Tag Content
UniProt Accession
Theoretical PI
Molecular Weight
49549 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Gene Synonyms/Alias
Protein Name
26S protease regulatory subunit 6A 
Protein Synonyms/Alias
26S proteasome AAA-ATPase subunit RPT5; Proteasome 26S subunit ATPase 3; Tat-binding protein 1;TBP-1 
Mus musculus (Mouse) 
NCBI Taxonomy ID
Chromosome Location
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Probability (GAS) of Function in Spermatogenesis
The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
Temporarily unavailable 
Abstract of related literatures
1. Tat binding protein-1 (TBP-1) is one of the molecules that interact with HIV Tat protein and have influence on Tat-mediated transactivation of HIV. In addition, TBP-1 has been recognized as a component of the 19S regulatory subunit of the multiprotein complex, the 26S proteasome, that is essential for many basic events in cells, e.g. cell cycle regulation, by degrading the ubiquitinized proteins. Here we have cloned a mouse TBP-1, confirmed its inhibitory action on Tat activity and revealed its in vivo heterogeneous expression pattern in the mouse. The cloned mouse TBP-1 cDNA is 1569 bp in size, longer than reported human TBP-1 cDNA, and another possible initiation site has been identified. Robust expression of TBP-1 mRNA can be observed in the testis, especially in the spermatogonia and spermatocytes. Our immunohistochemical study has revealed that TBP-1 is mainly localized in the nuclei of these testicular cells. Expression of TBP-1 mRNA in CD4+ lymphocytes is confirmed by RT-PCR. Localization of TBP-1 transcripts in vivo is similar to the reported distribution of constitutive components of the 20S proteasome. The heterogeneous and restricted expression of TBP-1 in vivo suggests that there may be a diverse reaction of tissues against the HIV proliferation and a diverse capability of tissues in degrading ubiquitinized proteins in vivo. PMID: [9714759] 

2. PSMC3 and PSMC4, components of the 19S complex of the 26S proteasome, show a significant degree of amino acid similarity, especially in the conserved ATPase domain (CAD). In this study, we characterized the mouse Psmc3 and Psmc4 genes. The genomic structures of both genes showed a significant degree of similarity. The Psmc3 gene was composed of 12 coding exons, whereas the Psmc4 gene had 11 exons. Exons encoding the leucine zipper domain and CAD were identical in number between the Psmc3 and Psmc4 genes. The Psmc3 gene mapped to mouse chromosome 2, whereas Psmc4 mapped to chromosome 7. We further addressed the biological roles of Psmc3 and Psmc4 through the generation of gene targeted mice. Both Psmc3- and Psmc4-deficient mice died before implantation, displaying defective blastocyst development. These findings indicate that Psmc3 and Psmc4 have similar and essential roles in early embryogenesis and further that both ATPases have noncompensatory functions in vivo. PMID: [10945464] 

3. The mouse (Mus musculus) is the premier animal model for understanding human disease and development. Here we show that a comprehensive understanding of mouse biology is only possible with the availability of a finished, high-quality genome assembly. The finished clone-based assembly of the mouse strain C57BL/6J reported here has over 175,000 fewer gaps and over 139 Mb more of novel sequence, compared with the earlier MGSCv3 draft genome assembly. In a comprehensive analysis of this revised genome sequence, we are now able to define 20,210 protein-coding genes, over a thousand more than predicted in the human genome (19,042 genes). In addition, we identified 439 long, non-protein-coding RNAs with evidence for transcribed orthologs in human. We analyzed the complex and repetitive landscape of 267 Mb of sequence that was missing or misassembled in the previously published assembly, and we provide insights into the reasons for its resistance to sequencing and assembly by whole-genome shotgun approaches. Duplicated regions within newly assembled sequence tend to be of more recent ancestry than duplicates in the published draft, correcting our initial understanding of recent evolution on the mouse lineage. These duplicates appear to be largely composed of sequence regions containing transposable elements and duplicated protein-coding genes; of these, some may be fixed in the mouse population, but at least 40% of segmentally duplicated sequences are copy number variable even among laboratory mouse strains. Mouse lineage-specific regions contain 3,767 genes drawn mainly from rapidly-changing gene families associated with reproductive functions. The finished mouse genome assembly, therefore, greatly improves our understanding of rodent-specific biology and allows the delineation of ancestral biological functions that are shared with human from derived functions that are not. PMID: [19468303] 

4. The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a random strategy to select clones from a large number of cDNA libraries from diverse tissues. Candidate clones were chosen based on 5'-EST sequences, and then fully sequenced to high accuracy and analyzed by algorithms developed for this project. Currently, more than 11,000 human and 10,000 mouse genes are represented in MGC by at least one clone with a full ORF. The random selection approach is now reaching a saturation point, and a transition to protocols targeted at the missing transcripts is now required to complete the mouse and human collections. Comparison of the sequence of the MGC clones to reference genome sequences reveals that most cDNA clones are of very high sequence quality, although it is likely that some cDNAs may carry missense variants as a consequence of experimental artifact, such as PCR, cloning, or reverse transcriptase errors. Recently, a rat cDNA component was added to the project, and ongoing frog (Xenopus) and zebrafish (Danio) cDNA projects were expanded to take advantage of the high-throughput MGC pipeline. PMID: [15489334] 

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The 26S protease is involved in the ATP-dependentdegradation of ubiquitinated proteins. The regulatory (or ATPase)complex confers ATP dependency and substrate specificity to the26S complex (By similarity). 
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Subcellular Location
Cytoplasm (Potential). Nucleus (Potential). 
Tissue Specificity
Gene Ontology
GO IDGO termEvidence
GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell.
GO:0005634 C:nucleus IEA:UniProtKB-SubCell.
GO:0000502 C:proteasome complex IEA:UniProtKB-KW.
GO:0005524 F:ATP binding IEA:UniProtKB-KW.
GO:0017111 F:nucleoside-triphosphatase activity IEA:InterPro.
GO:0001824 P:blastocyst development IMP:MGI.
GO:0030163 P:protein catabolic process IEA:InterPro.
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IPR005937;    26S_Psome_P45.
IPR003593;    AAA+_ATPase.
IPR003959;    ATPase_AAA_core.
IPR003960;    ATPase_AAA_CS.
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PF00004;    AAA;    1.
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SM00382;    AAA;    1.
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PS00674;    AAA;    1.
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Created Date
Record Type
GAS predicted 
Sequence Annotation
CHAIN         1    442       26S protease regulatory subunit 6A.
NP_BIND     230    237       ATP (Potential).
MOD_RES      12     12       Phosphoserine (By similarity).
CONFLICT    170    170       E -> D (in Ref. 1; BAA32559 and 2;
CONFLICT    399    399       C -> S (in Ref. 1; BAA32559 and 2;
CONFLICT    423    423       Y -> H (in Ref. 1; BAA32559 and 2;
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Nucleotide Sequence
Length: 1569 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 442 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
Gene Symbol Ref Databases
Other Protein-Protein interaction resources
String database  
View Microarray data