Protein kinase domain

Protein kinase domain

Pfam_box
Symbol = Pkinase
Name = Protein kinase domain


width =
caption =
Pfam= PF00069
InterPro= IPR000719
SMART= TyrKc
PROSITE = PDOC00629
SCOP = 1apm
TCDB =
OPM family=
OPM protein= 2bcj
PDB=PDB3|1ctpE:44-298 PDB3|2erzE:44-298 PDB3|1fotA:87-341 PDB3|1xjdA:380-634PDB3|1zrzA:245-513 PDB3|1vzoA:49-318 PDB3|1o6kA:152-409PDB3|1o6lA:152-409 PDB3|1gznA:152-409 PDB3|1gzkA:152-409PDB3|2etkB:76-338 PDB3|2etrB:76-338 PDB3|2esmB:76-338PDB3|2etoB:76-338 PDB3|1ym7D:191-453 PDB3|1omwA:191-453PDB3|1okyA:82-342 PDB3|1uu3A:82-342 PDB3|2bdwB:12-269PDB3|1a06 :20-276 PDB3|2phkA:20-288 PDB3|1phk :20-288PDB3|1ql6A:20-288 PDB3|2ac3A:83-338 PDB3|2ac5A:83-338PDB3|1nxkA:64-325 PDB3|1kwpA:64-325 PDB3|1ny3A:64-325PDB3|1mq4A:133-383 PDB3|2c6dA:133-383 PDB3|2bmcB:133-383PDB3|1ol6A:133-383 PDB3|1muoA:133-383 PDB3|2bfxA:103-353PDB3|2bfyB:103-353 PDB3|1kobB:47-302 PDB3|1koa :6261-6516PDB3|1wmkF:23-285 PDB3|1ig1A:13-275 PDB3|1jktB:13-275PDB3|1p4fA:13-275 PDB3|1jklA:13-275 PDB3|1jkkA:13-275PDB3|1jksA:13-275 PDB3|2brbA:9-265 PDB3|2c3lA:9-265PDB3|1nvrA:9-265 PDB3|2br1A:9-265 PDB3|1nvqA:9-265PDB3|1yhvA:270-521 PDB3|1yhwA:270-521 PDB3|1f3mD:270-521PDB3|2f57B:449-700 PDB3|1u5rB:28-281 PDB3|1u5qB:28-281PDB3|1s9jA:68-361 PDB3|1s9iB:72-369 PDB3|1t4hB:221-479PDB3|1z57A:161-477 PDB3|2eu9A:156-472 PDB3|2exeA:156-472PDB3|1wbpA:251-609 PDB3|1q8zB:370-706 PDB3|1q8yA:370-706PDB3|1howA:376-706 PDB3|1q99A:370-706 PDB3|1q97B:370-706PDB3|1zzlA:24-308 PDB3|1oz1A:24-308 PDB3|1w7hA:24-308PDB3|1ywrA:24-308 PDB3|1cm8B:27-311 PDB3|2b9hA:13-309PDB3|2b9fA:13-309 PDB3|2b9jA:13-309 PDB3|2b9iA:13-309PDB3|1gol :23-311 PDB3|3erk :23-311 PDB3|2erk :23-311PDB3|4erk :23-311 PDB3|1erk :23-311 PDB3|1pme :25-313PDB3|1wzyA:25-313 PDB3|1tvoA:25-313 PDB3|1pmqA:64-359PDB3|1jnk :64-359 PDB3|1pmuA:64-359 PDB3|1pmnA:64-359PDB3|1pmvA:64-359 PDB3|1ukhA:26-321 PDB3|1ukiA:26-321PDB3|1ungA:4-286 PDB3|1h4lA:4-286 PDB3|1unlB:4-286PDB3|1lfrA:4-286 PDB3|1unhB:4-286 PDB3|1h28C:4-286PDB3|1v0oA:4-284 PDB3|1v0pA:4-284 PDB3|1v0bA:4-284PDB3|1lchA:4-284 PDB3|1ld2A:6-295 PDB3|1blxA:13-300PDB3|1g3nE:13-300 PDB3|1bi8C:13-300 PDB3|1jowB:13-300PDB3|1xo2B:13-300 PDB3|1bi7A:13-300 PDB3|1ua2B:12-295PDB3|1pa8A:181-295 PDB3|1lg3A:12-295 PDB3|1pf6A:19-315PDB3|1i09A:56-340 PDB3|1q3wB:56-340 PDB3|1q4lB:56-340PDB3|1q3dA:56-340 PDB3|1h8fA:56-340 PDB3|1pjkA:39-324PDB3|1jwhB:39-324 PDB3|1na7A:39-324 PDB3|1ymiA:39-324PDB3|1m2pA:34-319 PDB3|1ds5D:34-319 PDB3|1zogA:34-319PDB3|1f0qA:34-319 PDB3|1lr4A:34-319 PDB3|1mruB:11-273PDB3|1o6yA:11-273 PDB3|1iasE:205-492 PDB3|1vjyA:205-492PDB3|1uwhA:457-714 PDB3|1uwjB:457-714 PDB3|1yxxA:129-381PDB3|2bzkB:129-381 PDB3|1yxvA:129-381 PDB3|1yxuC:129-381PDB3|2a19B:267-536 PDB3|2a1aB:267-536 PDB3|1x8bA:299-569PDB3|1zxeD:646-928 PDB3|1zydB:646-928 PDB3|1zy5B:646-928PDB3|1zycD:646-928 PDB3|1zy4A:646-928 PDB3|2bujA:20-290PDB3|1t53A:557-797 PDB3|2c47B:46-271 PDB3|1eh4A:12-237PDB3|2csn :12-237 PDB3|1csn :12-237 PDB3|1ckiB:9-247PDB3|1ckjB:9-247 PDB3|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 specificcite journal |author=Hunter T, Hanks SK, Quinn AM |title=The protein kinase family: conserved features and deduced phylogeny of the catalytic domains |journal=Science |volume=241 |issue=4861 |pages=42–51 |year=1988 |pmid=3291115 |doi=10.1126/science.3291115] .

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 differentiationcite journal |author=Hunter T, Plowman GD, Manning G, Sudarsanam S |title=Evolution of protein kinase signaling from yeast to man |journal=Trends Biochem. Sci. |volume=27 |issue=10 |pages=514–520 |year=2002 |pmid=12368087 |doi=10.1016/S0968-0004(02)02179-5] . 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 solvedcite journal |author=Foster PG, Stout TJ, Matthews DJ |title=High-throughput structural biology in drug discovery: protein kinases |journal=Curr Pharm Des |volume=10 |issue=10 |pages=- |year=2004 |pmid=15078142] , leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseasescite journal |author=Liu Y, Li B, Uno T, Gray N |title=Creating chemical diversity to target protein kinases |journal=Comb. Chem. High Throughput Screen. |volume=7 |issue=5 |pages=- |year=2004 |pmid=15320712] .Eukaryotic protein kinasescite journal |author=Hanks SK |title=Genomic analysis of the eukaryotic protein kinase superfamily: a perspective |journal=Genome Biol. |volume=4 |issue=5 |pages=111- |year=2003 |pmid=12734000 |doi=10.1186/gb-2003-4-5-111] cite journal |author=Hunter T, Hanks SK |title=Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification |journal=FASEB J. |volume=9 |issue=8 |pages=576–596 |year=1995 |pmid=7768349] cite journal |author=Hunter T |title=Protein kinase classification |journal=Meth. Enzymol. |volume=200 |issue= |pages=3–37 |year=1991 |pmid=1835513] cite journal |author=Hanks SK, Quinn AM |title=Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members |journal=Meth. Enzymol. |volume=200 |issue= |pages=38–62 |year=1991 |pmid=1956325] 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 isimportant for the catalytic activity of the enzymecite journal |author=Taylor SS, Xuong NH, Knighton DR, Ten Eyck LF, Ashford VA, Sowadski JM, Zheng JH |title=Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase |journal=Science |volume=253 |issue=5018 |pages=407–414 |year=1991 |pmid=1862342 |doi=10.1126/science.1862342] .

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;

References


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