Tubulin beta chain (TUBB)

The protein contains 444 amino acids for an estimated molecular weight of 49671 Da.

 

Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. (updated: April 1, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  3. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  4. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

Interpro domains
Total structural coverage: 100%
Model score: 97
MODL_MODELLER-9.18

(right-click above to access to more options from the contextual menu)

VariantDescription
CDCBM6
CDCBM6
CDCBM6
CSCSC1
CSCSC1

The reference OMIM entry for this protein is 191130

Tubulin, beta; tubb
Tubulin, beta, class i
Tubb5
M40

CLONING

Cowan et al. (1981) identified presumed tubulin pseudogenes, and Wilde et al. (1982) presented evidence that one such gene was derived from its corresponding mRNA. Wilde et al. (1982) described the structure of 2 pseudogenes. One had no introns but had a polyadenylate signal and an oligoadenylate trait at its 3-prime end. It may have originated by reverse transcription of a processed messenger RNA followed by reintegration of the complementary DNA copy into the genome. Cleveland and Sullivan (1985) stated that in the human and rat genomes a few authentic tubulin genes are present 'amid a sea of pseudogenes.' Many of these are 'retroposons': they lack all intervening sequences, have a long coded poly(A) tract at the 3-prime end, and have a 10- to 15-basepair direct repeat in the 5-prime and 3-prime flanking DNA. Isolation of cDNA clones indicate the existence of 2 functional alpha-tubulin genes and 3 functional beta-tubulin genes in man. There may be more. Crabtree et al. (2001) cloned beta-tubulin, which they designated beta-Ib tubulin, from a human retina cDNA library. Using database analysis, Leandro-Garcia et al. (2010) identified 8 major beta-tubulins, including TUBB. Quantitative RT-PCR showed variable TUBB expression in all 21 normal human tissues examined, with highest expression in thymus, followed by brain, heart, and ovary, and lowest expression in testis and prostate. TUBB was the major tubulin-beta isotype in ovary, lymph node, thymus, and fetal liver. Abnormal TUBB expressed was detected in several tumor tissues compared with their normal counterparts. Using quantitative real-time PCR, Breuss et al. (2012) found that TUBB5 was among a group of beta-tubulins highly expressed in human fetal brain. TUBB5 was more highly expressed at gestational week 13 than at gestational week 22. In mouse embryonic brain, Tubb5 was more highly expressed than other beta-tubulins at all time points examined, with highest expression at embryonic day 14.5 (E14.5). In situ hybridization detected high Tubb5 expression throughout developing cortex, with strong expression in the preplate at E12.5 and in the subventricular zone at E14.5. Use of a fluorescence-tagged reporter indicated that Tubb5 protein was expressed in radial glial cells, intermediate progenitors, migrating neurons, and postmitotic neurons.

GENE FAMILY

Microtubules are constituent parts of a diverse variety of eukaryotic cell structures, e.g., the mitotic apparatus, cilia, flagella, and elements of the cytoskeleton. They consist principally of 2 soluble proteins, alpha- and beta-tubulin, each with a molecular weight of about 55,000. They are transcribed from different genes. Using chicken alpha- and beta-tubulin cDNA, Cleveland et al. (1980) concluded that human DNA contains about 14 copies per genome of alpha- and beta-tubulin genes. There is much evidence for evolutionary conservation of the tubulins. See 602660 for additional background. Based on Southern blot analysis with a chicken beta-tubulin probe, Lee et al. (1983) stated that beta-tubulin in humans is coded by a large gene family with 15 to 20 members. One subfamily, identified by using the 3-prime untranslated region of a beta-tubulin gene as a probe to screen genomic libraries, consists of an expressed gene, designated M40, and 3 processed pseudogenes. Two alternative polyadenylation sites cause the M40 gene to be expressed as 2 mRNAs, 1.8 and 2.6 kb. Two of the pseudogenes are derived from t ... More on the omim web site

Subscribe to this protein entry history

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

June 20, 2017: Protein entry updated
Automatic update: comparative model was added.

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 191130 was added.