Tag Content
UniProt Accession
Theoretical PI
Molecular Weight
49831 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Gene Synonyms/Alias
Protein Name
Tubulin beta-4B chain 
Protein Synonyms/Alias
Tubulin beta-2C chain; 
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. We describe the structure of a novel and unusually heterologous beta-tubulin isotype (M beta 1) isolated from a mouse bone marrow cDNA library, and a second isotype (M beta 3) isolated from a mouse testis cDNA library. Comparison of M beta 1 and M beta 3 with the completed (M beta 4, M beta 5) or extended (M beta 2) sequence of three previously described beta-tubulin isotypes shows that each includes a distinctive carboxy-terminal region, in addition to multiple amino acid substitutions throughout the polypeptide chain. In every case where a mammalian interspecies comparison can be made, both the carboxy-terminal and internal amino acid substitutions that distinguish one isotype from another are absolutely conserved. We conclude that these characteristic differences are important in determining functional distinctions between different kinds of microtubule. The amino acid homologies between M beta 2, M beta 3, M beta 4, and M beta 5 are in the range of 95-97%; however the homology between M beta 1 and all the other isotypes is very much less (78%). The dramatic divergence in M beta 1 is due to multiple changes that occur throughout the polypeptide chain. The overall level of expression of M beta 1 is low, and is restricted to those tissues (bone marrow, spleen, developing liver and lung) that are active in hematopoiesis in the mouse. We predict that the M beta 1 isotype is functionally specialized for assembly into the mammalian marginal band. PMID: [3782288] 

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 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] 

5. Polyglutamylation of tubulin has been implicated in several functions of microtubules, but the identification of the responsible enzyme(s) has been challenging. We found that the neuronal tubulin polyglutamylase is a protein complex containing a tubulin tyrosine ligase-like (TTLL) protein, TTLL1. TTLL1 is a member of a large family of proteins with a TTL homology domain, whose members could catalyze ligations of diverse amino acids to tubulins or other substrates. In the model protist Tetrahymena thermophila, two conserved types of polyglutamylases were characterized that differ in substrate preference and subcellular localization. PMID: [15890843] 

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] 

7. Polyglycylation is a posttranslational modification that generates glycine side chains on proteins. Here we identify a family of evolutionarily conserved glycine ligases that modify tubulin using different enzymatic mechanisms. In mammals, two distinct enzyme types catalyze the initiation and elongation steps of polyglycylation, whereas Drosophila glycylases are bifunctional. We further show that the human elongating glycylase has lost enzymatic activity due to two amino acid changes, suggesting that the functions of protein glycylation could be sufficiently fulfilled by monoglycylation. Depletion of a glycylase in Drosophila using RNA interference results in adult flies with strongly decreased total glycylation levels and male sterility associated with defects in sperm individualization and axonemal maintenance. A more severe RNAi depletion is lethal at early developmental stages, indicating that protein glycylation is essential. Together with the observation that multiple proteins are glycylated, our functional data point towards a general role of glycylation in protein functions. PMID: [19524510] 

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Tubulin is the major constituent of microtubules. Itbinds two moles of GTP, one at an exchangeable site on the betachain and one at a non-exchangeable site on the alpha-chain. 
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Subcellular Location
Cytoplasm, cytoskeleton. 
Tissue Specificity
Gene Ontology
GO IDGO termEvidence
GO:0005737 C:cytoplasm IEA:UniProtKB-KW.
GO:0005874 C:microtubule IEA:UniProtKB-KW.
GO:0045298 C:tubulin complex NAS:UniProtKB.
GO:0005525 F:GTP binding NAS:UniProtKB.
GO:0003924 F:GTPase activity IEA:InterPro.
GO:0005198 F:structural molecule activity IEA:InterPro.
GO:0007018 P:microtubule-based movement IEA:InterPro.
GO:0007017 P:microtubule-based process NAS:UniProtKB.
GO:0051258 P:protein polymerization IEA:InterPro.
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IPR013838;    Beta-tubulin_BS.
IPR002453;    Beta_tubulin.
IPR008280;    Tub_FtsZ_C.
IPR000217;    Tubulin.
IPR018316;    Tubulin/FtsZ_2-layer-sand-dom.
IPR023123;    Tubulin_C.
IPR017975;    Tubulin_CS.
IPR003008;    Tubulin_FtsZ_GTPase.
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PF00091;    Tubulin;    1.
PF03953;    Tubulin_C;    1.
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SM00864;    Tubulin;    1.
SM00865;    Tubulin_C;    1.
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PS00227;    TUBULIN;    1.
PS00228;    TUBULIN_B_AUTOREG;    1.
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PR01163;    BETATUBULIN.;   
PR01161;    TUBULIN.;   
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Created Date
Record Type
GAS predicted 
Sequence Annotation
CHAIN         1    445       Tubulin beta-4B chain.
NP_BIND     140    146       GTP (Potential).
MOD_RES      51     51       Phosphotyrosine.
MOD_RES      55     55       Phosphothreonine (By similarity).
MOD_RES      58     58       N6-acetyllysine (By similarity).
MOD_RES     172    172       Phosphoserine; by CDK1 (By similarity).
MOD_RES     322    322       Phosphoserine (By similarity).
CONFLICT    207    207       L -> P (in Ref. 4; AAH05547).
CONFLICT    342    342       V -> A (in Ref. 2; BAE27282).
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Nucleotide Sequence
Length: bp   Go to nucleotide: FASTA
Protein Sequence
Length: 445 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
Other Protein-Protein interaction resources
String database  
View Microarray data