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P07437 (TBB5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tubulin beta chain
Alternative name(s):
Tubulin beta-5 chain
Gene names
Name:TUBB
Synonyms:TUBB5
ORF Names:OK/SW-cl.56
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length444 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

May interact with RNABP10 By similarity. Interacts with MX1 By similarity. 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. Interacts with PIFO. Ref.15

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

Ubiquitously expressed with highest levels in spleen, thymus and immature brain. Ref.14

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
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

cell division

Traceable author statement PubMed 12090300. Source: BHF-UCL

cellular component movement

Traceable author statement PubMed 16130169. Source: UniProtKB

cytoskeleton-dependent intracellular transport

Traceable author statement PubMed 12090300. Source: BHF-UCL

microtubule-based process

Traceable author statement PubMed 12090300. Source: BHF-UCL

natural killer cell mediated cytotoxicity

Non-traceable author statement PubMed 11120798. Source: UniProtKB

protein polymerization

Inferred from electronic annotation. Source: InterPro

spindle assembly

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell body

Inferred from direct assay PubMed 19567321. Source: DFLAT

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

nuclear envelope lumen

Inferred from direct assay PubMed 19567321. Source: DFLAT

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

MHC class I protein binding

Inferred from direct assay PubMed 11120798. Source: UniProtKB

structural constituent of cytoskeleton

Inferred from electronic annotation. Source: Ensembl

structural molecule activity

Traceable author statement PubMed 12090300. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LRRK2Q5S0073EBI-350864,EBI-5323863

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Tubulin beta chain
PRO_0000048243

Regions

Nucleotide binding140 – 1467GTP Potential

Amino acid modifications

Modified residue581N6-acetyllysine; alternate Ref.13
Modified residue581N6-succinyllysine; alternate By similarity
Modified residue1721Phosphoserine; by CDK1 By similarity
Modified residue3181Omega-N-methylarginine Ref.9
Cross-link58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Cross-link324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Experimental info

Sequence conflict2161K → R Ref.1
Sequence conflict2161K → R Ref.2
Sequence conflict2311A → G Ref.1
Sequence conflict2311A → G Ref.2
Sequence conflict234 – 2352SG → EC Ref.1
Sequence conflict234 – 2352SG → EC Ref.2
Sequence conflict2881E → D Ref.1
Sequence conflict2881E → D Ref.2
Sequence conflict2981N → D in AAH20946. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P07437 [UniParc].

Last modified December 21, 2004. Version 2.
Checksum: 1E6CD0A36773A103

FASTA44449,671
        10         20         30         40         50         60 
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY YNEATGGKYV 

        70         80         90        100        110        120 
PRAILVDLEP 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 QQVFDAKNMM 

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

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

       430        440 
EYQQYQDATA EEEEDFGEEA EEEA 

« Hide

References

« Hide 'large scale' references
[1]"Evolutionary history of a multigene family: an expressed human beta-tubulin gene and three processed pseudogenes."
Lee M.G.-S., Lewis S.A., Wilde C.D., Cowan N.J.
Cell 33:477-487(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Identification of two human beta-tubulin isotypes."
Hall J.L., Dudley L., Dobner P.R., Lewis S.A., Cowan N.J.
Mol. Cell. Biol. 3:854-862(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Tubulins in the primate retina: evidence that xanthophylls may be endogenous ligands for the paclitaxel-binding site."
Crabtree D.V., Ojima I., Geng X., Adler A.J.
Bioorg. Med. Chem. 9:1967-1976(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retina.
[4]Yu W., Gibbs R.A.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
Shiina S., Tamiya G., Oka A., Inoko H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Genome diversity in HLA: a new strategy for detection of genetic polymorphisms in expressed genes within the HLA class III and class I regions."
Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
Shichijo S., Itoh K.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon adenocarcinoma.
[8]"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, Eye, Lung, Muscle and Placenta.
[9]Bienvenut W.V., Campbell A., Ozanne B.W., Lourenco F., Olson M.F.
Submitted (DEC-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-19; 47-77; 104-174; 242-276; 283-297; 310-359 AND 363-390, METHYLATION AT ARG-318, MASS SPECTROMETRY.
Tissue: Foreskin fibroblast and Mammary carcinoma.
[10]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 3-19; 47-58; 63-77; 104-121; 163-174; 242-251; 253-276; 283-297; 310-318; 325-336 AND 381-390, MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[11]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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.
[13]"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].
[14]"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.
[15]"Pitchfork regulates primary cilia disassembly and left-right asymmetry."
Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.
Dev. Cell 19:66-77(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIFO.
[16]"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.

Web resources

Wikipedia

Tubulin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J00314 Genomic DNA. Translation: AAB59507.1.
AF141349 mRNA. Translation: AAD33873.1.
AF070561 mRNA. Translation: AAC28642.1.
AF070593 mRNA. Translation: AAC28650.1.
AF070600 mRNA. Translation: AAC28654.1.
BA000025 Genomic DNA. Translation: BAB63321.1.
AB088100 Genomic DNA. Translation: BAC54932.1.
AB062393 mRNA. Translation: BAB93480.1.
BC001938 mRNA. Translation: AAH01938.1.
BC002347 mRNA. Translation: AAH02347.1.
BC005838 mRNA. Translation: AAH05838.1.
BC007605 mRNA. Translation: AAH07605.1.
BC013374 mRNA. Translation: AAH13374.1.
BC019924 mRNA. Translation: AAH19924.1.
BC020946 mRNA. Translation: AAH20946.1.
BC021909 mRNA. Translation: AAH21909.1.
BC070326 mRNA. Translation: AAH70326.1.
PIRA26561.
RefSeqNP_821133.1. NM_178014.2.
UniGeneHs.636480.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QNZX-ray2.20C429-438[»]
3QO0X-ray2.30C422-441[»]
ProteinModelPortalP07437.
SMRP07437. Positions 2-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128444. 179 interactions.
IntActP07437. 71 interactions.
MINTMINT-1146393.
STRING9606.ENSP00000410071.

Chemistry

BindingDBP07437.
ChEMBLCHEMBL5444.
DrugBankDB01394. Colchicine.
DB00570. Vinblastine.
DB00541. Vincristine.
DB00361. Vinorelbine.
GuidetoPHARMACOLOGY2640.

PTM databases

PhosphoSiteP07437.

Polymorphism databases

DMDM56757569.

2D gel databases

OGPP07437.
REPRODUCTION-2DPAGEP07437.
SWISS-2DPAGEP07437.
UCD-2DPAGEP07437.

Proteomic databases

PaxDbP07437.
PRIDEP07437.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327892; ENSP00000339001; ENSG00000196230.
ENST00000383564; ENSP00000373058; ENSG00000183311.
ENST00000419792; ENSP00000401317; ENSG00000235067.
ENST00000421473; ENSP00000399155; ENSG00000224156.
ENST00000422650; ENSP00000400663; ENSG00000229684.
ENST00000422674; ENSP00000406811; ENSG00000227739.
ENST00000432462; ENSP00000410829; ENSG00000232421.
ENST00000436628; ENSP00000410071; ENSG00000232575.
GeneID203068.
KEGGhsa:203068.
UCSCuc003nrl.3. human.

Organism-specific databases

CTD203068.
GeneCardsGC06P030687.
GC06Pi30696.
GC06Pj30677.
GC06Pk30678.
GC06Pl30732.
GC06Pm30766.
GC06Pn30677.
GC06Po30679.
HGNCHGNC:20778. TUBB.
HPACAB005417.
CAB012406.
HPA043640.
HPA046280.
MIM191130. gene.
neXtProtNX_P07437.
PharmGKBPA358.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5023.
HOVERGENHBG000089.
InParanoidP07437.
KOK07375.
OMAELDYEDE.
PhylomeDBP07437.
TreeFamTF300298.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressP07437.
BgeeP07437.
CleanExHS_TUBB.
GenevestigatorP07437.

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

ChiTaRSTUBB. human.
GeneWikiTUBB.
GenomeRNAi203068.
NextBio90324.
PROP07437.
SOURCESearch...

Entry information

Entry nameTBB5_HUMAN
AccessionPrimary (citable) accession number: P07437
Secondary accession number(s): P05218, Q8WUC1, Q9CY33
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: December 21, 2004
Last modified: March 19, 2014
This is version 167 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM