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Protein

Tubulin alpha-8 chain

Gene

Tuba8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 bindingi142 – 1487GTPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-1445148. Translocation of GLUT4 to the plasma membrane.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1858225. Tuba8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Tubulin alpha-8 chainPRO_0000048125Add
BLAST

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.
PhosphoSiteiQ9JJZ2.

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

BgeeiQ9JJZ2.
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

IntActiQ9JJZ2. 1 interaction.
MINTiMINT-4137042.
STRINGi10090.ENSMUSP00000032233.

Structurei

3D structure databases

ProteinModelPortaliQ9JJZ2.
SMRiQ9JJZ2. Positions 1-436.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiQ9JJZ2.
KOiK07374.
OMAiIENANHE.
OrthoDBiEOG7TBC1W.
PhylomeDBiQ9JJZ2.
TreeFamiTF300314.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_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]
PRINTSiPR01162. ALPHATUBULIN.
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.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti447 – 4471E → G in BAB26288 (PubMed:16141072).Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ9JJZ2.
SMRiQ9JJZ2. Positions 1-436.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JJZ2. 1 interaction.
MINTiMINT-4137042.
STRINGi10090.ENSMUSP00000032233.

PTM databases

iPTMnetiQ9JJZ2.
PhosphoSiteiQ9JJZ2.

Proteomic databases

EPDiQ9JJZ2.
MaxQBiQ9JJZ2.
PaxDbiQ9JJZ2.
PeptideAtlasiQ9JJZ2.
PRIDEiQ9JJZ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51807.
MGIiMGI:1858225. Tuba8.

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiQ9JJZ2.
KOiK07374.
OMAiIENANHE.
OrthoDBiEOG7TBC1W.
PhylomeDBiQ9JJZ2.
TreeFamiTF300314.

Enzyme and pathway databases

ReactomeiR-MMU-1445148. Translocation of GLUT4 to the plasma membrane.

Miscellaneous databases

PROiQ9JJZ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJZ2.
CleanExiMM_TUBA8.
GenevisibleiQ9JJZ2. MM.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_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]
PRINTSiPR01162. ALPHATUBULIN.
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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "TUBA8: a new tissue-specific isoform of alpha-tubulin that is highly conserved in human and mouse."
    Stanchi F., Corso V., Scannapieco P., Ievolella C., Negrisolo E., Tiso N., Lanfranchi G., Valle G.
    Biochem. Biophys. Res. Commun. 270:1111-1118(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  2. "Tuba8 is expressed at low levels in the developing mouse and human brain."
    Braun A., Breuss M., Salzer M.C., Flint J., Cowan N.J., Keays D.A.
    Am. J. Hum. Genet. 86:819-822(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
    Tissue: Olfactory bulb.
  4. "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].
    Strain: C57BL/6J.
    Tissue: Eye.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-449.
    Strain: C57BL/6J.
    Tissue: Tongue.
  6. Cited for: GLUTAMYLATION.
  7. Cited for: DEVELOPMENTAL STAGE.
  8. "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.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Lung and Testis.

Entry informationi

Entry nameiTBA8_MOUSE
AccessioniPrimary (citable) accession number: Q9JJZ2
Secondary accession number(s): D4P911, Q9CV57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This tubulin does not have a C-terminal tyrosine.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.