TUBB3

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 key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	140 – 146	GTPSequence analysis		7

GO - Molecular functionⁱ

GTPase activity Source: InterPro
GTP binding Source: UniProtKB-KW
peptide binding Source: Ensembl
structural constituent of cytoskeleton Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

axon guidance
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20074521
microtubule-based process Source: InterPro
mitotic cell cycle Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Ligand	GTP-binding, Nucleotide-binding

Ligand

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactomeⁱ	R-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
SIGNORⁱ	Q13509

Reactomeⁱ

R-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

SIGNORⁱ

Q13509

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 16

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000258947.6
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:20772 TUBB3
MIMⁱ	602661 gene
neXtProtⁱ	NX_Q13509

Keywords - Cellular componentⁱ

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Fibrosis of extraocular muscles, congenital, 3A (CFEOM3A)1 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.

Cortical dysplasia, complex, with other brain malformations 1 (CDCBM1)1 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.

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_066206	178	T → M in CDCBM1; can form tubulin heterodimers that are properly incorporated into microtubules; the microtubules are less stable than wild-type. 1 PublicationCorresponds to variant dbSNP:rs747480526EnsemblClinVar.	1
Natural variantⁱVAR_066207	205	E → 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 PublicationCorresponds to variant dbSNP:rs878853257EnsemblClinVar.	1
Natural variantⁱVAR_066208	302	A → V in CDCBM1; does not form tubulin heterodimers. 1 PublicationCorresponds to variant dbSNP:rs878853258Ensembl.	1
Natural variantⁱVAR_066209	323	M → V in CDCBM1; reduced heterodimers formation. 1 PublicationCorresponds to variant dbSNP:rs878853256Ensembl.	1

Keywords - Diseaseⁱ

Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	10381
GeneReviewsⁱ	TUBB3
MalaCards human disease database More...MalaCardsⁱ	TUBB3
MIMⁱ	600638 phenotype 614039 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000258947
Orphanetⁱ	45358 Congenital fibrosis of extraocular muscles 300570 Cortical dysgenesis with pontocerebellar hypoplasia due to TUBB3 mutation
PharmGKBⁱ	PA134953867

Chemistry databases

ChEMBLⁱ	CHEMBL2597
Drug and drug target database More...DrugBankⁱ	DB05147 CYT997 DB03010 Epothilone B DB01873 Epothilone D DB04845 Ixabepilone DB06042 ZEN-012
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2752

Polymorphism and mutation databases

BioMutaⁱ	TUBB3
DMDMⁱ	20455526

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000048250	1 – 450	Tubulin beta-3 chainAdd BLAST		450

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	172	Phosphoserine; by CDK11 Publication	1
Modified residueⁱ	438	5-glutamyl polyglutamateBy similarity	1
Modified residueⁱ	444	PhosphoserineBy similarity	1

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

EPDⁱ	Q13509
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q13509
PaxDbⁱ	Q13509
PeptideAtlas More...PeptideAtlasⁱ	Q13509
PRIDEⁱ	Q13509
ProteomicsDBⁱ	59510
TopDownProteomicsⁱ	Q13509-1 [Q13509-1]

2D gel databases

USC-OGP 2-DE database More...OGPⁱ	Q13509

OGPⁱ

Q13509

PTM databases

iPTMnetⁱ	Q13509
PhosphoSitePlusⁱ	Q13509
SwissPalmⁱ	Q13509

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

Bgeeⁱ	ENSG00000258947
CleanExⁱ	HS_TUBB3 HS_TUBB4
ExpressionAtlasⁱ	Q13509 baseline and differential
Genevisibleⁱ	Q13509 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA043640 HPA046280

HPAⁱ

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

With	Entry	#Exp.	IntAct	Notes
TERF1	P54274	2	EBI-350989,EBI-710997
TUBA1B	P68363	3	EBI-350989,EBI-487083

Show more details

Protein-protein interaction databases

BioGridⁱ	115654, 261 interactors
Database of interacting proteins More...DIPⁱ	DIP-31505N
IntActⁱ	Q13509, 147 interactors
Molecular INTeraction database More...MINTⁱ	Q13509
STRINGⁱ	9606.ENSP00000320295

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q13509
SMRⁱ	Q13509
ModBaseⁱ	Search...
MobiDBⁱ	Search...

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

eggNOGⁱ	KOG1375 Eukaryota COG5023 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000119061
HOGENOMⁱ	HOG000165710
HOVERGENⁱ	HBG000089
InParanoidⁱ	Q13509
KEGG Orthology (KO) More...KOⁱ	K07375
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G06U2
PhylomeDBⁱ	Q13509
TreeFamⁱ	TF300298

Family and domain databases

Gene3Dⁱ	1.10.287.600, 1 hit 3.30.1330.20, 1 hit 3.40.50.1440, 1 hit
InterProⁱ	View 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
PANTHERⁱ	PTHR11588 PTHR11588, 1 hit PTHR11588:SF256 PTHR11588:SF256, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00091 Tubulin, 1 hit PF03953 Tubulin_C, 1 hit
PRINTSⁱ	PR01163 BETATUBULIN PR01161 TUBULIN
SMARTⁱ	View protein in SMART SM00864 Tubulin, 1 hit SM00865 Tubulin_C, 1 hit
SUPFAMⁱ	SSF52490 SSF52490, 1 hit SSF55307 SSF55307, 1 hit
PROSITEⁱ	View protein in PROSITE PS00227 TUBULIN, 1 hit PS00228 TUBULIN_B_AUTOREG, 1 hit

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform 1 (identifier: Q13509-1) [UniParc]FASTA Add 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]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MDSVRSGAFG HLFRPDNFIF GQSGAGNNWA KGHYTEGAEL VDSVLDVVRK 
        60         70         80         90        100
ECENCDCLQG FQLTHSLGGG TGSGMGTLLI SKVREEYPDR IMNTFSVVPS 
       110        120        130        140        150
PKVSDTVVEP YNATLSIHQL VENTDETYCI DNEALYDICF RTLKLATPTY 
       160        170        180        190        200
GDLNHLVSAT MSGVTTSLRF PGQLNADLRK LAVNMVPFPR LHFFMPGFAP 
       210        220        230        240        250
LTARGSQQYR ALTVPELTQQ MFDAKNMMAA CDPRHGRYLT VATVFRGRMS 
       260        270        280        290        300
MKEVDEQMLA IQSKNSSYFV EWIPNNVKVA VCDIPPRGLK MSSTFIGNST 
       310        320        330        340        350
AIQELFKRIS EQFTAMFRRK AFLHWYTGEG MDEMEFTEAE SNMNDLVSEY 
       360        370 
QQYQDATAEE EGEMYEDDEE ESEAQGPK

Note: No experimental confirmation available.

Show »

Length:378

Mass (Da):42,433

Checksum:ⁱA190AB5B6264F2AB

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	275	A → R in AAC52035 (PubMed:9473684).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_062758	62	R → Q in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 PublicationCorresponds to variant dbSNP:rs864321714EnsemblClinVar.	1
Natural variantⁱVAR_066206	178	T → M in CDCBM1; can form tubulin heterodimers that are properly incorporated into microtubules; the microtubules are less stable than wild-type. 1 PublicationCorresponds to variant dbSNP:rs747480526EnsemblClinVar.	1
Natural variantⁱVAR_066207	205	E → 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 PublicationCorresponds to variant dbSNP:rs878853257EnsemblClinVar.	1
Natural variantⁱVAR_062759	262	R → C in CFEOM3A; affects heterodimers formation; affects microtubules polymerization and depolymerization rates. 1 PublicationCorresponds to variant dbSNP:rs267607162EnsemblClinVar.	1
Natural variantⁱVAR_062760	262	R → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures; affects microtubules polymerization and depolymerization rates. 1 PublicationCorresponds to variant dbSNP:rs864321716EnsemblClinVar.	1
Natural variantⁱVAR_062761	302	A → T in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 PublicationCorresponds to variant dbSNP:rs267607163EnsemblClinVar.	1
Natural variantⁱVAR_066208	302	A → V in CDCBM1; does not form tubulin heterodimers. 1 PublicationCorresponds to variant dbSNP:rs878853258Ensembl.	1
Natural variantⁱVAR_066209	323	M → V in CDCBM1; reduced heterodimers formation. 1 PublicationCorresponds to variant dbSNP:rs878853256Ensembl.	1
Natural variantⁱVAR_062762	380	R → C in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 PublicationCorresponds to variant dbSNP:rs864321717EnsemblClinVar.	1
Natural variantⁱVAR_062763	410	E → 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 PublicationCorresponds to variant dbSNP:rs267607165EnsemblClinVar.	1
Natural variantⁱVAR_062764	417	D → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures. 1 PublicationCorresponds to variant dbSNP:rs267607164EnsemblClinVar.	1
Natural variantⁱVAR_062765	417	D → 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 PublicationCorresponds to variant dbSNP:rs267607164EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_054659	1 – 72	Missing in isoform 2. 1 PublicationAdd BLAST		72

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS10988.1 [Q13509-1] CCDS56012.1 [Q13509-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_001184110.1, NM_001197181.1 [Q13509-2] NP_006077.2, NM_006086.3 [Q13509-1]
UniGeneⁱ	Hs.511743

Genome annotation databases

Ensemblⁱ	ENST00000315491; ENSP00000320295; ENSG00000258947 [Q13509-1] ENST00000554444; ENSP00000451617; ENSG00000258947 [Q13509-2]
GeneIDⁱ	10381
KEGGⁱ	hsa:10381
UCSC genome browser More...UCSCⁱ	uc002fph.2 human [Q13509-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length
Q13509	Tubulin beta-3 chain		BOVIN		450
Tubulin beta-3 chain		MACFA		450
Tubulin beta chain		MACMU		450
Tubulin beta chain		PONAB		450
Tubulin beta chain		PANTR		450
+33

Protein	Similar proteins		Species	Score	Length
Q13509	Tubulin beta-3 chain		BOVIN		450
Tubulin beta-3 chain		MACFA		450
Tubulin beta chain		MACMU		450
Tubulin beta chain		PONAB		450
Tubulin beta chain		PANTR		450
+33

Protein	Similar proteins		Species	Score	Length
Q13509	Tubulin beta-3 chain		BOVIN		450
Tubulin beta-3 chain		MACFA		450
Tubulin beta chain		MACMU		450
Tubulin beta chain		PONAB		450
Tubulin beta chain		PANTR		450
+50

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS10988.1 [Q13509-1] CCDS56012.1 [Q13509-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_001184110.1, NM_001197181.1 [Q13509-2] NP_006077.2, NM_006086.3 [Q13509-1]
UniGeneⁱ	Hs.511743

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	5IJ0	electron microscopy	3.80	B	1-426	[»]
	5IJ9	electron microscopy	3.70	B	1-426	[»]
	5JCO	electron microscopy	4.00	C/D/I/J/K/L	1-426	[»]
ProteinModelPortalⁱ	Q13509
SMRⁱ	Q13509
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	115654, 261 interactors
Database of interacting proteins More...DIPⁱ	DIP-31505N
IntActⁱ	Q13509, 147 interactors
Molecular INTeraction database More...MINTⁱ	Q13509
STRINGⁱ	9606.ENSP00000320295

Chemistry databases

ChEMBLⁱ	CHEMBL2597
Drug and drug target database More...DrugBankⁱ	DB05147 CYT997 DB03010 Epothilone B DB01873 Epothilone D DB04845 Ixabepilone DB06042 ZEN-012
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2752

PTM databases

iPTMnetⁱ	Q13509
PhosphoSitePlusⁱ	Q13509
SwissPalmⁱ	Q13509

Polymorphism and mutation databases

BioMutaⁱ	TUBB3
DMDMⁱ	20455526

2D gel databases

USC-OGP 2-DE database More...OGPⁱ	Q13509

OGPⁱ

Q13509

Proteomic databases

EPDⁱ	Q13509
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q13509
PaxDbⁱ	Q13509
PeptideAtlas More...PeptideAtlasⁱ	Q13509
PRIDEⁱ	Q13509
ProteomicsDBⁱ	59510
TopDownProteomicsⁱ	Q13509-1 [Q13509-1]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	10381
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000315491; ENSP00000320295; ENSG00000258947 [Q13509-1] ENST00000554444; ENSP00000451617; ENSG00000258947 [Q13509-2]
GeneIDⁱ	10381
KEGGⁱ	hsa:10381
UCSC genome browser More...UCSCⁱ	uc002fph.2 human [Q13509-1]

Organism-specific databases

CTDⁱ	10381
DisGeNET More...DisGeNETⁱ	10381
EuPathDBⁱ	HostDB:ENSG00000258947.6
GeneCardsⁱ	TUBB3
GeneReviewsⁱ	TUBB3
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:20772 TUBB3
Human Protein Atlas More...HPAⁱ	HPA043640 HPA046280
MalaCards human disease database More...MalaCardsⁱ	TUBB3
MIMⁱ	600638 phenotype 602661 gene 614039 phenotype
neXtProtⁱ	NX_Q13509
Open Targets More...OpenTargetsⁱ	ENSG00000258947
Orphanetⁱ	45358 Congenital fibrosis of extraocular muscles 300570 Cortical dysgenesis with pontocerebellar hypoplasia due to TUBB3 mutation
PharmGKBⁱ	PA134953867
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1375 Eukaryota COG5023 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000119061
HOGENOMⁱ	HOG000165710
HOVERGENⁱ	HBG000089
InParanoidⁱ	Q13509
KEGG Orthology (KO) More...KOⁱ	K07375
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G06U2
PhylomeDBⁱ	Q13509
TreeFamⁱ	TF300298

Enzyme and pathway databases

Reactomeⁱ	R-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
SIGNORⁱ	Q13509

Reactomeⁱ

R-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

SIGNORⁱ

Q13509

Miscellaneous databases

ChiTaRSⁱ	TUBB3 human
GeneWikiⁱ	TUBB3
GenomeRNAiⁱ	10381
Protein Ontology More...PROⁱ	PR:Q13509
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000258947
CleanExⁱ	HS_TUBB3 HS_TUBB4
ExpressionAtlasⁱ	Q13509 baseline and differential
Genevisibleⁱ	Q13509 HS

Family and domain databases

Gene3Dⁱ	1.10.287.600, 1 hit 3.30.1330.20, 1 hit 3.40.50.1440, 1 hit
InterProⁱ	View 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
PANTHERⁱ	PTHR11588 PTHR11588, 1 hit PTHR11588:SF256 PTHR11588:SF256, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00091 Tubulin, 1 hit PF03953 Tubulin_C, 1 hit
PRINTSⁱ	PR01163 BETATUBULIN PR01161 TUBULIN
SMARTⁱ	View protein in SMART SM00864 Tubulin, 1 hit SM00865 Tubulin_C, 1 hit
SUPFAMⁱ	SSF52490 SSF52490, 1 hit SSF55307 SSF55307, 1 hit
PROSITEⁱ	View protein in PROSITE PS00227 TUBULIN, 1 hit PS00228 TUBULIN_B_AUTOREG, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	TBB3_HUMAN
Accessionⁱ	Q13509Primary (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:	July 18, 2018
	This is version 180 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

Human chromosome 16
Human chromosome 16: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

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UniProtKB - Q13509 (TBB3_HUMAN)

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Tubulin beta-3 chain

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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Functionⁱ

GO - Molecular functionⁱ

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Names & Taxonomyⁱ

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Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

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