spacer
spacer
EBIDatabasesInterPro

Jump to: InterProScan Databases Documentation FTP site Help
Click on the icon for context sensitive help from the user manual.
Advanced search

InterPro: IPR008271 Serine/threonine-protein kinase, active site

Protein matchesHelp
Open in usermanual
UniProtKB
Matches:
42845 proteins
AccessionHelp
Open in usermanual
IPR008271 Ser/Thr_prot_kinase_AS
SecondaryHelp
Open in usermanual
IPR002290
TypeHelp
Open in usermanual
Active_site
SignaturesHelp
Open in usermanual
InterPro RelationshipsHelp
Open in usermanual
Found in IPR000239 GPCR kinase
IPR000719 Protein kinase, catalytic domain
IPR002290 Serine/threonine-protein kinase domain
IPR002291 Phosphorylase kinase, gamma catalytic subunit
IPR003527 MAP kinase, conserved site
IPR008349 ERK1/2 MAP kinase
IPR008350 ERK3/4 MAP kinase
IPR008351 JNK MAP kinase
IPR011009 Protein kinase-like domain
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
IPR015515 Protein kinase GCN2
IPR015516 Haem-Regulated Eukaryotic Initiation Factor EIF-2-Alpha Kinase
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
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
IPR015751 Rho-associated coiled-coil containing protein kinase
IPR015769 TGF-beta type II receptor, C-terminal
IPR015783 ATMRK serine/threonine protein kinase-like
IPR015784 Tyrosine-protein kinase, ATN1-like
IPR015785 Mitogen activated protein kinase kinase kinase-like
IPR015786 Mitogen activated protein kinase kinase kinase-related
IPR016231 Mitogen-activated protein kinase kinase kinase, 9/10/11
IPR016232 cGMP-dependent protein kinase
IPR016234 Serine/threonine-protein kinase, Sbk1
IPR016235 Tyrosine/threonine-protein kinase, Cdc2 inhibitor
IPR016237 Serine/threonine-protein kinase, Ulk1/Ulk2
IPR016238 Ribosomal protein S6 kinase
IPR016239 Ribosomal protein S6 kinase II
IPR016240 Serine/threonine-protein kinase YKL116C, predicted
IPR016241 Serine/threonine-protein kinase YKL171W, predicted
IPR016242 Serine/threonine-protein kinase MPS1
IPR016254 Serine/threonine-protein kinase, asfivirus
IPR016255 Serine/threonine-protein kinase, GCN2
IPR016256 Serine/threonine-protein kinase RAD53
IPR017090 Serine/threonine-protein kinase, SNF1-like
IPR017164 Wee1-like protein kinase
IPR017184 Serine/threonine-protein kinase Unc-51
IPR017194 Transforming growth factor-beta receptor, type II
IPR017239 MAP kinase kinase kinase STE11
IPR017240 MAP kinase kinase kinase, SSK22
IPR017322 Receptor-interacting serine/threonine-protein kinase 2
IPR017348 Proto-oncogene serine/threonine-protein kinase Pim-1
IPR017405 Citron Rho-interacting kinase
IPR017419 Mitogen-activated protein kinase kinase kinase, 12/13
IPR017421 Mitogen-activated protein kinase kinase kinase 7
IPR017424 Mitogen-activated protein kinase kinase kinase 8
IPR017425 Mitogen-activated protein kinase kinase kinase 14
IPR017442 Serine/threonine-protein kinase-like domain
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
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
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
GO Term annotationHelp
Open in usermanual
Process GO:0006468 protein amino acid phosphorylation
Function GO:0004674 protein serine/threonine kinase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp
Open in usermanual

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, 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]. This signature contains the active site aspartate residue.
Structural linksHelp
Open in usermanual
PDB - click here
1a06 , 1apm , 1aq1 , 1atp , 1b38 , 1b39 , 1b6c , 1bi7 , 1bi8 , 1bkx , 1blx , 1buh , 1bx6 , 1cdk , 1cki , 1ckj , 1ckp , 1cmk , 1csn , 1ctp , 1daw , 1day , 1di8 , 1dm2 , 1ds5 , 1e1v , 1e1x , 1e9h , 1eh4 , 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 , 1how , 1i09 , 1ia8 , 1ias , 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 , 1kwp , 1l3r , 1lp4 , 1lpu , 1lr4 , 1m2p , 1m2q , 1m2r , 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 , 1p2a , 1p4f , 1p5e , 1pf8 , 1phk , 1pjk , 1pkd , 1pme , 1pmn , 1pmq , 1pmu , 1pmv , 1pw2 , 1pxi , 1pxj , 1pxk , 1pxl , 1pxm , 1pxn , 1pxo , 1pxp , 1py5 , 1pye , 1pyx , 1q24 , 1q3d , 1q3w , 1q41 , 1q4l , 1q5k , 1q61 , 1q62 , 1q8t , 1q8u , 1q8w , 1q8y , 1q8z , 1q97 , 1q99 , 1ql6 , 1qmz , 1r0e , 1r78 , 1rdq , 1re8 , 1rej , 1rek , 1rw8 , 1s9i , 1s9j , 1smh , 1stc , 1sve , 1svg , 1svh , 1syk , 1szm , 1tvo , 1u5q , 1u5r , 1ua2 , 1ukh , 1uki , 1ung , 1unh , 1unl , 1urc , 1urw , 1uu3 , 1uu7 , 1uu8 , 1uu9 , 1uv5 , 1uvr , 1uwh , 1uwj , 1v0b , 1v0o , 1v0p , 1v1k , 1veb , 1vjy , 1vyw , 1vyz , 1vzo , 1w0x , 1w8c , 1w98 , 1wak , 1wbp , 1wcc , 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 , 1yrp , 1ywv , 1yxs , 1yxt , 1yxu , 1yxv , 1yxx , 1z5m , 1zlt , 1zoe , 1zog , 1zoh , 1zrz , 1zys , 2a0c , 2a4l , 2ayp , 2b1p , 2b52 , 2b53 , 2b54 , 2b55 , 2b9f , 2b9h , 2b9i , 2b9j , 2bcj , 2bfx , 2bfy , 2bhe , 2bhh , 2bik , 2bil , 2biy , 2bkz , 2bmc , 2bpm , 2br1 , 2brb , 2brg , 2brh , 2brm , 2brn , 2bro , 2btr , 2bts , 2bzh , 2bzi , 2bzj , 2bzk , 2c1a , 2c1b , 2c3i , 2c3j , 2c3k , 2c3l , 2c47 , 2c4g , 2c5n , 2c5o , 2c5v , 2c5x , 2c5y , 2c68 , 2c69 , 2c6d , 2c6e , 2c6i , 2c6k , 2c6l , 2c6m , 2c6o , 2c6t , 2cch , 2cci , 2cgu , 2cgv , 2cgw , 2cgx , 2chl , 2cjm , 2clx , 2cmw , 2cpk , 2csn , 2ds1 , 2duv , 2dwb , 2dyl , 2e14 , 2e9n , 2e9o , 2e9p , 2e9u , 2e9v , 2erk , 2erz , 2euf , 2exc , 2exm , 2f2c , 2f49 , 2f7e , 2f7x , 2f7z , 2f9g , 2fa2 , 2fb8 , 2fum , 2fvd , 2fys , 2g01 , 2g9x , 2gcd , 2gdo , 2gfc , 2ghg , 2gmx , 2gnf , 2gng , 2gnh , 2gni , 2gnj , 2gnl , 2gph , 2h96 , 2hog , 2hxl , 2hxq , 2hy0 , 2hy8 , 2i0e , 2i40 , 2i6l , 2iw6 , 2iw8 , 2iw9 , 2iwi , 2izr , 2izs , 2izt , 2izu , 2j2i , 2j4z , 2j50 , 2j51 , 2j7t , 2j9m , 2jav , 2jbp , 2jd5 , 2jdo , 2jdr , 2jds , 2jed , 2jfl , 2jfm , 2jgz , 2no3 , 2o0u , 2o2u , 2o3p , 2o5k , 2o63 , 2o64 , 2o65 , 2obj , 2oh0 , 2oi4 , 2ojf , 2ojg , 2oji , 2ojj , 2ok1 , 2onl , 2ow3 , 2oxd , 2oxx , 2oxy , 2oza , 2p33 , 2p55 , 2pe0 , 2pe1 , 2pe2 , 2phk , 2pk9 , 2pmi , 2pvh , 2pvj , 2pvk , 2pvl , 2pvm , 2pvn , 2pvr , 2qc6 , 2qcs , 2qhm , 2qhn , 2qkr , 2qlu , 2qvs , 2r0u , 2r3f , 2r3g , 2r3h , 2r3i , 2r3j , 2r3k , 2r3l , 2r3m , 2r3n , 2r3o , 2r3p , 2r3q , 2r3r , 2r7b , 2r7i , 2r9s , 2uue , 2uv2 , 2uw9 , 2uzb , 2uzd , 2uze , 2uzl , 2uzn , 2uzo , 2v0d , 2v22 , 2vgp , 2vo7 , 2ywp , 2z7l , 2zdt , 2zdu , 3beg , 3bgp , 3bgq , 3bgz , 3bht , 3bhu , 3bhv , 3blh , 3blq , 3blr , 3bqc , 3bw5 , 3c13 , 3c4c , 3c4d , 3c4e , 3c9w , 3cgf , 3cgo , 3d0e , 3dcv , 3e87 , 3e88 , 3e8d , 3erk , 4erk
SCOP: d.144.1.7
CATH: 1.10.510.10
Database linksHelp
Open in usermanual
PDBe-motif: PS00108
Enzyme: EC:2.7.11
PROSITE doc: PDOC00100
InteractionsHelp
Open in usermanual
This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverageHelp
Open in usermanual

Overlapping InterPro entriesHelp
Open in usermanual
IPR008271 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
Open in usermanual
A2CG49 Kalirin

O00141 Serine/threonine-protein kinase Sgk1

O01427 Aurora/Ipl1-related protein kinase 2

P06244 cAMP-dependent protein kinase type 1

Q05652 Serine/threonine-protein kinase pelle

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001251 Cellular retinaldehyde-binding/triple function, C-terminal
IPR000488 Death
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
IPR011029 DEATH-like
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
IPR015787 Interleukin-1 receptor-associated kinase 4, C-terminal
ModBase
SWISS-MODEL
PDB Chain
CATH Domain
SCOP Domain

PublicationsHelp
Open in usermanual
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, 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
7. Hunter T.
Protein kinase classification.
Meth. Enzymol. 200 3-37 1991 [PubMed: 1835513]
http://dx.doi.org/10.1016/0076-6879(91)00125-G
8. 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
9. 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
Open in usermanual
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
Heerding DA, Rhodes N, Leber JD, Clark TJ, Keenan RM, Lafrance LV, Li M, Safonov IG, Takata DT, Venslavsky JW, Yamashita DS, Choudhry AE, Copeland RA, Lai Z, Schaber MD, Tummino PJ, Strum SL, Wood ER, Duckett DR, Eberwein D, Knick VB, Lansing TJ, McConnell RT, Zhang S, Minthorn EA, Concha NO, Warren GL, Kumar R.
Identification of 4-(2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-{[(3S)-3-piperidinylmethyl]oxy}-1H-imidazo[4,5-c]pyridin-4-yl)-2-methyl-3-butyn-2-ol (GSK690693), a novel inhibitor of AKT kinase.
J. Med. Chem. 51 2008 5663-79 [PubMed: 18800763]
http://dx.doi.org/10.1021/jm8004527
Asano Y, Kitamura S, Ohra T, Itoh F, Kajino M, Tamura T, Kaneko M, Ikeda S, Igata H, Kawamoto T, Sogabe S, Matsumoto S, Tanaka T, Yamaguchi M, Kimura H, Fukumoto S.
Discovery, synthesis and biological evaluation of isoquinolones as novel and highly selective JNK inhibitors (2).
Bioorg. Med. Chem. 16 2008 4699-714 [PubMed: 18313930]
http://dx.doi.org/10.1016/j.bmc.2008.02.028
Kirby R.
Evolutionary origin of aminoglycoside phosphotransferase resistance genes.
J. Mol. Evol. 30 1990 489-92 [PubMed: 2165531]
http://dx.doi.org/10.1007/BF02101103
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
Lee BH, Min X, Heise CJ, Xu BE, Chen S, Shu H, Luby-Phelps K, Goldsmith EJ, Cobb MH.
WNK1 phosphorylates synaptotagmin 2 and modulates its membrane binding.
Mol. Cell 15 2004 741-51 [PubMed: 15350218]
http://dx.doi.org/10.1016/j.molcel.2004.07.018
Caldwell JJ, Davies TG, Donald A, McHardy T, Rowlands MG, Aherne GW, Hunter LK, Taylor K, Ruddle R, Raynaud FI, Verdonk M, Workman P, Garrett MD, Collins I.
Identification of 4-(4-aminopiperidin-1-yl)-7H-pyrrolo[2,3-d]pyrimidines as selective inhibitors of protein kinase B through fragment elaboration.
J. Med. Chem. 51 2008 2147-57 [PubMed: 18345609]
http://dx.doi.org/10.1021/jm701437d
Bairoch A, Claverie JM.
Sequence patterns in protein kinases.
Nature 331 1988 22 [PubMed: 3340146]
http://dx.doi.org/10.1038/331022a0
spacer
spacer
Page rendered:
Database: IWEB
Request
Host tomcat-7.ebi.ac.uk
Server up Sun Nov 22 21:55:16 GMT 2009
Initialise JS Log Login settings Flush
InterPro 23.1