| UniProt ID | BAG3_HUMAN | |
|---|---|---|
| UniProt AC | O95817 | |
| Protein Name | BAG family molecular chaperone regulator 3 | |
| Gene Name | BAG3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 575 | |
| Subcellular Localization | Nucleus . Cytoplasm . Colocalizes with HSF1 to the nucleus upon heat stress (PubMed:26159920). | |
| Protein Description | Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. [PubMed: 9873016] | |
| Protein Sequence | MSAATHSPMMQVASGNGDRDPLPPGWEIKIDPQTGWPFFVDHNSRTTTWNDPRVPSEGPKETPSSANGPSREGSRLPPAREGHPVYPQLRPGYIPIPVLHEGAENRQVHPFHVYPQPGMQRFRTEAAAAAPQRSQSPLRGMPETTQPDKQCGQVAAAAAAQPPASHGPERSQSPAASDCSSSSSSASLPSSGRSSLGSHQLPRGYISIPVIHEQNVTRPAAQPSFHQAQKTHYPAQQGEYQTHQPVYHKIQGDDWEPRPLRAASPFRSSVQGASSREGSPARSSTPLHSPSPIRVHTVVDRPQQPMTHRETAPVSQPENKPESKPGPVGPELPPGHIPIQVIRKEVDSKPVSQKPPPPSEKVEVKVPPAPVPCPPPSPGPSAVPSSPKSVATEERAAPSTAPAEATPPKPGEAEAPPKHPGVLKVEAILEKVQGLEQAVDNFEGKKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQKAIDVPGQVQVYELQPSNLEADQPLQAIMEMGAVAADKGKKNAGNAEDPHTETQQPEATAAATSNPSSMTDTPGNPAAP | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSAATHSPM ------CCCCCCCCC | 26.98 | 20068231 | |
| 2 | Phosphorylation | ------MSAATHSPM ------CCCCCCCCC | 26.98 | 22210691 | |
| 5 | Phosphorylation | ---MSAATHSPMMQV ---CCCCCCCCCCCC | 23.70 | 22199227 | |
| 7 | Phosphorylation | -MSAATHSPMMQVAS -CCCCCCCCCCCCCC | 15.33 | 22199227 | |
| 14 | Phosphorylation | SPMMQVASGNGDRDP CCCCCCCCCCCCCCC | 33.65 | 22199227 | |
| 29 | Acetylation | LPPGWEIKIDPQTGW CCCCCEEEECCCCCC | 29.55 | 7706887 | |
| 60 | Ubiquitination | RVPSEGPKETPSSAN CCCCCCCCCCCCCCC | 82.28 | 21963094 | |
| 62 | Phosphorylation | PSEGPKETPSSANGP CCCCCCCCCCCCCCC | 34.30 | 26699800 | |
| 64 | Phosphorylation | EGPKETPSSANGPSR CCCCCCCCCCCCCCC | 49.88 | 26699800 | |
| 65 | Phosphorylation | GPKETPSSANGPSRE CCCCCCCCCCCCCCC | 27.27 | 26699800 | |
| 70 | Phosphorylation | PSSANGPSREGSRLP CCCCCCCCCCCCCCC | 44.34 | 22199227 | |
| 86 | Phosphorylation | AREGHPVYPQLRPGY CCCCCCCCCCCCCCC | 6.96 | 28796482 | |
| 90 | Methylation | HPVYPQLRPGYIPIP CCCCCCCCCCCCCCC | 19.83 | - | |
| 93 | Phosphorylation | YPQLRPGYIPIPVLH CCCCCCCCCCCCEEC | 13.25 | 28796482 | |
| 106 | Methylation | LHEGAENRQVHPFHV ECCCCCCCCCCCEEE | 31.25 | - | |
| 114 | Phosphorylation | QVHPFHVYPQPGMQR CCCCEEECCCCCCHH | 6.38 | 23917254 | |
| 121 | Dimethylation | YPQPGMQRFRTEAAA CCCCCCHHHHHHHHH | 17.70 | - | |
| 121 | Methylation | YPQPGMQRFRTEAAA CCCCCCHHHHHHHHH | 17.70 | - | |
| 123 | Methylation | QPGMQRFRTEAAAAA CCCCHHHHHHHHHHC | 33.57 | - | |
| 124 | O-linked_Glycosylation | PGMQRFRTEAAAAAP CCCHHHHHHHHHHCC | 27.54 | 23301498 | |
| 124 | Phosphorylation | PGMQRFRTEAAAAAP CCCHHHHHHHHHHCC | 27.54 | 28634298 | |
| 133 | Methylation | AAAAAPQRSQSPLRG HHHHCCCCCCCCCCC | 35.29 | - | |
| 134 | Phosphorylation | AAAAPQRSQSPLRGM HHHCCCCCCCCCCCC | 29.75 | 26055452 | |
| 136 | Phosphorylation | AAPQRSQSPLRGMPE HCCCCCCCCCCCCCC | 27.44 | 28355574 | |
| 139 | Methylation | QRSQSPLRGMPETTQ CCCCCCCCCCCCCCC | 42.63 | - | |
| 141 | Sulfoxidation | SQSPLRGMPETTQPD CCCCCCCCCCCCCCC | 1.88 | 30846556 | |
| 144 | O-linked_Glycosylation | PLRGMPETTQPDKQC CCCCCCCCCCCCCHH | 25.51 | 23301498 | |
| 144 | Phosphorylation | PLRGMPETTQPDKQC CCCCCCCCCCCCCHH | 25.51 | 23403867 | |
| 145 | O-linked_Glycosylation | LRGMPETTQPDKQCG CCCCCCCCCCCCHHH | 36.12 | 23301498 | |
| 145 | Phosphorylation | LRGMPETTQPDKQCG CCCCCCCCCCCCHHH | 36.12 | 29496963 | |
| 149 | Ubiquitination | PETTQPDKQCGQVAA CCCCCCCCHHHHHHH | 54.92 | 21963094 | |
| 165 | O-linked_Glycosylation | AAAQPPASHGPERSQ HHCCCCHHHCCCCCC | 34.45 | 23301498 | |
| 165 | Phosphorylation | AAAQPPASHGPERSQ HHCCCCHHHCCCCCC | 34.45 | 26074081 | |
| 171 | Phosphorylation | ASHGPERSQSPAASD HHHCCCCCCCCCCCC | 33.09 | 22167270 | |
| 173 | Phosphorylation | HGPERSQSPAASDCS HCCCCCCCCCCCCCC | 20.11 | 22167270 | |
| 177 | Phosphorylation | RSQSPAASDCSSSSS CCCCCCCCCCCCCCC | 41.05 | 23927012 | |
| 180 | Phosphorylation | SPAASDCSSSSSSAS CCCCCCCCCCCCCCC | 37.94 | 23927012 | |
| 181 | Phosphorylation | PAASDCSSSSSSASL CCCCCCCCCCCCCCC | 40.34 | 23927012 | |
| 182 | O-linked_Glycosylation | AASDCSSSSSSASLP CCCCCCCCCCCCCCC | 20.25 | 23301498 | |
| 182 | Phosphorylation | AASDCSSSSSSASLP CCCCCCCCCCCCCCC | 20.25 | 23927012 | |
| 183 | Phosphorylation | ASDCSSSSSSASLPS CCCCCCCCCCCCCCC | 30.20 | 23927012 | |
| 184 | Phosphorylation | SDCSSSSSSASLPSS CCCCCCCCCCCCCCC | 31.69 | 23927012 | |
| 185 | Phosphorylation | DCSSSSSSASLPSSG CCCCCCCCCCCCCCC | 24.67 | 23927012 | |
| 187 | Phosphorylation | SSSSSSASLPSSGRS CCCCCCCCCCCCCCC | 42.64 | 23927012 | |
| 190 | Phosphorylation | SSSASLPSSGRSSLG CCCCCCCCCCCCCCC | 51.20 | 23927012 | |
| 191 | Phosphorylation | SSASLPSSGRSSLGS CCCCCCCCCCCCCCC | 35.96 | 23927012 | |
| 194 | Phosphorylation | SLPSSGRSSLGSHQL CCCCCCCCCCCCCCC | 33.18 | 22167270 | |
| 195 | Phosphorylation | LPSSGRSSLGSHQLP CCCCCCCCCCCCCCC | 35.07 | 30278072 | |
| 198 | Phosphorylation | SGRSSLGSHQLPRGY CCCCCCCCCCCCCCE | 17.22 | 22617229 | |
| 203 | Methylation | LGSHQLPRGYISIPV CCCCCCCCCEEECEE | 60.17 | - | |
| 205 | Phosphorylation | SHQLPRGYISIPVIH CCCCCCCEEECEEEE | 7.87 | 28796482 | |
| 207 | Phosphorylation | QLPRGYISIPVIHEQ CCCCCEEECEEEECC | 16.62 | 18220336 | |
| 217 | Phosphorylation | VIHEQNVTRPAAQPS EEECCCCCCCCCCCC | 38.18 | 28857561 | |
| 218 | Methylation | IHEQNVTRPAAQPSF EECCCCCCCCCCCCH | 17.99 | - | |
| 224 | Phosphorylation | TRPAAQPSFHQAQKT CCCCCCCCHHHHHHH | 24.23 | 26657352 | |
| 230 | Methylation | PSFHQAQKTHYPAQQ CCHHHHHHHCCCCCC | 40.04 | - | |
| 230 | Ubiquitination | PSFHQAQKTHYPAQQ CCHHHHHHHCCCCCC | 40.04 | 29967540 | |
| 231 | Phosphorylation | SFHQAQKTHYPAQQG CHHHHHHHCCCCCCC | 17.98 | 21945579 | |
| 233 | Phosphorylation | HQAQKTHYPAQQGEY HHHHHHCCCCCCCCC | 12.90 | 21945579 | |
| 240 | Phosphorylation | YPAQQGEYQTHQPVY CCCCCCCCCCCCCCE | 26.07 | 21945579 | |
| 242 | Phosphorylation | AQQGEYQTHQPVYHK CCCCCCCCCCCCEEC | 22.90 | 21945579 | |
| 247 | Phosphorylation | YQTHQPVYHKIQGDD CCCCCCCEECCCCCC | 12.22 | 21945579 | |
| 249 | Ubiquitination | THQPVYHKIQGDDWE CCCCCEECCCCCCCC | 21.02 | 21963094 | |
| 258 | Methylation | QGDDWEPRPLRAASP CCCCCCCCCCCCCCC | 31.22 | - | |
| 261 | Methylation | DWEPRPLRAASPFRS CCCCCCCCCCCCCHH | 30.69 | - | |
| 264 | Phosphorylation | PRPLRAASPFRSSVQ CCCCCCCCCCHHHCC | 24.48 | 22167270 | |
| 267 | Methylation | LRAASPFRSSVQGAS CCCCCCCHHHCCCCC | 31.26 | - | |
| 268 | Phosphorylation | RAASPFRSSVQGASS CCCCCCHHHCCCCCC | 34.93 | 23401153 | |
| 269 | Phosphorylation | AASPFRSSVQGASSR CCCCCHHHCCCCCCC | 17.76 | 26055452 | |
| 274 | Phosphorylation | RSSVQGASSREGSPA HHHCCCCCCCCCCCC | 36.43 | 22167270 | |
| 275 | Phosphorylation | SSVQGASSREGSPAR HHCCCCCCCCCCCCC | 33.54 | 22167270 | |
| 279 | Phosphorylation | GASSREGSPARSSTP CCCCCCCCCCCCCCC | 15.61 | 22167270 | |
| 283 | Phosphorylation | REGSPARSSTPLHSP CCCCCCCCCCCCCCC | 40.44 | 29255136 | |
| 284 | Phosphorylation | EGSPARSSTPLHSPS CCCCCCCCCCCCCCC | 28.61 | 29255136 | |
| 285 | Phosphorylation | GSPARSSTPLHSPSP CCCCCCCCCCCCCCC | 30.99 | 29255136 | |
| 289 | Phosphorylation | RSSTPLHSPSPIRVH CCCCCCCCCCCCEEE | 34.45 | 19664994 | |
| 291 | Phosphorylation | STPLHSPSPIRVHTV CCCCCCCCCCEEEEE | 35.65 | 23927012 | |
| 297 | Phosphorylation | PSPIRVHTVVDRPQQ CCCCEEEEEECCCCC | 21.26 | 23186163 | |
| 307 | Phosphorylation | DRPQQPMTHRETAPV CCCCCCCCCCCCCCC | 25.19 | 28555341 | |
| 315 | Phosphorylation | HRETAPVSQPENKPE CCCCCCCCCCCCCCC | 38.67 | 25159151 | |
| 343 | Ubiquitination | HIPIQVIRKEVDSKP CCCCEEEEEHHCCCC | 30.17 | 17623298 | |
| 344 | Ubiquitination | IPIQVIRKEVDSKPV CCCEEEEEHHCCCCC | 51.47 | 29967540 | |
| 348 | Ubiquitination | VIRKEVDSKPVSQKP EEEEHHCCCCCCCCC | 43.99 | 17623298 | |
| 349 | Acetylation | IRKEVDSKPVSQKPP EEEHHCCCCCCCCCC | 45.00 | 26051181 | |
| 349 | Ubiquitination | IRKEVDSKPVSQKPP EEEHHCCCCCCCCCC | 45.00 | 29967540 | |
| 353 | Ubiquitination | VDSKPVSQKPPPPSE HCCCCCCCCCCCCCC | 63.61 | 17623298 | |
| 354 | Acetylation | DSKPVSQKPPPPSEK CCCCCCCCCCCCCCC | 52.57 | 26051181 | |
| 354 | Ubiquitination | DSKPVSQKPPPPSEK CCCCCCCCCCCCCCC | 52.57 | 17623298 | |
| 359 | Phosphorylation | SQKPPPPSEKVEVKV CCCCCCCCCCCEEEC | 56.68 | 28555341 | |
| 360 | Ubiquitination | QKPPPPSEKVEVKVP CCCCCCCCCCEEECC | 67.88 | 27667366 | |
| 361 | Ubiquitination | KPPPPSEKVEVKVPP CCCCCCCCCEEECCC | 48.29 | 27667366 | |
| 377 | Phosphorylation | PVPCPPPSPGPSAVP CCCCCCCCCCCCCCC | 48.54 | 29255136 | |
| 381 | Phosphorylation | PPPSPGPSAVPSSPK CCCCCCCCCCCCCCC | 48.06 | 29255136 | |
| 385 | Phosphorylation | PGPSAVPSSPKSVAT CCCCCCCCCCCCCCC | 53.31 | 29255136 | |
| 386 | Phosphorylation | GPSAVPSSPKSVATE CCCCCCCCCCCCCCC | 30.22 | 29255136 | |
| 389 | Phosphorylation | AVPSSPKSVATEERA CCCCCCCCCCCCCCC | 21.99 | 30576142 | |
| 392 | Phosphorylation | SSPKSVATEERAAPS CCCCCCCCCCCCCCC | 35.90 | 28464451 | |
| 399 | Phosphorylation | TEERAAPSTAPAEAT CCCCCCCCCCCCCCC | 32.26 | 23403867 | |
| 400 | Phosphorylation | EERAAPSTAPAEATP CCCCCCCCCCCCCCC | 35.28 | 23927012 | |
| 406 | Phosphorylation | STAPAEATPPKPGEA CCCCCCCCCCCCCCC | 31.46 | 29255136 | |
| 444 | Ubiquitination | QAVDNFEGKKTDKKY HHHHHCCCCCCCCHH | 32.40 | 23000965 | |
| 445 | 2-Hydroxyisobutyrylation | AVDNFEGKKTDKKYL HHHHCCCCCCCCHHE | 45.35 | - | |
| 445 | Acetylation | AVDNFEGKKTDKKYL HHHHCCCCCCCCHHE | 45.35 | 24468047 | |
| 445 | Sumoylation | AVDNFEGKKTDKKYL HHHHCCCCCCCCHHE | 45.35 | 25114211 | |
| 445 | Ubiquitination | AVDNFEGKKTDKKYL HHHHCCCCCCCCHHE | 45.35 | 23000965 | |
| 446 | Ubiquitination | VDNFEGKKTDKKYLM HHHCCCCCCCCHHEH | 73.20 | 23000965 | |
| 448 | Ubiquitination | NFEGKKTDKKYLMIE HCCCCCCCCHHEHHH | 55.09 | 23000965 | |
| 449 | Ubiquitination | FEGKKTDKKYLMIEE CCCCCCCCHHEHHHH | 48.85 | 21890473 | |
| 450 | 2-Hydroxyisobutyrylation | EGKKTDKKYLMIEEY CCCCCCCHHEHHHHH | 46.56 | - | |
| 450 | Ubiquitination | EGKKTDKKYLMIEEY CCCCCCCHHEHHHHH | 46.56 | 23000965 | |
| 451 | Phosphorylation | GKKTDKKYLMIEEYL CCCCCCHHEHHHHHH | 13.77 | 21406692 | |
| 457 | Phosphorylation | KYLMIEEYLTKELLA HHEHHHHHHHHHHHH | 13.59 | 21406692 | |
| 459 | Phosphorylation | LMIEEYLTKELLALD EHHHHHHHHHHHHHC | 22.90 | 21406692 | |
| 459 | Ubiquitination | LMIEEYLTKELLALD EHHHHHHHHHHHHHC | 22.90 | 17623298 | |
| 460 | Ubiquitination | MIEEYLTKELLALDS HHHHHHHHHHHHHCC | 43.71 | 17623298 | |
| 485 | Ubiquitination | QARRDGVRKVQTILE HHHHHHHHHHHHHHH | 38.67 | 17623298 | |
| 486 | Ubiquitination | ARRDGVRKVQTILEK HHHHHHHHHHHHHHH | 35.97 | 17623298 | |
| 492 | Ubiquitination | RKVQTILEKLEQKAI HHHHHHHHHHHHHCC | 52.31 | 17623298 | |
| 493 | Ubiquitination | KVQTILEKLEQKAID HHHHHHHHHHHHCCC | 54.61 | 29967540 | |
| 496 | Ubiquitination | TILEKLEQKAIDVPG HHHHHHHHHCCCCCC | 51.41 | 17623298 | |
| 497 | Ubiquitination | ILEKLEQKAIDVPGQ HHHHHHHHCCCCCCC | 37.62 | 17623298 | |
| 508 | Phosphorylation | VPGQVQVYELQPSNL CCCCEEEEECCCCCC | 8.20 | 22817900 | |
| 525 | Sulfoxidation | DQPLQAIMEMGAVAA CCHHHHHHHHHCHHH | 3.04 | 30846556 | |
| 527 | Sulfoxidation | PLQAIMEMGAVAADK HHHHHHHHHCHHHHH | 2.01 | 30846556 | |
| 555 | Phosphorylation | ETQQPEATAAATSNP CCCCHHHHHHHCCCC | 18.37 | 28555341 | |
| 560 | Phosphorylation | EATAAATSNPSSMTD HHHHHHCCCCCCCCC | 41.85 | 24275569 | |
| 563 | Phosphorylation | AAATSNPSSMTDTPG HHHCCCCCCCCCCCC | 36.67 | 28985074 | |
| 564 | Phosphorylation | AATSNPSSMTDTPGN HHCCCCCCCCCCCCC | 27.27 | 24719451 | |
| 566 | Phosphorylation | TSNPSSMTDTPGNPA CCCCCCCCCCCCCCC | 38.37 | 28555341 | |
| 568 | Phosphorylation | NPSSMTDTPGNPAAP CCCCCCCCCCCCCCC | 24.75 | 25627689 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 187 | S | Phosphorylation | Kinase | PRKCD | Q05655 | GPS |
| 285 | T | Phosphorylation | Kinase | MAPK3 | P27361 | GPS |
| 285 | T | Phosphorylation | Kinase | MTOR | P42345 | PSP |
| 289 | S | Phosphorylation | Kinase | MAPK3 | P27361 | GPS |
| 289 | S | Phosphorylation | Kinase | MTOR | P42345 | PSP |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BAG3_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of BAG3_HUMAN !! | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND MASSSPECTROMETRY. | |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-284; THR-285;SER-289; SER-291; SER-377; SER-381; SER-385; SER-386 AND THR-406, ANDMASS SPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-275; SER-279;THR-285; SER-289; SER-291; SER-377; SER-386 AND THR-406, AND MASSSPECTROMETRY. | |
| "Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-173; THR-285;SER-289 AND SER-291, AND MASS SPECTROMETRY. | |
| "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASSSPECTROMETRY. | |
| "Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-136; TYR-240;THR-285 AND SER-289, AND MASS SPECTROMETRY. | |
| "Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND MASSSPECTROMETRY. | |
| "A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-279; THR-285;SER-289 AND SER-291, AND MASS SPECTROMETRY. | |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-285 AND SER-289, ANDMASS SPECTROMETRY. | |
| "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-279 ANDSER-377, AND MASS SPECTROMETRY. | |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-406, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, AND MASSSPECTROMETRY. | |
| "Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-247, AND MASSSPECTROMETRY. | |
