Reviewed,
UniProtKB/Swiss-Prot Q9NYV4 (CDK12_HUMAN)
Last modified
February 9, 2010.
Version 87.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cell division protein kinase 12 EC=2.7.11.22 Alternative name(s): Cell division cycle 2-related protein kinase 7 Short name=CDC2-related protein kinase 7 Cdc2-related kinase, arginine/serine-rich Short name=CrkRS | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1490 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Involved in RNA splicing. Ref.1 |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. |
| Subunit structure | Interacts with CCNL1 and CCNL2 By similarity. |
| Subcellular location | Nucleus. Nucleus speckle. Note: Colocalized with nuclear speckles throughout interphase. Ref.1 |
| Tissue specificity | Ubiquitously expressed. 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 Polymorphism |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Serine/threonine-protein kinase Transferase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | protein amino acid autophosphorylation Ref.1 Inferred from direct assay. Source: HGNC |
| Cellular component | nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II transcription factor activity Ref.1Non-traceable author statement. Source: HGNC 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: Q9NYV4-1) 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: Q9NYV4-2) The sequence of this isoform differs from the canonical sequence as follows: 1254-1262: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1490 | 1490 | Cell division protein kinase 12 | PRO_0000085715 | |||||
Regions | |||||||||
| Domain | 727 – 1020 | 294 | Protein kinase | ||||||
| Nucleotide binding | 733 – 741 | 9 | ATP By similarity | ||||||
| Compositional bias | 407 – 413 | 7 | Poly-Ala | ||||||
| Compositional bias | 535 – 540 | 6 | Poly-Pro | ||||||
| Compositional bias | 1266 – 1280 | 15 | Poly-Pro | ||||||
Sites | |||||||||
| Active site | 859 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 756 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 14 | 1 | Phosphoserine | ||||||
| Modified residue | 24 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 25 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 29 | 1 | Phosphoserine | ||||||
| Modified residue | 32 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 57 | 1 | Phosphothreonine Ref.10 | ||||||
| Modified residue | 62 | 1 | Phosphoserine | ||||||
| Modified residue | 73 | 1 | Phosphotyrosine Ref.10 | ||||||
| Modified residue | 77 | 1 | Phosphoserine Ref.10 Ref.6 | ||||||
| Modified residue | 78 | 1 | Phosphoserine Ref.10 Ref.6 | ||||||
| Modified residue | 80 | 1 | Phosphoserine Ref.10 Ref.6 | ||||||
| Modified residue | 82 | 1 | Phosphothreonine | ||||||
| Modified residue | 84 | 1 | Phosphoserine Ref.10 Ref.6 | ||||||
| Modified residue | 215 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 228 | 1 | Phosphoserine | ||||||
| Modified residue | 236 | 1 | Phosphoserine Ref.10 Ref.15 | ||||||
| Modified residue | 238 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 249 | 1 | Phosphoserine Ref.10 Ref.5 Ref.11 | ||||||
| Modified residue | 265 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 274 | 1 | Phosphoserine Ref.10 Ref.6 Ref.8 | ||||||
| Modified residue | 276 | 1 | Phosphoserine Ref.10 Ref.6 Ref.8 | ||||||
| Modified residue | 279 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 291 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 293 | 1 | Phosphoserine Ref.10 Ref.5 | ||||||
| Modified residue | 301 | 1 | Phosphoserine Ref.10 Ref.11 | ||||||
| Modified residue | 303 | 1 | Phosphoserine Ref.10 Ref.5 Ref.11 | ||||||
| Modified residue | 318 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 319 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 320 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 323 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 325 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 332 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 333 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 334 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 341 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 343 | 1 | Phosphoserine Ref.10 Ref.11 | ||||||
| Modified residue | 345 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 382 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 383 | 1 | Phosphoserine Ref.10 Ref.15 Ref.11 Ref.8 | ||||||
| Modified residue | 385 | 1 | Phosphoserine Ref.10 Ref.15 Ref.11 Ref.8 | ||||||
| Modified residue | 393 | 1 | Phosphoserine | ||||||
| Modified residue | 400 | 1 | Phosphoserine Ref.10 Ref.11 | ||||||
| Modified residue | 420 | 1 | Phosphoserine | ||||||
| Modified residue | 423 | 1 | Phosphoserine Ref.10 Ref.6 Ref.5 Ref.11 Ref.8 Ref.7 | ||||||
| Modified residue | 434 | 1 | Phosphoserine | ||||||
| Modified residue | 504 | 1 | N6-acetyllysine Ref.16 | ||||||
| Modified residue | 514 | 1 | Phosphothreonine Ref.10 | ||||||
| Modified residue | 681 | 1 | Phosphoserine Ref.10 Ref.6 Ref.15 Ref.11 Ref.8 Ref.13 | ||||||
| Modified residue | 685 | 1 | Phosphoserine Ref.10 Ref.6 Ref.15 Ref.11 Ref.8 Ref.13 | ||||||
| Modified residue | 692 | 1 | Phosphothreonine Ref.10 Ref.5 Ref.11 Ref.7 Ref.13 | ||||||
| Modified residue | 892 | 1 | Phosphotyrosine | ||||||
| Modified residue | 893 | 1 | Phosphothreonine Ref.10 Ref.8 | ||||||
| Modified residue | 1053 | 1 | Phosphoserine | ||||||
| Modified residue | 1070 | 1 | Phosphothreonine | ||||||
| Modified residue | 1074 | 1 | Phosphothreonine | ||||||
| Modified residue | 1076 | 1 | Phosphothreonine Ref.13 | ||||||
| Modified residue | 1082 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 1083 | 1 | Phosphoserine Ref.10 Ref.5 Ref.13 Ref.9 | ||||||
| Modified residue | 1244 | 1 | Phosphothreonine Ref.10 Ref.15 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1254 – 1262 | 9 | Missing in isoform 2. | VSP_030284 | |||||
| Natural variant | 530 | 1 | P → A: dbSNP rs56121596. Ref.17 | VAR_041968 | |||||
| Natural variant | 912 | 1 | R → H in a colorectal adenocarcinoma sample; somatic mutation. Ref.17 | VAR_041969 | |||||
| Natural variant | 1189 | 1 | L → Q: dbSNP rs56362165. Ref.17 | VAR_041970 | |||||
| Natural variant | 1275 | 1 | P → L: dbSNP rs34070318. Ref.17 | VAR_041971 | |||||
Experimental info | |||||||||
| Sequence conflict | 639 | 1 | G → D in BAA74927. Ref.2 | ||||||
| Sequence conflict | 639 | 1 | G → D in AAI50266. Ref.4 | ||||||
| Sequence conflict | 745 | 1 | R → K in BAA74927. Ref.2 | ||||||
| Sequence conflict | 745 | 1 | R → K in AAI50266. Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "CrkRS: a novel conserved Cdc2-related protein kinase that colocalises with SC35 speckles." Ko T.K., Kelly E., Pines J. J. Cell Sci. 114:2591-2603(2001) [PubMed: 11683387] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION. |
| [2] | "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:355-364(1998) [PubMed: 10048485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain. |
| [3] | "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed: 12168954] [Abstract] Cited for: SEQUENCE REVISION. |
| [4] | "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). |
| [5] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-249; SER-265; SER-293; SER-303; SER-423; THR-692 AND SER-1083, MASS SPECTROMETRY. Tissue: Epithelium. |
| [6] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-78; SER-80; SER-84; SER-274; SER-276; SER-423; SER-681 AND SER-685, MASS SPECTROMETRY. Tissue: Epithelium. |
| [7] | "A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423 AND THR-692, MASS SPECTROMETRY. Tissue: Epithelium. |
| [8] | "Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-276; SER-383; SER-385; SER-423; SER-681; SER-685 AND THR-893, MASS SPECTROMETRY. |
| [9] | "Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1083, MASS SPECTROMETRY. |
| [10] | "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-25; SER-32; THR-57; TYR-73; SER-77; SER-78; SER-80; SER-84; SER-236; SER-238; SER-249; SER-274; SER-276; SER-291; SER-293; SER-301; SER-303; SER-341; SER-343; SER-383; SER-385; SER-400; SER-423; THR-514; SER-681; SER-685; THR-692; THR-893; SER-1083 AND THR-1244, MASS SPECTROMETRY. |
| [11] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; SER-301; SER-303; SER-318; SER-320; SER-323; SER-325; SER-332; SER-333; SER-334; SER-343; SER-345; SER-382; SER-383; SER-385; SER-400; SER-423; SER-681; SER-685 AND THR-692, MASS SPECTROMETRY. |
| [12] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [13] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-681; SER-685; THR-692; THR-1076; SER-1082 AND SER-1083, MASS SPECTROMETRY. |
| [14] | "Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-24; SER-29; THR-57; SER-62; THR-82; SER-84; SER-228; SER-236; SER-249; SER-274; SER-276; SER-291; SER-293; SER-301; SER-303; SER-323; SER-325; SER-332; SER-333; SER-334; SER-382; SER-383; SER-385; SER-393; SER-420; SER-423; SER-434; THR-514; SER-681; SER-685; THR-692; TYR-892; THR-893; SER-1053; THR-1070; THR-1074; THR-1076; SER-1082; SER-1083 AND THR-1244, MASS SPECTROMETRY. |
| [15] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-383; SER-385; SER-681; SER-685 AND THR-1244, MASS SPECTROMETRY. Tissue: T-cell. |
| [16] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-504, MASS SPECTROMETRY. |
| [17] | "Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. Stratton M.R.Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-530; HIS-912; GLN-1189 AND LEU-1275. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF227198 mRNA. Translation: AAF36401.1. AB020711 mRNA. Translation: BAA74927.2. Different initiation. BC150265 mRNA. Translation: AAI50266.1. |
| IPI | IPI00021175. IPI00868781. |
| RefSeq | NP_055898.1. NP_057591.2. |
| UniGene | Hs.416108 |
3D structure databases | |
| SMR | Q9NYV4. Positions 724-1025. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9NYV4. 6 interactions. |
| STRING | Q9NYV4. |
PTM databases | |
| PhosphoSite | Q9NYV4. |
Proteomic databases | |
| PRIDE | Q9NYV4. |
Genome annotation databases | |
| Ensembl | ENST00000447079; ENSP00000398880; ENSG00000167258; Homo sapiens. [Genome view] |
| GeneID | 51755. |
| KEGG | hsa:51755. |
| UCSC | uc002hrw.2. human. uc010cvv.1. human. |
Organism-specific databases | |
| CTD | 51755. |
| GeneCards | GC17P034872. |
| H-InvDB | HIX0013777. |
| HGNC | HGNC:24224. CDK12. |
| HPA | HPA008038. |
| PharmGKB | PA142672078. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG09762. |
| HOGENOM | HBG282140. |
| HOVERGEN | Q9NYV4. |
| InParanoid | Q9NYV4. |
| PhylomeDB | Q9NYV4. |
Enzyme and pathway databases | |
| BRENDA | 2.7.11.22. 247. |
Gene expression databases | |
| ArrayExpress | Q9NYV4. |
| Bgee | Q9NYV4. |
| CleanEx | HS_CRKRS. |
| Genevestigator | Q9NYV4. |
Family and domain databases | |
| InterPro | IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view] |
| Pfam | PF00069. Pkinase. 1 hit. [Graphical view] |
| 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 | 55858. |
Entry information
| Entry name | CDK12_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9NYV4 Secondary accession number(s): A7E2B2, O94978 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 17 Human chromosome 17: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| Human and mouse protein kinases Human and mouse protein kinases: classification and index |
| SIMILARITY comments Index of protein domains and families |

Clusters with


