| UniProt ID | A4_HUMAN | |
|---|---|---|
| UniProt AC | P05067 | |
| Protein Name | Amyloid-beta A4 protein | |
| Gene Name | APP | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 770 | |
| Subcellular Localization |
Membrane Single-pass type I membrane protein. Membrane, clathrin-coated pit. Cell surface protein that rapidly becomes internalized via clathrin-coated pits. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to |
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| Protein Description | Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.; Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Amyloid-beta protein 42 is a more effective reductant than amyloid-beta protein 40. Amyloid-beta peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. APP42-beta may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with overexpressed HADH2 leads to oxidative stress and neurotoxicity. Also binds GPC1 in lipid rafts.; Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain.; The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.; N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).. | |
| Protein Sequence | MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN | |
| 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 |
|---|---|---|---|---|---|
| 22 | O-linked_Glycosylation | ARALEVPTDGNAGLL HHHCCCCCCCCCCCC | 62.81 | OGP | |
| 35 | Sulfoxidation | LLAEPQIAMFCGRLN CCCCHHHHHHHCCCC | 4.63 | 29124171 | |
| 60 | Ubiquitination | DSDPSGTKTCIDTKE CCCCCCCCEEEECHH | 44.95 | - | |
| 107 | O-linked_Glycosylation | RGRKQCKTHPHFVIP HCHHHHCCCCCCEEC | 48.55 | 103260791 | |
| 115 | Phosphorylation | HPHFVIPYRCLVGEF CCCCEECHHHHHCCH | 11.66 | - | |
| 178 | Ubiquitination | LLPCGIDKFRGVEFV EEECCCCCCCCCEEE | 34.73 | - | |
| 186 | S-palmitoylation | FRGVEFVCCPLAEES CCCCEEEEEECCCCC | 2.10 | 23825420 | |
| 187 | S-palmitoylation | RGVEFVCCPLAEESD CCCEEEEEECCCCCC | 2.32 | 23825420 | |
| 193 | Phosphorylation | CCPLAEESDNVDSAD EEECCCCCCCCCCCC | 26.45 | 28348404 | |
| 198 | Phosphorylation | EESDNVDSADAEEDD CCCCCCCCCCCCCCC | 24.62 | 8999878 | |
| 206 | Phosphorylation | ADAEEDDSDVWWGGA CCCCCCCCCCCCCCC | 46.51 | 8999878 | |
| 217 | Sulfation | WGGADTDYADGSEDK CCCCCCCCCCCCCCC | 14.53 | - | |
| 235 (in isoform 10) | Phosphorylation | - | 20.56 | - | |
| 236 (in isoform 10) | Phosphorylation | - | 56.49 | - | |
| 239 (in isoform 10) | Phosphorylation | - | 67.33 | - | |
| 262 | Sulfation | EEEAEEPYEEATERT HHHHHCCHHHHHHHC | 29.67 | - | |
| 266 | Phosphorylation | EEPYEEATERTTSIA HCCHHHHHHHCCCEE | 29.31 | 26074081 | |
| 269 | Phosphorylation | YEEATERTTSIATTT HHHHHHHCCCEEEEC | 20.75 | 26074081 | |
| 270 | Phosphorylation | EEATERTTSIATTTT HHHHHHCCCEEEECC | 25.10 | 26074081 | |
| 271 | Phosphorylation | EATERTTSIATTTTT HHHHHCCCEEEECCC | 15.04 | 26074081 | |
| 274 | Phosphorylation | ERTTSIATTTTTTTE HHCCCEEEECCCCCC | 24.01 | 26074081 | |
| 275 | Phosphorylation | RTTSIATTTTTTTES HCCCEEEECCCCCCC | 17.08 | 26074081 | |
| 276 | Phosphorylation | TTSIATTTTTTTESV CCCEEEECCCCCCCH | 20.14 | 26074081 | |
| 277 | Phosphorylation | TSIATTTTTTTESVE CCEEEECCCCCCCHH | 21.76 | 30206219 | |
| 278 | Phosphorylation | SIATTTTTTTESVEE CEEEECCCCCCCHHH | 29.63 | 30206219 | |
| 279 | Phosphorylation | IATTTTTTTESVEEV EEEECCCCCCCHHHH | 26.86 | 30206219 | |
| 280 | Phosphorylation | ATTTTTTTESVEEVV EEECCCCCCCHHHHH | 24.95 | 30206219 | |
| 291 (in isoform 3) | O-linked_Glycosylation | - | 2.95 | OGP | |
| 291 (in isoform 3) | Phosphorylation | - | 2.95 | - | |
| 291 (in isoform 4) | O-linked_Glycosylation | - | 2.95 | 21182826 | |
| 291 (in isoform 4) | Phosphorylation | - | 2.95 | - | |
| 292 (in isoform 3) | O-linked_Glycosylation | - | 37.61 | OGP | |
| 292 (in isoform 3) | Phosphorylation | - | 37.61 | - | |
| 292 (in isoform 4) | O-linked_Glycosylation | - | 37.61 | 21182826 | |
| 292 (in isoform 4) | Phosphorylation | - | 37.61 | - | |
| 295 (in isoform 3) | Phosphorylation | - | 16.56 | - | |
| 295 (in isoform 4) | Phosphorylation | - | 16.56 | - | |
| 336 | Sulfation | NNFDTEEYCMAVCGS CCCCHHHHHHHHHHH | 4.94 | - | |
| 348 | Phosphorylation | CGSAMSQSLLKTTQE HHHHHHHHHHHHCCC | 28.50 | 24719451 | |
| 352 | O-linked_Glycosylation | MSQSLLKTTQEPLAR HHHHHHHHCCCCHHC | 33.41 | 55825033 | |
| 353 | O-linked_Glycosylation | SQSLLKTTQEPLARD HHHHHHHCCCCHHCC | 29.37 | 55825037 | |
| 363 | Ubiquitination | PLARDPVKLPTTAAS CHHCCCCCCCCCCCC | 54.88 | - | |
| 366 | O-linked_Glycosylation | RDPVKLPTTAASTPD CCCCCCCCCCCCCHH | 39.23 | 55829633 | |
| 367 | O-linked_Glycosylation | DPVKLPTTAASTPDA CCCCCCCCCCCCHHH | 20.49 | 28109483 | |
| 370 | O-linked_Glycosylation | KLPTTAASTPDAVDK CCCCCCCCCHHHHHH | 37.70 | 28109497 | |
| 371 | O-linked_Glycosylation | LPTTAASTPDAVDKY CCCCCCCCHHHHHHH | 22.06 | 55829651 | |
| 378 | Phosphorylation | TPDAVDKYLETPGDE CHHHHHHHCCCCCCC | 12.81 | - | |
| 381 | O-linked_Glycosylation | AVDKYLETPGDENEH HHHHHCCCCCCCCHH | 29.94 | 72268553 | |
| 381 | Phosphorylation | AVDKYLETPGDENEH HHHHHCCCCCCCCHH | 29.94 | 25159151 | |
| 393 | Ubiquitination | NEHAHFQKAKERLEA CHHHHHHHHHHHHHH | 61.56 | - | |
| 429 | Ubiquitination | NLPKADKKAVIQHFQ CCCHHHHHHHHHHHH | 48.73 | - | |
| 441 | Phosphorylation | HFQEKVESLEQEAAN HHHHHHHHHHHHHHH | 39.95 | 19664994 | |
| 468 | Methylation | VEAMLNDRRRLALEN HHHHHHHHHHHHHHH | 25.25 | - | |
| 495 | 2-Hydroxyisobutyrylation | RHVFNMLKKYVRAEQ HHHHHHHHHHHHHHH | 31.15 | - | |
| 497 | Phosphorylation | VFNMLKKYVRAEQKD HHHHHHHHHHHHHHH | 8.12 | 26091039 | |
| 542 | N-linked_Glycosylation | RVIYERMNQSLSLLY HHHHHHHHHHHHHHH | 34.21 | 16335952 | |
| 571 | N-linked_Glycosylation | ELLQKEQNYSDDVLA HHHHHHCCCCHHHHH | 39.09 | UniProtKB CARBOHYD | |
| 572 | Phosphorylation | LLQKEQNYSDDVLAN HHHHHCCCCHHHHHH | 17.11 | 25072903 | |
| 573 | Phosphorylation | LQKEQNYSDDVLANM HHHHCCCCHHHHHHH | 34.58 | 25072903 | |
| 576 (in isoform 4) | O-linked_Glycosylation | - | 6.98 | 21182826 | |
| 582 | Phosphorylation | DVLANMISEPRISYG HHHHHHHCCCCCCCC | 30.68 | 25072903 | |
| 587 | Phosphorylation | MISEPRISYGNDALM HHCCCCCCCCCCCCC | 28.41 | 25072903 | |
| 587 (in isoform 4) | Sumoylation | - | 28.41 | - | |
| 588 | Phosphorylation | ISEPRISYGNDALMP HCCCCCCCCCCCCCC | 19.99 | 25072903 | |
| 595 (in isoform 4) | Sumoylation | - | 27.34 | - | |
| 596 | Phosphorylation | GNDALMPSLTETKTT CCCCCCCCCCCCCCE | 33.68 | 25072903 | |
| 598 | Phosphorylation | DALMPSLTETKTTVE CCCCCCCCCCCCEEE | 46.04 | 25072903 | |
| 600 | O-linked_Glycosylation | LMPSLTETKTTVELL CCCCCCCCCCEEEEE | 28.58 | 55827585 | |
| 600 | Phosphorylation | LMPSLTETKTTVELL CCCCCCCCCCEEEEE | 28.58 | 25072903 | |
| 614 | O-linked_Glycosylation | LPVNGEFSLDDLQPW EEECCEECHHHCCCC | 26.96 | UniProtKB CARBOHYD | |
| 620 (in isoform 10) | Ubiquitination | - | 37.74 | 21890473 | |
| 623 | O-linked_Glycosylation | DDLQPWHSFGADSVP HHCCCCHHCCCCCCC | 22.85 | UniProtKB CARBOHYD | |
| 628 | O-linked_Glycosylation | WHSFGADSVPANTEN CHHCCCCCCCCCCCC | 29.48 | UniProtKB CARBOHYD | |
| 632 (in isoform 10) | Ubiquitination | - | 41.68 | 21890473 | |
| 633 | O-linked_Glycosylation | ADSVPANTENEVEPV CCCCCCCCCCCCCCC | 42.15 | 22576872 | |
| 651 | O-linked_Glycosylation | PAADRGLTTRPGSGL CCHHCCCCCCCCCCC | 24.47 | 22576872 | |
| 652 | O-linked_Glycosylation | AADRGLTTRPGSGLT CHHCCCCCCCCCCCC | 39.65 | 22576872 | |
| 656 | O-linked_Glycosylation | GLTTRPGSGLTNIKT CCCCCCCCCCCCCCH | 33.06 | 55827957 | |
| 658 (in isoform 3) | Ubiquitination | - | 3.38 | 21890473 | |
| 659 | O-linked_Glycosylation | TRPGSGLTNIKTEEI CCCCCCCCCCCHHHC | 38.12 | 22576872 | |
| 662 | Sumoylation | GSGLTNIKTEEISEV CCCCCCCCHHHCCEE | 52.53 | - | |
| 663 | O-linked_Glycosylation | SGLTNIKTEEISEVK CCCCCCCHHHCCEEE | 34.74 | 22576872 | |
| 667 | O-linked_Glycosylation | NIKTEEISEVKMDAE CCCHHHCCEEECCEE | 39.35 | 55827565 | |
| 670 | Sumoylation | TEEISEVKMDAEFRH HHHCCEEECCEEECC | 27.32 | - | |
| 670 | Sumoylation | TEEISEVKMDAEFRH HHHCCEEECCEEECC | 27.32 | - | |
| 670 (in isoform 3) | Ubiquitination | - | 27.32 | 21890473 | |
| 676 (in isoform 4) | Neddylation | - | 24.98 | - | |
| 676 (in isoform 4) | Ubiquitination | - | 24.98 | 21890473 | |
| 677 (in isoform 5) | Ubiquitination | - | 38.62 | 21890473 | |
| 679 | O-linked_Glycosylation | DAEFRHDSGYEVHHQ CEEECCCCCCCEEEE | 36.83 | UniProtKB CARBOHYD | |
| 679 | Phosphorylation | DAEFRHDSGYEVHHQ CEEECCCCCCCEEEE | 36.83 | 22267728 | |
| 681 | O-linked_Glycosylation | EFRHDSGYEVHHQKL EECCCCCCCEEEEEE | 20.80 | 22576872 | |
| 688 (in isoform 4) | Neddylation | - | 3.06 | - | |
| 688 (in isoform 4) | Ubiquitination | - | 3.06 | 21890473 | |
| 689 (in isoform 5) | Ubiquitination | - | 4.83 | 21890473 | |
| 695 (in isoform 6) | Ubiquitination | - | 7.34 | 21890473 | |
| 697 | O-linked_Glycosylation | FFAEDVGSNKGAIIG EEEECCCCCCCHHHH | 34.91 | UniProtKB CARBOHYD | |
| 697 | Phosphorylation | FFAEDVGSNKGAIIG EEEECCCCCCCHHHH | 34.91 | - | |
| 707 (in isoform 6) | Ubiquitination | - | 7.89 | 21890473 | |
| 714 (in isoform 7) | Ubiquitination | - | 10.31 | 21890473 | |
| 724 | Acetylation | VITLVMLKKKQYTSI HHHHHHHCCCCCCCC | 39.57 | 30586977 | |
| 725 | Acetylation | ITLVMLKKKQYTSIH HHHHHHCCCCCCCCC | 40.94 | 30586971 | |
| 726 (in isoform 7) | Ubiquitination | - | 47.12 | 21890473 | |
| 727 | Ubiquitination | LVMLKKKQYTSIHHG HHHHCCCCCCCCCCC | 56.46 | 21890473 | |
| 728 | Phosphorylation | VMLKKKQYTSIHHGV HHHCCCCCCCCCCCE | 16.01 | - | |
| 729 | Phosphorylation | MLKKKQYTSIHHGVV HHCCCCCCCCCCCEE | 20.79 | 17634293 | |
| 730 | Phosphorylation | LKKKQYTSIHHGVVE HCCCCCCCCCCCEEE | 18.26 | 22817900 | |
| 732 (in isoform 8) | Ubiquitination | - | 16.06 | 21890473 | |
| 733 (in isoform 9) | Ubiquitination | - | 29.13 | 21890473 | |
| 739 | Ubiquitination | HHGVVEVDAAVTPEE CCCEEEECCCCCHHH | 18.46 | 21890473 | |
| 743 | Phosphorylation | VEVDAAVTPEERHLS EEECCCCCHHHHHHH | 21.91 | 15178331 | |
| 744 (in isoform 8) | Ubiquitination | - | 34.55 | 21890473 | |
| 745 (in isoform 9) | Ubiquitination | - | 59.29 | 21890473 | |
| 751 | Ubiquitination | PEERHLSKMQQNGYE HHHHHHHHHHHCCCC | 47.27 | 21890473 | |
| 751 (in isoform 1) | Ubiquitination | - | 47.27 | 21890473 | |
| 757 | Phosphorylation | SKMQQNGYENPTYKF HHHHHCCCCCCHHHH | 21.78 | 25159151 | |
| 761 | Phosphorylation | QNGYENPTYKFFEQM HCCCCCCHHHHHHHH | 51.42 | 21945579 | |
| 762 | Phosphorylation | NGYENPTYKFFEQMQ CCCCCCHHHHHHHHC | 13.68 | 21945579 | |
| 763 | Ubiquitination | GYENPTYKFFEQMQN CCCCCHHHHHHHHCC | 46.16 | 21890473 | |
| 763 (in isoform 1) | Ubiquitination | - | 46.16 | 21890473 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 198 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 206 | S | Phosphorylation | Kinase | CK1 | - | Uniprot |
| 441 | S | Phosphorylation | Kinase | FAM20C | Q8IXL6 | Uniprot |
| 654 | T | Phosphorylation | Kinase | ROCK2 | O75116 | PSP |
| 668 | T | Phosphorylation | Kinase | CDK5 | Q00535 | PSP |
| 668 | T | Phosphorylation | Kinase | CDK5 | Q03114 | PSP |
| 668 | T | Phosphorylation | Kinase | MAPK8 | P45983 | GPS |
| 668 | T | Phosphorylation | Kinase | MAPK9 | P45984 | GPS |
| 668 | T | Phosphorylation | Kinase | MAPK10 | P53779 | GPS |
| 668 | T | Phosphorylation | Kinase | MAPK10 | P53779 | GPS |
| 679 | S | Phosphorylation | Kinase | PKACA | P17612 | PSP |
| 682 | Y | Phosphorylation | Kinase | ABL1 | P00520 | GPS |
| 730 | S | Phosphorylation | Kinase | APP-KINASE I | - | Uniprot |
| 743 | T | Phosphorylation | Kinase | LRRK2 | Q5S007 | PSP |
| 743 | T | Phosphorylation | Kinase | MAPK10 | P53779 | Uniprot |
| 743 | T | Phosphorylation | Kinase | GSK3B | P49841 | PhosphoELM |
| 743 | T | Phosphorylation | Kinase | CDK5 | Q00535 | Uniprot |
| 743 | T | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
| 757 | Y | Phosphorylation | Kinase | FYN | P06241 | PSP |
| - | K | Ubiquitination | E3 ubiquitin ligase | SYVN1 | Q86TM6 | PMID:20237263 |
| - | K | Ubiquitination | E3 ubiquitin ligase | FBXL2 | Q9UKC9 | PMID:22399757 |
* 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 A4_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| H00056 | Alzheimer's disease (AD) | |||||
| H01185 | Cerebral amyloid angiopathy (CAA); Hereditary cerebral hemorrhage with amyloidosis | |||||
| OMIM Disease | ||||||
| 104300 | Alzheimer disease 1 (AD1) | |||||
| 605714 | Cerebral amyloid angiopathy, APP-related (CAA-APP) | |||||
| Kegg Drug | ||||||
| D10231 | Flutemetamol F18 (USAN) | |||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-542, AND MASSSPECTROMETRY. | |
| O-linked Glycosylation | |
| Reference | PubMed |
| "Site-specific characterization of threonine, serine, and tyrosineglycosylations of amyloid precursor protein/amyloid beta-peptides inhuman cerebrospinal fluid."; Halim A., Brinkmalm G., Ruetschi U., Westman-Brinkmalm A.,Portelius E., Zetterberg H., Blennow K., Larson G., Nilsson J.; Proc. Natl. Acad. Sci. U.S.A. 108:11848-11853(2011). Cited for: GLYCOSYLATION AT THR-633; THR-651; THR-652; SER-656; THR-663 ANDSER-667 PROTEOLYTIC PROCESSING, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Tyrosine phosphorylation of the beta-amyloid precursor proteincytoplasmic tail promotes interaction with Shc."; Tarr P.E., Roncarati R., Pelicci G., Pelicci P.G., D'Adamio L.; J. Biol. Chem. 277:16798-16804(2002). Cited for: PHOSPHORYLATION AT TYROSINE RESIDUES, INTERACTION WITH SHC1, ANDMUTAGENESIS OF THR-743 AND TYR-757. | |
| "Cell cycle-dependent regulation of the phosphorylation and metabolismof the Alzheimer amyloid precursor protein."; Suzuki T., Oishi M., Marshak D.R., Czernik A.J., Nairn A.C.,Greengard P.; EMBO J. 13:1114-1122(1994). Cited for: PHOSPHORYLATION AT THR-743. | |
| "An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-757, AND MASSSPECTROMETRY. | |
| "Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-757 AND TYR-762, ANDMASS SPECTROMETRY. | |
