Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tubulin alpha-1A chain

Gene

TUBA1A

Organism
Sus scrofa (Pig)
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
Sitei451 – 4511Involved in polymerization

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

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-1A chain
Alternative name(s):
Alpha-tubulin 1
Tubulin alpha-1 chain
Gene namesi
Name:TUBA1A
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227 Componenti: Unplaced

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 – 451451Tubulin alpha-1A chainPRO_0000048131Add
BLAST

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.
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 (By similarity).By similarity
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

Proteomic databases

PaxDbiP02550.
PRIDEiP02550.

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

IntActiP02550. 3 interactions.
MINTiMINT-6439698.
STRINGi9823.ENSSSCP00000000199.

Structurei

Secondary structure

1
451
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106
Helixi11 – 188
Turni19 – 257
Beta strandi26 – 305
Beta strandi39 – 413
Beta strandi66 – 683
Helixi74 – 763
Beta strandi77 – 815
Helixi104 – 1074
Turni109 – 1179
Helixi118 – 1236
Turni124 – 1274
Beta strandi128 – 1303
Beta strandi135 – 1384
Turni144 – 1485
Helixi150 – 16011
Beta strandi180 – 1823
Helixi183 – 1908
Turni206 – 2083
Helixi209 – 2124
Turni213 – 2175
Helixi224 – 23613
Turni237 – 2393
Helixi240 – 2423
Beta strandi246 – 2483
Helixi253 – 2553
Turni257 – 2593
Beta strandi262 – 2643
Beta strandi269 – 2724
Beta strandi278 – 2803
Turni288 – 2903
Helixi294 – 2963
Helixi298 – 3003
Beta strandi301 – 3033
Helixi307 – 3093
Beta strandi318 – 3225
Helixi325 – 33612
Beta strandi345 – 3473
Turni364 – 3674
Beta strandi372 – 3798
Helixi384 – 3874
Helixi390 – 3923
Helixi393 – 3964
Helixi403 – 4064
Turni407 – 4115
Beta strandi415 – 4195
Turni420 – 4223
Turni424 – 4263
Helixi427 – 4315
Turni432 – 4365

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFXX-ray3.95A/C1-451[»]
1IA0electron microscopy15.00A1-451[»]
1TUBX-ray3.70A1-440[»]
2HXFelectron microscopy10.00A1-451[»]
2HXHelectron microscopy11.00A1-451[»]
2P4Nelectron microscopy9.00A1-451[»]
3J6Eelectron microscopy4.70A/C/E/G/I/K/M/O/Q1-439[»]
3J6Felectron microscopy4.90A/C/E/G/I/K/M/O/Q1-439[»]
3J6Gelectron microscopy5.50A/C/E/G/I/K/M/O/Q1-439[»]
3J6Helectron microscopy8.10A2-437[»]
3J6Pelectron microscopy8.20A1-451[»]
3J7Ielectron microscopy8.90A1-451[»]
4ABOelectron microscopy8.60B/D/F/H1-451[»]
ProteinModelPortaliP02550.
SMRiP02550. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02550.

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiCOG5023.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP02550.

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.

P02550-1 [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 GLQGFSVFHS 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 PYPRAHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG
360 370 380 390 400
FKVGINYEPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440 450
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE

Y
Length:451
Mass (Da):50,068
Last modified:July 21, 1986 - v1
Checksum:i48D7112D182B33CA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti265 – 2651A → G.
Natural varianti265 – 2651A → I.
Natural varianti266 – 2661H → I.
Natural varianti271 – 2733TYA → RFB.

Sequence databases

PIRiA93874. UBPGA.

Cross-referencesi

Sequence databases

PIRiA93874. UBPGA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFXX-ray3.95A/C1-451[»]
1IA0electron microscopy15.00A1-451[»]
1TUBX-ray3.70A1-440[»]
2HXFelectron microscopy10.00A1-451[»]
2HXHelectron microscopy11.00A1-451[»]
2P4Nelectron microscopy9.00A1-451[»]
3J6Eelectron microscopy4.70A/C/E/G/I/K/M/O/Q1-439[»]
3J6Felectron microscopy4.90A/C/E/G/I/K/M/O/Q1-439[»]
3J6Gelectron microscopy5.50A/C/E/G/I/K/M/O/Q1-439[»]
3J6Helectron microscopy8.10A2-437[»]
3J6Pelectron microscopy8.20A1-451[»]
3J7Ielectron microscopy8.90A1-451[»]
4ABOelectron microscopy8.60B/D/F/H1-451[»]
ProteinModelPortaliP02550.
SMRiP02550. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02550. 3 interactions.
MINTiMINT-6439698.
STRINGi9823.ENSSSCP00000000199.

Chemistry

BindingDBiP02550.
ChEMBLiCHEMBL2111354.

Proteomic databases

PaxDbiP02550.
PRIDEiP02550.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG5023.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP02550.

Miscellaneous databases

EvolutionaryTraceiP02550.

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

  1. "Complete amino acid sequence of alpha-tubulin from porcine brain."
    Ponstingl H., Krauhs E., Little M., Kempf T.
    Proc. Natl. Acad. Sci. U.S.A. 78:2757-2761(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Brain.
  2. "Localization of the ATP binding site on alpha-tubulin."
    Zabrecky J.R., Cole R.D.
    Arch. Biochem. Biophys. 225:475-481(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: BINDING SITE.

Entry informationi

Entry nameiTBA1A_PIG
AccessioniPrimary (citable) accession number: P02550
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 24, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The highly acidic C-terminal region may bind cations such as calcium.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.