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-4B chain

Gene

TUBB4B

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.

Regions

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

GO - Molecular functioni

  • double-stranded RNA binding Source: MGI
  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB-KW
  • MHC class I protein binding Source: UniProtKB
  • structural constituent of cytoskeleton Source: InterPro
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

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-6798695. Neutrophil degranulation.
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.
SIGNORiP68371.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-4B chain
Alternative name(s):
Tubulin beta-2 chain
Tubulin beta-2C chain
Gene namesi
Name:TUBB4B
Synonyms:TUBB2C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

EuPathDBiHostDB:ENSG00000188229.5.
HGNCiHGNC:20771. TUBB4B.

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

Organism-specific databases

DisGeNETi10383.
OpenTargetsiENSG00000188229.
PharmGKBiPA142670672.

Chemistry databases

ChEMBLiCHEMBL1848.
DrugBankiDB00518. Albendazole.
DB05147. CYT997.
DB03010. Epothilone B.
DB01873. Epothilone D.
DB00643. Mebendazole.
DB04910. Oxibendazole.

Polymorphism and mutation databases

BioMutaiTUBB4B.
DMDMi55977480.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000482481 – 445Tubulin beta-4B chainAdd BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei55PhosphothreonineCombined sources1
Modified residuei58N6-acetyllysineCombined sources1
Modified residuei172Phosphoserine; by CDK11 Publication1
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, Phosphoprotein

Proteomic databases

EPDiP68371.
MaxQBiP68371.
PaxDbiP68371.
PeptideAtlasiP68371.
PRIDEiP68371.
TopDownProteomicsiP68371.

2D gel databases

OGPiP05217.
REPRODUCTION-2DPAGEiIPI00007752.
SWISS-2DPAGEiP68371.

PTM databases

iPTMnetiP68371.
PhosphoSitePlusiP68371.
SwissPalmiP68371.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000188229.
CleanExiHS_TUBB2C.
GenevisibleiP68371. HS.

Organism-specific databases

HPAiCAB010880.
HPA043640.
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.

GO - Molecular functioni

  • MHC class I protein binding Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115656. 146 interactors.
IntActiP68371. 65 interactors.
MINTiMINT-1390314.
STRINGi9606.ENSP00000341289.

Structurei

3D structure databases

ProteinModelPortaliP68371.
SMRiP68371.
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.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiP68371.
KOiK07375.
OMAiDEHEEGR.
OrthoDBiEOG091G06U2.
PhylomeDBiP68371.
TreeFamiTF300298.

Family and domain databases

Gene3Di3.30.1330.20. 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.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
PANTHERiPTHR11588. PTHR11588. 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.

P68371-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY
60 70 80 90 100
YNEATGGKYV PRAVLVDLEP 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 QQMFDAKNMM
310 320 330 340 350
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEGEFEEEA EEEVA
Length:445
Mass (Da):49,831
Last modified:August 13, 1987 - v1
Checksum:iA552C52822AFA072
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02344 Genomic DNA. Translation: CAA26203.1.
BX255925 Genomic DNA. No translation available.
BC001911 mRNA. Translation: AAH01911.1.
BC002783 mRNA. Translation: AAH02783.1.
BC002885 mRNA. Translation: AAH02885.1.
BC004188 mRNA. Translation: AAH04188.1.
BC007889 mRNA. Translation: AAH07889.1.
BC012835 mRNA. Translation: AAH12835.1.
BC019359 mRNA. Translation: AAH19359.1.
BC019829 mRNA. Translation: AAH19829.1.
BC039175 mRNA. Translation: AAH39175.1.
BC071889 mRNA. Translation: AAH71889.1.
CCDSiCCDS7039.1.
PIRiI38370.
RefSeqiNP_006079.1. NM_006088.5.
UniGeneiHs.433615.

Genome annotation databases

EnsembliENST00000340384; ENSP00000341289; ENSG00000188229.
GeneIDi10383.
KEGGihsa:10383.
UCSCiuc004cmh.2. human.

Similar proteinsi

Entry informationi

Entry nameiTBB4B_HUMAN
AccessioniPrimary (citable) accession number: P68371
Secondary accession number(s): A2BFA2, P05217
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: October 25, 2017
This is version 144 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, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families