Q9H4B7 (TBB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulin beta-1 chain

Gene names

Name:

TUBB1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	451 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 By similarity.
Subunit structure	Dimer of alpha and beta chains By similarity. Interacts with RANBP10. Ref.5
Subcellular location	Cytoplasm › cytoskeleton Ref.9.
Tissue specificity	Hematopoietic cell-specific. Major isotype in leukocytes, where it represents 50% of all beta-tubulins. Ref.7
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.
Involvement in disease	Defects in TUBB1 are a cause of macrothrombocytopenia autosomal dominant TUBB1-related (MAD-TUBB1) [MIM:613112]. It is a congenital blood disorder characterized by increased platelet size and decreased number of circulating platelets. Ref.9
Sequence similarities	Belongs to the tubulin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	'de novo' posttranslational protein folding Traceable author statement. Source: Reactome microtubule-based movement Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay Ref.9. Source: UniProtKB microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 451	451	Tubulin beta-1 chain		PRO_0000048242
Regions
	Nucleotide binding	140 – 146	7	GTP Potential
Amino acid modifications
	Modified residue	172	1	Phosphoserine; by CDK1 By similarity
Natural variations
	Natural variant	43	1	Q → H. Corresponds to variant rs415064 [ dbSNP | Ensembl ].		VAR_034542
	Natural variant	43	1	Q → P. Ref.8 Ref.9 Corresponds to variant rs463312 [ dbSNP | Ensembl ].		VAR_034543
	Natural variant	274	1	T → M. Corresponds to variant rs35565630 [ dbSNP | Ensembl ].		VAR_052671
	Natural variant	307	1	R → H. Ref.9 Corresponds to variant rs6070697 [ dbSNP | Ensembl ].		VAR_052672
	Natural variant	318	1	R → W in MAD-TUBB1. Ref.9		VAR_063411

Sequences

	Sequence		Length	Mass (Da)
	Q9H4B7 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 6A3E5208C1C89AE4	FASTA	451	50,327
	10 20 30 40 50 60 MREIVHIQIG QCGNQIGAKF WEMIGEEHGI DLAGSDRGAS ALQLERISVY YNEAYGRKYV 70 80 90 100 110 120 PRAVLVDLEP GTMDSIRSSK LGALFQPDSF VHGNSGAGNN WAKGHYTEGA ELIENVLEVV 130 140 150 160 170 180 RHESESCDCL QGFQIVHSLG GGTGSGMGTL LMNKIREEYP DRIMNSFSVM PSPKVSDTVV 190 200 210 220 230 240 EPYNAVLSIH QLIENADACF CIDNEALYDI CFRTLKLTTP TYGDLNHLVS LTMSGITTSL 250 260 270 280 290 300 RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTAQGSQQ YRALSVAELT QQMFDARNTM 310 320 330 340 350 360 AACDLRRGRY LTVACIFRGK MSTKEVDQQL LSVQTRNSSC FVEWIPNNVK VAVCDIPPRG 370 380 390 400 410 420 LSMAATFIGN NTAIQEIFNR VSEHFSAMFK RKAFVHWYTS EGMDINEFGE AENNIHDLVS 430 440 450 EYQQFQDAKA VLEEDEEVTE EAEMEPEDKG H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mapping and characterization of the human TUBB1 gene." Gross C., Kussmann S., Hehr A., Hansmann I., Schlote D. Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 38-46 AND 263-281. Tissue: Platelet.
[5]	"RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates noncentrosomal microtubules." Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr., Shivdasani R.A. J. Biol. Chem. 283:14109-14119(2008) [PubMed: 18347012] [Abstract] Cited for: INTERACTION WITH RANBP10.
[6]	"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: 19524510] [Abstract] Cited for: GLYCYLATION.
[7]	"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: 20191564] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"The TUBB1 Q43P functional polymorphism reduces the risk of cardiovascular disease in men by modulating platelet function and structure." Freson K., De Vos R., Wittevrongel C., Thys C., Defoor J., Vanhees L., Vermylen J., Peerlinck K., Van Geet C. Blood 106:2356-2362(2005) [PubMed: 15956286] [Abstract] Cited for: VARIANT PRO-43.
[9]	"Mutation of the beta1-tubulin gene associated with congenital macrothrombocytopenia affecting microtubule assembly." Kunishima S., Kobayashi R., Itoh T.J., Hamaguchi M., Saito H. Blood 113:458-461(2009) [PubMed: 18849486] [Abstract] Cited for: VARIANTS PRO-43 AND HIS-307, VARIANT MAD-TUBB1 TRP-318, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ292757 mRNA. Translation: CAC16605.1. AL109840 Genomic DNA. Translation: CAC09371.2. BC033679 mRNA. Translation: AAH33679.1.
IPI	IPI00006510.
RefSeq	NP_110400.1. NM_030773.3.
UniGene	Hs.303023.
3D structure databases
ProteinModelPortal	Q9H4B7.
SMR	Q9H4B7. Positions 2-427.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H4B7. 5 interactions.
MINT	MINT-1891365.
STRING	Q9H4B7.
PTM databases
PhosphoSite	Q9H4B7.
Polymorphism databases
DMDM	62903515.
2D gel databases
OGP	Q9H4B7.
Proteomic databases
PeptideAtlas	Q9H4B7.
PRIDE	Q9H4B7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000217133; ENSP00000217133; ENSG00000101162.
GeneID	81027.
KEGG	hsa:81027.
UCSC	uc002yak.1. human.
Organism-specific databases
CTD	81027.
GeneCards	GC20P057594.
H-InvDB	HIX0015958.
HGNC	HGNC:16257. TUBB1.
HPA	CAB004286.
MIM	612901. gene. 613112. phenotype.
neXtProt	NX_Q9H4B7.
PharmGKB	PA38100.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18886.
GeneTree	ENSGT00600000084255.
HOGENOM	HBG750007.
HOVERGEN	HBG000089.
InParanoid	Q9H4B7.
OMA	DACFCID.
OrthoDB	EOG4QVCC0.
PhylomeDB	Q9H4B7.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_11123. Membrane Trafficking. REACT_152. Cell Cycle, Mitotic. REACT_17015. Metabolism of proteins. REACT_383. DNA Replication. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	Q9H4B7.
Bgee	Q9H4B7.
CleanEx	HS_TUBB1.
Genevestigator	Q9H4B7.
GermOnline	ENSG00000101162. Homo sapiens.
Family and domain databases
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]
Gene3D	G3DSA:3.30.1330.20. Tubulin/FtsZ_2-layer-sand-dom. 1 hit. G3DSA:1.10.287.600. Tubulin_C. 1 hit. G3DSA:3.40.50.1440. Tubulin_FtsZ. 1 hit.
KO	K07375.
PANTHER	PTHR11588. Tubulin. 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
DrugBank	DB01394. Colchicine. DB01248. Docetaxel. DB01229. Paclitaxel. DB00309. Vindesine.
NextBio	71348.
SOURCE	Search...

Entry information

Entry name

TBB1_HUMAN

Accession

Primary (citable) accession number: Q9H4B7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 86 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.