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UniProtKB/Swiss-Prot entry P35998


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

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Entry information
Entry name PRS7_HUMAN
Primary accession number P35998
Secondary accession numbers None
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 84)
Name and origin of the protein
Protein name 26S protease regulatory subunit 7
Synonyms Proteasome 26S subunit ATPase 2
Protein MSS1
Gene name
Name: PSMC2
Synonyms: MSS1
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=10.1038/357700a0; PubMed=1377363 [NCBI, ExPASy, EBI, Israel, Japan]
Shibuya H., Irie K., Ninomiya-Tsuji J., Goebl M., Taniguchi T., Matsumoto K.;
"New human gene encoding a positive modulator of HIV Tat-mediated transactivation.";
Nature 357:700-702(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[3]
PROTEIN SEQUENCE OF 2-10.
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).
[4]
PROTEIN SEQUENCE OF 269-284, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[5]
FUNCTION, AND INTERACTION WITH NDC80.
DOI=10.1074/jbc.272.38.24081; PubMed=9295362 [NCBI, ExPASy, EBI, Israel, Japan]
Chen Y., Sharp Z.D., Lee W.-H.;
"HEC binds to the seventh regulatory subunit of the 26 S proteasome and modulates the proteolysis of mitotic cyclins.";
J. Biol. Chem. 272:24081-24087(1997).
[6]
INTERACTION WITH NDC80.
PubMed=10409732 [NCBI, ExPASy, EBI, Israel, Japan]
Zheng L., Chen Y., Lee W.-H.;
"Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins.";
Mol. Cell. Biol. 19:5417-5428(1999).
[7]
INTERACTION WITH SQSTM1.
DOI=10.1128/MCB.24.18.8055-8068.2004; PubMed=15340068 [NCBI, ExPASy, EBI, Israel, Japan]
Seibenhener M.L., Babu J.R., Geetha T., Wong H.C., Krishna N.R., Wooten M.W.;
"Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation.";
Mol. Cell. Biol. 24:8055-8068(2004).
[8]
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).
[9]
CLEAVAGE OF INITIATOR METHIONINE [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
D11094; BAA01868.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002589; AAH02589.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S24353; S24353.
RefSeq NP_002794.1; -.
UniGene Hs.437366
3D structure databases
HSSP Q9LCZ4; 1IXZ. [HSSP ENTRY / PDB]
ModBase P35998.
Protein-protein interaction databases
DIP DIP:27554N; -.
IntAct P35998; -.
PTM databases
PhosphoSite P35998; -.
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 P35998; -.
REPRODUCTION-2DPAGE IPI00021435; -.
P35998; -.
Organism-specific databases
H-InvDB HIX0006971; -.
HGNC HGNC:9548; PSMC2.
GenAtlas PSMC2.
MIM 154365; gene. [NCBI / EBI]
PharmGKB PA33893; -.
GeneCards P35998.
Gene expression databases
ArrayExpress P35998; -.
CleanEx HS_PSMC2; -.
GermOnline ENSG00000161057; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from UniProtKB).
GO:0000502; Cellular component: proteasome complex (inferred from direct assay from UniProtKB).
GO:0016887; Molecular function: ATPase activity (inferred from direct assay from UniProtKB).
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 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 P35998.
Proteomic databases
PeptideAtlas P35998; -.
Genome annotation databases
Ensembl ENSG00000161057; Homo sapiens. [Contig view]
GeneID 5701; -.
KEGG hsa:5701; -.
Phylogenomic databases
HOGENOM P35998; -.
HOVERGEN P35998; -.
Other
SOURCE PSMC2; Homo sapiens.
ProtoNet P35998.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cytoplasm; Direct protein sequencing; Host-virus interaction; Nucleotide-binding; Nucleus; Proteasome.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   433  432     26S protease regulatory subunit 7. PRO_0000084709
NP_BIND   216   223  8     ATP (Potential). 
Sequence information
Length: 433 AA [This is the length of the unprocessed precursor] Molecular weight: 48634 Da [This is the MW of the unprocessed precursor] CRC64: 85FD95F6DF7A3E84 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPDYLGADQR KTKEDEKDDK PIRALDEGDI ALLKTYGQST YSRQIKQVED DIQQLLKKIN 

        70         80         90        100        110        120 
ELTGIKESDT GLAPPALWDL AADKQTLQSE QPLQVARCTK IINADSEDPK YIINVKQFAK 

       130        140        150        160        170        180 
FVVDLSDQVA PTDIEEGMRV GVDRNKYQIH IPLPPKIDPT VTMMQVEEKP DVTYSDVGGC 

       190        200        210        220        230        240 
KEQIEKLREV VETPLLHPER FVNLGIEPPK GVLLFGPPGT GKTLCARAVA NRTDACFIRV 

       250        260        270        280        290        300 
IGSELVQKYV GEGARMVREL FEMARTKKAC LIFFDEIDAI GGARFDDGAG GDNEVQRTML 

       310        320        330        340        350        360 
ELINQLDGFD PRGNIKVLMA TNRPDTLDPA LMRPGRLDRK IEFSLPDLEG RTHIFKIHAR 

       370        380        390        400        410        420 
SMSVERDIRF ELLARLCPNS TGAEIRSVCT EAGMFAIRAR RKIATEKDFL EAVNKVIKSY 

       430 
AKFSATPRYM TYN 

P35998 in FASTA format

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