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Protein

Tubulin alpha-1 chain

Gene

nda2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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
Sitei455 – 4551Involved in polymerizationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi146 – 1527GTPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-114608. Platelet degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-1 chain
Gene namesi
Name:nda2
ORF Names:SPBC16A3.15c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC16A3.15c.
PomBaseiSPBC16A3.15c. nda2.

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 – 455455Tubulin alpha-1 chainPRO_0000048225Add
BLAST

Proteomic databases

MaxQBiP04688.
PRIDEiP04688.

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

BioGridi276411. 14 interactions.
DIPiDIP-37976N.
IntActiP04688. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliP04688.
SMRiP04688. Positions 2-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

HOGENOMiHOG000165711.
InParanoidiP04688.
KOiK07374.
OMAiCMLYRGE.
OrthoDBiEOG7PVWZW.
PhylomeDBiP04688.

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.

P04688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREVISVHVG QAGVQIGNAC WELYCLEHGI GPDGFPTENS EVHKNNSYLN
60 70 80 90 100
DGFGTFFSET GQGKFVPRSI YVDLEPNVID QVRTGPYKDL FHPEQMVTGK
110 120 130 140 150
EDASNNYARG HYTVGKEMID SVLERIRRMA DNCSGLQGFL VFHSFGGGTG
160 170 180 190 200
SGLGALLLER LNMEYGKKSN LQFSVYPAPQ VSTSVVEPYN SVLTTHATLD
210 220 230 240 250
NSDCTFMVDN EACYDICRRN LDIERPTYEN LNRLIAQVVS SITASLRFAG
260 270 280 290 300
SLNVDLNEFQ TNLVPYPRIH FPLVTYSPIV SAAKAFHESN SVQEITNQCF
310 320 330 340 350
EPYNQMVKCD PRTGRYMATC LLYRGDVIPR DVQAAVTSIK SRRTIQFVDW
360 370 380 390 400
CPTGFKIGIC YEPPQHVPGS GIAKVNRAVC MLSNTTSIAE AWSRLDHKFD
410 420 430 440 450
LMYSKRAFVH WYVGEGMEEG EFSEAREDLA ALERDYEEVG QDSMDNEMYE

ADEEY
Length:455
Mass (Da):51,152
Last modified:July 15, 1999 - v2
Checksum:i924EAAB0C53CED41
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti155 – 1551A → T in AAA35350 (PubMed:6327053).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02841 Genomic DNA. Translation: AAA35350.1.
CU329671 Genomic DNA. Translation: CAA16866.1.
PIRiA25072.
T39537.
RefSeqiNP_596774.1. NM_001023795.2.

Genome annotation databases

EnsemblFungiiSPBC16A3.15c.1; SPBC16A3.15c.1:pep; SPBC16A3.15c.
GeneIDi2539864.
KEGGispo:SPBC16A3.15c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02841 Genomic DNA. Translation: AAA35350.1.
CU329671 Genomic DNA. Translation: CAA16866.1.
PIRiA25072.
T39537.
RefSeqiNP_596774.1. NM_001023795.2.

3D structure databases

ProteinModelPortaliP04688.
SMRiP04688. Positions 2-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276411. 14 interactions.
DIPiDIP-37976N.
IntActiP04688. 4 interactions.

Proteomic databases

MaxQBiP04688.
PRIDEiP04688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC16A3.15c.1; SPBC16A3.15c.1:pep; SPBC16A3.15c.
GeneIDi2539864.
KEGGispo:SPBC16A3.15c.

Organism-specific databases

EuPathDBiFungiDB:SPBC16A3.15c.
PomBaseiSPBC16A3.15c. nda2.

Phylogenomic databases

HOGENOMiHOG000165711.
InParanoidiP04688.
KOiK07374.
OMAiCMLYRGE.
OrthoDBiEOG7PVWZW.
PhylomeDBiP04688.

Enzyme and pathway databases

ReactomeiR-SPO-114608. Platelet degranulation.

Miscellaneous databases

NextBioi20801010.
PROiP04688.

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. "Identification of the pleiotropic cell division cycle gene NDA2 as one of two different alpha-tubulin genes in Schizosaccharomyces pombe."
    Toda T., Adachi Y., Hiraoka Y., Yanagida M.
    Cell 37:233-242(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiTBA1_SCHPO
AccessioniPrimary (citable) accession number: P04688
Secondary accession number(s): O42920
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: July 15, 1999
Last modified: January 20, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.