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Protein

Tubulin beta-4A chain

Gene

Tubb4a

Organism
Mus musculus (Mouse)
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.

Regions

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processCilium biogenesis/degradation
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-MMU-2132295 MHC class II antigen presentation
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition
R-MMU-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
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-437239 Recycling pathway of L1
R-MMU-5620912 Anchoring of the basal body to the plasma membrane
R-MMU-5620924 Intraflagellar transport
R-MMU-5626467 RHO GTPases activate IQGAPs
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-6807878 COPI-mediated anterograde transport
R-MMU-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-MMU-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-MMU-68877 Mitotic Prometaphase
R-MMU-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-MMU-8854518 AURKA Activation by TPX2
R-MMU-8955332 Carboxyterminal post-translational modifications of tubulin
R-MMU-983189 Kinesins

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-4A chain
Alternative name(s):
Tubulin beta-4 chain
Gene namesi
Name:Tubb4a
Synonyms:Tubb4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:107848 Tubb4a

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_00000482541 – 444Tubulin beta-4A chainAdd BLAST444

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei172Phosphoserine; by CDK1By similarity1
Modified residuei4365-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

Isopeptide bond, Phosphoprotein

Proteomic databases

MaxQBiQ9D6F9
PaxDbiQ9D6F9
PeptideAtlasiQ9D6F9
PRIDEiQ9D6F9
TopDownProteomicsiQ9D6F9

2D gel databases

REPRODUCTION-2DPAGEiIPI00109073
Q9D6F9

PTM databases

CarbonylDBiQ9D6F9
iPTMnetiQ9D6F9
PhosphoSitePlusiQ9D6F9
SwissPalmiQ9D6F9

Expressioni

Gene expression databases

BgeeiENSMUSG00000062591
CleanExiMM_TUBB4
GenevisibleiQ9D6F9 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

BioGridi204380, 10 interactors
IntActiQ9D6F9, 12 interactors
MINTiQ9D6F9
STRINGi10090.ENSMUSP00000071135

Structurei

3D structure databases

ProteinModelPortaliQ9D6F9
SMRiQ9D6F9
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
InParanoidiQ9D6F9
KOiK07375
OMAiRSNQSYR
OrthoDBiEOG091G06U2
PhylomeDBiQ9D6F9
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.

Q9D6F9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY
60 70 80 90 100
YNEATGGNYV PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDAVLDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEFP 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 LSVQSKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMAATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEGEFEEEAE EEVA
Length:444
Mass (Da):49,586
Last modified:May 1, 2007 - v3
Checksum:iF7429D057C11A3F5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti73M → I in AAA40509 (PubMed:3839797).Curated1
Sequence conflicti111E → Q in AAA40509 (PubMed:3839797).Curated1
Sequence conflicti270F → L in AAA40509 (PubMed:3839797).Curated1
Sequence conflicti293M → V in AAA40509 (PubMed:3839797).Curated1
Sequence conflicti303C → S in AAA40509 (PubMed:3839797).Curated1
Sequence conflicti351T → A in AAA40509 (PubMed:3839797).Curated1
Sequence conflicti400G → A in AAA40509 (PubMed:3839797).Curated1
Sequence conflicti427D → G in BAB28967 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013717 mRNA Translation: BAB28967.1
BC049112 mRNA Translation: AAH49112.1
BC054831 mRNA Translation: AAH54831.1
M28730 mRNA Translation: AAA40509.1
CCDSiCCDS28925.1
RefSeqiNP_033477.2, NM_009451.3
UniGeneiMm.7420

Genome annotation databases

EnsembliENSMUST00000071135; ENSMUSP00000071135; ENSMUSG00000062591
GeneIDi22153
KEGGimmu:22153
UCSCiuc008dea.1 mouse

Similar proteinsi

Entry informationi

Entry nameiTBB4A_MOUSE
AccessioniPrimary (citable) accession number: Q9D6F9
Secondary accession number(s): Q62364, Q80Y54
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: May 1, 2007
Last modified: May 23, 2018
This is version 152 of the entry and version 3 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

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