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Reviewed, UniProtKB/Swiss-Prot Q13885 (TBB2A_HUMAN)

Last modified November 25, 2008. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tubulin beta-2A chain
Gene names
Name: TUBB2A
Synonyms: TUBB2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 By similarity.

Subunit structure

Dimer of alpha and beta chains By similarity.

Sequence similarities

Belongs to the tubulin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MDM2Q009871EBI-711595,EBI-389668

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Tubulin beta-2A chain
PRO_0000262648

Regions

Nucleotide binding140 – 1467GTP Potential

Natural variations

Natural variant621R → W in a colorectal cancer sample; somatic mutation.
VAR_036197

Experimental info

Sequence conflict1911Q → H in AAN85571. Ref.2
Sequence conflict2021I → H in CAG46756. Ref.3
Sequence conflict2631L → V in CAG46756. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q13885-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 93B3213EB2A9367B

FASTA44549,907
        10         20         30         40         50         60 
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEAAGNKYV 

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

       130        140        150        160        170        180 
RKESESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVM PSPKVSDTVV 

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

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

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

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

       430        440 
EYQQYQDATA DEQGEFEEEE GEDEA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and vaccinia virus expression of a cDNA containing the complete coding sequence of human beta tubulin mRNA."
Leffers H., Wiemann S., Ansorge W.
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skin.
[2]"Class II beta tubulin sequence from MCF7 breast cancer cells."
Banerjee A.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye and Skin.
[6]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 78-121; 242-251; 263-276; 310-318 AND 381-390, MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[7]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-62.
+Additional computationally mapped references.

Cross-references

Sequence databases

X79535 mRNA. Translation: CAA56071.1.
AY159127 mRNA. Translation: AAN85571.1.
CR541958 mRNA. Translation: CAG46756.1.
AL031963 Genomic DNA. Translation: CAD70628.1.
BC001194 mRNA. Translation: AAH01194.1.
BC018780 mRNA. Translation: AAH18780.1.
PIRT08726.
RefSeqNP_001060.1.
UniGeneHs.654543

3D structure databases

HSSPHSSP built from PDB template 1FFX based on UniProtKB P02554.
SMRQ13885. Positions 2-427.
ModBaseSearch...

Protein-protein interaction databases

IntActQ13885.

PTM databases

PhosphoSiteQ13885.

Proteomic databases

PeptideAtlasQ13885.

Genome annotation databases

EnsemblENSG00000137267. Homo sapiens. [Contig view]
GeneID7280.
KEGGhsa:7280.

Organism-specific databases

HGNCHGNC:12412. TUBB2A.
HPACAB015339.
PharmGKBPA142670670.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENQ13885.

Gene expression databases

CleanExHS_TUBB2A.
GermOnlineENSG00000137267. Homo sapiens.

Family and domain databases

InterProIPR013838. Beta-tubulin_BS.
IPR002453. Beta_tubulin.
IPR000158. Cell_division_FtsZ_N.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR003008. Tubulin_FtsZ.
[Graphical view]
Gene3DG3DSA:3.40.50.1440. Tubulin_FtsZ. 1 hit.
PANTHERPTHR11588:SF9. Beta_tubulin. 1 hit.
PTHR11588. Tubulin. 1 hit.
PfamPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSPR01163. BETATUBULIN.
PR00423. CELLDVISFTSZ.
PR01161. TUBULIN.
PROSITEPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio28467.

Entry information

Entry nameTBB2A_HUMAN
AccessionPrimary (citable) accession number: Q13885
Secondary accession number(s): Q6FGZ8, Q8IWR2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 1, 1996
Last modified: November 25, 2008
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 6

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents