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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi140 – 146GTPSequence analysis7

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2788.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000482611 – 445Tubulin beta chainAdd BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40PhosphoserineBy similarity1
Modified residuei58N6-acetyllysine; alternateBy similarity1
Modified residuei58N6-succinyllysine; alternateBy similarity1
Cross-linki58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei172Phosphoserine; by CDK1By similarity1
Modified residuei285PhosphothreonineBy similarity1
Modified residuei290PhosphothreonineBy similarity1
Modified residuei318Omega-N-methylarginineBy similarity1
Cross-linki324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei4385-glutamyl polyglutamateBy similarity1

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglycylated, resulting in 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 polyglycylation is still unclear.By similarity
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (By similarity). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity).By similarity
Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP02554.
PeptideAtlasiP02554.
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. Interacts with NCKAP5L (PubMed:26482847).1 Publication

Protein-protein interaction databases

IntActiP02554. 2 interactors.
STRINGi9823.ENSSSCP00000001076.

Chemistry databases

BindingDBiP02554.

Structurei

Secondary structure

1445
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi10 – 28Combined sources19
Beta strandi34 – 36Combined sources3
Helixi41 – 43Combined sources3
Turni44 – 46Combined sources3
Helixi47 – 49Combined sources3
Beta strandi51 – 54Combined sources4
Turni55 – 57Combined sources3
Beta strandi58 – 61Combined sources4
Beta strandi63 – 70Combined sources8
Helixi71 – 78Combined sources8
Beta strandi79 – 81Combined sources3
Helixi82 – 84Combined sources3
Helixi87 – 89Combined sources3
Beta strandi90 – 92Combined sources3
Helixi101 – 105Combined sources5
Helixi108 – 125Combined sources18
Beta strandi132 – 142Combined sources11
Helixi143 – 158Combined sources16
Beta strandi162 – 170Combined sources9
Turni173 – 175Combined sources3
Helixi181 – 195Combined sources15
Beta strandi197 – 203Combined sources7
Helixi204 – 212Combined sources9
Helixi222 – 241Combined sources20
Beta strandi245 – 247Combined sources3
Helixi250 – 257Combined sources8
Beta strandi265 – 272Combined sources8
Beta strandi276 – 278Combined sources3
Helixi286 – 293Combined sources8
Helixi296 – 298Combined sources3
Beta strandi299 – 301Combined sources3
Helixi305 – 307Combined sources3
Beta strandi310 – 320Combined sources11
Helixi323 – 336Combined sources14
Helixi338 – 340Combined sources3
Beta strandi349 – 355Combined sources7
Beta strandi362 – 371Combined sources10
Helixi372 – 374Combined sources3
Helixi375 – 389Combined sources15
Turni390 – 395Combined sources6
Helixi396 – 399Combined sources4
Turni400 – 402Combined sources3
Helixi405 – 427Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3J6Helectron microscopy8.10B2-427[»]
3J6Pelectron microscopy8.20B1-445[»]
3J7Ielectron microscopy8.90B1-445[»]
3JAKelectron microscopy3.50B/D/F/G/H/I1-445[»]
3JALelectron microscopy3.50B/D/F/G/H/I1-445[»]
3JARelectron microscopy3.50B/D/F/G/H/I1-445[»]
3JASelectron microscopy3.50B/D/F/G/H/I1-445[»]
3JATelectron microscopy3.50B/D/F/G/H/I1-445[»]
3JAWelectron microscopy3.90B/D1-445[»]
4ABOelectron microscopy8.60A/C/E/G1-445[»]
4ZHQX-ray2.55B/D1-445[»]
4ZI7X-ray2.51B/D1-445[»]
4ZOLX-ray2.50B/D1-445[»]
5BMVX-ray2.50B/D1-445[»]
5FNVX-ray2.61B/D1-445[»]
5JQGX-ray2.24B/D1-445[»]
5KMGelectron microscopy3.50B1-431[»]
ProteinModelPortaliP02554.
SMRiP02554.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02554.

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
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)DescriptionActionsGraphical viewLength
Natural varianti37H → V in 2nd form. 1
Natural varianti48N → S in 2nd form. 1
Natural varianti55 – 57AGN → SSH in 2nd form. 3
Natural varianti275S → A in 2nd form. 1

Sequence databases

PIRiA02973. UBPGB.

Cross-referencesi

Sequence databases

PIRiA02973. UBPGB.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3J6Helectron microscopy8.10B2-427[»]
3J6Pelectron microscopy8.20B1-445[»]
3J7Ielectron microscopy8.90B1-445[»]
3JAKelectron microscopy3.50B/D/F/G/H/I1-445[»]
3JALelectron microscopy3.50B/D/F/G/H/I1-445[»]
3JARelectron microscopy3.50B/D/F/G/H/I1-445[»]
3JASelectron microscopy3.50B/D/F/G/H/I1-445[»]
3JATelectron microscopy3.50B/D/F/G/H/I1-445[»]
3JAWelectron microscopy3.90B/D1-445[»]
4ABOelectron microscopy8.60A/C/E/G1-445[»]
4ZHQX-ray2.55B/D1-445[»]
4ZI7X-ray2.51B/D1-445[»]
4ZOLX-ray2.50B/D1-445[»]
5BMVX-ray2.50B/D1-445[»]
5FNVX-ray2.61B/D1-445[»]
5JQGX-ray2.24B/D1-445[»]
5KMGelectron microscopy3.50B1-431[»]
ProteinModelPortaliP02554.
SMRiP02554.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02554. 2 interactors.
STRINGi9823.ENSSSCP00000001076.

Chemistry databases

BindingDBiP02554.
ChEMBLiCHEMBL2788.

Proteomic databases

PaxDbiP02554.
PeptideAtlasiP02554.
PRIDEiP02554.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
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...

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: November 30, 2016
This is version 135 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

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 one 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.