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Q6B856 (TBB2B_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. 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-2B chain
Gene names
Name:TUBB2B
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length445 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. 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 By similarity.

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 By similarity.

Sequence similarities

Belongs to the tubulin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Tubulin beta-2B chain
PRO_0000262654

Experimental info

Sequence conflict2011C → S in AAT84374. Ref.1

Secondary structure

............................................................................... 445
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q6B856 [UniParc].

Last modified November 28, 2006. Version 2.
Checksum: 4DC3956EFF880746

FASTA44549,953
        10         20         30         40         50         60 
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEATGNKYV 

        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 CIDNEALYDI 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]"Differentially expressed genes in bovine 8-cell embryo."
Hwang K.C., Park S.Y., Cui X.S., Kim N.H.
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The genome sequence of taurine cattle: a window to ruminant biology and evolution."
The bovine genome sequencing and analysis consortium
Science 324:522-528(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hereford.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY675081 mRNA. Translation: AAT84374.1.
RefSeqNP_001003900.1. NM_001003900.1.
UniGeneBt.105119.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SA0X-ray3.58B/D1-439[»]
1SA1X-ray4.20B/D1-439[»]
1TVKX-ray2.89B1-427[»]
1Z2BX-ray4.10B/D1-445[»]
2P4Nelectron microscopy9.00B1-445[»]
2WBEelectron microscopy9.40B1-445[»]
2XRPelectron microscopy8.20A/C/E/G1-445[»]
3DCOelectron microscopy1.90B1-445[»]
3DU7X-ray4.10B/D1-445[»]
3E22X-ray3.80B/D1-445[»]
3IZ0electron microscopy8.60B1-445[»]
3J1Telectron microscopy9.70C1-427[»]
3J1Uelectron microscopy9.70C1-427[»]
3J2Uelectron microscopy10.80B/D1-445[»]
4AQVelectron microscopy9.70B1-445[»]
4AQWelectron microscopy9.50B1-445[»]
4ATUelectron microscopy8.30A/C/E/G1-445[»]
4ATXelectron microscopy8.20A1-445[»]
4CK5electron microscopy10.00B1-445[»]
4CK6electron microscopy9.20B1-445[»]
4CK7electron microscopy9.20B1-445[»]
4I4TX-ray1.80B/D1-445[»]
4I50X-ray2.30B/D1-445[»]
4I55X-ray2.20B/D1-445[»]
4IHJX-ray2.00B/D1-445[»]
4IIJX-ray2.60B/D1-445[»]
4O2AX-ray2.50B/D1-445[»]
4O2BX-ray2.30B/D1-445[»]
4O4HX-ray2.10B/D1-445[»]
4O4IX-ray2.40B/D1-445[»]
4O4JX-ray2.20B/D1-445[»]
4O4LX-ray2.20B/D1-445[»]
ProteinModelPortalQ6B856.
SMRQ6B856. Positions 1-431.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid158875. 1 interaction.
IntActQ6B856. 6 interactions.
MINTMINT-6604256.

Chemistry

BindingDBQ6B856.
ChEMBLCHEMBL3394.

Proteomic databases

PaxDbQ6B856.
PRIDEQ6B856.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000005346; ENSBTAP00000005346; ENSBTAG00000004093.
GeneID281555.
KEGGbta:281555.

Organism-specific databases

CTD347733.

Phylogenomic databases

eggNOGCOG5023.
GeneTreeENSGT00740000115320.
HOGENOMHOG000165710.
HOVERGENHBG000089.
KOK07375.
OMAYQQEEEY.
OrthoDBEOG71ZP1H.
TreeFamTF300298.

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

EvolutionaryTraceQ6B856.
NextBio20805506.

Entry information

Entry nameTBB2B_BOVIN
AccessionPrimary (citable) accession number: Q6B856
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: July 9, 2014
This is version 87 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references