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UniProtKB/Swiss-Prot P21127 (CD2L1_HUMAN)
Last modified
June 16, 2009.
Version 110.
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Clusters with 100%,
90%,
50% identity |
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Names and origin
| Protein names | Recommended name: PITSLRE serine/threonine-protein kinase CDC2L1 EC=2.7.11.22 Alternative name(s): Cell division cycle 2-like protein kinase 1 Short name=CLK-1 p58 CLK-1 Galactosyltransferase-associated protein kinase p58/GTA CDK11 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 795 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Appears to play multiple roles in cell cycle progression, cytokinesis and apoptosis. The p110 isoforms have been suggested to be involved in pre-mRNA splicing, potentially by phosphorylating the splicing protein SFRS7. The p58 isoform may act as a negative regulator of normal cell cycle progression. Ref.1 Ref.11 Ref.12 |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. |
| Cofactor | Magnesium. |
| Enzyme regulation | Phosphorylation at Thr-448 or Tyr-449 inactivates the enzyme, while phosphorylation at Thr-595 activates it By similarity. |
| Subunit structure | The cleaved p110 isoform, p110C, binds to the serine/threonine kinase PAK1 and RANBP9. The cleaved p110 isoform interacts with RNPS1. The p58 isoform but not the p110 isoforms or p110C interacts with CCND3. The p110 isoforms are found in large molecular weight complexes containing CCNL1 and SFRS7. Ref.11 Ref.12 Ref.8 Ref.10 |
| Subcellular location | |
| Tissue specificity | Expressed ubiquitously. Some evidence of isoform-specific tissue distribution. Ref.4 Ref.5 |
| Induction | The p58 isoform is specifically induced in G2/M phase of the cell cycle. Ref.9 |
| Post-translational modification | During apoptosis, induced by Fas or tumor necrosis factor, specific PITSLRE p110 isoforms are cleaved by caspases to produce a protein (p110C) that contains the C-terminal kinase domain of the PITSLRE proteins. P110C can be autophosphorylated. Ref.10 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 |
| Miscellaneous | Duplicated gene. CDC2L1 and CDC2L2 encode almost identical protein kinases of 110 kDa that contain at their C termini the open reading frame of a smaller 58 kDa isoform which is expressed following IRES-mediated alternative initiation of translation. |
| Sequence similarities | Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain. |
| Caution | Many references talk about 'p110 isoforms' but it is not yet known if this refers to CDC2L1 and/or CDC2L2 or one/some of the isoforms of each. |
| Sequence caution | The sequence AAC83664.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| PAK1 | Q13153 | 2 | EBI-1298,EBI-1307 | |
| RNPS1 | Q15287 | 1 | EBI-1298,EBI-395959 |
Alternative products
| This entry describes 10 isoforms produced by alternative splicing and alternative initiation. [Align] [Select] | ||||||
| Isoform SV9 (identifier: P21127-1) Also known as: p110; 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 SV1 (identifier: P21127-2) Also known as: Alpha 2-1; The sequence of this isoform differs from the canonical sequence as follows: 252-265: GEARPARAQKPAQL → V | ||||||
| Isoform 2 (identifier: P21127-3) Also known as: Alpha 2-2; The sequence of this isoform differs from the canonical sequence as follows: 110-119: Missing. 165-165: R → RGNDGVCLFR 252-265: GEARPARAQKPAQL → V | ||||||
| Isoform 3 (identifier: P21127-4) Also known as: Alpha 1; The sequence of this isoform differs from the canonical sequence as follows: 2-335: Missing. | ||||||
| Isoform SV4 (identifier: P21127-5) The sequence of this isoform differs from the canonical sequence as follows: 1-269: Missing. | ||||||
| Isoform SV5 (identifier: P21127-6) The sequence of this isoform differs from the canonical sequence as follows: 1-34: Missing. 35-37: LKN → MSQ 110-119: Missing. 252-265: GEARPARAQKPAQL → V | ||||||
| Isoform 8 (identifier: P21127-8) Also known as: Alpha 2-3; The sequence of this isoform differs from the canonical sequence as follows: 110-119: Missing. 252-265: GEARPARAQKPAQL → V | ||||||
| Isoform SV10 (identifier: P21127-9) The sequence of this isoform differs from the canonical sequence as follows: 1-34: Missing. 35-37: LKN → MSQ 252-265: GEARPARAQKPAQL → V | ||||||
| Isoform SV11 (identifier: P21127-10) Also known as: Alpha 2-4; The sequence of this isoform differs from the canonical sequence as follows: 1-217: Missing. 252-265: GEARPARAQKPAQL → V | ||||||
| Isoform 7 (identifier: P21127-12) Also known as: p58; The sequence of this isoform differs from the canonical sequence as follows: 1-356: Missing. | ||||||
| Note: Produced by alternative initiation at Met-357 of isoform SV9. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 795 | 795 | PITSLRE serine/threonine-protein kinase CDC2L1 | PRO_0000024311 | |||||
Regions | |||||||||
| Domain | 438 – 723 | 286 | Protein kinase | ||||||
| Nucleotide binding | 444 – 452 | 9 | ATP By similarity | ||||||
| Compositional bias | 126 – 393 | 268 | Glu-rich | ||||||
Sites | |||||||||
| Active site | 562 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 467 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 65 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 283 | 1 | Phosphoserine Ref.13 Ref.15 | ||||||
| Modified residue | 381 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 384 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 395 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 410 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 414 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 448 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 449 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 589 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 594 | 1 | Phosphotyrosine Ref.17 | ||||||
| Modified residue | 595 | 1 | Phosphothreonine Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 | ||||||
| Modified residue | 751 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 752 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 356 | 356 | Missing in isoform 7. | VSP_018834 | |||||
| Alternative sequence | 1 – 269 | 269 | Missing in isoform SV4. | VSP_008275 | |||||
| Alternative sequence | 1 – 217 | 217 | Missing in isoform SV11. | VSP_008274 | |||||
| Alternative sequence | 1 – 34 | 34 | Missing in isoform SV5 and isoform SV10. | VSP_008273 | |||||
| Alternative sequence | 2 – 335 | 334 | Missing in isoform 3. | VSP_008276 | |||||
| Alternative sequence | 35 – 37 | 3 | LKN → MSQ in isoform SV5 and isoform SV10. | VSP_008277 | |||||
| Alternative sequence | 110 – 119 | 10 | Missing in isoform 2, isoform SV5 and isoform 8. | VSP_008278 | |||||
| Alternative sequence | 165 | 1 | R → RGNDGVCLFR in isoform 2. | VSP_008279 | |||||
| Alternative sequence | 252 – 265 | 14 | GEARP…KPAQL → V in isoform SV1, isoform 2, isoform SV5, isoform 8, isoform SV10 and isoform SV11. | VSP_008280 | |||||
| Natural variant | 57 | 1 | R → C Ref.4 Ref.18 | VAR_041958 | |||||
| Natural variant | 93 | 1 | R → W: dbSNP rs1059831. | VAR_057775 | |||||
| Natural variant | 201 | 1 | R → W Ref.18 | VAR_041959 | |||||
| Natural variant | 414 | 1 | S → L Ref.18 | VAR_041960 | |||||
| Natural variant | 452 | 1 | V → A Ref.18 | VAR_045577 | |||||
| Natural variant | 463 | 1 | I → V Ref.18 | VAR_041961 | |||||
| Natural variant | 506 | 1 | G → S Ref.18 | VAR_045578 | |||||
| Natural variant | 601 | 1 | L → Q Ref.18 Ref.3 | VAR_041962 | |||||
| Natural variant | 641 | 1 | K → N Ref.18 | VAR_041963 | |||||
| Natural variant | 670 | 1 | A → V Ref.18 | VAR_041964 | |||||
Experimental info | |||||||||
| Sequence conflict | 109 | 1 | Missing in AAA19582. Ref.4 | ||||||
| Sequence conflict | 109 | 1 | Missing in AAA19583. Ref.4 | ||||||
| Sequence conflict | 109 | 1 | Missing in AAC72079. Ref.5 | ||||||
| Sequence conflict | 126 | 1 | E → K in AAA19582. Ref.4 | ||||||
| Sequence conflict | 126 | 1 | E → K in AAA19583. Ref.4 | ||||||
| Sequence conflict | 126 | 1 | E → K in AAA19586. Ref.4 | ||||||
| Sequence conflict | 320 | 1 | S → T Ref.6 | ||||||
| Sequence conflict | 324 – 326 | 3 | Missing in AAA19582. Ref.4 | ||||||
| Sequence conflict | 324 – 326 | 3 | Missing in AAA19583. Ref.4 | ||||||
| Sequence conflict | 324 – 326 | 3 | Missing in AAA19584. Ref.4 | ||||||
| Sequence conflict | 324 – 326 | 3 | Missing in AAA19586. Ref.4 | ||||||
| Sequence conflict | 436 | 1 | E → D Ref.3 | ||||||
| Sequence conflict | 560 | 1 | H → Q Ref.6 | ||||||
| Sequence conflict | 567 | 1 | N → T Ref.6 | ||||||
| Sequence conflict | 678 | 1 | E → R Ref.4 | ||||||
| Sequence conflict | 678 | 1 | E → R Ref.6 | ||||||
| Sequence conflict | 694 | 1 | D → E Ref.3 | ||||||
| Sequence conflict | 697 | 1 | F → C Ref.6 | ||||||
| Sequence conflict | 712 | 1 | I → L Ref.3 | ||||||
| Sequence conflict | 715 | 1 | E → Q Ref.3 | ||||||
| Sequence conflict | 792 | 1 | S → R Ref.6 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Increased expression of a 58-kDa protein kinase leads to changes in the CHO cell cycle." Bunnell B.A., Heath L.S., Adams D.E., Lahti J.M., Kidd V.J. Proc. Natl. Acad. Sci. U.S.A. 87:7467-7471(1990) [PubMed: 2217177] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), FUNCTION. Tissue: Liver. |
| [2] | Erratum Bunnell B.A., Heath L.S., Adams D.E., Lahti J.M., Kidd V.J. Proc. Natl. Acad. Sci. U.S.A. 88:2612-2612(1991) [PubMed: 2006197] [Abstract] Cited for: SEQUENCE REVISION. |
| [3] | "Structure and expression of the human p58clk-1 protein kinase chromosomal gene." Eipers P.G., Lahti J.M., Kidd V.J. Genomics 13:613-621(1992) [PubMed: 1639388] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 7), VARIANT GLN-601. Tissue: Hematopoietic. |
| [4] | "Molecular cloning and expression of alternatively spliced PITSLRE protein kinase isoforms." Xiang J., Lahti J.M., Grenet J.A., Easton J.B., Kidd V.J. J. Biol. Chem. 269:15786-15794(1994) [PubMed: 8195233] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SV1; 2; 3; 8 AND SV11), VARIANT CYS-57, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Tissue: Cervix carcinoma. |
| [5] | "Duplication of a genomic region containing the Cdc2L1-2 and MMP21-22 genes on human chromosome 1p36.3 and their linkage to D1Z2." Gururajan R., Lahti J.M., Grenet J.A., Easton J., Gruber I., Ambros P.F., Kidd V.J. Genome Res. 8:929-939(1998) [PubMed: 9750192] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS SV1; SV4; SV5; SV9; SV10 AND SV11), TISSUE SPECIFICITY. Tissue: Cervix carcinoma. |
| [6] | Govindan M.V., Warriar N. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SV11). Tissue: Placenta. |
| [7] | "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] OF 288-795. Tissue: Uterus. |
| [8] | "The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinases in vivo." Loyer P., Trembley J.H., Lahti J.M., Kidd V.J. J. Cell Sci. 111:1495-1506(1998) [PubMed: 9580558] [Abstract] Cited for: INTERACTION WITH RNPS1. |
| [9] | "Identification and characterization of a novel cell cycle-regulated internal ribosome entry site." Cornelis S., Bruynooghe Y., Denecker G., Van Huffel S., Tinton S., Beyaert R. Mol. Cell 5:597-605(2000) [PubMed: 10882096] [Abstract] Cited for: ALTERNATIVE INITIATION (ISOFORM 7), INDUCTION. |
| [10] | "The cyclin-dependent kinase 11(p46) isoform interacts with RanBPM." Mikolajczyk M., Shi J., Vaillancourt R.R., Sachs N.A., Nelson M. Biochem. Biophys. Res. Commun. 310:14-18(2003) [PubMed: 14511641] [Abstract] Cited for: INTERACTION WITH RANBP9, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION. |
| [11] | "CDK11 complexes promote pre-mRNA splicing." Hu D., Mayeda A., Trembley J.H., Lahti J.M., Kidd V.J. J. Biol. Chem. 278:8623-8629(2003) [PubMed: 12501247] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CCNL1 AND SFRS7. |
| [12] | "The C-terminal kinase domain of the p34cdc2-related PITSLRE protein kinase (p110C) associates with p21-activated kinase 1 and inhibits its activity during anoikis." Chen S., Yin X., Zhu X., Yan J., Ji S., Chen C., Cai M., Zhang S., Zong H., Hu Y., Yuan Z., Shen Z., Gu J. J. Biol. Chem. 278:20029-20036(2003) [PubMed: 12624090] [Abstract] Cited for: FUNCTION, INTERACTION WITH PAK1. |
| [13] | "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-283; SER-589 AND THR-595, MASS SPECTROMETRY. Tissue: Epithelium. |
| [14] | "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 THR-595, MASS SPECTROMETRY. Tissue: Epithelium. |
| [15] | "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-283 AND THR-595, MASS SPECTROMETRY. Tissue: Epithelium. |
| [16] | "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-595, MASS SPECTROMETRY. |
| [17] | "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-65; SER-381; SER-384; THR-395; SER-410; SER-414; TYR-594 AND THR-595, MASS SPECTROMETRY. |
| [18] | "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] CYS-57; TRP-201; LEU-414; ALA-452; VAL-463; SER-506; GLN-601; ASN-641 AND VAL-670. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| M37712 mRNA. Translation: AAA36406.1. Sequence problems. M88563 M88562 Genomic DNA. Translation: AAB59449.1. Sequence problems.U04815 mRNA. Translation: AAA19581.1. U04816 mRNA. Translation: AAA19582.1. U04817 mRNA. Translation: AAA19583.1. U04818 mRNA. Translation: AAA19584.1. U04824 mRNA. Translation: AAA19586.1. AF067512 mRNA. Translation: AAC72077.1. AF067513 mRNA. Translation: AAC72078.1. AF067514 mRNA. Translation: AAC72079.1. AF067515 mRNA. Translation: AAC72080.1. AF067516 mRNA. Translation: AAC72081.1. AF067517 mRNA. Translation: AAC72082.1. AF080683 AF080682 Genomic DNA. Translation: AAC83662.1. AF080683 AF080682 Genomic DNA. Translation: AAC83663.1. AF080683 AF080682 Genomic DNA. Translation: AAC83664.1. Sequence problems.AF080683 AF080682 Genomic DNA. Translation: AAC83665.1. AF080683 AF080682 Genomic DNA. Translation: AAC83666.1. AF174497 mRNA. Translation: AAF36538.1. Different initiation. BC033069 mRNA. Translation: AAH33069.1. Different initiation. | |
| IPI | IPI00071185. IPI00071188. IPI00215999. IPI00337617. IPI00376979. IPI00376980. IPI00376983. IPI00395687. IPI00736011. IPI00759690. |
| PIR | A38282. B54024. E54024. F54024. H54024. T09568. |
| RefSeq | NP_277021.1. NP_277022.1. NP_277023.1. NP_277024.1. NP_277027.1. NP_277028.1. |
| UniGene | Hs.651228 Hs.709182 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1H00 based on UniProtKB P24941. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:29015N. |
| IntAct | P21127. 4 interactions. |
PTM databases | |
| PhosphoSite | P21127. |
Proteomic databases | |
| PRIDE | P21127. |
Genome annotation databases | |
| Ensembl | ENSG00000008128. Homo sapiens. [Contig view] |
| GeneID | 984. |
| KEGG | hsa:984. |
Organism-specific databases | |
| GeneCards | GC01M001626. GC01M001627. |
| H-InvDB | HIX0000039. |
| HGNC | HGNC:1729. CDC2L1. |
| HPA | CAB010467. |
| MIM | 176873. gene. |
| PharmGKB | PA26262. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | P21127. |
Enzyme and pathway databases | |
| BRENDA | 2.7.11.22. 247. |
| Pathway_Interaction_DB | ar_pathway. Coregulation of Androgen receptor activity. |
Gene expression databases | |
| Bgee | P21127. |
| GermOnline | ENSG00000008128. Homo sapiens. |
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. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 4128. |
| PMAP-CutDB | P21127. |
| SOURCE | Search... |
Entry information
| Entry name | CD2L1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P21127 Secondary accession number(s): O95265 Q9UP59 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 1 Human chromosome 1: 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 |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) 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 |

Clusters with


