O00311 · CDC7_HUMAN
- ProteinCell division cycle 7-related protein kinase
- GeneCDC7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids574 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]This reaction proceeds in the forward direction.
Cofactor
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | intercellular bridge | |
Cellular Component | mitotic spindle | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | kinase activity | |
Molecular Function | metal ion binding | |
Molecular Function | protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | cell cycle phase transition | |
Biological Process | cell division | |
Biological Process | double-strand break repair via break-induced replication | |
Biological Process | G1/S transition of mitotic cell cycle | |
Biological Process | positive regulation of cell population proliferation | |
Biological Process | positive regulation of G2/M transition of mitotic cell cycle | |
Biological Process | positive regulation of nuclear cell cycle DNA replication | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCell division cycle 7-related protein kinase
- EC number
- Short namesCDC7-related kinase; HsCdc7; huCdc7
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00311
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_019255 | 23 | in dbSNP:rs13447459 | |||
Sequence: Q → P | ||||||
Natural variant | VAR_019256 | 99 | in dbSNP:rs13447492 | |||
Sequence: I → V | ||||||
Natural variant | VAR_019257 | 112 | in dbSNP:rs13447493 | |||
Sequence: G → W | ||||||
Natural variant | VAR_019258 | 162 | in dbSNP:rs13447503 | |||
Sequence: F → L | ||||||
Natural variant | VAR_040403 | 208 | in dbSNP:rs34979509 | |||
Sequence: I → M | ||||||
Natural variant | VAR_040404 | 209 | in dbSNP:rs56327502 | |||
Sequence: E → D | ||||||
Natural variant | VAR_019259 | 441 | in dbSNP:rs13447539 | |||
Sequence: K → R | ||||||
Natural variant | VAR_040405 | 472 | in dbSNP:rs56381770 | |||
Sequence: T → I | ||||||
Natural variant | VAR_040406 | 498 | in dbSNP:rs35055915 | |||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 653 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 chain, modified residue, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000085763 | 1-574 | UniProt | Cell division cycle 7-related protein kinase | |||
Sequence: MEASLGIQMDEPMAFSPQRDRFQAEGSLKKNEQNFKLAGVKKDIEKLYEAVPQLSNVFKIEDKIGEGTFSSVYLATAQLQVGPEEKIALKHLIPTSHPIRIAAELQCLTVAGGQDNVMGVKYCFRKNDHVVIAMPYLEHESFLDILNSLSFQEVREYMLNLFKALKRIHQFGIVHRDVKPSNFLYNRRLKKYALVDFGLAQGTHDTKIELLKFVQSEAQQERCSQNKSHIITGNKIPLSGPVPKELDQQSTTKASVKRPYTNAQIQIKQGKDGKEGSVGLSVQRSVFGERNFNIHSSISHESPAVKLMKQSKTVDVLSRKLATKKKAISTKVMNSAVMRKTASSCPASLTCDCYATDKVCSICLSRRQQVAPRAGTPGFRAPEVLTKCPNQTTAIDMWSAGVIFLSLLSGRYPFYKASDDLTALAQIMTIRGSRETIQAAKTFGKSILCSKEVPAQDLRKLCERLRGMDSSTPKLTSDIQGHASHQPAISEKTDHKASCLVQTPPGQYSGNSFKKGDSNSCEHCFDEYNTNLEGWNEVPDEAYDLLDKLLDLNPASRITAEEALLHPFFKDMSL | |||||||
Modified residue | 27 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 27 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 268 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 277 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 296 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 297 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 302 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 490 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 503 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 503 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 509 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 512 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with CLASPIN (via the acidic patch); the interaction is required for phosphorylation of MCM proteins and CLASPIN (PubMed:27401717).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 58-574 | Protein kinase | ||||
Sequence: FKIEDKIGEGTFSSVYLATAQLQVGPEEKIALKHLIPTSHPIRIAAELQCLTVAGGQDNVMGVKYCFRKNDHVVIAMPYLEHESFLDILNSLSFQEVREYMLNLFKALKRIHQFGIVHRDVKPSNFLYNRRLKKYALVDFGLAQGTHDTKIELLKFVQSEAQQERCSQNKSHIITGNKIPLSGPVPKELDQQSTTKASVKRPYTNAQIQIKQGKDGKEGSVGLSVQRSVFGERNFNIHSSISHESPAVKLMKQSKTVDVLSRKLATKKKAISTKVMNSAVMRKTASSCPASLTCDCYATDKVCSICLSRRQQVAPRAGTPGFRAPEVLTKCPNQTTAIDMWSAGVIFLSLLSGRYPFYKASDDLTALAQIMTIRGSRETIQAAKTFGKSILCSKEVPAQDLRKLCERLRGMDSSTPKLTSDIQGHASHQPAISEKTDHKASCLVQTPPGQYSGNSFKKGDSNSCEHCFDEYNTNLEGWNEVPDEAYDLLDKLLDLNPASRITAEEALLHPFFKDMSL |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms may be produced.
O00311-1
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
- Length574
- Mass (Da)63,888
- Last updated1997-07-01 v1
- Checksum90D549BEE20AE583
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
B1AMW7 | B1AMW7_HUMAN | CDC7 | 157 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 89 | in Ref. 3; AAB97512 | ||||
Sequence: L → V |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB003698 EMBL· GenBank· DDBJ | BAA19962.1 EMBL· GenBank· DDBJ | mRNA | ||
AF015592 EMBL· GenBank· DDBJ | AAC52080.1 EMBL· GenBank· DDBJ | mRNA | ||
AF005209 EMBL· GenBank· DDBJ | AAB97512.1 EMBL· GenBank· DDBJ | mRNA | ||
AY585721 EMBL· GenBank· DDBJ | AAS79323.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL355871 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471097 EMBL· GenBank· DDBJ | EAW73114.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471097 EMBL· GenBank· DDBJ | EAW73115.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC110526 EMBL· GenBank· DDBJ | AAI10527.1 EMBL· GenBank· DDBJ | mRNA | ||
BC110527 EMBL· GenBank· DDBJ | AAI10528.1 EMBL· GenBank· DDBJ | mRNA | ||
BC111044 EMBL· GenBank· DDBJ | AAI11045.1 EMBL· GenBank· DDBJ | mRNA |