P68363 (TBA1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulin alpha-1B chain

Alternative name(s):
Alpha-tubulin ubiquitous
Tubulin K-alpha-1
Tubulin alpha-ubiquitous chain

Gene names

Name:

TUBA1B

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.
Subunit structure	Dimer of alpha and beta chains.
Subcellular location	Cytoplasm › cytoskeleton.
Post-translational modification	Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively By similarity. 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. Acetylation of alpha-tubulins at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling By similarity.
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	'de novo' posttranslational protein folding Traceable author statement. Source: Reactome cell division Traceable author statement. Source: BHF-UCL cytoskeleton-dependent intracellular transport Traceable author statement. Source: BHF-UCL microtubule-based movement Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 451	451	Tubulin alpha-1B chain		PRO_0000048108
Regions
	Nucleotide binding	142 – 148	7	GTP Potential
Sites
	Site	451	1	Involved in polymerization
Amino acid modifications
	Modified residue	40	1	N6-acetyllysine By similarity
	Modified residue	41	1	Phosphothreonine Ref.9
	Modified residue	48	1	Phosphoserine Ref.6 Ref.9
	Modified residue	232	1	Phosphoserine Ref.6 Ref.11
	Modified residue	272	1	Phosphotyrosine Ref.8
	Modified residue	334	1	Phosphothreonine Ref.9
	Modified residue	339	1	Omega-N-methylarginine Ref.6
	Modified residue	340	1	Phosphoserine Ref.11 Ref.13
	Modified residue	432	1	Phosphotyrosine Ref.13
	Modified residue	439	1	Phosphoserine Ref.9 Ref.13
	Modified residue	451	1	Phosphotyrosine Ref.13
	Cross-link	326		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10
	Cross-link	370		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10
Experimental info
	Sequence conflict	131	1	G → R in AAA91576. Ref.1
	Sequence conflict	290	1	E → D in AAA91576. Ref.1
	Sequence conflict	308	1	R → G in AAA91576. Ref.1
	Sequence conflict	340	1	S → T in AAA91576. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P68363 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 94355B4EC2086429	FASTA	451	50,152
	10 20 30 40 50 60 MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK 70 80 90 100 110 120 HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD 130 140 150 160 170 180 RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA 190 200 210 220 230 240 VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA 250 260 270 280 290 300 SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 310 320 330 340 350 360 QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP 370 380 390 400 410 420 TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE 430 440 450 AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of human alpha-tubulin genes: interspecies conservation of 3' untranslated regions." Cowan N.J., Dobner P., Fuchs E.V., Cleveland D.W. Mol. Cell. Biol. 3:1738-1745(1983) [PubMed: 6646120] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Keratinocyte.
[2]	de Hostos E.L. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Gene response of gangliocytes stimulated by Herpes simplex virus type 1." Li Q., Liu L., Ma S. Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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, Colon, Eye, Kidney, Lung, Muscle, Placenta, Prostate, Skin and Uterus.
[5]	Lubec G., Afjehi-Sadat L., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 41-60; 65-79; 113-121; 230-280; 312-320; 327-336; 340-370; 374-390; 395-401 AND 403-422, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[6]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 41-79; 65-79; 85-121; 125-164; 216-304; 312-370 AND 374-451, PHOSPHORYLATION AT SER-48 AND SER-232, METHYLATION AT ARG-339, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"C-terminal fragments of alpha- and beta-tubulin form amyloid fibrils in vitro and associate with amyloid deposits of familial cerebral amyloid angiopathy, British type." Baumann M.H., Wisniewski T., Levy E., Plant G.T., Ghiso J. Biochem. Biophys. Res. Commun. 219:238-242(1996) [PubMed: 8619814] [Abstract] Cited for: PROTEIN SEQUENCE OF 353-370 AND 395-401. Tissue: Brain.
[8]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-272, MASS SPECTROMETRY.
[9]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-41; SER-48; THR-334 AND SER-439, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 18781797] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-326 AND LYS-370, MASS SPECTROMETRY.
[11]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-340, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"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.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340; TYR-432; SER-439 AND TYR-451, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K00558 mRNA. Translation: AAA91576.1.
AF081484 mRNA. Translation: AAC31959.1.
DQ400107 mRNA. Translation: ABD60581.1.
BC000696 mRNA. Translation: AAH00696.1.
BC001128 mRNA. Translation: AAH01128.1.
BC006379 mRNA. Translation: AAH06379.1.
BC006481 mRNA. Translation: AAH06481.1.
BC008659 mRNA. Translation: AAH08659.1.
BC009314 mRNA. Translation: AAH09314.1.
BC009509 mRNA. Translation: AAH09509.1.
BC009512 mRNA. Translation: AAH09512.1.
BC009513 mRNA. Translation: AAH09513.1.
BC010494 mRNA. Translation: AAH10494.1.
BC011572 mRNA. Translation: AAH11572.1.
BC015883 mRNA. Translation: AAH15883.1.
BC017004 mRNA. Translation: AAH17004.1.
BC030820 mRNA. Translation: AAH30820.1.
BC071904 mRNA. Translation: AAH71904.1.

IPI

IPI00930688.

PIR

I77403.

RefSeq

NP_006073.2. NM_006082.2.

UniGene

Hs.524390.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E4H	NMR	-	B	416-451	[»]

ProteinModelPortal

P68363.

SMR

P68363. Positions 1-441.

DisProt

DP00115.

ModBase

Search...

Protein-protein interaction databases

IntAct

P68363. 9 interactions.

MINT

MINT-4998849.

STRING

P68363.

PTM databases

PhosphoSite

P68363.

Polymorphism databases

DMDM

55977474.

2D gel databases

SWISS-2DPAGE

P68363.

OGP

P68363.

Proteomic databases

PRIDE

P68363.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000336023; ENSP00000336799; ENSG00000123416.

GeneID

10376.

KEGG

hsa:10376.

UCSC

uc001rtk.1. human.

Organism-specific databases

CTD

10376.

GeneCards

GC12M049523.

HGNC

HGNC:18809. TUBA1B.

HPA

CAB011513.

MIM

602530. gene.

neXtProt

NX_P68363.

PharmGKB

PA162407332.

GenAtlas

Search...

Phylogenomic databases

eggNOG

maNOG21857.

GeneTree

ENSGT00600000084100.

HOGENOM

HBG750007.

HOVERGEN

HBG000089.

InParanoid

P68363.

OMA

VGIDSTT.

OrthoDB

EOG44J2HZ.

PhylomeDB

P68363.

Enzyme and pathway databases

Pathway_Interaction_DB

hdac_classii_pathway. Signaling events mediated by HDAC Class II.
hdac_classiii_pathway. Signaling events mediated by HDAC Class III.

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

P68363.

Bgee

P68363.

CleanEx

HS_TUBA1B.

Genevestigator

P68363.

GermOnline

ENSG00000123416. Homo sapiens.

Family and domain databases

InterPro

IPR002452. Alpha_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

K07374.

PANTHER

PTHR11588. Tubulin. 1 hit.

Pfam

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

PRINTS

PR01162. ALPHATUBULIN.
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.
[Graphical view]

ProtoNet

Search...

Other

NextBio

39315.

SOURCE

Search...

Entry information

Entry name

TBA1B_HUMAN

Accession

Primary (citable) accession number: P68363
Secondary accession number(s): P04687, P05209, Q27I68

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
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.