P07437 (TBB5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulin beta chain

Alternative name(s):
Tubulin beta-5 chain

Gene names

Name:	TUBB
Synonyms:	TUBB5
ORF Names:	OK/SW-cl.56

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Subunit structure	Dimer of alpha and beta chains. May interact with RNABP10 By similarity. Interacts with PIFO. Interacts with MX1 By similarity. Ref.16
Subcellular location	Cytoplasm › cytoskeleton.
Tissue specificity	Ubiquitously expressed with highest levels in spleen, thymus and immature brain. Ref.15
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.
Sequence similarities	Belongs to the tubulin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome cell division Traceable author statement PubMed 12090300. Source: BHF-UCL cellular component movement Traceable author statement PubMed 16130169. Source: UniProtKB cytoskeleton-dependent intracellular transport Traceable author statement PubMed 12090300. Source: BHF-UCL microtubule-based process Traceable author statement PubMed 12090300. Source: BHF-UCL natural killer cell mediated cytotoxicity Non-traceable author statement PubMed 11120798. Source: UniProtKB protein polymerization Inferred from electronic annotation. Source: InterPro spindle assembly Inferred from electronic annotation. Source: Compara
Cellular_component	cell body Inferred from direct assay PubMed 19567321. Source: DFLAT cytosol Traceable author statement. Source: Reactome extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB microtubule Inferred from direct assay PubMed 21525035. Source: UniProtKB nuclear envelope lumen Inferred from direct assay PubMed 19567321. Source: DFLAT plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro MHC class I protein binding Inferred from direct assay PubMed 11120798. Source: UniProtKB structural constituent of cytoskeleton Inferred from electronic annotation. Source: Compara structural molecule activity Traceable author statement PubMed 12090300. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 444	444	Tubulin beta chain		PRO_0000048243
Regions
	Nucleotide binding	140 – 146	7	GTP Potential
Amino acid modifications
	Modified residue	58	1	N6-acetyllysine; alternate Ref.14
	Modified residue	172	1	Phosphoserine; by CDK1 By similarity
	Modified residue	318	1	Omega-N-methylarginine Ref.9
	Modified residue	340	1	Phosphotyrosine By similarity
	Modified residue	382	1	Phosphoserine By similarity
	Cross-link	58		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.12
	Cross-link	324		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12
Experimental info
	Sequence conflict	216	1	K → R Ref.1
	Sequence conflict	216	1	K → R Ref.2
	Sequence conflict	231	1	A → G Ref.1
	Sequence conflict	231	1	A → G Ref.2
	Sequence conflict	234 – 235	2	SG → EC Ref.1
	Sequence conflict	234 – 235	2	SG → EC Ref.2
	Sequence conflict	288	1	E → D Ref.1
	Sequence conflict	288	1	E → D Ref.2
	Sequence conflict	298	1	N → D in AAH20946. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P07437 [UniParc]. Last modified December 21, 2004. Version 2. Checksum: 1E6CD0A36773A103	FASTA	444	49,671
	10 20 30 40 50 60 MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY YNEATGGKYV 70 80 90 100 110 120 PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV 130 140 150 160 170 180 RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV 190 200 210 220 230 240 EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL 250 260 270 280 290 300 RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQVFDAKNMM 310 320 330 340 350 360 AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG 370 380 390 400 410 420 LKMAVTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS 430 440 EYQQYQDATA EEEEDFGEEA EEEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evolutionary history of a multigene family: an expressed human beta-tubulin gene and three processed pseudogenes." Lee M.G.-S., Lewis S.A., Wilde C.D., Cowan N.J. Cell 33:477-487(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Identification of two human beta-tubulin isotypes." Hall J.L., Dudley L., Dobner P.R., Lewis S.A., Cowan N.J. Mol. Cell. Biol. 3:854-862(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Tubulins in the primate retina: evidence that xanthophylls may be endogenous ligands for the paclitaxel-binding site." Crabtree D.V., Ojima I., Geng X., Adler A.J. Bioorg. Med. Chem. 9:1967-1976(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[4]	Yu W., Gibbs R.A. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region." Shiina S., Tamiya G., Oka A., Inoko H. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Genome diversity in HLA: a new strategy for detection of genetic polymorphisms in expressed genes within the HLA class III and class I regions." Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients." Shichijo S., Itoh K. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon adenocarcinoma.
[8]	"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]. Tissue: Brain, Eye, Lung, Muscle and Placenta.
[9]	Bienvenut W.V., Campbell A., Ozanne B.W., Lourenco F., Olson M.F. Submitted (DEC-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-19; 47-77; 104-174; 242-276; 283-297; 310-359 AND 363-390, METHYLATION AT ARG-318, MASS SPECTROMETRY. Tissue: Foreskin fibroblast and Mammary carcinoma.
[10]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 3-19; 47-58; 63-77; 104-121; 163-174; 242-251; 253-276; 283-297; 310-318; 325-336 AND 381-390, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[11]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-58 AND LYS-324, MASS SPECTROMETRY.
[13]	"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.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, MASS SPECTROMETRY.
[15]	"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.
[16]	"Pitchfork regulates primary cilia disassembly and left-right asymmetry." Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H. Dev. Cell 19:66-77(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PIFO.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

Wikipedia

Tubulin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J00314 Genomic DNA. Translation: AAB59507.1.
AF141349 mRNA. Translation: AAD33873.1.
AF070561 mRNA. Translation: AAC28642.1.
AF070593 mRNA. Translation: AAC28650.1.
AF070600 mRNA. Translation: AAC28654.1.
BA000025 Genomic DNA. Translation: BAB63321.1.
AB088100 Genomic DNA. Translation: BAC54932.1.
AB062393 mRNA. Translation: BAB93480.1.
BC001938 mRNA. Translation: AAH01938.1.
BC002347 mRNA. Translation: AAH02347.1.
BC005838 mRNA. Translation: AAH05838.1.
BC007605 mRNA. Translation: AAH07605.1.
BC013374 mRNA. Translation: AAH13374.1.
BC019924 mRNA. Translation: AAH19924.1.
BC020946 mRNA. Translation: AAH20946.1.
BC021909 mRNA. Translation: AAH21909.1.
BC070326 mRNA. Translation: AAH70326.1.

IPI

IPI01019113.

PIR

A26561.

RefSeq

NP_821133.1. NM_178014.2.

UniGene

Hs.636480.
Hs.714425.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3QNZ	X-ray	2.20	C	429-438	[»]
3QO0	X-ray	2.30	C	422-441	[»]

ProteinModelPortal

P07437.

ModBase

Search...

Protein-protein interaction databases

IntAct

P07437. 62 interactions.

MINT

MINT-1146393.

STRING

9606.ENSP00000410071.

PTM databases

PhosphoSite

P07437.

Polymorphism databases

DMDM

56757569.

2D gel databases

OGP

P07437.

REPRODUCTION-2DPAGE

P07437.

SWISS-2DPAGE

P07437.

UCD-2DPAGE

P07437.

Proteomic databases

PaxDb

P07437.

PRIDE

P07437.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000327892; ENSP00000339001; ENSG00000196230.
ENST00000383564; ENSP00000373058; ENSG00000183311.
ENST00000419792; ENSP00000401317; ENSG00000235067.
ENST00000421473; ENSP00000399155; ENSG00000224156.
ENST00000422650; ENSP00000400663; ENSG00000229684.
ENST00000422674; ENSP00000406811; ENSG00000227739.
ENST00000432462; ENSP00000410829; ENSG00000232421.
ENST00000436628; ENSP00000410071; ENSG00000232575.

GeneID

203068.

KEGG

hsa:203068.

UCSC

uc003nrl.3. human.

Organism-specific databases

CTD

203068.

GeneCards

GC06P030687.

HGNC

HGNC:20778. TUBB.

HPA

CAB005417.
CAB012406.
HPA043640.
HPA046280.

MIM

191130. gene.

neXtProt

NX_P07437.

PharmGKB

PA358.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5023.

HOVERGEN

HBG000089.

InParanoid

P07437.

KO

K07375.

OMA

RYQGEND.

OrthoDB

EOG4DFPNJ.

PhylomeDB

P07437.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.

Gene expression databases

ArrayExpress

P07437.

Bgee

P07437.

CleanEx

HS_TUBB.

Genevestigator

P07437.

GermOnline

ENSG00000196230. Homo sapiens.

Family and domain databases

Gene3D

1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.

InterPro

IPR013838. 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]

PANTHER

PTHR11588. PTHR11588. 1 hit.

Pfam

PF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]

PRINTS

PR01163. BETATUBULIN.
PR01161. TUBULIN.

SMART

SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]

SUPFAM

SSF55307. Tub_FtsZ_C. 1 hit.
SSF52490. Tubulin_FtsZ. 1 hit.

PROSITE

PS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P07437.

ChEMBL

CHEMBL5444.

ChiTaRS

TUBB. human.

DrugBank

DB01394. Colchicine.
DB00570. Vinblastine.
DB00541. Vincristine.
DB00361. Vinorelbine.

GenomeRNAi

203068.

NextBio

90324.

SOURCE

Search...

Entry information

Entry name

TBB5_HUMAN

Accession

Primary (citable) accession number: P07437
Secondary accession number(s): P05218, Q8WUC1, Q9CY33

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 158 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.