Reviewed,
UniProtKB/Swiss-Prot Q3MJK5 (CD2L7_RAT)
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June 16, 2009.
Version 36.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
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 Cyclin-dependent kinase 12 Protein kinase for splicing component | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
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. Ref.1 |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. |
| Subunit structure | Interacts with CCNL1 and CCNL2. Ref.1 |
| Subcellular location | |
| Tissue specificity | Expressed in embryonic tissues such as brain, spinal cord, heart, lung, liver, gut and limb. Levels are lower in adult tissues. Ref.1 |
| Developmental stage | Expressed at E10.5 and E14.5. Ref.1 |
| 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 | 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 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q3MJK5-1) Also known as: CDK12(L); 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: Q3MJK5-2) Also known as: CDK12(S); The sequence of this isoform differs from the canonical sequence as follows: 1250-1258: ACPPHILPP → GKQTGHESQ 1259-1484: Missing. |
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_0000314471 | |||||
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 By similarity | ||||||
| Modified residue | 275 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 278 | 1 | Phosphotyrosine By similarity | ||||||
| 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 By similarity | ||||||
| Modified residue | 319 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 322 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 324 | 1 | Phosphoserine By similarity | ||||||
| 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 By similarity | ||||||
| Modified residue | 384 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 399 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 422 | 1 | Phosphoserine 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 By similarity | ||||||
| Modified residue | 1079 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1240 | 1 | Phosphothreonine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1250 – 1258 | 9 | ACPPHILPP → GKQTGHESQ in isoform 2. | VSP_030288 | |||||
| Alternative sequence | 1259 – 1484 | 226 | Missing in isoform 2. | VSP_030289 | |||||
Sequences
| ||||||||||||||||||||||||
References
| [1] | "Identification and characterization of the CDK12/cyclin L1 complex involved in alternative splicing regulation." Chen H.-H., Wang Y.-C., Fann M.-J. Mol. Cell. Biol. 26:2736-2745(2006) [PubMed: 16537916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH CCNL1 AND CCNL2, SUBCELLULAR LOCATION, FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY. Strain: Sprague-Dawley. |
Cross-references
Sequence databases | |
|---|---|
| AY072294 mRNA. Translation: AAL69525.1. AY962568 mRNA. Translation: AAY41734.1. | |
| IPI | IPI00200175. IPI00569900. |
| RefSeq | NP_001029039.1. NP_620271.1. |
| UniGene | Rn.48817 |
3D structure databases | |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q3MJK5. |
Genome annotation databases | |
| Ensembl | ENSRNOG00000006000. Rattus norvegicus. [Contig view] |
| GeneID | 192350. |
| KEGG | rno:192350. |
Organism-specific databases | |
| RGD | 621111. Crkrs. |
Phylogenomic databases | |
| HOVERGEN | Q3MJK5. |
| OMA | Q3MJK5. LMKTQEP. |
Enzyme and pathway databases | |
| BRENDA | 2.7.11.22. 248. |
Gene expression databases | |
| ArrayExpress | Q3MJK5. |
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 | 623019. |
Entry information
| Entry name | CD2L7_RAT | ||||||||
| Accession | Primary (citable) accession number: Q3MJK5 Secondary accession number(s): Q8R458 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
