Protein kinase domain

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Protein kinase domain
Identifiers
Symbol Pkinase
Pfam PF00069
InterPro IPR000719
SMART TyrKc
PROSITE PDOC00629
SCOP 1apm
OPM protein 2bcj
Available PDB structures:

1ctpE:44-298 2erzE:44-298 1fotA:87-341 1xjdA:380-634 1zrzA:245-513 1vzoA:49-318 1o6kA:152-409 1o6lA:152-409 1gznA:152-409 1gzkA:152-409 2etkB:76-338 2etrB:76-338 2esmB:76-338 2etoB:76-338 1ym7D:191-453 1omwA:191-453 1okyA:82-342 1uu3A:82-342 2bdwB:12-269 1a06 :20-276 2phkA:20-288 1phk :20-288 1ql6A:20-288 2ac3A:83-338 2ac5A:83-338 1nxkA:64-325 1kwpA:64-325 1ny3A:64-325 1mq4A:133-383 2c6dA:133-383 2bmcB:133-383 1ol6A:133-383 1muoA:133-383 2bfxA:103-353 2bfyB:103-353 1kobB:47-302 1koa :6261-6516 1wmkF:23-285 1ig1A:13-275 1jktB:13-275 1p4fA:13-275 1jklA:13-275 1jkkA:13-275 1jksA:13-275 2brbA:9-265 2c3lA:9-265 1nvrA:9-265 2br1A:9-265 1nvqA:9-265 1yhvA:270-521 1yhwA:270-521 1f3mD:270-521 2f57B:449-700 1u5rB:28-281 1u5qB:28-281 1s9jA:68-361 1s9iB:72-369 1t4hB:221-479 1z57A:161-477 2eu9A:156-472 2exeA:156-472 1wbpA:251-609 1q8zB:370-706 1q8yA:370-706 1howA:376-706 1q99A:370-706 1q97B:370-706 1zzlA:24-308 1oz1A:24-308 1w7hA:24-308 1ywrA:24-308 1cm8B:27-311 2b9hA:13-309 2b9fA:13-309 2b9jA:13-309 2b9iA:13-309 1gol :23-311 3erk :23-311 2erk :23-311 4erk :23-311 1erk :23-311 1pme :25-313 1wzyA:25-313 1tvoA:25-313 1pmqA:64-359 1jnk :64-359 1pmuA:64-359 1pmnA:64-359 1pmvA:64-359 1ukhA:26-321 1ukiA:26-321 1ungA:4-286 1h4lA:4-286 1unlB:4-286 1lfrA:4-286 1unhB:4-286 1h28C:4-286 1v0oA:4-284 1v0pA:4-284 1v0bA:4-284 1lchA:4-284 1ld2A:6-295 1blxA:13-300 1g3nE:13-300 1bi8C:13-300 1jowB:13-300 1xo2B:13-300 1bi7A:13-300 1ua2B:12-295 1pa8A:181-295 1lg3A:12-295 1pf6A:19-315 1i09A:56-340 1q3wB:56-340 1q4lB:56-340 1q3dA:56-340 1h8fA:56-340 1pjkA:39-324 1jwhB:39-324 1na7A:39-324 1ymiA:39-324 1m2pA:34-319 1ds5D:34-319 1zogA:34-319 1f0qA:34-319 1lr4A:34-319 1mruB:11-273 1o6yA:11-273 1iasE:205-492 1vjyA:205-492 1uwhA:457-714 1uwjB:457-714 1yxxA:129-381 2bzkB:129-381 1yxvA:129-381 1yxuC:129-381 2a19B:267-536 2a1aB:267-536 1x8bA:299-569 1zxeD:646-928 1zydB:646-928 1zy5B:646-928 1zycD:646-928 1zy4A:646-928 2bujA:20-290 1t53A:557-797 2c47B:46-271 1eh4A:12-237 2csn :12-237 1csn :12-237 1ckiB:9-247 1ckjB:9-247 1lhxA:9-276

Protein kinases are a group of enzymes that possess a catalytic subunit which transfers the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. The enzymes fall into two broad classes, characterised with respect to substrate specificity: serine/threonine specific and tyrosine specific[1].

Protein kinase function has been evolutionarily conserved from Escherichia coli to Homo sapiens. Protein kinases play a role in a mulititude of cellular processes, including division, proliferation, apoptosis, and differentiation[2]. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins.

The catalytic subunits of protein kinases are highly conserved, and several structures have been solved[3], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases[4]. Eukaryotic protein kinases[5][6][7][8][1] are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is a glycine-rich stretch of residues in the vicinity of a lysine residue, which has been shown to be involved in ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residue which is important for the catalytic activity of the enzyme[9].

[edit] Human proteins containing this domain

AAK1; ACVR1; ACVR1B; ACVR1C; ACVR2A; ACVR2B; ACVRL1; ADRBK1; ADRBK2; AKT1; AKT2; AKT3; ALS2CR2; ALS2CR7; AMHR2; ANKK1; ARAF; AURKA; AURKB; AURKC; BMP2K; BMPR1A; BMPR1B; BMPR2; BRAF; BRSK1; BRSK2; BUB1; C14orf20; CAMK1; CAMK1D; CAMK1G; CAMK2A; CAMK2B; CAMK2D; CAMK2G; CAMK4; CAMKK1; CAMKK2; CAMKV; CASK; CCRK; CDC2; CDC2L1; CDC2L2; CDC2L5; CDC2L6; CDC42BPA; CDC42BPB; CDC42BPG; CDC7; CDK10; CDK2; CDK3; CDK4; CDK5; CDK6; CDK7; CDK8; CDK9; CDKL1; CDKL2; CDKL3; CDKL4; CDKL5; CHEK1; CHEK2; CHUK; CIT; CLK1; CLK2; CLK3; CLK4; CRKRS; CSNK1A1; CSNK1A1L; CSNK1D; CSNK1E; CSNK1G1; CSNK1G2; CSNK1G3; CSNK2A1; CSNK2A2; DAPK1; DAPK2; DAPK3; DCAMKL1; DCLK1; DCLK2; DCLK3; DMPK; DYRK1A; DYRK1B; DYRK2; DYRK3; DYRK4; EIF2AK1; EIF2AK3; EIF2AK4; ERN1; ERN2; GAK; GRK1; GRK4; GRK5; GRK6; GRK7; GSK3A; GSK3B; GUCY2C; GUCY2D; GUCY2F; HIPK1; HIPK2; HIPK3; HIPK4; HUNK; ICK; IKBKB; IKBKE; IRAK1; IRAK2; IRAK3; IRAK4; KALRN; KIAA0999; KSR2; LATS1; LATS2; LIMK1; LIMK2; LOC402468; LOC407835; LRRK1; LRRK2; MAK; MAP2K1; MAP2K2; MAP2K3; MAP2K4; MAP2K5; MAP2K6; MAP2K7; MAP3K1; MAP3K10; MAP3K11; MAP3K12; MAP3K13; MAP3K14; MAP3K15; MAP3K2; MAP3K3; MAP3K4; MAP3K5; MAP3K6; MAP3K7; MAP3K8; MAP3K9; MAP4K1; MAP4K2; MAP4K3; MAP4K4; MAP4K5; MAPK1; MAPK10; MAPK12; MAPK13; MAPK14; MAPK15; MAPK3; MAPK4; MAPK6; MAPK7; MAPK8; MAPK9; MAPKAPK2; MAPKAPK3; MAPKAPK5; MARK1; MARK2; MARK3; MARK4; MAST1; MAST2; MAST3; MAST4; MASTL; MELK; MELKv2; MELKv3; MINK; MINK1; MKNK1; MKNK2; MLK4; MLKL; MOS; MST094; MST4; MYLK; MYLK2; MYLK3; MYO3A; MYO3B; NEK1; NEK10; NEK11; NEK2; NEK3; NEK4; NEK5; NEK6; NEK7; NEK8; NEK9; NIM1; NLK; NPR2; NRBP1; NRK; NUAK1; NUAK2; OBSCN; OXSR1; PAK1; PAK2; PAK3; PAK4; PAK6; PAK7; PASK; PBK; PCTK1; PCTK2; PCTK3; PDIK1L; PDPK1; PDPK2; PFTK1; PHKG1; PHKG2; PIK3R4; PIM1; PIM2; PIM3; PINK1; PKMYT1; PKN1; PKN2; PKN3; PLK1; PLK2; PLK3; PLK5; PNCK; PRKAA1; PRKAA2; PRKACA; PRKACB; PRKACG; PRKCA; PRKCB1; PRKCD; PRKCE; PRKCG; PRKCH; PRKCI; PRKCN; PRKCQ; PRKCZ; PRKD1; PRKD2; PRKD3; PRKG1; PRKG2; PRKX; PRKY; PRPF4B; PSKH1; PSKH2; QSK; RAF1; RAGE; RIP3; RIPK1; RIPK2; RIPK3; RIPK4; RIPK5; RK; RNASEL; ROCK1; ROCK2; RPS6KA1; RPS6KA2; RPS6KA3; RPS6KA4; RPS6KA5; RPS6KA6; RPS6KB1; RPS6KB2; RPS6KC1; RPS6KL1; SBK1; SCYL2; SCYL3; SGK; SGK069; SGK071; SGK085; SGK110; SGK196; SGK2; SGK269; SGK3; SGK494; SGKL; SLK; SNF1LK; SNF1LK2; SNRK; SPEG; SRPK1; SRPK2; SRPK3; STK10; STK11; STK16; STK17A; STK17B; STK24; STK25; STK3; STK31; STK32A; STK32B; STK32C; STK33; STK35; STK36; STK38; STK38L; STK39; STK4; STK40; STRAD; TAK1; TAOK1; TAOK2; TAOK3; TBCK; TBK1; TESK1; TESK2; TGFBR1; TGFBR2; TLK1; TLK2; TNIK; TRIB1; TRIB2; TRIB3; TRIO; TSSK1; TSSK1B; TSSK2; TSSK3; TSSK4; TSSK6; TTBK1; TTBK2; TTK; TTN; UHMK1; ULK1; ULK2; ULK3; ULK4; VRK1; VRK2; WEE1; WEE1B; WNK1; WNK2; WNK3; WNK4; YSK4; dik;

[edit] References

  1. ^ a b Hunter T, Hanks SK, Quinn AM (1988). "The protein kinase family: conserved features and deduced phylogeny of the catalytic domains". Science 241 (4861): 42–51. doi:10.1126/science.3291115. PMID 3291115. 
  2. ^ Hunter T, Plowman GD, Manning G, Sudarsanam S (2002). "Evolution of protein kinase signaling from yeast to man". Trends Biochem. Sci. 27 (10): 514–520. doi:10.1016/S0968-0004(02)02179-5. PMID 12368087. 
  3. ^ Foster PG, Stout TJ, Matthews DJ (2004). "High-throughput structural biology in drug discovery: protein kinases". Curr Pharm Des 10 (10): -. PMID 15078142. 
  4. ^ Liu Y, Li B, Uno T, Gray N (2004). "Creating chemical diversity to target protein kinases". Comb. Chem. High Throughput Screen. 7 (5): -. PMID 15320712. 
  5. ^ Hanks SK (2003). "Genomic analysis of the eukaryotic protein kinase superfamily: a perspective". Genome Biol. 4 (5): 111-. doi:10.1186/gb-2003-4-5-111. PMID 12734000. 
  6. ^ Hunter T, Hanks SK (1995). "Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification". FASEB J. 9 (8): 576–596. PMID 7768349. 
  7. ^ Hunter T (1991). "Protein kinase classification". Meth. Enzymol. 200: 3–37. PMID 1835513. 
  8. ^ Hanks SK, Quinn AM (1991). "Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members". Meth. Enzymol. 200: 38–62. PMID 1956325. 
  9. ^ Taylor SS, Xuong NH, Knighton DR, Ten Eyck LF, Ashford VA, Sowadski JM, Zheng JH (1991). "Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase". Science 253 (5018): 407–414. doi:10.1126/science.1862342. PMID 1862342. 
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