Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tubulin alpha-4A chain

Gene

Tuba4a

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.

Miscellaneous

This tubulin does not have a C-terminal tyrosine.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi142 – 148GTPSequence analysis7

GO - Molecular functioni

GO - Biological processi

Keywordsi

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-114608 Platelet degranulation
R-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-5610787 Hedgehog 'off' state
R-MMU-5617833 Cilium Assembly
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-5632684 Hedgehog 'on' state
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 alpha-4A chain
Alternative name(s):
Alpha-tubulin 4
Alpha-tubulin isotype M-alpha-4
Tubulin alpha-4 chain
Gene namesi
Name:Tuba4a
Synonyms:Tuba4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1095410 Tuba4a

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_00000481231 – 448Tubulin alpha-4A chainAdd BLAST448

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40N6-acetyllysineBy similarity1
Modified residuei48PhosphoserineBy similarity1
Modified residuei83Nitrated tyrosineCombined sources1
Modified residuei432PhosphotyrosineBy similarity1
Modified residuei439PhosphoserineBy 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
Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly.By similarity
Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability.By similarity

Keywords - PTMi

Acetylation, Methylation, Nitration, Phosphoprotein

Proteomic databases

EPDiP68368
MaxQBiP68368
PaxDbiP68368
PeptideAtlasiP68368
PRIDEiP68368

PTM databases

CarbonylDBiP68368
iPTMnetiP68368
PhosphoSitePlusiP68368
SwissPalmiP68368

Expressioni

Gene expression databases

BgeeiENSMUSG00000026202 Expressed in 290 organ(s), highest expression level in brain
CleanExiMM_TUBA4A
ExpressionAtlasiP68368 baseline and differential
GenevisibleiP68368 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. Interacts with CFAP157 (PubMed:27965440).1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204375, 11 interactors
IntActiP68368, 20 interactors
MINTiP68368
STRINGi10090.ENSMUSP00000078429

Structurei

3D structure databases

ProteinModelPortaliP68368
SMRiP68368
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1376 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00760000119060
HOGENOMiHOG000165711
HOVERGENiHBG000089
InParanoidiP68368
KOiK07374
PhylomeDBiP68368
TreeFamiTF300314

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
IPR002452 Alpha_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
PfamiView protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit
PRINTSiPR01162 ALPHATUBULIN
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

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 6 potential isoforms that are computationally mapped.Show allAlign All

P68368-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRECISVHVG QAGVQMGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFT
60 70 80 90 100
TFFCETGAGK HVPRAVFVDL EPTVIDEIRN GPYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTI GKEIIDPVLD RIRKLSDQCT GLQGFLVFHS FGGGTGSGFT
160 170 180 190 200
SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIAAIKTKRS IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGIDSY EDEDEGEE
Length:448
Mass (Da):49,924
Last modified:August 13, 1987 - v1
Checksum:iC00ED90A183FE8F2
GO

Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0A0MQA5A0A0A0MQA5_MOUSE
Tubulin alpha chain
Tuba4a
477Annotation score:
A0A087WSB0A0A087WSB0_MOUSE
Tubulin alpha-4A chain
Tuba4a
81Annotation score:
A0A087WS35A0A087WS35_MOUSE
Tubulin alpha-4A chain
Tuba4a
75Annotation score:
A0A087WSL5A0A087WSL5_MOUSE
Tubulin alpha-4A chain
Tuba4a
89Annotation score:
A0A087WRB4A0A087WRB4_MOUSE
Tubulin alpha-4A chain
Tuba4a
100Annotation score:
A0A087WQS4A0A087WQS4_MOUSE
Tubulin alpha-4A chain
Tuba4a
125Annotation score:

Sequence cautioni

The sequence BAE34732 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1M → G in BAE34732 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13444 mRNA Translation: AAA40502.1
AK002427 mRNA Translation: BAB22094.1
AK078355 mRNA Translation: BAC37234.1
AK158934 mRNA Translation: BAE34732.1 Different initiation.
BC019959 mRNA Translation: AAH19959.1
CCDSiCCDS35623.1
PIRiI77427
RefSeqiNP_033473.1, NM_009447.4
UniGeneiMm.1155

Genome annotation databases

EnsembliENSMUST00000186213; ENSMUSP00000140657; ENSMUSG00000026202
GeneIDi22145
KEGGimmu:22145
UCSCiuc007bok.1 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13444 mRNA Translation: AAA40502.1
AK002427 mRNA Translation: BAB22094.1
AK078355 mRNA Translation: BAC37234.1
AK158934 mRNA Translation: BAE34732.1 Different initiation.
BC019959 mRNA Translation: AAH19959.1
CCDSiCCDS35623.1
PIRiI77427
RefSeqiNP_033473.1, NM_009447.4
UniGeneiMm.1155

3D structure databases

ProteinModelPortaliP68368
SMRiP68368
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204375, 11 interactors
IntActiP68368, 20 interactors
MINTiP68368
STRINGi10090.ENSMUSP00000078429

PTM databases

CarbonylDBiP68368
iPTMnetiP68368
PhosphoSitePlusiP68368
SwissPalmiP68368

Proteomic databases

EPDiP68368
MaxQBiP68368
PaxDbiP68368
PeptideAtlasiP68368
PRIDEiP68368

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000186213; ENSMUSP00000140657; ENSMUSG00000026202
GeneIDi22145
KEGGimmu:22145
UCSCiuc007bok.1 mouse

Organism-specific databases

CTDi7277
MGIiMGI:1095410 Tuba4a

Phylogenomic databases

eggNOGiKOG1376 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00760000119060
HOGENOMiHOG000165711
HOVERGENiHBG000089
InParanoidiP68368
KOiK07374
PhylomeDBiP68368
TreeFamiTF300314

Enzyme and pathway databases

ReactomeiR-MMU-114608 Platelet degranulation
R-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-5610787 Hedgehog 'off' state
R-MMU-5617833 Cilium Assembly
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-5632684 Hedgehog 'on' state
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

Miscellaneous databases

ChiTaRSiTuba4a mouse
PROiPR:P68368
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026202 Expressed in 290 organ(s), highest expression level in brain
CleanExiMM_TUBA4A
ExpressionAtlasiP68368 baseline and differential
GenevisibleiP68368 MM

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
IPR002452 Alpha_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
PfamiView protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit
PRINTSiPR01162 ALPHATUBULIN
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
ProtoNetiSearch...

Entry informationi

Entry nameiTBA4A_MOUSE
AccessioniPrimary (citable) accession number: P68368
Secondary accession number(s): P05215, Q3TY31
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: September 12, 2018
This is version 145 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
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again