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Protein

Tubulin beta-2B chain

Gene

Tubb2b

Organism
Rattus norvegicus (Rat)
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 (By similarity). TUBB2B is implicated in neuronal migration.By similarity1 Publication

Regions

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

GO - Molecular functioni

GO - Biological processi

  • microtubule-based process Source: InterPro
  • neuron migration Source: UniProtKB
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-2B chain
Alternative name(s):
T beta-15
Gene namesi
Name:Tubb2b
Synonyms:Tubb2a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi1309427. Tubb2b.

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 – 445445Tubulin beta-2B chainPRO_0000262653Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401PhosphoserineBy similarity
Modified residuei55 – 551PhosphothreonineCombined sources
Modified residuei58 – 581N6-acetyllysine; alternateBy similarity
Modified residuei58 – 581N6-succinyllysine; alternateBy similarity
Cross-linki58 – 58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei172 – 1721Phosphoserine; by CDK1By similarity
Modified residuei285 – 2851PhosphothreonineBy similarity
Modified residuei290 – 2901PhosphothreonineBy similarity
Modified residuei318 – 3181Omega-N-methylarginineBy similarity
Cross-linki324 – 324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei438 – 43815-glutamyl polyglutamateBy 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

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ3KRE8.
PRIDEiQ3KRE8.

PTM databases

iPTMnetiQ3KRE8.
PhosphoSiteiQ3KRE8.

Expressioni

Gene expression databases

BgeeiENSRNOG00000017445.
GenevisibleiQ3KRE8. 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

BioGridi253414. 5 interactions.
IntActiQ3KRE8. 4 interactions.
MINTiMINT-236031.
STRINGi10116.ENSRNOP00000023582.

Structurei

3D structure databases

ProteinModelPortaliQ3KRE8.
SMRiQ3KRE8. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ3KRE8.
KOiK07375.
OMAiFWEVICA.
OrthoDBiEOG091G06U2.
PhylomeDBiQ3KRE8.
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.

Q3KRE8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY
60 70 80 90 100
YNEATGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEYP DRIMNTFSVM PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM
310 320 330 340 350
AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEE GEDEA
Length:445
Mass (Da):49,953
Last modified:November 8, 2005 - v1
Checksum:i4DC3956EFF880746
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181A → P in CAA27067 (PubMed:2868892).Curated
Sequence conflicti55 – 551T → A in CAA27067 (PubMed:2868892).Curated
Sequence conflicti417 – 4171D → E in CAA27067 (PubMed:2868892).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03369 mRNA. Translation: CAA27067.1.
BC105754 mRNA. Translation: AAI05755.1.
PIRiA25113.
RefSeqiNP_001013908.2. NM_001013886.2.
UniGeneiRn.37849.

Genome annotation databases

EnsembliENSRNOT00000023582; ENSRNOP00000023582; ENSRNOG00000017445.
ENSRNOT00000083705; ENSRNOP00000073323; ENSRNOG00000017445.
GeneIDi291081.
KEGGirno:291081.
UCSCiRGD:1309427. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03369 mRNA. Translation: CAA27067.1.
BC105754 mRNA. Translation: AAI05755.1.
PIRiA25113.
RefSeqiNP_001013908.2. NM_001013886.2.
UniGeneiRn.37849.

3D structure databases

ProteinModelPortaliQ3KRE8.
SMRiQ3KRE8. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi253414. 5 interactions.
IntActiQ3KRE8. 4 interactions.
MINTiMINT-236031.
STRINGi10116.ENSRNOP00000023582.

PTM databases

iPTMnetiQ3KRE8.
PhosphoSiteiQ3KRE8.

Proteomic databases

PaxDbiQ3KRE8.
PRIDEiQ3KRE8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023582; ENSRNOP00000023582; ENSRNOG00000017445.
ENSRNOT00000083705; ENSRNOP00000073323; ENSRNOG00000017445.
GeneIDi291081.
KEGGirno:291081.
UCSCiRGD:1309427. rat.

Organism-specific databases

CTDi347733.
RGDi1309427. Tubb2b.

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ3KRE8.
KOiK07375.
OMAiFWEVICA.
OrthoDBiEOG091G06U2.
PhylomeDBiQ3KRE8.
TreeFamiTF300298.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ3KRE8.

Gene expression databases

BgeeiENSRNOG00000017445.
GenevisibleiQ3KRE8. 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 nameiTBB2B_RAT
AccessioniPrimary (citable) accession number: Q3KRE8
Secondary accession number(s): A3KMR7, P04691
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 8, 2005
Last modified: September 7, 2016
This is version 101 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.