Tag Content
UniProt Accession
Theoretical PI
Molecular Weight
41493 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Gene Synonyms/Alias
Mrg15, Tex189 
Protein Name
Mortality factor 4-like protein 1 
Protein Synonyms/Alias
MORF-related gene 15 protein; Testis-expressed gene 189 protein; Transcription factor-like protein MRG15; 
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. The seven member, human MORF4 related gene (MRG) family was recently identified based on the ability of Mortality factor on chromosome 4 (MORF4) to induce replicative senescence in immortal cell lines assigned to complementation group B (Bertram et al., 1999. Mol. Cell Biol. 19, 1479-1485). Initial computer based similarity searches identified human retinoblastoma binding protein 1 (RBP-1), Drosophila melanogaster male specific lethal-3 (Msl-3), S. pombe altered polarity-13 (Alp13) and S. cerevisiae Eaf3p, a component of the yeast NuA4 HAT complex (Galarneau et al., 2000. Mol. Cell 5, 927-937), as having similarity to the human MRG protein family. This suggested that the MRG family might be found in multiple species, and analysis of other homologs would provide functional and evolutionary insights into this gene family. Here, we report that MRG family members are present in twenty-three species based on molecular assays and sequence similarity searches. The new family members were divided into two groups based on similarity to the predominant human MRG family members, MRG15 and MRGX. The family members similar to MRG15 define a new, highly conserved subsection of the chromo domain superfamily. Additionally, conservation in the C-terminal two thirds of all the MRG family members and the Drosophila and human MSL-3 proteins defines a new protein domain, the MRG domain. These results indicate a highly conserved role for the MRG family in transcriptional regulation via chromatin remodeling by histone acetylation. PMID: [11290425] 

2. This study describes comprehensive polling of transcription start and termination sites and analysis of previously unidentified full-length complementary DNAs derived from the mouse genome. We identify the 5' and 3' boundaries of 181,047 transcripts with extensive variation in transcripts arising from alternative promoter usage, splicing, and polyadenylation. There are 16,247 new mouse protein-coding transcripts, including 5154 encoding previously unidentified proteins. Genomic mapping of the transcriptome reveals transcriptional forests, with overlapping transcription on both strands, separated by deserts in which few transcripts are observed. The data provide a comprehensive platform for the comparative analysis of mammalian transcriptional regulation in differentiation and development. PMID: [16141072] 

3. 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] 

4. PAM14 has been found to associate in complexes with the MORF4/MRG family of proteins as well as Rb, the tumor suppressor protein. This suggested that it might be involved in cell growth, immortalization, and/or senescence. To elucidate the in vivo function of PAM14, we characterized the expression pattern of mouse Pam14 and generated PAM14-deficient (Pam14(-/-)) mice. Pam14 was widely expressed in all mouse tissues and as early as 7 days during embryonic development. Despite this ubiquitous expression in wild-type mice, Pam14(-/-) mice were healthy and fertile. Response to mitogenic stimulation and production of interleukin-2 were the same in stimulated splenic T cells from Pam14(-/-) mice as in control littermates. Cell growth rates of mouse embryonic fibroblasts (MEFs) from all three genotypes were the same, and immortalized cells were obtained from all cell cultures during continuous culture. There was also no difference in expression of growth-related genes in response to serum stimulation in the null versus control MEFs. These data demonstrate that PAM14 is not essential for normal mouse development and cell cycle control. PAM14 likely acts as an adaptor protein in nucleoprotein complexes and is probably compensated for by another functionally redundant protein(s). PMID: [15367658] 

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Component of the NuA4 histone acetyltransferase complexwhich is involved in transcriptional activation of select genesprincipally by acetylation of nucleosomal histones H4 and H2A.This modification may both alter nucleosome - DNA interactions andpromote interaction of the modified histones with other proteinswhich positively regulate transcription. This complex may berequired for the activation of transcriptional programs associatedwith oncogene and proto-oncogene mediated growth induction, tumorsuppressor mediated growth arrest and replicative senescence,apoptosis, and DNA repair. The NuA4 complex ATPase and helicaseactivities seem to be, at least in part, contributed by theassociation of RUVBL1 and RUVBL2 with EP400. NuA4 may also play adirect role in DNA repair when directly recruited to sites of DNAdamage. Also component of the mSin3A complex which acts to represstranscription by deacetylation of nucleosomal histones. Requiredfor homologous recombination repair (HRR) and resistance tomitomycin C (MMC). Involved in the localization of PALB2, BRCA2and RAD51, but not BRCA1, to DNA-damage foci (By similarity). 
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Subcellular Location
Nucleus (By similarity). 
Tissue Specificity
Gene Ontology
GO IDGO termEvidence
GO:0035267 C:NuA4 histone acetyltransferase complex ISS:UniProtKB.
GO:0016580 C:Sin3 complex ISS:UniProtKB.
GO:0003682 F:chromatin binding IDA:MGI.
GO:0008283 P:cell proliferation IMP:MGI.
GO:0006338 P:chromatin remodeling TAS:MGI.
GO:0000724 P:double-strand break repair via homologous recombination ISS:UniProtKB.
GO:0016575 P:histone deacetylation ISS:UniProtKB.
GO:0043968 P:histone H2A acetylation ISS:UniProtKB.
GO:0043967 P:histone H4 acetylation ISS:UniProtKB.
GO:0040008 P:regulation of growth IEA:UniProtKB-KW.
GO:0006355 P:regulation of transcription, DNA-dependent IEA:UniProtKB-KW.
GO:0006351 P:transcription, DNA-dependent IEA:UniProtKB-KW.
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IPR016197;    Chromodomain-like.
IPR017398;    EAF3/MRG15.
IPR008676;    MRG.
IPR026541;    MRG_dom.
IPR025995;    Tudor-knot.
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PF05712;    MRG;    1.
PF11717;    Tudor-knot;    1.
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PS51640;    MRG;    1.
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Created Date
Record Type
GAS predicted 
Sequence Annotation
CHAIN         1    362       Mortality factor 4-like protein 1.
DOMAIN      191    362       MRG.
REGION       26     62       Interaction with KAT8 (By similarity).
REGION      133    266       Sufficient for interaction with SIN3A (By
REGION      164    230       Interaction with RB1-1 (By similarity).
REGION      188    342       Sufficient for interaction with PHF12 (By
REGION      323    344       Interaction with RB1-2 (By similarity).
MOTIF       135    146       Nuclear localization signal (Potential).
MOD_RES     143    143       N6-acetyllysine (By similarity).
                             -> N (in isoform 2).
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Nucleotide Sequence
Length: 1711 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 362 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
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