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Identification
HMDB Protein ID HMDBP08049
Secondary Accession Numbers
  • 13760
Name Tubulin beta-6 chain
Synonyms Not Available
Gene Name TUBB6
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:1
Locus 18p11.21
SNPs TUBB6
Gene Sequence
>1341 bp
ATGAGGGAGATCGTGCACATCCAGGCGGGCCAGTGCGGGAACCAGATCGGCACCAAGTTT
TGGGAAGTGATCAGCGATGAGCACGGCATCGACCCGGCCGGAGGCTACGTGGGAGACTCG
GCGCTGCAGCTGGAGAGAATCAACGTCTACTACAATGAGTCATCGTCTCAGAAATATGTG
CCCAGGGCCGCCCTGGTGGACTTAGAGCCAGGCACCATGGACAGCGTGCGGTCTGGGCCT
TTTGGGCAGCTTTTCCGGCCTGACAACTTCATCTTTGGCCAGACGGGTGCAGGGAACAAC
TGGGCGAAAGGGCACTACACGGAGGGCGCGGAGCTGGTGGACGCAGTGCTGGACGTGGTG
CGGAAGGAGTGCGAGCACTGCGACTGCCTGCAGGGCTTCCAGCTCACGCACTCGCTGGGC
GGCGGCACGGGCTCAGGCATGGGCACGCTGCTCATCAGCAAGATCCGTGAGGAGTTCCCG
GACCGCATCATGAACACCTTCAGCGTCATGCCCTCGCCCAAGGTGTCGGACACGGTGGTG
GAGCCCTACAATGCCACACTGTCGGTGCACCAGCTGGTGGAGAATACAGACGAGACCTAC
TGCATCGACAACGAGGCGCTCTATGACATCTGCTTCCGCACTCTGAAGCTGACAACGCCC
ACCTACGGGGACCTCAACCACCTGGTGTCCGCCACCATGAGTGGGGTCACCACCTCGCTG
CGCTTCCCGGGCCAGCTCAATGCTGACCTGCGCAAGCTGGCGGTGAACATGGTGCCCTTC
CCGCGCCTGCACTTCTTCATGCCTGGCTTCGCGCCGCTCACCAGCCGCGGCAGCCAGCAG
TACCGGGCCCTGACCGTGCCCGAGCTCACCCAGCAGATGTTCGACGCCAGGAACATGATG
GCCGCCTGCGATCCGCGCCATGGCCGCTACCTGACCGTGGCCACCGTGTTCCGCGGGCCC
ATGTCCATGAAGGAGGTGGACGAGCAGATGCTGGCCATCCAGAGTAAGAACAGCAGCTAC
TTCGTGGAGTGGATTCCCAACAACGTGAAGGTGGCCGTGTGCGACATCCCGCCCCGCGGC
CTGAAGATGGCCTCCACCTTCATCGGCAACAGCACGGCCATCCAGGAGCTGTTCAAGCGC
ATCTCCGAGCAGTTCTCAGCCATGTTCCGGCGCAAGGCCTTCCTGCACTGGTTCACGGGT
GAGGGCATGGATGAAATGGAGTTCACCGAGGCGGAGAGCAACATGAACGACCTGGTATCC
GAGTACCAGCAGTACCAGGATGCCACCGCCAATGACGGGGAGGAAGCTTTTGAGGATGAG
GAAGAGGAGATCGATGGATAG
Protein Properties
Number of Residues 446
Molecular Weight 49856.8
Theoretical pI 4.51
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Tubulin beta-6 chain
MREIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGGYVGDSALQLERINVYYNESSSQKYV
PRAALVDLEPGTMDSVRSGPFGQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVV
RKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFPDRIMNTFSVMPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTSL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDARNMM
AACDPRHGRYLTVATVFRGPMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRG
LKMASTFIGNSTAIQELFKRISEQFSAMFRRKAFLHWFTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATANDGEEAFEDEEEEIDG
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q9BUF5
UniProtKB/Swiss-Prot Entry Name TBB6_HUMAN
PDB IDs
GenBank Gene ID AK001295
GeneCard ID TUBB6
GenAtlas ID TUBB6
HGNC ID HGNC:20776
References
General References
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  3. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed:17525332 ]
  4. Rogowski K, Juge F, van Dijk J, Wloga D, Strub JM, Levilliers N, Thomas D, Bre MH, Van Dorsselaer A, Gaertig J, Janke C: Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation. Cell. 2009 Jun 12;137(6):1076-87. doi: 10.1016/j.cell.2009.05.020. [PubMed:19524510 ]