TUBB

Protein-coding gene in the species Homo sapiens

TUBB

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
3QNZ, 3QO0

Identifiers

Aliases

TUBB, CDCBM6, M40, OK/SW-cl.56, TUBB1, TUBB5, CSCSC1, tubulin beta class I

External IDs

OMIM: 191130; MGI: 107812; HomoloGene: 69099; GeneCards: TUBB; OMA:TUBB - orthologs

Gene location (Human)

Chr.	Chromosome 6 (human)^[1]

Band	6p21.33	Start	30,717,435 bp^[1]
Band	6p21.33	End	30,725,538 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 17 (mouse)^[2]

Band	17\|17 B1	Start	36,144,813 bp^[2]
Band	17\|17 B1	End	36,149,198 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

ganglionic eminence

smooth muscle tissue

stromal cell of endometrium

appendix

ovary

islet of Langerhans

placenta

lymph node

myometrium

gallbladder

Top expressed in

medial ganglionic eminence

saccule

otic placode

maxillary prominence

primitive streak

somite

hand

abdominal wall

dermis

internal carotid artery

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	GTPase activating protein binding nucleotide binding protein domain specific binding protein-containing complex binding GTP binding structural molecule activity structural constituent of cytoskeleton protein binding GTPase activity MHC class I protein binding ubiquitin protein ligase binding
Cellular component	cell body extracellular region nuclear envelope lumen cytoplasmic ribonucleoprotein granule extracellular exosome extracellular matrix microtubule cytoskeleton nucleus microtubule cytoskeleton azurophil granule lumen cytoplasm membrane raft protein-containing complex
Biological process	cytoskeleton-dependent intracellular transport spindle assembly cell division G2/M transition of mitotic cell cycle cellular process natural killer cell mediated cytotoxicity microtubule-based process neutrophil degranulation ciliary basal body-plasma membrane docking regulation of G2/M transition of mitotic cell cycle microtubule cytoskeleton organization mitotic cell cycle regulation of synapse organization cytoskeleton organization
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


203068


22154

Ensembl

ENSG00000196230 ENSG00000232421 ENSG00000183311 ENSG00000224156 ENSG00000235067
ENSG00000232575 ENSG00000227739 ENSG00000229684


ENSMUSG00000001525

UniProt


P07437 Q5SU16


P99024

RefSeq (mRNA)

NM_001293212 NM_001293213 NM_001293214 NM_001293215 NM_001293216
NM_178014


NM_011655

RefSeq (protein)

NP_001280141 NP_001280142 NP_001280143 NP_001280144 NP_001280145
NP_821133 NP_821133.1


NP_035785

Location (UCSC)

Chr 6: 30.72 – 30.73 Mb

Chr 17: 36.14 – 36.15 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Tubulin beta chain is a protein that in humans is encoded by the TUBB gene.^[5]^[6]^[7]

Interactions

TUBB has been shown to interact with NCOA6^[8] and SYT9.^[9]

References

^ ^a ^b ^c ENSG00000232421, ENSG00000183311, ENSG00000224156, ENSG00000235067, ENSG00000232575, ENSG00000227739, ENSG00000229684 GRCh38: Ensembl release 89: ENSG00000196230, ENSG00000232421, ENSG00000183311, ENSG00000224156, ENSG00000235067, ENSG00000232575, ENSG00000227739, ENSG00000229684 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000001525 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Crabtree DV, Ojima I, Geng X, Adler AJ (Aug 2001). "Tubulins in the primate retina: evidence that xanthophylls may be endogenous ligands for the paclitaxel-binding site". Bioorganic & Medicinal Chemistry. 9 (8): 1967–76. doi:10.1016/S0968-0896(01)00103-1. PMID 11504633.
^ Volz A, Weiss E, Trowsdale J, Ziegler A (Jan 1994). "Presence of an expressed beta-tubulin gene (TUBB) in the HLA class I region may provide the genetic basis for HLA-linked microtubule dysfunction". Human Genetics. 93 (1): 42–6. doi:10.1007/BF00218911. PMID 8270253. S2CID 7853030.
^ "Entrez Gene: TUBB tubulin, beta".
^ Goo YH, Sohn YC, Kim DH, Kim SW, Kang MJ, Jung DJ, Kwak E, Barlev NA, Berger SL, Chow VT, Roeder RG, Azorsa DO, Meltzer PS, Suh PG, Song EJ, Lee KJ, Lee YC, Lee JW (Jan 2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Molecular and Cellular Biology. 23 (1): 140–9. doi:10.1128/MCB.23.1.140-149.2003. PMC 140670. PMID 12482968.
^ Haberman Y, Grimberg E, Fukuda M, Sagi-Eisenberg R (Nov 2003). "Synaptotagmin IX, a possible linker between the perinuclear endocytic recycling compartment and the microtubules". Journal of Cell Science. 116 (Pt 21): 4307–18. doi:10.1242/jcs.00719. PMID 12966166.

Berrieman HK, Lind MJ, Cawkwell L (Mar 2004). "Do beta-tubulin mutations have a role in resistance to chemotherapy?". The Lancet. Oncology. 5 (3): 158–64. doi:10.1016/S1470-2045(04)01411-1. PMID 15003198.
Horisberger MA (Aug 1992). "Interferon-induced human protein MxA is a GTPase which binds transiently to cellular proteins". Journal of Virology. 66 (8): 4705–9. doi:10.1128/JVI.66.8.4705-4709.1992. PMC 241296. PMID 1629950.
Wang D, Villasante A, Lewis SA, Cowan NJ (Nov 1986). "The mammalian beta-tubulin repertoire: hematopoietic expression of a novel, heterologous beta-tubulin isotype". The Journal of Cell Biology. 103 (5): 1903–10. doi:10.1083/jcb.103.5.1903. PMC 2114403. PMID 3782288.
Lee MG, Lewis SA, Wilde CD, Cowan NJ (Jun 1983). "Evolutionary history of a multigene family: an expressed human beta-tubulin gene and three processed pseudogenes". Cell. 33 (2): 477–87. doi:10.1016/0092-8674(83)90429-4. PMID 6688039.
Hall JL, Dudley L, Dobner PR, Lewis SA, Cowan NJ (May 1983). "Identification of two human beta-tubulin isotypes". Molecular and Cellular Biology. 3 (5): 854–62. doi:10.1128/mcb.3.5.854. PMC 368608. PMID 6865944.
Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Apr 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (Apr 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
Kinnunen T, Kaksonen M, Saarinen J, Kalkkinen N, Peng HB, Rauvala H (Apr 1998). "Cortactin-Src kinase signaling pathway is involved in N-syndecan-dependent neurite outgrowth". The Journal of Biological Chemistry. 273 (17): 10702–8. doi:10.1074/jbc.273.17.10702. PMID 9553134.
Niethammer M, Valtschanoff JG, Kapoor TM, Allison DW, Weinberg RJ, Craig AM, Sheng M (Apr 1998). "CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90". Neuron. 20 (4): 693–707. doi:10.1016/S0896-6273(00)81009-0. PMID 9581762. S2CID 16068361.
Rasmussen RK, Ji H, Eddes JS, Moritz RL, Reid GE, Simpson RJ, Dorow DS (May 1998). "Two-dimensional electrophoretic analysis of mixed lineage kinase 2 N-terminal domain binding proteins". Electrophoresis. 19 (5): 809–17. doi:10.1002/elps.1150190535. PMID 9629920. S2CID 21204230.
Ciruela F, Robbins MJ, Willis AC, McIlhinney RA (Jan 1999). "Interactions of the C terminus of metabotropic glutamate receptor type 1alpha with rat brain proteins: evidence for a direct interaction with tubulin". Journal of Neurochemistry. 72 (1): 346–54. doi:10.1046/j.1471-4159.1999.0720346.x. PMID 9886087. S2CID 3923065.
Chau MF, Radeke MJ, de Inés C, Barasoain I, Kohlstaedt LA, Feinstein SC (Dec 1998). "The microtubule-associated protein tau cross-links to two distinct sites on each alpha and beta tubulin monomer via separate domains". Biochemistry. 37 (51): 17692–703. doi:10.1021/bi9812118. PMID 9922135.
Piredda L, Farrace MG, Lo Bello M, Malorni W, Melino G, Petruzzelli R, Piacentini M (Feb 1999). "Identification of 'tissue' transglutaminase binding proteins in neural cells committed to apoptosis". FASEB Journal. 13 (2): 355–64. doi:10.1096/fasebj.13.2.355. PMID 9973324. S2CID 16417170.
Feng Y, Hodge DR, Palmieri G, Chase DL, Longo DL, Ferris DK (Apr 1999). "Association of polo-like kinase with alpha-, beta- and gamma-tubulins in a stable complex". The Biochemical Journal. 339 (2): 435–42. doi:10.1042/0264-6021:3390435. PMC 1220175. PMID 10191277.
Martín L, Fanarraga ML, Aloria K, Zabala JC (Mar 2000). "Tubulin folding cofactor D is a microtubule destabilizing protein". FEBS Letters. 470 (1): 93–5. Bibcode:2000FEBSL.470...93M. doi:10.1016/S0014-5793(00)01293-X. PMID 10722852. S2CID 35012741.
Tarazona R, López-Lluch G, Galiani MD, Aguado E, Barahona F, Solana R, Peña J (Dec 2000). "HLA-B2702 (77-83/83-77) peptide binds to beta-tubulin on human NK cells and blocks their cytotoxic capacity". Journal of Immunology. 165 (12): 6776–82. doi:10.4049/jimmunol.165.12.6776. PMID 11120798.
Bonnet C, Boucher D, Lazereg S, Pedrotti B, Islam K, Denoulet P, Larcher JC (Apr 2001). "Differential binding regulation of microtubule-associated proteins MAP1A, MAP1B, and MAP2 by tubulin polyglutamylation". The Journal of Biological Chemistry. 276 (16): 12839–48. doi:10.1074/jbc.M011380200. PMID 11278895.
Ivings L, Pennington SR, Jenkins R, Weiss JL, Burgoyne RD (May 2002). "Identification of Ca2+-dependent binding partners for the neuronal calcium sensor protein neurocalcin delta: interaction with actin, clathrin and tubulin". The Biochemical Journal. 363 (Pt 3): 599–608. doi:10.1042/0264-6021:3630599. PMC 1222513. PMID 11964161.

PDB gallery

1ffx: TUBULIN:STATHMIN-LIKE DOMAIN COMPLEX
1ia0: KIF1A HEAD-MICROTUBULE COMPLEX STRUCTURE IN ATP-FORM
1jff: Refined structure of alpha-beta tubulin from zinc-induced sheets stabilized with taxol
1sa0: TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX
1sa1: Tubulin-podophyllotoxin: stathmin-like domain complex
1tub: TUBULIN ALPHA-BETA DIMER, ELECTRON DIFFRACTION
1tvk: The binding mode of epothilone A on a,b-tubulin by electron crystallography
1z2b: Tubulin-colchicine-vinblastine: stathmin-like domain complex
2hxf: KIF1A head-microtubule complex structure in amppnp-form
2hxh: KIF1A head-microtubule complex structure in adp-form

Proteins of the cytoskeleton

Human

Microfilaments
and ABPs

Myofilament

Actins	A1 A2 B C1 G1 G2
Myosins	I MYO1A MYO1B MYO1C MYO1D MYO1E MYO1F MYO1G MYO1H) II MYH1 MYH2 MYH3 MYH4 MYH6 MYH7 MYH7B MYH8 MYH9 MYH10 MYH11 MYH13 MYH14 MYH15 MYH16 III MYO3A MYO3B V MYO5A MYO5B MYO5C VI MYO6 VII MYO7A MYO7B IX MYO9A MYO9B X MYO10 XV MYO15A XVIII MYO18A MYO18B LC MYL1 MYL2 MYL3 MYL4 MYL5 MYL6 MYL6B MYL7 MYL9 MYLIP MYLK MYLK2 MYLL1
Other	Tropomodulin 1 2 3 4 Troponin T 1 2 3 C 1 2 I 1 2 3 Tropomyosin 1 2 3 4 Actinin 1 2 3 4 Arp2/3 complex actin depolymerizing factors Cofilin 1 2 Destrin Gelsolin Profilin 1 2 Titin

Other

Intermediate
filaments

Type 1/2
(Keratin,
Cytokeratin)

Epithelial keratins (soft alpha-keratins)	type I/chromosome 17 9 10 12 13 14 15 16 17 19 20 chromosome 12 18 none 21 type II/chromosome 12 1 2A 3 4 5 6A 6B 6C 7 8
Hair keratins (hard alpha-keratins)	type I/chromosome 17 31 32 33A 33B 34 35 36 37 38 type II/chromosome 12 81 82 83 84 85 86
Ungrouped alpha	chromosome 17 23 24 25 26 27 28 39 40 chromosome 12 71 72 73 74 75 76 77 78 79 80
Not alpha	Beta-keratin

Type 3

Type 4

Type 5

Microtubules
and MAPs

Tubulins	TUBA1A TUBA1B TUBA1C TUBA3C TUBA3D TUBA3E TUBA4A TUBA8 TUBB TUBB1 TUBB2A TUBB2B TUBB2C TUBB3 TUBB4 TUBB4Q TUBB6 TUBB8 TUBG1 TUBG2 TUBGCP2 TUBGCP3 TUBGCP4 TUBGCP5 TUBGCP6 TUBD1 TUBE1
MAPs	EB1 EB2 EB3 MAP1A MAP1B MAP2 MAP4
Kinesins	KIF1A KIF1B KIF2A KIF2C KIF3B KIF3C KIF4A KIF4B KIF5A KIF5B KIF5C KIF6 KIF7 KIF9 KIF11 KIF12 KIF13A KIF13B KIF14 KIF15 KIF16B KIF17 KIF18A KIF18B KIF19 KIF20A KIF20B KIF21A KIF21B KIF22 KIF23 KIF24 KIF25 KIF26A KIF26B KIF27 KIFC1 KIFC2 KIFC3
Dyneins	axonemal: DNAH1 DNAH2 DNAH3 DNAH5 DNAH6 DNAH7 DNAH8 DNAH9 DNAH10 DNAH11 DNAH12 DNAH13 DNAH14 DNAH17 DNAI1 DNAI2 DNALI1 DNAL1 DNAL4 cytoplasmic: DYNC1H1 DYNC2H1 DYNC1I1 DYNC1I2 DYNC1LI1 DYNC1LI2 DYNC2LI1 DYNLL1 DYNLL2 DYNLRB1 DYNLRB2 DYNLT1 DYNLT3
Microtubule organising proteins	CAMSAP1 CAMSAP2 CAMSAP3 Centrin 1 Centrin 2 Centrin 3 PCM1
Microtubule severing proteins	Katanin Spastin
Other	Tau protein Dynactin DCTN1 Stathmin Tektin TEKT1 TEKT2 TEKT3 TEKT4 TEKT5 Dynamin DNM1 DNM2 DNM3