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Protein

Tubulin alpha-1C chain

Gene

TUBA1C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei449Involved in polymerization1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi142 – 148GTPSequence analysis7

GO - Molecular functioni

  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB-KW
  • structural constituent of cytoskeleton Source: InterPro
  • structural molecule activity Source: BHF-UCL

GO - Biological processi

  • cell division Source: BHF-UCL
  • cytoskeleton-dependent intracellular transport Source: BHF-UCL
  • microtubule-based process Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000167553-MONOMER.
ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-190840. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
R-HSA-190861. Gap junction assembly.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
R-HSA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
R-HSA-389960. Formation of tubulin folding intermediates by CCT/TriC.
R-HSA-389977. Post-chaperonin tubulin folding pathway.
R-HSA-437239. Recycling pathway of L1.
R-HSA-5610787. Hedgehog 'off' state.
R-HSA-5617833. Assembly of the primary cilium.
R-HSA-5620924. Intraflagellar transport.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6807878. COPI-mediated anterograde transport.
R-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-983189. Kinesins.
SIGNORiQ9BQE3.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-1C chain
Alternative name(s):
Alpha-tubulin 6
Tubulin alpha-6 chain
Cleaved into the following chain:
Gene namesi
Name:TUBA1C
Synonyms:TUBA6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:20768. TUBA1C.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-KW
  • microtubule Source: BHF-UCL
  • nucleus Source: UniProtKB
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

DisGeNETi84790.
OpenTargetsiENSG00000167553.
PharmGKBiPA162407345.

Chemistry databases

ChEMBLiCHEMBL2095182.

Polymorphism and mutation databases

BioMutaiTUBA1C.
DMDMi20455322.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000481121 – 449Tubulin alpha-1C chainAdd BLAST449
ChainiPRO_00004373941 – 448Detyrosinated tubulin alpha-1C chain1 PublicationAdd BLAST448

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40N6-acetyllysine1 Publication1
Modified residuei282Nitrated tyrosineBy similarity1
Modified residuei432PhosphotyrosineCombined sources1
Modified residuei439PhosphoserineCombined sources1
Modified residuei4493'-nitrotyrosineBy similarity1

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (PubMed:26875866).1 Publication
Some glutamate residues at the C-terminus are 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). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of monoglycylation is still unclear (Probable).1 Publication
Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly.1 Publication
Nitration of Tyr-449 is irreversible and interferes with normal dynein intracellular distribution.By similarity
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.2 Publications
Tubulin alpha-1C chain: Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (By similarity). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules (PubMed:26972003). In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity).By similarity1 Publication
Detyrosinated tubulin alpha-1C chain: Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator (PubMed:25908662). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle. In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (By similarity).By similarity1 Publication

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

EPDiQ9BQE3.
MaxQBiQ9BQE3.
PaxDbiQ9BQE3.
PeptideAtlasiQ9BQE3.
PRIDEiQ9BQE3.
TopDownProteomicsiQ9BQE3.

2D gel databases

REPRODUCTION-2DPAGEQ9BQE3.

PTM databases

iPTMnetiQ9BQE3.
PhosphoSitePlusiQ9BQE3.
SwissPalmiQ9BQE3.

Miscellaneous databases

PMAP-CutDBQ9BQE3.

Expressioni

Gene expression databases

BgeeiENSG00000167553.
CleanExiHS_TUBA1C.
ExpressionAtlasiQ9BQE3. baseline and differential.
GenevisibleiQ9BQE3. HS.

Organism-specific databases

HPAiHPA039247.
HPA043684.
HPA063394.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
VIMP086703EBI-1103245,EBI-353844

Protein-protein interaction databases

BioGridi124259. 178 interactors.
IntActiQ9BQE3. 160 interactors.
MINTiMINT-3060519.
STRINGi9606.ENSP00000301072.

Structurei

3D structure databases

ProteinModelPortaliQ9BQE3.
SMRiQ9BQE3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOVERGENiHBG000089.
InParanoidiQ9BQE3.
KOiK07374.
PhylomeDBiQ9BQE3.
TreeFamiTF300314.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. 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]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9BQE3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN
60 70 80 90 100
TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT
160 170 180 190 200
SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLTVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAVAEAWAR LDHKFDLMYA
410 420 430 440
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGADSA DGEDEGEEY
Length:449
Mass (Da):49,895
Last modified:June 1, 2001 - v1
Checksum:i0CFE7212CB5E14F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8782.1.
RefSeqiNP_116093.1. NM_032704.4.
UniGeneiHs.652390.
Hs.739076.

Genome annotation databases

EnsembliENST00000301072; ENSP00000301072; ENSG00000167553.
GeneIDi84790.
KEGGihsa:84790.
UCSCiuc001rtt.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8782.1.
RefSeqiNP_116093.1. NM_032704.4.
UniGeneiHs.652390.
Hs.739076.

3D structure databases

ProteinModelPortaliQ9BQE3.
SMRiQ9BQE3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124259. 178 interactors.
IntActiQ9BQE3. 160 interactors.
MINTiMINT-3060519.
STRINGi9606.ENSP00000301072.

Chemistry databases

ChEMBLiCHEMBL2095182.

PTM databases

iPTMnetiQ9BQE3.
PhosphoSitePlusiQ9BQE3.
SwissPalmiQ9BQE3.

Polymorphism and mutation databases

BioMutaiTUBA1C.
DMDMi20455322.

2D gel databases

REPRODUCTION-2DPAGEQ9BQE3.

Proteomic databases

EPDiQ9BQE3.
MaxQBiQ9BQE3.
PaxDbiQ9BQE3.
PeptideAtlasiQ9BQE3.
PRIDEiQ9BQE3.
TopDownProteomicsiQ9BQE3.

Protocols and materials databases

DNASUi84790.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301072; ENSP00000301072; ENSG00000167553.
GeneIDi84790.
KEGGihsa:84790.
UCSCiuc001rtt.2. human.

Organism-specific databases

CTDi84790.
DisGeNETi84790.
GeneCardsiTUBA1C.
HGNCiHGNC:20768. TUBA1C.
HPAiHPA039247.
HPA043684.
HPA063394.
neXtProtiNX_Q9BQE3.
OpenTargetsiENSG00000167553.
PharmGKBiPA162407345.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOVERGENiHBG000089.
InParanoidiQ9BQE3.
KOiK07374.
PhylomeDBiQ9BQE3.
TreeFamiTF300314.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000167553-MONOMER.
ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-190840. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
R-HSA-190861. Gap junction assembly.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
R-HSA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
R-HSA-389960. Formation of tubulin folding intermediates by CCT/TriC.
R-HSA-389977. Post-chaperonin tubulin folding pathway.
R-HSA-437239. Recycling pathway of L1.
R-HSA-5610787. Hedgehog 'off' state.
R-HSA-5617833. Assembly of the primary cilium.
R-HSA-5620924. Intraflagellar transport.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6807878. COPI-mediated anterograde transport.
R-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-983189. Kinesins.
SIGNORiQ9BQE3.

Miscellaneous databases

ChiTaRSiTUBA1C. human.
GeneWikiiTUBA1C.
GenomeRNAii84790.
PMAP-CutDBQ9BQE3.
PROiQ9BQE3.

Gene expression databases

BgeeiENSG00000167553.
CleanExiHS_TUBA1C.
ExpressionAtlasiQ9BQE3. baseline and differential.
GenevisibleiQ9BQE3. HS.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. 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]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTBA1C_HUMAN
AccessioniPrimary (citable) accession number: Q9BQE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: June 1, 2001
Last modified: November 30, 2016
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.