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Protein

Tubulin beta-3 chain

Gene

TUBB3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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. TUBB3 plays a critical role in proper axon guidance and mantainance.1 Publication

Regions

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

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. peptide binding Source: Ensembl
  4. structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  1. 'de novo' posttranslational protein folding Source: Reactome
  2. axon guidance Source: UniProtKB
  3. cellular protein metabolic process Source: Reactome
  4. microtubule-based process Source: InterPro
  5. mitotic nuclear division Source: Ensembl
  6. protein folding Source: Reactome
  7. protein polymerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_121399. MHC class II antigen presentation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_16967. Post-chaperonin tubulin folding pathway.
REACT_22365. Recycling pathway of L1.
REACT_25201. Kinesins.
REACT_267634. Hedgehog 'off' state.
REACT_267716. Orphan transporters.
REACT_682. Mitotic Prometaphase.
REACT_9509. Gap junction assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-3 chain
Alternative name(s):
Tubulin beta-4 chain
Tubulin beta-III
Gene namesi
Name:TUBB3
Synonyms:TUBB4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:20772. TUBB3.

Subcellular locationi

GO - Cellular componenti

  1. axon Source: Ensembl
  2. cell periphery Source: Ensembl
  3. cytoplasm Source: UniProtKB-KW
  4. dendrite Source: ParkinsonsUK-UCL
  5. extracellular vesicular exosome Source: UniProtKB
  6. microtubule Source: UniProtKB
  7. neuronal cell body Source: Ensembl
  8. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Congenital fibrosis of extraocular muscles 3A1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA congenital ocular motility disorder marked by restrictive ophthalmoplegia affecting extraocular muscles innervated by the oculomotor and/or trochlear nerves. It is clinically characterized by anchoring of the eyes in downward gaze, ptosis, and backward tilt of the head. Congenital fibrosis of extraocular muscles type 3 presents as a non-progressive, autosomal dominant disorder with variable expression. Patients may be bilaterally or unilaterally affected, and their oculo-motility defects range from complete ophthalmoplegia (with the eyes fixed in a hypo- and exotropic position), to mild asymptomatic restrictions of ocular movement. Ptosis, refractive error, amblyopia, and compensatory head positions are associated with the more severe forms of the disorder. In some cases, the ocular phenotype is accompanied by additional features including developmental delay, corpus callosum agenesis, basal ganglia dysmorphism, facial weakness, polyneuropathy.

See also OMIM:600638
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti62 – 621R → Q in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 Publication
VAR_062758
Natural varianti262 – 2621R → C in CFEOM3A; affects heterodimers formation; affects microtubules polymerization and depolymerization rates. 1 Publication
VAR_062759
Natural varianti262 – 2621R → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures; affects microtubules polymerization and depolymerization rates. 1 Publication
VAR_062760
Natural varianti302 – 3021A → T in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 Publication
VAR_062761
Natural varianti380 – 3801R → C in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 Publication
VAR_062762
Natural varianti410 – 4101E → K in CFEOM3A; severe phenotype with congenital facial weakness; lower extremity weakness and sensory loss in the second to third decade of life in one patient; affects microtubules polymerization and depolymerization rates. 1 Publication
VAR_062763
Natural varianti417 – 4171D → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures. 1 Publication
VAR_062764
Natural varianti417 – 4171D → N in CFEOM3A; some patients with lower extremity weakness and sensory loss in the second to third decade of life; also found in patients without CFEOM3A who developed polyneuropathy. 1 Publication
VAR_062765
Cortical dysplasia, complex, with other brain malformations 11 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder of aberrant neuronal migration and disturbed axonal guidance. Affected individuals have mild to severe mental retardation, strabismus, axial hypotonia, and spasticity. Brain imaging shows variable malformations of cortical development, including polymicrogyria, gyral disorganization, and fusion of the basal ganglia, as well as thin corpus callosum, hypoplastic brainstem, and dysplastic cerebellar vermis. Extraocular muscles are not involved.

See also OMIM:614039
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti178 – 1781T → M in CDCBM1; can form tubulin heterodimers that are properly incorporated into microtubules; the microtubules are less stable than wild-type. 1 Publication
VAR_066206
Natural varianti205 – 2051E → K in CDCBM1; does not form tubulin heterodimers; patient fibroblasts show no major alterations in the microtubule network, but the microtubules are less stable than wild-type. 1 Publication
VAR_066207
Natural varianti302 – 3021A → V in CDCBM1; does not form tubulin heterodimers. 1 Publication
VAR_066208
Natural varianti323 – 3231M → V in CDCBM1; reduced heterodimers formation. 1 Publication
VAR_066209

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi172 – 1721S → A: Loss of CDK1-mediated phosphorylation. 1 Publication
Mutagenesisi172 – 1721S → D or E: Mimics phosphorylation, unable to incorporate into microtubules. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi600638. phenotype.
614039. phenotype.
Orphaneti45358. Congenital fibrosis of extraocular muscles.
300570. Cortical dysgenesis with pontocerebellar hypoplasia due to TUBB3 mutation.
PharmGKBiPA134953867.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Tubulin beta-3 chainPRO_0000048250Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721Phosphoserine; by CDK11 Publication

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
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

Phosphoprotein

Proteomic databases

MaxQBiQ13509.
PRIDEiQ13509.

2D gel databases

OGPiQ13509.

PTM databases

PhosphoSiteiQ13509.

Expressioni

Tissue specificityi

Expression is primarily restricted to central and peripheral nervous system. Greatly increased expression in most cancerous tissues.2 Publications

Gene expression databases

BgeeiQ13509.
CleanExiHS_TUBB3.
HS_TUBB4.
ExpressionAtlasiQ13509. baseline.
GenevestigatoriQ13509.

Organism-specific databases

HPAiCAB011512.
HPA043640.
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.

Binary interactionsi

WithEntry#Exp.IntActNotes
TUBA1BP683633EBI-350989,EBI-487083

Protein-protein interaction databases

BioGridi115654. 93 interactions.
DIPiDIP-31505N.
IntActiQ13509. 19 interactions.
MINTiMINT-1163245.
STRINGi9606.ENSP00000320295.

Structurei

3D structure databases

ProteinModelPortaliQ13509.
SMRiQ13509. Positions 2-427.
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

GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ13509.
KOiK07375.
PhylomeDBiQ13509.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13509-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY
60 70 80 90 100
YNEASSHKYV PRAILVDLEP GTMDSVRSGA FGHLFRPDNF IFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKECENCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKVREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSIH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLATP TYGDLNHLVS ATMSGVTTSL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALTVPELT QQMFDAKNMM
310 320 330 340 350
AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK
360 370 380 390 400
VAVCDIPPRG LKMSSTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440 450
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEGEMYEDD EEESEAQGPK
Length:450
Mass (Da):50,433
Last modified:May 2, 2002 - v2
Checksum:i4B9CDE7DBA102949
GO
Isoform 2 (identifier: Q13509-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Note: No experimental confirmation available.

Show »
Length:378
Mass (Da):42,433
Checksum:iA190AB5B6264F2AB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti275 – 2751A → R in AAC52035. (PubMed:9473684)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti62 – 621R → Q in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 Publication
VAR_062758
Natural varianti178 – 1781T → M in CDCBM1; can form tubulin heterodimers that are properly incorporated into microtubules; the microtubules are less stable than wild-type. 1 Publication
VAR_066206
Natural varianti205 – 2051E → K in CDCBM1; does not form tubulin heterodimers; patient fibroblasts show no major alterations in the microtubule network, but the microtubules are less stable than wild-type. 1 Publication
VAR_066207
Natural varianti262 – 2621R → C in CFEOM3A; affects heterodimers formation; affects microtubules polymerization and depolymerization rates. 1 Publication
VAR_062759
Natural varianti262 – 2621R → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures; affects microtubules polymerization and depolymerization rates. 1 Publication
VAR_062760
Natural varianti302 – 3021A → T in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 Publication
VAR_062761
Natural varianti302 – 3021A → V in CDCBM1; does not form tubulin heterodimers. 1 Publication
VAR_066208
Natural varianti323 – 3231M → V in CDCBM1; reduced heterodimers formation. 1 Publication
VAR_066209
Natural varianti380 – 3801R → C in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 Publication
VAR_062762
Natural varianti410 – 4101E → K in CFEOM3A; severe phenotype with congenital facial weakness; lower extremity weakness and sensory loss in the second to third decade of life in one patient; affects microtubules polymerization and depolymerization rates. 1 Publication
VAR_062763
Natural varianti417 – 4171D → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures. 1 Publication
VAR_062764
Natural varianti417 – 4171D → N in CFEOM3A; some patients with lower extremity weakness and sensory loss in the second to third decade of life; also found in patients without CFEOM3A who developed polyneuropathy. 1 Publication
VAR_062765

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7272Missing in isoform 2. 1 PublicationVSP_054659Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47634 mRNA. Translation: AAC52035.1.
AF427491 mRNA. Translation: AAL28094.1.
AK122757 mRNA. Translation: BAG53710.1.
AK292219 mRNA. Translation: BAF84908.1.
AC092143 Genomic DNA. No translation available.
CH471184 Genomic DNA. Translation: EAW66674.1.
BC000748 mRNA. Translation: AAH00748.1.
BC003021 mRNA. Translation: AAH03021.2.
CCDSiCCDS10988.1. [Q13509-1]
CCDS56012.1. [Q13509-2]
RefSeqiNP_001184110.1. NM_001197181.1. [Q13509-2]
NP_006077.2. NM_006086.3. [Q13509-1]
UniGeneiHs.511743.

Genome annotation databases

EnsembliENST00000315491; ENSP00000320295; ENSG00000258947. [Q13509-1]
ENST00000554444; ENSP00000451617; ENSG00000258947. [Q13509-2]
GeneIDi10381.
KEGGihsa:10381.
UCSCiuc002fpf.2. human. [Q13509-1]

Polymorphism databases

DMDMi20455526.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47634 mRNA. Translation: AAC52035.1.
AF427491 mRNA. Translation: AAL28094.1.
AK122757 mRNA. Translation: BAG53710.1.
AK292219 mRNA. Translation: BAF84908.1.
AC092143 Genomic DNA. No translation available.
CH471184 Genomic DNA. Translation: EAW66674.1.
BC000748 mRNA. Translation: AAH00748.1.
BC003021 mRNA. Translation: AAH03021.2.
CCDSiCCDS10988.1. [Q13509-1]
CCDS56012.1. [Q13509-2]
RefSeqiNP_001184110.1. NM_001197181.1. [Q13509-2]
NP_006077.2. NM_006086.3. [Q13509-1]
UniGeneiHs.511743.

3D structure databases

ProteinModelPortaliQ13509.
SMRiQ13509. Positions 2-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115654. 93 interactions.
DIPiDIP-31505N.
IntActiQ13509. 19 interactions.
MINTiMINT-1163245.
STRINGi9606.ENSP00000320295.

Chemistry

ChEMBLiCHEMBL2597.
DrugBankiDB04845. Ixabepilone.

PTM databases

PhosphoSiteiQ13509.

Polymorphism databases

DMDMi20455526.

2D gel databases

OGPiQ13509.

Proteomic databases

MaxQBiQ13509.
PRIDEiQ13509.

Protocols and materials databases

DNASUi10381.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000315491; ENSP00000320295; ENSG00000258947. [Q13509-1]
ENST00000554444; ENSP00000451617; ENSG00000258947. [Q13509-2]
GeneIDi10381.
KEGGihsa:10381.
UCSCiuc002fpf.2. human. [Q13509-1]

Organism-specific databases

CTDi10381.
GeneCardsiGC16P089999.
GC16P090000.
GeneReviewsiTUBB3.
HGNCiHGNC:20772. TUBB3.
HPAiCAB011512.
HPA043640.
HPA046280.
MIMi600638. phenotype.
602661. gene.
614039. phenotype.
neXtProtiNX_Q13509.
Orphaneti45358. Congenital fibrosis of extraocular muscles.
300570. Cortical dysgenesis with pontocerebellar hypoplasia due to TUBB3 mutation.
PharmGKBiPA134953867.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ13509.
KOiK07375.
PhylomeDBiQ13509.
TreeFamiTF300298.

Enzyme and pathway databases

ReactomeiREACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_121399. MHC class II antigen presentation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_16967. Post-chaperonin tubulin folding pathway.
REACT_22365. Recycling pathway of L1.
REACT_25201. Kinesins.
REACT_267634. Hedgehog 'off' state.
REACT_267716. Orphan transporters.
REACT_682. Mitotic Prometaphase.
REACT_9509. Gap junction assembly.

Miscellaneous databases

ChiTaRSiTUBB3. human.
GeneWikiiTUBB3.
GenomeRNAii10381.
NextBioi39327.
PROiQ13509.
SOURCEiSearch...

Gene expression databases

BgeeiQ13509.
CleanExiHS_TUBB3.
HS_TUBB4.
ExpressionAtlasiQ13509. baseline.
GenevestigatoriQ13509.

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. "Cloning and sequencing of human betaIII-tubulin cDNA: induction of betaIII isotype in human prostate carcinoma cells by acute exposure to antimicrotubule agents."
    Ranganathan S., Dexter D.W., Benetatos C.A., Hudes G.R.
    Biochim. Biophys. Acta 1395:237-245(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Banerjee A.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Mammary cancer.
  3. "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] (ISOFORM 2).
    Tissue: Brain and Esophagus.
  4. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Lung.
  7. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 63-77; 104-121; 242-251; 163-174 AND 381-390, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  8. "Class III beta-tubulin isotype: a key cytoskeletal protein at the crossroads of developmental neurobiology and tumor neuropathology."
    Katsetos C.D., Legido A., Perentes E., Mork S.J.
    J. Child Neurol. 18:851-866(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. Erratum
    Katsetos C.D., Legido A., Perentes E., Mork S.J.
    J. Child Neurol. 19:531-531(2004)
  10. "Microtubule regulation in mitosis: tubulin phosphorylation by the cyclin-dependent kinase Cdk1."
    Fourest-Lieuvin A., Peris L., Gache V., Garcia-Saez I., Juillan-Binard C., Lantez V., Job D.
    Mol. Biol. Cell 17:1041-1050(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-172 BY CDK1, MUTAGENESIS OF SER-172.
  11. "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.
  12. Cited for: FUNCTION, VARIANTS CFEOM3A GLN-62; CYS-262; HIS-262; THR-302; CYS-380; LYS-410; HIS-417 AND ASN-417, CHARACTERIZATION OF VARIANTS CFEOM3A GLN-62; CYS-262; HIS-262; THR-302; CYS-380 AND LYS-410.
  13. Cited for: TISSUE SPECIFICITY.
  14. Cited for: VARIANTS CDCBM1 MET-178; LYS-205; VAL-302 AND VAL-323, CHARACTERIZATION OF VARIANTS CDCBM1 MET-178; LYS-205; VAL-302 AND VAL-323.

Entry informationi

Entry nameiTBB3_HUMAN
AccessioniPrimary (citable) accession number: Q13509
Secondary accession number(s): A8K854, Q9BTZ0, Q9BW10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 2, 2002
Last modified: January 7, 2015
This is version 143 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.