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UniProtKB/Swiss-Prot entry P43686


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

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Entry information
Entry name PRS6B_HUMAN
Primary accession number P43686
Secondary accession numbers Q96FV5 Q9UBM3 Q9UEX3
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on May 10, 2002 (Sequence version 2)
Annotations were last modified on    June 10, 2008 (Entry version 80)
Name and origin of the protein
Protein name 26S protease regulatory subunit 6B
Synonyms Proteasome 26S subunit ATPase 4
MB67-interacting protein
MIP224
TAT-binding protein 7
TBP-7
Gene name
Name: PSMC4
Synonyms: MIP224, TBP7
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].
PubMed=8419915 [NCBI, ExPASy, EBI, Israel, Japan]
Ohana B., Moore P.A., Ruben S.M., Southgate C.D., Green M.R., Rosen C.A.;
"The type 1 human immunodeficiency virus Tat binding protein is a transcriptional activator belonging to an additional family of evolutionarily conserved genes.";
Proc. Natl. Acad. Sci. U.S.A. 90:138-142(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Blood;
Zhang Q., Mao M., Huang Q., Zhou J., Fu G., Wu J., Wang Y., Chen S., Chen Z.;
"Human 26S proteasome ATPase subunit gene expressed in hematopoietic progenitor CD34+ cell.";
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH NR1I3.
DOI=10.1016/0960-0760(95)00220-0; PubMed=8603043 [NCBI, ExPASy, EBI, Israel, Japan]
Choi H.S., Seol W., Moore D.D.;
"A component of the 26S proteasome binds on orphan member of the nuclear hormone receptor superfamily.";
J. Steroid Biochem. Mol. Biol. 56:23-30(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Bi A., Yu L., Zheng L.;
"Cloning and expression analysis of a novel human gene homologous to mouse proteasomal ATPase (Tat-binding protein 7).";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan]
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung, Pancreas, and Skin;
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).
[8]
PROTEIN SEQUENCE OF 1-10; 218-229; 307-313 AND 343-369, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
Submitted (JUL-2007) to UniProtKB.
[9]
PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
PubMed=8060531 [NCBI, ExPASy, EBI, Israel, Japan]
Dubiel W., Ferrell K., Rechsteiner M.;
"Tat-binding protein 7 is a subunit of the 26S protease.";
Biol. Chem. Hoppe-Seyler 375:237-240(1994).
[10]
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).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
[12]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 337-418 IN COMPLEX WITH MOUSE PSMD10.
DOI=10.1016/j.str.2006.11.015; PubMed=17292836 [NCBI, ExPASy, EBI, Israel, Japan]
Nakamura Y., Nakano K., Umehara T., Kimura M., Hayashizaki Y., Tanaka A., Horikoshi M., Padmanabhan B., Yokoyama S.;
"Structure of the oncoprotein gankyrin in complex with S6 ATPase of the 26S proteasome.";
Structure 15:179-189(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
AF038965; AAC26843.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U27515; AAC99817.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF020736; AAC32612.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007232; AAP35896.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC007842; AAD39267.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000343; AAH00343.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010396; AAH10396.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014488; AAH14488.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_006494.1; -.
NP_694546.1; -.
UniGene Hs.211594
3D structure databases
PDB
2DVW; X-ray; 2.30 A; B=337-418.[ExPASy / RCSB / EBI]
PDBsum 2DVW; -.
ModBase P43686.
Protein-protein interaction databases
IntAct P43686; -.
PTM databases
PhosphoSite P43686; -.
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 P43686; -.
Organism-specific databases
H-InvDB HIX0015127; -.
HGNC HGNC:9551; PSMC4.
GeneLynx PSMC4; Homo sapiens.
GenAtlas PSMC4.
HPA HPA002044; -.
MIM 602707; gene. [NCBI / EBI]
PharmGKB PA33896; -.
GeneCards P43686.
Gene expression databases
ArrayExpress P43686; -.
CleanEx HS_PSMC4; -.
GermOnline ENSG00000013275; Homo sapiens.
Ontologies
GO
GO:0000502; Cellular component: proteasome complex (traceable author statement from ProtInc).
GO:0016887; Molecular function: ATPase activity (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 IPR005937; 26S_proteasome_P45.
IPR003593; AAA+_ATPase_core.
IPR003959; AAA_ATPase_core.
IPR003960; AAA_ATPase_CS.
IPR001270; Chaprnin_clpA/B.
Graphical view of domain structure.
Pfam PF00004; AAA; 1.
Pfam graphical view of domain structure.
PRINTS PR00300; CLPPROTEASEA.
SMART SM00382; AAA; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR01242; 26Sp45; 1.
PROSITE PS00674; AAA; 1.
BLOCKS P43686.
Genome annotation databases
Ensembl ENSG00000013275; Homo sapiens. [Contig view]
GeneID 5704; -.
KEGG hsa:5704; -.
Phylogenomic databases
HOGENOM P43686; -.
HOVERGEN P43686; -.
Other
SOURCE PSMC4; Homo sapiens.
ProtoNet P43686.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Nucleus; Proteasome.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   418  418     26S protease regulatory subunit 6B. PRO_0000084686
NP_BIND   206   213  8     ATP (Potential). 
MOD_RES   1     1        N-acetylmethionine. 
VAR_SEQ   46    76        Missing (in isoform 2). VSP_000022
CONFLICT   73    73        L -> F (in Ref. 4; AAC32612). 
CONFLICT   110   110        N -> S (in Ref. 4; AAC32612). 
CONFLICT   118   118        T -> A (in Ref. 1). 
CONFLICT   157   157        D -> G (in Ref. 4; AAC32612). 
CONFLICT   185   185        L -> V (in Ref. 4; AAC32612). 
HELIX   338   348  11      
TURN   349   351  3      
HELIX   361   364  4      
HELIX   372   388  17      
STRAND   392   394  3      
HELIX   396   406  11      
Sequence information
Length: 418 AA [This is the length of the unprocessed precursor] Molecular weight: 47366 Da [This is the MW of the unprocessed precursor] CRC64: 80F9523C61B88F0C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEEIGILVEK AQDEIPALSV SRPQTGLSFL GPEPEDLEDL YSRYKKLQQE LEFLEVQEEY 

        70         80         90        100        110        120 
IKDEQKNLKK EFLHAQEEVK RIQSIPLVIG QFLEAVDQNT AIVGSTTGSN YYVRILSTID 

       130        140        150        160        170        180 
RELLKPNASV ALHKHSNALV DVLPPEADSS IMMLTSDQKP DVMYADIGGM DIQKQEVREA 

       190        200        210        220        230        240 
VELPLTHFEL YKQIGIDPPR GVLMYGPPGC GKTMLAKAVA HHTTAAFIRV VGSEFVQKYL 

       250        260        270        280        290        300 
GEGPRMVRDV FRLAKENAPA IIFIDEIDAI ATKRFDAQTG ADREVQRILL ELLNQMDGFD 

       310        320        330        340        350        360 
QNVNVKVIMA TNRADTLDPA LLRPGRLDRK IEFPLPDRRQ KRLIFSTITS KMNLSEEVDL 

       370        380        390        400        410 
EDYVARPDKI SGADINSICQ ESGMLAVREN RYIVLAKDFE KAYKTVIKKD EQEHEFYK 

P43686 in FASTA format

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View entry in raw text format (no links)
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