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P68369

- TBA1A_MOUSE

UniProt

P68369 - TBA1A_MOUSE

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Protein

Tubulin alpha-1A chain

Gene

Tuba1a

Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei451 – 4511Involved in polymerization

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1487GTPSequence Analysis

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  1. microtubule-based process Source: InterPro
  2. protein polymerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_196550. MHC class II antigen presentation.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_199117. Kinesins.
REACT_207679. Separation of Sister Chromatids.
REACT_218773. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_227366. Gap junction assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-1A chain
Alternative name(s):
Alpha-tubulin 1
Alpha-tubulin isotype M-alpha-1
Tubulin alpha-1 chain
Gene namesi
Name:Tuba1a
Synonyms:Tuba1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:98869. Tuba1a.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmic microtubule Source: MGI
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Tubulin alpha-1A chainPRO_0000048120Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481PhosphoserineBy similarity
Modified residuei83 – 831Nitrated tyrosineBy similarity
Modified residuei282 – 2821Nitrated tyrosineBy similarity
Modified residuei432 – 4321PhosphotyrosineBy similarity
Modified residuei439 – 4391PhosphoserineBy similarity

Post-translational modificationi

Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.By similarity
Some glutamate residues at the C-terminus are either polyglutamylated or polyglycylated. These 2 modifications occur exclusively on glutamate residues and result in either polyglutamate or 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 such modifications is still unclear but they are regulate the assembly and dynamics of axonemal microtubules.
Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarity).By similarity

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

MaxQBiP68369.
PaxDbiP68369.
PRIDEiP68369.

2D gel databases

SWISS-2DPAGEP68369.

PTM databases

PhosphoSiteiP68369.

Miscellaneous databases

PMAP-CutDBP68369.

Expressioni

Tissue specificityi

Ubiquitously expressed, although primarily in lung and brain.1 Publication

Gene expression databases

BgeeiP68369.
CleanExiMM_TUBA1A.
GenevestigatoriP68369.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
CyldQ80TQ25EBI-400542,EBI-943859

Protein-protein interaction databases

BioGridi204372. 29 interactions.
IntActiP68369. 18 interactions.
MINTiMINT-3288915.
STRINGi10090.ENSMUSP00000094778.

Structurei

3D structure databases

ProteinModelPortaliP68369.
SMRiP68369. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00760000119060.
HOVERGENiHBG000089.
InParanoidiP68369.
KOiK07374.
OMAiTRATHEA.
OrthoDBiEOG7TBC1W.
PhylomeDBiP68369.
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.

P68369-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN
60 70 80 90 100
TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT
160 170 180 190 200
SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440 450
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE

Y
Length:451
Mass (Da):50,136
Last modified:July 21, 1986 - v1
Checksum:i00F8429A4A10E5FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241K → E in BAE40598. (PubMed:16141072)Curated
Sequence conflicti132 – 1321L → P in BAE26417. (PubMed:16141072)Curated
Sequence conflicti257 – 2571T → I in BAE37745. (PubMed:16141072)Curated
Sequence conflicti273 – 2731A → S in AAH83344. (PubMed:15489334)Curated
Sequence conflicti328 – 3281V → G in BAE26417. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M13445 mRNA. Translation: AAA40499.1.
AK077529 mRNA. Translation: BAC36848.1.
AK145404 mRNA. Translation: BAE26417.1.
AK146983 mRNA. Translation: BAE27586.1.
AK164335 mRNA. Translation: BAE37745.1.
AK167687 mRNA. Translation: BAE39734.1.
AK168762 mRNA. Translation: BAE40598.1.
AK169610 mRNA. Translation: BAE41258.1.
BC056169 mRNA. Translation: AAH56169.1.
BC083343 mRNA. Translation: AAH83343.1.
BC083345 mRNA. Translation: AAH83345.1.
BC085256 mRNA. Translation: AAH85256.1.
M28729 mRNA. Translation: AAA40506.1.
BC083344 mRNA. Translation: AAH83344.1.
CCDSiCCDS37196.1.
PIRiI77424.
RefSeqiNP_035783.1. NM_011653.2.
UniGeneiMm.405359.

Genome annotation databases

EnsembliENSMUST00000097014; ENSMUSP00000094778; ENSMUSG00000072235.
GeneIDi22142.
KEGGimmu:22142.
UCSCiuc007xok.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M13445 mRNA. Translation: AAA40499.1 .
AK077529 mRNA. Translation: BAC36848.1 .
AK145404 mRNA. Translation: BAE26417.1 .
AK146983 mRNA. Translation: BAE27586.1 .
AK164335 mRNA. Translation: BAE37745.1 .
AK167687 mRNA. Translation: BAE39734.1 .
AK168762 mRNA. Translation: BAE40598.1 .
AK169610 mRNA. Translation: BAE41258.1 .
BC056169 mRNA. Translation: AAH56169.1 .
BC083343 mRNA. Translation: AAH83343.1 .
BC083345 mRNA. Translation: AAH83345.1 .
BC085256 mRNA. Translation: AAH85256.1 .
M28729 mRNA. Translation: AAA40506.1 .
BC083344 mRNA. Translation: AAH83344.1 .
CCDSi CCDS37196.1.
PIRi I77424.
RefSeqi NP_035783.1. NM_011653.2.
UniGenei Mm.405359.

3D structure databases

ProteinModelPortali P68369.
SMRi P68369. Positions 1-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204372. 29 interactions.
IntActi P68369. 18 interactions.
MINTi MINT-3288915.
STRINGi 10090.ENSMUSP00000094778.

Chemistry

BindingDBi P68369.

PTM databases

PhosphoSitei P68369.

2D gel databases

SWISS-2DPAGE P68369.

Proteomic databases

MaxQBi P68369.
PaxDbi P68369.
PRIDEi P68369.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000097014 ; ENSMUSP00000094778 ; ENSMUSG00000072235 .
GeneIDi 22142.
KEGGi mmu:22142.
UCSCi uc007xok.1. mouse.

Organism-specific databases

CTDi 7846.
MGIi MGI:98869. Tuba1a.

Phylogenomic databases

eggNOGi COG5023.
GeneTreei ENSGT00760000119060.
HOVERGENi HBG000089.
InParanoidi P68369.
KOi K07374.
OMAi TRATHEA.
OrthoDBi EOG7TBC1W.
PhylomeDBi P68369.
TreeFami TF300314.

Enzyme and pathway databases

Reactomei REACT_196550. MHC class II antigen presentation.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_199117. Kinesins.
REACT_207679. Separation of Sister Chromatids.
REACT_218773. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_227366. Gap junction assembly.

Miscellaneous databases

ChiTaRSi TUBA1A. mouse.
NextBioi 302038.
PMAP-CutDB P68369.
PROi P68369.
SOURCEi Search...

Gene expression databases

Bgeei P68369.
CleanExi MM_TUBA1A.
Genevestigatori P68369.

Family and domain databases

Gene3Di 1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProi IPR002452. 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 ]
PANTHERi PTHR11588. PTHR11588. 1 hit.
Pfami PF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view ]
PRINTSi PR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTi SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view ]
SUPFAMi SSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEi PS00227. TUBULIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis-specific expression of two sister genes."
    Villasante A., Wang D., Dobner P., Dolph P., Lewis S.A., Cowan N.J.
    Mol. Cell. Biol. 6:2409-2419(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Heart, Kidney, Placenta, Spinal ganglion and Thymus.
  3. "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/6.
    Tissue: Brain and Olfactory epithelium.
  4. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 41-60; 65-79; 85-121; 157-163; 216-280; 312-320; 327-336; 340-370; 374-401 AND 403-440, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  5. "Five mouse tubulin isotypes and their regulated expression during development."
    Lewis S.A., Lee M.G.-S., Cowan N.J.
    J. Cell Biol. 101:852-861(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 254-451.
  6. Cited for: POLYGLUTAMYLATION.
  7. "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: POLYGLYCYLATION.

Entry informationi

Entry nameiTBA1A_MOUSE
AccessioniPrimary (citable) accession number: P68369
Secondary accession number(s): P02551
, P05210, P05212, Q3TGF0, Q3TIW2, Q3TPJ1, Q3ULN1, Q5XJF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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

External Data

Dasty 3