ENSP00000005198 312 T YES 15610029 T312A retains only basal activity, 1-3% of WT autoactivation? 0 ENSP00000011619 483 S NA 15345747 Mouse brain phosphoproteomics 0 ENSP00000011619 487 S NA 15345747 Mouse brain phosphoproteomics 0 ENSP00000251527 733 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000260600 1076 S NA 9768837,8798667 Not tested. CaMKII 0 ENSP00000250003 200 S YES 9710583 Site-directed mutagenesis of potential CDK phosphorylation sites in MyoD revealed that S200 is required for MyoD hyperphosphorylation as well as the normally short half-life of the MyoD protein. 0 ENSP00000250003 115 T YES 1335366 A myogenin mutant lacking the PKC phosphorylation site is not repressed by FGF, confirming this site as a molecular target for FGF-dependent repression of muscle transcription. Site not mentioned in abstract. Pkc 0 ENSP00000261597 77 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000261597 165 S YES 12386167 Whereas wild-type human Hec1 rescues lethality resulting from deletion of Hec1 in Saccharomyces cerevesiae, a human Hec1 mutant or yeast Hec1 mutant changing Ser(165) to Ala or yeast Hec1 mutant changing Ser(201) to Ala does not. Mutations changing the same Ser residues to Glu, to mimic the negative charge created by phosphorylation, partially rescue lethality but result in a high incidence of errors in chromosomal segregation. Nek2 0 ENSP00000261597 76 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000251849 621 S YES 9710607,9091312,11971957 Mutation of serine 259 increased the basal Raf-1 activity and rendered it largely resistant to inhibition by PKA. This supports a paradigm in which the effects of phosphorylation on serine as well as tyrosine residues are mediated by inducible protein-protein interactions. Site different from abstract. Pka 0 ENSP00000251849 289 S NA 15664191 Site not mentioned in abstract. 0 ENSP00000251849 491 T YES 11447113 Here we demonstrate that phosphorylation of C-Raf in the kinase activation loop (residues T491 and S494) is necessary, but not sufficient, for activation 0 ENSP00000251849 269 T PROBYES 7477354 Here we report that CAP kinase phosphorylates Raf1 on Thr 269, increasing its activity towards MEK (MAP kinase or ERK kinase). 0 ENSP00000251849 494 S YES 11447113 Here we demonstrate that phosphorylation of C-Raf in the kinase activation loop (residues T491 and S494) is necessary, but not sufficient, for activation, 0 ENSP00000251849 338 S YES 11733498,10205168,9234708,12551923,9823899 Mutations which prevent phosphorylation at either site block Raf-1 activation and maximal activity is seen only when both are phosphorylated. By using a combination of mitogenic and enzymatic assays, we found that phosphorylation of the adjacent residue, serine 338, and, to a lesser extent, serine 339 is essential for the biological and enzymatic activities of Raf-1. Replacement of S338 with alanine blocked the ability of prenylated Raf-CX to transform Rat-1 fibroblasts Pak1 0 ENSP00000251849 29 S NA 15664191 Site not mentioned in abstract. 0 ENSP00000251849 301 S NA 15664191 Site not mentioned in abstract. 0 ENSP00000251849 233 S NA 11997508 Not tested. 0 ENSP00000251849 339 S PROBYES 9234708 Consistent with phosphorylation of S338-S339, acidic amino acid substitutions of these residues partially restored transforming activity to Raf-CX, as well as kinase activation of Raf-1 by Ras[V12] or v-Src. 0 ENSP00000251849 259 S YES 11997508,11971957,10576742 Mutation of serine 259 increased the basal Raf-1 activity and rendered it largely resistant to inhibition by PKA. Pka 0 ENSP00000251849 268 T NA 8349614 Not tested 0 ENSP00000251849 296 S NA 15664191 Site not mentioned in abstract 0 ENSP00000251849 499 S YES 8321321 Mutation of serine at this position or at residue 259 does not abrogate Raf-1 stimulation by a combination of Ras plus the src tyrosine kinase Lck, but severely impedes Raf-1 activation by PKC alpha. The Ser499 phosphorylation site is necessary for this synergism. Pkc 0 ENSP00000251849 642 S NA 15664191 Site not mentioned in abstract. 0 ENSP00000251849 43 S PROBYES 11997508,11971957 Serine 43 phosphorylation decreased the binding to Ras in serum-starved but not in mitogen-stimulated cells Pka 0 ENSP00000202816 694 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000202816 657 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000202816 75 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000202816 663 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000261313 153 S NA 14654844,12551925 Not tested. 0 ENSP00000262461 212 T NA 16669787 Not tested. 0 ENSP00000262461 203 T NA 16669787 Not tested. 0 ENSP00000262461 207 T NA 16669787 Not tested. 0 ENSP00000263125 538 T YES 11772397 >100-fold reduction in the T538A mutant 0 ENSP00000263125 219 T YES 16252004 The T219A mutation abrogated the capacity of PKCtheta to mediate NF-kappaB, NF-AT and interleukin-2 promoter transactivation, and reduced PKCtheta s ability in Jurkat T cells to phosphorylate endogenous cellular substrates 0 ENSP00000263125 676 S PROBNOT 11772397 In contrast with mechanisms proposed for other PKC isoforms, phosphorylation at the other two sites does not reconstitute catalytic activity 0 ENSP00000263125 695 S PROBNOT 11772397 In contrast with mechanisms proposed for other PKC isoforms, phosphorylation at the other two sites does not reconstitute catalytic activity 0 ENSP00000232424 38 S PROBYES 9389649 Mutation of these sites generates a constitutively active protein that strongly and persistently blocks response to NGF. No details on the sites. 0 ENSP00000232424 37 S PROBYES 9389649 Mutation of these sites generates a constitutively active protein that strongly and persistently blocks response to NGF. No details on the sites. 0 ENSP00000222812 188 S YES 12730201 Syntaxin-1A phosphorylation by DAP kinase or its S188D mutant, which mimics a state of complete phosphorylation, significantly decreases syntaxin binding to Munc18-1 0 ENSP00000222812 14 S PROBYES 10844023,9930733 hosphorylated syntaxin is preferentially associated with SNAP-25 and localizes to discrete domains of the axonal plasma membrane that do not colocalize with pools of synaptic vesicles 0 ENSP00000261173 1178 S PROBYES 2548572 The effect of the phosphorylation is to decrease the Km for Ca2+ of the purified ATPase from about 10 microM to about 1.4 microM and to increase the Vmax of ATP hydrolysis about 2-fold. cAMP-dependent protein kinase 0 ENSP00000261173 1116 T NA 1827443 Site not mentioned in abstract. 0 ENSP00000223641 17 S NA 16083285 Large scale phosphoproteomics 0 ENSP00000263277 438 S NA 15345747,15302935 Phosphoproteomics 0 ENSP00000257934 1508 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000234961 363 S YES 11040053 Truncation (Delta15) or substitutions (T358A, T361A, and S363G single or triple mutants) at the DOR cytoplasmic tail caused 80 to 100% loss of opioid-stimulated receptor phosphorylation, indicating that T358, T361, and S363 all contribute and are cooperatively involved in agonist-stimulated DOR phosphorylation 0 ENSP00000234961 361 T YES 11040053 Truncation (Delta15) or substitutions (T358A, T361A, and S363G single or triple mutants) at the DOR cytoplasmic tail caused 80 to 100% loss of opioid-stimulated receptor phosphorylation, indicating that T358, T361, and S363 all contribute and are cooperatively involved in agonist-stimulated DOR phosphorylation 0 ENSP00000234961 358 T YES 11040053 Truncation (Delta15) or substitutions (T358A, T361A, and S363G single or triple mutants) at the DOR cytoplasmic tail caused 80 to 100% loss of opioid-stimulated receptor phosphorylation, indicating that T358, T361, and S363 all contribute and are cooperatively involved in agonist-stimulated DOR phosphorylation 0 ENSP00000219302 61 S YES 11042679 The integrity of the NDP kinase activity and the presence of a serine residue in position 61 seem essential for the ability of DR-nm23 to trigger differentiation and to bind other Nm23 proteins 0 ENSP00000242576 60 T NA 15302935 Large scale phosphoproteomics 0 ENSP00000262445 261 T NA 9162092 Site does not correspond to abstract. 0 ENSP00000262445 80 S YES 11707464 The SEK1 mutant SEK1(S78A) was resistant to Akt-induced inhibition. Finally, activated Akt inhibited SEK1-mediated apoptosis, and this effect of Akt was prevented by overexpression of SEK(S78A). Site different from abstract. Akt 0 ENSP00000262445 257 S NA 9162092 Site not mentioned in abstract. 0 ENSP00000281043 261 S NA 1425701 8247525: speculates that DNA binding is affected but no mutational evidence. CKII 0 ENSP00000281043 263 S NA 1425701 8247525: speculates that DNA binding is affected but no mutational evidence. CKII 0 ENSP00000221249 306 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000217026 440 T PROBNOT 10095772 Six sites in B-Myb fulfil the requirements for recognition by Cdk2. Using point mutation of the phosphorylation sites to nonphosphorylatable amino acids, we show that five of these sites are targets for Cdk2 in vivo. Mutation of one of these residues (T524) to alanine diminished the ability of B-Myb to promote transcription of a reporter gene Cdk2 0 ENSP00000217026 577 S PROBYES 9840932 One phosphorylation site (Ser(581)) appeared to negatively regulate DNA binding, as mutation of this site enhanced the ability of B-Myb to bind a Myb-binding sequence ? Serine 581 or 577? 0 ENSP00000217026 452 S NA 10593981 Site different from abstract 0 ENSP00000217026 282 S NA 10593981 Site different from abstract 0 ENSP00000217026 518 T NA 10593981 Site different from abstract 0 ENSP00000217026 266 T NA 10593981 Site different from abstract 0 ENSP00000217026 520 T PROBYES 10593981,10095772 Mutation of one of these residues (T524) to alanine diminished the ability of B-Myb to promote transcription of a reporter gene The site does not correspond to the abstract Cdk2 0 ENSP00000217026 393 S 10593981,15302935 The site does not correspond to the abstract 0 ENSP00000217026 487 T PROBYES 9840932 The site does not correspond to the abstract. Several sites mutated at the same time but B-Myb transactivation activity was significantly reduced in a mutant containing amino acid substitutions at all four identified cyclin A/Cdk2 sites and was constitutively low in Saos-2 cells where endogenous cyclin A/Cdk2 activity was unable to phosphorylate ectopically expressed B-Myb Cdk2 0 ENSP00000217026 444 T PROBYES 9840932 The site does not correspond to the abstract. Several sites mutated at the same time but B-Myb transactivation activity was significantly reduced in a mutant containing amino acid substitutions at all four identified cyclin A/Cdk2 sites and was constitutively low in Saos-2 cells where endogenous cyclin A/Cdk2 activity was unable to phosphorylate ectopically expressed B-Myb 0 ENSP00000304592 2204 T NA 600212 Not tested 0 ENSP00000244573 4 T NA 7499230 Not tested 0 ENSP00000244573 2 S NA 7499230 Not tested 0 ENSP00000216277 553 S NA 15302935 Phosphoproteomics 0 ENSP00000178640 315 T NA 7759517 Not tested 0 ENSP00000178640 311 S NA 7759517 Not tested 0 ENSP00000216554 174 S NA 11861906 Not tested CK2 0 ENSP00000216554 390 S NA 11861906 Not tested CK2 0 ENSP00000216554 389 S NA 11861906 Not tested CK2 0 ENSP00000219431 252 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000164139 15 S NA 16083285 Phosphoproteomics 0 ENSP00000216540 226 S YES 16027164 Mutation of only Ser-226 resulted in 30% decrease in Ntcp phosphorylation and in 2.5 and 3.2-fold increases in taurocholate uptake and Ntcp retention in the plasma membrane, respectively 0 ENSP00000253699 215 S PROBYES 16138080 We found that p38alpha can phosphorylate the Rab5 effectors EEA1 and Rabenosyn-5 on Thr-1392 and Ser-215, respectively, and these phosphorylation events regulate the recruitment of EEA1 and Rabenosyn-5 to membranes p38alpha 0 ENSP00000247461 564 S NA 9642293 Not tested Ck2 0 ENSP00000247461 562 T NA 16565220 Large scale phosphoproteomics 0 ENSP00000247461 554 S NA 9642293 Not tested 0 ENSP00000247461 583 S NA 16565220,9642293 Large scale phosphoproteomics 0 ENSP00000250617 124 S NA 15144186 Phosphoproteomics 0 ENSP00000250617 123 S NA 15144186 Phosphoproteomics 0 ENSP00000250617 122 S NA 15144186 Phosphoproteomics 0 ENSP00000250617 684 S NA 15144186 Phosphoproteomics 0 ENSP00000250617 126 S NA 15144186 Phosphoproteomics 0 ENSP00000250617 150 S NA 15144186 Phosphoproteomics 0 ENSP00000265165 166 S PROBYES 12556497 Mutation of both residues to alanine enhanced LEF-1 transcriptional activity and rendered it resistant to inhibition by NLK. Phosphorylation of TCF-4 by NLK inhibited DNA binding by the beta-catenin-TCF-4 complex. However, this inhibition was abrogated when a mutant form of TCF-4 was used in which both threonines were replaced with valines. These results suggest that NLK phosphorylation on these sites contributes to the down-regulation of LEF-1/TCF transcriptional activity. Site not mentioned in abstract. 0 ENSP00000265165 155 T PROBYES 12556497 Mutation of both residues to alanine enhanced LEF-1 transcriptional activity and rendered it resistant to inhibition by NLK. Phosphorylation of TCF-4 by NLK inhibited DNA binding by the beta-catenin-TCF-4 complex. However, this inhibition was abrogated when a mutant form of TCF-4 was used in which both threonines were replaced with valines. These results suggest that NLK phosphorylation on these sites contributes to the down-regulation of LEF-1/TCF transcriptional activity. Site not mentioned in abstract. 0 ENSP00000246069 3 S YES 11418599,8674111,7615564 Cells also expressed high levels of mutant ADF when Ser3 was deleted or converted to either Ala or Glu 0 ENSP00000229812 74 T PROBYES 12493777 Thr-74 seems to be involved only in binding to S100B rather than directly regulating NDR1 activity per se 0 ENSP00000229812 281 S PROBYES 12493777 Previously, we demonstrated that the activity of NDR1 is controlled by phosphorylation of two regulatory residues, Ser-281 and Thr-444 0 ENSP00000229812 444 T PROBYES 12493777 Previously, we demonstrated that the activity of NDR1 is controlled by phosphorylation of two regulatory residues, Ser-281 and Thr-444 0 ENSP00000250559 179 S NA 12089143 Not tested Pka 0 ENSP00000260386 311 T PROBYES 9155020,9374536 Phosphorylation resulted in 8- to 10-fold enzyme activation and a 25-fold increase in sensitivity to the Ca2+:CaM complex CaM kinase II 0 ENSP00000362409 641 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000258960 47 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000251076 1400 S NA 15144186 Phosphoproteomics 0 ENSP00000251076 1404 S NA 15144186 Phosphoproteomics 0 ENSP00000262995 312 T NA 15379552 Not tested. 0 ENSP00000262995 476 T NA 15379552 Not tested. 0 ENSP00000262995 597 S NA 15379552 Not tested. 0 ENSP00000262995 381 S NA 15379552 Not tested. 0 ENSP00000262995 454 S NA 15379552 Not tested. 0 ENSP00000262995 581 S NA 15379552 Not tested. 0 ENSP00000233668 269 S NA 16094384 Large scale phosphoproteomics 0 ENSP00000233668 450 S NA 15144186 Large scale phosphoproteomics 0 ENSP00000233668 291 S NA 15570572 Large scale phosphoproteomics 0 ENSP00000265563 99 S NA 6293815 Site not mentioned in abstract. 0 ENSP00000265563 80 S NA 6293815 Site not mentioned in abstract. 0 ENSP00000265563 78 S NA 6293815 Site not mentioned in abstract. 0 ENSP00000265563 48 S NA 6293815 Site not mentioned in abstract. 0 ENSP00000234420 137 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000234420 254 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000234420 252 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000234420 830 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000234420 261 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000234420 256 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000234420 227 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000267812 116 S NA 16565220,15302935 Not tested. Phosphoproteomics. 0 ENSP00000267812 118 S NA 16565220,15302935 Not tested. Phosphoproteomics. 0 ENSP00000267812 132 S NA 15345747,15302935 Not tested. Phosphoproteomics. 0 ENSP00000267812 267 T NA 16565220,15302935 Not tested. Phosphoproteomics. 0 ENSP00000267812 133 S NA 15345747,15302935 Not tested. Phosphoproteomics. 0 ENSP00000235382 64 S NA 14608379 Not tested PKGI-alpha 0 ENSP00000235382 46 S NA 14608379 Not tested PKGI-alpha 0 ENSP00000261396 27 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000261396 28 T NA 16565220 Large scale phosphoproteomics 0 ENSP00000261396 45 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000222330 21 S PROBYES 11035810,12054501,8524413,11884598,15733869,11749387 GSK-3 activity is inhibited through phosphorylation of serine 21 in GSK-3 alpha and serine 9 in GSK-3 beta Pka 0 ENSP00000258780 284 S NA 15144186 Phosphoproteomics 0 ENSP00000224073 91 T NA 10816571 Not tested 0 ENSP00000225387 127 T NA 12060738 Phosphoproteomics 0 ENSP00000225387 160 S NA 12060738 Phosphoproteomics 0 ENSP00000262033 113 S NA 16094384 Phosphoproteomics 0 ENSP00000248901 356 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000220003 364 S YES 11181701 PKA phosphorylates Csk at S364 in vitro and in vivo leading to a two- to fourfold increase in Csk activity that is necessary for cAMP-mediated inhibition of TCR-induced interleukin 2 secretion 0 ENSP00000264705 456 T NA 12438317 Not tested. 0 ENSP00000264705 1859 S PROBYES 11986331,4092695 Phosphorylation activates the ammonia-dependent carbamyl phosphate synthetase activity of the complex by reducing the apparent Km for ATP 0 ENSP00000264705 1406 S PROBYES 11986331,4092695 Phosphorylation activates the ammonia-dependent carbamyl phosphate synthetase activity of the complex by reducing the apparent Km for ATP 0 ENSP00000264705 1037 T PROBYES 11986331,12438317 Phosphorylation activates the ammonia-dependent carbamyl phosphate synthetase activity of the complex by reducing the apparent Km for ATP 0 ENSP00000260210 375 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000260210 325 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000260210 358 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000268766 162 T NA 11864968 Not tested. 0 ENSP00000380373 85 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000226225 278 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000221232 299 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000225792 557 S NA 7525583 Pkc 0 ENSP00000254976 138 T NA 12459461 Not tested Pka 0 ENSP00000254976 187 S NA 12459461 Not tested. Pkc 0 ENSP00000262241 257 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000261845 189 S PROBYES 11741894,8621539 Ser189 of ERK3, which corresponds to Thr183, one of the activating phosphorylation sites of ERK2, is autophosphorylated in vitro and phosphorylated in vivo. 0 ENSP00000234739 315 T NA 15302935 Large scale phosphoproteomics 0 ENSP00000234739 687 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000001008 143 T NA 9405642 This is a test ime2 0 ENSP00000203630 238 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000219476 664 S NA 15851026 Site not mentioned in abstract 0 ENSP00000219476 939 S PROBYES 12438239 All seven 14-3-3 isoforms (beta, gamma, zeta, epsilon, tau, eta, and sigma) could bind tuberin, and this interaction was abrogated by competition with phosphorylated but not unphosphorylated Ser(939) tuberin peptide 0 ENSP00000219476 540 S NA 15851026 Site not mentioned in the abstract 0 ENSP00000219476 1254 S PROBYES 12582162 The site does not correspond to the abstract 0 ENSP00000219476 1462 T NA 12150915 Constitutively phosphorylated in PTEN(-/-) tumor-derived cell lines 0 ENSP00000252818 259 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000252818 255 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000257181 281 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000263274 66 S PROBYES 15302935,10523317 We propose that dephosphorylation of Ser66 is part of a novel control mechanism to establish the pre-replicative form of DNA ligase I. Ck2 0 ENSP00000228740 416 S NA 9395533 Not tested 0 ENSP00000254508 1844 T NA 16565220 Phosphoproteomics 0 ENSP00000254508 1881 S NA 8672508 Not tested 0 ENSP00000265164 257 S YES 15273717 Moreover, mutant caspase-6, in which the Ser257 was substituted by Ala (caspase-6/SA), induced cell death and FLIP degradation, even in SW480 cells. 0 ENSP00000253458 857 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000253458 909 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000229854 713 T NA 15302935 Large scale phosphoproteomics 0 ENSP00000229854 722 T NA 15302935 Large scale phosphoproteomics 0 ENSP00000262105 32 S PROBYES 16519687,12714602,16517729 16519687: Unexpectedly, MCM4 phosphorylated at site 32 was enriched in the nucleolus through the cell cycle. Cdk1 0 ENSP00000262105 3 S NA 16519687,16517729 Not tested. 0 ENSP00000262105 7 T NA 16519687,12714602,16517729 Not tested. Cdk2 0 ENSP00000262105 88 S NA 16519687 Not tested. 0 ENSP00000262105 19 T NA 16519687,12714602,16517729 Not tested. 0 ENSP00000262105 54 S NA 12714602,16517729 Not tested. 0 ENSP00000262105 110 T NA 16519687,12714602,16517729 Not tested. 0 ENSP00000257497 27 S NA 2457390 Not tested. Pkc 0 ENSP00000257497 216 T NA 2457390 Not tested. 0 ENSP00000257497 5 S PROBYES 15485879 The N-terminal region plays a crucial role in interaction of annexin 1 with other proteins and membranes, and therefore, phosphorylation of annexin 1 at Ser5 by TRPM7 kinase may modulate function of annexin 1. 0 ENSP00000263228 233 S PROBYES 12037680 Following CK2-dependent phosphorylation both UBC3B and UBC3 bind to the F-box protein beta-TrCP, the substrate recognition subunit of an SCF (Skp1, Cul1, F-box) ubiquitin ligase Ck2 0 ENSP00000215793 359 S NA 15302935 Phosphoproteomics 0 ENSP00000254657 662 S NA 9349507,11232563 Not tested CK1delta CK1epsilon 0 ENSP00000254657 977 S NA 16097765 Site not mentioned in abstract. 0 ENSP00000258198 194 S NA 15302935 Large scale phosphoproteomics. 0 ENSP00000230449 432 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000264758 408 S NA 8810272 Not tested. Pka 0 ENSP00000264758 445 T YES 10209029 he microinjection of Botulinum C3 ADP-ribosyl-transferase, dominant negative Rho-kinase, or alpha-adducinT445A,T480A (substitution of Thr445 and Thr480 by Ala) inhibited the TPA-induced membrane ruffling in MDCK cells and wound-induced migration in NRK49F cells. alpha-AdducinT445D,T480D (substitution of Thr445 and Thr480 by Asp), but not alpha-adducinT445A,T480A, counteracted the inhibitory effect of the dominant negative Rho-kinase on the TPA-induced membrane ruffling in MDCK cell 0 ENSP00000264758 436 S NA 8810272 Did not test this site specifically. 0 ENSP00000264758 726 S YES 8810272,9679146 hysiological consequences of the two PKC phosphorylation sites in the MARCKS-related domain were investigated by stably transfecting MDCK cells with either wild-type or PKC-unphosphorylatable S716A/S726A mutant alpha adducin. The mutant alpha adducin was no longer concentrated at the cell membrane at sites of cell-cell contact, and instead it was distributed as a cytoplasmic punctate pattern Pkc 0 ENSP00000264758 511 T PROBYES 10209029 The microinjection of Botulinum C3 ADP-ribosyl-transferase, dominant negative Rho-kinase, or alpha-adducinT445A,T480A (substitution of Thr445 and Thr480 by Ala) inhibited the TPA-induced membrane ruffling in MDCK cells and wound-induced migration in NRK49F cells. alpha-AdducinT445D,T480D (substitution of Thr445 and Thr480 by Asp), but not alpha-adducinT445A,T480A, counteracted the inhibitory effect of the dominant negative Rho-kinase on the TPA-induced membrane ruffling in MDCK cells. This site is not mentioned in the abstract. 0 ENSP00000260731 926 T YES 16565220,8548803,9235942 Mutation of Thr-927 to nonphosphorylatable residues prevents HsEg5 from binding to centrosomes, indicating that phosphorylation controls the association of this motor with the spindle apparatus 0 ENSP00000260731 931 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000236192 30 S NA 15345747,14608369 Large scale phosphoproteomics 0 ENSP00000221448 137 S PROBNOT 12548559 Synthesize peptides with S137 and S140 phosphorylation and report results for S140 only. 0 ENSP00000221448 140 S PROBYES 12548559 Synthesize peptides with S137 and S140 phosphorylation and report results for S140 only. 0 ENSP00000221448 226 S NA 15144186 Large scale phosphoproteomics 0 ENSP00000225402 203 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000225402 320 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000225402 321 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000225402 316 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000263208 687 S NA 11238922 Not tested cdk2 0 ENSP00000263208 555 T NA 11238922 Not tested 0 ENSP00000261461 28 S NA 10866685 Site not mentioned in abstract. 0 ENSP00000216117 188 S YES 15581622 S188D has 1.8 fold higher activity Protein kinase Akt/PKB 0 ENSP00000250896 27 S NA 11154262 Site not mentioned in the abstract. 0 ENSP00000250896 437 S NA 11154262 Site not mentioned in the abstract. 0 ENSP00000250896 440 S NA 11154262 Site not mentioned in the abstract. 0 ENSP00000250896 379 T NA 11154262 Site not mentioned in the abstract. 0 ENSP00000250896 452 S NA 11154262 Site not mentioned in the abstract. 0 ENSP00000250896 220 S NA 11154262 Site not mentioned in the abstract. 0 ENSP00000250896 454 S NA 11154262 Site not mentioned in the abstract. 0 ENSP00000262570 50 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000216492 398 S NA 9115255 0 ENSP00000216492 402 S NA 9115255 0 ENSP00000216492 333 S NA 9115255,9852066 0 ENSP00000216492 322 S NA 14997482 Small scale phosphoproteomics 0 ENSP00000216492 270 S NA 9852066 Not tested 0 ENSP00000216492 218 S NA 9852066 Not tested 0 ENSP00000239938 391 T NA 8662759 Site not mentioned in abstract CK2 0 ENSP00000239938 526 T NA 8662759 Site not mentioned in abstract 0 ENSP00000239938 378 S NA 8662759 Site not mentioned in abstract 0 ENSP00000262415 554 T NA 16094384 Phosphoproteomics 0 ENSP00000262415 557 S NA 16094384 Phosphoproteomics 0 ENSP00000230402 598 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000221566 303 T NA 15302935 Large scale phosphoproteomics 0 ENSP00000242719 135 T YES 16123141 There is also reduced 14-3-3 binding to T135E RNF11 0 ENSP00000257979 231 S NA 2176601 Site not mentioned in abstract. 0 ENSP00000257979 229 S NA 2176601 Site not mentioned in abstract. 0 ENSP00000257979 235 S NA 10067969 The major site of phosphorylation was determined to be at serine 235. Site not mentioned in abstract. 0 ENSP00000003084 790 S NA 1377674 Not tested 0 ENSP00000003084 737 S NA 1377674 Not tested 0 ENSP00000003084 660 S NA 1377674 Not tested 0 ENSP00000003084 795 S NA 1377674 Not tested 0 ENSP00000003084 700 S NA 1377674 Not tested 0 ENSP00000003084 686 S NA 1377674 Not tested 0 ENSP00000003084 813 S NA 1377674 Not tested 0 ENSP00000003084 768 S NA 1377674 Not tested 0 ENSP00000218364 702 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000218364 642 S NA 15345747 Large scale phosphoproteomics 0 ENSP00000218364 624 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000265717 114 S PROBYES 7479855 These data suggest that autophosphorylation and nuclear location signal sequences are integral parts of the growth regulatory mechanism of RII beta 0 ENSP00000244020 314 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000244020 316 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000244020 301 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000264657 727 S YES 9343414,12576423,12763138,9872331,14551213,10446219,10521505,11350938,11335711 Importantly, serine 727 phosphorylation negatively modulates STAT3 tyrosine phosphorylation, which is required for dimer formation, nuclear translocation, and the DNA binding activity of this transcriptional regulator. ERK family of mitogen-activated protein (MAP) kinases, but not JNK or p38 0 ENSP00000165698 152 S NA 15345747 Phosphoproteomics 0 ENSP00000309591 339 S NA 221492,6262777,8395513 Not tested 0 ENSP00000221784 119 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000267064 347 S NA 15345747,15302935 Not tested. Phosphoproteomics. 0 ENSP00000249647 161 S PROBYES 12930825 SNAP-23 mutants that mimic phosphorylation at Ser23/Thr24 inhibited syntaxin 4 interactions, whereas a phosphorylation mutant of Ser161 had only minor effects. Pkc 0 ENSP00000249647 24 T YES 12930825 SNAP-23 mutants that mimic phosphorylation at Ser23/Thr24 inhibited syntaxin 4 interactions, whereas a phosphorylation mutant of Ser161 had only minor effects. Pkc 0 ENSP00000249647 23 S YES 12930825 SNAP-23 mutants that mimic phosphorylation at Ser23/Thr24 inhibited syntaxin 4 interactions, whereas a phosphorylation mutant of Ser161 had only minor effects. Pkc 0 ENSP00000212015 27 S NA 15302935 Phosphoproteomics 0 ENSP00000212015 47 S NA 15302935 Large scale phosphoproteomics Phosphoproteomics 0 ENSP00000219865 208 S NA 15345747 Large scale phosphoproteomics 0 ENSP00000234170 629 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000234170 835 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000260404 560 S NA 14573606 Site not mentioned in abstract. 0 ENSP00000020673 1001 S NA 15345747 Mouse brain phosphoproteomics 0 ENSP00000020673 993 S NA 15345747 Mouse brain phosphoproteomics 0 ENSP00000020673 992 S NA 15345747 Mouse brain phosphoproteomics 0 ENSP00000262320 614 S PROBYES 10581160 Substitutions for one or more of these residues, which lie within a beta-catenin binding site, reduce the ability of Axin to modulate Wnt-induced signaling in a Lef/Tcf reporter assay. These amino acid substitutions also reduce the binding between Axin and beta-catenin 0 ENSP00000241014 421 S NA 12756254 Site not mentioned in abstract 0 ENSP00000241014 197 S NA 12756254 Site not mentioned in abstract 0 ENSP00000241014 205 T NA 12756254 Site not mentioned in abstract 0 ENSP00000241014 103 T NA 12756254 Site not mentioned in abstract 0 ENSP00000241014 284 T NA 12756254 Site not mentioned in abstract 0 ENSP00000241014 341 S NA 12756254 Site not mentioned in abstract 0 ENSP00000241014 29 S NA 12756254 Site not mentioned in abstract 0 ENSP00000241014 15 S NA 12756254 Site not mentioned in abstract 0 ENSP00000356047 466 S YES 1322130,12853467 1322130: Phosphorylation by PKA (S466) decreased the apparent Km of PFK-2 for one of its substrates, fructose 6-phosphate, while phosphorylation by PKC (T475) did not correlate with any change in PFK-2 activity 12853467: 4-3-3 binding was abolished by selectively dephosphorylating Ser483, and 14-3-3 binding was restored when both Ser466 and Ser483 were phosphorylated with PKB 1322130:PKA, 12853467:PKB 0 ENSP00000356047 483 S YES 12853467 12853467: 4-3-3 binding was abolished by selectively dephosphorylating Ser483, and 14-3-3 binding was restored when both Ser466 and Ser483 were phosphorylated with PKB 12853467:PKB 0 ENSP00000356047 475 T NA 1322130 Phosphorylation by PKA (S466) decreased the apparent Km of PFK-2 for one of its substrates, fructose 6-phosphate, while phosphorylation by PKC (T475) did not correlate with any change in PFK-2 activity. This does not mean it has no function though PKC 0 ENSP00000257430 2054 S YES 11050185 Changing a serine residue (Ser(2054)) to aspartic acid mutated the potential protein kinase A site adjacent to NLS2(APC), resulting in both inhibition of the NLS2(APC)-mediated nuclear import of a chimeric beta-galactosidase fusion protein and a reduction of full-length APC nuclear localization. 0 ENSP00000257430 1392 S PROBYES 11487578 Mutation of conserved serine residues in the beta-catenin regulatory motifs of APC interfered with both axin-dependent phosphorylation and phosphorylation by CKIepsilon and impaired the ability of APC to regulate beta-catenin. 0 ENSP00000257430 1279 S PROBYES 11487578 Mutation of conserved serine residues in the beta-catenin regulatory motifs of APC interfered with both axin-dependent phosphorylation and phosphorylation by CKIepsilon and impaired the ability of APC to regulate beta-catenin. 0 ENSP00000268957 152 S YES 12050114 Oncogenic Ras-induced transformation and growth-factor-induced cell proliferation are efficiently suppressed by mutant Tob that carries alanines but not glutamates, mimicking phosphoserines, at these sites. Erk1, Erk2 0 ENSP00000268957 154 S YES 12050114 Oncogenic Ras-induced transformation and growth-factor-induced cell proliferation are efficiently suppressed by mutant Tob that carries alanines but not glutamates, mimicking phosphoserines, at these sites. Erk1, Erk2 0 ENSP00000268957 164 S YES 12050114 Oncogenic Ras-induced transformation and growth-factor-induced cell proliferation are efficiently suppressed by mutant Tob that carries alanines but not glutamates, mimicking phosphoserines, at these sites. Erk1, Erk2 0 ENSP00000239138 203 T PROBYES 12399457 These results therefore suggest that PKA blocks Rho activation by phosphorylation of Galpha(13) Thr(203) Pka 0 ENSP00000225577 252 T YES 9427642,10601311,9271440 Thr252 in the activation loop of the p70 catalytic domain, the phosphorylation of which is stimulated by PI 3-kinase in vivo and is indispensable for p70 activity 0 ENSP00000225577 412 T YES 10601311,9271440 Moreover, once Thr252 was phosphorylated, its ability to cause activation of the p70 S6 kinase was also controlled by the p70 carboxy-terminal tail and by phosphorylation of p70 Ser394, and most importantly, Thr412 0 ENSP00000225577 470 T PROBNOT 9271440 A mutation of T367 or T447 to either alanine or glutamic acid had no apparent effect on p70s6k activity, whereas similar mutations of S371 abolished kinase activity The site does not correspond to the abstract 0 ENSP00000225577 390 T PROBNOT 9271440 A mutation of T367 or T447 to either alanine or glutamic acid had no apparent effect on p70s6k activity, whereas similar mutations of S371 abolished kinase activity The site does not correspond to the abstract 0 ENSP00000225577 394 S YES 12586835,11914378,9271440 Moreover, once Thr252 was phosphorylated, its ability to cause activation of the p70 S6 kinase was also controlled by the p70 carboxy-terminal tail and by phosphorylation of p70 Ser394, and most importantly, Thr412 0 ENSP00000225577 441 S PROBYES 9271440 This might be a good example. Need to check the sources! A mutation of T367 or T447 to either alanine or glutamic acid had no apparent effect on p70s6k activity, whereas similar mutations of S371 abolished kinase activity. 0 ENSP00000225577 434 S NA 12586835,9271440 The site does not correspond to the abstract 0 ENSP00000233154 92 T NA 15345747 Large scale phosphoproteomics 0 ENSP00000233154 90 S NA 15345747 Large scale phosphoproteomics 0 ENSP00000229179 4 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000229179 11 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000229179 64 T NA 16565220 Large scale phosphoproteomics 0 ENSP00000229179 46 T NA 16565220 Large scale phosphoproteomics 0 ENSP00000229179 58 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000229179 55 T NA 16565220 Large scale phosphoproteomics 0 ENSP00000262238 118 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000262238 247 S NA 16565220,15302935 Large scale phosphoproteomics 0 ENSP00000248996 27 S PROBYES 7559455,9166747,8429024 Loss of both serine residues, but not either one alone, impaired the receptor-independent inhibition of adenylyl cyclase by the GTPase-deficient mutant. Maybe be redundant. Primary site of phosphorylation. Pkc 0 ENSP00000248996 16 S NA 7559455,9166747,8429024 Not primary site of phosphorylation Pkc 0 ENSP00000217971 181 S NA 16565220,15302935 Large scale phosphoproteomics 0 ENSP00000217971 57 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000261366 391 S NA 16565220,16083285 Phosphoproteomics 0 ENSP00000261366 395 S NA 8034666 Not tested. 0 ENSP00000261366 393 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000261366 405 S NO 8034666 Not tested. 0 ENSP00000261366 23 S NA 8034666,16565220 Not tested. 0 ENSP00000261366 20 T NA 16565220 Large scale phosphoproteomics 0 ENSP00000260956 362 T PROBNOT 10715123 The analysis of mutants of La, in which the respective phosphorylated residues were replaced by either a neutral (alanine) or an acidic (aspartate) residue, by microinjection into Xenopus laevis oocytes on the one hand and transfection of HEp-2 cells on the other hand revealed that the subcellular distribution of this protein was not affected by these amino acid substitutions. 0 ENSP00000260956 302 T PROBNOT 10715123 The analysis of mutants of La, in which the respective phosphorylated residues were replaced by either a neutral (alanine) or an acidic (aspartate) residue, by microinjection into Xenopus laevis oocytes on the one hand and transfection of HEp-2 cells on the other hand revealed that the subcellular distribution of this protein was not affected by these amino acid substitutions. 0 ENSP00000260956 366 S PROBNOT 10715123 The analysis of mutants of La, in which the respective phosphorylated residues were replaced by either a neutral (alanine) or an acidic (aspartate) residue, by microinjection into Xenopus laevis oocytes on the one hand and transfection of HEp-2 cells on the other hand revealed that the subcellular distribution of this protein was not affected by these amino acid substitutions. 0 ENSP00000260956 325 S PROBNOT 10715123 The analysis of mutants of La, in which the respective phosphorylated residues were replaced by either a neutral (alanine) or an acidic (aspartate) residue, by microinjection into Xenopus laevis oocytes on the one hand and transfection of HEp-2 cells on the other hand revealed that the subcellular distribution of this protein was not affected by these amino acid substitutions. 0 ENSP00000215832 185 T NA 1712480,1378617,91184134 There is a Tyrosine at pos 185, not a Threonine Autoactivation 0 ENSP00000215832 29 S NA 15664191 No mutation 0 ENSP00000215832 41 S NA 1378617 No mutation 0 ENSP00000216714 123 S PROBYES 10023679 Phosphorylation of APE/Ref-1 did not alter the repair activity of the enzyme, whereas it stimulated its redox capability towards AP-1, thus promoting DNA binding activity of AP-1 CK2 0 ENSP00000248437 48 S NA 15345747 Large scale phosphoproteomics 0 ENSP00000211998 1101 S NA 11741957 Site different from abstract PKCalpha 0 ENSP00000211998 1113 S NA 11741957 PKCalpha 0 ENSP00000262053 63 S YES 11018520,9016641,11909979,8663317,8384217 9016641 : Phosphorylation of ATF-1 at Ser63 enhanced its binding to the ATF/CRE site in both the homodimeric and heterodimeric forms 0 ENSP00000262053 36 S NA 9685505 Site not mentioned in abstract. Ck2 0 ENSP00000228136 17 S NA 16094384 Phosphoproteomics 0 ENSP00000227520 18 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000227520 91 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000227520 113 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000227520 110 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000253108 42 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000253108 41 T NA 15345747 Phosphoproteomics 0 ENSP00000258531 50 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000258531 57 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000258531 86 T NA 16565220 Large scale phosphoproteomics 0 ENSP00000222693 36 S PROBYES 12743374 Mutation of the primary phosphorylation sites on caveolin-2, serine 23 and 36, reduces the number of plasmalemma-attached caveolae and increases the accumulation of noncoated vesicles. More than one sites are mutated at the same time. 0 ENSP00000222693 23 S PROBYES 12743374 Mutation of the primary phosphorylation sites on caveolin-2, serine 23 and 36, reduces the number of plasmalemma-attached caveolae and increases the accumulation of noncoated vesicles. More than one sites are mutated at the same time. 0 ENSP00000238647 662 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000238647 657 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000238647 659 S NA 15345747,15302935 Large scale phosphoproteomics 0 ENSP00000227251 59 S NA 12060738 Phosphoproteomics 0 ENSP00000227251 21 S NA 12060738 Phosphoproteomics 0 ENSP00000227251 53 S NA 12060738 Phosphoproteomics 0 ENSP00000227251 45 S NA 12060738 Phosphoproteomics 0 ENSP00000227251 43 S NA 12060738 Phosphoproteomics 0 ENSP00000227251 76 S NA 12060738 Phosphoproteomics 0 ENSP00000227251 19 S NA 12060738 Phosphoproteomics 0 ENSP00000216455 243 S PROBNOT 8619999 The in vitro phosphorylation of the proteasome by CKII does not affect its proteolytic activity CK2 0 ENSP00000216455 250 S NA 12376572,15302935 small scale or phosphoproteomics 0 ENSP00000216520 18 T NA 9074495 Show conservation of the sites But not tested 0 ENSP00000216520 24 S NA 9074495 Show conservation of the sites but not tested 0 ENSP00000238081 232 S PROBYES 16045749,9360956 We have now shown that in vivo phosphorylation of 14-3-3 zeta at the CKIalpha site (Thr-233) negatively regulates its binding to c-Raf, and may be important in Raf-mediated signal transduction 0 ENSP00000267569 148 T NA 11602244,12225289 The precise role of JDP2 phosphorylation on its function is not yet known. Not tested. 0 ENSP00000244050 92 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000262613 290 S NA 15302935,10446210 Not tested. 0 ENSP00000263409 1044 S YES 7777512 Expression in rat H-35 hepatoma cells of LIFR or chimeric granulocyte-colony-stimulating factor receptor (G-CSFR)-LIFR mutants lacking Ser-1044 failed to affect cytokine-stimulated expression of a reporter gene under the control of the beta-fibrinogen gene promoter but eliminated the insulin-induced attenuation of cytokine-stimulated gene expression MAPK 0 ENSP00000258201 367 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000258201 1131 S NA 15051728 Not tested. 0 ENSP00000264033 667 S NA 16094384 Not tested. 0 ENSP00000264033 639 S NA 11024037 Not tested. 0 ENSP00000264033 675 S NA 16094384 Not tested. 0 ENSP00000264033 623 S NA 11024037 Not tested. 0 ENSP00000264033 619 S NA 11024037 Not tested. 0 ENSP00000264033 642 S NA 11024037 Not tested. 0 ENSP00000264033 669 S NA 15144186,12522270 Not tested. 0 ENSP00000245541 368 S YES 16135791 Phosphorylation of GGA3 on S368 causes an increase in the hydrodynamic radius of the protein, indicating a transition to a more asymmetric shape. Mutation of S368 and S372 to a phosphomimic aspartate residue decreases the association of GGA3 with membranes. 0 ENSP00000245541 372 S YES 16135791 Phosphorylation of GGA3 on S368 causes an increase in the hydrodynamic radius of the protein, indicating a transition to a more asymmetric shape. Mutation of S368 and S372 to a phosphomimic aspartate residue decreases the association of GGA3 with membranes 0 ENSP00000252725 21 T YES 14749719 Pak1 phosphorylates p41-Arc on threonine 21 in the first WD repeat, and its mutation has functional implications in vivo. Threonine 21 phosphorylation by Pak1 is required for both constitutive and growth-factor-induced cell motility Pak1 0 ENSP00000259486 210 T YES 8798697 A single amino acid in the phosphodiesterase catalytic site, Thr210, is found to be necessary for motility stimulation, phosphodiesterase activity, and phosphorylation. Two mutant recombinant proteins, Ala210- and Asp210-ATX, lack motility stimulation and lack both enzymatic activities Ser210-ATX possesses intermediate activities 0 ENSP00000263056 413 S NA 12138205 Site not mentioned in abstract 0 ENSP00000263056 400 S YES 12138205 Mutation of S400 in Cot does indeed abolish its ability to activate I kappa B-kinase (IKK) complexes, but paradoxically it allows for increased Cot association with the IKK complex. Pkb 0 ENSP00000231509 203 S PROBYES 12000743 Our results suggest that differentially phosphorylated receptor species are located in unique subcellular compartments, likely modulating distinct aspects of receptor function. 0 ENSP00000231509 141 S NA 2019585,7873448 The site does not correspond to the abstract 0 ENSP00000231509 509 S NA 9038175 The site does not correspond to the abstract. This site occurs adjacent the GR nuclear localization sequence between the DNA and ligand binding domains of GR, and thus its phosphorylation, if confirmed, has the potential to affect receptor function in vivo. 0 ENSP00000231509 226 S YES 9199329,12351702 Furthermore, overexpression of a dominant negative SEK1 mutant also abrogated the effects of UV exposure on GR export. 0 ENSP00000265433 397 S YES 10839545,11252893 Reconstituting NBS cells with a mutant form of Nbs that cannot be phosphorylated at selected, ATM-dependent serine residues led to a specific reduction in clonogenic survival after gamma-radiation. Thus, phosphorylation of Nbs by Atm is critical for certain responses of human cells to DNA damage. 0 ENSP00000265433 278 S PROBYES 10839544 We have identified two residues of NBS1, Ser 278 and Ser 343 that are phosphorylated in vitro by ATM and whose modification in vivo is essential for the cellular response to DNA damage ATM 0 ENSP00000265433 343 S PROBYES 10608806,10839544,10839545,11252893 We have identified two residues of NBS1, Ser 278 and Ser 343 that are phosphorylated in vitro by ATM and whose modification in vivo is essential for the cellular response to DNA damage ATM 0 ENSP00000245923 44 S NA 15345747 Large scale phosphoproteomics 0 ENSP00000244534 147 T NA 15595731 Not tested 0 ENSP00000244534 155 T NA 15595731 Not tested 0 ENSP00000244534 189 S NA 15595731 Not tested 0 ENSP00000244534 180 T NA 15595731 Not tested 0 ENSP00000261182 62 T NA 15345747,16565220 Large scale phosphoproteomics 0 ENSP00000246548 207 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000263980 718 T NA 11604491 Not tested. p38 MAPK 0 ENSP00000263980 693 S NA 15253667 Not tested. 0 ENSP00000263980 770 S NA 15253667 Not tested. 0 ENSP00000263980 729 S NA 11604491 Not tested. p38 MAPK 0 ENSP00000263980 726 S NA 11604491 Not tested. p38 MAPK 0 ENSP00000263980 723 S NA 11604491 Not tested. p38 MAPK 0 ENSP00000263980 779 T NA 15253667 Not tested. 0 ENSP00000263980 766 S NA 15253667 Not tested. 0 ENSP00000263980 785 S NA 15253667 Not tested. 0 ENSP00000156825 24 S NA 12354758 no func assay Aurora-A 0 ENSP00000250535 59 T NA 15302935 Large scale phosphoproteomics 0 ENSP00000222005 13 S YES 15082798,12930845,16330544 In addition, nonphosphorylatable mutants of Cdc37 significantly suppressed the association of Hsp90 with protein kinases Mutation of Ser13 to either Ala or Glu compromises the recruitment of Cdc37 to Hsp90-kinase complexes but has only modest effects on its basal (client-free) binding to Hsp90. Furthermore, Cdc37 containing the complementing Ser to Glu mutation showed altered interactions with Hsp90-kinase complexes consistent with compromised Cdc37 modulation of the Hsp90 ATP-driven reaction cycle Ck2 0 ENSP00000265465 147 S PROBYES 12546699 New phosphorylation-specific antibodies specifically recognize the phosphorylated subunit, p68, of the four subunit DNA polymerase alpha-primase and show that the phosphorylated polypeptide is exclusively nuclear. 0 ENSP00000265465 141 S PROBYES 15302935,12546699 New phosphorylation-specific antibodies specifically recognize the phosphorylated subunit, p68, of the four subunit DNA polymerase alpha-primase and show that the phosphorylated polypeptide is exclusively nuclear. 0 ENSP00000219700 79 S NA 14527438 Not tested 0 ENSP00000264867 266 S NA 11741533 Not mentioned in abstract. 0 ENSP00000264867 263 T NA 11741533 Not mentioned in abstract. 0 ENSP00000264867 299 T NA 11741533 Not mentioned in abstract. 0 ENSP00000176763 438 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000216639 390 T PROBNOT 11883897 The VRK1 protein is autophosphorylated in multiple residues without effect on its activity Autophosphorylation 0 ENSP00000216639 305 T PROBNOT 11883897 The VRK1 protein is autophosphorylated in multiple residues without effect on its activity 0 ENSP00000216639 355 T PROBNOT 11883897 The VRK1 protein is autophosphorylated in multiple residues without effect on its activity 0 ENSP00000265056 26 S NA 16083285 Phosphoproteomics 0 ENSP00000234626 376 T YES 10846177 Replacement of Thr-376, corresponding to the activating threonine of Cdk, with alanine (T376A mutant) dramatically reduces kinase activity 0 ENSP00000220959 327 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000220959 287 S NA 16083285 Large scale phosphoproteomics 0 ENSP00000262643 77 T PROBYES 14536078 And that two additional phosphorylation sites, T62 and S372, are also required for turnover. Sites do not match the abstract. 0 ENSP00000262643 387 S PROBYES 14536078 And that two additional phosphorylation sites, T62 and S372, are also required for turnover. Sites do not match the abstract. 0 ENSP00000262643 395 T YES 8861947,14536078 The following observations indicate that autophosphorylation of CDK2/cyclin E on Thr380 of the cyclin regulates cyclin E destruction: (i) mutation of Thr380 to Ala stabilizes cyclin E in yeast and mammalian cells (ii) cyclin E/CDK2 autophosphorylates on cyclin E in vitro and cyclin E is a phosphoprotein in vivo in mammalian cells (iii) the T380A mutation eliminates phosphorylation on the same site in mammalian cells and in vitro (iv) inhibiting CDK2 activity in vivo stabilizes cyclin E (v) the T380A mutation prevents ubiquitination of cyclin E. Sites do not correspond to abstract. 0 ENSP00000262643 399 S PROBYES 14536078 Cdk2 activity is required for cyclin E turnover in vivo because it phosphorylates S384. Sites do not correspond to abstract. 0 ENSP00000219255 278 S NA 15345747 Large scale phosphoproteomics 0 ENSP00000229390 189 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000253792 447 T NA 10653665 Site not mentioned in abstract. 0 ENSP00000253792 455 S NA 10653665 Site not mentioned in abstract. 0 ENSP00000253792 451 S NA 10653665 Site not mentioned in abstract. 0 ENSP00000228741 363 S NA 11042694 Not tested 0 ENSP00000228741 357 S NA 11042694 Not tested 0 ENSP00000228741 245 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000217381 201 S NA 10212242 Not tested SAPK3 0 ENSP00000217381 193 S NA 10212242 Not tested 0 ENSP00000236996 129 S YES 12162494 Using mutational analysis we show that S129 and S133 are required for EGF-induced transcriptional activity GSK-3beta 0 ENSP00000236996 133 S YES 12235136,9829964,11175347,9687510,11909979,15733869,8688081,8887554,11018520,11160957,11698596 Akt/PKB stimulated target gene expression via CREB in a phospho(Ser-133)-dependent manner PKB 0 ENSP00000219548 23 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000219548 19 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000264160 383 S NA 15570572 Not tested. 0 ENSP00000217159 40 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000262213 365 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000261531 232 S NA 16083285 Phosphoproteomics 0 ENSP00000261531 224 S NA 16083285 Phosphoproteomics 0 ENSP00000269305 6 S 9765199 This is a review paper. 0 ENSP00000269305 371 S YES 9571186 Mutation of serine 371 caused a small decline in p53 activation by PKC alpha and PKC zeta Pkc 0 ENSP00000269305 155 T PROBYES 12628923 CK2 phosphoryl ates Thr155, which targets p53 to degradation by the Ub system. Ck2 0 ENSP00000269305 33 S YES 11483158,11709713,16552184,12064478 Mutation of either serine 33 or serine 37 of p53 to alanine blocked the ability of GSK3beta to regulate p53 transcriptional activity 0 ENSP00000269305 9 S PROBYES 9765199,11875057 p53 C-terminal acetylation at Lys(320) and Lys(382), which may stabilize p53 and activate sequence-specific DNA binding, required Ser(15) phosphorylation by ATM and was enhanced by phosphorylation at nearby residues including Ser(6), Ser(9), and Thr(18) ATM 0 ENSP00000256015 158 T NA 9820826 Site not mentioned in abstract. 0 ENSP00000256015 159 S YES 9820826 In vitro the hCAF-1/BTG1 complex formation was dependent on the phosphorylation of a putative p34cdc2 kinase site on BTG1 (Ser-159). In yeast, the Ala-159 mutant did not interact with hCAF-1. 0 ENSP00000265421 44 S PROBYES 2040602 Amino acid sequence analysis of the phosphopeptides revealed that the phosphorylated sites were 2 serine residues at positions 44 and 55 from the NH2 terminus, either or both of which might be involved in the catalytic activity of DNA polymerase beta Pkc 0 ENSP00000265421 55 S PROBYES 2040602 Amino acid sequence analysis of the phosphopeptides revealed that the phosphorylated sites were 2 serine residues at positions 44 and 55 from the NH2 terminus, either or both of which might be involved in the catalytic activity of DNA polymerase beta 0 ENSP00000254605 171 S NA 16565220 Phosphoproteomics 0 ENSP00000254605 176 S NA 16565220 Phosphoproteomics 0 ENSP00000254605 223 S NA 16565220 Phosphoproteomics 0 ENSP00000254029 96 S NA 15302935 Large scale phosphoproteomics. 0 ENSP00000209728 74 S PROBYES 10339564,9889196 Test three sites simultaneously,Ser-54, Ser-74, and Ser-106, and mutating all three together changes localization in the cell Cdk2 0 ENSP00000209728 106 S PROBYES 10339564 Test three sites simultaneously,Ser-54, Ser-74, and Ser-106, and mutating all three together changes localization in the cell Cdk2 0 ENSP00000209728 54 S PROBYES 10339564,9889196 Test three sites simultaneously,Ser-54, Ser-74, and Ser-106, and mutating all three together changes localization in the cell Cdk2 0 ENSP00000263025 202 T NA 7687743,8626767 Not tested. 0 ENSP00000264670 139 S YES 17215513 In vitro methylation experiments revealed that the Aurora-B-phosphorylation and the phosphorylation-mimic mutation (S139E) suppressed methyltransferase activities of NSUN2 Aurora-B 0 ENSP00000264057 70 S YES 15228384 The aspartate mutation, which mimics phosphoserine, at Ser-22 or Ser-26, inhibited the translocation of full-length DGKdelta1 and the PH domain markedly, suggesting that the phosphorylation regulates negatively the enzyme translocation. Site different from abstract. 0 ENSP00000264057 66 S YES 15228384 The aspartate mutation, which mimics phosphoserine, at Ser-22 or Ser-26, inhibited the translocation of full-length DGKdelta1 and the PH domain markedly, suggesting that the phosphorylation regulates negatively the enzyme translocation. Site different from abstract. 0 ENSP00000234160 225 T NA 11408587 Not tested 0 ENSP00000256442 147 S YES 11242082 A mutant cyclin B1 in which S133 and S147 are replaced by alanines remains in the cytoplasm, whereas wild-type cyclin B1 accumulates in the nucleus during prophase. Polo-like kinase (Plk)-1 0 ENSP00000256442 128 S NA 11242082 Site not mentioned in the abstract. 0 ENSP00000256442 133 S YES 11242082 A mutant cyclin B1 in which S133 and S147 are replaced by alanines remains in the cytoplasm, whereas wild-type cyclin B1 accumulates in the nucleus during prophase. Polo-like kinase (Plk)-1 0 ENSP00000256442 126 S NA 11242082 Site not mentioned in the abstract. 0 ENSP00000248553 83 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000248553 78 S PROBYES 1332886,8774846,7799959 7799959: to determine the role of HSP27 phosphorylation in the heat shock response [...] wild-type HSP27 (HU27 cells) or a nonphosphorylatable form of human HSP27 (HU27pm3 cells) were developed. In contrast to HU27 cells, which showed increased survival after heat shock, HU27pm3 cells showed only slightly enhanced survival. [...] induction of HSP27 phosphorylation by stressing agents or mitogens caused a reduction in the multimeric size of the wild-type protein 1332886:MAPKAP kinase-2, 8774846:MAPKAP kinase-3 0 ENSP00000248553 82 S PROBYES 1332886,8774846,16565220,7799959 7799959: to determine the role of HSP27 phosphorylation in the heat shock response [...] wild-type HSP27 (HU27 cells) or a nonphosphorylatable form of human HSP27 (HU27pm3 cells) were developed. In contrast to HU27 cells, which showed increased survival after heat shock, HU27pm3 cells showed only slightly enhanced survival. [...] induction of HSP27 phosphorylation by stressing agents or mitogens caused a reduction in the multimeric size of the wild-type protein 0 ENSP00000248553 15 S PROBYES 1332886,8774846,16565220,7799959 7799959: to determine the role of HSP27 phosphorylation in the heat shock response [...] wild-type HSP27 (HU27 cells) or a nonphosphorylatable form of human HSP27 (HU27pm3 cells) were developed. In contrast to HU27 cells, which showed increased survival after heat shock, HU27pm3 cells showed only slightly enhanced survival. [...] induction of HSP27 phosphorylation by stressing agents or mitogens caused a reduction in the multimeric size of the wild-type protein 0 ENSP00000195419 1055 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000260363 682 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000260363 912 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000260363 160 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000260363 911 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000260363 684 S NA 16565220,15302935 Large scale phosphoproteomics 0 ENSP00000250615 205 S PROBYES 11336675 Association that is phosphorylation dependent. Site not metioned in abstract. 0 ENSP00000250615 31 T PROBYES 11336675 Association that is phosphorylation dependent. Site not metioned in abstract. 0 ENSP00000226218 69 T PROBYES 9733784 that the double mutant T50E/T57E (in which the neutral Thr residues are replaced by the negatively charged Glu residues considered analogs of Thr-P) ?Need to update site ID? Ck2 0 ENSP00000226218 397 S NA 1706595 The site does not correspond to the abstract Pkc 0 ENSP00000226218 76 T PROBYES 9733784 that the double mutant T50E/T57E (in which the neutral Thr residues are replaced by the negatively charged Glu residues considered analogs of Thr-P) has a significantly enhanced capacity to promote cell adhesion ?Need to change site ID? Ck2 0 ENSP00000226218 381 S YES 9030777 We show that the PKC phosphorylation at Ser362 alters the functional properties of vitronectin, attenuating its cleavage by plasmin at Arg361-Ser362. The site does not correspond to the abstrac Pkc 0 ENSP00000253692 45 T NA 15144186 Phosphoproteomics 0 ENSP00000253692 43 S NA 15144186 Phosphoproteomics 0 ENSP00000253692 44 S NA 15144186 Phosphoproteomics 0 ENSP00000256935 1706 S NA 15144186 Phosphoproteomics 0 ENSP00000256935 1689 T NA 15144186 Phosphoproteomics 0 ENSP00000256935 1688 S NA 15144186 Phosphoproteomics 0 ENSP00000262752 232 S PROBYES 15632195 Constitutive activation appeared to result from constitutive phosphorylation of Ser232, Ser372, and Ser389 0 ENSP00000262752 372 S PROBYES 15632195 Constitutive activation appeared to result from constitutive phosphorylation of Ser232, Ser372, and Ser389 0 ENSP00000262752 389 S PROBYES 15632195 Constitutive activation appeared to result from constitutive phosphorylation of Ser232, Ser372, and Ser389 0 ENSP00000222968 60 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000222968 63 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000251636 200 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000170168 610 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000170168 358 S NA 15302935 Large scale phosphoproteomics 0 ENSP00000215574 231 S PROBYES 11546811 Test five sites simultaneously,Ser-203, Ser-222, Ser-231, Thr-233, and Ser-236, and mutating all five together changes localization in the cell CK2 0 ENSP00000215574 233 T PROBYES 11546811 Test five sites simultaneously,Ser-203, Ser-222, Ser-231, Thr-233, and Ser-236, and mutating all five together changes localization in the cell CK2 0 ENSP00000215574 203 S PROBYES 11546811 Test five sites simultaneously,Ser-203, Ser-222, Ser-231, Thr-233, and Ser-236, and mutating all five together changes localization in the cell CK2 0 ENSP00000215574 236 S PROBYES 11546811 Test five sites simultaneously,Ser-203, Ser-222, Ser-231, Thr-233, and Ser-236, and mutating all five together changes localization in the cell CK2 0 ENSP00000215574 222 S PROBYES 11546811 Test five sites simultaneously,Ser-203, Ser-222, Ser-231, Thr-233, and Ser-236, and mutating all five together changes localization in the cell CK2 0 ENSP00000200135 438 T NA 16565220 Large scale phosphoproteomics 0 ENSP00000239223 359 S PROBYES 10617468 This phosphorylation did not modify MKP-1 s intrinsic ability to dephosphorylate p44(MAPK) but led to stabilization of the protein. Two 0 ENSP00000239223 296 S PROBYES 16286470 The DEF and Ser(296)/Ser(323) sites were essential for ubiquitin-mediated MKP-1 proteolysis stimulated by MKK1-ERK signaling in H293 cells, whereas the N-terminal domain and Ser(359)/Ser(364) sites were dispensable 0 ENSP00000239223 323 S PROBYES 16286470 The DEF and Ser(296)/Ser(323) sites were essential for ubiquitin-mediated MKP-1 proteolysis stimulated by MKK1-ERK signaling in H293 cells, whereas the N-terminal domain and Ser(359)/Ser(364) sites were dispensable 0 ENSP00000239223 364 S PROBYES 10617468 This phosphorylation did not modify MKP-1 s intrinsic ability to dephosphorylate p44(MAPK) but led to stabilization of the protein MAPK 0 ENSP00000256383 52 S PROBYES 16179258,8099443,1677563,10542257,9819435 In the Saccharomyces model system, PEK functionally substituted for the endogenous yeast eIF-2alpha kinase, GCN2, by a process requiring the serine-51 phosphorylation site in eIF-2alpha. Site different from abstract. 0 ENSP00000256383 49 S PROBYES 2116318 Phosphorylation of both sites is required for inhibition of protein synthesis. 0 ENSP00000227507 197 S NA 8058338 Not tested 0 ENSP00000227507 90 S NA 8058338 Not tested 0 ENSP00000227507 286 T YES 10910956,9832503 Recently, it has been shown that phosphorylation of cyclin D1 by glycogen synthase kinase 3beta (GSK-3beta) on a single threonine residue (Thr-286) positively regulates proteosomal degradation of cyclin D1. 0 ENSP00000227507 234 S NA 8058338 Not tested 0 ENSP00000248673 52 S NA 14688255 Not tested 0 ENSP00000248673 60 S NA 14688255 Not tested 0 ENSP00000248673 228 S NA 95286626,7768935 Not tested. Site is different from abstract. MAP kinase 0 ENSP00000248673 186 S NA 14688255 Not tested. Site different from abstract. MK2 0 ENSP00000229328 182 S NA 9305909 Not tested 0 ENSP00000229328 24 S NA 9305909 Not tested 0 ENSP00000229328 108 S NA 9305909 Not tested 0 ENSP00000244289 951 S PROBYES 9417067,14641008 Ser-659 and Ser-660 was necessary to abolish the activation of HSL toward a triolein substrate after phosphorylation with PKA. The site is different from abstract. Pka 0 ENSP00000244289 950 S PROBYES 9417067,14641008 Ser-659 and Ser-660 was necessary to abolish the activation of HSL toward a triolein substrate after phosphorylation with PKA. The site is different from abstract. Pka 0 ENSP00000244289 891 T NA 11581251 Site different from abstract 0 ENSP00000244289 853 S PROBNOT 9417067 Mutation of Ser-563 to alanine did not cause significant change of activation compared with wild-type HSL, The site is different from abstract. Pka 0 ENSP00000244289 565 S NA 16188906 Site different from the abstract Pka 0 ENSP00000244289 855 S NA 9417067 Site different from the abstract 0 ENSP00000256443 170 T YES 11113184 Full activation of CDK7 requires association with a positive regulatory subunit, cyclin H, and phosphorylation of a conserved threonine residue at position 170 in its own T loop. Our results suggest that the primary amino acid sequence of the T loop plays only a minor role, if any, in determining the specificity of cyclin-dependent CAKs for their CDK substrates and that protein-protein interactions involving sequences outside the T loop can influence substrate specificity both positively and negatively. 0 ENSP00000256443 164 S NA 11113184 Not tested. 0 ENSP00000266970 160 T YES 10934208,11532001,14597612,11113184 Full activation of cyclin-dependent kinases (Cdks) requires binding to a cyclin and phosphorylation on an activating site equivalent to Thr160 in Cdk2 by the Cdk-activating kinase 0 ENSP00000266970 14 T YES 12972555,15144186,15302935,12912980,12388094 Inhibition of cyclin-dependent kinases (CDKs) by Thr14/Tyr15 phosphorylation is critical for normal cell cycle progression and is a converging event for several cell cycle checkpoints. 0 ENSP00000262160 240 S NA 11027280 Not tested. 0 ENSP00000262160 250 S NA 10197981 Site not mentioned in abstract. 0 ENSP00000262160 245 S NA 10197981 Site not mentioned in abstract. 0 ENSP00000262160 465 S YES 9346908,9892009 Phosphorylation at both sites is required to mediate association of Smad2 with Smad4 in mammalian cells, while in yeast, Smad2 interacts directly with Smad4 and does not require phosphorylation 0 ENSP00000262160 220 T NA 10197981 Site not mentioned in abstract. 0 ENSP00000262160 464 S NA 9892009 Serine 464 is not a site of phosphorylation, but is important for efficient phosphorylation of Smad2. ##this is not a phosphosite## 0 ENSP00000262160 8 T NA 12193595,11027280 Site not mentioned in abstract. 0 ENSP00000262160 467 S YES 9346908,9892009 Phosphorylation at both sites is required to mediate association of Smad2 with Smad4 in mammalian cells, while in yeast, Smad2 interacts directly with Smad4 and does not require phosphorylation. Mutation of either serine residue 465 or 467 prevents dissociation of Smad2 from activated TbetaRI and blocks TGF-beta-dependent signaling and Smad2 transcriptional activity 0 ENSP00000262160 260 S NA 11027280 Not tested. 0 ENSP00000262160 110 S NA 11027280 Not tested. 0 ENSP00000227378 477 T NA 15302935 Large scale phosphoproteomics 0 ENSP00000218432 44 S PROBYES 12860119 Mutation of Ser19 to Ala abolishes phosphorylation and alters the subcellular localization of hPar14 from predominantly nuclear to significantly cytoplasmic. The site does not correspond to the abstract 0 ENSP00000265354 103 S YES 8413226,10318869,10753652,12171911 hosphorylation of serine 103 significantly enhances the affinity and rate with which SRF associates with its binding site, the serum response element, within the c-fos promoter. 0 ENSP00000265354 83 S YES 2046671,1740119 A mutant that contained glutamate residues in place of these serines had only low-level binding activity however, when the serines were replaced with glutamates and further mutations were made that increased the negative charge of the region, the resulting mutant showed a constitutively high level of binding equal to that achieved by phosphorylation of wild-type SRF Ck2 0 ENSP00000265354 446 S YES 8407951 Amino acid substitutions that interfered with phosphorylation by DNA-PK at Ser-435/446 in GAL4-SRF fusion proteins were reduced in transactivation potency 0 ENSP00000265354 160 T PROBYES 10753652 The location of Thr-160 in the 3-D structure of SRF suggests that its phosphorylation by nuclear CaMKII may directly influence DNA binding of SRF and other MADS box factors. 0 ENSP00000265354 435 S PROBYES 8407951 Amino acid substitutions that interfered with phosphorylation by DNA-PK at Ser-435/446 in GAL4-SRF fusion proteins were reduced in transactivation potency 0 ENSP00000256897 304 S NA 10993082 Site not mentioned in abstract. 0 ENSP00000256897 5 S NA 10993082 Site not mentioned in abstract. 0 ENSP00000172229 303 S NA 12682012 Site different from abstract S303 vs S304 0 ENSP00000262418 42 T NA 1998697 Not tested. 0 ENSP00000262418 50 S NA 1998697 Not tested. 0 ENSP00000262418 39 T NA 1998697 Not tested. 0 ENSP00000262418 49 T NA 1998697 Not tested. 0 ENSP00000262418 44 T NA 1998697 Not tested. 0 ENSP00000262418 29 S NA 1998697 Not tested. 0 ENSP00000262418 48 T NA 1998697 Not tested. 0 ENSP00000262418 54 T NA 1998697 Not tested. 0 ENSP00000240423 605 T NA 16565220 Large scale phosphoproteomics 0 ENSP00000240423 78 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000240423 81 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000240423 92 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000240423 201 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000240423 49 T NA 16565220 Large scale phosphoproteomics 0 ENSP00000240423 335 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000240423 96 S NA 16565220 Large scale phosphoproteomics 0 ENSP00000262735 21 S YES 10187842 However, it is intriguing that the activity of this AF-1 region is modulated by the phosphorylation of two serine residues, both of which must be phosphorylated in order to activate transcription. 0