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UniProtKB - P07437 (TBB5_HUMAN)

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Protein

Tubulin beta chain

Gene

TUBB

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.

Regions

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

GO - Molecular functioni

  • GTPase activating protein binding Source: Ensembl
  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB-KW
  • MHC class I protein binding Source: UniProtKB
  • protein-containing complex binding Source: Ensembl
  • protein domain specific binding Source: Ensembl
  • structural constituent of cytoskeleton Source: Ensembl
  • structural molecule activity Source: BHF-UCL
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cell division Source: BHF-UCL
  • cellular process Source: DFLAT
  • 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
  • natural killer cell mediated cytotoxicity Source: UniProtKB
  • neutrophil degranulation Source: Reactome
  • regulation of G2/M transition of mitotic cell cycle Source: Reactome
  • spindle assembly Source: Ensembl
View the complete GO annotation on QuickGO ...

Keywordsi

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-2565942 Regulation of PLK1 Activity at G2/M Transition
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-5620912 Anchoring of the basal body to the plasma membrane
R-HSA-6798695 Neutrophil degranulation
R-HSA-8854518 AURKA Activation by TPX2
SIGNORiP07437

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta chain
Alternative name(s):
Tubulin beta-5 chain
Gene namesi
Name:TUBB
Synonyms:TUBB5
ORF Names:OK/SW-cl.56
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000196230.12
HGNCiHGNC:20778 TUBB
MIMi191130 gene
neXtProtiNX_P07437

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 6 (CDCBM6)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. Affected individuals have microcephaly, ataxia, and severe delayed psychomotor development. Brain imaging shows variable malformations of cortical development, including white matter streaks, dysmorphic basal ganglia, corpus callosum abnormalities, brainstem and cerebellar hypoplasia, cortical dysplasia, polymicrogyria.
See also OMIM:615771
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071763299M → V in CDCBM6; decreases the ability of the protein to assemble into tubulin heterodimers. 1 PublicationCorresponds to variant dbSNP:rs587777355EnsemblClinVar.1
Natural variantiVAR_071764353V → I in CDCBM6; does not affect the ability of the mutant polypeptides to assemble into heterodimers and incorporate into microtubules. 1 PublicationCorresponds to variant dbSNP:rs587777356EnsemblClinVar.1
Natural variantiVAR_071765401E → K in CDCBM6; arrests the assembly pathway of alpha/beta-tubulin; the mutant protein is unable to coassemble into a tubulin heterodimer but is instead distributed throughout the cytoplasm. 1 PublicationCorresponds to variant dbSNP:rs587777357EnsemblClinVar.1
Skin creases, congenital symmetric circumferential, 1 (CSCSC1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disease characterized by multiple, symmetric, circumferential rings of folded skin, affecting primarily the limbs. Affected individuals also exhibit intellectual disability, cleft palate, and dysmorphic features.
See also OMIM:156610
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07654315Q → K in CSCSC1; disrupts heterodimer assembly and microtubule dynamics. 1 PublicationCorresponds to variant dbSNP:rs864321676EnsemblClinVar.1
Natural variantiVAR_076544222Y → F in CSCSC1; disrupts heterodimer assembly and microtubule dynamics. 1 PublicationCorresponds to variant dbSNP:rs864321677EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi203068
MalaCardsiTUBB
MIMi156610 phenotype
615771 phenotype
OpenTargetsiENSG00000196230
PharmGKBiPA358

Chemistry databases

ChEMBLiCHEMBL5444
DrugBankiDB05284 CA4P
DB01394 Colchicine
DB05147 CYT997
DB03010 Epothilone B
DB01873 Epothilone D
DB01179 Podofilox
DB00570 Vinblastine
DB00541 Vincristine
DB00361 Vinorelbine
DB06042 ZEN-012
GuidetoPHARMACOLOGYi2640

Polymorphism and mutation databases

BioMutaiTUBB
DMDMi56757569

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000482431 – 444Tubulin beta chainAdd BLAST444

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40PhosphoserineBy similarity1
Modified residuei55PhosphothreonineCombined sources1
Modified residuei58N6-acetyllysine; alternateCombined sources1
Modified residuei58N6-succinyllysine; alternateBy similarity1
Cross-linki58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei172Phosphoserine; by CDK11 Publication1
Modified residuei285PhosphothreonineCombined sources1
Modified residuei290PhosphothreonineCombined sources1
Modified residuei318Omega-N-methylarginine1 Publication1
Cross-linki324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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

EPDiP07437
PaxDbiP07437
PeptideAtlasiP07437
PRIDEiP07437
ProteomicsDBi52002
TopDownProteomicsiP07437

2D gel databases

OGPiP07437
REPRODUCTION-2DPAGEiP07437
SWISS-2DPAGEiP07437
UCD-2DPAGEiP07437

PTM databases

iPTMnetiP07437
PhosphoSitePlusiP07437
SwissPalmiP07437

Expressioni

Tissue specificityi

Ubiquitously expressed with highest levels in spleen, thymus and immature brain.1 Publication

Gene expression databases

BgeeiENSG00000196230
CleanExiHS_TUBB
ExpressionAtlasiP07437 baseline and differential
GenevisibleiP07437 HS

Organism-specific databases

HPAiCAB005417
CAB012406
HPA043640
HPA046280

Interactioni

Subunit structurei

Heterodimer of alpha and beta chains (PubMed:26637975). 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 PIFO (PubMed:20643351). Interacts with DIAPH1 (PubMed:23325789). Interacts with MX1 (By similarity). May interact with RNABP10 (By similarity). Interacts with CFAP157 (By similarity).By similarity3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • GTPase activating protein binding Source: Ensembl
  • MHC class I protein binding Source: UniProtKB
  • protein domain specific binding Source: Ensembl
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi128444, 270 interactors
CORUMiP07437
DIPiDIP-32772N
IntActiP07437, 146 interactors
MINTiP07437
STRINGi9606.ENSP00000339001

Structurei

3D structure databases

ProteinModelPortaliP07437
SMRiP07437
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
HOVERGENiHBG000089
InParanoidiP07437
KOiK07375
OMAiESEKMRE
OrthoDBiEOG09370T84
PhylomeDBiP07437
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.

P07437-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY 
        60         70         80         90        100
YNEATGGKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN 
       110        120        130        140        150
WAKGHYTEGA ELVDSVLDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL 
       160        170        180        190        200
LISKIREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY 
       210        220        230        240        250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL 
       260        270        280        290        300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQVFDAKNMM 
       310        320        330        340        350
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK 
       360        370        380        390        400
TAVCDIPPRG LKMAVTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG 
       410        420        430        440 
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEEDFGEEA EEEA
Length:444
Mass (Da):49,671
Last modified:December 21, 2004 - v2
Checksum:i1E6CD0A36773A103
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti216K → R no nucleotide entry (PubMed:6688039).Curated1
Sequence conflicti216K → R in AAB59507 (PubMed:6865944).Curated1
Sequence conflicti231A → G no nucleotide entry (PubMed:6688039).Curated1
Sequence conflicti231A → G in AAB59507 (PubMed:6865944).Curated1
Sequence conflicti234 – 235SG → EC no nucleotide entry (PubMed:6688039).Curated2
Sequence conflicti234 – 235SG → EC in AAB59507 (PubMed:6865944).Curated2
Sequence conflicti288E → D no nucleotide entry (PubMed:6688039).Curated1
Sequence conflicti288E → D in AAB59507 (PubMed:6865944).Curated1
Sequence conflicti298N → D in AAH20946 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07654315Q → K in CSCSC1; disrupts heterodimer assembly and microtubule dynamics. 1 PublicationCorresponds to variant dbSNP:rs864321676EnsemblClinVar.1
Natural variantiVAR_076544222Y → F in CSCSC1; disrupts heterodimer assembly and microtubule dynamics. 1 PublicationCorresponds to variant dbSNP:rs864321677EnsemblClinVar.1
Natural variantiVAR_071763299M → V in CDCBM6; decreases the ability of the protein to assemble into tubulin heterodimers. 1 PublicationCorresponds to variant dbSNP:rs587777355EnsemblClinVar.1
Natural variantiVAR_071764353V → I in CDCBM6; does not affect the ability of the mutant polypeptides to assemble into heterodimers and incorporate into microtubules. 1 PublicationCorresponds to variant dbSNP:rs587777356EnsemblClinVar.1
Natural variantiVAR_071765401E → K in CDCBM6; arrests the assembly pathway of alpha/beta-tubulin; the mutant protein is unable to coassemble into a tubulin heterodimer but is instead distributed throughout the cytoplasm. 1 PublicationCorresponds to variant dbSNP:rs587777357EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00314 Genomic DNA Translation: AAB59507.1
AF141349 mRNA Translation: AAD33873.1
AF070561 mRNA Translation: AAC28642.1
AF070593 mRNA Translation: AAC28650.1
AF070600 mRNA Translation: AAC28654.1
BA000025 Genomic DNA Translation: BAB63321.1
AB088100 Genomic DNA Translation: BAC54932.1
AB062393 mRNA Translation: BAB93480.1
BC001938 mRNA Translation: AAH01938.1
BC002347 mRNA Translation: AAH02347.1
BC005838 mRNA Translation: AAH05838.1
BC007605 mRNA Translation: AAH07605.1
BC013374 mRNA Translation: AAH13374.1
BC019924 mRNA Translation: AAH19924.1
BC020946 mRNA Translation: AAH20946.1
BC021909 mRNA Translation: AAH21909.1
BC070326 mRNA Translation: AAH70326.1
CCDSiCCDS4687.1
PIRiA26561
RefSeqiNP_001280141.1, NM_001293212.1
NP_001280142.1, NM_001293213.1
NP_001280143.1, NM_001293214.1
NP_001280144.1, NM_001293215.1
NP_001280145.1, NM_001293216.1
NP_821133.1, NM_178014.3
UniGeneiHs.636480

Genome annotation databases

EnsembliENST00000327892; ENSP00000339001; ENSG00000196230
ENST00000383564; ENSP00000373058; ENSG00000183311
ENST00000419792; ENSP00000401317; ENSG00000235067
ENST00000421473; ENSP00000399155; ENSG00000224156
ENST00000422650; ENSP00000400663; ENSG00000229684
ENST00000422674; ENSP00000406811; ENSG00000227739
ENST00000432462; ENSP00000410829; ENSG00000232421
ENST00000436628; ENSP00000410071; ENSG00000232575
GeneIDi203068
KEGGihsa:203068

Similar proteinsi

Entry informationi

Entry nameiTBB5_HUMAN
AccessioniPrimary (citable) accession number: P07437
Secondary accession number(s): P05218, Q8WUC1, Q9CY33
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: December 21, 2004
Last modified: July 18, 2018
This is version 215 of the entry and version 2 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 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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