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Q9ERD7 (TBB3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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-3 chain
Gene names
Name:Tubb3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length450 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. TUBB3 plays a critical role in proper axon guidance and mantainance. Ref.7

Subunit structure

Dimer of alpha and beta chains.

Subcellular location

Cytoplasm › cytoskeleton.

Domain

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

Post-translational modification

Some glutamate residues at the C-terminus are either polyglutamylated or polyglycylated. These 2 modifications occur exclusively on glutamate residues and result in either polyglutamate or polyglycine chains on the gamma-carboxyl group. Glycylation 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 polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they are regulate the assembly and dynamics of axonemal microtubules.

Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules.

Sequence similarities

Belongs to the tubulin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Tubulin beta-3 chain
PRO_0000048251

Regions

Nucleotide binding140 – 1467GTP Potential

Amino acid modifications

Modified residue1721Phosphoserine; by CDK1 By similarity

Experimental info

Mutagenesis2621R → C: Brain from homozygous mice shows defects in the guidance of commissural axons and nerves, without evidence of cortical cells migration defects. Ref.7
Sequence conflict2061A → S in BAE28719. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9ERD7 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 4B9D9B7DBA102949

FASTA45050,419
        10         20         30         40         50         60 
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY YNEASSHKYV 

        70         80         90        100        110        120 
PRAILVDLEP GTMDSVRSGA FGHLFRPDNF IFGQSGAGNN WAKGHYTEGA ELVDSVLDVV 

       130        140        150        160        170        180 
RKECENCDCL QGFQLTHSLG GGTGSGMGTL LISKVREEYP DRIMNTFSVV PSPKVSDTVV 

       190        200        210        220        230        240 
EPYNATLSIH QLVENTDETY CIDNEALYDI CFRTLKLATP TYGDLNHLVS ATMSGVTTSL 

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

       310        320        330        340        350        360 
AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK VAVCDIPPRG 

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

       430        440        450 
EYQQYQDATA EEEGEMYEDD DEESEAQGPK

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of mouse tubulin beta-3 isotype."
Wu Y., Li C., Zhao S.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo, Spinal ganglion and Sympathetic ganglion.
[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: Olfactory epithelium and Retina.
[4]Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 63-77; 104-121; 217-251; 253-276; 310-318; 337-350 AND 381-390, MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[5]"Tubulin polyglutamylase enzymes are members of the TTL domain protein family."
Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M., Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S., Gaertig J., Edde B.
Science 308:1758-1762(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYGLUTAMYLATION.
[6]"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: POLYGLYCYLATION.
[7]"Human TUBB3 mutations perturb microtubule dynamics, kinesin interactions, and axon guidance."
Tischfield M.A., Baris H.N., Wu C., Rudolph G., Van Maldergem L., He W., Chan W.M., Andrews C., Demer J.L., Robertson R.L., Mackey D.A., Ruddle J.B., Bird T.D., Gottlob I., Pieh C., Traboulsi E.I., Pomeroy S.L., Hunter D.G. expand/collapse author list , Soul J.S., Newlin A., Sabol L.J., Doherty E.J., de Uzcategui C.E., de Uzcategui N., Collins M.L., Sener E.C., Wabbels B., Hellebrand H., Meitinger T., de Berardinis T., Magli A., Schiavi C., Pastore-Trossello M., Koc F., Wong A.M., Levin A.V., Geraghty M.T., Descartes M., Flaherty M., Jamieson R.V., Moller H.U., Meuthen I., Callen D.F., Kerwin J., Lindsay S., Meindl A., Gupta M.L. Jr., Pellman D., Engle E.C.
Cell 140:74-87(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-262.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF312873 mRNA. Translation: AAG26010.1.
AK012528 mRNA. Translation: BAB28299.1.
AK051298 mRNA. Translation: BAC34596.1.
AK149014 mRNA. Translation: BAE28719.1.
BC031357 mRNA. Translation: AAH31357.1.
BC088749 mRNA. Translation: AAH88749.1.
IPIIPI00112251.
RefSeqNP_075768.1. NM_023279.2.
UniGeneMm.40068.

3D structure databases

ProteinModelPortalQ9ERD7.
SMRQ9ERD7. Positions 2-427.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48419N.
IntActQ9ERD7. 7 interactions.

PTM databases

PhosphoSiteQ9ERD7.

2D gel databases

REPRODUCTION-2DPAGEIPI00112251.
Q9ERD7.
UCD-2DPAGEQ9ERD7.

Proteomic databases

PaxDbQ9ERD7.
PRIDEQ9ERD7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000071134; ENSMUSP00000071134; ENSMUSG00000062380.
GeneID22152.
KEGGmmu:22152.

Organism-specific databases

CTD10381.
MGIMGI:107813. Tubb3.

Phylogenomic databases

eggNOGCOG5023.
GeneTreeENSGT00700000104200.
HOGENOMHOG000165710.
HOVERGENHBG000089.
InParanoidQ9ERD7.
KOK07375.
OMAVIDVLTC.
OrthoDBEOG4W6NW0.

Enzyme and pathway databases

ReactomeREACT_147847. Translocation of Glut4 to the Plasma Membrane.
REACT_88307. Membrane Trafficking.

Gene expression databases

ArrayExpressQ9ERD7.
BgeeQ9ERD7.
CleanExMM_TUBB3.
GenevestigatorQ9ERD7.
GermOnlineENSMUSG00000062380. Mus musculus.

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]
SUPFAMSSF55307. Tub_FtsZ_C. 1 hit.
SSF52490. Tubulin_FtsZ. 1 hit.
PROSITEPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ9ERD7.
NextBio302066.
SOURCESearch...

Entry information

Entry nameTBB3_MOUSE
AccessionPrimary (citable) accession number: Q9ERD7
Secondary accession number(s): Q3UF42, Q5I036
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: March 1, 2001
Last modified: May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents