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Q9BQE3 (TBA1C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tubulin alpha-1C chain
Alternative name(s):
Alpha-tubulin 6
Tubulin alpha-6 chain
Gene names
Name:TUBA1C
Synonyms:TUBA6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length449 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
Nitration
Phosphoprotein
   Technical termComplete 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

cytoskeleton-dependent intracellular transport

Traceable author statement PubMed 12090300. Source: BHF-UCL

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

Traceable author statement PubMed 12090300. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 21630459PubMed 22720776. Source: UniProt

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 22720776. Source: UniProt

structural constituent of cytoskeleton

Inferred from electronic annotation. Source: InterPro

structural molecule activity

Traceable author statement PubMed 12090300. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Tubulin alpha-1C chain
PRO_0000048112

Regions

Nucleotide binding142 – 1487GTP Potential

Sites

Site4491Involved in polymerization

Amino acid modifications

Modified residue481Phosphoserine By similarity
Modified residue831Nitrated tyrosine By similarity
Modified residue2821Nitrated tyrosine By similarity
Modified residue4321Phosphotyrosine Ref.8
Modified residue4391Phosphoserine Ref.3 Ref.4 Ref.5 Ref.8 Ref.9 Ref.11

Sequences

Sequence LengthMass (Da)Tools
Q9BQE3 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 0CFE7212CB5E14F9

FASTA44949,895
        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 AYHEQLTVAE ITNACFEPAN 

       310        320        330        340        350        360 
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP 

       370        380        390        400        410        420 
TVVPGGDLAK VQRAVCMLSN TTAVAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE 

       430        440 
AREDMAALEK DYEEVGADSA DGEDEGEEY 

« Hide

References

« Hide 'large scale' references
[1]"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: Bone marrow, Duodenum, Lymph and Skin.
[2]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 65-79 AND 244-280, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[3]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[4]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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.
[8]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-432 AND SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC004949 mRNA. Translation: AAH04949.1.
BC005946 mRNA. Translation: AAH05946.1.
BC011790 mRNA. Translation: AAH11790.1.
BC019298 mRNA. Translation: AAH19298.1.
BC021088 mRNA. Translation: AAH21088.1.
BC051297 mRNA. Translation: AAH51297.1.
BC063036 mRNA. Translation: AAH63036.1.
CCDSCCDS8782.1.
RefSeqNP_116093.1. NM_032704.3.
UniGeneHs.652390.

3D structure databases

ProteinModelPortalQ9BQE3.
SMRQ9BQE3. Positions 1-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124259. 79 interactions.
IntActQ9BQE3. 46 interactions.
MINTMINT-3060519.
STRING9606.ENSP00000301072.

Chemistry

ChEMBLCHEMBL2095182.

PTM databases

PhosphoSiteQ9BQE3.

Polymorphism databases

DMDM20455322.

2D gel databases

REPRODUCTION-2DPAGEQ9BQE3.

Proteomic databases

MaxQBQ9BQE3.
PRIDEQ9BQE3.

Protocols and materials databases

DNASU84790.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301072; ENSP00000301072; ENSG00000167553.
GeneID84790.
KEGGhsa:84790.
UCSCuc001rtt.1. human.

Organism-specific databases

CTD84790.
GeneCardsGC12P049658.
HGNCHGNC:20768. TUBA1C.
HPAHPA039247.
HPA043684.
neXtProtNX_Q9BQE3.
PharmGKBPA162407345.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG000089.
InParanoidQ9BQE3.
KOK07374.
PhylomeDBQ9BQE3.
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

ArrayExpressQ9BQE3.
BgeeQ9BQE3.
CleanExHS_TUBA1C.
GenevestigatorQ9BQE3.

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

ChiTaRSTUBA1C. human.
GeneWikiTUBA1C.
GenomeRNAi84790.
NextBio74948.
PMAP-CutDBQ9BQE3.
PROQ9BQE3.

Entry information

Entry nameTBA1C_HUMAN
AccessionPrimary (citable) accession number: Q9BQE3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 132 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

Human chromosome 12

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