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Q2HJ86

- TBA1D_BOVIN

UniProt

Q2HJ86 - TBA1D_BOVIN

Protein

Tubulin alpha-1D chain

Gene

TUBA1D

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (21 Mar 2006)
      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 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei452 – 4521Involved in polymerizationBy similarity

    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-1D chain
    Gene namesi
    Name:TUBA1D
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 2

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity

    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 – 452452Tubulin alpha-1D chainPRO_0000288849Add
    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.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 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

    PaxDbiQ2HJ86.
    PRIDEiQ2HJ86.

    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

    STRINGi9913.ENSBTAP00000038183.

    Structurei

    Secondary structure

    1
    452
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 94
    Helixi20 – 278
    Turni50 – 523
    Beta strandi63 – 686
    Beta strandi70 – 723
    Helixi74 – 785
    Turni84 – 863
    Helixi89 – 913
    Helixi115 – 12511
    Beta strandi136 – 1405
    Helixi150 – 16011
    Beta strandi167 – 1726
    Turni175 – 1784
    Helixi183 – 19311
    Helixi194 – 1974
    Beta strandi199 – 2057
    Helixi206 – 21510
    Helixi224 – 2307
    Helixi234 – 24411
    Helixi252 – 2598
    Beta strandi261 – 2644
    Helixi288 – 2936
    Helixi298 – 3003
    Beta strandi302 – 3054
    Helixi325 – 33713
    Helixi383 – 3853
    Helixi386 – 39914
    Turni400 – 4045
    Helixi405 – 4073
    Helixi418 – 43417

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JFFelectron microscopy3.50A1-452[»]
    1SA0X-ray3.58A/C1-452[»]
    1SA1X-ray4.20A/C1-452[»]
    1TVKX-ray2.89A1-440[»]
    1Z2BX-ray4.10A/C1-451[»]
    2WBEelectron microscopy9.40A1-452[»]
    2XRPelectron microscopy8.20B/D/F/H1-449[»]
    3EDLelectron microscopy28.00F1-452[»]
    3IZ0electron microscopy8.60A1-452[»]
    4AQVelectron microscopy9.70A1-452[»]
    4AQWelectron microscopy9.50A1-452[»]
    4ATUelectron microscopy8.30B/D/F/H1-452[»]
    4ATXelectron microscopy8.20B1-452[»]
    4CK5electron microscopy10.00A1-452[»]
    4CK6electron microscopy9.20A1-452[»]
    4CK7electron microscopy9.20A1-452[»]
    ProteinModelPortaliQ2HJ86.
    SMRiQ2HJ86. Positions 1-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ2HJ86.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    eggNOGiCOG5023.
    GeneTreeiENSGT00750000117421.
    HOGENOMiHOG000165711.
    HOVERGENiHBG000089.
    InParanoidiQ2HJ86.
    KOiK07374.
    OMAiSAAKATH.
    OrthoDBiEOG7TBC1W.
    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.

    Q2HJ86-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRECISVHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN    50
    TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA 100
    NNYARGHYTI GKELIDLVLD RIRKLADQCT GLQGFLIFHS FGGGTGSGFT 150
    SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC 200
    AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV 250
    DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 300
    QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG 350
    FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA 400
    KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGMDSV EGEGEEEEGD 450
    EY 452
    Length:452
    Mass (Da):50,283
    Last modified:March 21, 2006 - v1
    Checksum:iBF41F4296CAC7A56
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC113253 mRNA. Translation: AAI13254.1.
    RefSeqiNP_001039875.1. NM_001046410.1.
    UniGeneiBt.55718.

    Genome annotation databases

    EnsembliENSBTAT00000038369; ENSBTAP00000038183; ENSBTAG00000030973.
    GeneIDi535605.
    KEGGibta:535605.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC113253 mRNA. Translation: AAI13254.1 .
    RefSeqi NP_001039875.1. NM_001046410.1.
    UniGenei Bt.55718.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JFF electron microscopy 3.50 A 1-452 [» ]
    1SA0 X-ray 3.58 A/C 1-452 [» ]
    1SA1 X-ray 4.20 A/C 1-452 [» ]
    1TVK X-ray 2.89 A 1-440 [» ]
    1Z2B X-ray 4.10 A/C 1-451 [» ]
    2WBE electron microscopy 9.40 A 1-452 [» ]
    2XRP electron microscopy 8.20 B/D/F/H 1-449 [» ]
    3EDL electron microscopy 28.00 F 1-452 [» ]
    3IZ0 electron microscopy 8.60 A 1-452 [» ]
    4AQV electron microscopy 9.70 A 1-452 [» ]
    4AQW electron microscopy 9.50 A 1-452 [» ]
    4ATU electron microscopy 8.30 B/D/F/H 1-452 [» ]
    4ATX electron microscopy 8.20 B 1-452 [» ]
    4CK5 electron microscopy 10.00 A 1-452 [» ]
    4CK6 electron microscopy 9.20 A 1-452 [» ]
    4CK7 electron microscopy 9.20 A 1-452 [» ]
    ProteinModelPortali Q2HJ86.
    SMRi Q2HJ86. Positions 1-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000038183.

    Proteomic databases

    PaxDbi Q2HJ86.
    PRIDEi Q2HJ86.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000038369 ; ENSBTAP00000038183 ; ENSBTAG00000030973 .
    GeneIDi 535605.
    KEGGi bta:535605.

    Organism-specific databases

    CTDi 535605.

    Phylogenomic databases

    eggNOGi COG5023.
    GeneTreei ENSGT00750000117421.
    HOGENOMi HOG000165711.
    HOVERGENi HBG000089.
    InParanoidi Q2HJ86.
    KOi K07374.
    OMAi SAAKATH.
    OrthoDBi EOG7TBC1W.
    TreeFami TF300314.

    Miscellaneous databases

    EvolutionaryTracei Q2HJ86.
    NextBioi 20876788.

    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. NIH - Mammalian Gene Collection (MGC) project
      Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Uterus.

    Entry informationi

    Entry nameiTBA1D_BOVIN
    AccessioniPrimary (citable) accession number: Q2HJ86
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: March 21, 2006
    Last modified: October 1, 2014
    This is version 72 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

    3D-structure, Complete proteome, 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