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UniProtKB/Swiss-Prot entry P62195


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

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Entry information
Entry name PRS8_HUMAN
Primary accession number P62195
Secondary accession numbers O35051 O43208 P47210 P52915 P52916
Integrated into Swiss-Prot on June 21, 2004
Sequence was last modified on June 21, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 48)
Name and origin of the protein
Protein name 26S protease regulatory subunit 8
Synonyms Proteasome 26S subunit ATPase 5
Proteasome subunit p45
p45/SUG
Thyroid hormone receptor-interacting protein 1
TRIP1
Gene name
Name: PSMC5
Synonyms: SUG1
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=Hepatoma;
DOI=10.1016/0014-5793(95)00304-R; PubMed=7729537 [NCBI, ExPASy, EBI, Israel, Japan]
Akiyama K., Yokota K., Kagawa S., Shimbara N., Demartino G.N., Slaughter C.A., Noda C., Tanaka K.;
"cDNA cloning of a new putative ATPase subunit p45 of the human 26S proteasome, a homolog of yeast transcriptional factor Sug1p.";
FEBS Lett. 363:151-156(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1210/me.9.2.243; PubMed=7776974 [NCBI, ExPASy, EBI, Israel, Japan]
Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
"Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor.";
Mol. Endocrinol. 9:243-254(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung carcinoma;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-406.
TISSUE=Brain;
PubMed=9110174 [NCBI, ExPASy, EBI, Israel, Japan]
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
"Large-scale concatenation cDNA sequencing.";
Genome Res. 7:353-358(1997).
[5]
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 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]
VARIANT [LARGE SCALE ANALYSIS] GLN-60.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
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
D44467; BAA07919.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L38810; AAC41735.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001932; AAH01932.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002367; AAH02367.3; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF035309; AAB88187.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S60343; S60343.
S65536; S65536.
RefSeq NP_002796.4; -.
UniGene Hs.79387
3D structure databases
HSSP Q9LCZ4; 1IY0. [HSSP ENTRY / PDB]
ModBase P62195.
Protein-protein interaction databases
IntAct P62195; -.
PTM databases
PhosphoSite P62195; -.
Organism-specific databases
HGNC HGNC:9552; PSMC5.
GenAtlas PSMC5.
MIM 601681; gene. [NCBI / EBI]
PharmGKB PA33897; -.
GeneCards P62195.
Gene expression databases
CleanEx HS_PSMC5; -.
GermOnline ENSG00000087191; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
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:0031531; Molecular function: thyrotropin-releasing hormone receptor binding (inferred from physical interaction from UniProtKB).
GO:0003712; Molecular function: transcription cofactor activity (traceable author statement from ProtInc).
GO:0031145; Biological process: anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from experiment from Reactome).
GO:0043069; Biological process: negative regulation of programmed cell death (non-traceable author statement from UniProtKB).
GO:0051436; Biological process: negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
GO:0043193; Biological process: positive regulation of gene-specific transcription (non-traceable author statement from UniProtKB).
GO:0051437; Biological process: positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
GO:0006366; Biological process: transcription from RNA polymerase II promoter (traceable author statement from ProtInc).
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 P62195.
Genome annotation databases
Ensembl ENSG00000087191; Homo sapiens. [Contig view]
GeneID 5705; -.
KEGG hsa:5705; -.
Phylogenomic databases
HOGENOM P62195; -.
HOVERGEN P62195; -.
Other
SOURCE PSMC5; Homo sapiens.
ProtoNet P62195.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Polymorphism; Proteasome.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   406  405     26S protease regulatory subunit 8. PRO_0000084721
NP_BIND   190   197  8     ATP (Potential). 
MOD_RES   2     2        N-acetylalanine. 
VARIANT   60    60  1     R -> Q (in a colorectal cancer sample; somatic mutation). VAR_035901 
CONFLICT   61    61        E -> R (in Ref. 1; BAA07919). 
CONFLICT   127   128        LP -> ML (in Ref. 4; AAB88187). 
CONFLICT   266   266        D -> S (in Ref. 2; AAC41735). 
CONFLICT   272   272        T -> Q (in Ref. 2; AAC41735). 
CONFLICT   300   300        I -> M (in Ref. 2; AAC41735). 
Sequence information
Length: 406 AA [This is the length of the unprocessed precursor] Molecular weight: 45626 Da [This is the MW of the unprocessed precursor] CRC64: 29C6410C4A85A7F7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MALDGPEQME LEEGKAGSGL RQYYLSKIEE LQLIVNDKSQ NLRRLQAQRN ELNAKVRLLR 

        70         80         90        100        110        120 
EELQLLQEQG SYVGEVVRAM DKKKVLVKVH PEGKFVVDVD KNIDINDVTP NCRVALRNDS 

       130        140        150        160        170        180 
YTLHKILPNK VDPLVSLMMV EKVPDSTYEM IGGLDKQIKE IKEVIELPVK HPELFEALGI 

       190        200        210        220        230        240 
AQPKGVLLYG PPGTGKTLLA RAVAHHTDCT FIRVSGSELV QKFIGEGARM VRELFVMARE 

       250        260        270        280        290        300 
HAPSIIFMDE IDSIGSSRLE GGSGGDSEVQ RTMLELLNQL DGFEATKNIK VIMATNRIDI 

       310        320        330        340        350        360 
LDSALLRPGR IDRKIEFPPP NEEARLDILK IHSRKMNLTR GINLRKIAEL MPGASGAEVK 

       370        380        390        400 
GVCTEAGMYA LRERRVHVTQ EDFEMAVAKV MQKDSEKNMS IKKLWK 

P62195 in FASTA format

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