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 beta-2A chain

Gene

TUBB2A

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 (By similarity).By similarity

Regions

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

GO - Molecular functioni

  • GTPase activity Source: InterPro
  • GTP binding Source: GO_Central
  • structural constituent of cytoskeleton Source: GO_Central

GO - Biological processi

Keywordsi

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-1445148 Translocation of SLC2A4 (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-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
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-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-8955332 Carboxyterminal post-translational modifications of tubulin
R-HSA-983189 Kinesins
SIGNORiQ13885

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-2A chain
Alternative name(s):
Tubulin beta class IIa
Gene namesi
Name:TUBB2A
Synonyms:TUBB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000137267.5
HGNCiHGNC:12412 TUBB2A
MIMi615101 gene
neXtProtiNX_Q13885

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

Cortical dysplasia, complex, with other brain malformations 5 (CDCBM5)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of aberrant neuronal migration and disturbed axonal guidance. Clinical features include seizures, global developmental delay, and various brain malformations such as a diffuse simplified gyral pattern with reduced volume of white matter, globular basal ganglia, thin and dysmorphic corpus callosum, mild brainstem hypoplasia with a flat pons, mild cerebellar vermis hypoplasia, and mildly enlarged posterior fossa.
See also OMIM:615763
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071168247N → K in CDCBM5; abolishes coassembly with tubulin subunits and incorporation into the microtubule polymer network. 1 PublicationCorresponds to variant dbSNP:rs886037663EnsemblClinVar.1
Natural variantiVAR_071169248A → V in CDCBM5; reduces coassembly with tubulin subunits and incorporation into the microtubule polymer network. 1 PublicationCorresponds to variant dbSNP:rs2808001EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi7280
MalaCardsiTUBB2A
MIMi615763 phenotype
OpenTargetsiENSG00000137267
PharmGKBiPA142670670

Chemistry databases

ChEMBLiCHEMBL3797012
DrugBankiDB05147 CYT997

Polymorphism and mutation databases

BioMutaiTUBB2A
DMDMi74762137

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002626481 – 445Tubulin beta-2A chainAdd BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40PhosphoserineBy similarity1
Modified residuei58N6-acetyllysine; alternateBy similarity1
Modified residuei58N6-succinyllysine; alternateBy similarity1
Cross-linki58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei172Phosphoserine; by CDK11 Publication1
Modified residuei285PhosphothreonineBy similarity1
Modified residuei290PhosphothreonineBy similarity1
Modified residuei318Omega-N-methylarginineBy similarity1
Cross-linki324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei4385-glutamyl polyglutamateBy similarity1

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
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.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13885
MaxQBiQ13885
PaxDbiQ13885
PeptideAtlasiQ13885
PRIDEiQ13885
ProteomicsDBi59713
TopDownProteomicsiQ13885

PTM databases

iPTMnetiQ13885
PhosphoSitePlusiQ13885
SwissPalmiQ13885

Expressioni

Tissue specificityi

High expression in brain, where it represents 30% of all beta-tubulins.1 Publication

Gene expression databases

BgeeiENSG00000137267 Expressed in 236 organ(s), highest expression level in parietal lobe
CleanExiHS_TUBB2A
GenevisibleiQ13885 HS

Organism-specific databases

HPAiCAB015339
HPA043640
HPA046280

Interactioni

Subunit structurei

Interacts with ZNRF1 (By similarity). Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity (By similarity). 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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ACDQ96AP02EBI-711595,EBI-717666

Protein-protein interaction databases

BioGridi113131, 132 interactors
IntActiQ13885, 64 interactors
MINTiQ13885
STRINGi9606.ENSP00000369703

Structurei

3D structure databases

ProteinModelPortaliQ13885
SMRiQ13885
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00760000119061
HOGENOMiHOG000165710
HOVERGENiHBG000089
InParanoidiQ13885
KOiK07375
OMAiTADEMGE
OrthoDBiEOG091G06U2
PhylomeDBiQ13885
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.

Q13885-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY
60 70 80 90 100
YNEAAGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEYP DRIMNTFSVM PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
SIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM
310 320 330 340 350
AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEE GEDEA
Length:445
Mass (Da):49,907
Last modified:November 1, 1996 - v1
Checksum:i93B3213EB2A9367B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti191Q → H in AAN85571 (Ref. 2) Curated1
Sequence conflicti202I → H in CAG46756 (Ref. 3) Curated1
Sequence conflicti263L → V in CAG46756 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03619762R → W in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs774124807Ensembl.1
Natural variantiVAR_071168247N → K in CDCBM5; abolishes coassembly with tubulin subunits and incorporation into the microtubule polymer network. 1 PublicationCorresponds to variant dbSNP:rs886037663EnsemblClinVar.1
Natural variantiVAR_071169248A → V in CDCBM5; reduces coassembly with tubulin subunits and incorporation into the microtubule polymer network. 1 PublicationCorresponds to variant dbSNP:rs2808001EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79535 mRNA Translation: CAA56071.1
AY159127 mRNA Translation: AAN85571.1
CR541958 mRNA Translation: CAG46756.1
AL031963 Genomic DNA No translation available.
BC001194 mRNA Translation: AAH01194.1
BC018780 mRNA Translation: AAH18780.1
CCDSiCCDS4484.1
PIRiT08726
RefSeqiNP_001060.1, NM_001069.2
NP_001297244.1, NM_001310315.1
UniGeneiHs.654543

Genome annotation databases

EnsembliENST00000333628; ENSP00000369703; ENSG00000137267
GeneIDi7280
KEGGihsa:7280
UCSCiuc003mvc.5 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79535 mRNA Translation: CAA56071.1
AY159127 mRNA Translation: AAN85571.1
CR541958 mRNA Translation: CAG46756.1
AL031963 Genomic DNA No translation available.
BC001194 mRNA Translation: AAH01194.1
BC018780 mRNA Translation: AAH18780.1
CCDSiCCDS4484.1
PIRiT08726
RefSeqiNP_001060.1, NM_001069.2
NP_001297244.1, NM_001310315.1
UniGeneiHs.654543

3D structure databases

ProteinModelPortaliQ13885
SMRiQ13885
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113131, 132 interactors
IntActiQ13885, 64 interactors
MINTiQ13885
STRINGi9606.ENSP00000369703

Chemistry databases

ChEMBLiCHEMBL3797012
DrugBankiDB05147 CYT997

PTM databases

iPTMnetiQ13885
PhosphoSitePlusiQ13885
SwissPalmiQ13885

Polymorphism and mutation databases

BioMutaiTUBB2A
DMDMi74762137

Proteomic databases

EPDiQ13885
MaxQBiQ13885
PaxDbiQ13885
PeptideAtlasiQ13885
PRIDEiQ13885
ProteomicsDBi59713
TopDownProteomicsiQ13885

Protocols and materials databases

DNASUi7280
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333628; ENSP00000369703; ENSG00000137267
GeneIDi7280
KEGGihsa:7280
UCSCiuc003mvc.5 human

Organism-specific databases

CTDi7280
DisGeNETi7280
EuPathDBiHostDB:ENSG00000137267.5
GeneCardsiTUBB2A
H-InvDBiHIX0164828
HGNCiHGNC:12412 TUBB2A
HPAiCAB015339
HPA043640
HPA046280
MalaCardsiTUBB2A
MIMi615101 gene
615763 phenotype
neXtProtiNX_Q13885
OpenTargetsiENSG00000137267
PharmGKBiPA142670670
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1375 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00760000119061
HOGENOMiHOG000165710
HOVERGENiHBG000089
InParanoidiQ13885
KOiK07375
OMAiTADEMGE
OrthoDBiEOG091G06U2
PhylomeDBiQ13885
TreeFamiTF300298

Enzyme and pathway databases

ReactomeiR-HSA-1445148 Translocation of SLC2A4 (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-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
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-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-8955332 Carboxyterminal post-translational modifications of tubulin
R-HSA-983189 Kinesins
SIGNORiQ13885

Miscellaneous databases

ChiTaRSiTUBB2A human
GeneWikiiTUBB2A
GenomeRNAii7280
PROiPR:Q13885
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137267 Expressed in 236 organ(s), highest expression level in parietal lobe
CleanExiHS_TUBB2A
GenevisibleiQ13885 HS

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
ProtoNetiSearch...

Entry informationi

Entry nameiTBB2A_HUMAN
AccessioniPrimary (citable) accession number: Q13885
Secondary accession number(s): Q6FGZ8, Q8IWR2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 1, 1996
Last modified: November 7, 2018
This is version 176 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
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