Reviewed,
UniProtKB/Swiss-Prot Q14AX6 (CD2L7_MOUSE)
Last modified
November 3, 2009.
Version 36.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cell division cycle 2-related protein kinase 7 Short name=CDC2-related protein kinase 7 EC=2.7.11.22 Alternative name(s): Cdc2-related kinase, arginine/serine-rich Short name=CrkRS | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 1484 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Involved in the regulation of alternative mRNA splicing By similarity. |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. |
| Subunit structure | Interacts with CCNL1 and CCNL2 By similarity. |
| Subcellular location | Nucleus. Nucleus speckle By similarity. |
| Sequence similarities | Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Nucleus |
| Coding sequence diversity | Alternative splicing |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Serine/threonine-protein kinase Transferase |
| PTM | Acetylation Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro |
| Cellular component | nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cyclin-dependent protein kinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q14AX6-1) 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. | ||||||
| Isoform 2 (identifier: Q14AX6-2) The sequence of this isoform differs from the canonical sequence as follows: 1250-1258: ACPPHILPP → GKQTGHESH 1259-1484: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 3 (identifier: Q14AX6-3) The sequence of this isoform differs from the canonical sequence as follows: 1250-1258: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1484 | 1484 | Cell division cycle 2-related protein kinase 7 | PRO_0000314470 | |||||
Regions | |||||||||
| Domain | 723 – 1016 | 294 | Protein kinase | ||||||
| Nucleotide binding | 729 – 737 | 9 | ATP By similarity | ||||||
| Compositional bias | 137 – 393 | 257 | Ser-rich | ||||||
| Compositional bias | 406 – 412 | 7 | Poly-Ala | ||||||
| Compositional bias | 524 – 703 | 180 | Pro-rich | ||||||
| Compositional bias | 1234 – 1276 | 43 | Pro-rich | ||||||
Sites | |||||||||
| Active site | 855 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 752 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 24 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 25 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 32 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 57 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 73 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 77 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 78 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 80 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 84 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 214 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 235 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 237 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 248 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 264 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 273 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 275 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 278 | 1 | Phosphotyrosine Ref.4 | ||||||
| Modified residue | 290 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 292 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 300 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 302 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 317 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 318 | 1 | Phosphotyrosine Ref.4 | ||||||
| Modified residue | 319 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 322 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 324 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 331 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 332 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 333 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 340 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 342 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 344 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 381 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 382 | 1 | Phosphoserine Ref.4 Ref.7 | ||||||
| Modified residue | 384 | 1 | Phosphoserine Ref.4 Ref.7 | ||||||
| Modified residue | 399 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 422 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 501 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 511 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 677 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 681 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 688 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 889 | 1 | Phosphothreonine Ref.5 | ||||||
| Modified residue | 1071 | 1 | Phosphothreonine Ref.4 | ||||||
| Modified residue | 1079 | 1 | Phosphoserine Ref.5 Ref.6 | ||||||
| Modified residue | 1240 | 1 | Phosphothreonine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1250 – 1258 | 9 | ACPPHILPP → GKQTGHESH in isoform 2. | VSP_030285 | |||||
| Alternative sequence | 1250 – 1258 | 9 | Missing in isoform 3. | VSP_030286 | |||||
| Alternative sequence | 1259 – 1484 | 226 | Missing in isoform 2. | VSP_030287 | |||||
Experimental info | |||||||||
| Sequence conflict | 425 – 427 | 3 | ILP → FCL in BAC98047. Ref.3 | ||||||
Sequences
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References
| [1] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). |
| [3] | "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H. DNA Res. 10:167-180(2003) [PubMed: 14621295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 425-1484 (ISOFORM 3). Tissue: Embryonic tail. |
| [4] | "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-278; TYR-318; SER-322; SER-324; SER-382; SER-384 AND THR-1071, MASS SPECTROMETRY. Tissue: Liver. |
| [5] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; THR-889 AND SER-1079, MASS SPECTROMETRY. |
| [6] | "The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1079, MASS SPECTROMETRY. Tissue: Macrophage. |
| [7] | "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382 AND SER-384, MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| AL591205 Genomic DNA. Translation: CAM21267.1. AL591205 Genomic DNA. Translation: CAM21268.1. AL591205 Genomic DNA. Translation: CAM21269.1. BC116645 mRNA. Translation: AAI16646.1. AK129237 mRNA. Translation: BAC98047.1. | |
| IPI | IPI00321774. IPI00648022. IPI00649269. |
| RefSeq | NP_001103096.1. NP_001103098.1. NP_081228.2. |
| UniGene | Mm.260516 |
3D structure databases | |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q14AX6. |
Proteomic databases | |
| PRIDE | Q14AX6. |
Genome annotation databases | |
| Ensembl | ENSMUST00000003203; ENSMUSP00000003203; ENSMUSG00000003119; Mus musculus. [Genome view] ENSMUST00000107538; ENSMUSP00000103162; ENSMUSG00000003119; Mus musculus. [Genome view] |
| GeneID | 69131. |
| KEGG | mmu:69131. |
| NMPDR | fig|10090.3.peg.25190. |
| UCSC | uc007lfs.1. mouse. |
Organism-specific databases | |
| CTD | 69131. |
| MGI | MGI:1098802. Crkrs. |
| Rouge | Search... |
Phylogenomic databases | |
| HOVERGEN | Q14AX6. |
| OMA | LMKTQEP. |
Enzyme and pathway databases | |
| BRENDA | 2.7.11.22. 244. |
Gene expression databases | |
| ArrayExpress | Q14AX6. |
| Bgee | Q14AX6. |
| CleanEx | MM_CRKRS. |
| Genevestigator | Q14AX6. |
Family and domain databases | |
| InterPro | IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view] |
| Pfam | PF00069. Pkinase. 1 hit. [Graphical view] |
| ProDom | PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00220. S_TKc. 1 hit. [Graphical view] |
| PROSITE | PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 328674. |
| SOURCE | Search... |
Entry information
| Entry name | CD2L7_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q14AX6 Secondary accession number(s): A2A530, A2A531, Q6ZQ27 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| Human and mouse protein kinases Human and mouse protein kinases: classification and index |
| SIMILARITY comments Index of protein domains and families |

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