Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P81947

- TBA1B_BOVIN

UniProt

P81947 - TBA1B_BOVIN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Tubulin alpha-1B chain

Gene
N/A
Organism
Bos taurus (Bovine)
Status
Reviewed - 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

  1. double-stranded RNA binding Source: Ensembl
  2. GTPase activity Source: InterPro
  3. GTP binding Source: UniProtKB-KW
  4. structural constituent of cytoskeleton Source: Ensembl

GO - Biological processi

  1. cellular response to interleukin-4 Source: Ensembl
  2. microtubule cytoskeleton organization Source: Ensembl
  3. protein polymerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_214148. Formation of tubulin folding intermediates by CCT/TriC.

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: Chromosome 5

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmic microtubule Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
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.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
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.
OMAiCVRARTI.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
BC146060 mRNA. Translation: AAI46061.1 .
RefSeqi NP_001108328.1. NM_001114856.1.
UniGenei Bt.106995.
Bt.109492.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3DCO electron microscopy 1.90 A 1-451 [» ]
3EDL electron microscopy 28.00 A/F 1-451 [» ]
3IZ0 electron microscopy 8.60 A 1-451 [» ]
3J1T electron microscopy 9.70 B 1-451 [» ]
3J1U electron microscopy 9.70 B 1-451 [» ]
3J2U electron microscopy 10.80 A/C 1-451 [» ]
4I4T X-ray 1.80 A/C 1-450 [» ]
4I50 X-ray 2.30 A/C 1-451 [» ]
4I55 X-ray 2.20 A/C 1-450 [» ]
4IHJ X-ray 2.00 A/C 1-450 [» ]
4IIJ X-ray 2.60 A/C 1-451 [» ]
4O2A X-ray 2.50 A/C 1-451 [» ]
4O2B X-ray 2.30 A/C 1-451 [» ]
4O4H X-ray 2.10 A/C 1-451 [» ]
4O4I X-ray 2.40 A/C 1-451 [» ]
4O4J X-ray 2.20 A/C 1-451 [» ]
4O4L X-ray 2.20 A/C 1-451 [» ]
4TUY X-ray 2.10 A/C 1-451 [» ]
4TV8 X-ray 2.10 A/C 1-451 [» ]
4TV9 X-ray 2.00 A/C 1-451 [» ]
ProteinModelPortali P81947.
SMRi P81947. Positions 1-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-235448.

Proteomic databases

PaxDbi P81947.
PRIDEi P81947.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000016242 ; ENSBTAP00000016242 ; ENSBTAG00000012244 .
GeneIDi 539882.
KEGGi bta:539882.

Organism-specific databases

CTDi 10376.

Phylogenomic databases

eggNOGi COG5023.
GeneTreei ENSGT00760000119060.
HOGENOMi HOG000165711.
HOVERGENi HBG000089.
InParanoidi P81947.
KOi K07374.
OMAi CVRARTI.
OrthoDBi EOG7TBC1W.
TreeFami TF300314.

Enzyme and pathway databases

Reactomei REACT_214148. Formation of tubulin folding intermediates by CCT/TriC.

Miscellaneous databases

EvolutionaryTracei P81947.
NextBioi 20878279.

Gene expression databases

ExpressionAtlasi P81947. baseline.

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

« 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: October 29, 2014
This is version 86 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