P68371 (TBB4B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulin beta-4B chain

Alternative name(s):
Tubulin beta-2 chain
Tubulin beta-2C chain

Gene names

Name:	TUBB4B
Synonyms:	TUBB2C

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	445 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.
Subcellular location	Cytoplasm › cytoskeleton.
Tissue specificity	Ubiquitous. Ref.6
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 Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' posttranslational protein folding Traceable author statement. Source: Reactome G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome cellular component movement Traceable author statement PubMed 16130169. Source: ProtInc microtubule-based process Inferred from electronic annotation. Source: InterPro natural killer cell mediated cytotoxicity Non-traceable author statement PubMed 11120798. Source: UniProtKB protein polymerization Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Traceable author statement. Source: Reactome microtubule Inferred from direct assay PubMed 21525035. Source: UniProtKB 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 Traceable author statement PubMed 11120798. Source: UniProtKB structural constituent of cytoskeleton Inferred from electronic annotation. Source: InterPro unfolded protein binding Non-traceable author statement PubMed 11120798. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 445	445	Tubulin beta-4B chain		PRO_0000048248
Regions
	Nucleotide binding	140 – 146	7	GTP Potential
Amino acid modifications
	Modified residue	51	1	Phosphotyrosine By similarity
	Modified residue	58	1	N6-acetyllysine Ref.5
	Modified residue	172	1	Phosphoserine; by CDK1 Probable

Sequences

	Sequence		Length	Mass (Da)
	P68371 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: A552C52822AFA072	FASTA	445	49,831
	10 20 30 40 50 60 MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY YNEATGGKYV 70 80 90 100 110 120 PRAVLVDLEP 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 QQMFDAKNMM 310 320 330 340 350 360 AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG 370 380 390 400 410 420 LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS 430 440 EYQQYQDATA EEEGEFEEEA EEEVA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Three expressed sequences within the human beta-tubulin multigene family each define a distinct isotype." Lewis S.A., Gilmartin M.E., Hall J.L., Cowan N.J. J. Mol. Biol. 182:11-20(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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, Cervix, Lung, Lymph, Muscle, Skin and Uterus.
[4]	"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.
[5]	"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.
[6]	"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.
[7]	"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X02344 Genomic DNA. Translation: CAA26203.1. BX255925 Genomic DNA. Translation: CAM24148.1. BC001911 mRNA. Translation: AAH01911.1. BC002783 mRNA. Translation: AAH02783.1. BC002885 mRNA. Translation: AAH02885.1. BC004188 mRNA. Translation: AAH04188.1. BC007889 mRNA. Translation: AAH07889.1. BC012835 mRNA. Translation: AAH12835.1. BC019359 mRNA. Translation: AAH19359.1. BC019829 mRNA. Translation: AAH19829.1. BC039175 mRNA. Translation: AAH39175.1. BC071889 mRNA. Translation: AAH71889.1.
IPI	IPI00007752.
PIR	I38370.
RefSeq	NP_006079.1. NM_006088.5.
UniGene	Hs.433615.
3D structure databases
ProteinModelPortal	P68371.
ModBase	Search...
Protein-protein interaction databases
IntAct	P68371. 33 interactions.
MINT	MINT-1390314.
STRING	9606.ENSP00000341289.
PTM databases
PhosphoSite	P68371.
Polymorphism databases
DMDM	55977480.
2D gel databases
OGP	P05217.
REPRODUCTION-2DPAGE	IPI00007752.
SWISS-2DPAGE	P68371.
Proteomic databases
PeptideAtlas	P68371.
PRIDE	P68371.
Protocols and materials databases
DNASU	10383.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000340384; ENSP00000341289; ENSG00000188229.
GeneID	10383.
KEGG	hsa:10383.
UCSC	uc004cmg.1. human.
Organism-specific databases
CTD	10383.
GeneCards	GC09P140136.
HGNC	HGNC:20771. TUBB4B.
HPA	CAB010880. HPA043640. HPA046280.
MIM	602660. gene.
neXtProt	NX_P68371.
PharmGKB	PA142670672.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HOG000165710.
HOVERGEN	HBG000089.
InParanoid	P68371.
KO	K07375.
OMA	YNEAGSN.
OrthoDB	EOG4DFPNJ.
PhylomeDB	P68371.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_11123. Membrane Trafficking. REACT_115566. Cell Cycle. REACT_17015. Metabolism of proteins. REACT_21300. Mitotic M-M/G1 phases. REACT_604. Hemostasis. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	P68371.
Bgee	P68371.
CleanEx	HS_TUBB2C.
Genevestigator	P68371.
GermOnline	ENSG00000188229. 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	P68371.
ChEMBL	CHEMBL1848.
ChiTaRS	TUBB4B. human.
GenomeRNAi	10383.
NextBio	39335.
SOURCE	Search...

Entry information

Entry name

TBB4B_HUMAN

Accession

Primary (citable) accession number: P68371
Secondary accession number(s): A2BFA2, P05217

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	May 1, 2013
This is version 97 of the entry and version 1 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.