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Protein

Tubulin beta-3 chain

Gene

TUBB3

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. TUBB3 plays a critical role in proper axon guidance and mantainance (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi140 – 146GTPSequence analysis7

GO - Molecular functioni

GO - Biological processi

Keywordsi

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-3 chain
Gene namesi
Name:TUBB3
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 18

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002330241 – 450Tubulin beta-3 chainAdd BLAST450

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei172Phosphoserine; by CDK1By similarity1
Modified residuei4385-glutamyl polyglutamate1 Publication1
Modified residuei444Phosphoserine1 Publication1

Post-translational modificationi

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
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 (PubMed:2052551). 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 similarity1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein

Proteomic databases

PaxDbiQ2T9S0
PeptideAtlasiQ2T9S0
PRIDEiQ2T9S0

PTM databases

iPTMnetiQ2T9S0

Expressioni

Gene expression databases

BgeeiENSBTAG00000023730

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

IntActiQ2T9S0, 1 interactor
STRINGi9913.ENSBTAP00000000568

Structurei

3D structure databases

ProteinModelPortaliQ2T9S0
SMRiQ2T9S0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The highly acidic C-terminal region may bind cations such as calcium.

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00760000119061
HOGENOMiHOG000165710
HOVERGENiHBG000089
InParanoidiQ2T9S0
KOiK07375
OMAiDEMEGEC
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.

Q2T9S0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY
60 70 80 90 100
YNEASSHKYV PRAILVDLEP GTMDSVRSGA FGHLFRPDNF IFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKECENCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKVREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSIH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLATP TYGDLNHLVS ATMSGVTTSL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALTVPELT QQMFDAKNMM
310 320 330 340 350
AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK
360 370 380 390 400
VAVCDIPPRG LKMSSTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440 450
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEGEMYEDD EEESEAQGPK
Length:450
Mass (Da):50,433
Last modified:January 24, 2006 - v1
Checksum:i4B9CDE7DBA102949
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC111295 mRNA Translation: AAI11296.1
RefSeqiNP_001070595.1, NM_001077127.1
UniGeneiBt.56074

Genome annotation databases

EnsembliENSBTAT00000000568; ENSBTAP00000000568; ENSBTAG00000023730
GeneIDi768070
KEGGibta:768070

Similar proteinsi

Entry informationi

Entry nameiTBB3_BOVIN
AccessioniPrimary (citable) accession number: Q2T9S0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: January 24, 2006
Last modified: May 23, 2018
This is version 99 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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