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P68363 (TBA1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tubulin alpha-1B chain
Alternative name(s):
Alpha-tubulin ubiquitous
Tubulin K-alpha-1
Tubulin alpha-ubiquitous chain
Gene names
Name:TUBA1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Protein existenceEvidence 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. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Subcellular location

Cytoplasmcytoskeleton.

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 chains 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 componentCytoplasm
Cytoskeleton
Microtubule
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Isopeptide bond
Methylation
Nitration
Phosphoprotein
Ubl conjugation
   Technical term3D-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 PubMed 12090300. Source: BHF-UCL

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to interleukin-4

Inferred from electronic annotation. Source: Ensembl

cytoskeleton-dependent intracellular transport

Traceable author statement PubMed 12090300. Source: BHF-UCL

microtubule cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

microtubule-based process

Traceable author statement PubMed 12090300. Source: BHF-UCL

protein folding

Traceable author statement. Source: Reactome

protein polymerization

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasmic microtubule

Inferred from electronic annotation. Source: Ensembl

microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

double-stranded RNA binding

Inferred from direct assay PubMed 21266579. Source: MGI

protein binding

Inferred from physical interaction PubMed 11698390. Source: UniProtKB

structural constituent of cytoskeleton

Inferred from electronic annotation. Source: Ensembl

structural molecule activity

Traceable author statement PubMed 12090300. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TUBB3Q135093EBI-487083,EBI-350989

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Tubulin alpha-1B chain
PRO_0000048108

Regions

Nucleotide binding142 – 1487GTP Potential

Sites

Site4511Involved in polymerization

Amino acid modifications

Modified residue481Phosphoserine Ref.6
Modified residue831Nitrated tyrosine By similarity
Modified residue2321Phosphoserine Ref.6
Modified residue2821Nitrated tyrosine By similarity
Modified residue3391Omega-N-methylarginine Ref.6
Modified residue4321Phosphotyrosine By similarity
Modified residue4391Phosphoserine By similarity
Cross-link326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Experimental info

Sequence conflict1311G → R in AAA91576. Ref.1
Sequence conflict2901E → D in AAA91576. Ref.1
Sequence conflict3081R → G in AAA91576. Ref.1
Sequence conflict3401S → T in AAA91576. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P68363 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 94355B4EC2086429

FASTA45150,152
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 353-370 AND 395-401.
Tissue: Brain.
[8]"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.
+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.
CCDSCCDS31792.1.
PIRI77403.
RefSeqNP_006073.2. NM_006082.2.
UniGeneHs.524390.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E4HNMR-B416-451[»]
ProteinModelPortalP68363.
SMRP68363. Positions 1-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115651. 75 interactions.
IntActP68363. 20 interactions.
MINTMINT-4998849.
STRING9606.ENSP00000336799.

Chemistry

ChEMBLCHEMBL2095182.

PTM databases

PhosphoSiteP68363.

Polymorphism databases

DMDM55977474.

2D gel databases

OGPP68363.
SWISS-2DPAGEP68363.

Proteomic databases

MaxQBP68363.
PaxDbP68363.
PRIDEP68363.

Protocols and materials databases

DNASU10376.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336023; ENSP00000336799; ENSG00000123416.
GeneID10376.
KEGGhsa:10376.
UCSCuc001rtl.3. human.

Organism-specific databases

CTD10376.
GeneCardsGC12M049523.
H-InvDBHIX0079488.
HGNCHGNC:18809. TUBA1B.
HPACAB011513.
HPA039247.
HPA043684.
MIM602530. gene.
neXtProtNX_P68363.
PharmGKBPA162407332.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5023.
HOGENOMHOG000165711.
HOVERGENHBG000089.
InParanoidP68363.
KOK07374.
OMACVRARTI.
OrthoDBEOG7TBC1W.
PhylomeDBP68363.
TreeFamTF300314.

Enzyme and pathway databases

ReactomeREACT_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

ArrayExpressP68363.
BgeeP68363.
CleanExHS_TUBA1B.
GenevestigatorP68363.

Family and domain databases

Gene3D1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProIPR002452. 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]
PANTHERPTHR11588. PTHR11588. 1 hit.
PfamPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEPS00227. TUBULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTUBA1B. human.
EvolutionaryTraceP68363.
GeneWikiTUBA1B.
GenomeRNAi10376.
NextBio39315.
PROP68363.
SOURCESearch...

Entry information

Entry nameTBA1B_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM