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Q13509 (TBB3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tubulin beta-3 chain
Alternative name(s):
Tubulin beta-4 chain
Tubulin beta-III
Gene names
Name:TUBB3
Synonyms:TUBB4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12

Subunit structure

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.

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

Expression is primarily restricted to central and peripheral nervous system. Greatly increased expression in most cancerous tissues. Ref.8 Ref.13

Domain

The highly acidic C-terminal region may bind cations such as calcium.

Post-translational modification

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.

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. Ref.10

Involvement in disease

Congenital fibrosis of extraocular muscles 3A (CFEOM3A) [MIM:600638]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Cortical dysplasia, complex, with other brain malformations 1 (CDCBM1) [MIM:614039]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

Sequence similarities

Belongs to the tubulin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TUBA1BP683633EBI-350989,EBI-487083

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13509-1)

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.
Isoform 2 (identifier: Q13509-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Tubulin beta-3 chain
PRO_0000048250

Regions

Nucleotide binding140 – 1467GTP Potential

Amino acid modifications

Modified residue1721Phosphoserine; by CDK1 Ref.10

Natural variations

Alternative sequence1 – 7272Missing in isoform 2.
VSP_054659
Natural variant621R → Q in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. Ref.12
VAR_062758
Natural variant1781T → M in CDCBM1; can form tubulin heterodimers that are properly incorporated into microtubules; the microtubules are less stable than wild-type. Ref.14
VAR_066206
Natural variant2051E → 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. Ref.14
VAR_066207
Natural variant2621R → C in CFEOM3A; affects heterodimers formation; affects microtubules polymerization and depolymerization rates. Ref.12
VAR_062759
Natural variant2621R → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures; affects microtubules polymerization and depolymerization rates. Ref.12
VAR_062760
Natural variant3021A → T in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. Ref.12
VAR_062761
Natural variant3021A → V in CDCBM1; does not form tubulin heterodimers. Ref.14
VAR_066208
Natural variant3231M → V in CDCBM1; reduced heterodimers formation. Ref.14
VAR_066209
Natural variant3801R → C in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. Ref.12
VAR_062762
Natural variant4101E → 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. Ref.12
VAR_062763
Natural variant4171D → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures. Ref.12
VAR_062764
Natural variant4171D → 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. Ref.12
VAR_062765

Experimental info

Mutagenesis1721S → A: Loss of CDK1-mediated phosphorylation. Ref.10
Mutagenesis1721S → D or E: Mimics phosphorylation, unable to incorporate into microtubules. Ref.10
Sequence conflict2751A → R in AAC52035. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 2, 2002. Version 2.
Checksum: 4B9CDE7DBA102949

FASTA45050,433
        10         20         30         40         50         60 
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY YNEASSHKYV 

        70         80         90        100        110        120 
PRAILVDLEP GTMDSVRSGA FGHLFRPDNF IFGQSGAGNN WAKGHYTEGA ELVDSVLDVV 

       130        140        150        160        170        180 
RKECENCDCL QGFQLTHSLG GGTGSGMGTL LISKVREEYP DRIMNTFSVV PSPKVSDTVV 

       190        200        210        220        230        240 
EPYNATLSIH QLVENTDETY CIDNEALYDI CFRTLKLATP TYGDLNHLVS ATMSGVTTSL 

       250        260        270        280        290        300 
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALTVPELT QQMFDAKNMM 

       310        320        330        340        350        360 
AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK VAVCDIPPRG 

       370        380        390        400        410        420 
LKMSSTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS 

       430        440        450 
EYQQYQDATA EEEGEMYEDD EEESEAQGPK 

« Hide

Isoform 2 [UniParc].

Checksum: A190AB5B6264F2AB
Show »

FASTA37842,433

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Human TUBB3 mutations perturb microtubule dynamics, kinesin interactions, and axon guidance."
Tischfield M.A., Baris H.N., Wu C., Rudolph G., Van Maldergem L., He W., Chan W.M., Andrews C., Demer J.L., Robertson R.L., Mackey D.A., Ruddle J.B., Bird T.D., Gottlob I., Pieh C., Traboulsi E.I., Pomeroy S.L., Hunter D.G. expand/collapse author list , Soul J.S., Newlin A., Sabol L.J., Doherty E.J., de Uzcategui C.E., de Uzcategui N., Collins M.L., Sener E.C., Wabbels B., Hellebrand H., Meitinger T., de Berardinis T., Magli A., Schiavi C., Pastore-Trossello M., Koc F., Wong A.M., Levin A.V., Geraghty M.T., Descartes M., Flaherty M., Jamieson R.V., Moller H.U., Meuthen I., Callen D.F., Kerwin J., Lindsay S., Meindl A., Gupta M.L. Jr., Pellman D., Engle E.C.
Cell 140:74-87(2010) [PubMed] [Europe PMC] [Abstract]
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]"Tumoral and tissue-specific expression of the major human beta-tubulin isotypes."
Leandro-Garcia L.J., Leskela S., Landa I., Montero-Conde C., Lopez-Jimenez E., Leton R., Cascon A., Robledo M., Rodriguez-Antona C.
Cytoskeleton 67:214-223(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[14]"Mutations in the neuronal ss-tubulin subunit TUBB3 result in malformation of cortical development and neuronal migration defects."
Poirier K., Saillour Y., Bahi-Buisson N., Jaglin X.H., Fallet-Bianco C., Nabbout R., Castelnau-Ptakhine L., Roubertie A., Attie-Bitach T., Desguerre I., Genevieve D., Barnerias C., Keren B., Lebrun N., Boddaert N., Encha-Razavi F., Chelly J.
Hum. Mol. Genet. 19:4462-4473(2010) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10988.1.
RefSeqNP_001184110.1. NM_001197181.1. [Q13509-2]
NP_006077.2. NM_006086.3. [Q13509-1]
UniGeneHs.511743.

3D structure databases

ProteinModelPortalQ13509.
SMRQ13509. Positions 2-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115654. 71 interactions.
IntActQ13509. 19 interactions.
MINTMINT-1163245.
STRING9606.ENSP00000320295.

Chemistry

BindingDBQ13509.
ChEMBLCHEMBL2597.

PTM databases

PhosphoSiteQ13509.

Polymorphism databases

DMDM20455526.

2D gel databases

OGPQ13509.

Proteomic databases

MaxQBQ13509.
PRIDEQ13509.

Protocols and materials databases

DNASU10381.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304984; ENSP00000302777; ENSG00000258947.
ENST00000315491; ENSP00000320295; ENSG00000198211.
GeneID10381.
KEGGhsa:10381.
UCSCuc002fpf.2. human. [Q13509-1]

Organism-specific databases

CTD10381.
GeneCardsGC16P089996.
GC16P089997.
GeneReviewsTUBB3.
HGNCHGNC:20772. TUBB3.
HPACAB011512.
HPA043640.
HPA046280.
MIM600638. phenotype.
602661. gene.
614039. phenotype.
neXtProtNX_Q13509.
Orphanet45358. Congenital fibrosis of extraocular muscles.
300570. Cortical dysgenesis with pontocerebellar hypoplasia due to TUBB3 mutation.
PharmGKBPA134953867.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000165710.
HOVERGENHBG000089.
KOK07375.
PhylomeDBQ13509.
TreeFamTF300298.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_11123. Membrane Trafficking.
REACT_115566. Cell Cycle.
REACT_17015. Metabolism of proteins.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

BgeeQ13509.
CleanExHS_TUBB3.
HS_TUBB4.
GenevestigatorQ13509.

Family and domain databases

Gene3D1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProIPR013838. 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]
PANTHERPTHR11588. PTHR11588. 1 hit.
PfamPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSPR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTUBB3. human.
GeneWikiTUBB3.
GenomeRNAi10381.
NextBio39327.
PROQ13509.
SOURCESearch...

Entry information

Entry nameTBB3_HUMAN
AccessionPrimary (citable) accession number: Q13509
Secondary accession number(s): A8K854, Q9BTZ0, Q9BW10
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 2, 2002
Last modified: July 9, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM