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Protein

Tubulin beta-3 chain

Gene

Tubb3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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. TUBB3 plays a critical role in proper axon guidance and mantainance (By similarity).By similarity

Regions

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

GO - Molecular functioni

  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB-KW
  • peptide binding Source: RGD
  • structural constituent of cytoskeleton Source: RGD

GO - Biological processi

  • axon guidance Source: UniProtKB
  • microtubule-based process Source: InterPro
  • mitotic nuclear division Source: RGD
  • neuron differentiation Source: RGD
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-5610787. Hedgehog 'off' state.
R-RNO-5620924. Intraflagellar transport.
R-RNO-5632684. Hedgehog 'on' state.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-3 chain
Alternative name(s):
Neuron-specific class III beta-tubulin
Gene namesi
Name:Tubb3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi628595. Tubb3.

Subcellular locationi

GO - Cellular componenti

  • axon Source: MGI
  • cell periphery Source: Ensembl
  • cytoplasm Source: UniProtKB-KW
  • dendrite Source: ParkinsonsUK-UCL
  • extracellular exosome Source: Ensembl
  • microtubule Source: UniProtKB-KW
  • neuronal cell body Source: Ensembl
  • nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Tubulin beta-3 chainPRO_0000233027Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721Phosphoserine; by CDK1By similarity
Modified residuei438 – 43815-glutamyl polyglutamateBy similarity
Modified residuei444 – 4441PhosphoserineBy similarity

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

Isopeptide bond, Phosphoprotein

Proteomic databases

PaxDbiQ4QRB4.
PRIDEiQ4QRB4.

PTM databases

iPTMnetiQ4QRB4.
PhosphoSiteiQ4QRB4.

Expressioni

Gene expression databases

BgeeiENSRNOG00000017209.
GenevisibleiQ4QRB4. RN.

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

BioGridi251505. 2 interactions.
IntActiQ4QRB4. 6 interactions.
MINTiMINT-2982718.
STRINGi10116.ENSRNOP00000023452.

Structurei

3D structure databases

ProteinModelPortaliQ4QRB4.
SMRiQ4QRB4. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The highly acidic C-terminal region may bind cations such as calcium.

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ4QRB4.
KOiK07375.
OMAiNEASCEH.
OrthoDBiEOG091G06U2.
PhylomeDBiQ4QRB4.
TreeFamiTF300298.

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.

Q4QRB4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY
60 70 80 90 100
YNEASSHKYV PRAILVDLEP GTMDSVRSGA FGHLFRPDNF IFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKECENCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKVREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSIH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLATP TYGDLNHLVS ATMSGVTTSL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALTVPELT QQMFDAKNMM
310 320 330 340 350
AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK
360 370 380 390 400
VAVCDIPPRG LKMSSTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440 450
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEGEMYEDD DEESEAQGPK
Length:450
Mass (Da):50,419
Last modified:July 19, 2005 - v1
Checksum:i4B9D9B7DBA102949
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti249 – 2491D → H in AAM28438 (PubMed:12234689).Curated
Sequence conflicti390 – 3901Missing in AAM28438 (PubMed:12234689).Curated
Sequence conflicti401 – 4011E → Q in AAM28438 (PubMed:12234689).Curated
Sequence conflicti446 – 4461A → R in AAM28438 (PubMed:12234689).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF459021 mRNA. Translation: AAM28438.1.
BC097281 mRNA. Translation: AAH97281.1.
RefSeqiNP_640347.2. NM_139254.2.
UniGeneiRn.43958.

Genome annotation databases

EnsembliENSRNOT00000023452; ENSRNOP00000023452; ENSRNOG00000017209.
GeneIDi246118.
KEGGirno:246118.
UCSCiRGD:628595. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF459021 mRNA. Translation: AAM28438.1.
BC097281 mRNA. Translation: AAH97281.1.
RefSeqiNP_640347.2. NM_139254.2.
UniGeneiRn.43958.

3D structure databases

ProteinModelPortaliQ4QRB4.
SMRiQ4QRB4. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251505. 2 interactions.
IntActiQ4QRB4. 6 interactions.
MINTiMINT-2982718.
STRINGi10116.ENSRNOP00000023452.

PTM databases

iPTMnetiQ4QRB4.
PhosphoSiteiQ4QRB4.

Proteomic databases

PaxDbiQ4QRB4.
PRIDEiQ4QRB4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023452; ENSRNOP00000023452; ENSRNOG00000017209.
GeneIDi246118.
KEGGirno:246118.
UCSCiRGD:628595. rat.

Organism-specific databases

CTDi10381.
RGDi628595. Tubb3.

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ4QRB4.
KOiK07375.
OMAiNEASCEH.
OrthoDBiEOG091G06U2.
PhylomeDBiQ4QRB4.
TreeFamiTF300298.

Enzyme and pathway databases

ReactomeiR-RNO-5610787. Hedgehog 'off' state.
R-RNO-5620924. Intraflagellar transport.
R-RNO-5632684. Hedgehog 'on' state.

Miscellaneous databases

PROiQ4QRB4.

Gene expression databases

BgeeiENSRNOG00000017209.
GenevisibleiQ4QRB4. RN.

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 nameiTBB3_RAT
AccessioniPrimary (citable) accession number: Q4QRB4
Secondary accession number(s): Q8K5B6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: July 19, 2005
Last modified: September 7, 2016
This is version 100 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.