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Identification
HMDB Protein ID HMDBP08598
Secondary Accession Numbers
  • 14313
Name Tubulin alpha-4A chain
Synonyms
  1. Alpha-tubulin 1
  2. Testis-specific alpha-tubulin
  3. Tubulin H2-alpha
  4. Tubulin alpha-1 chain
Gene Name TUBA4A
Protein Type Unknown
Biological Properties
General Function Involved in structural molecule activity
Specific Function 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
Pathways Not Available
Reactions Not Available
GO Classification
Component
macromolecular complex
protein complex
microtubule
Function
purine nucleotide binding
binding
nucleotide binding
catalytic activity
hydrolase activity
guanyl nucleotide binding
guanyl ribonucleotide binding
gtp binding
structural molecule activity
gtpase activity
nucleoside-triphosphatase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
pyrophosphatase activity
Process
cellular process
cellular component organization or biogenesis
cellular component organization
cellular component assembly
macromolecular complex assembly
cellular protein complex assembly
microtubule-based process
microtubule-based movement
protein complex assembly
protein polymerization
Cellular Location
  1. Cytoplasmic
Gene Properties
Chromosome Location Chromosome:2
Locus 2q35
SNPs TUBA4A
Gene Sequence
>1347 bp
ATGCGTGAATGCATCTCAGTCCACGTGGGGCAGGCAGGTGTCCAGATGGGCAATGCCTGC
TGGGAGCTCTATTGCTTGGAACATGGGATTCAGCCTGATGGGCAGATGCCCAGTGACAAG
ACCATTGGTGGAGGGGACGACTCCTTCACCACCTTCTTCTGTGAAACTGGTGCTGGAAAA
CACGTACCCCGGGCAGTTTTTGTGGATCTGGAGCCTACGGTCATTGATGAGATCCGAAAT
GGCCCATACCGACAGCTCTTCCACCCAGAGCAGCTCATCACTGGGAAAGAGGATGCTGCC
AACAACTATGCCCGTGGTCACTATACCATTGGCAAGGAGATCATTGACCCAGTGCTGGAT
CGGATCCGCAAGCTGTCTGACCAGTGCACAGGACTTCAGGGCTTCCTGGTGTTCCACAGC
TTTGGTGGGGGCACTGGCTCTGGCTTCACCTCACTCCTGATGGAGCGGCTCTCTGTTGAC
TATGGCAAGAAATCCAAGCTGGAATTCTCCATCTACCCAGCCCCCCAGGTGTCTACAGCC
GTGGTCGAGCCCTACAACTCTATCCTGACCACCCACACCACCCTGGAGCACTCAGACTGT
GCCTTCATGGTGGACAACGAAGCAATCTATGACATCTGCCGCCGCAACCTAGACATCGAG
CGCCCAACCTACACCAACCTCAATCGCCTCATTAGCCAAATTGTCTCCTCCATCACAGCT
TCTCTGCGCTTTGACGGGGCCCTCAATGTGGACCTGACAGAGTTCCAGACCAACCTGGTG
CCCTACCCTCGCATCCACTTCCCCCTGGCCACCTATGCACCAGTCATCTCTGCAGAAAAG
GCATACCACGAGCAGCTGTCGGTGGCAGAGATCACCAATGCCTGCTTTGAGCCTGCCAAC
CAGATGGTAAAGTGTGATCCCCGGCACGGCAAGTACATGGCCTGCTGCCTGCTGTACCGT
GGAGATGTGGTGCCCAAGGATGTCAACGCTGCCATTGCCGCCATCAAGACCAAGCGCAGC
ATTCAGTTTGTGGACTGGTGCCCCACAGGCTTCAAGGTTGGTATCAACTACCAGCCTCCC
ACTGTGGTGCCTGGGGGTGACCTGGCCAAGGTGCAGCGTGCCGTGTGCATGCTGAGCAAC
ACGACCGCCATCGCCGAGGCCTGGGCCCGCCTGGACCACAAGTTCGACCTGATGTATGCC
AAGAGGGCGTTTGTGCACTGGTATGTGGGTGAGGGCATGGAGGAGGGTGAGTTCTCCGAG
GCCCGTGAGGATATGGCTGCCCTGGAGAAGGATTATGAGGAGGTGGGCATCGACTCCTAT
GAGGACGAGGATGAGGGAGAAGAATAG
Protein Properties
Number of Residues 448
Molecular Weight 49924.0
Theoretical pI 4.69
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Tubulin alpha-4A chain
MRECISVHVGQAGVQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFTTFFCETGAGK
HVPRAVFVDLEPTVIDEIRNGPYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDPVLD
RIRKLSDQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIAAIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGIDSYEDEDEGEE
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P68366
UniProtKB/Swiss-Prot Entry Name TBA4A_HUMAN
PDB IDs
GenBank Gene ID BT006731
GeneCard ID TUBA4A
GenAtlas ID TUBA4A
HGNC ID HGNC:12407
References
General References
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  3. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed:15592455 ]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  5. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  7. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  8. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed:18088087 ]
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  10. Dobner PR, Kislauskis E, Wentworth BM, Villa-Komaroff L: Alternative 5' exons either provide or deny an initiator methionine codon to the same alpha-tubulin coding region. Nucleic Acids Res. 1987 Jan 12;15(1):199-218. [PubMed:3029670 ]