NSD2_HUMAN - dbPTM
NSD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NSD2_HUMAN
UniProt AC O96028
Protein Name Histone-lysine N-methyltransferase NSD2
Gene Name NSD2 {ECO:0000312|HGNC:HGNC:12766}
Organism Homo sapiens (Human).
Sequence Length 1365
Subcellular Localization Nucleus . Chromosome .
Isoform 4: Cytoplasm.
Protein Description Histone methyltransferase with histone H3 'Lys-27' (H3K27me) methyltransferase activity. Isoform 2 may act as a transcription regulator that binds DNA and suppresses IL5 transcription through HDAC recruitment..
Protein Sequence MEFSIKQSPLSVQSVVKCIKMKQAPEILGSANGKTPSCEVNRECSVFLSKAQLSSSLQEGVMQKFNGHDALPFIPADKLKDLTSRVFNGEPGAHDAKLRFESQEMKGIGTPPNTTPIKNGSPEIKLKITKTYMNGKPLFESSICGDSAADVSQSEENGQKPENKARRNRKRSIKYDSLLEQGLVEAALVSKISSPSDKKIPAKKESCPNTGRDKDHLLKYNVGDLVWSKVSGYPWWPCMVSADPLLHSYTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVAFEGEGQFEKLCQESAKQAPTKAEKIKLLKPISGKLRAQWEMGIVQAEEAASMSVEERKAKFTFLYVGDQLHLNPQVAKEAGIAAESLGEMAESSGVSEEAAENPKSVREECIPMKRRRRAKLCSSAETLESHPDIGKSTPQKTAEADPRRGVGSPPGRKKTTVSMPRSRKGDAASQFLVFCQKHRDEVVAEHPDASGEEIEELLRSQWSLLSEKQRARYNTKFALVAPVQAEEDSGNVNGKKRNHTKRIQDPTEDAEAEDTPRKRLRTDKHSLRKRDTITDKTARTSSYKAMEAASSLKSQAATKNLSDACKPLKKRNRASTAASSALGFSKSSSPSASLTENEVSDSPGDEPSESPYESADETQTEVSVSSKKSERGVTAKKEYVCQLCEKPGSLLLCEGPCCGAFHLACLGLSRRPEGRFTCSECASGIHSCFVCKESKTDVKRCVVTQCGKFYHEACVKKYPLTVFESRGFRCPLHSCVSCHASNPSNPRPSKGKMMRCVRCPVAYHSGDACLAAGCSVIASNSIICTAHFTARKGKRHHAHVNVSWCFVCSKGGSLLCCESCPAAFHPDCLNIEMPDGSWFCNDCRAGKKLHFQDIIWVKLGNYRWWPAEVCHPKNVPPNIQKMKHEIGEFPVFFFGSKDYYWTHQARVFPYMEGDRGSRYQGVRGIGRVFKNALQEAEARFREIKLQREARETQESERKPPPYKHIKVNKPYGKVQIYTADISEIPKCNCKPTDENPCGFDSECLNRMLMFECHPQVCPAGEFCQNQCFTKRQYPETKIIKTDGKGWGLVAKRDIRKGEFVNEYVGELIDEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFMNHSCQPNCETLKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTVCRCGASNCSGFLGDRPKTSTTLSSEEKGKKTKKKTRRRRAKGEGKRQSEDECFRCGDGGQLVLCDRKFCTKAYHLSCLGLGKRPFGKWECPWHHCDVCGKPSTSFCHLCPNSFCKEHQDGTAFSCTPDGRSYCCEHDLGAASVRSTKTEKPPPEPGKPKGKRRRRRGWRRVTEGK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
4Phosphorylation----MEFSIKQSPLS
----CCCCCCCCCCC
31.9724719451
8PhosphorylationMEFSIKQSPLSVQSV
CCCCCCCCCCCHHHH
23.8621815630
11PhosphorylationSIKQSPLSVQSVVKC
CCCCCCCCHHHHHHH
22.8422199227
14PhosphorylationQSPLSVQSVVKCIKM
CCCCCHHHHHHHHHH
27.0722199227
17AcetylationLSVQSVVKCIKMKQA
CCHHHHHHHHHHHCC
28.2525953088
30PhosphorylationQAPEILGSANGKTPS
CCCHHHCCCCCCCCC
18.3421815630
34AcetylationILGSANGKTPSCEVN
HHCCCCCCCCCCCCC
58.0025953088
35PhosphorylationLGSANGKTPSCEVNR
HCCCCCCCCCCCCCH
23.1021815630
50UbiquitinationECSVFLSKAQLSSSL
HHEEEEEHHHHCHHH
42.1529967540
54PhosphorylationFLSKAQLSSSLQEGV
EEEHHHHCHHHHHHH
13.0519691289
55PhosphorylationLSKAQLSSSLQEGVM
EEHHHHCHHHHHHHH
43.5919691289
56PhosphorylationSKAQLSSSLQEGVMQ
EHHHHCHHHHHHHHH
30.6025159151
78AcetylationLPFIPADKLKDLTSR
CCCCCHHHHHHHHHH
60.5923749302
78UbiquitinationLPFIPADKLKDLTSR
CCCCCHHHHHHHHHH
60.5929967540
80UbiquitinationFIPADKLKDLTSRVF
CCCHHHHHHHHHHHH
57.3329967540
97UbiquitinationEPGAHDAKLRFESQE
CCCCCCCEEEEECCC
46.3729967540
102PhosphorylationDAKLRFESQEMKGIG
CCEEEEECCCCCCCC
28.8217525332
110PhosphorylationQEMKGIGTPPNTTPI
CCCCCCCCCCCCCCC
33.3829255136
114PhosphorylationGIGTPPNTTPIKNGS
CCCCCCCCCCCCCCC
39.4629255136
115PhosphorylationIGTPPNTTPIKNGSP
CCCCCCCCCCCCCCC
29.6529255136
121PhosphorylationTTPIKNGSPEIKLKI
CCCCCCCCCCCEEEE
28.8423927012
136AcetylationTKTYMNGKPLFESSI
EEEEECCEECEECCC
33.2826051181
154PhosphorylationSAADVSQSEENGQKP
CHHHCCHHHHCCCCH
39.10-
172PhosphorylationARRNRKRSIKYDSLL
HHHHHHHHCHHHHHH
26.8522617229
175PhosphorylationNRKRSIKYDSLLEQG
HHHHHCHHHHHHHCC
14.7521712546
177PhosphorylationKRSIKYDSLLEQGLV
HHHCHHHHHHHCCHH
31.5921712546
190PhosphorylationLVEAALVSKISSPSD
HHHHHHHHHCCCCCC
25.7326074081
191UbiquitinationVEAALVSKISSPSDK
HHHHHHHHCCCCCCC
38.8429967540
193PhosphorylationAALVSKISSPSDKKI
HHHHHHCCCCCCCCC
39.6826074081
194PhosphorylationALVSKISSPSDKKIP
HHHHHCCCCCCCCCC
31.7128985074
196PhosphorylationVSKISSPSDKKIPAK
HHHCCCCCCCCCCCC
65.1026074081
198AcetylationKISSPSDKKIPAKKE
HCCCCCCCCCCCCCC
57.8723749302
220PhosphorylationDKDHLLKYNVGDLVW
CHHHHHHCCCCHHHH
18.30-
231PhosphorylationDLVWSKVSGYPWWPC
HHHHHCCCCCCCCCE
36.0225072903
233PhosphorylationVWSKVSGYPWWPCMV
HHHCCCCCCCCCEEE
6.5425072903
241PhosphorylationPWWPCMVSADPLLHS
CCCCEEEECCHHHHC
10.4825072903
248PhosphorylationSADPLLHSYTKLKGQ
ECCHHHHCHHHCCCC
34.1725072903
249PhosphorylationADPLLHSYTKLKGQK
CCHHHHCHHHCCCCC
9.3525072903
250PhosphorylationDPLLHSYTKLKGQKK
CHHHHCHHHCCCCCC
32.6825072903
266 (in isoform 7)Phosphorylation-7.8030266825
267 (in isoform 7)Phosphorylation-4.9030266825
280O-linked_GlycosylationRAWIFEKSLVAFEGE
EEEEEEEEEEEEECC
22.3730379171
292UbiquitinationEGEGQFEKLCQESAK
ECCCHHHHHHHHHHH
56.7132015554
369PhosphorylationEAGIAAESLGEMAES
HHCCCHHHHHHHHHH
36.6327732954
376PhosphorylationSLGEMAESSGVSEEA
HHHHHHHHCCCCHHH
23.8920068231
377PhosphorylationLGEMAESSGVSEEAA
HHHHHHHCCCCHHHH
34.4222777824
380PhosphorylationMAESSGVSEEAAENP
HHHHCCCCHHHHHCC
32.9922777824
389PhosphorylationEAAENPKSVREECIP
HHHHCCHHHHHHHHC
27.8827251275
398AcetylationREECIPMKRRRRAKL
HHHHHCHHHHHHHHH
37.0825953088
404AcetylationMKRRRRAKLCSSAET
HHHHHHHHHCCCCHH
48.4923749302
407PhosphorylationRRRAKLCSSAETLES
HHHHHHCCCCHHHHH
42.9125159151
408PhosphorylationRRAKLCSSAETLESH
HHHHHCCCCHHHHHC
29.1825159151
411PhosphorylationKLCSSAETLESHPDI
HHCCCCHHHHHCCCC
35.2321712546
414PhosphorylationSSAETLESHPDIGKS
CCCHHHHHCCCCCCC
43.3522167270
420AcetylationESHPDIGKSTPQKTA
HHCCCCCCCCCCCCC
52.0326051181
421PhosphorylationSHPDIGKSTPQKTAE
HCCCCCCCCCCCCCC
39.8623401153
422PhosphorylationHPDIGKSTPQKTAEA
CCCCCCCCCCCCCCC
32.9730266825
437PhosphorylationDPRRGVGSPPGRKKT
CCCCCCCCCCCCCCC
26.0530266825
442UbiquitinationVGSPPGRKKTTVSMP
CCCCCCCCCCEECCC
61.4624816145
443TrimethylationGSPPGRKKTTVSMPR
CCCCCCCCCEECCCC
48.33-
443AcetylationGSPPGRKKTTVSMPR
CCCCCCCCCEECCCC
48.3326051181
443MethylationGSPPGRKKTTVSMPR
CCCCCCCCCEECCCC
48.3323644510
444PhosphorylationSPPGRKKTTVSMPRS
CCCCCCCCEECCCCC
35.1520860994
445PhosphorylationPPGRKKTTVSMPRSR
CCCCCCCEECCCCCC
21.3320860994
447PhosphorylationGRKKTTVSMPRSRKG
CCCCCEECCCCCCCC
22.4520860994
479PhosphorylationVAEHPDASGEEIEEL
HHHCCCCCHHHHHHH
54.86-
481 (in isoform 6)Phosphorylation-53.9920068231
492PhosphorylationELLRSQWSLLSEKQR
HHHHHHHHHHCHHHH
16.2826270265
495PhosphorylationRSQWSLLSEKQRARY
HHHHHHHCHHHHHHH
48.3021815630
497AcetylationQWSLLSEKQRARYNT
HHHHHCHHHHHHHCC
41.5326051181
518PhosphorylationPVQAEEDSGNVNGKK
EEECCCCCCCCCCCC
35.2321815630
524AcetylationDSGNVNGKKRNHTKR
CCCCCCCCCCCCCCC
43.2726051181
536PhosphorylationTKRIQDPTEDAEAED
CCCCCCCCCCCCCCC
55.5823403867
544PhosphorylationEDAEAEDTPRKRLRT
CCCCCCCCCCHHHHC
19.2529255136
551PhosphorylationTPRKRLRTDKHSLRK
CCCHHHHCCHHHHCC
54.7326434776
555PhosphorylationRLRTDKHSLRKRDTI
HHHCCHHHHCCCCCC
35.2926434776
565AcetylationKRDTITDKTARTSSY
CCCCCCCHHHCHHHH
35.1225953088
568UbiquitinationTITDKTARTSSYKAM
CCCCHHHCHHHHHHH
40.1324816145
571PhosphorylationDKTARTSSYKAMEAA
CHHHCHHHHHHHHHH
30.0029214152
573AcetylationTARTSSYKAMEAASS
HHCHHHHHHHHHHHH
43.1125953088
579PhosphorylationYKAMEAASSLKSQAA
HHHHHHHHHHHHHHH
43.1626714015
580PhosphorylationKAMEAASSLKSQAAT
HHHHHHHHHHHHHHH
34.7820068231
582MethylationMEAASSLKSQAATKN
HHHHHHHHHHHHHCC
42.33115978571
582UbiquitinationMEAASSLKSQAATKN
HHHHHHHHHHHHHCC
42.3332015554
583PhosphorylationEAASSLKSQAATKNL
HHHHHHHHHHHHCCH
30.2819413330
587PhosphorylationSLKSQAATKNLSDAC
HHHHHHHHCCHHHHH
24.3919413330
588AcetylationLKSQAATKNLSDACK
HHHHHHHCCHHHHHH
51.6825953088
588MethylationLKSQAATKNLSDACK
HHHHHHHCCHHHHHH
51.68115978579
588UbiquitinationLKSQAATKNLSDACK
HHHHHHHCCHHHHHH
51.68-
591PhosphorylationQAATKNLSDACKPLK
HHHHCCHHHHHHHHH
32.33-
595AcetylationKNLSDACKPLKKRNR
CCHHHHHHHHHHCCH
55.9225953088
604PhosphorylationLKKRNRASTAASSAL
HHHCCHHHHHHHHHH
18.4930266825
605PhosphorylationKKRNRASTAASSALG
HHCCHHHHHHHHHHC
25.8430266825
608PhosphorylationNRASTAASSALGFSK
CHHHHHHHHHHCCCC
17.4330266825
609PhosphorylationRASTAASSALGFSKS
HHHHHHHHHHCCCCC
23.8425850435
614PhosphorylationASSALGFSKSSSPSA
HHHHHCCCCCCCCCC
29.8110470851
615MethylationSSALGFSKSSSPSAS
HHHHCCCCCCCCCCC
52.69115978587
616PhosphorylationSALGFSKSSSPSASL
HHHCCCCCCCCCCCC
34.5519690332
616 (in isoform 3)Phosphorylation-34.5530108239
616 (in isoform 5)Phosphorylation-34.5521955146
617PhosphorylationALGFSKSSSPSASLT
HHCCCCCCCCCCCCC
50.4319690332
617 (in isoform 3)Phosphorylation-50.4330108239
617 (in isoform 5)Phosphorylation-50.4321955146
618PhosphorylationLGFSKSSSPSASLTE
HCCCCCCCCCCCCCC
29.9323663014
618 (in isoform 3)Phosphorylation-29.9330108239
618 (in isoform 5)Phosphorylation-29.9325159151
620PhosphorylationFSKSSSPSASLTENE
CCCCCCCCCCCCCCC
32.2228985074
620 (in isoform 3)Phosphorylation-32.2228387310
620 (in isoform 5)Phosphorylation-32.2230108239
622PhosphorylationKSSSPSASLTENEVS
CCCCCCCCCCCCCCC
39.91-
622 (in isoform 3)Phosphorylation-39.9130108239
622 (in isoform 5)Phosphorylation-39.9130108239
624 (in isoform 3)Phosphorylation-33.9827251275
624 (in isoform 5)Phosphorylation-33.9830108239
633 (in isoform 3)Phosphorylation-56.7327732954
658O-linked_GlycosylationVSVSSKKSERGVTAK
EECCCCCCCCCCCCC
35.9430379171
721AcetylationIHSCFVCKESKTDVK
CEEEEEECCCCCCCC
60.7726051181
737AcetylationCVVTQCGKFYHEACV
EEEEECCHHHHHHHH
50.8326051181
750PhosphorylationCVKKYPLTVFESRGF
HHHHCCEEEEECCCC
20.7428555341
754PhosphorylationYPLTVFESRGFRCPL
CCEEEEECCCCCCCC
26.6628555341
779AcetylationPSNPRPSKGKMMRCV
CCCCCCCCCCCEEEE
66.2919608861
781AcetylationNPRPSKGKMMRCVRC
CCCCCCCCCEEEEEC
33.0119608861
912SumoylationPPNIQKMKHEIGEFP
CCCHHHHHCCCCCCC
45.16-
912SumoylationPPNIQKMKHEIGEFP
CCCHHHHHCCCCCCC
45.16-
992UbiquitinationERKPPPYKHIKVNKP
HCCCCCCCCEECCCC
44.63-
1006PhosphorylationPYGKVQIYTADISEI
CCCEEEEEECCHHHC
4.4527642862
1007PhosphorylationYGKVQIYTADISEIP
CCEEEEEECCHHHCC
21.3430576142
1011PhosphorylationQIYTADISEIPKCNC
EEEECCHHHCCCCCC
29.9830576142
1030PhosphorylationENPCGFDSECLNRML
CCCCCCCHHHHHHHH
28.1330576142
1059AcetylationCQNQCFTKRQYPETK
HCCCCCCCCCCCCCE
19.7726051181
1059UbiquitinationCQNQCFTKRQYPETK
HCCCCCCCCCCCCCE
19.77-
1062PhosphorylationQCFTKRQYPETKIIK
CCCCCCCCCCCEEEE
13.6823403867
1065PhosphorylationTKRQYPETKIIKTDG
CCCCCCCCEEEECCC
24.0423403867
1066UbiquitinationKRQYPETKIIKTDGK
CCCCCCCEEEECCCC
40.5529967540
1069SumoylationYPETKIIKTDGKGWG
CCCCEEEECCCCCCE
44.00-
1069SumoylationYPETKIIKTDGKGWG
CCCCEEEECCCCCCE
44.00-
1070PhosphorylationPETKIIKTDGKGWGL
CCCEEEECCCCCCEE
39.3123403867
1080AcetylationKGWGLVAKRDIRKGE
CCCEEEEECCCCCCC
43.0225953088
1133UbiquitinationRIIDAGPKGNYSRFM
CEECCCCCCCHHHHC
59.89-
1207MethylationGFLGDRPKTSTTLSS
CCCCCCCCCCCCCCH
56.8798666279
1213PhosphorylationPKTSTTLSSEEKGKK
CCCCCCCCHHHHCCC
33.3424732914
1214PhosphorylationKTSTTLSSEEKGKKT
CCCCCCCHHHHCCCC
53.5421815630
1217MethylationTTLSSEEKGKKTKKK
CCCCHHHHCCCCCHH
72.4824129315
1231AcetylationKTRRRRAKGEGKRQS
HHHHHHHCCCCCCCC
56.547479669
1238PhosphorylationKGEGKRQSEDECFRC
CCCCCCCCCCCCEEC
51.5625159151
1272AcetylationLSCLGLGKRPFGKWE
HHHCCCCCCCCCCCC
63.0423749302
1280UbiquitinationRPFGKWECPWHHCDV
CCCCCCCCCCCCCCC
4.2624816145
1316PhosphorylationDGTAFSCTPDGRSYC
CCCCEEECCCCCCEE
24.1825159151
1332PhosphorylationEHDLGAASVRSTKTE
CCCCCCCCCCCCCCC
19.9629396449
1335PhosphorylationLGAASVRSTKTEKPP
CCCCCCCCCCCCCCC
31.9021712546
1338PhosphorylationASVRSTKTEKPPPEP
CCCCCCCCCCCCCCC
49.7022210691
1349UbiquitinationPPEPGKPKGKRRRRR
CCCCCCCCCCCCCCC
79.2424816145

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
102SPhosphorylationKinaseATMQ13315
PSP
172SPhosphorylationKinaseAKT1P31749
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NSD2_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 NSD2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANDR_HUMANARphysical
19481544
HDAC1_HUMANHDAC1physical
16197452
SIN3B_HUMANSIN3Bphysical
16197452
NSD2_HUMANWHSC1physical
18156491
HDAC1_HUMANHDAC1physical
18156491
HDAC2_HUMANHDAC2physical
18156491
SIN3A_HUMANSIN3Aphysical
18156491
HDAC1_HUMANHDAC1physical
18172012
HDAC2_HUMANHDAC2physical
18172012
H32_HUMANHIST2H3Cphysical
21720545
IQGA1_HUMANIQGAP1physical
22028615
TIAM1_HUMANTIAM1physical
22028615
CTNB1_HUMANCTNNB1physical
22028615
MDC1_HUMANMDC1physical
21293379
A4_HUMANAPPphysical
21832049
TIF1B_HUMANTRIM28physical
22972034
HDAC1_HUMANHDAC1physical
22972034
H31T_HUMANHIST3H3physical
23269674
H31_HUMANHIST1H3Aphysical
19481544
ESR1_HUMANESR1physical
24101509
NSD2_HUMANWHSC1physical
24101509
GEMI4_HUMANGEMIN4physical
24923560
GEMI5_HUMANGEMIN5physical
24923560
DDX20_HUMANDDX20physical
24923560
GOGA3_HUMANGOLGA3physical
24923560
MBB1A_HUMANMYBBP1Aphysical
24923560
PLEC_HUMANPLECphysical
24923560
DAPLE_HUMANCCDC88Cphysical
24923560
RL6_HUMANRPL6physical
24923560
RBM10_HUMANRBM10physical
24923560
KPRB_HUMANPRPSAP2physical
24923560
TR150_HUMANTHRAP3physical
24923560
RLA0_HUMANRPLP0physical
24923560
PTN13_HUMANPTPN13physical
24923560
SMN_HUMANSMN1physical
24923560
KIF11_HUMANKIF11physical
24923560
MEP50_HUMANWDR77physical
24923560
MYCB2_HUMANMYCBP2physical
24923560
MAP1B_HUMANMAP1Bphysical
24923560
SK2L2_HUMANSKIV2L2physical
24923560
H31_HUMANHIST1H3Aphysical
25494638
PCNA_HUMANPCNAphysical
26771714

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NSD2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-779 AND LYS-781, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 THR-110; THR-114; SER-121;SER-376 AND THR-544, AND MASS SPECTROMETRY.
"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 THR-110; THR-114; THR-115;SER-121 AND THR-544, AND MASS 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 THR-110; THR-115; SER-121AND THR-544, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND THR-544, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND MASSSPECTROMETRY.
"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-544, AND MASSSPECTROMETRY.

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