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Protein

Tubulin beta-8 chain

Gene

TUBB8

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). TUBB8 has a key role in meiotic spindle assembly and oocyte maturation (PubMed:26789871).By similarity1 Publication

Regions

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

GO - Molecular functioni

GO - Biological processi

  • oocyte maturation Source: UniProtKB
  • spindle assembly involved in female meiosis Source: UniProtKB

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-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
R-HSA-437239 Recycling pathway of L1
R-HSA-5617833 Cilium Assembly
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

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-8 chainCurated
Alternative name(s):
Tubulin beta 8 class VIIIImported
Gene namesi
Name:TUBB8Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000261456.5
HGNCiHGNC:20773 TUBB8
MIMi616768 gene
neXtProtiNX_Q3ZCM7

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

Oocyte maturation defect 2 (OOMD2)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant infertility disorder caused by defective oocyte maturation. Oocytes are arrested at metaphase I, and have an abnormal or no detectable spindle on polarization microscopy.
See also OMIM:616780
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0768982R → K in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025273EnsemblClinVar.1
Natural variantiVAR_07689927 – 33Missing in OOMD2; loss of alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly. 1 Publication7
Natural variantiVAR_076900176S → L in OOMD2; loss of function in oocyte maturation; loss of function in meiotic spindle assembly; decreased alpha/beta-tubulin heterodimer assembly. 2 PublicationsCorresponds to variant dbSNP:rs869025609EnsemblClinVar.1
Natural variantiVAR_076901210I → V in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs781853492Ensembl.1
Natural variantiVAR_076902229V → A in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025271EnsemblClinVar.1
Natural variantiVAR_076903238T → M in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly. 1 Publication1
Natural variantiVAR_076904255V → M in OOMD2; loss of function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs782269374Ensembl.1
Natural variantiVAR_076905262R → Q in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025610EnsemblClinVar.1
Natural variantiVAR_076906262R → W in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; does not affect function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs782486119Ensembl.1
Natural variantiVAR_076907285T → P in OOMD2; loss of function in meiotic spindle assembly. 1 Publication1
Natural variantiVAR_076908300M → I in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025612EnsemblClinVar.1
Natural variantiVAR_076909348N → S in OOMD2; loss of function in meiotic spindle assembly. 1 Publication1
Natural variantiVAR_076910363M → T in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025611EnsemblClinVar.1
Natural variantiVAR_076911417D → N in OOMD2; loss of function in oocyte maturation; loss of function in meiotic spindle assembly; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025272EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi347688
MalaCardsiTUBB8
MIMi616780 phenotype
OpenTargetsiENSG00000261456

Chemistry databases

ChEMBLiCHEMBL2095182

Polymorphism and mutation databases

BioMutaiTUBB8
DMDMi182705285

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003206311 – 444Tubulin beta-8 chainAdd BLAST444

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei172Phosphoserine; by CDK11 Publication1
Modified residuei4365-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

Isopeptide bond, Phosphoprotein

Proteomic databases

EPDiQ3ZCM7
MaxQBiQ3ZCM7
PaxDbiQ3ZCM7
PeptideAtlasiQ3ZCM7
PRIDEiQ3ZCM7
ProteomicsDBi61904

PTM databases

iPTMnetiQ3ZCM7
PhosphoSitePlusiQ3ZCM7
SwissPalmiQ3ZCM7

Expressioni

Tissue specificityi

Expressed at a high level in oocytes, at different stages of development.1 Publication

Gene expression databases

BgeeiENSG00000261456
ExpressionAtlasiQ3ZCM7 baseline and differential

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.

Protein-protein interaction databases

BioGridi131462, 200 interactors
IntActiQ3ZCM7, 13 interactors
MINTiQ3ZCM7
STRINGi9606.ENSP00000328808

Structurei

3D structure databases

ProteinModelPortaliQ3ZCM7
SMRiQ3ZCM7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00760000119061
HOGENOMiHOG000165710
HOVERGENiHBG000089
InParanoidiQ3ZCM7
KOiK07375
OMAiLTQIGQC
OrthoDBiEOG091G06U2
PhylomeDBiQ3ZCM7
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.

Q3ZCM7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVLTQIG QCGNQIGAKF WEVISDEHAI DSAGTYHGDS HLQLERINVY
60 70 80 90 100
YNEASGGRYV PRAVLVDLEP GTMDSVRSGP FGQVFRPDNF IFGQCGAGNN
110 120 130 140 150
WAKGHYTEGA ELMESVMDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LLSKIREEYP DRIINTFSIL PSPKVSDTVV EPYNATLSVH QLIENADETF
210 220 230 240 250
CIDNEALYDI CSKTLKLPTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVAELT QQMFDAKNMM
310 320 330 340 350
AACDPRHGRY LTAAAIFRGR MPMREVDEQM FNIQDKNSSY FADWLPNNVK
360 370 380 390 400
TAVCDIPPRG LKMSATFIGN NTAIQELFKR VSEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEEDEEYAE EEVA
Length:444
Mass (Da):49,776
Last modified:February 26, 2008 - v2
Checksum:i3EC4AC10946BF590
GO

Sequence cautioni

The sequence CAI16221 differs from that shown. Reason: Erroneous gene model prediction.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0768982R → K in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025273EnsemblClinVar.1
Natural variantiVAR_07689927 – 33Missing in OOMD2; loss of alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly. 1 Publication7
Natural variantiVAR_076900176S → L in OOMD2; loss of function in oocyte maturation; loss of function in meiotic spindle assembly; decreased alpha/beta-tubulin heterodimer assembly. 2 PublicationsCorresponds to variant dbSNP:rs869025609EnsemblClinVar.1
Natural variantiVAR_076901210I → V in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs781853492Ensembl.1
Natural variantiVAR_076902229V → A in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025271EnsemblClinVar.1
Natural variantiVAR_076903238T → M in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly. 1 Publication1
Natural variantiVAR_076904255V → M in OOMD2; loss of function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs782269374Ensembl.1
Natural variantiVAR_076905262R → Q in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025610EnsemblClinVar.1
Natural variantiVAR_076906262R → W in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; does not affect function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs782486119Ensembl.1
Natural variantiVAR_076907285T → P in OOMD2; loss of function in meiotic spindle assembly. 1 Publication1
Natural variantiVAR_076908300M → I in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025612EnsemblClinVar.1
Natural variantiVAR_039240345L → F. Corresponds to variant dbSNP:rs4880608Ensembl.1
Natural variantiVAR_076909348N → S in OOMD2; loss of function in meiotic spindle assembly. 1 Publication1
Natural variantiVAR_076910363M → T in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025611EnsemblClinVar.1
Natural variantiVAR_076911417D → N in OOMD2; loss of function in oocyte maturation; loss of function in meiotic spindle assembly; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025272EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF355127 Genomic DNA Translation: AAL32434.1
CR590375 mRNA No translation available.
AL713922 Genomic DNA Translation: CAI16221.1 Sequence problems.
CH471072 Genomic DNA Translation: EAW86545.1
BC101270 mRNA Translation: AAI01271.1
BC101271 mRNA Translation: AAI01272.1
CCDSiCCDS7051.1
RefSeqiNP_817124.1, NM_177987.2
UniGeneiHs.532659

Genome annotation databases

EnsembliENST00000568584; ENSP00000456206; ENSG00000261456
GeneIDi347688
KEGGihsa:347688
UCSCiuc001ifi.3 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiTBB8_HUMAN
AccessioniPrimary (citable) accession number: Q3ZCM7
Secondary accession number(s): Q5SQX9, Q8WZ78
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: June 20, 2018
This is version 121 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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

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