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Protein

Tubulin beta-6 chain

Gene

TUBB6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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).By similarity

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-HSA-1445148 Translocation of GLUT4 to the plasma membrane
R-HSA-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-HSA-190861 Gap junction assembly
R-HSA-2132295 MHC class II antigen presentation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
R-HSA-389957 Prefoldin mediated transfer of substrate to CCT/TriC
R-HSA-389960 Formation of tubulin folding intermediates by CCT/TriC
R-HSA-389977 Post-chaperonin tubulin folding pathway
R-HSA-437239 Recycling pathway of L1
R-HSA-5610787 Hedgehog 'off' state
R-HSA-5617833 Cilium Assembly
R-HSA-5620924 Intraflagellar transport
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-6807878 COPI-mediated anterograde transport
R-HSA-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-HSA-68877 Mitotic Prometaphase
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8955332 Carboxyterminal post-translational modifications of tubulin
R-HSA-983189 Kinesins
SIGNORiQ9BUF5

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-6 chain
Alternative name(s):
Tubulin beta class V
Gene namesi
Name:TUBB6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

EuPathDBiHostDB:ENSG00000176014.12
HGNCiHGNC:20776 TUBB6
MIMi615103 gene
neXtProtiNX_Q9BUF5

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

Pathology & Biotechi

Organism-specific databases

DisGeNETi84617
OpenTargetsiENSG00000176014
PharmGKBiPA128394736

Chemistry databases

ChEMBLiCHEMBL2095182
DrugBankiDB05147 CYT997

Polymorphism and mutation databases

BioMutaiTUBB6
DMDMi68776070

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000482551 – 446Tubulin beta-6 chainAdd BLAST446

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei172Phosphoserine; by CDK11 Publication1
Modified residuei4385-glutamyl polyglutamateBy similarity1

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866). 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 (PubMed:26875866).1 Publication
Some glutamate residues at the C-terminus are monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of monoglycylation is still unclear (Probable).1 Publication
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.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein

Proteomic databases

EPDiQ9BUF5
MaxQBiQ9BUF5
PaxDbiQ9BUF5
PeptideAtlasiQ9BUF5
PRIDEiQ9BUF5

PTM databases

iPTMnetiQ9BUF5
PhosphoSitePlusiQ9BUF5
SwissPalmiQ9BUF5

Expressioni

Tissue specificityi

Ubiquitous. Maximal expression in breast and lung, where it represents around 10% of all beta-tubulins. Largely decreased expression in most cancerous tissues.1 Publication

Gene expression databases

BgeeiENSG00000176014
CleanExiHS_TUBB6
ExpressionAtlasiQ9BUF5 baseline and differential
GenevisibleiQ9BUF5 HS

Organism-specific databases

HPAiHPA043640
HPA046280

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

BioGridi124148, 75 interactors
IntActiQ9BUF5, 38 interactors
MINTiQ9BUF5
STRINGi9606.ENSP00000318697

Structurei

3D structure databases

ProteinModelPortaliQ9BUF5
SMRiQ9BUF5
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
HOVERGENiHBG000089
InParanoidiQ9BUF5
KOiK07375
OMAiAVFRGPM
OrthoDBiEOG091G06U2
PhylomeDBiQ9BUF5
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.

Q9BUF5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHIQAG QCGNQIGTKF WEVISDEHGI DPAGGYVGDS ALQLERINVY
60 70 80 90 100
YNESSSQKYV PRAALVDLEP GTMDSVRSGP FGQLFRPDNF IFGQTGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDAVLDVV RKECEHCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEFP DRIMNTFSVM PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTSL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDARNMM
310 320 330 340 350
AACDPRHGRY LTVATVFRGP MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK
360 370 380 390 400
VAVCDIPPRG LKMASTFIGN STAIQELFKR ISEQFSAMFR RKAFLHWFTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA NDGEEAFEDE EEEIDG
Length:446
Mass (Da):49,857
Last modified:June 1, 2001 - v1
Checksum:iE9884AC2BD676BB2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti91I → V in BAB14016 (PubMed:14702039).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001295 mRNA Translation: BAG50888.1
AK022340 mRNA Translation: BAB14016.1
BC002654 mRNA Translation: AAH02654.1
CCDSiCCDS11858.1
RefSeqiNP_001290453.1, NM_001303524.1
NP_001290454.1, NM_001303525.1
NP_001290455.1, NM_001303526.1
NP_001290456.1, NM_001303527.1
NP_001290457.1, NM_001303528.1
NP_001290458.1, NM_001303529.1
NP_001290459.1, NM_001303530.1
NP_115914.1, NM_032525.2
UniGeneiHs.193491
Hs.744066

Genome annotation databases

EnsembliENST00000317702; ENSP00000318697; ENSG00000176014
GeneIDi84617
KEGGihsa:84617
UCSCiuc002kqw.4 human

Similar proteinsi

Entry informationi

Entry nameiTBB6_HUMAN
AccessioniPrimary (citable) accession number: Q9BUF5
Secondary accession number(s): B3KM76, Q9HA42
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: June 1, 2001
Last modified: April 25, 2018
This is version 156 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health