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Protein

Tubulin alpha-8 chain

Gene

Tuba8

Organism
Mus musculus (Mouse)
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-MMU-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-MMU-2132295 MHC class II antigen presentation
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-MMU-380320 Recruitment of NuMA to mitotic centrosomes
R-MMU-437239 Recycling pathway of L1
R-MMU-5626467 RHO GTPases activate IQGAPs
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-6807878 COPI-mediated anterograde transport
R-MMU-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-MMU-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-MMU-68877 Mitotic Prometaphase
R-MMU-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-MMU-8955332 Carboxyterminal post-translational modifications of tubulin
R-MMU-983189 Kinesins

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-8 chain
Alternative name(s):
Alpha-tubulin 8
Gene namesi
Name:Tuba8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1858225 Tuba8

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000481251 – 449Tubulin alpha-8 chainAdd BLAST449

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation 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 polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear.1 Publication
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). 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 (By similarity).By similarity1 Publication

Proteomic databases

EPDiQ9JJZ2
MaxQBiQ9JJZ2
PaxDbiQ9JJZ2
PeptideAtlasiQ9JJZ2
PRIDEiQ9JJZ2

PTM databases

iPTMnetiQ9JJZ2
PhosphoSitePlusiQ9JJZ2
SwissPalmiQ9JJZ2

Expressioni

Tissue specificityi

Expressed at highest levels in the testis, followed by skeletal and heart muscle. Expressed at low levels in the developing brain.1 Publication

Developmental stagei

At embryonic day (E) 13.5, expressed in the cortical preplate and cingulate cortex. By E15. 5, the strongest expression is seen in the cortical plate. By E18.5, cortical expression is most intense in the upper layers and subplate. There is strong expression in the areas CA1-3 of the hippocampus. At P0, cortical expression is strongest in the dense cortical plate and subplate. Hippocampal expression is more intense in areas CA1-3 than in the dentate gyrus. At P8, lamination is almost complete and cortical expression is strongest in layers II-III and V and the subplate. There is also expression in the mediodorsal nuclei of the thalamus, the mitral cell layer of the olfactory bulb, and the external granular layer, molecular layer, and internal granular cell layer of the cerebellum.2 Publications

Gene expression databases

BgeeiENSMUSG00000030137
CleanExiMM_TUBA8
GenevisibleiQ9JJZ2 MM

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

BioGridi207491, 1 interactor
IntActiQ9JJZ2, 2 interactors
MINTiQ9JJZ2
STRINGi10090.ENSMUSP00000032233

Structurei

3D structure databases

ProteinModelPortaliQ9JJZ2
SMRiQ9JJZ2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1376 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00760000119060
HOGENOMiHOG000165711
HOVERGENiHBG000089
InParanoidiQ9JJZ2
KOiK07374
OMAiNMAISHI
OrthoDBiEOG091G0736
PhylomeDBiQ9JJZ2
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

Sequencei

Sequence statusi: Complete.

Q9JJZ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRECISVHVG QAGVQIGNAC WELFCLEHGI QADGTFGTQA SKINDDDSFT
60 70 80 90 100
TFFSETGNGK HVPRAVMVDL 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):50,052
Last modified:October 1, 2000 - v1
Checksum:iAA979E2DB21FC5DD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti447E → G in BAB26288 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ245923 mRNA Translation: CAB88033.1
GU591980 mRNA Translation: ADD82895.1
CH466523 Genomic DNA Translation: EDK99659.1
BC017631 mRNA Translation: AAH17631.1
AK009439 mRNA Translation: BAB26288.1
CCDSiCCDS39615.1
RefSeqiNP_059075.1, NM_017379.2
UniGeneiMm.32884

Genome annotation databases

EnsembliENSMUST00000032233; ENSMUSP00000032233; ENSMUSG00000030137
GeneIDi53857
KEGGimmu:53857
UCSCiuc009dof.1 mouse

Similar proteinsi

Entry informationi

Entry nameiTBA8_MOUSE
AccessioniPrimary (citable) accession number: Q9JJZ2
Secondary accession number(s): D4P911, Q9CV57
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 1, 2000
Last modified: May 23, 2018
This is version 146 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health