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Protein

Tubulin alpha-1A chain

Gene

TUBA1A

Organism
Homo sapiens (Human)
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei451Involved in polymerizationBy similarity1

Regions

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

GO - Molecular functioni

GO - Biological processi

  • cell division Source: BHF-UCL
  • ciliary basal body-plasma membrane docking Source: Reactome
  • cytoskeleton-dependent intracellular transport Source: BHF-UCL
  • G2/M transition of mitotic cell cycle Source: Reactome
  • microtubule-based process Source: BHF-UCL
  • regulation of G2/M transition of mitotic cell cycle Source: Reactome

Keywordsi

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-1445148 Translocation of GLUT4 to the plasma membrane
R-HSA-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-HSA-190861 Gap junction assembly
R-HSA-2132295 MHC class II antigen presentation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-2565942 Regulation of PLK1 Activity at G2/M Transition
R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-380259 Loss of Nlp from mitotic centrosomes
R-HSA-380270 Recruitment of mitotic centrosome proteins and complexes
R-HSA-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
R-HSA-389957 Prefoldin mediated transfer of substrate to CCT/TriC
R-HSA-389960 Formation of tubulin folding intermediates by CCT/TriC
R-HSA-389977 Post-chaperonin tubulin folding pathway
R-HSA-437239 Recycling pathway of L1
R-HSA-5610787 Hedgehog 'off' state
R-HSA-5617833 Cilium Assembly
R-HSA-5620912 Anchoring of the basal body to the plasma membrane
R-HSA-5620924 Intraflagellar transport
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-6807878 COPI-mediated anterograde transport
R-HSA-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-HSA-68877 Mitotic Prometaphase
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854518 AURKA Activation by TPX2
R-HSA-8955332 Carboxyterminal post-translational modifications of tubulin
R-HSA-983189 Kinesins
SIGNORiQ71U36

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-1A chain
Alternative name(s):
Alpha-tubulin 3
Tubulin B-alpha-1
Tubulin alpha-3 chain
Cleaved into the following chain:
Gene namesi
Name:TUBA1A
Synonyms:TUBA3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000167552.13
HGNCiHGNC:20766 TUBA1A
MIMi602529 gene
neXtProtiNX_Q71U36

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

Pathology & Biotechi

Involvement in diseasei

Lissencephaly 3 (LIS3)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA classic type lissencephaly associated with psychomotor retardation and seizures. Features include agyria or pachygyria or laminar heterotopia, severe mental retardation, motor delay, variable presence of seizures, and abnormalities of corpus callosum, hippocampus, cerebellar vermis and brainstem.
See also OMIM:611603
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_039332188I → L in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853045EnsemblClinVar.1
Natural variantiVAR_039333263P → T in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853046EnsemblClinVar.1
Natural variantiVAR_039334264R → C in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853043EnsemblClinVar.1
Natural variantiVAR_039335286L → F in LIS3. 1 Publication1
Natural variantiVAR_039336402R → C in LIS3. 1 PublicationCorresponds to variant dbSNP:rs587784483EnsemblClinVar.1
Natural variantiVAR_039337402R → H in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853044EnsemblClinVar.1
Natural variantiVAR_078711402R → L in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853044EnsemblClinVar.1
Natural variantiVAR_039338419S → L in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853047EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Lissencephaly

Organism-specific databases

DisGeNETi7846
MalaCardsiTUBA1A
MIMi611603 phenotype
OpenTargetsiENSG00000167552
Orphaneti171680 Lissencephaly due to TUBA1A mutation
PharmGKBiPA162407319

Chemistry databases

ChEMBLiCHEMBL3661
DrugBankiDB00518 Albendazole
DB05147 CYT997
DB03010 Epothilone B
DB01873 Epothilone D
DB00643 Mebendazole
DB00570 Vinblastine

Polymorphism and mutation databases

BioMutaiTUBA1A
DMDMi55977864

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000481111 – 451Tubulin alpha-1A chainAdd BLAST451
ChainiPRO_00004373781 – 450Detyrosinated tubulin alpha-1A chain1 PublicationAdd BLAST450

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40N6-acetyllysine1 Publication1
Modified residuei282Nitrated tyrosineBy similarity1
Modified residuei439PhosphoserineBy similarity1
Modified residuei4455-glutamyl polyglutamateBy similarity1
Modified residuei4513'-nitrotyrosine1 Publication1

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866). 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 (PubMed:26875866).1 Publication
Some glutamate residues at the C-terminus are monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of monoglycylation is still unclear (Probable).1 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.1 Publication
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
Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution.1 Publication
Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.3 Publications
Tubulin alpha-1A chain: Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1. Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules (PubMed:26972003, PubMed:26968983). In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (PubMed:26968983).2 Publications
Detyrosinated tubulin alpha-1A chain: Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator (PubMed:25908662). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle. In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (By similarity).By similarity1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein

Proteomic databases

EPDiQ71U36
MaxQBiQ71U36
PaxDbiQ71U36
PeptideAtlasiQ71U36
PRIDEiQ71U36
ProteomicsDBi68631
TopDownProteomicsiQ71U36-1 [Q71U36-1]

PTM databases

iPTMnetiQ71U36
PhosphoSitePlusiQ71U36
SwissPalmiQ71U36

Miscellaneous databases

PMAP-CutDBiQ71U36

Expressioni

Tissue specificityi

Expressed at a high level in fetal brain.1 Publication

Gene expression databases

BgeeiENSG00000167552
CleanExiHS_TUBA1A
ExpressionAtlasiQ71U36 baseline and differential
GenevisibleiQ71U36 HS

Organism-specific databases

HPAiCAB008686
HPA039247
HPA043684
HPA063394

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 SETD2; the interaction is independent on alpha-tubulin acetylation on Lys-40.

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi113603, 282 interactors
CORUMiQ71U36
DIPiDIP-32773N
ELMiQ71U36
IntActiQ71U36, 352 interactors
MINTiQ71U36
STRINGi9606.ENSP00000301071

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5JCOelectron microscopy4.00A/B/E/F/G/H1-437[»]
ProteinModelPortaliQ71U36
SMRiQ71U36
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1376 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00760000119060
HOGENOMiHOG000165711
HOVERGENiHBG000089
InParanoidiQ71U36
KOiK07374
OMAiMDSTDGE
OrthoDBiEOG091G0736
PhylomeDBiQ71U36
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

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q71U36-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN
60 70 80 90 100
TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT
160 170 180 190 200
SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440 450
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE

Y
Length:451
Mass (Da):50,136
Last modified:July 5, 2004 - v1
Checksum:i00F8429A4A10E5FE
GO
Isoform 2 (identifier: Q71U36-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.

Note: No experimental confirmation available.
Show »
Length:416
Mass (Da):46,297
Checksum:iBF1E2C9AC0754A68
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti131G → R in CAA25855 (PubMed:3839072).Curated1
Sequence conflicti131G → R in AAA91575 (PubMed:6646120).Curated1
Sequence conflicti290E → D in AAA91575 (PubMed:6646120).Curated1
Sequence conflicti308R → G in CAA25855 (PubMed:3839072).Curated1
Sequence conflicti308R → G in AAA91575 (PubMed:6646120).Curated1
Sequence conflicti438D → H in CAA25855 (PubMed:3839072).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_039332188I → L in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853045EnsemblClinVar.1
Natural variantiVAR_039333263P → T in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853046EnsemblClinVar.1
Natural variantiVAR_039334264R → C in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853043EnsemblClinVar.1
Natural variantiVAR_039335286L → F in LIS3. 1 Publication1
Natural variantiVAR_039336402R → C in LIS3. 1 PublicationCorresponds to variant dbSNP:rs587784483EnsemblClinVar.1
Natural variantiVAR_039337402R → H in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853044EnsemblClinVar.1
Natural variantiVAR_078711402R → L in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853044EnsemblClinVar.1
Natural variantiVAR_039338419S → L in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853047EnsemblClinVar.1
Natural variantiVAR_034540447E → K. Corresponds to variant dbSNP:rs1065730Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0467821 – 35Missing in isoform 2. CuratedAdd BLAST35

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01703 Genomic DNA Translation: CAA25855.1
AF141347 mRNA Translation: AAD33871.1
AK289483 mRNA Translation: BAF82172.1
AC010173 Genomic DNA No translation available.
CH471111 Genomic DNA Translation: EAW58052.1
CH471111 Genomic DNA Translation: EAW58054.1
CH471111 Genomic DNA Translation: EAW58055.1
BC006468 mRNA Translation: AAH06468.1
BC050637 mRNA Translation: AAH50637.1
K00557 mRNA Translation: AAA91575.1
CCDSiCCDS58226.1 [Q71U36-2]
CCDS58227.1 [Q71U36-1]
CCDS8781.1 [Q71U36-1]
RefSeqiNP_001257328.1, NM_001270399.1 [Q71U36-1]
NP_001257329.1, NM_001270400.1 [Q71U36-2]
NP_006000.2, NM_006009.3 [Q71U36-1]
UniGeneiHs.654422

Genome annotation databases

EnsembliENST00000295766; ENSP00000439020; ENSG00000167552 [Q71U36-1]
ENST00000301071; ENSP00000301071; ENSG00000167552 [Q71U36-1]
ENST00000550767; ENSP00000446637; ENSG00000167552 [Q71U36-2]
GeneIDi7846
KEGGihsa:7846
UCSCiuc001rtp.5 human [Q71U36-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiTBA1A_HUMAN
AccessioniPrimary (citable) accession number: Q71U36
Secondary accession number(s): A8K0B8
, G3V1U9, P04687, P05209
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: July 5, 2004
Last modified: June 20, 2018
This is version 152 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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