Tmic
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NameTubulin alpha-1C chain
Synonyms
  • Alpha-tubulin 6
  • TUBA6
  • Tubulin alpha-6 chain
Gene NameTUBA1C
OrganismHuman
Amino acid sequence
>lcl|BSEQ0010972|Tubulin alpha-1C chain
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLTVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAVAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGADSADGEDEGEEY
Number of residues449
Molecular Weight49894.93
Theoretical pI4.73
GO Classification
Functions
  • structural molecule activity
  • GTP binding
  • GTPase activity
  • structural constituent of cytoskeleton
Processes
  • microtubule-based process
  • protein folding
  • cell division
  • 'de novo' posttranslational protein folding
  • cellular protein metabolic process
  • cytoskeleton-dependent intracellular transport
Components
  • cytoplasm
  • microtubule
  • nucleus
  • vesicle
General FunctionStructural molecule activity
Specific FunctionTubulin 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.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID13436317
UniProtKB IDQ9BQE3
UniProtKB Entry NameTBA1C_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0002754|1350 bp
ATGCGTGAGTGCATCTCCATCCACGTTGGCCAGGCTGGTGTCCAGATTGGCAATGCCTGC
TGGGAGCTCTACTGCCTGGAACACGGCATCCAGCCCGATGGCCAGATGCCAAGTGACAAG
ACCATTGGGGGAGGAGATGATTCCTTCAACACCTTCTTCAGTGAAACGGGTGCTGGCAAG
CATGTGCCCCGGGCAGTGTTTGTAGACTTGGAACCCACAGTCATTGATGAAGTTCGCACT
GGCACCTACCGCCAGCTCTTCCACCCTGAGCAGCTCATCACAGGCAAGGAAGATGCTGCC
AATAACTATGCCCGAGGGCACTACACCATTGGCAAGGAGATCATTGACCTCGTGTTGGAC
CGAATTCGCAAGCTGGCTGACCAGTGCACCGGTCTTCAGGGCTTCTTGGTTTTCCACAGC
TTTGGTGGGGGAACTGGTTCTGGGTTCACCTCGCTGCTCATGGAACGTCTCTCAGTTGAT
TATGGCAAGAAGTCCAAGCTGGAGTTCTCTATTTACCCGGCGCCCCAGGTTTCCACAGCT
GTAGTTGAGCCCTACAACTCCATCCTCACCACCCACACCACCCTGGAGCACTCTGATTGT
GCCTTCATGGTAGACAATGAGGCCATCTATGACATCTGTCGTAGAAACCTCGATATCGAG
CGCCCAACCTACACTAACCTTAACCGCCTTATTAGCCAGATTGTGTCCTCCATCACTGCT
TCCCTGAGATTTGATGGAGCCCTGAATGTTGACCTGACAGAATTCCAGACCAACCTGGTG
CCCTACCCCCGCATCCACTTCCCTCTGGCCACATATGCCCCTGTCATCTCTGCTGAGAAA
GCCTACCATGAACAGCTTACTGTAGCAGAGATCACCAATGCTTGCTTTGAGCCAGCCAAC
CAGATGGTGAAATGTGACCCTCGCCATGGTAAATACATGGCTTGCTGCCTGTTATACCGT
GGTGACGTGGTTCCCAAAGATGTCAATGCTGCCATTGCCACCATCAAAACCAAGCGTACC
ATCCAGTTTGTGGATTGGTGCCCCACTGGCTTCAAGGTTGGCATTAATTACCAGCCTCCC
ACTGTGGTGCCTGGCGGAGACCTGGCCAAGGTACAGAGAGCTGTGTGCATGCTGAGCAAT
ACCACAGCTGTTGCTGAGGCCTGGGCTCGCCTGGACCACAAGTTTGACCTGATGTATGCC
AAGCGTGCCTTTGTTCACTGGTACGTGGGTGAGGGGATGGAGGAAGGCGAGTTTTCAGAG
GCCCGTGAGGACATGGCTGCCCTTGAGAAGGATTATGAGGAGGTTGGAGCAGATAGTGCT
GACGGAGAGGATGAGGGTGAAGAGTATTAA
GenBank Gene IDBC004949
GeneCard IDNot Available
GenAtlas IDTUBA1C
HGNC IDHGNC:20768
Chromosome LocationNot Available
Locus12q12-q14
References
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  2. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. 17081983
  3. 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. 18691976
  4. 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. 18669648
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  9. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. 21269460
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