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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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi140 – 1467GTPSequence Analysis

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

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_121399. MHC class II antigen presentation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_16967. Post-chaperonin tubulin folding pathway.
REACT_22365. Recycling pathway of L1.
REACT_25201. Kinesins.
REACT_267965. Anchoring of the basal body to the plasma membrane.
REACT_268024. Intraflagellar transport.
REACT_268265. Assembly of the primary cilium.
REACT_268323. Hedgehog 'off' state.
REACT_355252. RHO GTPases Activate Formins.
REACT_355469. RHO GTPases activate IQGAPs.
REACT_682. Mitotic Prometaphase.
REACT_9509. Gap junction assembly.

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
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:20771. TUBB4B.

Subcellular locationi

GO - Cellular componenti

  • cytoskeleton Source: ProtInc
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular vesicle Source: UniProtKB
  • microtubule Source: UniProtKB
  • myelin sheath Source: Ensembl
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670672.

Chemistry

DrugBankiDB00518. Albendazole.
DB00643. Mebendazole.

Polymorphism and mutation databases

BioMutaiTUBB4B.
DMDMi55977480.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Tubulin beta-4B chainPRO_0000048248Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581N6-acetyllysine1 Publication
Modified residuei172 – 1721Phosphoserine; by CDK1Curated

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also 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) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules (Probable).1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP68371.
PeptideAtlasiP68371.
PRIDEiP68371.

2D gel databases

OGPiP05217.
REPRODUCTION-2DPAGEIPI00007752.
SWISS-2DPAGEP68371.

PTM databases

PhosphoSiteiP68371.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiP68371.
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.

Protein-protein interaction databases

BioGridi115656. 109 interactions.
IntActiP68371. 43 interactions.
MINTiMINT-1390314.
STRINGi9606.ENSP00000341289.

Structurei

3D structure databases

ProteinModelPortaliP68371.
SMRiP68371. Positions 2-427.
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

GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiP68371.
KOiK07375.
OMAiFWEVICA.
OrthoDBiEOG71ZP1H.
PhylomeDBiP68371.
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.

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. Translation: CAM24148.1.
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.
UCSCiuc004cmg.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02344 Genomic DNA. Translation: CAA26203.1.
BX255925 Genomic DNA. Translation: CAM24148.1.
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.

3D structure databases

ProteinModelPortaliP68371.
SMRiP68371. Positions 2-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115656. 109 interactions.
IntActiP68371. 43 interactions.
MINTiMINT-1390314.
STRINGi9606.ENSP00000341289.

Chemistry

ChEMBLiCHEMBL2095182.
DrugBankiDB00518. Albendazole.
DB00643. Mebendazole.

PTM databases

PhosphoSiteiP68371.

Polymorphism and mutation databases

BioMutaiTUBB4B.
DMDMi55977480.

2D gel databases

OGPiP05217.
REPRODUCTION-2DPAGEIPI00007752.
SWISS-2DPAGEP68371.

Proteomic databases

MaxQBiP68371.
PeptideAtlasiP68371.
PRIDEiP68371.

Protocols and materials databases

DNASUi10383.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340384; ENSP00000341289; ENSG00000188229.
GeneIDi10383.
KEGGihsa:10383.
UCSCiuc004cmg.1. human.

Organism-specific databases

CTDi10383.
GeneCardsiGC09P140136.
HGNCiHGNC:20771. TUBB4B.
HPAiCAB010880.
HPA043640.
HPA046280.
MIMi602660. gene.
neXtProtiNX_P68371.
PharmGKBiPA142670672.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiP68371.
KOiK07375.
OMAiFWEVICA.
OrthoDBiEOG71ZP1H.
PhylomeDBiP68371.
TreeFamiTF300298.

Enzyme and pathway databases

ReactomeiREACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_121399. MHC class II antigen presentation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_16967. Post-chaperonin tubulin folding pathway.
REACT_22365. Recycling pathway of L1.
REACT_25201. Kinesins.
REACT_267965. Anchoring of the basal body to the plasma membrane.
REACT_268024. Intraflagellar transport.
REACT_268265. Assembly of the primary cilium.
REACT_268323. Hedgehog 'off' state.
REACT_355252. RHO GTPases Activate Formins.
REACT_355469. RHO GTPases activate IQGAPs.
REACT_682. Mitotic Prometaphase.
REACT_9509. Gap junction assembly.

Miscellaneous databases

ChiTaRSiTUBB4B. human.
GeneWikiiTUBB2C.
GenomeRNAii10383.
NextBioi39335.
PROiP68371.
SOURCEiSearch...

Gene expression databases

BgeeiP68371.
CleanExiHS_TUBB2C.
GenevisibleiP68371. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Three expressed sequences within the human beta-tubulin multigene family each define a distinct isotype."
    Lewis S.A., Gilmartin M.E., Hall J.L., Cowan N.J.
    J. Mol. Biol. 182:11-20(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain, Cervix, Lung, Lymph, Muscle, Skin and Uterus.
  4. "Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
    Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.
    Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCYLATION.
  5. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: TISSUE SPECIFICITY.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTBB4B_HUMAN
AccessioniPrimary (citable) accession number: P68371
Secondary accession number(s): A2BFA2, P05217
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 22, 2015
This is version 120 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, 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

External Data

Dasty 3

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 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.