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 alpha-8 chain

Gene

TUBA8

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.

Miscellaneous

This tubulin does not have a C-terminal tyrosine.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi142 – 148GTPSequence analysis7

GO - Molecular functioni

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-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
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-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
SIGNORiQ9NY65

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-8 chain
Alternative name(s):
Alpha-tubulin 8
Tubulin alpha chain-like 2
Gene namesi
Name:TUBA8
Synonyms:TUBAL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

EuPathDBiHostDB:ENSG00000183785.14
HGNCiHGNC:12410 TUBA8
MIMi605742 gene
neXtProtiNX_Q9NY65

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 8 (CDCBM8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by extensive polymicrogyria, optic nerve hypoplasia, severe developmental delay, hypotonia, seizures, a dysplastic or absent corpus callosum and colpocephaly. Polymicrogyria is a malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. Polymicrogyria is a heterogeneous disorder, considered to be the result of postmigratory abnormal cortical organization.
See also OMIM:613180

Organism-specific databases

DisGeNETi1962
51807
MalaCardsiTUBA8
MIMi613180 phenotype
OpenTargetsiENSG00000183785
Orphaneti250972 Polymicrogyria with optic nerve hypoplasia
PharmGKBiPA37074

Chemistry databases

ChEMBLiCHEMBL3714503
DrugBankiDB03010 Epothilone B
DB01873 Epothilone D

Polymorphism and mutation databases

BioMutaiTUBA8
DMDMi12585376

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000481131 – 449Tubulin alpha-8 chainAdd BLAST449

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

Proteomic databases

MaxQBiQ9NY65
PaxDbiQ9NY65
PeptideAtlasiQ9NY65
PRIDEiQ9NY65
ProteomicsDBi83183
83184 [Q9NY65-2]

PTM databases

iPTMnetiQ9NY65
PhosphoSitePlusiQ9NY65
SwissPalmiQ9NY65

Miscellaneous databases

PMAP-CutDBiQ9NY65

Expressioni

Tissue specificityi

Preferentially expressed in heart, skeletal muscle and testis. Expressed at low levels in the developing brain.1 Publication

Gene expression databases

BgeeiENSG00000183785
CleanExiHS_TUBA8
ExpressionAtlasiQ9NY65 baseline and differential
GenevisibleiQ9NY65 HS

Organism-specific databases

HPAiCAB046031
HPA043684
HPA063394

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

BioGridi108282, 31 interactors
119733, 33 interactors
DIPiDIP-40751N
IntActiQ9NY65, 6 interactors
STRINGi9606.ENSP00000333326

Structurei

3D structure databases

ProteinModelPortaliQ9NY65
SMRiQ9NY65
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1376 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00920000149044
HOGENOMiHOG000165711
HOVERGENiHBG000089
InParanoidiQ9NY65
KOiK07374
PhylomeDBiQ9NY65
TreeFamiTF300314

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
IPR002452 Alpha_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
PfamiView protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit
PRINTSiPR01162 ALPHATUBULIN
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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NY65-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRECISVHVG QAGVQIGNAC WELFCLEHGI QADGTFDAQA SKINDDDSFT
60 70 80 90 100
TFFSETGNGK HVPRAVMIDL EPTVVDEVRA GTYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTV GKESIDLVLD RIRKLTDACS GLQGFLIFHS FGGGTGSGFT
160 170 180 190 200
SLLMERLSLD YGKKSKLEFA IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLV TYAPIISAEK AYHEQLSVAE ITSSCFEPNS
310 320 330 340 350
QMVKCDPRHG KYMACCMLYR GDVVPKDVNV AIAAIKTKRT IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440
KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGTDSF EEENEGEEF
Length:449
Mass (Da):50,094
Last modified:October 1, 2000 - v1
Checksum:i8D1AFB9D131529BD
GO
Isoform 2 (identifier: Q9NY65-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Show »
Length:383
Mass (Da):42,954
Checksum:iFA174EB2B97AF2D5
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052670128A → V. Corresponds to variant dbSNP:rs2234331EnsemblClinVar.1
Natural variantiVAR_024680301Q → R. Corresponds to variant dbSNP:rs2234333EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0428101 – 66Missing in isoform 2. 1 PublicationAdd BLAST66

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ245922 mRNA Translation: CAB88036.1
CR456600 mRNA Translation: CAG30486.1
AK056947 mRNA Translation: BAG51831.1
AK315316 mRNA Translation: BAG37719.1
AC007934 Genomic DNA No translation available.
AC128680 Genomic DNA No translation available.
CH471193 Genomic DNA Translation: EAW57788.1
CH471193 Genomic DNA Translation: EAW57789.1
BC074827 mRNA Translation: AAH74827.1
BC104845 mRNA Translation: AAI04846.1
CCDSiCCDS13751.1 [Q9NY65-1]
CCDS54495.1 [Q9NY65-2]
RefSeqiNP_001180343.1, NM_001193414.1 [Q9NY65-2]
NP_061816.1, NM_018943.2 [Q9NY65-1]
UniGeneiHs.137400

Genome annotation databases

EnsembliENST00000316027; ENSP00000318575; ENSG00000183785 [Q9NY65-2]
ENST00000330423; ENSP00000333326; ENSG00000183785 [Q9NY65-1]
GeneIDi51807
KEGGihsa:51807
UCSCiuc002znv.3 human [Q9NY65-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiTBA8_HUMAN
AccessioniPrimary (citable) accession number: Q9NY65
Secondary accession number(s): B2RCX2
, B3KPW9, B4DWG3, Q2M3N4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 1, 2000
Last modified: June 20, 2018
This is version 165 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health