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Protein

Tubulin beta-6 chain

Gene

TUBB6

Organism
Homo sapiens (Human)
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).By similarity

Regions

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-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-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. Assembly of the primary cilium.
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-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

HGNCiHGNC:20776. TUBB6.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-KW
  • extracellular exosome Source: UniProtKB
  • microtubule Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394736.

Chemistry

ChEMBLiCHEMBL2095182.

Polymorphism and mutation databases

BioMutaiTUBB6.
DMDMi68776070.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446Tubulin beta-6 chainPRO_0000048255Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581N6-acetyllysineBy similarity
Modified residuei172 – 1721Phosphoserine; by CDK1By similarity
Modified residuei438 – 43815-glutamyl polyglutamateBy similarity

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein

Proteomic databases

EPDiQ9BUF5.
MaxQBiQ9BUF5.
PaxDbiQ9BUF5.
PeptideAtlasiQ9BUF5.
PRIDEiQ9BUF5.

PTM databases

iPTMnetiQ9BUF5.
PhosphoSiteiQ9BUF5.
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

BgeeiQ9BUF5.
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. 61 interactions.
IntActiQ9BUF5. 25 interactions.
MINTiMINT-1139343.
STRINGi9606.ENSP00000318697.

Structurei

3D structure databases

ProteinModelPortaliQ9BUF5.
SMRiQ9BUF5. 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.
HOVERGENiHBG000089.
InParanoidiQ9BUF5.
KOiK07375.
OMAiAVFRGPM.
PhylomeDBiQ9BUF5.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911I → V in BAB14016 (PubMed:14702039).Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ9BUF5.
SMRiQ9BUF5. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124148. 61 interactions.
IntActiQ9BUF5. 25 interactions.
MINTiMINT-1139343.
STRINGi9606.ENSP00000318697.

Chemistry

ChEMBLiCHEMBL2095182.

PTM databases

iPTMnetiQ9BUF5.
PhosphoSiteiQ9BUF5.
SwissPalmiQ9BUF5.

Polymorphism and mutation databases

BioMutaiTUBB6.
DMDMi68776070.

Proteomic databases

EPDiQ9BUF5.
MaxQBiQ9BUF5.
PaxDbiQ9BUF5.
PeptideAtlasiQ9BUF5.
PRIDEiQ9BUF5.

Protocols and materials databases

DNASUi84617.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi84617.
GeneCardsiTUBB6.
HGNCiHGNC:20776. TUBB6.
HPAiHPA043640.
HPA046280.
MIMi615103. gene.
neXtProtiNX_Q9BUF5.
PharmGKBiPA128394736.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOVERGENiHBG000089.
InParanoidiQ9BUF5.
KOiK07375.
OMAiAVFRGPM.
PhylomeDBiQ9BUF5.
TreeFamiTF300298.

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-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. Assembly of the primary cilium.
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-983189. Kinesins.
SIGNORiQ9BUF5.

Miscellaneous databases

ChiTaRSiTUBB6. human.
GenomeRNAii84617.
PROiQ9BUF5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BUF5.
CleanExiHS_TUBB6.
ExpressionAtlasiQ9BUF5. baseline and differential.
GenevisibleiQ9BUF5. HS.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary gland.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  3. "Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
    Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.
    Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCYLATION.
  4. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  5. Cited for: TISSUE SPECIFICITY.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  9. "Graded control of microtubule severing by tubulin glutamylation."
    Valenstein M.L., Roll-Mecak A.
    Cell 164:911-921(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLUTAMYLATION.

Entry informationi

Entry nameiTBB6_HUMAN
AccessioniPrimary (citable) accession number: Q9BUF5
Secondary accession number(s): B3KM76, Q9HA42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 141 of the entry and version 1 of the sequence. [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

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.