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Q9D6F9 (TBB4A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. 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

Names and origin

Protein namesRecommended name:
Tubulin beta-4A chain
Alternative name(s):
Tubulin beta-4 chain
Gene names
Name:Tubb4a
Synonyms:Tubb4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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

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.

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.

Sequence similarities

Belongs to the tubulin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Tubulin beta-4A chain
PRO_0000048254

Regions

Nucleotide binding140 – 1467GTP Potential

Amino acid modifications

Modified residue1721Phosphoserine; by CDK1 By similarity

Experimental info

Sequence conflict731M → I in AAA40509. Ref.4
Sequence conflict1111E → Q in AAA40509. Ref.4
Sequence conflict2701F → L in AAA40509. Ref.4
Sequence conflict2931M → V in AAA40509. Ref.4
Sequence conflict3031C → S in AAA40509. Ref.4
Sequence conflict3511T → A in AAA40509. Ref.4
Sequence conflict4001G → A in AAA40509. Ref.4
Sequence conflict4271D → G in BAB28967. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9D6F9 [UniParc].

Last modified May 1, 2007. Version 3.
Checksum: F7429D057C11A3F5

FASTA44449,586
        10         20         30         40         50         60 
MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY YNEATGGNYV 

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

       130        140        150        160        170        180 
RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEFP 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 LSVQSKNSSY FVEWIPNNVK TAVCDIPPRG 

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

       430        440 
EYQQYQDATA EEGEFEEEAE EEVA 

« Hide

References

« Hide 'large scale' references
[1]"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: Hippocampus.
[2]"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].
Strain: C57BL/6.
Tissue: Brain and Olfactory epithelium.
[3]Lubec G., Klug S., Kang S.U.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 3-19; 47-77; 104-121; 163-174; 242-276; 283-297; 310-318; 321-359; 363-379 AND 381-390, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[4]"Five mouse tubulin isotypes and their regulated expression during development."
Lewis S.A., Lee M.G.-S., Cowan N.J.
J. Cell Biol. 101:852-861(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-444.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK013717 mRNA. Translation: BAB28967.1.
BC049112 mRNA. Translation: AAH49112.1.
BC054831 mRNA. Translation: AAH54831.1.
M28730 mRNA. Translation: AAA40509.1.
RefSeqNP_033477.2. NM_009451.3.
UniGeneMm.7420.

3D structure databases

ProteinModelPortalQ9D6F9.
SMRQ9D6F9. Positions 2-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204380. 5 interactions.
IntActQ9D6F9. 8 interactions.
MINTMINT-4137071.

Chemistry

BindingDBQ9D6F9.

PTM databases

PhosphoSiteQ9D6F9.

2D gel databases

REPRODUCTION-2DPAGEIPI00109073.
Q9D6F9.

Proteomic databases

PRIDEQ9D6F9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000071135; ENSMUSP00000071135; ENSMUSG00000062591.
GeneID22153.
KEGGmmu:22153.
UCSCuc008dea.1. mouse.

Organism-specific databases

CTD10382.
MGIMGI:107848. Tubb4a.

Phylogenomic databases

GeneTreeENSGT00750000117394.
HOGENOMHOG000165710.
HOVERGENHBG000089.
InParanoidQ9D6F9.
KOK07375.
OMAAENSDCL.
OrthoDBEOG71ZP1H.
PhylomeDBQ9D6F9.
TreeFamTF300298.

Enzyme and pathway databases

ReactomeREACT_147847. Translocation of Glut4 to the Plasma Membrane.

Gene expression databases

BgeeQ9D6F9.
CleanExMM_TUBB4.
GenevestigatorQ9D6F9.

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

NextBio302070.
PROQ9D6F9.
SOURCESearch...

Entry information

Entry nameTBB4A_MOUSE
AccessionPrimary (citable) accession number: Q9D6F9
Secondary accession number(s): Q62364, Q80Y54
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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