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Protein

Tubulin beta-4B chain

Gene

Tubb4b

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.

Regions

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

GO - Molecular functioni

  • double-stranded RNA binding Source: MGI
  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB
  • structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  • microtubule-based process Source: UniProtKB

Keywordsi

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-380320. Recruitment of NuMA to mitotic centrosomes.
R-MMU-5610787. Hedgehog 'off' state.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-5620924. Intraflagellar transport.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-8854518. AURKA Activation by TPX2.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-4B chain
Alternative name(s):
Tubulin beta-2C chain
Gene namesi
Name:Tubb4b
Synonyms:Tubb2c
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1915472. Tubb4b.

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_00000482491 – 445Tubulin beta-4B chainAdd BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei55PhosphothreonineBy similarity1
Modified residuei58N6-acetyllysineCombined sources1
Modified residuei172Phosphoserine; by CDK1By similarity1
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.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

Acetylation, Isopeptide bond, Phosphoprotein

Proteomic databases

EPDiP68372.
MaxQBiP68372.
PaxDbiP68372.
PeptideAtlasiP68372.
PRIDEiP68372.

2D gel databases

REPRODUCTION-2DPAGEiIPI00169463.
P68372.
UCD-2DPAGEiP68372.

PTM databases

iPTMnetiP68372.
PhosphoSitePlusiP68372.
SwissPalmiP68372.

Expressioni

Gene expression databases

BgeeiENSMUSG00000036752.
CleanExiMM_TUBB2C.
GenevisibleiP68372. 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

BioGridi230642. 28 interactors.
IntActiP68372. 41 interactors.
MINTiMINT-4137100.
STRINGi10090.ENSMUSP00000042342.

Structurei

3D structure databases

ProteinModelPortaliP68372.
SMRiP68372.
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.
InParanoidiP68372.
KOiK07375.
OMAiDEHEEGR.
OrthoDBiEOG091G06U2.
PhylomeDBiP68372.
TreeFamiTF300298.

Family and domain databases

Gene3Di3.30.1330.20. 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.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
PANTHERiPTHR11588. PTHR11588. 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.

P68372-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY
60 70 80 90 100
YNEATGGKYV PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
310 320 330 340 350
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEGEFEEEA EEEVA
Length:445
Mass (Da):49,831
Last modified:August 13, 1987 - v1
Checksum:iA552C52822AFA072
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti207L → P in AAH05547 (PubMed:15489334).Curated1
Sequence conflicti342V → A in BAE27282 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK146587 mRNA. Translation: BAE27282.1.
AK167022 mRNA. Translation: BAE39195.1.
AL732309 Genomic DNA. Translation: CAM14671.1.
BC005547 mRNA. Translation: AAH05547.1.
BC022919 mRNA. Translation: AAH22919.1.
BC083319 mRNA. Translation: AAH83319.1.
CCDSiCCDS15753.1.
PIRiC25437.
RefSeqiNP_666228.1. NM_146116.2.
UniGeneiMm.227260.
Mm.491119.

Genome annotation databases

EnsembliENSMUST00000043584; ENSMUSP00000042342; ENSMUSG00000036752.
GeneIDi227613.
KEGGimmu:227613.
UCSCiuc008iqs.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiTBB4B_MOUSE
AccessioniPrimary (citable) accession number: P68372
Secondary accession number(s): P05217
, Q3TKF0, Q3UJ73, Q99JZ6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 22, 2017
This is version 138 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families