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Protein

Tubulin alpha chain

Gene
N/A
Organism
Tetrahymena thermophila
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei449Involved in polymerization1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi142 – 148GTPSequence analysis7

GO - Molecular functioni

GO - Biological processi

Keywordsi

LigandGTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha chain
Alternative name(s):
Alpha-tubulin
Cleaved into the following chain:
OrganismiTetrahymena thermophila
Taxonomic identifieri5911 [NCBI]
Taxonomic lineageiEukaryotaAlveolataCiliophoraIntramacronucleataOligohymenophoreaHymenostomatidaTetrahymeninaTetrahymenidaeTetrahymena

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi40K → R: Produces faster growing cells in medium with paclitaxel, a microtubule-stabilizing drug. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000482311 – 449Tubulin alpha chainAdd BLAST449
ChainiPRO_00004374081 – 448Detyrosinated tubulin alpha chainBy similarityAdd BLAST448

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40N6-acetyllysine2 Publications1

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. 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 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.2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP41351

PTM databases

iPTMnetiP41351

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.

Structurei

3D structure databases

ProteinModelPortaliP41351
SMRiP41351
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1376 Eukaryota
COG5023 LUCA

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P41351-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MREVISIHVG QGGIQVGNAC WELFCLEHGI QPDGQMPSDK TIGGGDDAFN
60 70 80 90 100
TFFSETGAGK HVPRAVFLDL EPTVIDEVRT GTYRQLFHPE QLISGKEDAA
110 120 130 140 150
NNFARGHYTI GKEIVDLCLD RIRKLADNCT GLQGFLVFNS VGGGTGSGLG
160 170 180 190 200
SLLLERLSVD YGKKSKLGFT IYPSPQVSTA VVEPYNSILS THSLLEHTDV
210 220 230 240 250
AVMLDNEAIY DICRRNLDIE RPTYTNLNRL IAQVISSLTA SLRFDGALNV
260 270 280 290 300
DITEFQTNLV PYPRIHFMLS SYAPIISAEK AYHEQLSVAE ITNSAFEPAN
310 320 330 340 350
MMAKCDPRHG KYMACSMMYR GDVVPKDVNA SIATIKTKRT IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VMRAVCMISN STAIAEVFSR LDHKFDLMYA
410 420 430 440
KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGIETA EGEGEEEGY
Length:449
Mass (Da):49,587
Last modified:February 1, 1995 - v1
Checksum:iCE21C107A5DDA0B9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86723 Genomic DNA Translation: AAA21350.1

Similar proteinsi

Entry informationi

Entry nameiTBA_TETTH
AccessioniPrimary (citable) accession number: P41351
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 28, 2018
This is version 91 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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