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Q2HJ86

- TBA1D_BOVIN

UniProt

Q2HJ86 - TBA1D_BOVIN

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Protein
Tubulin alpha-1D chain
Gene
TUBA1D
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 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 By similarity.

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1487GTP Reviewed prediction

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. GTPase activity Source: InterPro
  3. structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  1. microtubule-based process Source: InterPro
  2. protein polymerization Source: InterPro
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 452452Tubulin alpha-1D chain
PRO_0000288849Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481Phosphoserine By similarity
Modified residuei83 – 831Nitrated tyrosine By similarity
Modified residuei282 – 2821Nitrated tyrosine By similarity
Modified residuei432 – 4321Phosphotyrosine By similarity
Modified residuei439 – 4391Phosphoserine By 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.
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.

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

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.

Miscellaneous databases

EvolutionaryTraceiQ2HJ86.

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.

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

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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: July 9, 2014
This is version 71 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

Similar proteinsi