasome non-ATPase regulatory subunit 12. PRO_0000173861
DOMAIN   237   417  181     PCI. 
MOD_RES   2     2        N-acetylalanine. 
VARIANT   358   358  1     V -> A (in dbSNP:rs2230680 [NCBI]). VAR_051558 
CONFLICT   300   300        P -> S (in Ref. 2; BAD96399). 
CONFLICT   398   398        V -> D (in Ref. 2; BAD96399). 
Sequence information
Length: 456 AA [This is the length of the unprocessed precursor] Molecular weight: 52904 Da [This is the MW of the unprocessed precursor] CRC64: 97D0BDBDB0C96195 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MADGGSERAD GRIVKMEVDY SATVDQRLPE CAKLAKEGRL QEVIETLLSL EKQTRTASDM 

        70         80         90        100        110        120 
VSTSRILVAV VKMCYEAKEW DLLNENIMLL SKRRSQLKQA VAKMVQQCCT YVEEITDLPI 

       130        140        150        160        170        180 
KLRLIDTLRM VTEGKIYVEI ERARLTKTLA TIKEQNGDVK EAASILQELQ VETYGSMEKK 

       190        200        210        220        230        240 
ERVEFILEQM RLCLAVKDYI RTQIISKKIN TKFFQEENTE KLKLKYYNLM IQLDQHEGSY 

       250        260        270        280        290        300 
LSICKHYRAI YDTPCIQAES EKWQQALKSV VLYVILAPFD NEQSDLVHRI SGDKKLEEIP 

       310        320        330        340        350        360 
KYKDLLKLFT TMELMRWSTL VEDYGMELRK GSLESPATDV FGSTEEGEKR WKDLKNRVVE 

       370        380        390        400        410        420 
HNIRIMAKYY TRITMKRMAQ LLDLSVDESE AFLSNLVVNK TIFAKVDRLA GIINFQRPKD 

       430        440        450 
PNNLLNDWSQ KLNSLMSLVN KTTHLIAKEE MIHNLQ 

O00232 in FASTA format

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View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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