TUBB

Protein-coding gene in the species Homo sapiens

For persons named Tubb, see Tubb.

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
| Gene location (Human)

Chr.| Chromosome 6 (human)[1]

Band| 6p21.33| Start| 30,717,435 bp[1]
End| 30,725,538 bp[1]
| Gene location (Mouse)

Chr.| Chromosome 17 (mouse)[2]

Band| 17|17 B1| Start| 36,144,813 bp[2]
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[edit]

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

## See also[edit]

* Tubulin

## References[edit]

1. ^ 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
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001525 \- Ensembl, May 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ 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.
6. ^ 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.
7. ^ "Entrez Gene: TUBB tubulin, beta".
8. ^ 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.
9. ^ 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.

## Further reading[edit]

* 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. 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.

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* t
* e

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

* v
* t
* e

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|

* Wiskott–Aldrich syndrome protein
* Fibrillin
* Filamin
* FLNA
* FLNB
* FLNC
* Espin
* TRIOBP

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|

* Desmin
* GFAP
* Peripherin
* Vimentin

Type 4|

* Internexin
* Nestin
* Neurofilament
* NEFL
* NEFM
* NEFH
* Synemin
* Syncoilin

Type 5|

* Nuclear lamins: A/C
* B1
* B2

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

Catenins|

* Alpha catenin
* Beta catenin
* APC
* Plakoglobin (gamma catenin)
* Delta catenin
* GAN

Membrane|

* Dystrophin
* Dystroglycan
* Utrophin
* Ankyrin
* ANK1
* ANK2
* ANK3
* Spectrin
* SPTA1
* SPTAN1
* SPTB
* SPTBN1
* SPTBN2
* SPTBN4
* SPTBN5

Other|

* Plakins
* Corneodesmosin
* Desmoplakin
* Dystonin
* Envoplakin
* MACF1
* Periplakin
* Plectin
* Talin
* TLN1
* Vinculin
* Plakophilin
* PKP1
* PKP2
* ACF7
* PLEKHA7

Nonhuman|

* Major sperm proteins
* Prokaryotic cytoskeleton
* Crescentin
* FtsZ
* MreB
* ParM

See also: cytoskeletal defects

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