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Protein

Tubulin beta-2B chain

Gene

TUBB2B

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-5610787. Hedgehog 'off' state.
R-BTA-5620924. Intraflagellar transport.
R-BTA-5632684. Hedgehog 'on' state.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-2B chain
Gene namesi
Name:TUBB2B
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 23

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2111464.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Tubulin beta-2B chainPRO_0000262654Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401PhosphoserineBy similarity
Modified residuei55 – 551PhosphothreonineBy similarity
Modified residuei58 – 581N6-acetyllysine; alternateBy similarity
Modified residuei58 – 581N6-succinyllysine; alternateBy similarity
Cross-linki58 – 58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei285 – 2851PhosphothreonineBy similarity
Modified residuei290 – 2901PhosphothreonineBy similarity
Modified residuei318 – 3181Omega-N-methylarginineBy similarity
Cross-linki324 – 324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei438 – 43815-glutamyl polyglutamateBy similarity

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglycylated, resulting in 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 polyglycylation is still unclear.By similarity
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (By similarity). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ6B856.
PeptideAtlasiQ6B856.
PRIDEiQ6B856.

PTM databases

iPTMnetiQ6B856.

Expressioni

Gene expression databases

BgeeiENSBTAG00000004093.
ExpressionAtlasiQ6B856. baseline.

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. 3 interactions.
DIPiDIP-47524N.
IntActiQ6B856. 6 interactions.
MINTiMINT-6604256.
STRINGi9913.ENSBTAP00000005346.

Chemistry

BindingDBiQ6B856.

Structurei

Secondary structure

1
445
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi10 – 2718Combined sources
Beta strandi34 – 363Combined sources
Beta strandi39 – 413Combined sources
Helixi42 – 454Combined sources
Helixi47 – 493Combined sources
Beta strandi51 – 544Combined sources
Turni55 – 573Combined sources
Beta strandi58 – 614Combined sources
Beta strandi63 – 708Combined sources
Helixi71 – 788Combined sources
Helixi82 – 843Combined sources
Helixi87 – 893Combined sources
Beta strandi90 – 923Combined sources
Helixi101 – 1055Combined sources
Helixi108 – 12518Combined sources
Beta strandi132 – 14211Combined sources
Helixi143 – 15816Combined sources
Beta strandi162 – 1709Combined sources
Helixi173 – 1753Combined sources
Helixi181 – 19515Combined sources
Beta strandi197 – 2037Combined sources
Helixi204 – 21310Combined sources
Helixi222 – 23615Combined sources
Helixi238 – 2414Combined sources
Beta strandi245 – 2473Combined sources
Helixi250 – 2578Combined sources
Beta strandi259 – 2624Combined sources
Beta strandi265 – 2717Combined sources
Helixi278 – 2803Combined sources
Helixi286 – 2938Combined sources
Helixi296 – 2983Combined sources
Beta strandi299 – 3024Combined sources
Helixi305 – 3073Combined sources
Beta strandi310 – 32011Combined sources
Helixi323 – 33614Combined sources
Helixi338 – 3403Combined sources
Beta strandi343 – 3453Combined sources
Beta strandi349 – 3557Combined sources
Beta strandi362 – 37110Combined sources
Helixi372 – 3743Combined sources
Helixi375 – 38915Combined sources
Turni390 – 3956Combined sources
Helixi396 – 3994Combined sources
Turni400 – 4023Combined sources
Helixi405 – 42622Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4TUYX-ray2.10B/D1-445[»]
4TV8X-ray2.10B/D1-445[»]
4TV9X-ray2.00B/D1-445[»]
4UXOelectron microscopy6.30B1-445[»]
4UXPelectron microscopy6.30B1-445[»]
4UXRelectron microscopy7.00B1-445[»]
4UXSelectron microscopy7.00B1-445[»]
4UXTelectron microscopy7.40B1-445[»]
4UXYelectron microscopy6.50B1-445[»]
4UY0electron microscopy7.70B2-427[»]
4WBNX-ray2.30B/D1-445[»]
4YJ2X-ray2.60B/D1-445[»]
4YJ3X-ray3.75B/D1-445[»]
5ITZX-ray2.20B1-445[»]
5JVDX-ray2.39B/D1-445[»]
ProteinModelPortaliQ6B856.
SMRiQ6B856. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6B856.

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ6B856.
KOiK07375.
OMAiFWEVICA.
OrthoDBiEOG091G06U2.
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

        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY
60 70 80 90 100
YNEATGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEYP DRIMNTFSVM PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM
310 320 330 340 350
AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEE GEDEA
Length:445
Mass (Da):49,953
Last modified:November 28, 2006 - v2
Checksum:i4DC3956EFF880746
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AY675081 mRNA. Translation: AAT84374.1.
RefSeqiNP_001003900.1. NM_001003900.1.
UniGeneiBt.105119.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4TUYX-ray2.10B/D1-445[»]
4TV8X-ray2.10B/D1-445[»]
4TV9X-ray2.00B/D1-445[»]
4UXOelectron microscopy6.30B1-445[»]
4UXPelectron microscopy6.30B1-445[»]
4UXRelectron microscopy7.00B1-445[»]
4UXSelectron microscopy7.00B1-445[»]
4UXTelectron microscopy7.40B1-445[»]
4UXYelectron microscopy6.50B1-445[»]
4UY0electron microscopy7.70B2-427[»]
4WBNX-ray2.30B/D1-445[»]
4YJ2X-ray2.60B/D1-445[»]
4YJ3X-ray3.75B/D1-445[»]
5ITZX-ray2.20B1-445[»]
5JVDX-ray2.39B/D1-445[»]
ProteinModelPortaliQ6B856.
SMRiQ6B856. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi158875. 3 interactions.
DIPiDIP-47524N.
IntActiQ6B856. 6 interactions.
MINTiMINT-6604256.
STRINGi9913.ENSBTAP00000005346.

Chemistry

BindingDBiQ6B856.
ChEMBLiCHEMBL2111464.

PTM databases

iPTMnetiQ6B856.

Proteomic databases

PaxDbiQ6B856.
PeptideAtlasiQ6B856.
PRIDEiQ6B856.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi347733.

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ6B856.
KOiK07375.
OMAiFWEVICA.
OrthoDBiEOG091G06U2.
TreeFamiTF300298.

Enzyme and pathway databases

ReactomeiR-BTA-5610787. Hedgehog 'off' state.
R-BTA-5620924. Intraflagellar transport.
R-BTA-5632684. Hedgehog 'on' state.

Miscellaneous databases

EvolutionaryTraceiQ6B856.
PROiQ6B856.

Gene expression databases

BgeeiENSBTAG00000004093.
ExpressionAtlasiQ6B856. baseline.

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]
ProtoNetiSearch...

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 7, 2016
This is version 109 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.