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Protein

Tubulin beta-3 chain

Gene

Tubb3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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. TUBB3 plays a critical role in proper axon guidance and mantainance.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi140 – 1467GTPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • axon guidance Source: UniProtKB
  • microtubule-based process Source: InterPro
  • mitotic nuclear division Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-1445148. Translocation of GLUT4 to the plasma membrane.
R-MMU-5610787. Hedgehog 'off' state.
R-MMU-5620924. Intraflagellar transport.
R-MMU-5632684. Hedgehog 'on' state.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-3 chain
Gene namesi
Name:Tubb3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:107813. Tubb3.

Subcellular locationi

GO - Cellular componenti

  • axon Source: MGI
  • cell periphery Source: MGI
  • cytoplasm Source: MGI
  • dendrite Source: ParkinsonsUK-UCL
  • extracellular exosome Source: MGI
  • intracellular Source: MGI
  • microtubule Source: MGI
  • microtubule cytoskeleton Source: MGI
  • neuronal cell body Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi262 – 2621R → C: Brain from homozygous mice shows defects in the guidance of commissural axons and nerves, without evidence of cortical cells migration defects. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Tubulin beta-3 chainPRO_0000048251Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721Phosphoserine; by CDK1By similarity
Modified residuei438 – 43815-glutamyl polyglutamateBy similarity
Modified residuei444 – 4441PhosphoserineBy 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.1 Publication
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). 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
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

Isopeptide bond, Phosphoprotein

Proteomic databases

EPDiQ9ERD7.
MaxQBiQ9ERD7.
PaxDbiQ9ERD7.
PeptideAtlasiQ9ERD7.
PRIDEiQ9ERD7.
TopDownProteomicsiQ9ERD7.

2D gel databases

REPRODUCTION-2DPAGEIPI00112251.
Q9ERD7.
UCD-2DPAGEQ9ERD7.

PTM databases

iPTMnetiQ9ERD7.
PhosphoSiteiQ9ERD7.
SwissPalmiQ9ERD7.

Expressioni

Gene expression databases

BgeeiENSMUSG00000062380.
CleanExiMM_TUBB3.
GenevisibleiQ9ERD7. MM.

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

BioGridi204379. 5 interactions.
DIPiDIP-48419N.
IntActiQ9ERD7. 12 interactions.
MINTiMINT-1869621.
STRINGi10090.ENSMUSP00000071134.

Structurei

3D structure databases

ProteinModelPortaliQ9ERD7.
SMRiQ9ERD7. Positions 1-431.
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.
InParanoidiQ9ERD7.
KOiK07375.
OMAiNEASCEH.
OrthoDBiEOG091G06U2.
PhylomeDBiQ9ERD7.
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.

Q9ERD7-1 [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 DEESEAQGPK
Length:450
Mass (Da):50,419
Last modified:March 1, 2001 - v1
Checksum:i4B9D9B7DBA102949
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061A → S in BAE28719 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF312873 mRNA. Translation: AAG26010.1.
AK012528 mRNA. Translation: BAB28299.1.
AK051298 mRNA. Translation: BAC34596.1.
AK149014 mRNA. Translation: BAE28719.1.
BC031357 mRNA. Translation: AAH31357.1.
BC088749 mRNA. Translation: AAH88749.1.
CCDSiCCDS22757.1.
RefSeqiNP_075768.1. NM_023279.2.
UniGeneiMm.40068.

Genome annotation databases

EnsembliENSMUST00000071134; ENSMUSP00000071134; ENSMUSG00000062380.
GeneIDi22152.
KEGGimmu:22152.
UCSCiuc009nvt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF312873 mRNA. Translation: AAG26010.1.
AK012528 mRNA. Translation: BAB28299.1.
AK051298 mRNA. Translation: BAC34596.1.
AK149014 mRNA. Translation: BAE28719.1.
BC031357 mRNA. Translation: AAH31357.1.
BC088749 mRNA. Translation: AAH88749.1.
CCDSiCCDS22757.1.
RefSeqiNP_075768.1. NM_023279.2.
UniGeneiMm.40068.

3D structure databases

ProteinModelPortaliQ9ERD7.
SMRiQ9ERD7. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204379. 5 interactions.
DIPiDIP-48419N.
IntActiQ9ERD7. 12 interactions.
MINTiMINT-1869621.
STRINGi10090.ENSMUSP00000071134.

PTM databases

iPTMnetiQ9ERD7.
PhosphoSiteiQ9ERD7.
SwissPalmiQ9ERD7.

2D gel databases

REPRODUCTION-2DPAGEIPI00112251.
Q9ERD7.
UCD-2DPAGEQ9ERD7.

Proteomic databases

EPDiQ9ERD7.
MaxQBiQ9ERD7.
PaxDbiQ9ERD7.
PeptideAtlasiQ9ERD7.
PRIDEiQ9ERD7.
TopDownProteomicsiQ9ERD7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000071134; ENSMUSP00000071134; ENSMUSG00000062380.
GeneIDi22152.
KEGGimmu:22152.
UCSCiuc009nvt.1. mouse.

Organism-specific databases

CTDi10381.
MGIiMGI:107813. Tubb3.

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ9ERD7.
KOiK07375.
OMAiNEASCEH.
OrthoDBiEOG091G06U2.
PhylomeDBiQ9ERD7.
TreeFamiTF300298.

Enzyme and pathway databases

ReactomeiR-MMU-1445148. Translocation of GLUT4 to the plasma membrane.
R-MMU-5610787. Hedgehog 'off' state.
R-MMU-5620924. Intraflagellar transport.
R-MMU-5632684. Hedgehog 'on' state.

Miscellaneous databases

PROiQ9ERD7.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000062380.
CleanExiMM_TUBB3.
GenevisibleiQ9ERD7. MM.

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 nameiTBB3_MOUSE
AccessioniPrimary (citable) accession number: Q9ERD7
Secondary accession number(s): Q3UF42, Q5I036
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: March 1, 2001
Last modified: September 7, 2016
This is version 142 of the entry and version 1 of the sequence. [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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.