Q9BVW5 · TIPIN_HUMAN
- ProteinTIMELESS-interacting protein
- GeneTIPIN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids301 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays an important role in the control of DNA replication and the maintenance of replication fork stability (PubMed:17102137, PubMed:23359676, PubMed:35585232).
Important for cell survival after DNA damage or replication stress (PubMed:17116885).
May be specifically required for the ATR-CHEK1 pathway in the replication checkpoint induced by hydroxyurea or ultraviolet light (PubMed:17296725).
Forms a complex with TIMELESS and this complex regulates DNA replication processes under both normal and stress conditions, stabilizes replication forks and influences both CHEK1 phosphorylation and the intra-S phase checkpoint in response to genotoxic stress (PubMed:17102137, PubMed:17116885, PubMed:17296725, PubMed:23359676, PubMed:35585232).
Important for cell survival after DNA damage or replication stress (PubMed:17116885).
May be specifically required for the ATR-CHEK1 pathway in the replication checkpoint induced by hydroxyurea or ultraviolet light (PubMed:17296725).
Forms a complex with TIMELESS and this complex regulates DNA replication processes under both normal and stress conditions, stabilizes replication forks and influences both CHEK1 phosphorylation and the intra-S phase checkpoint in response to genotoxic stress (PubMed:17102137, PubMed:17116885, PubMed:17296725, PubMed:23359676, PubMed:35585232).
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 | chromatin | |
Cellular Component | cytoplasm | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | replication fork protection complex | |
Molecular Function | DNA binding | |
Biological Process | cell cycle phase transition | |
Biological Process | cell division | |
Biological Process | DNA replication checkpoint signaling | |
Biological Process | mitotic intra-S DNA damage checkpoint signaling | |
Biological Process | positive regulation of cell population proliferation | |
Biological Process | regulation of nuclear cell cycle DNA replication | |
Biological Process | replication fork arrest | |
Biological Process | replication fork processing | |
Biological Process | response to UV |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTIMELESS-interacting protein
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BVW5
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_035194 | 53 | in dbSNP:rs9806123 | |||
Sequence: R → P | ||||||
Natural variant | VAR_035195 | 111 | in dbSNP:rs2063690 | |||
Sequence: A → G | ||||||
Natural variant | VAR_053952 | 260 | in dbSNP:rs3759787 | |||
Sequence: L → P | ||||||
Natural variant | VAR_035196 | 267 | in dbSNP:rs3759786 | |||
Sequence: A → S | ||||||
Natural variant | VAR_062207 | 270 | in dbSNP:rs34848112 | |||
Sequence: N → D | ||||||
Natural variant | VAR_054483 | 270 | in dbSNP:rs780014564 | |||
Sequence: N → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 310 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_0000305253 | 1-301 | UniProt | TIMELESS-interacting protein | |||
Sequence: MLEPQENGVIDLPDYEHVEDETFPPFPPPASPERQDGEGTEPDEESGNGAPVRVPPKRTVKRNIPKLDAQRLISERGLPALRHVFDKAKFKGKGHEAEDLKMLIRHMEHWAHRLFPKLQFEDFIDRVEYLGSKKEVQTCLKRIRLDLPILHEDFVSNNDEVAENNEHDVTSTELDPFLTNLSESEMFASELSRSLTEEQQQRIERNKQLALERRQAKLLSNSQTLGNDMLMNTPRAHTVEEVNTDEDQKEESNGLNEDILDNPCNDAIANTLNEEETLLDQSFKNVQQQLDATSRNITEAR | |||||||
Modified residue (large scale data) | 31 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 194 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 194 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 196 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 220 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 222 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 222 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 233 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 233 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 244 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 244 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with TIMELESS (via N-terminus), which impairs TIMELESS self-association (PubMed:17102137, PubMed:17116885, PubMed:17296725, PubMed:23359676, PubMed:28334766, PubMed:34694004, PubMed:34700328).
Associates with the MCM2-7 complex (PubMed:34694004, PubMed:34700328).
Interacts with RPA2, PRDX2 (PubMed:17141802, PubMed:17296725).
Associates with the MCM2-7 complex (PubMed:34694004, PubMed:34700328).
Interacts with RPA2, PRDX2 (PubMed:17141802, PubMed:17296725).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BVW5 | GSC2 O15499 | 3 | EBI-2515360, EBI-19954058 | |
BINARY | Q9BVW5 | RPA2 P15927 | 4 | EBI-2515360, EBI-621404 | |
BINARY | Q9BVW5 | SPRED1 Q7Z699 | 3 | EBI-2515360, EBI-5235340 | |
BINARY | Q9BVW5 | TEX11 Q8IYF3 | 3 | EBI-2515360, EBI-742397 | |
BINARY | Q9BVW5 | TIMELESS Q9UNS1 | 4 | EBI-2515360, EBI-2212315 |
Protein-protein interaction databases
Miscellaneous
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-61 | Disordered | ||||
Sequence: MLEPQENGVIDLPDYEHVEDETFPPFPPPASPERQDGEGTEPDEESGNGAPVRVPPKRTVK | ||||||
Region | 67-143 | Interaction with TIMELESS | ||||
Sequence: LDAQRLISERGLPALRHVFDKAKFKGKGHEAEDLKMLIRHMEHWAHRLFPKLQFEDFIDRVEYLGSKKEVQTCLKRI | ||||||
Compositional bias | 240-256 | Basic and acidic residues | ||||
Sequence: EEVNTDEDQKEESNGLN | ||||||
Region | 240-261 | Disordered | ||||
Sequence: EEVNTDEDQKEESNGLNEDILD |
Sequence similarities
Belongs to the CSM3 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length301
- Mass (Da)34,555
- Last updated2010-05-18 v2
- ChecksumB0C69117A636CE3A
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 201 | in Ref. 1; BAA91229 | ||||
Sequence: Q → R | ||||||
Compositional bias | 240-256 | Basic and acidic residues | ||||
Sequence: EEVNTDEDQKEESNGLN |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK000523 EMBL· GenBank· DDBJ | BAA91229.1 EMBL· GenBank· DDBJ | mRNA | ||
EU551725 EMBL· GenBank· DDBJ | ACB21044.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC055855 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471082 EMBL· GenBank· DDBJ | EAW77762.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000870 EMBL· GenBank· DDBJ | AAH00870.1 EMBL· GenBank· DDBJ | mRNA | ||
BK001386 EMBL· GenBank· DDBJ | DAA01365.1 EMBL· GenBank· DDBJ | mRNA |