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-1D chain

Gene

TUBA1D

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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).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
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_203101. Mitotic Prometaphase.
REACT_204570. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_207055. Gap junction assembly.
REACT_209545. Resolution of Sister Chromatid Cohesion.
REACT_211133. MHC class II antigen presentation.
REACT_212887. Separation of Sister Chromatids.
REACT_214148. Formation of tubulin folding intermediates by CCT/TriC.
REACT_215331. Recruitment of NuMA to mitotic centrosomes.
REACT_217718. Translocation of GLUT4 to the plasma membrane.
REACT_222513. Kinesins.
REACT_223239. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_223433. Recycling pathway of L1.
REACT_270061. Hedgehog 'off' state.

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 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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiQ2HJ86.
KOiK07374.
OMAiNEITTAC.
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

        10         20         30         40         50
MRECISVHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN
60 70 80 90 100
TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTI GKELIDLVLD RIRKLADQCT GLQGFLIFHS 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 PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440 450
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGMDSV EGEGEEEEGD

EY
Length:452
Mass (Da):50,283
Last modified:March 21, 2006 - v1
Checksum:iBF41F4296CAC7A56
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
BC113253 mRNA. Translation: AAI13254.1.
RefSeqiNP_001039875.1. NM_001046410.1.
UniGeneiBt.55718.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000038183.

Proteomic databases

PaxDbiQ2HJ86.
PRIDEiQ2HJ86.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi535605.

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiQ2HJ86.
KOiK07374.
OMAiNEITTAC.
OrthoDBiEOG7TBC1W.
TreeFamiTF300314.

Enzyme and pathway databases

ReactomeiREACT_203101. Mitotic Prometaphase.
REACT_204570. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_207055. Gap junction assembly.
REACT_209545. Resolution of Sister Chromatid Cohesion.
REACT_211133. MHC class II antigen presentation.
REACT_212887. Separation of Sister Chromatids.
REACT_214148. Formation of tubulin folding intermediates by CCT/TriC.
REACT_215331. Recruitment of NuMA to mitotic centrosomes.
REACT_217718. Translocation of GLUT4 to the plasma membrane.
REACT_222513. Kinesins.
REACT_223239. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_223433. Recycling pathway of L1.
REACT_270061. Hedgehog 'off' state.

Miscellaneous databases

EvolutionaryTraceiQ2HJ86.
NextBioi20876788.

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. 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: January 7, 2015
This is version 75 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

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.