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A2AQ07 (TBB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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-1 chain
Gene names
Name:Tubb1
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 length451 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 By similarity.

Subunit structure

Dimer of alpha and beta chains By similarity. Interacts with RANBP10. Ref.4

Subcellular location

Cytoplasm › cytoskeleton By similarity.

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 glycylated. 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 may regulate the assembly and dynamics of axonemal microtubules By similarity.

Sequence similarities

Belongs to the tubulin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Tubulin beta-1 chain
PRO_0000413097

Regions

Nucleotide binding140 – 1467GTP Potential

Amino acid modifications

Modified residue1721Phosphoserine; by CDK1 By similarity

Sequences

Sequence LengthMass (Da)Tools
A2AQ07 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 9E68D52353E9850F

FASTA45150,441
        10         20         30         40         50         60 
MREIVHIQIG QCGNQIGAKF WEVIGEEHGI DCAGSYCGTS ALQLERISVY YNEAYGKKYV 

        70         80         90        100        110        120 
PRAVLVDLEP GTMDSIRSSR LGVLFQPDSF VHGNSGAGNN WAKGHYTEGA ELIENVMDVV 

       130        140        150        160        170        180 
RRESESCDCL QGFQIVHSLG GGTGSGMGTL LMNKIREEYP DRILNSFSVM PSPKVSDTVV 

       190        200        210        220        230        240 
EPYNAVLSIH QLIENTDACF CIDNEALYDI CFRTLRLTTP TYGDLNHLVS LTMSGITTSL 

       250        260        270        280        290        300 
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTAQGSQQ YRALSVAELT QQMFDARNIM 

       310        320        330        340        350        360 
AACDPRRGRY LTVACIFRGK MSTKEVDQQL LSIQTRNSNC FVEWIPNNVK VAVCDIPPRG 

       370        380        390        400        410        420 
LNMAATFLGN NTAIQELFTR VSEHFSAMFR RRAFVHWYTS EGMDISEFGE AESDIHDLVS 

       430        440        450 
EYQQFQDVRA GLEDSEEDVE EAEVEAEDKD H

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
[4]"RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates noncentrosomal microtubules."
Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr., Shivdasani R.A.
J. Biol. Chem. 283:14109-14119(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RANBP10.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL844534 Genomic DNA. Translation: CAM26336.1.
CH466551 Genomic DNA. Translation: EDL06679.1.
BC147322 mRNA. Translation: AAI47323.1.
BC147323 mRNA. Translation: AAI47324.1.
BC147687 mRNA. Translation: AAI47688.1.
BC147698 mRNA. Translation: AAI47699.1.
IPIIPI00348094.
RefSeqNP_001074440.1. NM_001080971.2.
UniGeneMm.45285.
Mm.458353.

3D structure databases

ProteinModelPortalA2AQ07.
SMRA2AQ07. Positions 2-427.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000016399.

PTM databases

PhosphoSiteA2AQ07.

Proteomic databases

PaxDbA2AQ07.
PRIDEA2AQ07.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000016399; ENSMUSP00000016399; ENSMUSG00000016255.
GeneID545486.
KEGGmmu:545486.
UCSCuc008ofe.1. mouse.

Organism-specific databases

CTD81027.
MGIMGI:107814. Tubb1.

Phylogenomic databases

eggNOGCOG5023.
GeneTreeENSGT00700000104200.
HOGENOMHOG000165710.
HOVERGENHBG000089.
InParanoidA2AQ07.
KOK07375.
OMADACFCID.
OrthoDBEOG4QVCC0.

Enzyme and pathway databases

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

Gene expression databases

BgeeA2AQ07.
GenevestigatorA2AQ07.

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

NextBio412643.
SOURCESearch...

Entry information

Entry nameTBB1_MOUSE
AccessionPrimary (citable) accession number: A2AQ07
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: February 20, 2007
Last modified: May 1, 2013
This is version 62 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

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