EHMT2_HUMAN - dbPTM
EHMT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EHMT2_HUMAN
UniProt AC Q96KQ7
Protein Name Histone-lysine N-methyltransferase EHMT2
Gene Name EHMT2
Organism Homo sapiens (Human).
Sequence Length 1210
Subcellular Localization Nucleus . Chromosome . Associates with euchromatic regions. Does not associate with heterochromatin.
Protein Description Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself..
Protein Sequence MAAAAGAAAAAAAEGEAPAEMGALLLEKETRGATERVHGSLGDTPRSEETLPKATPDSLEPAGPSSPASVTVTVGDEGADTPVGATPLIGDESENLEGDGDLRGGRILLGHATKSFPSSPSKGGSCPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAAAAGSEPPPATTSPEGQPKVHRARKTMSKPGNGQPPVPEKRPPEIQHFRMSDDVHSLGKVTSDLAKRRKLNSGGGLSEELGSARRSGEVTLTKGDPGSLEEWETVVGDDFSLYYDSYSVDERVDSDSKSEVEALTEQLSEEEEEEEEEEEEEEEEEEEEEEEEDEESGNQSDRSGSSGRRKAKKKWRKDSPWVKPSRKRRKREPPRAKEPRGVNGVGSSGPSEYMEVPLGSLELPSEGTLSPNHAGVSNDTSSLETERGFEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELSGCNAAILKRETMRPSSRVALMVLCETHRARMVKHHCCPGCGYFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDASEAQEVTIPRGDGVTPPAGTAAPAPPPLSQDVPGRADTSQPSARMRGHGEPRRPPCDPLADTIDSSGPSLTLPNGGCLSAVGLPLGPGREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNAQDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFALQLNRKLRLGVGNRAIRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSRLARLDPHPELLPELGSLPPVNT
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
2Acetylation------MAAAAGAAA
------CHHHHHHHH		19.6722814378
40PhosphorylationATERVHGSLGDTPRS
CCHHCCCCCCCCCCC		17.8225159151
44PhosphorylationVHGSLGDTPRSEETL
CCCCCCCCCCCCCCC		20.8525159151
47PhosphorylationSLGDTPRSEETLPKA
CCCCCCCCCCCCCCC		40.7725159151
50PhosphorylationDTPRSEETLPKATPD
CCCCCCCCCCCCCCC		44.2923403867
55PhosphorylationEETLPKATPDSLEPA
CCCCCCCCCCCCCCC		33.4820068231
58PhosphorylationLPKATPDSLEPAGPS
CCCCCCCCCCCCCCC		35.5230278072
65PhosphorylationSLEPAGPSSPASVTV
CCCCCCCCCCCEEEE		48.3030576142
66PhosphorylationLEPAGPSSPASVTVT
CCCCCCCCCCEEEEE		27.8430576142
69PhosphorylationAGPSSPASVTVTVGD
CCCCCCCEEEEEECC		23.0030278072
71PhosphorylationPSSPASVTVTVGDEG
CCCCCEEEEEECCCC		14.1530576142
73PhosphorylationSPASVTVTVGDEGAD
CCCEEEEEECCCCCC		14.9220068231
81PhosphorylationVGDEGADTPVGATPL
ECCCCCCCCCCCCCC		21.2429496963
86PhosphorylationADTPVGATPLIGDES
CCCCCCCCCCCCCCC		16.8220068231
93PhosphorylationTPLIGDESENLEGDG
CCCCCCCCCCCCCCC		36.2028348404
113PhosphorylationRILLGHATKSFPSSP
EEEEEEEECCCCCCC		22.8827174698
114TrimethylationILLGHATKSFPSSPS
EEEEEEECCCCCCCC		51.38-
114MethylationILLGHATKSFPSSPS
EEEEEEECCCCCCCC		51.38-
115PhosphorylationLLGHATKSFPSSPSK
EEEEEECCCCCCCCC		37.7323403867
118PhosphorylationHATKSFPSSPSKGGS
EEECCCCCCCCCCCC		53.5230266825
119PhosphorylationATKSFPSSPSKGGSC
EECCCCCCCCCCCCC		33.1730266825
121PhosphorylationKSFPSSPSKGGSCPS
CCCCCCCCCCCCCCC		45.9730266825
122MethylationSFPSSPSKGGSCPSR
CCCCCCCCCCCCCCC		71.34-
125PhosphorylationSSPSKGGSCPSRAKM
CCCCCCCCCCCCCCC		31.3626552605
128PhosphorylationSKGGSCPSRAKMSMT
CCCCCCCCCCCCCCC		49.5523312004
131MethylationGSCPSRAKMSMTGAG
CCCCCCCCCCCCCCC		30.33-
133PhosphorylationCPSRAKMSMTGAGKS
CCCCCCCCCCCCCCC		16.7023927012
135PhosphorylationSRAKMSMTGAGKSPP
CCCCCCCCCCCCCCH		19.3023927012
139AcetylationMSMTGAGKSPPSVQS
CCCCCCCCCCHHHHH		60.2925953088
140PhosphorylationSMTGAGKSPPSVQSL
CCCCCCCCCHHHHHH		40.9229255136
140 (in isoform 2)Phosphorylation-40.9218220336
143PhosphorylationGAGKSPPSVQSLAMR
CCCCCCHHHHHHHHH		35.8529255136
146PhosphorylationKSPPSVQSLAMRLLS
CCCHHHHHHHHHHHC		18.8823927012
149SulfoxidationPSVQSLAMRLLSMPG
HHHHHHHHHHHCCCC		3.6321406390
153PhosphorylationSLAMRLLSMPGAQGA
HHHHHHHCCCCCCCH		27.7622199227
165PhosphorylationQGAAAAGSEPPPATT
CCHHHCCCCCCCCCC		42.0530266825
171PhosphorylationGSEPPPATTSPEGQP
CCCCCCCCCCCCCCC		33.3130266825
172PhosphorylationSEPPPATTSPEGQPK
CCCCCCCCCCCCCCC		44.3730266825
173PhosphorylationEPPPATTSPEGQPKV
CCCCCCCCCCCCCCC		19.3230266825
184MethylationQPKVHRARKTMSKPG
CCCCCCCCCCCCCCC		34.63-
185"N6,N6,N6-trimethyllysine"PKVHRARKTMSKPGN
CCCCCCCCCCCCCCC		47.82-
185MethylationPKVHRARKTMSKPGN
CCCCCCCCCCCCCCC		47.8218438403
189MethylationRARKTMSKPGNGQPP
CCCCCCCCCCCCCCC		46.2324129315
211PhosphorylationEIQHFRMSDDVHSLG
CCCEEECCCCHHHHC		26.8020068231
216PhosphorylationRMSDDVHSLGKVTSD
ECCCCHHHHCHHHHH		38.3720068231
219AcetylationDDVHSLGKVTSDLAK
CCHHHHCHHHHHHHH		47.8625953088
219SumoylationDDVHSLGKVTSDLAK
CCHHHHCHHHHHHHH		47.8628112733
221PhosphorylationVHSLGKVTSDLAKRR
HHHHCHHHHHHHHHC		21.7329083192
222PhosphorylationHSLGKVTSDLAKRRK
HHHCHHHHHHHHHCC		33.3529083192
229SumoylationSDLAKRRKLNSGGGL
HHHHHHCCCCCCCCC		56.9328112733
229UbiquitinationSDLAKRRKLNSGGGL
HHHHHHCCCCCCCCC		56.93-
232PhosphorylationAKRRKLNSGGGLSEE
HHHCCCCCCCCCCHH		49.6129255136
232 (in isoform 2)Phosphorylation-49.6118220336
237PhosphorylationLNSGGGLSEELGSAR
CCCCCCCCHHHHCCC		32.0925159151
242PhosphorylationGLSEELGSARRSGEV
CCCHHHHCCCCCCEE		31.0925159151
246PhosphorylationELGSARRSGEVTLTK
HHHCCCCCCEEEEEC		33.4830266825
250PhosphorylationARRSGEVTLTKGDPG
CCCCCEEEEECCCCC		25.1429449344
252PhosphorylationRSGEVTLTKGDPGSL
CCCEEEEECCCCCCH		24.50-
258PhosphorylationLTKGDPGSLEEWETV
EECCCCCCHHHEEEE		37.6922468782
327PhosphorylationEEEEDEESGNQSDRS
HHHHHHHCCCCCCCC		40.7825137130
331PhosphorylationDEESGNQSDRSGSSG
HHHCCCCCCCCCCHH		38.7025137130
336PhosphorylationNQSDRSGSSGRRKAK
CCCCCCCCHHHHHHH		30.7619651622
337PhosphorylationQSDRSGSSGRRKAKK
CCCCCCCHHHHHHHH		39.5825137130
350PhosphorylationKKKWRKDSPWVKPSR
HHHHHCCCCCCCCCH		24.5623927012
356PhosphorylationDSPWVKPSRKRRKRE
CCCCCCCCHHCCCCC		44.7219691289
378 (in isoform 2)Phosphorylation-29.7025159151
379PhosphorylationGVNGVGSSGPSEYME
CCCCCCCCCCHHCEE		49.1219691289
379 (in isoform 2)Phosphorylation-49.1225849741
391PhosphorylationYMEVPLGSLELPSEG
CEEECCCCCCCCCCC		26.7626074081
396PhosphorylationLGSLELPSEGTLSPN
CCCCCCCCCCCCCCC		62.3726074081
399PhosphorylationLELPSEGTLSPNHAG
CCCCCCCCCCCCCCC		21.7326074081
401PhosphorylationLPSEGTLSPNHAGVS
CCCCCCCCCCCCCCC		24.4028387310
408PhosphorylationSPNHAGVSNDTSSLE
CCCCCCCCCCCCCCC		28.2428450419
411PhosphorylationHAGVSNDTSSLETER
CCCCCCCCCCCCCCC		25.1919691289
412PhosphorylationAGVSNDTSSLETERG
CCCCCCCCCCCCCCC		35.4728176443
413PhosphorylationGVSNDTSSLETERGF
CCCCCCCCCCCCCCC		32.1128176443
416PhosphorylationNDTSSLETERGFEEL
CCCCCCCCCCCCCCC		35.9519691289
445MethylationISERAGHKCMATESV
HHHHHCCCEEEECCC		25.45-
468PhosphorylationAAILKRETMRPSSRV
EEHHHHCCCCCCHHH		23.63-
555PhosphorylationIPRGDGVTPPAGTAA
ECCCCCCCCCCCCCC		29.1430266825
560PhosphorylationGVTPPAGTAAPAPPP
CCCCCCCCCCCCCCC		23.0430266825
569PhosphorylationAPAPPPLSQDVPGRA
CCCCCCCCCCCCCCC		30.0617525332
634SumoylationPGREALEKALVIQES
CCHHHHHHHHHHCHH		48.1228112733
634UbiquitinationPGREALEKALVIQES
CCHHHHHHHHHHCHH		48.12-
641PhosphorylationKALVIQESERRKKLR
HHHHHCHHHHHHHCC		21.74-
659UbiquitinationRQLYLSVKQGELQKV
HHHEEEECCHHHHHH		49.57-
685UbiquitinationFQSDQQSKRTPLHAA
CCCCHHHCCCHHHHH		56.82-
747AcetylationRGGCVYSKEEDGSTC
CCCCEEECCCCCCCC		47.6526051181
747UbiquitinationRGGCVYSKEEDGSTC
CCCCEEECCCCCCCC		47.65-
848 (in isoform 2)Ubiquitination-24.7021890473
882UbiquitinationANPELRNKEGDTAWD
CCHHHCCCCCCCCCC		57.55-
882 (in isoform 1)Ubiquitination-57.5521890473
920UbiquitinationNRAIRTEKIICRDVA
CHHHHCEEEEEHHHH		36.44-
998UbiquitinationSIRCWYDKDGRLLQE
EEEEEECCCCCCHHH		46.52-
1013UbiquitinationFNKIEPPLIFECNQA
HHCCCCCEEEEECCC		11.6521890473
1013 (in isoform 2)Ubiquitination-11.6521890473
1047UbiquitinationLQLYRTAKMGWGVRA
HHHHHHHCCCCCEEE		37.0121890473
1047UbiquitinationLQLYRTAKMGWGVRA
HHHHHHHCCCCCEEE		37.01-
1047 (in isoform 1)Ubiquitination-37.0121890473
1084PhosphorylationADVREDDSYLFDLDN
CCCCCCCCEEEECCC		35.7427499020
1085PhosphorylationDVREDDSYLFDLDNK
CCCCCCCEEEECCCC		20.55-
1103PhosphorylationVYCIDARYYGNISRF
EEEEECEEECCHHHH		19.9020860994
1104PhosphorylationYCIDARYYGNISRFI
EEEECEEECCHHHHH		9.7220860994
1108PhosphorylationARYYGNISRFINHLC
CEEECCHHHHHHHHC		25.7420860994
1164UbiquitinationRFWDIKSKYFTCQCG
CCEEECCCEEECCCC		39.11-
1187PhosphorylationEAIALEQSRLARLDP
HHHHHHHHHHHHCCC		21.6429743597
1204PhosphorylationELLPELGSLPPVNT-
HHCHHHCCCCCCCC-		50.7823663014
1210PhosphorylationGSLPPVNT-------
CCCCCCCC-------		39.9721082442
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
211SPhosphorylationKinaseCSNK2A1P68400
GPS
569SPhosphorylationKinaseATMQ13315
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
185KMethylation

18438403
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 EHMT2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRC2B_HUMANPRRC2Bphysical
16189514
LCOR_HUMANC10orf12physical
16189514
THAP7_HUMANTHAP7physical
16189514
KLF12_HUMANKLF12physical
16189514
LNX1_HUMANLNX1physical
16189514
CCD33_HUMANCCDC33physical
16189514
PRDM1_HUMANPRDM1physical
19124609
H14_HUMANHIST1H1Ephysical
19144645
UHRF1_HUMANUHRF1physical
19943104
UHRF1_HUMANUHRF1physical
19056828
CBX1_HUMANCBX1physical
19706462
RELB_HUMANRELBphysical
19690169
DNMT1_HUMANDNMT1physical
17085482
Z512B_HUMANZNF512Bphysical
20211142
MED12_HUMANMED12physical
18691967
EHMT1_MOUSEEhmt1physical
16702210
WIZ_MOUSEWizphysical
16702210
WIZ_HUMANWIZphysical
16702210
CTBP1_HUMANCTBP1physical
16702210
CTBP2_HUMANCTBP2physical
16702210
GFI1B_HUMANGFI1Bphysical
16688220
MED23_HUMANMED23physical
18691967
CDK8_HUMANCDK8physical
18691967
MED6_HUMANMED6physical
18691967
EVI1_HUMANMECOMphysical
18619962
GRIP1_HUMANGRIP1physical
16461774
GFI1_HUMANGFI1physical
16287849
ESCO2_HUMANESCO2physical
18501190
H31_HUMANHIST1H3Aphysical
16185068
EHMT2_HUMANEHMT2physical
17962312
CBX5_HUMANCBX5physical
17962312
CBX1_HUMANCBX1physical
17962312
CBX3_HUMANCBX3physical
17962312
PRDM5_HUMANPRDM5physical
17636019
KDM1B_HUMANKDM1Bphysical
20670891
SMC1A_HUMANSMC1Aphysical
20670891
ESCO1_HUMANESCO1physical
20331966
H31_HUMANHIST1H3Aphysical
20118233
P53_HUMANTP53physical
20118233
PO5F1_HUMANPOU5F1physical
21151833
H31T_HUMANHIST3H3physical
12700765
NR0B2_HUMANNR0B2physical
21566081
SMRCD_HUMANSMARCAD1physical
21549307
UHRF1_HUMANUHRF1physical
22064703
UHRF2_HUMANUHRF2physical
22064703
H32_HUMANHIST2H3Cphysical
22387026
DNM3A_HUMANDNMT3Aphysical
22086334
H32_HUMANHIST2H3Cphysical
21495674
H32_HUMANHIST2H3Cphysical
15269344
CUX1_HUMANCUX1physical
15269344
CASP_HUMANCUX1physical
15269344
MIER1_HUMANMIER1physical
21258344
HDAC2_HUMANHDAC2physical
21258344
WIZ_HUMANWIZphysical
21258344
EHMT1_HUMANEHMT1physical
21258344
CDYL_HUMANCDYLphysical
21258344
REST_HUMANRESTphysical
15200951
CBX5_HUMANCBX5physical
15200951
CBX1_HUMANCBX1physical
15200951
CBX3_HUMANCBX3physical
15200951
CTNA3_HUMANCTNNA3physical
23718855
PRDM1_HUMANPRDM1physical
14985713
H11_HUMANHIST1H1Aphysical
14985713
PML_HUMANPMLphysical
23768491
LCOR_HUMANC10orf12physical
25416956
CHCH2_HUMANCHCHD2physical
25416956
KLF3_HUMANKLF3physical
25416956
F161A_HUMANFAM161Aphysical
25416956
PNCB_HUMANNAPRTphysical
25416956
ZN785_HUMANZNF785physical
25416956
ZBT38_HUMANZBTB38physical
25416956
RD3_HUMANRD3physical
25416956
KAT2B_HUMANKAT2Bphysical
24492005
AB17A_HUMANABHD17Aphysical
21516116
H31_BOVINHIST1H3Cphysical
25420628
DNLI1_HUMANLIG1physical
28803780
DNLI1_MOUSELig1physical
28803780
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 EHMT2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-232, AND MASS SPECTROMETRY.
Methylation
ReferencePubMed
"Protein lysine methyltransferase G9a acts on non-histone targets.";
Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R.,Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.;
Nat. Chem. Biol. 4:344-346(2008).
Cited for: FUNCTION, METHYLATION AT LYS-185, AND MASS SPECTROMETRY.
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 SER-232, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-232, 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 SER-140; SER-173; SER-232;SER-246 AND THR-1210, AND MASS SPECTROMETRY.
"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-140 AND SER-232, ANDMASS 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-246, AND MASSSPECTROMETRY.
"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-569, 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-246, AND MASSSPECTROMETRY.

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