Q9Y2S7 · PDIP2_HUMAN
- ProteinPolymerase delta-interacting protein 2
- GenePOLDIP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids368 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in DNA damage tolerance by regulating translesion synthesis (TLS) of templates carrying DNA damage lesions such as 8oxoG and abasic sites (PubMed:24191025).
May act by stimulating activity of DNA polymerases involved in TLS, such as PRIMPOL and polymerase delta (POLD1) (PubMed:24191025, PubMed:26984527).
May act by stimulating activity of DNA polymerases involved in TLS, such as PRIMPOL and polymerase delta (POLD1) (PubMed:24191025, PubMed:26984527).
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 | cell-cell junction | |
Cellular Component | midbody | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrial nucleoid | |
Cellular Component | mitochondrion | |
Cellular Component | mitotic spindle | |
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Biological Process | error-free translesion synthesis | |
Biological Process | mitochondrion organization | |
Biological Process | mitotic spindle assembly | |
Biological Process | negative regulation of macroautophagy | |
Biological Process | positive regulation of focal adhesion assembly | |
Biological Process | positive regulation of mitotic cell cycle | |
Biological Process | positive regulation of mitotic cytokinesis | |
Biological Process | vascular associated smooth muscle cell proliferation |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePolymerase delta-interacting protein 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y2S7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Mainly localizes to the mitochondrial matrix; a small fraction localizes in the nucleus.
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 351 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 transit peptide, chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-51 | UniProt | Mitochondrion | ||||
Sequence: MAACTARRALAVGSRWWSRSLTGARWPRPLCAAAGAGAFSPASTTTTRRHL | |||||||
Chain | PRO_0000197975 | 52-368 | UniProt | Polymerase delta-interacting protein 2 | |||
Sequence: SSRNRPEGKVLETVGVFEVPKQNGKYETGQLFLHSIFGYRGVVLFPWQARLYDRDVASAAPEKAENPAGHGSKEVKGKTHTYYQVLIDARDCPHISQRSQTEAVTFLANHDDSRALYAIPGLDYVSHEDILPYTSTDQVPIQHELFERFLLYDQTKAPPFVARETLRAWQEKNHPWLELSDVHRETTENIRVTVIPFYMGMREAQNSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLSKEQPAFQYSSHVSLQASSGHMWGTFRFERPDGSHFDVRIPPFSLESNKDEKTPPSGLHW | |||||||
Modified residue (large scale data) | 290 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 292 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 292 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 295 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with PCNA and POLD2 (PubMed:12522211).
Interacts with SSBP1 (PubMed:16428295).
Interacts with PRIMPOL; leading to enhance DNA polymerase activity of PRIMPOL (PubMed:26984527).
Interacts with POLH (PubMed:20554254).
Interacts with POLD1; leading to stimulate DNA polymerase activity of POLD1 (PubMed:24191025).
Interacts with SSBP1 (PubMed:16428295).
Interacts with PRIMPOL; leading to enhance DNA polymerase activity of PRIMPOL (PubMed:26984527).
Interacts with POLH (PubMed:20554254).
Interacts with POLD1; leading to stimulate DNA polymerase activity of POLD1 (PubMed:24191025).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y2S7 | AGTRAP Q6RW13-2 | 3 | EBI-713000, EBI-11522760 | |
BINARY | Q9Y2S7 | ALAS1 P13196 | 4 | EBI-713000, EBI-3905054 | |
BINARY | Q9Y2S7 | CHCHD2 Q9Y6H1 | 8 | EBI-713000, EBI-2321769 | |
BINARY | Q9Y2S7 | DNAAF6 Q9NQM4 | 3 | EBI-713000, EBI-10239299 | |
BINARY | Q9Y2S7 | MTUS2 Q5JR59 | 3 | EBI-713000, EBI-742948 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 235-360 | ApaG | ||||
Sequence: RETTENIRVTVIPFYMGMREAQNSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLSKEQPAFQYSSHVSLQASSGHMWGTFRFERPDGSHFDVRIPPFSLESNKDEK |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length368
- Mass (Da)42,033
- Last updated1999-11-01 v1
- Checksum1882F93273542CCF
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
B4DEM9 | B4DEM9_HUMAN | POLDIP2 | 350 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 9 | in Ref. 1; AAK92018 | ||||
Sequence: A → P | ||||||
Sequence conflict | 28 | in Ref. 1; AAK92018 | ||||
Sequence: R → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF179891 EMBL· GenBank· DDBJ | AAK92018.1 EMBL· GenBank· DDBJ | mRNA | ||
AF077203 EMBL· GenBank· DDBJ | AAD26998.1 EMBL· GenBank· DDBJ | mRNA | ||
AK313232 EMBL· GenBank· DDBJ | BAG36043.1 EMBL· GenBank· DDBJ | mRNA | ||
BC000655 EMBL· GenBank· DDBJ | AAH00655.1 EMBL· GenBank· DDBJ | mRNA | ||
BC009265 EMBL· GenBank· DDBJ | AAH09265.1 EMBL· GenBank· DDBJ | mRNA |