TUBB3 tubulin, beta 3 class III [Homo sapiens (human)] - Gene

Summary

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Official Symbol: TUBB3provided by HGNC
Official Full Name: tubulin, beta 3 class IIIprovided by HGNC
Primary source: HGNC:20772
See related: Ensembl:ENSG00000258947; HPRD:04044; MIM:602661; Vega:OTTHUMG00000138985
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: CDCBM; TUBB4; beta-4; CFEOM3A
Summary: This gene encodes a class III member of the beta tubulin protein family. Beta tubulins are one of two core protein families (alpha and beta tubulins) that heterodimerize and assemble to form microtubules. This protein is primarily expressed in neurons and may be involved in neurogenesis and axon guidance and maintenance. Mutations in this gene are the cause of congenital fibrosis of the extraocular muscles type 3. Alternate splicing results in multiple transcript variants. A pseudogene of this gene is found on chromosome 6. [provided by RefSeq, Oct 2010]

Genomic context

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Location :: 16q24.3

Sequence :: Chromosome: 16; NC_000016.9 (89988417..90002505)

See TUBB3 in Epigenomics, MapViewer

Chromosome 16 - NC_000016.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence

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Go to reference sequence details

Bibliography

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GeneRIFs: Gene References Into Functions What's a GeneRIF?

A novel syndrome caused by E410K amino acid substitution in TUBB3 is linked to Kallmann syndrome, cyclic vomiting and Moebius syndrome.
Title: A novel syndrome caused by the E410K amino acid substitution in the neuronal β-tubulin isotype 3.
In postoperative NSCLC patients who are receiving adjuvant chemotherapy, patients with high expression of beta-tubulin 3 tend to be resistant to taxane drugs.
Title: [Expression and predictive role of excision repair cross complementation group 1, ribonucleotide reductase subunit M1, and β-tubulin 3 in postoperative patients with non-small cell lung cancer receiving adjuvant chemotherapy].
negative REST and positive TUBB3 protein expression was detected as independent prognostic factors.
Title: Clinical implications of REST and TUBB3 in ovarian cancer and its relationship to paclitaxel resistance.
in colorectal cancer patients, there was a link between poor survival, the expression of TUBB3/TUBB6, and androgen receptor only in females
Title: Gender influences the class III and V β-tubulin ability to predict poor outcome in colorectal cancer.
High beta III-tubulin expression is associated with drug resistance to docetaxel in patients with advanced breast cancer.
Title: Expression of β-tubulin III and survivin in advance stage breast cancer correlates with chemotherapeutic effects of docetaxel.
Overexpression of betaIII-tubulin is associated with drug resistance to docetaxel-based chemotherapy in advanced gastric cancer.
Title: Overexpression of βIII-tubulin and survivin associated with drug resistance to docetaxel-based chemotherapy in advanced gastric cancer.
Higher levels of TUBB3 were detected in uterine carcinosarcoma (CS) cell lines and fresh frozen tissues when compared to ovarian CS and were associated with sensitivity to patupilone.
Title: Differential in vitro sensitivity to patupilone versus paclitaxel in uterine and ovarian carcinosarcoma cell lines is linked to tubulin-beta-III expression.
TUBB3 expression occurs in a cell cycle-dependent manner.
Title: Transcriptional and post-transcriptional regulation of βIII-tubulin protein expression in relation with cell cycle-dependent regulation of tumor cells.
Data suggest that the increased betaII- and betaIII-tubulin contributed significantly to the resistance phenotype.
Title: βII-tubulin and βIII-tubulin mediate sensitivity to peloruside A and laulimalide, but not paclitaxel or vinblastine, in human ovarian carcinoma cells.
The expression level of BRCA1 and class IIIbeta-tubulin in tumor tissue is probably a predictor for the efficacy of chemotherapy in non-small cell lung cancer patients.
Title: [The correlation between chemotherapeutic efficacy and breast cancer susceptibility gene 1 and class IIIβ-tubulin protein expression in non-small cell lung cancer patients].

Submit: New GeneRIF Correction See all (52)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Congenital Fibrosis of the Extraocular Muscles 1B

Genetic Testing Registry

Summary from GeneReviews: Congenital Fibrosis of the Extraocular Muscles

Congenital fibrosis of the extraocular muscles (CFEOM) refers to at least seven genetically defined strabismus syndromes: CFEOM1A, CFEOM1B, CFEOM2, CFEOM3A, CFEOM3B, CFEOM3C, and Tukel syndrome, characterized by congenital non-progressive ophthalmoplegia (inability to move the eyes) with or without ptosis (droopy eyelids) affecting part or all of the oculomotor nucleus and nerve (cranial nerve III) and its innervated muscles (superior, medial, and inferior recti, inferior oblique, and levator palpabrae superioris) and/or the trochlear nucleus and nerve (cranial nerve IV) and its innervated muscle (the superior oblique). In general, affected individuals have severe limitation of vertical gaze (usually upgaze) and variable limitation of horizontal gaze. Individuals with CFEOM frequently compensate for the ophthalmoplegia by maintaining abnormal head positions at rest and by moving their heads rather than their eyes to track objects. Individuals with CFEOM3A may also have intellectual disability, social disability, facial weakness, and/or a progressive axonal peripheral neuropathy (a form of Charcot-Marie-Tooth disease). Individuals with CFEOM3C also have intellectual disability and facial dysmorphism reminiscent of Albright hereditary osteodystrophy-like syndrome. Individuals with Tukel syndrome also have postaxial oligodactyly or oligosyndactyly of the hands.

Diagnosis Testing

The diagnosis of CFEOM is based on ophthalmologic findings, and some subtypes depend on the identification of associated findings. Three CFEOM ophthalmic phenotypes are recognized: CFEOM1, CFEOM2, and CFEOM3. KIF21A mutations are associated with most familial CFEOM1, simplex CFEOM1, and CFEOM3B. PHOX2A mutations are associated with CFEOM2. TUBB3 mutations are associated with CFEOM3A and, rarely, CFEOM1B. Molecular genetic testing of TUBB3, KIF21A, and PHOX2A is available on a clinical basis. Linkage to the CFEOM3C and Tukel syndrome loci is available on a research basis only.

Genetic Counseling

CFEOM1A, CFEOM1B, and CFEOM3A, B, and C are inherited in an autosomal dominant manner. Probands may have inherited the disease-causing mutation or have a de novo mutation. Each child of an individual with CFEOM1 or CFEOM3 has a 50% chance of inheriting the condition. CFEOM1 and CFEOM3A can also result from germline mosaicism in one parent, resulting in more than one affected offspring of unaffected parents. CFEOM2 and Tukel syndrome are inherited in an autosomal recessive manner. At conception, each sib of an individual with CFEOM2 or Tukel syndrome has a 25% chance of being affected, a 50% chance of being an asymptomatic carrier, and a 25% chance of being unaffected and not a carrier. Prenatal diagnosis for pregnancies at risk for some types of CFEOM is possible if the mutation has been identified in an affected family member. Prenatal testing for other forms of congenital fibrosis of the extraocular muscles may be available through laboratories offering custom prenatal mutation analysis for families in which the disease-causing mutation(s) have been identified.

References

PMID: 20301522

Cortical dysplasia, complex, with other brain malformations

MIM: 614039

Genetic Testing Registry

Fibrosis of extraocular muscles, congenital, 3a, with or without extraocular involvement

MIM: 600638

Genetic Testing Registry

Summary from GeneReviews: Congenital Fibrosis of the Extraocular Muscles

Disease Characteristics

Congenital fibrosis of the extraocular muscles (CFEOM) refers to at least seven genetically defined strabismus syndromes: CFEOM1A, CFEOM1B, CFEOM2, CFEOM3A, CFEOM3B, CFEOM3C, and Tukel syndrome, characterized by congenital non-progressive ophthalmoplegia (inability to move the eyes) with or without ptosis (droopy eyelids) affecting part or all of the oculomotor nucleus and nerve (cranial nerve III) and its innervated muscles (superior, medial, and inferior recti, inferior oblique, and levator palpabrae superioris) and/or the trochlear nucleus and nerve (cranial nerve IV) and its innervated muscle (the superior oblique). In general, affected individuals have severe limitation of vertical gaze (usually upgaze) and variable limitation of horizontal gaze. Individuals with CFEOM frequently compensate for the ophthalmoplegia by maintaining abnormal head positions at rest and by moving their heads rather than their eyes to track objects. Individuals with CFEOM3A may also have intellectual disability, social disability, facial weakness, and/or a progressive axonal peripheral neuropathy (a form of Charcot-Marie-Tooth disease). Individuals with CFEOM3C also have intellectual disability and facial dysmorphism reminiscent of Albright hereditary osteodystrophy-like syndrome. Individuals with Tukel syndrome also have postaxial oligodactyly or oligosyndactyly of the hands.

Diagnosis Testing

The diagnosis of CFEOM is based on ophthalmologic findings, and some subtypes depend on the identification of associated findings. Three CFEOM ophthalmic phenotypes are recognized: CFEOM1, CFEOM2, and CFEOM3. KIF21A mutations are associated with most familial CFEOM1, simplex CFEOM1, and CFEOM3B. PHOX2A mutations are associated with CFEOM2. TUBB3 mutations are associated with CFEOM3A and, rarely, CFEOM1B. Molecular genetic testing of TUBB3, KIF21A, and PHOX2A is available on a clinical basis. Linkage to the CFEOM3C and Tukel syndrome loci is available on a research basis only.

Genetic Counseling

CFEOM1A, CFEOM1B, and CFEOM3A, B, and C are inherited in an autosomal dominant manner. Probands may have inherited the disease-causing mutation or have a de novo mutation. Each child of an individual with CFEOM1 or CFEOM3 has a 50% chance of inheriting the condition. CFEOM1 and CFEOM3A can also result from germline mosaicism in one parent, resulting in more than one affected offspring of unaffected parents. CFEOM2 and Tukel syndrome are inherited in an autosomal recessive manner. At conception, each sib of an individual with CFEOM2 or Tukel syndrome has a 25% chance of being affected, a 50% chance of being an asymptomatic carrier, and a 25% chance of being unaffected and not a carrier. Prenatal diagnosis for pregnancies at risk for some types of CFEOM is possible if the mutation has been identified in an affected family member. Prenatal testing for other forms of congenital fibrosis of the extraocular muscles may be available through laboratories offering custom prenatal mutation analysis for families in which the disease-causing mutation(s) have been identified.

References

PMID: 20301522

HIV-1 protein interactions

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Protein	Gene	Interaction	Pubs
Env, gp160, envelope glycoprotein	env	Treatment of cells with actin-depolymerizing agents or tubulin polymerization inhibitors largely reduces the percentage of cells with capped HIV-1 Gag and Env, indicating an intact actin and tubulin cytoskeleton is required for efficient assembly of HIV-1	PubMed
Gag, Pr55	gag	Treatment of cells with actin-depolymerizing agents or tubulin polymerization inhibitors largely reduces the percentage of cells with capped HIV-1 Gag and Env, indicating an intact actin and tubulin cytoskeleton is required for efficient assembly of HIV-1	PubMed
Rev, p19	rev	HIV-1 Rev interacting protein, TUBB3, is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells	PubMed
	rev	Rev acts to depolymerize microtubules that are formed by tubulin, an effect that is observed during HIV-1 infection	PubMed
Tat, p14	tat	In Jurkat cells expressing HIV-1 Tat, decreased expression levels are found for basic cytoskeletal proteins such as actin, beta-tubulin, annexin, cofilin, gelsolin, and Rac/Rho-GDI complex	PubMed
	tat	HIV-1 Tat (specifically, amino acids 38-72), enhances tubulin polymerization and triggers the mitochondrial pathway to induce T cell apoptosis as shown in vitro by the release of cytochrome c from isolated mitochondria	PubMed
	tat	HIV-1 Tat (amino acids 36-39) binds tubulin alpha/beta dimers and polymerized microtubules leading to the alteration of microtubule dynamics and activation of a mitochondria-dependent apoptotic pathway that is facilitated by the Bcl-2 relative Bim	PubMed
Vpr, p15	vpr	Concurrent exposure of HIV-1 Vpr with HCV core protein causes significantly increased human fetal neuron (HFN) injury, as indicated by reduced beta-III-tubulin, than HFN treated with HIV-1 Vpr alone	PubMed

Go to the HIV-1, Human Protein Interaction Database

Interactions

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Products	Interactant	Other Gene	Source	Pubs	Description
Q13509	Q14155	ARHGEF7	HPRD	PubMed
Q13509	KIAA1543 protein	CAMSAP3	HPRD	PubMed
Q13509	Q13838	DDX39B	HPRD	PubMed
Q13509	P26641	EEF1G	HPRD	PubMed
Q13509	O95166	GABARAP	HPRD	PubMed
Q13509	Hexosaminidase (glycosyl hydrolase family 20, catalytic domain) containing	HEXDC	HPRD	PubMed
Q13509	Q01101	INSM1	HPRD	PubMed
Q13509	Q07666	KHDRBS1	HPRD	PubMed
Q13509	Q15012	LAPTM4A	HPRD	PubMed
Q13509	P18858	LIG1	HPRD	PubMed
Q13509	Q13084	MRPL28	HPRD	PubMed
Q13509	Pleckstrin homology domain interacting protein	PHIP	HPRD	PubMed
Q13509	Hypothetical protein MGC7036	RILPL2	HPRD	PubMed
Q13509	Q9Y6N7	ROBO1	HPRD	PubMed
Q13509	KIAA0746	SEL1L3	HPRD	PubMed
Q13509	Q969W0	SPTSSA	HPRD	PubMed
Q13509	P02787	TF	HPRD	PubMed
BioGRID:115654	BioGRID:106557	ACAT2	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:106807	ANXA7	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:107587	AP2M1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:114393	ARHGEF7	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:106902	ARRB2	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:122917	CAMKMT	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:107279	CAPZA1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:107282	CAPZB	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:107460	CDKN1A	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:107788	CRK	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:114030	CUL3	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:113649	DDX39B	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:108118	DYNC1I1	BioGRID	PubMed	Affinity Capture-Western
BioGRID:115654	BioGRID:108257	EEF1G	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:108309	ELAVL1	BioGRID	PubMed	Affinity Capture-RNA
BioGRID:115654	BioGRID:108403	ESR1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:575703	FAM86B2	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:117646	FBXO25	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:116465	GABARAP	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:109258	GZMK	BioGRID	PubMed	Biochemical Activity
BioGRID:115654	BioGRID:129726	HEXDC	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:109848	INPPL1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:109853	INSM1	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:115015	IQCB1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:115900	KHDRBS1	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:115089	LAPTM4A	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:121008	LIN37	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:110185	LMAN1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:116804	MDN1	BioGRID	PubMed	Co-fractionation
BioGRID:115654	BioGRID:117403	METTL21B	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:122744	METTL21D	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:122539	METTL22	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:125870	METTL23	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:115824	MRPL28	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:110584	MSN	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:119722	MST4	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:114522	PAPSS1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:111218	PEX14	BioGRID	PubMed	Co-purification
BioGRID:115654	BioGRID:120353	PHIP	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:111362	PLK1	BioGRID	PubMed	Affinity Capture-Western; Reconstituted Complex
BioGRID:115654	BioGRID:111852	RARS	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:107529	RCC1	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:128200	RILPL2	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:112018	ROBO1	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:116836	SEL1L3	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:112361	SHC1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:112490	SMN1	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:112550	SP1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:128143	SPTSSA	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:112657	STAU1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:113188	SUMO1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:112872	TERF1	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:112876	TF	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:112938	TK1	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:113031	TPTE	BioGRID	PubMed	Two-hybrid
BioGRID:115654	BioGRID:113603	TUBA1A	BioGRID	PubMed	Co-fractionation
BioGRID:115654	BioGRID:115651	TUBA1B	BioGRID	PubMed	Co-fractionation
BioGRID:115654	BioGRID:124259	TUBA1C	BioGRID	PubMed	Co-fractionation
BioGRID:115654	BioGRID:113128	TUBA4A	BioGRID	PubMed	Co-fractionation
BioGRID:115654	BioGRID:113164	UBC	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:113257	VCL	BioGRID	PubMed	Affinity Capture-MS
BioGRID:115654	BioGRID:1205542	rev	BioGRID	PubMed	Affinity Capture-MS

Pathways from BioSystems

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Chaperonin-mediated protein folding, organism-specific biosystem (from REACTOME)
Chaperonin-mediated protein folding, organism-specific biosystemThe eukaryotic chaperonin TCP-1 ring complex (TRiC/ CCT) plays an essential role in the folding of a subset of proteins prominent among which are the actins and tubulins (reviewed in Altschuler and...
Class A/1 (Rhodopsin-like receptors), organism-specific biosystem (from REACTOME)
Class A/1 (Rhodopsin-like receptors), organism-specific biosystemRhodopsin-like receptors (class A/1) are the largest group of GPCRs and are the best studied group from a functional and structural point of view. They show great diversity at the sequence level and ...
Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding, organism-specific biosystem (from REACTOME)
Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding, organism-specific biosystemIn the case of actin and tubulin folding, and perhaps other substrates, the emerging polypeptide chain is transferred from the ribosome to TRiC via Prefoldin (Vainberg et al., 1998).
Diurnally regulated genes with circadian orthologs, organism-specific biosystem (from WikiPathways)
Diurnally regulated genes with circadian orthologs, organism-specific biosystemHuman genes regulated in the diurnal comparison with orthologues that display circadian regulation in mouse heart and liver (Panda 2002, Storch 2002), and SCN (Panda 2002). The 608 significantly regu...
Formation of tubulin folding intermediates by CCT/TriC, organism-specific biosystem (from REACTOME)
Formation of tubulin folding intermediates by CCT/TriC, organism-specific biosystemTriC/CCT forms a binary complex with unfolded alpha- or beta-tubulin (Frydman et al., 1992; Gao et al., 1993). The tubulin folding intermediates produced by TriC are unstable (Gao et al., 1993). Fiv...
G alpha (s) signalling events, organism-specific biosystem (from REACTOME)
G alpha (s) signalling events, organism-specific biosystemThe general function of the G alpha (s) subunit (Gs) is to activate adenylate cyclase, which in turn produces cAMP, leading to the activation of cAMP-dependent protein kinases (often referred to col...
GPCR downstream signaling, organism-specific biosystem (from REACTOME)
GPCR downstream signaling, organism-specific biosystemG protein-coupled receptors (GPCRs) are classically defined as the receptor, G-protein and downstream effectors, the alpha subunit of the G-protein being the primary signaling molecule. However, it h...
GPCR ligand binding, organism-specific biosystem (from REACTOME)
GPCR ligand binding, organism-specific biosystemThere are more than 800 G-protein coupled receptor (GPCRs) in the human genome, making it the largest receptor superfamily. GPCRs are also the largest class of drug targets, involved in virtually all...
Gap junction, organism-specific biosystem (from KEGG)
Gap junction, organism-specific biosystemGap junctions contain intercellular channels that allow direct communication between the cytosolic compartments of adjacent cells. Each gap junction channel is formed by docking of two 'hemichannels'...
Gap junction, conserved biosystem (from KEGG)
Gap junction, conserved biosystemGap junctions contain intercellular channels that allow direct communication between the cytosolic compartments of adjacent cells. Each gap junction channel is formed by docking of two 'hemichannels'...
Metabolism of proteins, organism-specific biosystem (from REACTOME)
Metabolism of proteins, organism-specific biosystemProtein metabolism comprises the pathways of translation, post-translational modification and protein folding.
Parkin-Ubiquitin Proteasomal System pathway, organism-specific biosystem (from WikiPathways)
Parkin-Ubiquitin Proteasomal System pathway, organism-specific biosystemThis pathway describes the Parkin-Ubiquitin proteasome degradation system.
Pathogenic Escherichia coli infection, organism-specific biosystem (from KEGG)
Pathogenic Escherichia coli infection, organism-specific biosystemEnteropathogenic E. coli (EPEC) and enterohemorrhagic E. coli (EHEC) are closely related pathogenic strains of Escherichia coli. The hallmark of EPEC/EHEC infections [DS:H00278 H00277] is induction o...
Pathogenic Escherichia coli infection, organism-specific biosystem (from WikiPathways)
Pathogenic Escherichia coli infection, organism-specific biosystemSources: [http://www.genome.jp/kegg/pathway/hsa/hsa05130.html KEGG]
Pathogenic Escherichia coli infection, conserved biosystem (from KEGG)
Pathogenic Escherichia coli infection, conserved biosystemEnteropathogenic E. coli (EPEC) and enterohemorrhagic E. coli (EHEC) are closely related pathogenic strains of Escherichia coli. The hallmark of EPEC/EHEC infections [DS:H00278 H00277] is induction o...
Peptide ligand-binding receptors, organism-specific biosystem (from REACTOME)
Peptide ligand-binding receptors, organism-specific biosystemThese receptors, a subset of the Class A/1 (Rhodopsin-like) family, all bind peptide ligands which include the chemokines, opioids and somatostatins.
Phagosome, organism-specific biosystem (from KEGG)
Phagosome, organism-specific biosystemPhagocytosis is the process of taking in relatively large particles by a cell, and is a central mechanism in the tissue remodeling, inflammation, and defense against infectious agents. A phagosome is...
Phagosome, conserved biosystem (from KEGG)
Phagosome, conserved biosystemPhagocytosis is the process of taking in relatively large particles by a cell, and is a central mechanism in the tissue remodeling, inflammation, and defense against infectious agents. A phagosome is...
Post-chaperonin tubulin folding pathway, organism-specific biosystem (from REACTOME)
Post-chaperonin tubulin folding pathway, organism-specific biosystemAlpha and beta tubulin folding intermediates are formed through ATPâ??dependent interaction with TriC/CCT. In order to form a functional heterodimer, these folding intermediates undergo a series of...
Prefoldin mediated transfer of substrate to CCT/TriC, organism-specific biosystem (from REACTOME)
Prefoldin mediated transfer of substrate to CCT/TriC, organism-specific biosystemUnfolded actins and tubulins bound to prefoldin are transferred to CCT via a docking mechanism (McCormack and Willison, 2001).
Protein folding, organism-specific biosystem (from REACTOME)
Protein folding, organism-specific biosystemDue to the crowded envirnoment within the cell, many proteins must interact with molecular chaperones to attain their native conformation (reviewed in Young et al., 2004). Chaperones recognize and...
Signal Transduction, organism-specific biosystem (from REACTOME)
Signal Transduction, organism-specific biosystemSignal transduction is a process in which extracellular signals elicit changes in cell state and activity. Transmembrane receptors sense changes in the cellular environment by binding ligands, such a...
Signaling by GPCR, organism-specific biosystem (from REACTOME)
Signaling by GPCR, organism-specific biosystemG protein-coupled receptors (GPCRs; 7TM receptors; seven transmembrane domain receptors; heptahelical receptors; G protein-linked receptors [GPLR]) are the largest family of transmembrane receptors i...

General gene information

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Markers

PMC156124P3 (e-PCR)
- UniSTS:271361

GDB:312714 (e-PCR)
- UniSTS:156429

MARC_24021-24022:1029778648:1 (e-PCR)
- UniSTS:268829

RH65809 (e-PCR)
- UniSTS:52004

SHGC-60611 (e-PCR)
- UniSTS:54588

RH65263 (e-PCR)
- UniSTS:48263

Genotypes

Related pseudogene(s)

2 found Review record(s) in Gene

Potential readthrough

Included gene: MC1R

Homology

Homologs of the TUBB3 gene: The TUBB3 gene is conserved in chimpanzee, cow, mouse, rat, and chicken.
Map Viewer (Mouse, Rat)
OrthoDB: The Hierarchical Catalog of Eukaryotic Orthologs

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
GTP binding	IEA Inferred from Electronic Annotation more info
GTPase activity	IEA Inferred from Electronic Annotation more info
peptide binding	IEA Inferred from Electronic Annotation more info
structural constituent of cytoskeleton	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
'de novo' posttranslational protein folding	TAS Traceable Author Statement more info
axon guidance	IMP Inferred from Mutant Phenotype more info
cellular protein metabolic process	TAS Traceable Author Statement more info
microtubule-based process	IEA Inferred from Electronic Annotation more info
mitosis	IEA Inferred from Electronic Annotation more info
protein folding	TAS Traceable Author Statement more info
protein polymerization	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
axon	IEA Inferred from Electronic Annotation more info
cytoplasm	IDA Inferred from Direct Assay more info
microtubule	IDA Inferred from Direct Assay more info
microtubule cytoskeleton	IDA Inferred from Direct Assay more info
plasma membrane	IDA Inferred from Direct Assay more info

General protein information

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Preferred Names: tubulin beta-3 chain

Names: tubulin beta-3 chain; tubulin beta-III; tubulin beta-4 chain; class III beta-tubulin

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

NG_027810.1 RefSeqGene

Range

5001..19089

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001197181.1 → NP_001184110.1 tubulin beta-3 chain isoform 2

Status: REVIEWED

Description

Transcript Variant: This variant (2) differs in the 5' UTR, lacks a portion of the 5' coding region, and initiates translation at a downstream start codon, compared to variant 1. The encoded isoform (2) is shorter at the N-terminus, compared to isoform 1.

Source sequence(s)

AC092143, AK292219, BC003021

Consensus CDS

CCDS56012.1

UniProtKB/TrEMBL

A8K854

UniProtKB/Swiss-Prot

Q13509

Related

ENSP00000451617, OTTHUMP00000245288, ENST00000554444, OTTHUMT00000412017

Conserved Domains (2) summary

pfam03953
Location:189 – 311
Blast Score: 556

Tubulin_C; Tubulin C-terminal domain

pfam00091
Location:12 – 152
Blast Score: 316

Tubulin; Tubulin/FtsZ family, GTPase domain
NM_006086.3 → NP_006077.2 tubulin beta-3 chain isoform 1

Status: REVIEWED

Description

Transcript Variant: This variant (1) encodes the longest isoform (1).

Source sequence(s)

AK223039, BC003021, DA054466

Consensus CDS

CCDS10988.1

UniProtKB/Swiss-Prot

Q13509

UniProtKB/TrEMBL

Q53G92

Related

ENSP00000320295, OTTHUMP00000176846, ENST00000315491, OTTHUMT00000272874

Conserved Domains (2) summary

cd02187
Location:2 – 426
Blast Score: 2395

beta_tubulin; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of ...

PLN00220
Location:1 – 426
Blast Score: 2283

PLN00220; tubulin beta chain; Provisional

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 104

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh37.p10 Primary Assembly

Genomic

NC_000016.9 Reference GRCh37.p10 Primary Assembly

Range

89988417..90002505

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Alternate HuRef

Genomic

AC_000148.1 Alternate HuRef

Range

75681526..75695522

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Alternate CHM1_1.0

Genomic

NC_018927.1 Alternate CHM1_1.0

Range

90984704..90999076

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Nucleotide		Protein
Heading	Accession and Version	Protein
genomic	ABBA01014120.1	None
genomic	ABBA01014121.1	None
genomic	ABBA01014122.1	None
genomic	AC092143.4 (50396..63156)	None
genomic	AMYH01007941.1 (12836..27208)	None
genomic	CH471184.2	EAW66669.1
		EAW66674.1
		EAW66675.1
mRNA	AF427491.3	AAL28094.1
mRNA	AK058140.1	None
mRNA	AK122757.1	BAG53710.1
mRNA	AK127418.1	None
mRNA	AK223039.1	BAD96759.1
mRNA	AK292219.1	BAF84908.1
mRNA	AK307201.1	None
mRNA	AK314616.1	BAG37182.1
mRNA	AU142509.1	None
mRNA	BC000748.2	AAH00748.1
mRNA	BC001678.2	AAH01678.2
mRNA	BC003021.1	AAH03021.2
mRNA	BC047518.1	AAH47518.1
mRNA	BC064975.1	None
mRNA	CD621827.1	None
mRNA	DA054466.1	None
mRNA	S62643.1	None
mRNA	U47634.1	AAC52035.1