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Protein

Tubulin beta-5 chain

Gene
N/A
Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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

Keywordsi

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-5 chain
Alternative name(s):
Beta-tubulin class-V
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 2

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_00000482671 – 446Tubulin beta-5 chainAdd BLAST446

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

Keywords - PTMi

Isopeptide bond

Proteomic databases

PaxDbiP09653
PRIDEiP09653

Expressioni

Gene expression databases

BgeeiENSGALG00000027684

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

STRINGi9031.ENSGALP00000000073

Structurei

3D structure databases

ProteinModelPortaliP09653
SMRiP09653
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00760000119061
HOGENOMiHOG000165710
HOVERGENiHBG000089
KOiK07375
OMAiAVFRGPM
OrthoDBiEOG091G06U2
PhylomeDBiP09653

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.

P09653-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHIQAG QCGNQIGTKF WEVISDEHGI DPAGGYVGDS ALQLERINVY
60 70 80 90 100
YNESSSQKYV PRAVLVDLEP GTMDSVRSGP FGQLFRPDNF IFGQTGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKECEHCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEYP DRIMNTFSVM PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTSL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALTVPELT QQMFDAKNMM
310 320 330 340 350
AACDPRHGRY LTVATVFRGP MSMKEVDEQM LAIQNKNSSY FVEWIPNNVK
360 370 380 390 400
VAVCDIPPRG LKMASTFIGN STAIQELFKR ISEQFSAMFR RKAFLHWFTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQEATA NDGEEAFEDD EEEINE
Length:446
Mass (Da):49,971
Last modified:July 1, 1989 - v1
Checksum:i5AEC755D15A4B0A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29435, M14681, M14682 Genomic DNA Translation: AAA49126.1
PIRiB27554
RefSeqiNP_001026183.1, NM_001031012.2
UniGeneiGga.7794

Genome annotation databases

EnsembliENSGALT00000074135; ENSGALP00000055967; ENSGALG00000031275
GeneIDi421037
KEGGigga:421037

Similar proteinsi

Entry informationi

Entry nameiTBB5_CHICK
AccessioniPrimary (citable) accession number: P09653
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: February 28, 2018
This is version 126 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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