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InterPro: IPR002290 Serine/threonine-protein kinase domain

Protein matchesHelp
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UniProtKB
Matches:
17941 proteins
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IPR002290 Ser/Thr_prot_kinase_dom
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Domain
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InterPro RelationshipsHelp
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Parent IPR017442 Serine/threonine-protein kinase-like domain
Children IPR008349 ERK1/2 MAP kinase
IPR008350 ERK3/4 MAP kinase
IPR008351 JNK MAP kinase
IPR008352 MAP kinase, p38
IPR015746 Serine/threonine-protein kinase-1, 3-phosphoinositide dependent
IPR015747 Mitogen activated protein kinase kinase kinase 4
IPR015748 Mitogen activated protein kinase kinase kinase 3
IPR015749 Mitogen activated protein kinase kinase kinase-1
IPR015750 Serine/threonine-protein kinase, Pak-related
Found in IPR000239 GPCR kinase
IPR002291 Phosphorylase kinase, gamma catalytic subunit
IPR012233 Protein kinase C, zeta/iota
IPR013334 Hormonally upregulated Neu-associated kinase
IPR013336 Serine/threonine-protein kinase, Unc-51/Ulk
IPR014375 Protein kinase C, alpha/beta/gamma types
IPR014376 Protein kinase C, delta/epsilon/eta/theta types
IPR015725 Myosin light chain kinase
IPR015726 Serine/threonine protein kinase, striated muscle-specific
IPR015727 Protein kinase C mu-related
IPR015728 Serine/threonine-protein kinase, Polo-like
IPR015729 Serine/threonine-protein kinase, Checkpoint 1/Hal4
IPR015730 Myosin light chain kinase 2
IPR015731 MAP Kinase Interacting Kinase
IPR015732 Serine/threonine-protein kinase PSKH
IPR015733 Calcium/calmodulin-dependent protein kinase IV
IPR015734 Calcium/calmodulin-dependent protein kinase 1
IPR015735 Serine/threonine-protein kinase STK
IPR015737 Serine/threonine-protein kinase, testis-specific
IPR015738 Protein kinase, Snf1-like
IPR015739 Maternal embryonic leucine zipper kinase
IPR015740 Serine/threonine-protein kinase-like, plant
IPR015741 Protein kinase, Snf1-like AMPK
IPR015742 Calcium/calmodulin-dependent protein kinase II isoform
IPR015743 Beta-adrenergic receptor kinase
IPR015744 Rac serine/threonine kinase
IPR015745 Protein kinase C
IPR015751 Rho-associated coiled-coil containing protein kinase
IPR016232 cGMP-dependent protein kinase
IPR016237 Serine/threonine-protein kinase, Ulk1/Ulk2
IPR016238 Ribosomal protein S6 kinase
IPR016239 Ribosomal protein S6 kinase II
IPR016242 Serine/threonine-protein kinase MPS1
IPR016256 Serine/threonine-protein kinase RAD53
IPR017090 Serine/threonine-protein kinase, SNF1-like
IPR017184 Serine/threonine-protein kinase Unc-51
IPR017239 MAP kinase kinase kinase STE11
IPR017240 MAP kinase kinase kinase, SSK22
IPR017348 Proto-oncogene serine/threonine-protein kinase Pim-1
IPR017405 Citron Rho-interacting kinase
IPR020636 Calcium/calmodulin-dependent protein kinase-like
IPR020640 Serine/threonine-protein kinase, SIK1
IPR020641 Protein kinase, predicted
IPR020642 Calcium-dependent protein kinase
IPR020643 Serine/threonine-protein kinase 2, predicted
IPR020644 Serine/threonine-protein kinase 17
IPR020645 Serine/threonine-protein kinase 33
IPR020646 MAP kinase-activated protein kinase (MAPKAPK)
IPR020647 Meiosis-specific serine/threonine-protein kinase Mek1
IPR020648 Serine/threonine-protein kinase Chk2
IPR020649 Serine/threonine-protein kinase DCLK
IPR020650 Calcium/calmodulin-dependent protein kinase type II
IPR020651 Calcium/calmodulin-dependent protein kinase CMK
IPR020654 CaM kinase-like vesicle-associated protein
IPR020655 Serine/threonine-protein kinase, putative
IPR020656 Serine/threonine-protein kinase ATG1
IPR020657 Calcium/calmodulin-dependent protein kinase kinase
IPR020658 Serine/threonine-protein kinase, AMPK-related
IPR020660 CBL-interacting protein kinase
IPR020661 SNF-related serine/threonine-protein kinase, SNRK
IPR020662 Serine/threonine-protein kinase ipl1
IPR020663 Spindle assembly checkpoint kinase
IPR020664 Serine/threonine-protein kinase PLK4
IPR020665 SNF1-like kinase, NUAK-type
IPR020668 Serine/threonine-protein kinase NIM1
IPR020669 MAP/microtubule affinity-regulating kinase 3
IPR020670 MAP/microtubule affinity-regulating kinase 1/2/4
IPR020671 BR serine/threonine-protein kinase
IPR020673 Serine/threonine-protein kinase KIN1/2
IPR020674 Serine/threonine-protein kinase KIN4-related
IPR020675 Myosin light chain kinase-related
IPR020676 Death-associated protein kinase
IPR020677 Serine/threonine-protein kinase Y2666, predicted
IPR020679 Serine/threonine-protein kinase YMR291W, predicted
IPR020682 Obscurin/Myosin light chain kinase
IPR020684 Rho-associated coiled-coil containing protein kinase-like
Contains IPR003527 MAP kinase, conserved site
IPR008271 Serine/threonine-protein kinase, active site
IPR017441 Protein kinase, ATP binding site
GO Term annotationHelp
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Process GO:0006468 protein amino acid phosphorylation
Function GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp
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Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of 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. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [1]:

  • Serine/threonine-protein kinases
  • Tyrosine-protein kinases
  • Dual specific protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)

Protein kinase function has been evolutionarily conserved from Escherichia coli to human [2]. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation [3]. 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 [4], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [5].

Eukaryotic protein kinases [6, 7, 8, 9, 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 [10].
Structural linksHelp
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PDB - click here
1a06 , 1a9u , 1apm , 1aq1 , 1atp , 1b38 , 1b39 , 1bi7 , 1bi8 , 1bkx , 1bl6 , 1bl7 , 1blx , 1bmk , 1buh , 1bx6 , 1cdk , 1ckp , 1cm8 , 1cmk , 1ctp , 1daw , 1day , 1di8 , 1di9 , 1dm2 , 1ds5 , 1e1v , 1e1x , 1e9h , 1erk , 1f0q , 1f3m , 1f5q , 1fin , 1fmo , 1fot , 1fq1 , 1fvt , 1fvv , 1g3n , 1g5s , 1gih , 1gii , 1gij , 1gng , 1gol , 1gy3 , 1gz8 , 1gzk , 1gzn , 1gzo , 1h00 , 1h01 , 1h07 , 1h08 , 1h0v , 1h0w , 1h1p , 1h1q , 1h1r , 1h1s , 1h1w , 1h24 , 1h25 , 1h26 , 1h27 , 1h28 , 1h4l , 1h8f , 1hck , 1hcl , 1i09 , 1ia8 , 1ian , 1ig1 , 1j1b , 1j1c , 1j3h , 1j91 , 1jam , 1jbp , 1jkk , 1jkl , 1jks , 1jkt , 1jlu , 1jnk , 1jow , 1jst , 1jsu , 1jsv , 1jvp , 1jwh , 1ke5 , 1ke6 , 1ke7 , 1ke8 , 1ke9 , 1koa , 1kob , 1kv1 , 1kv2 , 1kwp , 1l3r , 1lez , 1lp4 , 1lpu , 1lr4 , 1m2p , 1m2q , 1m2r , 1m7q , 1mq4 , 1mru , 1mrv , 1mry , 1muo , 1na7 , 1nvq , 1nvr , 1nvs , 1nxk , 1ny3 , 1o6k , 1o6l , 1o6y , 1o9u , 1ob3 , 1ogu , 1oi9 , 1oiq , 1oir , 1oit , 1oiu , 1oiy , 1okv , 1okw , 1oky , 1okz , 1ol1 , 1ol2 , 1ol5 , 1ol6 , 1ol7 , 1om1 , 1omw , 1ouk , 1ouy , 1ove , 1oz1 , 1p2a , 1p38 , 1p4f , 1p5e , 1pf8 , 1phk , 1pjk , 1pkd , 1pme , 1pmn , 1pmq , 1pmu , 1pmv , 1pw2 , 1pxi , 1pxj , 1pxk , 1pxl , 1pxm , 1pxn , 1pxo , 1pxp , 1pye , 1pyx , 1q24 , 1q3d , 1q3w , 1q41 , 1q4l , 1q5k , 1q61 , 1q62 , 1q8t , 1q8u , 1q8w , 1ql6 , 1qmz , 1r0e , 1r39 , 1r3c , 1r78 , 1rdq , 1re8 , 1rej , 1rek , 1s9i , 1s9j , 1smh , 1stc , 1sve , 1svg , 1svh , 1syk , 1szm , 1tki , 1tvo , 1u5q , 1u5r , 1ua2 , 1ukh , 1uki , 1ung , 1unh , 1unl , 1urc , 1urw , 1uu3 , 1uu7 , 1uu8 , 1uu9 , 1uv5 , 1uvr , 1v0b , 1v0o , 1v0p , 1v1k , 1veb , 1vyw , 1vyz , 1vzo , 1w0x , 1w7h , 1w82 , 1w83 , 1w84 , 1w8c , 1w98 , 1wbn , 1wbo , 1wbs , 1wbt , 1wbv , 1wbw , 1wcc , 1wfc , 1wvw , 1wvx , 1wvy , 1wzy , 1xh4 , 1xh5 , 1xh6 , 1xh7 , 1xh8 , 1xh9 , 1xha , 1xjd , 1xo2 , 1xqz , 1xr1 , 1xws , 1y8y , 1y91 , 1ydr , 1yds , 1ydt , 1yhv , 1yhw , 1yi3 , 1yi4 , 1ykr , 1ym7 , 1yqj , 1yrp , 1yw2 , 1ywr , 1ywv , 1yxs , 1yxt , 1yxu , 1yxv , 1yxx , 1z57 , 1z5m , 1zlt , 1zoe , 1zog , 1zoh , 1zrz , 1zyj , 1zys , 1zz2 , 1zzl , 2a0c , 2a4l , 2ayp , 2b1p , 2b52 , 2b53 , 2b54 , 2b55 , 2b9f , 2b9h , 2b9i , 2b9j , 2baj , 2bak , 2bal , 2baq , 2bcj , 2bfx , 2bfy , 2bhe , 2bhh , 2bik , 2bil , 2biy , 2bkz , 2bmc , 2bpm , 2br1 , 2brb , 2brg , 2brh , 2brm , 2brn , 2bro , 2btr , 2bts , 2bva , 2bzh , 2bzi , 2bzj , 2bzk , 2c1a , 2c1b , 2c30 , 2c3i , 2c3j , 2c3k , 2c3l , 2c4g , 2c5n , 2c5o , 2c5v , 2c5x , 2c5y , 2c68 , 2c69 , 2c6d , 2c6e , 2c6i , 2c6k , 2c6l , 2c6m , 2c6o , 2c6t , 2cch , 2cci , 2cdz , 2cgu , 2cgv , 2cgw , 2cgx , 2cjm , 2clx , 2cpk , 2ds1 , 2duv , 2dwb , 2dyl , 2e14 , 2e9n , 2e9o , 2e9p , 2e9u , 2e9v , 2erk , 2erz , 2euf , 2ewa , 2exc , 2exm , 2f2c , 2f49 , 2f57 , 2f7e , 2f7x , 2f7z , 2f9g , 2fa2 , 2fsl , 2fsm , 2fso , 2fst , 2fum , 2fvd , 2fys , 2g01 , 2g9x , 2gcd , 2gdo , 2gfc , 2gfs , 2ghg , 2ghl , 2ghm , 2gmx , 2gnf , 2gng , 2gnh , 2gni , 2gnj , 2gnl , 2gph , 2gtm , 2gtn , 2h96 , 2hog , 2hxl , 2hxq , 2hy0 , 2hy8 , 2i0e , 2i0h , 2i40 , 2i6l , 2iw6 , 2iw8 , 2iw9 , 2iwi , 2j0i , 2j2i , 2j4z , 2j50 , 2j51 , 2j7t , 2j9m , 2jav , 2jbp , 2jdo , 2jdr , 2jds , 2jed , 2jfl , 2jfm , 2jgz , 2no3 , 2npq , 2o0u , 2o2u , 2o3p , 2o5k , 2o63 , 2o64 , 2o65 , 2obj , 2oh0 , 2oi4 , 2ojf , 2ojg , 2oji , 2ojj , 2ok1 , 2okr , 2onl , 2ow3 , 2oxd , 2oxx , 2oxy , 2oza , 2p33 , 2p55 , 2pe0 , 2pe1 , 2pe2 , 2phk , 2pk9 , 2pkj , 2pmi , 2ptj , 2pto , 2pv5 , 2pv8 , 2pvh , 2pvj , 2pvk , 2pvl , 2pvm , 2pvn , 2pvr , 2q0n , 2qc6 , 2qcs , 2qd9 , 2qhm , 2qhn , 2qkr , 2qvs , 2r0u , 2r3f , 2r3g , 2r3h , 2r3i , 2r3j , 2r3k , 2r3l , 2r3m , 2r3n , 2r3o , 2r3p , 2r3q , 2r3r , 2r7b , 2r7i , 2r9s , 2rg5 , 2rg6 , 2uue , 2uv2 , 2uw9 , 2uzb , 2uzd , 2uze , 2uzl , 2uzn , 2uzo , 2v0d , 2v22 , 2vgp , 2vo7 , 2ywp , 2z7l , 2zaz , 2zb0 , 2zb1 , 2zdt , 2zdu , 3bgp , 3bgq , 3bgz , 3bht , 3bhu , 3bhv , 3blh , 3blq , 3blr , 3bqc , 3bv2 , 3bv3 , 3bw5 , 3bx5 , 3c13 , 3c4e , 3c5u , 3c9w , 3cg2 , 3cgf , 3cgo , 3ckw , 3ckx , 3coi , 3com , 3d0e , 3d7z , 3d83 , 3dcv , 3ds6 , 3dt1 , 3e87 , 3e88 , 3e8d , 3e92 , 3e93 , 3erk , 4erk
SCOP: d.144.1.7
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Enzyme: EC:2.7.11
InteractionsHelp
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This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverageHelp
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Overlapping InterPro entriesHelp
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IPR002290 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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A2CG49 Kalirin

O00141 Serine/threonine-protein kinase Sgk1

O01427 Aurora/Ipl1-related protein kinase 2

O61267 Ovarian-specific serine/threonine-protein kinase Lok

P06244 cAMP-dependent protein kinase type 1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001251 Cellular retinaldehyde-binding/triple function, C-terminal
IPR017441 Protein kinase, ATP binding site
IPR017442 Serine/threonine-protein kinase-like domain
IPR013098 Immunoglobulin I-set
IPR017892 Protein kinase, C-terminal
IPR011009 Protein kinase-like domain
IPR008957 Fibronectin, type III-like fold
IPR018159 Spectrin/alpha-actinin
IPR000719 Protein kinase, catalytic domain
IPR002290 Serine/threonine-protein kinase domain
IPR020636 Calcium/calmodulin-dependent protein kinase-like
IPR011511 Variant SH3
IPR003961 Fibronectin, type III
IPR002017 Spectrin repeat
IPR011993 Pleckstrin homology-type
IPR007110 Immunoglobulin-like
IPR003598 Immunoglobulin subtype 2
IPR001849 Pleckstrin homology
IPR000219 Dbl homology (DH) domain
IPR001452 Src homology-3 domain
IPR008271 Serine/threonine-protein kinase, active site
IPR020663 Spindle assembly checkpoint kinase
IPR000961 AGC-kinase, C-terminal
IPR020648 Serine/threonine-protein kinase Chk2
IPR000253 Forkhead-associated
IPR008984 SMAD/FHA domain
ModBase
SWISS-MODEL
PDB Chain
CATH Domain
SCOP Domain

PublicationsHelp
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1. Hanks SK, Quinn AM, Hunter T.
The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.
Science 241 42-52 1988 [PubMed: 3291115]
http://www.sciencemag.org/cgi/content/abstract/241/4861/42
2. Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S.
The protein kinase complement of the human genome.
Science 298 1912-34 2002 [PubMed: 12471243]
http://dx.doi.org/10.1126/science.1075762
3. Manning G, Plowman GD, Hunter T, Sudarsanam S.
Evolution of protein kinase signaling from yeast to man.
Trends Biochem. Sci. 27 514-20 2002 [PubMed: 12368087]
http://dx.doi.org/10.1016/S0968-0004(02)02179-5
4. Stout TJ, Foster PG, Matthews DJ.
High-throughput structural biology in drug discovery: protein kinases.
Curr. Pharm. Des. 10 1069-82 2004 [PubMed: 15078142]
http://dx.doi.org/10.2174/1381612043452695
5. Li B, Liu Y, Uno T, Gray N.
Creating chemical diversity to target protein kinases.
Comb. Chem. High Throughput Screen. 7 453-72 2004 [PubMed: 15320712]
http://openurl.ingenta.com/content?genre=article&issn=1386-2073&volume=7&issue=5&spage=453
6. Hanks SK.
Eukaryotic protein kinases.
Curr. Opin. Struct. Biol. 1 369-83 1991
7. Hanks SK, Hunter T.
Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification.
FASEB J. 9 576-96 1995 [PubMed: 7768349]
http://www.fasebj.org/cgi/content/abstract/9/8/576
8. Hunter T.
Protein kinase classification.
Meth. Enzymol. 200 3-37 1991 [PubMed: 1835513]
http://dx.doi.org/10.1016/0076-6879(91)00125-G
9. Hanks SK, Quinn AM.
Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members.
Meth. Enzymol. 200 38-62 1991 [PubMed: 1956325]
http://dx.doi.org/10.1016/0076-6879(91)00126-H
10. Knighton DR, Zheng JH, Ten Eyck LF, Ashford VA, Xuong NH, Taylor SS, Sowadski JM.
Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.
Science 253 407-14 1991 [PubMed: 1862342]
http://www.sciencemag.org/cgi/content/abstract/253/5018/407

Additional ReadingHelp
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Lamson RE, Winters MJ, Pryciak PM.
Cdc42 regulation of kinase activity and signaling by the yeast p21-activated kinase Ste20.
Mol. Cell. Biol. 22 2002 2939-51 [PubMed: 11940652]
http://dx.doi.org/10.1128/MCB.22.9.2939-2951.2002
Baumli S, Lolli G, Lowe ED, Troiani S, Rusconi L, Bullock AN, Debreczeni JE, Knapp S, Johnson LN.
The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation.
EMBO J. 27 2008 1907-18 [PubMed: 18566585]
http://dx.doi.org/10.1038/emboj.2008.121
Wrobleski ST, Lin S, Hynes J Jr, Wu H, Pitt S, Shen DR, Zhang R, Gillooly KM, Shuster DJ, McIntyre KW, Doweyko AM, Kish KF, Tredup JA, Duke GJ, Sack JS, McKinnon M, Dodd J, Barrish JC, Schieven GL, Leftheris K.
Synthesis and SAR of new pyrrolo[2,1-f][1,2,4]triazines as potent p38 alpha MAP kinase inhibitors.
Bioorg. Med. Chem. Lett. 18 2008 2739-44 [PubMed: 18364256]
http://dx.doi.org/10.1016/j.bmcl.2008.02.067
Raaf J, Klopffleisch K, Issinger OG, Niefind K.
The catalytic subunit of human protein kinase CK2 structurally deviates from its maize homologue in complex with the nucleotide competitive inhibitor emodin.
J. Mol. Biol. 377 2008 1-8 [PubMed: 18242640]
http://dx.doi.org/10.1016/j.jmb.2008.01.008
Raaf J, Brunstein E, Issinger OG, Niefind K.
The CK2 alpha/CK2 beta interface of human protein kinase CK2 harbors a binding pocket for small molecules.
Chem. Biol. 15 2008 111-7 [PubMed: 18291315]
http://dx.doi.org/10.1016/j.chembiol.2007.12.012
Rouse MB, Seefeld MA, Leber JD, McNulty KC, Sun L, Miller WH, Zhang S, Minthorn EA, Concha NO, Choudhry AE, Schaber MD, Heerding DA.
Aminofurazans as potent inhibitors of AKT kinase.
Bioorg. Med. Chem. Lett. 19 2009 1508-11 [PubMed: 19179070]
http://dx.doi.org/10.1016/j.bmcl.2009.01.002
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