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Protein

Tubulin beta-8 chain

Gene

TUBB8

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). 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
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-437239. Recycling pathway of L1.
R-HSA-5617833. Assembly of the primary cilium.
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-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

HGNCiHGNC:20773. TUBB8.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-KW
  • extracellular exosome Source: UniProtKB
  • meiotic spindle Source: UniProtKB
  • microtubule Source: UniProtKB-KW
Complete GO annotation...

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 Publication1
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 Publications1
Natural variantiVAR_076901210I → V in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly. 1 Publication1
Natural variantiVAR_076902229V → A in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 Publication1
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 Publication1
Natural variantiVAR_076905262R → Q in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 Publication1
Natural variantiVAR_076906262R → W in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; does not affect function in meiotic spindle assembly. 1 Publication1
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 Publication1
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 Publication1
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 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

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 residuei40PhosphoserineBy similarity1
Modified residuei172Phosphoserine; by CDK11 Publication1
Modified residuei285PhosphothreonineBy similarity1
Modified residuei290PhosphothreonineBy similarity1
Modified residuei318Omega-N-methylarginineBy similarity1
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, Methylation, Phosphoprotein

Proteomic databases

EPDiQ3ZCM7.
MaxQBiQ3ZCM7.
PaxDbiQ3ZCM7.
PeptideAtlasiQ3ZCM7.
PRIDEiQ3ZCM7.

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

BgeeiENSG00000173876.
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. 93 interactors.
IntActiQ3ZCM7. 5 interactors.
MINTiMINT-1144251.
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.
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.

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 Publication1
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 Publications1
Natural variantiVAR_076901210I → V in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly. 1 Publication1
Natural variantiVAR_076902229V → A in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 Publication1
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 Publication1
Natural variantiVAR_076905262R → Q in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 Publication1
Natural variantiVAR_076906262R → W in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; does not affect function in meiotic spindle assembly. 1 Publication1
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 Publication1
Natural variantiVAR_039240345L → F.Corresponds to variant rs4880608dbSNPEnsembl.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 Publication1
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 Publication1

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

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ3ZCM7.
SMRiQ3ZCM7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi131462. 93 interactors.
IntActiQ3ZCM7. 5 interactors.
MINTiMINT-1144251.
STRINGi9606.ENSP00000328808.

Chemistry databases

ChEMBLiCHEMBL2095182.

PTM databases

iPTMnetiQ3ZCM7.
PhosphoSitePlusiQ3ZCM7.
SwissPalmiQ3ZCM7.

Polymorphism and mutation databases

BioMutaiTUBB8.
DMDMi182705285.

Proteomic databases

EPDiQ3ZCM7.
MaxQBiQ3ZCM7.
PaxDbiQ3ZCM7.
PeptideAtlasiQ3ZCM7.
PRIDEiQ3ZCM7.

Protocols and materials databases

DNASUi347688.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi347688.
GeneCardsiTUBB8.
H-InvDBHIX0029368.
HGNCiHGNC:20773. TUBB8.
HPAiHPA043640.
HPA046280.
MIMi616768. gene.
616780. phenotype.
neXtProtiNX_Q3ZCM7.
OpenTargetsiENSG00000261456.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ3ZCM7.
KOiK07375.
OMAiLTQIGQC.
OrthoDBiEOG091G06U2.
PhylomeDBiQ3ZCM7.
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-437239. Recycling pathway of L1.
R-HSA-5617833. Assembly of the primary cilium.
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

GenomeRNAii347688.
PROiQ3ZCM7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000173876.
ExpressionAtlasiQ3ZCM7. baseline and differential.

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 nameiTBB8_HUMAN
AccessioniPrimary (citable) accession number: Q3ZCM7
Secondary accession number(s): Q5SQX9, Q8WZ78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: November 30, 2016
This is version 108 of the entry and version 2 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 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

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.