Skip Header

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

Tubulin beta-2B chain

Gene

Tubb2b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Tubulin is the major constituent of microtubules (PubMed:19465910). 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. Plays a critical role in proper axon guidance in both central and peripheral axon tracts. Implicated in neuronal migration (By similarity).By similarity1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi140 – 146GTPSequence analysis7

GO - Molecular functioni

GO - Biological processi

  • microtubule-based process Source: UniProtKB
  • neuron migration Source: UniProtKB
  • positive regulation of axon guidance Source: UniProtKB

Keywordsi

Biological processNeurogenesis
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-RNO-2132295 MHC class II antigen presentation
R-RNO-2467813 Separation of Sister Chromatids
R-RNO-2500257 Resolution of Sister Chromatid Cohesion
R-RNO-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-RNO-380320 Recruitment of NuMA to mitotic centrosomes
R-RNO-437239 Recycling pathway of L1
R-RNO-5620924 Intraflagellar transport
R-RNO-5626467 RHO GTPases activate IQGAPs
R-RNO-5663220 RHO GTPases Activate Formins
R-RNO-6807878 COPI-mediated anterograde transport
R-RNO-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-RNO-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-RNO-68877 Mitotic Prometaphase
R-RNO-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-RNO-8955332 Carboxyterminal post-translational modifications of tubulin
R-RNO-983189 Kinesins

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi1309427 Tubb2b

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002626531 – 445Tubulin beta-2B chainAdd BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40PhosphoserineBy similarity1
Modified residuei55PhosphothreonineCombined sources1
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

PaxDbiQ3KRE8
PRIDEiQ3KRE8

PTM databases

iPTMnetiQ3KRE8
PhosphoSitePlusiQ3KRE8
SwissPalmiQ3KRE8

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.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi253414, 5 interactors
IntActiQ3KRE8, 4 interactors
STRINGi10116.ENSRNOP00000023582

Structurei

3D structure databases

ProteinModelPortaliQ3KRE8
SMRiQ3KRE8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00760000119061
HOGENOMiHOG000165710
HOVERGENiHBG000089
InParanoidiQ3KRE8
KOiK07375
OMAiFRDRISM
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
InterProiView protein in InterPro
IPR013838 Beta-tubulin_BS
IPR002453 Beta_tubulin
IPR008280 Tub_FtsZ_C
IPR000217 Tubulin
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR037103 Tubulin/FtsZ_C_sf
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR023123 Tubulin_C
IPR017975 Tubulin_CS
IPR003008 Tubulin_FtsZ_GTPase
PANTHERiPTHR11588 PTHR11588, 1 hit
PTHR11588:SF256 PTHR11588:SF256, 1 hit
PfamiView protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit
PRINTSiPR01163 BETATUBULIN
PR01161 TUBULIN
SMARTiView protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit
SUPFAMiSSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit
PROSITEiView protein in PROSITE
PS00227 TUBULIN, 1 hit
PS00228 TUBULIN_B_AUTOREG, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti18A → P in CAA27067 (PubMed:2868892).Curated1
Sequence conflicti55T → A in CAA27067 (PubMed:2868892).Curated1
Sequence conflicti417D → E in CAA27067 (PubMed:2868892).Curated1

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.225893
Rn.37849

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiTBB2B_RAT
AccessioniPrimary (citable) accession number: Q3KRE8
Secondary accession number(s): A3KMR7, P04691
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 8, 2005
Last modified: May 23, 2018
This is version 114 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health