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Protein

Tubulin beta-2B chain

Gene

TUBB2B

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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. Plays a critical role in proper axon guidance in both central and peripheral axon tracts. Implicated in neuronal migration.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processNeurogenesis
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-BTA-2132295 MHC class II antigen presentation
R-BTA-2467813 Separation of Sister Chromatids
R-BTA-2500257 Resolution of Sister Chromatid Cohesion
R-BTA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-BTA-380320 Recruitment of NuMA to mitotic centrosomes
R-BTA-437239 Recycling pathway of L1
R-BTA-5610787 Hedgehog 'off' state
R-BTA-5617833 Cilium Assembly
R-BTA-5620924 Intraflagellar transport
R-BTA-5626467 RHO GTPases activate IQGAPs
R-BTA-5632684 Hedgehog 'on' state
R-BTA-5663220 RHO GTPases Activate Formins
R-BTA-6807878 COPI-mediated anterograde transport
R-BTA-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-BTA-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-BTA-68877 Mitotic Prometaphase
R-BTA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-BTA-8955332 Carboxyterminal post-translational modifications of tubulin
R-BTA-983189 Kinesins

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3394

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002626541 – 445Tubulin beta-2B chainAdd BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40PhosphoserineBy similarity1
Modified residuei55PhosphothreonineBy similarity1
Modified residuei58N6-acetyllysine; alternateBy similarity1
Modified residuei58N6-succinyllysine; alternateBy similarity1
Cross-linki58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei172Phosphoserine; by CDK1By similarity1
Modified residuei285PhosphothreonineBy similarity1
Modified residuei290PhosphothreonineBy similarity1
Modified residuei318Omega-N-methylarginineBy similarity1
Cross-linki324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei4385-glutamyl polyglutamateBy similarity1

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
Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules.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.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi158875, 3 interactors
CORUMiQ6B856
DIPiDIP-47524N
IntActiQ6B856, 7 interactors
MINTiQ6B856
STRINGi9913.ENSBTAP00000005346

Chemistry databases

BindingDBiQ6B856

Structurei

Secondary structure

1445
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi10 – 27Combined sources18
Beta strandi34 – 36Combined sources3
Beta strandi39 – 41Combined sources3
Helixi42 – 45Combined sources4
Helixi47 – 49Combined sources3
Beta strandi51 – 54Combined sources4
Turni55 – 57Combined sources3
Beta strandi58 – 61Combined sources4
Beta strandi63 – 70Combined sources8
Helixi71 – 78Combined sources8
Beta strandi79 – 81Combined sources3
Helixi82 – 84Combined sources3
Helixi87 – 89Combined sources3
Beta strandi90 – 92Combined sources3
Helixi101 – 105Combined sources5
Helixi108 – 125Combined sources18
Beta strandi126 – 128Combined sources3
Beta strandi132 – 142Combined sources11
Helixi143 – 158Combined sources16
Beta strandi162 – 170Combined sources9
Turni173 – 175Combined sources3
Beta strandi177 – 180Combined sources4
Helixi181 – 195Combined sources15
Beta strandi197 – 203Combined sources7
Helixi204 – 213Combined sources10
Helixi222 – 236Combined sources15
Helixi238 – 241Combined sources4
Beta strandi245 – 247Combined sources3
Helixi250 – 257Combined sources8
Beta strandi259 – 262Combined sources4
Beta strandi265 – 271Combined sources7
Helixi278 – 280Combined sources3
Helixi286 – 293Combined sources8
Helixi296 – 298Combined sources3
Beta strandi299 – 302Combined sources4
Helixi305 – 307Combined sources3
Beta strandi310 – 320Combined sources11
Helixi323 – 336Combined sources14
Helixi338 – 340Combined sources3
Beta strandi343 – 345Combined sources3
Beta strandi349 – 355Combined sources7
Turni359 – 361Combined sources3
Beta strandi362 – 371Combined sources10
Helixi372 – 374Combined sources3
Helixi375 – 389Combined sources15
Turni390 – 395Combined sources6
Helixi396 – 399Combined sources4
Turni400 – 402Combined sources3
Helixi405 – 426Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5EIBX-ray2.10D1-445[»]
5EZYX-ray2.05B/D1-445[»]
5GONX-ray2.48B/D1-431[»]
5H74X-ray2.60B/D1-445[»]
5H7OX-ray2.80B/D1-445[»]
5HNWelectron microscopy6.60B2-445[»]
5HNXelectron microscopy6.60B1-445[»]
5HNYelectron microscopy6.30B2-427[»]
5HNZelectron microscopy5.80B1-445[»]
5ITZX-ray2.20B1-445[»]
5IYZX-ray1.80B/D1-445[»]
5J2TX-ray2.20B/D1-445[»]
5J2UX-ray2.50B/D1-445[»]
5JH7X-ray2.25B/D1-445[»]
5JVDX-ray2.39B/D1-445[»]
5LA6X-ray2.10B/D1-445[»]
5LOVX-ray2.40B/D1-445[»]
5LP6X-ray2.90B/D1-445[»]
5LXSX-ray2.20B/D1-445[»]
5LXTX-ray1.90B/D1-445[»]
5LYJX-ray2.40B/D1-445[»]
5M50electron microscopy5.30B/E1-427[»]
5M54electron microscopy8.00B/E2-427[»]
5M5Celectron microscopy4.80B/E2-427[»]
5M5Ielectron microscopy9.30B1-445[»]
5M5Lelectron microscopy9.30B1-445[»]
5M5Melectron microscopy9.30B1-445[»]
5M5Nelectron microscopy9.30B1-445[»]
5M5Oelectron microscopy9.30B1-445[»]
5M7EX-ray2.05B/D1-445[»]
5M7GX-ray2.25B/D1-445[»]
5M8DX-ray2.25B/D1-445[»]
5M8GX-ray2.15B/D1-445[»]
5MF4X-ray2.30B/D1-445[»]
5ND2electron microscopy5.80B1-445[»]
5ND3electron microscopy6.10B1-445[»]
5ND4electron microscopy4.40B2-427[»]
5ND7electron microscopy7.90B1-445[»]
5NFZX-ray2.10B/D1-445[»]
5NG1X-ray2.20B/D1-445[»]
5NJHX-ray2.39B/D1-445[»]
5NM5X-ray2.05B1-445[»]
5NQTX-ray2.15B1-445[»]
5NQUX-ray1.80B1-445[»]
5O7AX-ray2.50B/D1-445[»]
5OSKX-ray2.11B/D1-445[»]
5OV7X-ray2.40B/D1-445[»]
5XAFX-ray2.55B/D1-445[»]
5XAGX-ray2.56B/D1-445[»]
5XLTX-ray2.81B/D1-445[»]
5XLZX-ray2.30B/D1-445[»]
6FKJX-ray2.15B/D1-445[»]
6FKLX-ray2.10B/D1-445[»]
ProteinModelPortaliQ6B856
SMRiQ6B856
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
OMAiFRDRISM
OrthoDBiEOG091G06U2
TreeFamiTF300298

Family and domain databases

Gene3Di1.10.287.600, 1 hit
3.30.1330.20, 1 hit
3.40.50.1440, 1 hit
InterProiView protein in InterPro
IPR013838 Beta-tubulin_BS
IPR002453 Beta_tubulin
IPR008280 Tub_FtsZ_C
IPR000217 Tubulin
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR037103 Tubulin/FtsZ_C_sf
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR023123 Tubulin_C
IPR017975 Tubulin_CS
IPR003008 Tubulin_FtsZ_GTPase
PANTHERiPTHR11588 PTHR11588, 1 hit
PTHR11588:SF256 PTHR11588:SF256, 1 hit
PfamiView protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit
PRINTSiPR01163 BETATUBULIN
PR01161 TUBULIN
SMARTiView protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit
SUPFAMiSSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit
PROSITEiView protein in PROSITE
PS00227 TUBULIN, 1 hit
PS00228 TUBULIN_B_AUTOREG, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti201C → S in AAT84374 (Ref. 1) Curated1

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

Similar proteinsi

Entry informationi

Entry nameiTBB2B_BOVIN
AccessioniPrimary (citable) accession number: Q6B856
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: May 23, 2018
This is version 127 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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