Q9H7T9 · AUNIP_HUMAN
- ProteinAurora kinase A- and ninein-interacting protein
- GeneAUNIP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids357 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
DNA-binding protein that accumulates at DNA double-strand breaks (DSBs) following DNA damage and promotes DNA resection and homologous recombination (PubMed:29042561).
Serves as a sensor of DNA damage: binds DNA with a strong preference for DNA substrates that mimic structures generated at stalled replication forks, and anchors RBBP8/CtIP to DSB sites to promote DNA end resection and ensuing homologous recombination repair (PubMed:29042561).
Inhibits non-homologous end joining (NHEJ) (PubMed:29042561).
Required for the dynamic movement of AURKA at the centrosomes and spindle apparatus during the cell cycle (PubMed:20596670).
Serves as a sensor of DNA damage: binds DNA with a strong preference for DNA substrates that mimic structures generated at stalled replication forks, and anchors RBBP8/CtIP to DSB sites to promote DNA end resection and ensuing homologous recombination repair (PubMed:29042561).
Inhibits non-homologous end joining (NHEJ) (PubMed:29042561).
Required for the dynamic movement of AURKA at the centrosomes and spindle apparatus during the cell cycle (PubMed:20596670).
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 | centrosome | |
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | site of DNA damage | |
Cellular Component | spindle pole | |
Molecular Function | damaged DNA binding | |
Biological Process | double-strand break repair via homologous recombination | |
Biological Process | negative regulation of double-strand break repair via nonhomologous end joining | |
Biological Process | spindle organization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAurora kinase A- and ninein-interacting protein
- Short namesAIBp
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H7T9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_031776 | 82 | in dbSNP:rs34449716 | |||
Sequence: K → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 400 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000284572 | 1-357 | UniProt | Aurora kinase A- and ninein-interacting protein | |||
Sequence: MRRTGPEEEACGVWLDAAALKRRKVQTHLIKPGTKMLTLLPGERKANIYFTQRRAPSTGIHQRSIASFFTLQPGKTNGSDQKSVSSHTESQINKESKKNATQLDHLIPGLAHDCMASPLATSTTADIQEAGLSPQSLQTSGHHRMKTPFSTELSLLQPDTPDCAGDSHTPLAFSFTEDLESSCLLDRKEEKGDSARKWEWLHESKKNYQSMEKHTKLPGDKCCQPLGKTKLERKVSAKENRQAPVLLQTYRESWNGENIESVKQSRSPVSVFSWDNEKNDKDSWSQLFTEDSQGQRVIAHNTRAPFQDVTNNWNWDLGPFPNSPWAQCQEDGPTQNLKPDLLFTQDSEGNQVIRHQF | |||||||
Modified residue (large scale data) | 265 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 267 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 267 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 292 | UniProt | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts (via C-terminus) with AURKA (via C-terminus) (PubMed:20596670).
Interacts (via N-terminus) with NIN; this interaction blocks NIN phosphorylation by both AURKA and GSK3B (PubMed:20596670).
Identified in a complex with NIN and AURKA (PubMed:20596670).
Interacts with RBBP8/CtIP (PubMed:29042561).
Interacts (via N-terminus) with NIN; this interaction blocks NIN phosphorylation by both AURKA and GSK3B (PubMed:20596670).
Identified in a complex with NIN and AURKA (PubMed:20596670).
Interacts with RBBP8/CtIP (PubMed:29042561).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9H7T9 | C14orf119 Q9NWQ9 | 3 | EBI-10693257, EBI-725606 | |
BINARY | Q9H7T9 | DR1 Q01658 | 3 | EBI-10693257, EBI-750300 | |
BINARY | Q9H7T9 | FGFR3 P22607 | 3 | EBI-10693257, EBI-348399 | |
BINARY | Q9H7T9 | GSN P06396 | 3 | EBI-10693257, EBI-351506 | |
BINARY | Q9H7T9 | GTF3C3 Q9Y5Q9 | 3 | EBI-10693257, EBI-1054873 | |
BINARY | Q9H7T9 | HRAS P01112 | 3 | EBI-10693257, EBI-350145 | |
BINARY | Q9H7T9 | NXF1 Q9UBU9 | 3 | EBI-10693257, EBI-398874 | |
BINARY | Q9H7T9 | PRKAB2 O43741 | 3 | EBI-10693257, EBI-1053424 | |
BINARY | Q9H7T9 | Q9Y649 | 3 | EBI-10693257, EBI-25900580 | |
BINARY | Q9H7T9 | TRIM68 Q6AZZ1 | 2 | EBI-10693257, EBI-2130449 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 71-90 | Polar residues | ||||
Sequence: LQPGKTNGSDQKSVSSHTES | ||||||
Region | 71-98 | Disordered | ||||
Sequence: LQPGKTNGSDQKSVSSHTESQINKESKK | ||||||
Region | 187-357 | Interaction with AURKA | ||||
Sequence: RKEEKGDSARKWEWLHESKKNYQSMEKHTKLPGDKCCQPLGKTKLERKVSAKENRQAPVLLQTYRESWNGENIESVKQSRSPVSVFSWDNEKNDKDSWSQLFTEDSQGQRVIAHNTRAPFQDVTNNWNWDLGPFPNSPWAQCQEDGPTQNLKPDLLFTQDSEGNQVIRHQF | ||||||
Region | 281-357 | Interaction with RBBP8/CtIP | ||||
Sequence: KDSWSQLFTEDSQGQRVIAHNTRAPFQDVTNNWNWDLGPFPNSPWAQCQEDGPTQNLKPDLLFTQDSEGNQVIRHQF |
Sequence similarities
Belongs to the AUNIP family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9H7T9-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length357
- Mass (Da)40,253
- Last updated2001-03-01 v1
- Checksum8080DCF2E3CAB569
Q9H7T9-2
- Name2
- Differences from canonical
- 349-357: GNQVIRHQF → VQALACQQDCCRRSILKRQKHLR
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 71-90 | Polar residues | ||||
Sequence: LQPGKTNGSDQKSVSSHTES | ||||||
Alternative sequence | VSP_044288 | 349-357 | in isoform 2 | |||
Sequence: GNQVIRHQF → VQALACQQDCCRRSILKRQKHLR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GQ844687 EMBL· GenBank· DDBJ | ACV90488.1 EMBL· GenBank· DDBJ | mRNA | ||
AK024326 EMBL· GenBank· DDBJ | BAB14886.1 EMBL· GenBank· DDBJ | mRNA | ||
AK223419 EMBL· GenBank· DDBJ | BAD97139.1 EMBL· GenBank· DDBJ | mRNA | ||
AL020996 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL033528 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC000209 EMBL· GenBank· DDBJ | AAH00209.1 EMBL· GenBank· DDBJ | mRNA |