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Protein

Tubulin beta-2B chain

Gene

TUBB2B

Organism
Homo sapiens (Human)
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 (By similarity). TUBB2B is implicated in neuronal migration.By similarity1 Publication

Regions

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

GO - Molecular functioni

GO - Biological processi

  • microtubule-based process Source: InterPro
  • neuron migration Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

GTP-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-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. Assembly of the primary cilium.
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-983189. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-2B chain
Gene namesi
Name:TUBB2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:30829. TUBB2B.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-KW
  • microtubule Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Cortical dysplasia, complex, with other brain malformations 7 (CDCBM7)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. Polymicrogyria is a heterogeneous disorder, considered to be the result of postmigratory abnormal cortical organization.
See also OMIM:610031
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063389172S → P in CDCBM7; affects microtubules assembly. 1 PublicationCorresponds to variant rs137853194dbSNPEnsembl.1
Natural variantiVAR_063391210I → T in CDCBM7. 1 Publication1
Natural variantiVAR_063392228L → P in CDCBM7. 1 PublicationCorresponds to variant rs137853195dbSNPEnsembl.1
Natural variantiVAR_063393265F → L in CDCBM7; affects microtubules assembly. 1 PublicationCorresponds to variant rs137853196dbSNPEnsembl.1
Natural variantiVAR_063394312T → M in CDCBM7. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi347733.
MalaCardsiTUBB2B.
MIMi610031. phenotype.
OpenTargetsiENSG00000137285.
Orphaneti45358. Congenital fibrosis of extraocular muscles.
300573. Polymicrogyria due to TUBB2B mutation.
PharmGKBiPA142670671.

Chemistry databases

ChEMBLiCHEMBL2095182.

Polymorphism and mutation databases

BioMutaiTUBB2B.
DMDMi74761283.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002626511 – 445Tubulin beta-2B chainAdd BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40PhosphoserineBy similarity1
Modified residuei55PhosphothreonineBy 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

EPDiQ9BVA1.
MaxQBiQ9BVA1.
PaxDbiQ9BVA1.
PeptideAtlasiQ9BVA1.
PRIDEiQ9BVA1.
TopDownProteomicsiQ9BVA1.

PTM databases

iPTMnetiQ9BVA1.
PhosphoSitePlusiQ9BVA1.
SwissPalmiQ9BVA1.

Expressioni

Tissue specificityi

High expression in brain.1 Publication

Gene expression databases

BgeeiENSG00000137285.
CleanExiHS_TUBB2B.
GenevisibleiQ9BVA1. HS.

Organism-specific databases

HPAiHPA043640.
HPA046280.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
CACNA1AO005552EBI-355665,EBI-766279

Protein-protein interaction databases

BioGridi131483. 67 interactors.
IntActiQ9BVA1. 22 interactors.
MINTiMINT-1152234.
STRINGi9606.ENSP00000259818.

Structurei

3D structure databases

ProteinModelPortaliQ9BVA1.
SMRiQ9BVA1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ9BVA1.
KOiK07375.
OMAiFWEVICA.
OrthoDBiEOG091G06U2.
PhylomeDBiQ9BVA1.
TreeFamiTF300298.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR013838. Beta-tubulin_BS.
IPR002453. Beta_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BVA1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY
60 70 80 90 100
YNEATGNKYV 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
CIDNEALYDI 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):49,953
Last modified:June 1, 2001 - v1
Checksum:i4DC3956EFF880746
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063389172S → P in CDCBM7; affects microtubules assembly. 1 PublicationCorresponds to variant rs137853194dbSNPEnsembl.1
Natural variantiVAR_063390201C → S.1 PublicationCorresponds to variant rs1054331dbSNPEnsembl.1
Natural variantiVAR_063391210I → T in CDCBM7. 1 Publication1
Natural variantiVAR_063392228L → P in CDCBM7. 1 PublicationCorresponds to variant rs137853195dbSNPEnsembl.1
Natural variantiVAR_063393265F → L in CDCBM7; affects microtubules assembly. 1 PublicationCorresponds to variant rs137853196dbSNPEnsembl.1
Natural variantiVAR_063394312T → M in CDCBM7. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT019930 mRNA. Translation: AAV38733.1.
CR456788 mRNA. Translation: CAG33069.1.
AK289433 mRNA. Translation: BAF82122.1.
AL445309 Genomic DNA. Translation: CAI40952.1.
CH471087 Genomic DNA. Translation: EAW55125.1.
BC001352 mRNA. Translation: AAH01352.1.
BC063610 mRNA. Translation: AAH63610.1.
CCDSiCCDS4485.1.
RefSeqiNP_821080.1. NM_178012.4.
UniGeneiHs.300701.

Genome annotation databases

EnsembliENST00000259818; ENSP00000259818; ENSG00000137285.
GeneIDi347733.
KEGGihsa:347733.
UCSCiuc003mvg.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT019930 mRNA. Translation: AAV38733.1.
CR456788 mRNA. Translation: CAG33069.1.
AK289433 mRNA. Translation: BAF82122.1.
AL445309 Genomic DNA. Translation: CAI40952.1.
CH471087 Genomic DNA. Translation: EAW55125.1.
BC001352 mRNA. Translation: AAH01352.1.
BC063610 mRNA. Translation: AAH63610.1.
CCDSiCCDS4485.1.
RefSeqiNP_821080.1. NM_178012.4.
UniGeneiHs.300701.

3D structure databases

ProteinModelPortaliQ9BVA1.
SMRiQ9BVA1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi131483. 67 interactors.
IntActiQ9BVA1. 22 interactors.
MINTiMINT-1152234.
STRINGi9606.ENSP00000259818.

Chemistry databases

ChEMBLiCHEMBL2095182.

PTM databases

iPTMnetiQ9BVA1.
PhosphoSitePlusiQ9BVA1.
SwissPalmiQ9BVA1.

Polymorphism and mutation databases

BioMutaiTUBB2B.
DMDMi74761283.

Proteomic databases

EPDiQ9BVA1.
MaxQBiQ9BVA1.
PaxDbiQ9BVA1.
PeptideAtlasiQ9BVA1.
PRIDEiQ9BVA1.
TopDownProteomicsiQ9BVA1.

Protocols and materials databases

DNASUi347733.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000259818; ENSP00000259818; ENSG00000137285.
GeneIDi347733.
KEGGihsa:347733.
UCSCiuc003mvg.4. human.

Organism-specific databases

CTDi347733.
DisGeNETi347733.
GeneCardsiTUBB2B.
HGNCiHGNC:30829. TUBB2B.
HPAiHPA043640.
HPA046280.
MalaCardsiTUBB2B.
MIMi610031. phenotype.
612850. gene.
neXtProtiNX_Q9BVA1.
OpenTargetsiENSG00000137285.
Orphaneti45358. Congenital fibrosis of extraocular muscles.
300573. Polymicrogyria due to TUBB2B mutation.
PharmGKBiPA142670671.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ9BVA1.
KOiK07375.
OMAiFWEVICA.
OrthoDBiEOG091G06U2.
PhylomeDBiQ9BVA1.
TreeFamiTF300298.

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-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. Assembly of the primary cilium.
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-983189. Kinesins.

Miscellaneous databases

ChiTaRSiTUBB2B. human.
GenomeRNAii347733.
PROiQ9BVA1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137285.
CleanExiHS_TUBB2B.
GenevisibleiQ9BVA1. HS.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR013838. Beta-tubulin_BS.
IPR002453. Beta_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTBB2B_HUMAN
AccessioniPrimary (citable) accession number: Q9BVA1
Secondary accession number(s): A8K068
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: June 1, 2001
Last modified: November 30, 2016
This is version 152 of the entry and version 1 of the sequence. [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. Human chromosome 6
    Human chromosome 6: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.