Tag Content
SG ID
SG00019781 
UniProt Accession
Theoretical PI
5.31  
Molecular Weight
41793 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Actg1 
Gene Synonyms/Alias
Actg 
Protein Name
Actin, cytoplasmic 2 Actin, cytoplasmic 2, N-terminally processed 
Protein Synonyms/Alias
Gamma-actin;Contains: 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:11;120207004-120209856;-1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.049300407 
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.
Description
Temporarily unavailable 
Abstract of related literatures
1. Actin was purified from calf thymus, bovine brain and SV40-transformed mouse 3T3 cells grown in tissue culture. Isoelectric focusing analysis showed the presence of the two actin polypeptides beta and gamma typical for non-muscle actins in all three actins. Tryptic and thermolytic peptides accounting for the complete amino-acid sequence of the cytoplasmic actins were separated and isolated by preparative fingerprint techniques. All peptides were characterized by amino-acid analysis and compared with the corresponding peptides from rabbit skeletal muscle actin. Peptides which differed in amino-acid composition from the corresponding skeletal muscle actin peptides were subjected to sequence analysis in order to localize the amino-acid replacement. The results obtained show that all three mammalian cytoplasmic actins studied contain the same amino-acid exchanges indicating that mammalian cytoplasmic actins are very similar if not identical in amino-acid sequence. The presence of two different isoelectric species beta and gamma in cytoplasmic actins from higher vertebrates is acccounted for by the isolation of two very similar but not identical amino-terminal peptides in all three actin preparations. The nature of the amino-acid replacements in these two peptides not only accounts for the different isoelectric forms but also shows that beta and gamma cytoplasmic actins are the products of two different structural genes expressed in the same cell. The total number of amino-acid replacements so far detected in the comparison of these cytoplasmic actins and skeletal muscle actin is 25 for the beta chain and 24 for the gamma chain. With the exception of the amino-terminal three or four residues, which are responsible for the isoelectric differences, the replacements do not involve charged amino acids. The exchanges are not randomly distributed. No replacements were detected in regions 18--75 and 299--356 while the regions between residues 2--17 and 259--298 show a high number of replacements. In addition documentation for a few minor revisions of the amino acid sequence of rabbit skeletal muscle actin is provided. PMID: [213279] 

2. We described the structures of mouse cytoskeletal gamma-actin cDNA clones and showed that there is strong conservation of the untranslated regions with human gamma-actin cDNA. In addition, we found that the expression levels of beta- and gamma-actin mRNAs are differentially controlled in various mouse tissues and cell types but are coordinately increased in the cellular growing state. These results suggest that there are multiple regulatory mechanisms of cytoskeletal actin genes and are consistent with the argument that beta- and gamma-actins might have functional diversity in mammalian cells. PMID: [3221869] 

3. 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] 

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] 

5. The nucleotide sequence corresponding to almost the whole of a mouse gamma-cytoskeletal actin mRNA was determined from overlapping cloned DNA copies derived from brain mRNA. Several gamma-actin processed pseudogenes were isolated from a library of cloned DBA mouse genomic DNA, and the nucleotide sequences of these were determined and compared with that of the cDNA. This showed that two of these pseudogenes had arisen from a gene duplication or amplification event, and indicated that they had subsequently undergone partial correction against one another. The relative ages of the pseudogenes were estimated on the basis of their percentage divergence from the cDNA sequence and these were compared with an estimation based on the number of presumed silent mutations in the cDNA since each pseudogene had arisen. Consistent results were obtained, except in the case of one pseudogene which also showed an anomalous regional distribution of differences from the cDNA sequence. One way of accounting for the features of this anomalous pseudogene is by postulating that it is derived from a second functional gene for gamma-actin, different from that represented by the cDNA described here. PMID: [3210229] 

6. Metazoans employ reversible tyrosine phosphorylation to regulate innumerable biological processes. Thus, the large-scale identification of tyrosine phosphorylation sites from primary tissues is an essential step toward a molecular systems understanding of dynamic regulation in vivo. The relative paucity of phosphotyrosine has greatly limited its identification in large-scale phosphoproteomic experiments. However, using antiphosphotyrosine peptide immunoprecipitations, we report the largest study to date of tyrosine phosphorylation sites from primary tissue, identifying 414 unique tyrosine phosphorylation sites from murine brain. To measure the conservation of phosphorylated tyrosines and their surrounding residues, we constructed a computational pipeline and identified patterns of conservation within the signature of phosphotyrosine. PMID: [18034455] 

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Function
Actins are highly conserved proteins that are involvedin various types of cell motility and are ubiquitously expressedin all eukaryotic cells. 
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Subcellular Location
Cytoplasm, cytoskeleton. 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0030424 C:axon IEA:Compara.
GO:0043034 C:costamere TAS:MGI.
GO:0005829 C:cytosol IEA:Compara.
GO:0031941 C:filamentous actin IDA:MGI.
GO:0005524 F:ATP binding IEA:UniProtKB-KW.
GO:0005200 F:structural constituent of cytoskeleton IDA:MGI.
GO:0007409 P:axonogenesis IEA:Compara.
GO:0051592 P:response to calcium ion IEA:Compara.
GO:0045214 P:sarcomere organization IDA:MGI.
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Interpro
IPR004000;    Actin-like.
IPR020902;    Actin/actin-like_CS.
IPR004001;    Actin_CS.
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Pfam
PF00022;    Actin;    1.
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SMART
SM00268;    ACTIN;    1.
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PROSITE
PS00406;    ACTINS_1;    1.
PS00432;    ACTINS_2;    1.
PS01132;    ACTINS_ACT_LIKE;    1.
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PRINTS
PR00190;    ACTIN.;   
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Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
CHAIN         1    375       Actin, cytoplasmic 2.
                             /FTId=PRO_0000367101.
INIT_MET      1      1       Removed; alternate.
CHAIN         2    375       Actin, cytoplasmic 2, N-terminally
                             processed.
                             /FTId=PRO_0000000833.
MOD_RES       1      1       N-acetylmethionine; in Actin, cytoplasmic
                             2; alternate.
MOD_RES       2      2       N-acetylglutamate; in Actin, cytoplasmic
                             2, N-terminally processed.
MOD_RES      44     44       Methionine sulfoxide (By similarity).
MOD_RES      73     73       Tele-methylhistidine.
MOD_RES     169    169       Phosphotyrosine.
MOD_RES     198    198       Phosphotyrosine (By similarity).
MOD_RES     294    294       Phosphotyrosine (By similarity).
MOD_RES     318    318       Phosphothreonine (By similarity).
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Nucleotide Sequence
Length: 1779 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 375 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
Other Protein-Protein interaction resources
String database  
View Microarray data
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