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Q6B856

- TBB2B_BOVIN

UniProt

Q6B856 - TBB2B_BOVIN

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Protein
Tubulin beta-2B chain
Gene
TUBB2B
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. GTPase activity Source: InterPro
  3. structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  1. microtubule-based process Source: InterPro
  2. neuron migration Source: Ensembl
  3. protein polymerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_209545. Resolution of Sister Chromatid Cohesion.
REACT_211133. MHC class II antigen presentation.
REACT_212887. Separation of Sister Chromatids.
REACT_214148. Formation of tubulin folding intermediates by CCT/TriC.
REACT_215331. Recruitment of NuMA to mitotic centrosomes.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-2B chain
Gene namesi
Name:TUBB2B
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 23

Subcellular locationi

Cytoplasmcytoskeleton By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. microtubule Source: UniProtKB-KW
  3. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Tubulin beta-2B chain
PRO_0000262654Add
BLAST

Post-translational modificationi

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.

Proteomic databases

PaxDbiQ6B856.
PRIDEiQ6B856.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi158875. 1 interaction.
IntActiQ6B856. 6 interactions.
MINTiMINT-6604256.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96
Helixi10 – 2718
Beta strandi34 – 363
Beta strandi39 – 413
Helixi42 – 454
Helixi47 – 493
Beta strandi51 – 544
Turni55 – 573
Beta strandi58 – 614
Beta strandi63 – 708
Helixi71 – 788
Helixi82 – 843
Helixi87 – 893
Beta strandi90 – 923
Helixi101 – 1055
Helixi108 – 12518
Beta strandi132 – 14211
Helixi143 – 15816
Beta strandi162 – 1709
Helixi173 – 1753
Helixi181 – 19515
Beta strandi197 – 2037
Helixi204 – 21310
Helixi222 – 23615
Helixi238 – 2414
Beta strandi245 – 2473
Helixi250 – 2578
Beta strandi265 – 2717
Beta strandi276 – 2783
Beta strandi280 – 2823
Helixi286 – 2938
Helixi296 – 2983
Beta strandi299 – 3024
Helixi305 – 3073
Beta strandi310 – 32011
Helixi323 – 33614
Helixi338 – 3403
Beta strandi343 – 3453
Beta strandi349 – 3557
Beta strandi362 – 37110
Helixi372 – 3743
Helixi375 – 38915
Turni390 – 3956
Helixi396 – 3994
Turni400 – 4023
Helixi405 – 42622

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ6B856.
SMRiQ6B856. Positions 1-431.

Miscellaneous databases

EvolutionaryTraceiQ6B856.

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00740000115320.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
KOiK07375.
OMAiYQQEEEY.
OrthoDBiEOG71ZP1H.
TreeFamiTF300298.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR013838. 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]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6B856-1 [UniParc]FASTAAdd to Basket

« Hide

MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY    50
YNEATGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN 100
WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL 150
LISKIREEYP DRIMNTFSVM PSPKVSDTVV EPYNATLSVH QLVENTDETY 200
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL 250
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM 300
AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK 350
TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG 400
EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEE GEDEA 445
Length:445
Mass (Da):49,953
Last modified:November 28, 2006 - v2
Checksum:i4DC3956EFF880746
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011C → S in AAT84374. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY675081 mRNA. Translation: AAT84374.1.
RefSeqiNP_001003900.1. NM_001003900.1.
UniGeneiBt.105119.

Genome annotation databases

EnsembliENSBTAT00000005346; ENSBTAP00000005346; ENSBTAG00000004093.
GeneIDi281555.
KEGGibta:281555.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY675081 mRNA. Translation: AAT84374.1 .
RefSeqi NP_001003900.1. NM_001003900.1.
UniGenei Bt.105119.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SA0 X-ray 3.58 B/D 1-439 [» ]
1SA1 X-ray 4.20 B/D 1-439 [» ]
1TVK X-ray 2.89 B 1-427 [» ]
1Z2B X-ray 4.10 B/D 1-445 [» ]
2P4N electron microscopy 9.00 B 1-445 [» ]
2WBE electron microscopy 9.40 B 1-445 [» ]
2XRP electron microscopy 8.20 A/C/E/G 1-445 [» ]
3DCO electron microscopy 1.90 B 1-445 [» ]
3DU7 X-ray 4.10 B/D 1-445 [» ]
3E22 X-ray 3.80 B/D 1-445 [» ]
3IZ0 electron microscopy 8.60 B 1-445 [» ]
3J1T electron microscopy 9.70 C 1-427 [» ]
3J1U electron microscopy 9.70 C 1-427 [» ]
3J2U electron microscopy 10.80 B/D 1-445 [» ]
4AQV electron microscopy 9.70 B 1-445 [» ]
4AQW electron microscopy 9.50 B 1-445 [» ]
4ATU electron microscopy 8.30 A/C/E/G 1-445 [» ]
4ATX electron microscopy 8.20 A 1-445 [» ]
4CK5 electron microscopy 10.00 B 1-445 [» ]
4CK6 electron microscopy 9.20 B 1-445 [» ]
4CK7 electron microscopy 9.20 B 1-445 [» ]
4I4T X-ray 1.80 B/D 1-445 [» ]
4I50 X-ray 2.30 B/D 1-445 [» ]
4I55 X-ray 2.20 B/D 1-445 [» ]
4IHJ X-ray 2.00 B/D 1-445 [» ]
4IIJ X-ray 2.60 B/D 1-445 [» ]
4O2A X-ray 2.50 B/D 1-445 [» ]
4O2B X-ray 2.30 B/D 1-445 [» ]
4O4H X-ray 2.10 B/D 1-445 [» ]
4O4I X-ray 2.40 B/D 1-445 [» ]
4O4J X-ray 2.20 B/D 1-445 [» ]
4O4L X-ray 2.20 B/D 1-445 [» ]
ProteinModelPortali Q6B856.
SMRi Q6B856. Positions 1-431.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 158875. 1 interaction.
IntActi Q6B856. 6 interactions.
MINTi MINT-6604256.

Chemistry

BindingDBi Q6B856.
ChEMBLi CHEMBL3394.

Proteomic databases

PaxDbi Q6B856.
PRIDEi Q6B856.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000005346 ; ENSBTAP00000005346 ; ENSBTAG00000004093 .
GeneIDi 281555.
KEGGi bta:281555.

Organism-specific databases

CTDi 347733.

Phylogenomic databases

eggNOGi COG5023.
GeneTreei ENSGT00740000115320.
HOGENOMi HOG000165710.
HOVERGENi HBG000089.
KOi K07375.
OMAi YQQEEEY.
OrthoDBi EOG71ZP1H.
TreeFami TF300298.

Enzyme and pathway databases

Reactomei REACT_209545. Resolution of Sister Chromatid Cohesion.
REACT_211133. MHC class II antigen presentation.
REACT_212887. Separation of Sister Chromatids.
REACT_214148. Formation of tubulin folding intermediates by CCT/TriC.
REACT_215331. Recruitment of NuMA to mitotic centrosomes.

Miscellaneous databases

EvolutionaryTracei Q6B856.
NextBioi 20805506.

Family and domain databases

Gene3Di 1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProi IPR013838. 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 ]
PANTHERi PTHR11588. PTHR11588. 1 hit.
Pfami PF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view ]
PRINTSi PR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTi SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view ]
SUPFAMi SSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEi PS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiTBB2B_BOVIN
AccessioniPrimary (citable) accession number: Q6B856
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: September 3, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi