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P68371 (TBB4B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tubulin beta-4B chain
Alternative name(s):
Tubulin beta-2 chain
Tubulin beta-2C chain
Gene names
Name:TUBB4B
Synonyms:TUBB2C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

Ubiquitous. Ref.6

Domain

The highly acidic C-terminal region may bind cations such as calcium.

Post-translational modification

Some glutamate residues at the C-terminus are polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules Probable.

Sequence similarities

Belongs to the tubulin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' posttranslational protein folding

Traceable author statement. Source: Reactome

G2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

cellular component movement

Traceable author statement PubMed 16130169. Source: ProtInc

cellular protein metabolic process

Traceable author statement. Source: Reactome

microtubule-based process

Inferred from electronic annotation. Source: InterPro

mitotic cell cycle

Traceable author statement. Source: Reactome

natural killer cell mediated cytotoxicity

Non-traceable author statement PubMed 11120798. Source: UniProtKB

protein folding

Traceable author statement. Source: Reactome

protein polymerization

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoskeleton

Traceable author statement PubMed 16130169. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

MHC class I protein binding

Traceable author statement PubMed 11120798. Source: UniProtKB

double-stranded RNA binding

Inferred from direct assay PubMed 21266579. Source: MGI

structural constituent of cytoskeleton

Inferred from electronic annotation. Source: InterPro

unfolded protein binding

Non-traceable author statement PubMed 11120798. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Tubulin beta-4B chain
PRO_0000048248

Regions

Nucleotide binding140 – 1467GTP Potential

Amino acid modifications

Modified residue581N6-acetyllysine Ref.5
Modified residue1721Phosphoserine; by CDK1 Probable

Sequences

Sequence LengthMass (Da)Tools
P68371 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: A552C52822AFA072

FASTA44549,831
        10         20         30         40         50         60 
MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY YNEATGGKYV 

        70         80         90        100        110        120 
PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV 

       130        140        150        160        170        180 
RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV 

       190        200        210        220        230        240 
EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL 

       250        260        270        280        290        300 
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM 

       310        320        330        340        350        360 
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG 

       370        380        390        400        410        420 
LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS 

       430        440 
EYQQYQDATA EEEGEFEEEA EEEVA 

« Hide

References

« Hide 'large scale' references
[1]"Three expressed sequences within the human beta-tubulin multigene family each define a distinct isotype."
Lewis S.A., Gilmartin M.E., Hall J.L., Cowan N.J.
J. Mol. Biol. 182:11-20(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Cervix, Lung, Lymph, Muscle, Skin and Uterus.
[4]"Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.
Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCYLATION.
[5]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Tumoral and tissue-specific expression of the major human beta-tubulin isotypes."
Leandro-Garcia L.J., Leskela S., Landa I., Montero-Conde C., Lopez-Jimenez E., Leton R., Cascon A., Robledo M., Rodriguez-Antona C.
Cytoskeleton 67:214-223(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02344 Genomic DNA. Translation: CAA26203.1.
BX255925 Genomic DNA. Translation: CAM24148.1.
BC001911 mRNA. Translation: AAH01911.1.
BC002783 mRNA. Translation: AAH02783.1.
BC002885 mRNA. Translation: AAH02885.1.
BC004188 mRNA. Translation: AAH04188.1.
BC007889 mRNA. Translation: AAH07889.1.
BC012835 mRNA. Translation: AAH12835.1.
BC019359 mRNA. Translation: AAH19359.1.
BC019829 mRNA. Translation: AAH19829.1.
BC039175 mRNA. Translation: AAH39175.1.
BC071889 mRNA. Translation: AAH71889.1.
CCDSCCDS7039.1.
PIRI38370.
RefSeqNP_006079.1. NM_006088.5.
UniGeneHs.433615.

3D structure databases

ProteinModelPortalP68371.
SMRP68371. Positions 2-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115656. 116 interactions.
IntActP68371. 40 interactions.
MINTMINT-1390314.
STRING9606.ENSP00000341289.

Chemistry

BindingDBP68371.
ChEMBLCHEMBL2095182.

PTM databases

PhosphoSiteP68371.

Polymorphism databases

DMDM55977480.

2D gel databases

OGPP05217.
REPRODUCTION-2DPAGEIPI00007752.
SWISS-2DPAGEP68371.

Proteomic databases

MaxQBP68371.
PeptideAtlasP68371.
PRIDEP68371.

Protocols and materials databases

DNASU10383.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340384; ENSP00000341289; ENSG00000188229.
GeneID10383.
KEGGhsa:10383.
UCSCuc004cmg.1. human.

Organism-specific databases

CTD10383.
GeneCardsGC09P140136.
HGNCHGNC:20771. TUBB4B.
HPACAB010880.
HPA043640.
HPA046280.
MIM602660. gene.
neXtProtNX_P68371.
PharmGKBPA142670672.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000165710.
HOVERGENHBG000089.
InParanoidP68371.
KOK07375.
OMAREIVSIQ.
OrthoDBEOG71ZP1H.
PhylomeDBP68371.
TreeFamTF300298.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_11123. Membrane Trafficking.
REACT_115566. Cell Cycle.
REACT_17015. Metabolism of proteins.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP68371.
BgeeP68371.
CleanExHS_TUBB2C.
GenevestigatorP68371.

Family and domain databases

Gene3D1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProIPR013838. 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.
[Graphical view]
PANTHERPTHR11588. PTHR11588. 1 hit.
PfamPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSPR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTUBB4B. human.
GeneWikiTUBB2C.
GenomeRNAi10383.
NextBio39335.
PROP68371.
SOURCESearch...

Entry information

Entry nameTBB4B_HUMAN
AccessionPrimary (citable) accession number: P68371
Secondary accession number(s): A2BFA2, P05217
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM