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P02550

- TBA1A_PIG

UniProt

P02550 - TBA1A_PIG

Protein

Tubulin alpha-1A chain

Gene

TUBA1A

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    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

    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: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. microtubule Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 451451Tubulin alpha-1A chainPRO_0000048131Add
    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.
    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, Nitration, Phosphoprotein

    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.

    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:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.

    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

    MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN    50
    TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA 100
    NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFSVFHS FGGGTGSGFT 150
    SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC 200
    AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV 250
    DLTEFQTNLV PYPRAHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 300
    QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG 350
    FKVGINYEPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA 400
    KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE 450
    Y 451
    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

    PIRi A93874. UBPGA.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FFX X-ray 3.95 A/C 1-451 [» ]
    1IA0 electron microscopy 15.00 A 1-451 [» ]
    1TUB X-ray 3.70 A 1-440 [» ]
    2HXF electron microscopy 10.00 A 1-451 [» ]
    2HXH electron microscopy 11.00 A 1-451 [» ]
    2P4N electron microscopy 9.00 A 1-451 [» ]
    3J6E electron microscopy 4.70 A/C/E/G/I/K/M/O/Q 1-439 [» ]
    3J6F electron microscopy 4.90 A/C/E/G/I/K/M/O/Q 1-439 [» ]
    3J6G electron microscopy 5.50 A/C/E/G/I/K/M/O/Q 1-439 [» ]
    4ABO electron microscopy 8.60 B/D/F/H 1-451 [» ]
    ProteinModelPortali P02550.
    SMRi P02550. Positions 1-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P02550. 3 interactions.
    MINTi MINT-6439698.

    Chemistry

    BindingDBi P02550.
    ChEMBLi CHEMBL2111354.

    Proteomic databases

    PaxDbi P02550.
    PRIDEi P02550.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG5023.
    HOGENOMi HOG000165711.
    HOVERGENi HBG000089.

    Miscellaneous databases

    EvolutionaryTracei P02550.

    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

    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: October 1, 2014
    This is version 107 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