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UniProtKB/Swiss-Prot entry P62333


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

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Entry information
Entry name PRS10_HUMAN
Primary accession number P62333
Secondary accession numbers P49719 Q6IBU3 Q92524
Integrated into Swiss-Prot on July 5, 2004
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 47)
Name and origin of the protein
Protein name 26S protease regulatory subunit S10B
Synonyms Proteasome 26S subunit ATPase 6
Proteasome subunit p42
Gene name
Name: PSMC6
Synonyms: SUG2
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].
TISSUE=Aorta;
DOI=10.1016/0014-5793(96)00489-9; PubMed=8674546 [NCBI, ExPASy, EBI, Israel, Japan]
Fujiwara T., Watanabe T.K., Tanaka K., Slaughter C.A., Demartino G.N.;
"cDNA cloning of p42, a shared subunit of two proteasome regulatory proteins, reveals a novel member of the AAA protein family.";
FEBS Lett. 387:184-188(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Li Y., Benezra R.;
"Human SUG2.";
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Urinary bladder;
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).
[6]
PARTIAL PROTEIN SEQUENCE.
DOI=10.1074/jbc.271.6.3112; PubMed=8621709 [NCBI, ExPASy, EBI, Israel, Japan]
Demartino G.N., Proske R.J., Moomaw C.R., Strong A.A., Song X., Hisamatsu H., Tanaka K., Slaughter C.A.;
"Identification, purification, and characterization of a PA700-dependent activator of the proteasome.";
J. Biol. Chem. 271:3112-3118(1996).
[7]
INTERACTION WITH PAAF1.
DOI=10.1128/MCB.25.9.3842-3853.2005; PubMed=15831487 [NCBI, ExPASy, EBI, Israel, Japan]
Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.;
"Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases.";
Mol. Cell. Biol. 25:3842-3853(2005).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] 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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-207, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(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
D78275; BAA11338.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF006305; AAB61616.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006843; AAP35489.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456709; CAG32990.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005390; AAH05390.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S71316; S71316.
RefSeq NP_002797.2; -.
UniGene Hs.156171
3D structure databases
HSSP P43773; 1IM2. [HSSP ENTRY / PDB]
ModBase P62333.
Protein-protein interaction databases
IntAct P62333; -.
PTM databases
PhosphoSite P62333; -.
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
REPRODUCTION-2DPAGE IPI00021926; -.
Organism-specific databases
H-InvDB HIX0011661; -.
HIX0034665; -.
HGNC HGNC:9553; PSMC6.
GenAtlas PSMC6.
MIM 602708; gene. [NCBI / EBI]
PharmGKB PA33898; -.
GeneCards P62333.
Gene expression databases
CleanEx HS_PSMC6; -.
GermOnline ENSG00000100519; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0000502; Cellular component: proteasome complex (inferred from direct assay from UniProtKB).
GO:0016887; Molecular function: ATPase activity (traceable author statement from UniProtKB).
GO:0030674; Molecular function: protein binding, bridging (non-traceable author statement from UniProtKB).
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 IPR005937; 26S_Psome_P45.
IPR003593; AAA+_ATPase_core.
IPR003959; AAA_ATPase_core.
IPR003960; AAA_ATPase_CS.
Graphical view of domain structure.
Pfam PF00004; AAA; 1.
Pfam graphical view of domain structure.
SMART SM00382; AAA; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR01242; 26Sp45; 1.
PROSITE PS00674; AAA; 1.
BLOCKS P62333.
Proteomic databases
PeptideAtlas P62333; -.
Genome annotation databases
Ensembl ENSG00000100519; Homo sapiens. [Contig view]
GeneID 5706; -.
KEGG hsa:5706; -.
Phylogenomic databases
HOGENOM P62333; -.
HOVERGEN P62333; -.
Other
LinkHub P62333; -.
SOURCE PSMC6; Homo sapiens.
ProtoNet P62333.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Nucleus; Phosphoprotein; Proteasome.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   389  388     26S protease regulatory subunit S10B. PRO_0000084732
NP_BIND   174   181  8     ATP (Potential). 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   207   207        Phosphotyrosine. 
CONFLICT   276   276        I -> T (in Ref. 1; BAA11338). 
Sequence information
Length: 389 AA [This is the length of the unprocessed precursor] Molecular weight: 44173 Da [This is the MW of the unprocessed precursor] CRC64: B26421295742CACD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MADPRDKALQ DYRKKLLEHK EIDGRLKELR EQLKELTKQY EKSENDLKAL QSVGQIVGEV 

        70         80         90        100        110        120 
LKQLTEEKFI VKATNGPRYV VGCRRQLDKS KLKPGTRVAL DMTTLTIMRY LPREVDPLVY 

       130        140        150        160        170        180 
NMSHEDPGNV SYSEIGGLSE QIRELREVIE LPLTNPELFQ RVGIIPPKGC LLYGPPGTGK 

       190        200        210        220        230        240 
TLLARAVASQ LDCNFLKVVS SSIVDKYIGE SARLIREMFN YARDHQPCII FMDEIDAIGG 

       250        260        270        280        290        300 
RRFSEGTSAD REIQRTLMEL LNQMDGFDTL HRVKMIMATN RPDTLDPALL RPGRLDRKIH 

       310        320        330        340        350        360 
IDLPNEQARL DILKIHAGPI TKHGEIDYEA IVKLSDGFNG ADLRNVCTEA GMFAIRADHD 

       370        380 
FVVQEDFMKA VRKVADSKKL ESKLDYKPV 

P62333 in FASTA format

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