Q99MU0 · DBF4A_CRIGR
- ProteinProtein DBF4 homolog A
- GeneDBF4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids676 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Regulatory subunit for CDC7 which activates its kinase activity thereby playing a central role in DNA replication and cell proliferation. Required for progression of S phase. The complex CDC7-DBF4A selectively phosphorylates MCM2 subunit at 'Ser-40' and 'Ser-53' and then is involved in regulating the initiation of DNA replication during cell cycle (By similarity).
Features
Showing features for binding site.
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 | Dbf4-dependent protein kinase complex | |
Molecular Function | nucleic acid binding | |
Molecular Function | protein serine/threonine kinase activator activity | |
Molecular Function | zinc ion binding | |
Biological Process | DNA replication | |
Biological Process | positive regulation of nuclear cell cycle DNA replication | |
Biological Process | regulation of cell cycle phase transition |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameProtein DBF4 homolog A
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Cricetidae > Cricetinae > Cricetulus
Accessions
- Primary accessionQ99MU0
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000234060 | 1-676 | Protein DBF4 homolog A | |||
Sequence: MNSGAMRIHSKGHFQGGIQVKNEKNRPSLKSLKTDNRPEKSKCKPLWEKVFYLDLPSVTISEKLQKDIKDLGGRVEEFLSKDISYLVSNKKEAKYAQTLGQVSPVPSPESAYTAETTSPHPSHDGSSFKSPDRVCLSRGKLLAEKAVKDHDFIPANSILSNALTWGVKILHIDDIRYYIEQKKKELCSLKKSSTSVRDSGKKAGTTIQKARTGRLKKPFLKVEDVNRSYRPFYLQLTSVPSINYATHKPCSPFDIEKPSSVQKQAQPKPRPNTDGDKCGGTPVQLQLKEKRKKGYCECCLQKYEDLETHLLSEKHKNFAQSNQYQVVDDIVSKLVFDFVEYERDTPKKKRIKYSVGSFSSVSANVLKNTEPKEKLQLEPIFQKDMVESNGQLPEEIFQCEDIQCEDIQKPEQRLVLASEPMSYSSTGLKGRDEKAASMLNASEPDIKQKFTQLPPCKNEQEGILDVSEHKLIINRNDLEQRVGDSVGVPRSCVQVSHLSPENSLPQPKLTADTTHFSAKDLQEKDLHFVFGHDSDLVTLNTSKEQLTVKAGTPSCGPQQPNECDTENTDNLPCGKIQRKVRLLLGQKKKNVDPSAELDKKRTEFLPMCEDRTCGSPVQSLLDLFQTSGEKSDFLGFTSYTENSGLCDVLDVWEDENSSSLLSTFFSSPSASTFIGF | ||||||
Modified residue | 273 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 312 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 345 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 354 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 359 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 418 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 627 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 669 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 671 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation increases its interaction with PSIP1.
Keywords
- PTM
Proteomic databases
Expression
Induction
Up-regulated when cells reaches the G1/S boundary. Down-regulated by gamma-irradiation.
Interaction
Subunit
Forms a complex with CDC7. Note that CDC7 forms distinct complex either with DBF4A or DBF4B. Such complexes are stable upon replication stress. Interacts with MEN1, MCM2, ORC2, ORC4 and ORC6 (By similarity).
Interacts (via IBM motifs) with PSIP1 (via IBD domain); phosphorylation increases its affinity for PSIP1 (By similarity).
Interacts (via IBM motifs) with PSIP1 (via IBD domain); phosphorylation increases its affinity for PSIP1 (By similarity).
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, zinc finger, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-40 | Disordered | ||||
Sequence: MNSGAMRIHSKGHFQGGIQVKNEKNRPSLKSLKTDNRPEK | ||||||
Compositional bias | 26-40 | Basic and acidic residues | ||||
Sequence: RPSLKSLKTDNRPEK | ||||||
Domain | 40-128 | BRCT 1 | ||||
Sequence: KSKCKPLWEKVFYLDLPSVTISEKLQKDIKDLGGRVEEFLSKDISYLVSNKKEAKYAQTLGQVSPVPSPESAYTAETTSPHPSHDGSSF | ||||||
Compositional bias | 98-125 | Polar residues | ||||
Sequence: TLGQVSPVPSPESAYTAETTSPHPSHDG | ||||||
Region | 98-132 | Disordered | ||||
Sequence: TLGQVSPVPSPESAYTAETTSPHPSHDGSSFKSPD | ||||||
Domain | 154-179 | BRCT 2 | ||||
Sequence: PANSILSNALTWGVKILHIDDIRYYI | ||||||
Region | 253-281 | Disordered | ||||
Sequence: FDIEKPSSVQKQAQPKPRPNTDGDKCGGT | ||||||
Zinc finger | 289-337 | DBF4-type | ||||
Sequence: EKRKKGYCECCLQKYEDLETHLLSEKHKNFAQSNQYQVVDDIVSKLVFD | ||||||
Motif | 616-640 | Integrase domain-binding motif 1 (IBM1) | ||||
Sequence: PVQSLLDLFQTSGEKSDFLGFTSYT | ||||||
Motif | 657-676 | Integrase domain-binding motif 2 (IBM2) | ||||
Sequence: SSSLLSTFFSSPSASTFIGF |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length676
- Mass (Da)75,850
- Last updated2001-06-01 v1
- ChecksumEC7EEBDD80D40B8C
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 26-40 | Basic and acidic residues | ||||
Sequence: RPSLKSLKTDNRPEK | ||||||
Compositional bias | 98-125 | Polar residues | ||||
Sequence: TLGQVSPVPSPESAYTAETTSPHPSHDG |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF292400 EMBL· GenBank· DDBJ | AAK21856.1 EMBL· GenBank· DDBJ | mRNA |