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Protein

Tubulin beta-8 chain

Gene

TUBB8

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

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-8 chain
Gene namesi
Name:TUBB8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componentsi: Chromosome 10, Unplaced

Organism-specific databases

HGNCiHGNC:20773. TUBB8.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Polymorphism and mutation databases

BioMutaiTUBB8.
DMDMi182705285.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Tubulin beta-8 chainPRO_0000320631Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721Phosphoserine; by CDK1By similarity

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also 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) 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 glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules (Probable).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ3ZCM7.
PRIDEiQ3ZCM7.

PTM databases

PhosphoSiteiQ3ZCM7.

Expressioni

Gene expression databases

BgeeiQ3ZCM7.
ExpressionAtlasiQ3ZCM7. baseline.
GenevestigatoriQ3ZCM7.

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

BioGridi131462. 64 interactions.
IntActiQ3ZCM7. 4 interactions.
MINTiMINT-1144251.

Structurei

3D structure databases

ProteinModelPortaliQ3ZCM7.
SMRiQ3ZCM7. Positions 1-428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ3ZCM7.
KOiK07375.
OMAiLTQIGQC.
PhylomeDBiQ3ZCM7.
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.

Q3ZCM7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVLTQIG QCGNQIGAKF WEVISDEHAI DSAGTYHGDS HLQLERINVY
60 70 80 90 100
YNEASGGRYV PRAVLVDLEP GTMDSVRSGP FGQVFRPDNF IFGQCGAGNN
110 120 130 140 150
WAKGHYTEGA ELMESVMDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LLSKIREEYP DRIINTFSIL PSPKVSDTVV EPYNATLSVH QLIENADETF
210 220 230 240 250
CIDNEALYDI CSKTLKLPTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVAELT QQMFDAKNMM
310 320 330 340 350
AACDPRHGRY LTAAAIFRGR MPMREVDEQM FNIQDKNSSY FADWLPNNVK
360 370 380 390 400
TAVCDIPPRG LKMSATFIGN NTAIQELFKR VSEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEEDEEYAE EEVA
Length:444
Mass (Da):49,776
Last modified:February 26, 2008 - v2
Checksum:i3EC4AC10946BF590
GO

Sequence cautioni

The sequence CAI16221.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti345 – 3451L → F.
Corresponds to variant rs4880608 [ dbSNP | Ensembl ].
VAR_039240

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF355127 Genomic DNA. Translation: AAL32434.1.
CR590375 mRNA. No translation available.
AL713922 Genomic DNA. Translation: CAI16221.1. Sequence problems.
CH471072 Genomic DNA. Translation: EAW86545.1.
BC101270 mRNA. Translation: AAI01271.1.
BC101271 mRNA. Translation: AAI01272.1.
CCDSiCCDS7051.1.
RefSeqiNP_817124.1. NM_177987.2.
UniGeneiHs.532659.

Genome annotation databases

EnsembliENST00000309812; ENSP00000311042; ENSG00000173876.
ENST00000568584; ENSP00000456206; ENSG00000261456.
GeneIDi347688.
KEGGihsa:347688.
UCSCiuc001ifi.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF355127 Genomic DNA. Translation: AAL32434.1.
CR590375 mRNA. No translation available.
AL713922 Genomic DNA. Translation: CAI16221.1. Sequence problems.
CH471072 Genomic DNA. Translation: EAW86545.1.
BC101270 mRNA. Translation: AAI01271.1.
BC101271 mRNA. Translation: AAI01272.1.
CCDSiCCDS7051.1.
RefSeqiNP_817124.1. NM_177987.2.
UniGeneiHs.532659.

3D structure databases

ProteinModelPortaliQ3ZCM7.
SMRiQ3ZCM7. Positions 1-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi131462. 64 interactions.
IntActiQ3ZCM7. 4 interactions.
MINTiMINT-1144251.

Chemistry

ChEMBLiCHEMBL2095182.

PTM databases

PhosphoSiteiQ3ZCM7.

Polymorphism and mutation databases

BioMutaiTUBB8.
DMDMi182705285.

Proteomic databases

MaxQBiQ3ZCM7.
PRIDEiQ3ZCM7.

Protocols and materials databases

DNASUi347688.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309812; ENSP00000311042; ENSG00000173876.
ENST00000568584; ENSP00000456206; ENSG00000261456.
GeneIDi347688.
KEGGihsa:347688.
UCSCiuc001ifi.2. human.

Organism-specific databases

CTDi347688.
GeneCardsiGC10M000093.
H-InvDBHIX0029368.
HGNCiHGNC:20773. TUBB8.
HPAiHPA043640.
HPA046280.
neXtProtiNX_Q3ZCM7.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ3ZCM7.
KOiK07375.
OMAiLTQIGQC.
PhylomeDBiQ3ZCM7.
TreeFamiTF300298.

Miscellaneous databases

GenomeRNAii347688.
NextBioi99218.
PROiQ3ZCM7.

Gene expression databases

BgeeiQ3ZCM7.
ExpressionAtlasiQ3ZCM7. baseline.
GenevestigatoriQ3ZCM7.

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. "A cascade of complex subtelomeric duplications during the evolution of the hominoid and Old World monkey genomes."
    van Geel M., Eichler E.E., Beck A.F., Shan Z., Haaf T., van der Maarel S.M., Frants R.R., de Jong P.J.
    Am. J. Hum. Genet. 70:269-278(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brain.
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] OF 4-444.
  6. "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.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTBB8_HUMAN
AccessioniPrimary (citable) accession number: Q3ZCM7
Secondary accession number(s): Q5SQX9, Q8WZ78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: May 27, 2015
This is version 92 of the entry and version 2 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 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.