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Protein

Tubulin alpha-1C chain

Gene

Tuba1c

Organism
Mus musculus (Mouse)
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei449 – 4491Involved 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. GTP catabolic process Source: InterPro
  2. microtubule-based process Source: InterPro
  3. 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_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.
REACT_245663. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_246290. Recruitment of NuMA to mitotic centrosomes.
REACT_247933. Post-chaperonin tubulin folding pathway.
REACT_256756. Mitotic Prometaphase.
REACT_257923. Recycling pathway of L1.
REACT_258053. Formation of tubulin folding intermediates by CCT/TriC.
REACT_269412. Hedgehog 'off' state.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-1C chain
Alternative name(s):
Alpha-tubulin 6
Alpha-tubulin isotype M-alpha-6
Tubulin alpha-6 chain
Gene namesi
Name:Tuba1c
Synonyms:Tuba6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1095409. Tuba1c.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmic microtubule Source: MGI
  2. nucleus Source: MGI
  3. vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Tubulin alpha-1C chainPRO_0000048124Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481PhosphoserineBy similarity
Modified residuei83 – 831Nitrated tyrosineBy similarity
Modified residuei282 – 2821Nitrated tyrosine1 Publication
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

MaxQBiP68373.
PaxDbiP68373.
PRIDEiP68373.

2D gel databases

REPRODUCTION-2DPAGEP68373.
SWISS-2DPAGEP99040.

PTM databases

PhosphoSiteiP68373.

Expressioni

Tissue specificityi

Minor alpha-tubulin expressed in all tissues.1 Publication

Gene expression databases

BgeeiP68373.
CleanExiMM_TUBA1C.
ExpressionAtlasiP68373. baseline and differential.
GenevestigatoriP68373.

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

BioGridi204376. 3 interactions.
IntActiP68373. 9 interactions.
MINTiMINT-4137025.

Structurei

3D structure databases

ProteinModelPortaliP68373.
SMRiP68373. Positions 1-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiCOG5023.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP68373.
KOiK07374.
OMAiCDSKREC.
OrthoDBiEOG7TBC1W.
PhylomeDBiP68373.
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.

P68373-1 [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 ISQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLTVAE 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
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGADSA EGDDEGEEY
Length:449
Mass (Da):49,909
Last modified:August 13, 1987 - v1
Checksum:i0DA9F082D9DC8549
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1671L → P in BAB28608 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13441 mRNA. Translation: AAA40503.1.
BC004745 mRNA. Translation: AAH04745.1.
BC022182 mRNA. Translation: AAH22182.1.
BC026753 mRNA. Translation: AAH26753.1.
AK013029 mRNA. Translation: BAB28608.1.
CCDSiCCDS37198.1.
PIRiI77428.
PH0108.
RefSeqiNP_033474.1. NM_009448.4.
UniGeneiMm.88212.

Genome annotation databases

EnsembliENSMUST00000058914; ENSMUSP00000051033; ENSMUSG00000043091.
GeneIDi22146.
KEGGimmu:22146.
UCSCiuc007xom.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13441 mRNA. Translation: AAA40503.1.
BC004745 mRNA. Translation: AAH04745.1.
BC022182 mRNA. Translation: AAH22182.1.
BC026753 mRNA. Translation: AAH26753.1.
AK013029 mRNA. Translation: BAB28608.1.
CCDSiCCDS37198.1.
PIRiI77428.
PH0108.
RefSeqiNP_033474.1. NM_009448.4.
UniGeneiMm.88212.

3D structure databases

ProteinModelPortaliP68373.
SMRiP68373. Positions 1-439.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204376. 3 interactions.
IntActiP68373. 9 interactions.
MINTiMINT-4137025.

PTM databases

PhosphoSiteiP68373.

2D gel databases

REPRODUCTION-2DPAGEP68373.
SWISS-2DPAGEP99040.

Proteomic databases

MaxQBiP68373.
PaxDbiP68373.
PRIDEiP68373.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000058914; ENSMUSP00000051033; ENSMUSG00000043091.
GeneIDi22146.
KEGGimmu:22146.
UCSCiuc007xom.1. mouse.

Organism-specific databases

CTDi84790.
MGIiMGI:1095409. Tuba1c.

Phylogenomic databases

eggNOGiCOG5023.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP68373.
KOiK07374.
OMAiCDSKREC.
OrthoDBiEOG7TBC1W.
PhylomeDBiP68373.
TreeFamiTF300314.

Enzyme and pathway databases

ReactomeiREACT_196550. MHC class II antigen presentation.
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.
REACT_245663. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_246290. Recruitment of NuMA to mitotic centrosomes.
REACT_247933. Post-chaperonin tubulin folding pathway.
REACT_256756. Mitotic Prometaphase.
REACT_257923. Recycling pathway of L1.
REACT_258053. Formation of tubulin folding intermediates by CCT/TriC.
REACT_269412. Hedgehog 'off' state.

Miscellaneous databases

NextBioi302054.
PROiP68373.
SOURCEiSearch...

Gene expression databases

BgeeiP68373.
CleanExiMM_TUBA1C.
ExpressionAtlasiP68373. baseline and differential.
GenevestigatoriP68373.

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. "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 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: FVB/N.
    Tissue: Liver and Mammary tumor.
  3. "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 106-449.
    Strain: C57BL/6J.
    Tissue: Embryo.
  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; 374-390; 395-401 AND 403-430, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  5. Cited for: POLYGLUTAMYLATION.
  6. Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  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 nameiTBA1C_MOUSE
AccessioniPrimary (citable) accession number: P68373
Secondary accession number(s): P05216, Q9CSE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: March 4, 2015
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

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 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.