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-1B chain

Gene
N/A
Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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 polymerizationBy similarity

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

Enzyme and pathway databases

ReactomeiREACT_284336. Translocation of GLUT4 to the plasma membrane.
REACT_288507. Assembly of the primary cilium.
REACT_290141. Resolution of Sister Chromatid Cohesion.
REACT_291730. Separation of Sister Chromatids.
REACT_298191. Gap junction assembly.
REACT_302969. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_306084. Mitotic Prometaphase.
REACT_311810. Hedgehog 'on' state.
REACT_315489. Recruitment of NuMA to mitotic centrosomes.
REACT_319227. MHC class II antigen presentation.
REACT_325957. Hedgehog 'off' state.
REACT_332298. Formation of tubulin folding intermediates by CCT/TriC.
REACT_343758. Recycling pathway of L1.
REACT_345117. Kinesins.
REACT_358501. Intraflagellar transport.
REACT_360529. RHO GTPases activate IQGAPs.
REACT_362588. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-1B chain
Alternative name(s):
Alpha-tubulin ubiquitous
Tubulin K-alpha-1
Tubulin alpha-ubiquitous chain
OrganismiBos taurus (Bovine)Curated
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 5

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-1B chainPRO_0000048114Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481PhosphoserineBy similarity
Modified residuei83 – 831Nitrated tyrosineBy similarity
Modified residuei232 – 2321PhosphoserineBy similarity
Modified residuei282 – 2821Nitrated tyrosineBy similarity
Cross-linki326 – 326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei339 – 3391Omega-N-methylarginineBy similarity
Cross-linki370 – 370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By 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, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP81947.
PRIDEiP81947.

Expressioni

Gene expression databases

ExpressionAtlasiP81947. baseline.

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

MINTiMINT-235448.
STRINGi9913.ENSBTAP00000016242.

Structurei

Secondary structure

1
451
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi10 – 2819Combined sources
Beta strandi41 – 433Combined sources
Helixi48 – 514Combined sources
Beta strandi53 – 553Combined sources
Beta strandi61 – 633Combined sources
Beta strandi65 – 728Combined sources
Helixi73 – 808Combined sources
Helixi84 – 863Combined sources
Helixi89 – 913Combined sources
Beta strandi92 – 943Combined sources
Helixi103 – 1075Combined sources
Turni108 – 1103Combined sources
Helixi111 – 12616Combined sources
Beta strandi134 – 14310Combined sources
Helixi144 – 16017Combined sources
Turni161 – 1633Combined sources
Beta strandi164 – 1729Combined sources
Turni175 – 1773Combined sources
Helixi183 – 19412Combined sources
Helixi195 – 1973Combined sources
Beta strandi199 – 2057Combined sources
Helixi206 – 21611Combined sources
Helixi224 – 24320Combined sources
Beta strandi247 – 2493Combined sources
Helixi252 – 2598Combined sources
Beta strandi261 – 2644Combined sources
Beta strandi269 – 2735Combined sources
Beta strandi277 – 2793Combined sources
Helixi288 – 2936Combined sources
Helixi294 – 2963Combined sources
Helixi298 – 3003Combined sources
Beta strandi301 – 3033Combined sources
Helixi307 – 3093Combined sources
Beta strandi312 – 32211Combined sources
Helixi325 – 33612Combined sources
Beta strandi349 – 35810Combined sources
Beta strandi366 – 3683Combined sources
Beta strandi372 – 38110Combined sources
Helixi382 – 3843Combined sources
Helixi385 – 39915Combined sources
Turni400 – 4045Combined sources
Helixi405 – 4095Combined sources
Turni410 – 4123Combined sources
Helixi415 – 43622Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DCOelectron microscopy1.90A1-451[»]
3EDLelectron microscopy28.00A/F1-451[»]
3IZ0electron microscopy8.60A1-451[»]
3J1Telectron microscopy9.70B1-451[»]
3J1Uelectron microscopy9.70B1-451[»]
3J2Uelectron microscopy10.80A/C1-451[»]
4I4TX-ray1.80A/C1-450[»]
4I50X-ray2.30A/C1-451[»]
4I55X-ray2.20A/C1-450[»]
4IHJX-ray2.00A/C1-450[»]
4IIJX-ray2.60A/C1-451[»]
4O2AX-ray2.50A/C1-451[»]
4O2BX-ray2.30A/C1-451[»]
4O4HX-ray2.10A/C1-451[»]
4O4IX-ray2.40A/C1-451[»]
4O4JX-ray2.20A/C1-451[»]
4O4LX-ray2.20A/C1-451[»]
4TUYX-ray2.10A/C1-451[»]
4TV8X-ray2.10A/C1-451[»]
4TV9X-ray2.00A/C1-451[»]
4UXOelectron microscopy6.30A1-451[»]
4UXPelectron microscopy6.30A1-451[»]
4UXRelectron microscopy7.00A1-451[»]
4UXSelectron microscopy7.00A1-451[»]
4UXTelectron microscopy7.40A1-451[»]
4UXYelectron microscopy6.50A1-451[»]
4UY0electron microscopy7.70A1-451[»]
4WBNX-ray2.30A/C1-451[»]
4YJ2X-ray2.60A/C1-451[»]
4YJ3X-ray3.75A/C1-451[»]
ProteinModelPortaliP81947.
SMRiP81947. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81947.

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP81947.
KOiK07374.
OMAiKAHHETI.
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.

P81947-1 [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 GLQGFLVFHS FGGGTGSGFT
160 170 180 190 200
SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440 450
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE

Y
Length:451
Mass (Da):50,152
Last modified:February 10, 2009 - v2
Checksum:i94355B4EC2086429
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC146060 mRNA. Translation: AAI46061.1.
RefSeqiNP_001108328.1. NM_001114856.1.
UniGeneiBt.106995.
Bt.109492.

Genome annotation databases

EnsembliENSBTAT00000016242; ENSBTAP00000016242; ENSBTAG00000012244.
GeneIDi539882.
KEGGibta:539882.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC146060 mRNA. Translation: AAI46061.1.
RefSeqiNP_001108328.1. NM_001114856.1.
UniGeneiBt.106995.
Bt.109492.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DCOelectron microscopy1.90A1-451[»]
3EDLelectron microscopy28.00A/F1-451[»]
3IZ0electron microscopy8.60A1-451[»]
3J1Telectron microscopy9.70B1-451[»]
3J1Uelectron microscopy9.70B1-451[»]
3J2Uelectron microscopy10.80A/C1-451[»]
4I4TX-ray1.80A/C1-450[»]
4I50X-ray2.30A/C1-451[»]
4I55X-ray2.20A/C1-450[»]
4IHJX-ray2.00A/C1-450[»]
4IIJX-ray2.60A/C1-451[»]
4O2AX-ray2.50A/C1-451[»]
4O2BX-ray2.30A/C1-451[»]
4O4HX-ray2.10A/C1-451[»]
4O4IX-ray2.40A/C1-451[»]
4O4JX-ray2.20A/C1-451[»]
4O4LX-ray2.20A/C1-451[»]
4TUYX-ray2.10A/C1-451[»]
4TV8X-ray2.10A/C1-451[»]
4TV9X-ray2.00A/C1-451[»]
4UXOelectron microscopy6.30A1-451[»]
4UXPelectron microscopy6.30A1-451[»]
4UXRelectron microscopy7.00A1-451[»]
4UXSelectron microscopy7.00A1-451[»]
4UXTelectron microscopy7.40A1-451[»]
4UXYelectron microscopy6.50A1-451[»]
4UY0electron microscopy7.70A1-451[»]
4WBNX-ray2.30A/C1-451[»]
4YJ2X-ray2.60A/C1-451[»]
4YJ3X-ray3.75A/C1-451[»]
ProteinModelPortaliP81947.
SMRiP81947. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-235448.
STRINGi9913.ENSBTAP00000016242.

Proteomic databases

PaxDbiP81947.
PRIDEiP81947.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000016242; ENSBTAP00000016242; ENSBTAG00000012244.
GeneIDi539882.
KEGGibta:539882.

Organism-specific databases

CTDi10376.

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP81947.
KOiK07374.
OMAiKAHHETI.
OrthoDBiEOG7TBC1W.
TreeFamiTF300314.

Enzyme and pathway databases

ReactomeiREACT_284336. Translocation of GLUT4 to the plasma membrane.
REACT_288507. Assembly of the primary cilium.
REACT_290141. Resolution of Sister Chromatid Cohesion.
REACT_291730. Separation of Sister Chromatids.
REACT_298191. Gap junction assembly.
REACT_302969. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_306084. Mitotic Prometaphase.
REACT_311810. Hedgehog 'on' state.
REACT_315489. Recruitment of NuMA to mitotic centrosomes.
REACT_319227. MHC class II antigen presentation.
REACT_325957. Hedgehog 'off' state.
REACT_332298. Formation of tubulin folding intermediates by CCT/TriC.
REACT_343758. Recycling pathway of L1.
REACT_345117. Kinesins.
REACT_358501. Intraflagellar transport.
REACT_360529. RHO GTPases activate IQGAPs.
REACT_362588. RHO GTPases Activate Formins.

Miscellaneous databases

EvolutionaryTraceiP81947.
NextBioi20878279.

Gene expression databases

ExpressionAtlasiP81947. baseline.

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

« Hide 'large scale' publications
  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Uterus.
  2. "Differential assembly kinetics of alpha-tubulin isoforms in the presence of paclitaxel."
    Banerjee A., Kasmala L.T.
    Biochem. Biophys. Res. Commun. 245:349-351(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 430-451.
    Tissue: Brain cortex.

Entry informationi

Entry nameiTBA1B_BOVIN
AccessioniPrimary (citable) accession number: P81947
Secondary accession number(s): A6H700
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: February 10, 2009
Last modified: July 22, 2015
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.