Q9Y6A5 · TACC3_HUMAN
- ProteinTransforming acidic coiled-coil-containing protein 3
- GeneTACC3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids838 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors (By similarity).
Acts as a component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (PubMed:21297582, PubMed:23532825).
May be involved in the control of cell growth and differentiation. May contribute to cancer (PubMed:14767476).
Acts as a component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (PubMed:21297582, PubMed:23532825).
May be involved in the control of cell growth and differentiation. May contribute to cancer (PubMed:14767476).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | centriolar satellite | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | mitotic spindle | |
Cellular Component | spindle pole | |
Biological Process | cell division | |
Biological Process | cell population proliferation | |
Biological Process | cerebral cortex development | |
Biological Process | metaphase/anaphase transition of mitotic cell cycle | |
Biological Process | microtubule cytoskeleton organization | |
Biological Process | microtubule cytoskeleton organization involved in mitosis | |
Biological Process | mitotic spindle organization | |
Biological Process | regulation of mitotic spindle organization |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTransforming acidic coiled-coil-containing protein 3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y6A5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In complex with CKAP5 localized to microtubule plus-ends in mitosis and interphase. In complex with CKAP5 and clathrin localized to inter-microtubule bridges in mitotic spindles.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_053714 | 143 | in dbSNP:rs34205238 | |||
Sequence: E → K | ||||||
Natural variant | VAR_053715 | 275 | in dbSNP:rs17132047 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_053716 | 287 | in dbSNP:rs1063743 | |||
Sequence: G → S | ||||||
Natural variant | VAR_053717 | 514 | in dbSNP:rs17680881 | |||
Sequence: G → E | ||||||
Mutagenesis | 558 | Disrupts localization to mitotic spindle and impairs recruitment of clathrin to mitotic spindle. | ||||
Sequence: S → A | ||||||
Mutagenesis | 566-567 | Impairs localization to mitotic spindle. | ||||
Sequence: LL → AA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,077 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Chain | PRO_0000179990 | 2-838 | UniProt | Transforming acidic coiled-coil-containing protein 3 | |||
Sequence: SLQVLNDKNVSNEKNTENCDFLFSPPEVTGRSSVLRVSQKENVPPKNLAKAMKVTFQTPLRDPQTHRILSPSMASKLEAPFTQDDTLGLENSHPVWTQKENQQLIKEVDAKTTHGILQKPVEADTDLLGDASPAFGSGSSSESGPGALADLDCSSSSQSPGSSENQMVSPGKVSGSPEQAVEENLSSYSLDRRVTPASETLEDPCRTESQHKAETPHGAEEECKAETPHGAEEECRHGGVCAPAAVATSPPGAIPKEACGGAPLQGLPGEALGCPAGVGTPVPADGTQTLTCAHTSAPESTAPTNHLVAGRAMTLSPQEEVAAGQMASSSRSGPVKLEFDVSDGATSKRAPPPRRLGERSGLKPPLRKAAVRQQKAPQEVEEDDGRSGAGEDPPMPASRGSYHLDWDKMDDPNFIPFGGDTKSGCSEAQPPESPETRLGQPAAEQLHAGPATEEPGPCLSQQLHSASAEDTPVVQLAAETPTAESKERALNSASTSLPTSCPGSEPVPTHQQGQPALELKEESFRDPAEVLGTGAEVDYLEQFGTSSFKESALRKQSLYLKFDPLLRDSPGRPVPVATETSSMHGANETPSGRPREAKLVEFDFLGALDIPVPGPPPGVPAPGGPPLSTGPIVDLLQYSQKDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDLFKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQAEALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDLISKMEKI | |||||||
Modified residue | 25 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 39 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 39 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 59 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 71 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 71 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 87 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 175 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 175 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 177 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 177 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 216 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 228 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 249 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 250 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 250 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 315 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 317 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 317 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 402 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 402 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 434 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 434 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 481 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 505 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 524 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 540 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 558 | UniProt | Phosphoserine; by AURKA | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 558 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 570 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 590 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 799 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Up-regulated in various cancer cell lines.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with microtubules. Interacts with CKAP5 independently of clathrin. Interacts with CKAP5 and clathrin forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges; TACC3 (phosphorylated at Ser-558 by AURKA) and CLTC are proposed to form a composite microtubule interaction surface (PubMed:21297582, PubMed:23918938, PubMed:25596274).
Interacts with CCDC100/CEP120. The coiled coil C-terminal region interacts with AH receptor nuclear translocator protein (ARNT) and ARNT2 (By similarity).
Interacts with GCN5L2 and PCAF (PubMed:14767476).
Interacts with CCDC100/CEP120. The coiled coil C-terminal region interacts with AH receptor nuclear translocator protein (ARNT) and ARNT2 (By similarity).
Interacts with GCN5L2 and PCAF (PubMed:14767476).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 123-227 | Disordered | ||||
Sequence: EADTDLLGDASPAFGSGSSSESGPGALADLDCSSSSQSPGSSENQMVSPGKVSGSPEQAVEENLSSYSLDRRVTPASETLEDPCRTESQHKAETPHGAEEECKAE | ||||||
Compositional bias | 135-195 | Polar residues | ||||
Sequence: AFGSGSSSESGPGALADLDCSSSSQSPGSSENQMVSPGKVSGSPEQAVEENLSSYSLDRRV | ||||||
Compositional bias | 197-227 | Basic and acidic residues | ||||
Sequence: PASETLEDPCRTESQHKAETPHGAEEECKAE | ||||||
Region | 311-527 | Disordered | ||||
Sequence: GRAMTLSPQEEVAAGQMASSSRSGPVKLEFDVSDGATSKRAPPPRRLGERSGLKPPLRKAAVRQQKAPQEVEEDDGRSGAGEDPPMPASRGSYHLDWDKMDDPNFIPFGGDTKSGCSEAQPPESPETRLGQPAAEQLHAGPATEEPGPCLSQQLHSASAEDTPVVQLAAETPTAESKERALNSASTSLPTSCPGSEPVPTHQQGQPALELKEESFRD | ||||||
Compositional bias | 375-390 | Basic and acidic residues | ||||
Sequence: QKAPQEVEEDDGRSGA | ||||||
Compositional bias | 486-512 | Polar residues | ||||
Sequence: SKERALNSASTSLPTSCPGSEPVPTHQ | ||||||
Region | 522-577 | Necessary but not sufficient for spindle localization | ||||
Sequence: EESFRDPAEVLGTGAEVDYLEQFGTSSFKESALRKQSLYLKFDPLLRDSPGRPVPV | ||||||
Region | 569-594 | Disordered | ||||
Sequence: DSPGRPVPVATETSSMHGANETPSGR | ||||||
Region | 594-838 | Necessary but not sufficient for spindle localization | ||||
Sequence: RPREAKLVEFDFLGALDIPVPGPPPGVPAPGGPPLSTGPIVDLLQYSQKDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDLFKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQAEALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDLISKMEKI | ||||||
Coiled coil | 637-837 | |||||
Sequence: LQYSQKDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDLFKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQAEALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDLISKMEK |
Sequence similarities
Belongs to the TACC family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length838
- Mass (Da)90,360
- Last updated1999-11-01 v1
- Checksum07F056678096775E
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F8WC55 | F8WC55_HUMAN | TACC3 | 63 | ||
H0Y8F2 | H0Y8F2_HUMAN | TACC3 | 217 | ||
C9JA91 | C9JA91_HUMAN | TACC3 | 230 | ||
A0A494BZT8 | A0A494BZT8_HUMAN | TACC3 | 834 | ||
A0A494C117 | A0A494C117_HUMAN | TACC3 | 325 | ||
E7EMT0 | E7EMT0_HUMAN | TACC3 | 272 | ||
A0A087WUE2 | A0A087WUE2_HUMAN | TACC3 | 478 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 135-195 | Polar residues | ||||
Sequence: AFGSGSSSESGPGALADLDCSSSSQSPGSSENQMVSPGKVSGSPEQAVEENLSSYSLDRRV | ||||||
Compositional bias | 197-227 | Basic and acidic residues | ||||
Sequence: PASETLEDPCRTESQHKAETPHGAEEECKAE | ||||||
Sequence conflict | 342 | in Ref. 2; CAB53009 | ||||
Sequence: V → L | ||||||
Compositional bias | 375-390 | Basic and acidic residues | ||||
Sequence: QKAPQEVEEDDGRSGA | ||||||
Sequence conflict | 406 | in Ref. 2; CAB53009 | ||||
Sequence: D → G | ||||||
Compositional bias | 486-512 | Polar residues | ||||
Sequence: SKERALNSASTSLPTSCPGSEPVPTHQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF093543 EMBL· GenBank· DDBJ | AAD25964.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ243997 EMBL· GenBank· DDBJ | CAB53009.1 EMBL· GenBank· DDBJ | mRNA | ||
BC106071 EMBL· GenBank· DDBJ | AAI06072.1 EMBL· GenBank· DDBJ | mRNA | ||
BC111771 EMBL· GenBank· DDBJ | AAI11772.1 EMBL· GenBank· DDBJ | mRNA |