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Protein

Tubulin beta chain

Gene
N/A
Organism
Sus scrofa (Pig)
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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi140 – 1467GTPSequence 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

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta chain
Alternative name(s):
Beta-tubulin
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

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 – 445445Tubulin beta chainPRO_0000048261Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721Phosphoserine; by CDK1By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP02554.
PRIDEiP02554.

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

IntActiP02554. 2 interactions.
STRINGi9823.ENSSSCP00000001076.

Structurei

Secondary structure

1
445
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64
Helixi10 – 2011
Turni21 – 255
Helixi26 – 283
Beta strandi32 – 343
Beta strandi39 – 424
Helixi47 – 493
Beta strandi53 – 553
Turni70 – 723
Helixi73 – 775
Turni81 – 844
Helixi101 – 1044
Turni105 – 1128
Helixi116 – 1249
Beta strandi126 – 1283
Beta strandi130 – 1345
Beta strandi136 – 1427
Turni143 – 1453
Helixi146 – 15510
Turni156 – 1583
Beta strandi160 – 1645
Beta strandi167 – 1704
Beta strandi177 – 1804
Helixi181 – 19212
Turni193 – 1953
Helixi206 – 2127
Helixi222 – 23615
Helixi238 – 2403
Helixi250 – 2578
Turni276 – 2783
Helixi289 – 2935
Beta strandi295 – 3039
Helixi305 – 3073
Beta strandi316 – 3205
Helixi323 – 33513
Helixi338 – 3403
Beta strandi343 – 3453
Beta strandi352 – 3565
Beta strandi364 – 3685
Turni372 – 3765
Helixi377 – 38913
Turni390 – 3945
Helixi395 – 3995
Helixi407 – 42317

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFXX-ray3.95B/D1-445[»]
1IA0electron microscopy15.00B1-445[»]
1JFFX-ray3.50B1-445[»]
1TUBX-ray3.70B1-427[»]
2HXFelectron microscopy10.00B1-435[»]
2HXHelectron microscopy11.00B1-435[»]
3J6Eelectron microscopy4.70B/D/F/H/J/L/N/P/R1-427[»]
3J6Felectron microscopy4.90B/D/F/H/J/L/N/P/R1-427[»]
3J6Gelectron microscopy5.50B/D/F/H/J/L/N/P/R1-427[»]
3J7Ielectron microscopy8.90B1-445[»]
4ABOelectron microscopy8.60A/C/E/G1-445[»]
ProteinModelPortaliP02554.
SMRiP02554. Positions 1-427.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02554.

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiCOG5023.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR013838. Beta-tubulin_BS.
IPR002453. Beta_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]
PRINTSiPR01163. BETATUBULIN.
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.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02554-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY
60 70 80 90 100
YNEAAGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
310 320 330 340 350
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEG EEDEA
Length:445
Mass (Da):49,861
Last modified:July 21, 1986 - v1
Checksum:iEF71423B12C5E1B2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371H → V in 2nd form.
Natural varianti48 – 481N → S in 2nd form.
Natural varianti55 – 573AGN → SSH in 2nd form.
Natural varianti275 – 2751S → A in 2nd form.

Sequence databases

PIRiA02973. UBPGB.

Cross-referencesi

Sequence databases

PIRiA02973. UBPGB.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFXX-ray3.95B/D1-445[»]
1IA0electron microscopy15.00B1-445[»]
1JFFX-ray3.50B1-445[»]
1TUBX-ray3.70B1-427[»]
2HXFelectron microscopy10.00B1-435[»]
2HXHelectron microscopy11.00B1-435[»]
3J6Eelectron microscopy4.70B/D/F/H/J/L/N/P/R1-427[»]
3J6Felectron microscopy4.90B/D/F/H/J/L/N/P/R1-427[»]
3J6Gelectron microscopy5.50B/D/F/H/J/L/N/P/R1-427[»]
3J7Ielectron microscopy8.90B1-445[»]
4ABOelectron microscopy8.60A/C/E/G1-445[»]
ProteinModelPortaliP02554.
SMRiP02554. Positions 1-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02554. 2 interactions.
STRINGi9823.ENSSSCP00000001076.

Chemistry

ChEMBLiCHEMBL2111354.

Proteomic databases

PaxDbiP02554.
PRIDEiP02554.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG5023.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.

Miscellaneous databases

EvolutionaryTraceiP02554.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR013838. Beta-tubulin_BS.
IPR002453. Beta_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]
PRINTSiPR01163. BETATUBULIN.
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.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: PROTEIN SEQUENCE.
    Tissue: Brain.
  2. "The GTP-binding peptide of beta-tubulin. Localization by direct photoaffinity labeling and comparison with nucleotide-binding proteins."
    Linse K., Mandelkow E.M.
    J. Biol. Chem. 263:15205-15210(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 63-77.
  3. "Localization of the ATP binding site on alpha-tubulin."
    Zabrecky J.R., Cole R.D.
    Arch. Biochem. Biophys. 225:475-481(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: GUANINE NUCLEOTIDE-BINDING SITES.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (3.95 ANGSTROMS).
  5. "Structure of the alpha beta tubulin dimer by electron crystallography."
    Nogales E., Wolf S.G., Downing K.H.
    Nature 391:199-203(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.7 ANGSTROMS) OF 1-427.
  6. "15 A resolution model of the monomeric kinesin motor, KIF1A."
    Kikkawa M., Okada Y., Hirokawa N.
    Cell 100:241-252(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (15.0 ANGSTROMS).
  7. "Refined structure of alpha beta-tubulin at 3.5 A resolution."
    Loewe J., Li H., Downing K.H., Nogales E.
    J. Mol. Biol. 313:1045-1057(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS).

Entry informationi

Entry nameiTBB_PIG
AccessioniPrimary (citable) accession number: P02554
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 4, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The highly acidic C-terminal region may bind cations such as calcium.
Pig brain contains at least two forms of this protein.

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.