MEPCE_HUMAN - dbPTM
MEPCE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MEPCE_HUMAN
UniProt AC Q7L2J0
Protein Name 7SK snRNA methylphosphate capping enzyme
Gene Name MEPCE
Organism Homo sapiens (Human).
Sequence Length 689
Subcellular Localization
Protein Description S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA, leading to stabilize it..
Protein Sequence MIEMAAEKEPFLVPAPPPPLKDESGGGGGPTVPPHQEAASGELRGGTERGPGRCAPSAGSPAAAVGRESPGAAATSSSGPQAQQHRGGGPQAQSHGEARLSDPPGRAAPPDVGEERRGGGGTELGPPAPPRPRNGYQPHRPPGGGGGKRRNSCNVGGGGGGFKHPAFKRRRRVNSDCDSVLPSNFLLGGNIFDPLNLNSLLDEEVSRTLNAETPKSSPLPAKGRDPVEILIPKDITDPLSLNTCTDEGHVVLASPLKTGRKRHRHRGQHHQQQQAAGGSESHPVPPTAPLTPLLHGEGASQQPRHRGQNRDAPQPYELNTAINCRDEVVSPLPSALQGPSGSLSAPPAASVISAPPSSSSRHRKRRRTSSKSEAGARGGGQGSKEKGRGSWGGRHHHHHPLPAAGFKKQQRKFQYGNYCKYYGYRNPSCEDGRLRVLKPEWFRGRDVLDLGCNVGHLTLSIACKWGPSRMVGLDIDSRLIHSARQNIRHYLSEELRLPPQTLEGDPGAEGEEGTTTVRKRSCFPASLTASRGPIAAPQVPLDGADTSVFPNNVVFVTGNYVLDRDDLVEAQTPEYDVVLCLSLTKWVHLNWGDEGLKRMFRRIYRHLRPGGILVLEPQPWSSYGKRKTLTETIYKNYYRIQLKPEQFSSYLTSPDVGFSSYELVATPHNTSKGFQRPVYLFHKARSPSH
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
1Acetylation-------MIEMAAEK
-------CCCCCCCC
5.4419413330
21SumoylationPAPPPPLKDESGGGG
CCCCCCCCCCCCCCC
66.28-
57PhosphorylationGPGRCAPSAGSPAAA
CCCCCCCCCCCCCCC
27.0829255136
60PhosphorylationRCAPSAGSPAAAVGR
CCCCCCCCCCCCCCC
15.8729255136
69PhosphorylationAAAVGRESPGAAATS
CCCCCCCCCCCCCCC
27.5529255136
75PhosphorylationESPGAAATSSSGPQA
CCCCCCCCCCCCHHH
25.1523927012
76PhosphorylationSPGAAATSSSGPQAQ
CCCCCCCCCCCHHHH
20.1330278072
77PhosphorylationPGAAATSSSGPQAQQ
CCCCCCCCCCHHHHC
34.6530278072
78PhosphorylationGAAATSSSGPQAQQH
CCCCCCCCCHHHHCC
55.0230278072
86MethylationGPQAQQHRGGGPQAQ
CHHHHCCCCCCCCHH
40.91-
94PhosphorylationGGGPQAQSHGEARLS
CCCCCHHCCCCCCCC
36.1529523821
101PhosphorylationSHGEARLSDPPGRAA
CCCCCCCCCCCCCCC
42.3823401153
117MethylationPDVGEERRGGGGTEL
CCCCCCCCCCCCCCC
51.92-
122PhosphorylationERRGGGGTELGPPAP
CCCCCCCCCCCCCCC
31.1728555341
136PhosphorylationPPRPRNGYQPHRPPG
CCCCCCCCCCCCCCC
23.5527642862
148AcetylationPPGGGGGKRRNSCNV
CCCCCCCCCCCCCCC
52.0025953088
152PhosphorylationGGGKRRNSCNVGGGG
CCCCCCCCCCCCCCC
12.7829255136
158UbiquitinationNSCNVGGGGGGFKHP
CCCCCCCCCCCCCCH
26.1629967540
163UbiquitinationGGGGGGFKHPAFKRR
CCCCCCCCCHHHHCC
52.5329967540
163AcetylationGGGGGGFKHPAFKRR
CCCCCCCCCHHHHCC
52.5325953088
166UbiquitinationGGGFKHPAFKRRRRV
CCCCCCHHHHCCCCC
23.4721890473
175PhosphorylationKRRRRVNSDCDSVLP
HCCCCCCCCCCCCCC
36.4425159151
179PhosphorylationRVNSDCDSVLPSNFL
CCCCCCCCCCCCCCE
31.7025159151
183PhosphorylationDCDSVLPSNFLLGGN
CCCCCCCCCCEECCC
35.7328464451
199PhosphorylationFDPLNLNSLLDEEVS
CCCCCHHHHCCHHHH
33.2122115753
206PhosphorylationSLLDEEVSRTLNAET
HHCCHHHHHHHCCCC
23.8726074081
208PhosphorylationLDEEVSRTLNAETPK
CCHHHHHHHCCCCCC
19.5030266825
213PhosphorylationSRTLNAETPKSSPLP
HHHHCCCCCCCCCCC
33.3419664994
215UbiquitinationTLNAETPKSSPLPAK
HHCCCCCCCCCCCCC
71.6233845483
216PhosphorylationLNAETPKSSPLPAKG
HCCCCCCCCCCCCCC
38.0919664994
217PhosphorylationNAETPKSSPLPAKGR
CCCCCCCCCCCCCCC
36.2622167270
222UbiquitinationKSSPLPAKGRDPVEI
CCCCCCCCCCCCCEE
53.1729967540
233UbiquitinationPVEILIPKDITDPLS
CCEEECCCCCCCCCC
55.5629967540
236PhosphorylationILIPKDITDPLSLNT
EECCCCCCCCCCCCC
41.5223927012
240PhosphorylationKDITDPLSLNTCTDE
CCCCCCCCCCCCCCC
25.5923927012
243PhosphorylationTDPLSLNTCTDEGHV
CCCCCCCCCCCCCCE
23.2923927012
244GlutathionylationDPLSLNTCTDEGHVV
CCCCCCCCCCCCCEE
4.3722555962
245PhosphorylationPLSLNTCTDEGHVVL
CCCCCCCCCCCCEEE
34.7423401153
254PhosphorylationEGHVVLASPLKTGRK
CCCEEEECCCCCCCC
26.9729255136
257UbiquitinationVVLASPLKTGRKRHR
EEEECCCCCCCCHHC
52.9329967540
258PhosphorylationVLASPLKTGRKRHRH
EEECCCCCCCCHHCC
50.3225159151
266MethylationGRKRHRHRGQHHQQQ
CCCHHCCCCHHHHHH
46.56-
279PhosphorylationQQQAAGGSESHPVPP
HHHHCCCCCCCCCCC
34.7023927012
281PhosphorylationQAAGGSESHPVPPTA
HHCCCCCCCCCCCCC
34.4923927012
287PhosphorylationESHPVPPTAPLTPLL
CCCCCCCCCCCCCCC
34.5323401153
291PhosphorylationVPPTAPLTPLLHGEG
CCCCCCCCCCCCCCC
15.7223401153
300PhosphorylationLLHGEGASQQPRHRG
CCCCCCCCCCCCCCC
39.9629255136
304MethylationEGASQQPRHRGQNRD
CCCCCCCCCCCCCCC
28.00-
316PhosphorylationNRDAPQPYELNTAIN
CCCCCCCCCCCCHHC
28.0028796482
330PhosphorylationNCRDEVVSPLPSALQ
CCCCCCCCCCCHHHC
26.3729255136
334PhosphorylationEVVSPLPSALQGPSG
CCCCCCCHHHCCCCC
49.6629255136
340PhosphorylationPSALQGPSGSLSAPP
CHHHCCCCCCCCCCC
48.0829255136
342PhosphorylationALQGPSGSLSAPPAA
HHCCCCCCCCCCCCH
24.4029255136
344PhosphorylationQGPSGSLSAPPAASV
CCCCCCCCCCCCHHH
40.1929255136
350PhosphorylationLSAPPAASVISAPPS
CCCCCCHHHCCCCCC
23.3025850435
353PhosphorylationPPAASVISAPPSSSS
CCCHHHCCCCCCCCH
32.3520873877
357PhosphorylationSVISAPPSSSSRHRK
HHCCCCCCCCHHHHH
41.6220873877
358PhosphorylationVISAPPSSSSRHRKR
HCCCCCCCCHHHHHH
37.8020873877
359PhosphorylationISAPPSSSSRHRKRR
CCCCCCCCHHHHHHH
35.4120873877
360PhosphorylationSAPPSSSSRHRKRRR
CCCCCCCHHHHHHHC
33.7720873877
369PhosphorylationHRKRRRTSSKSEAGA
HHHHHCCCCCHHHCC
33.6828176443
370PhosphorylationRKRRRTSSKSEAGAR
HHHHCCCCCHHHCCC
39.3228176443
372PhosphorylationRRRTSSKSEAGARGG
HHCCCCCHHHCCCCC
34.3328176443
377MethylationSKSEAGARGGGQGSK
CCHHHCCCCCCCCCC
43.29-
384MethylationRGGGQGSKEKGRGSW
CCCCCCCCCCCCCCC
70.98-
390PhosphorylationSKEKGRGSWGGRHHH
CCCCCCCCCCCCCCC
22.6126055452
412AcetylationGFKKQQRKFQYGNYC
CCHHHHHHHHCCCCC
32.2626051181
412UbiquitinationGFKKQQRKFQYGNYC
CCHHHHHHHHCCCCC
32.2629967540
418PhosphorylationRKFQYGNYCKYYGYR
HHHHCCCCCHHCCCC
5.9722817900
438UbiquitinationDGRLRVLKPEWFRGR
CCCEEECCCHHHCCC
37.73-
521PhosphorylationTTTVRKRSCFPASLT
CCEEEECCCCCCCCE
24.1228555341
526PhosphorylationKRSCFPASLTASRGP
ECCCCCCCCEECCCC
26.8728555341
582PhosphorylationYDVVLCLSLTKWVHL
CCEEEEEECCEEECC
32.7524719451
627UbiquitinationWSSYGKRKTLTETIY
CCCCCCCCCHHHHHH
51.9129967540
628PhosphorylationSSYGKRKTLTETIYK
CCCCCCCCHHHHHHH
42.84-
630PhosphorylationYGKRKTLTETIYKNY
CCCCCCHHHHHHHHH
35.9930631047
632PhosphorylationKRKTLTETIYKNYYR
CCCCHHHHHHHHHEE
25.1130631047
635AcetylationTLTETIYKNYYRIQL
CHHHHHHHHHEEEEC
34.3225953088
635UbiquitinationTLTETIYKNYYRIQL
CHHHHHHHHHEEEEC
34.3221890473
635UbiquitinationTLTETIYKNYYRIQL
CHHHHHHHHHEEEEC
34.3221890473
643SumoylationNYYRIQLKPEQFSSY
HHEEEECCHHHHHHH
30.0828112733
661PhosphorylationPDVGFSSYELVATPH
CCCCCCCEEEEECCC
16.4522817900
666PhosphorylationSSYELVATPHNTSKG
CCEEEEECCCCCCCC
20.0125627689
686PhosphorylationYLFHKARSPSH----
EEEECCCCCCC----
35.3020068231
688PhosphorylationFHKARSPSH------
EECCCCCCC------
42.9720068231

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

Oops, there are no upstream regulatory protein records of MEPCE_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MEPCE_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 MEPCE_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
U520_HUMANSNRNP200physical
17643375
CCD87_HUMANCCDC87physical
17643375
TCPD_HUMANCCT4physical
17643375
CDK9_HUMANCDK9physical
17643375
DDX5_HUMANDDX5physical
17643375
FBRL_HUMANFBLphysical
17643375
ROA1_HUMANHNRNPA1physical
17643375
ROA2_HUMANHNRNPA2B1physical
17643375
HNRH1_HUMANHNRNPH1physical
17643375
HNRPK_HUMANHNRNPKphysical
17643375
HNRPR_HUMANHNRNPRphysical
17643375
IF2B1_HUMANIGF2BP1physical
17643375
ILF2_HUMANILF2physical
17643375
IMA1_HUMANKPNA2physical
17643375
IMB1_HUMANKPNB1physical
17643375
LARP7_HUMANLARP7physical
17643375
MET16_HUMANMETTL16physical
17643375
NOP56_HUMANNOP56physical
17643375
PCBP2_HUMANPCBP2physical
17643375
PRPF3_HUMANPRPF3physical
17643375
PRP31_HUMANPRPF31physical
17643375
PRP4_HUMANPRPF4physical
17643375
STPAP_HUMANTUT1physical
17643375
RPAP1_HUMANRPAP1physical
17643375
CNOT9_HUMANRQCD1physical
17643375
RUVB1_HUMANRUVBL1physical
17643375
RUVB2_HUMANRUVBL2physical
17643375
SART3_HUMANSART3physical
17643375
HNRPQ_HUMANSYNCRIPphysical
17643375
PPIH_HUMANPPIHphysical
17643375
IF4A1_HUMANEIF4A1physical
17643375
HNRL1_HUMANHNRNPUL1physical
17643375
TCPB_HUMANCCT2physical
17643375
GTF2I_HUMANGTF2Iphysical
17643375
RFC4_HUMANRFC4physical
17643375
U5S1_HUMANEFTUD2physical
17643375
HEXI1_HUMANHEXIM1physical
17643375
CKAP5_HUMANCKAP5physical
17643375
HNRL2_HUMANHNRNPUL2physical
17643375
RSMB_HUMANSNRPBphysical
17643375
RSMN_HUMANSNRPNphysical
17643375
AN32A_HUMANANP32Aphysical
17643375
GRP78_HUMANHSPA5physical
17643375
YBOX1_HUMANYBX1physical
17643375
NH2L1_HUMANNHP2L1physical
17643375
KINH_HUMANKIF5Bphysical
17643375
SNUT1_HUMANSART1physical
17643375
CCNT1_HUMANCCNT1physical
17643375
LRC40_HUMANLRRC40physical
17643375
LSM2_HUMANLSM2physical
17643375
SRP72_HUMANSRP72physical
17643375
CD11B_HUMANCDK11Bphysical
17643375
AN32B_HUMANANP32Bphysical
17643375
ARI3B_HUMANARID3Bphysical
17643375
LC7L3_HUMANLUC7L3physical
17643375
CSK2B_HUMANCSNK2Bphysical
17643375
S30BP_HUMANSAP30BPphysical
17643375
ROA0_HUMANHNRNPA0physical
17643375
CAND1_HUMANCAND1physical
17643375
LSM4_HUMANLSM4physical
17643375
ACTB_HUMANACTBphysical
17643375
ACTG_HUMANACTG1physical
17643375
TIF1B_HUMANTRIM28physical
17643375
PRP6_HUMANPRPF6physical
17643375
IMA7_HUMANKPNA6physical
17643375
RS4X_HUMANRPS4Xphysical
17643375
IF2B2_HUMANIGF2BP2physical
17643375
ZFR_HUMANZFRphysical
17643375
NTPCR_HUMANNTPCRphysical
17643375
HNRPD_HUMANHNRNPDphysical
17643375
HEXI2_HUMANHEXIM2physical
17643375
HS90B_HUMANHSP90AB1physical
17643375
CCAR2_HUMANCCAR2physical
17643375
ILF3_HUMANILF3physical
17643375
TCPQ_HUMANCCT8physical
17643375
AKA7A_HUMANAKAP7physical
17643375
AKA7G_HUMANAKAP7physical
17643375
SET_HUMANSETphysical
17643375
HSP72_HUMANHSPA2physical
17643375
DDX23_HUMANDDX23physical
17643375
DDX17_HUMANDDX17physical
17643375
DDX42_HUMANDDX42physical
17643375
MATR3_HUMANMATR3physical
17643375
MP2K2_HUMANMAP2K2physical
17643375
TRIPC_HUMANTRIP12physical
17643375
RS2_HUMANRPS2physical
17643375
RBMX_HUMANRBMXphysical
17643375
SMD2_HUMANSNRPD2physical
17643375
RHG23_HUMANARHGAP23physical
17643375
DHX9_HUMANDHX9physical
17643375
IPO5_HUMANIPO5physical
17643375
IF2B3_HUMANIGF2BP3physical
17643375
LC7L2_HUMANLUC7L2physical
17643375
YTHD2_HUMANYTHDF2physical
17643375
IMA5_HUMANKPNA1physical
17643375
SNR27_HUMANSNRNP27physical
17643375
SNUT2_HUMANUSP39physical
17643375
SERA_HUMANPHGDHphysical
17643375
UBE2S_HUMANUBE2Sphysical
17643375
RFC5_HUMANRFC5physical
17643375
PARP1_HUMANPARP1physical
17643375
CPNS1_HUMANCAPNS1physical
17643375
LSM7_HUMANLSM7physical
17643375
RU2A_HUMANSNRPA1physical
17643375
PRP8_HUMANPRPF8physical
17643375
ARHG1_HUMANARHGEF1physical
17643375
RUXG_HUMANSNRPGphysical
17643375
DOCK1_HUMANDOCK1physical
17643375
SF3B2_HUMANSF3B2physical
17643375
RFC3_HUMANRFC3physical
17643375
PCH2_HUMANTRIP13physical
17643375
THOC4_HUMANALYREFphysical
17643375
YBOX3_HUMANYBX3physical
17643375
HNRPC_HUMANHNRNPCphysical
17643375
AN32E_HUMANANP32Ephysical
17643375
HNRH2_HUMANHNRNPH2physical
17643375
SMD3_HUMANSNRPD3physical
17643375
ARF6_HUMANARF6physical
17643375
CSK22_HUMANCSNK2A2physical
17643375
IPO9_HUMANIPO9physical
17643375
MAGD2_HUMANMAGED2physical
17643375
RAGP1_HUMANRANGAP1physical
17643375
IMA4_HUMANKPNA3physical
17643375
1433Z_HUMANYWHAZphysical
17643375
SRP68_HUMANSRP68physical
17643375
KAD2_HUMANAK2physical
17643375
CAPZB_HUMANCAPZBphysical
17643375
EXOS5_HUMANEXOSC5physical
17643375
RLA0_HUMANRPLP0physical
17643375
XPO1_HUMANXPO1physical
17643375
RUXF_HUMANSNRPFphysical
17643375
IMA6_HUMANKPNA5physical
17643375
CCNT2_HUMANCCNT2physical
17643375
U2AF1_HUMANU2AF1physical
17643375
CN166_HUMANC14orf166physical
17643375
LSM3_HUMANLSM3physical
17643375
RS3_HUMANRPS3physical
17643375
TRI26_HUMANTRIM26physical
17643375
BAX_HUMANBAXphysical
17643375
DYN2_HUMANDNM2physical
17643375
MOB1A_HUMANMOB1Aphysical
17643375
ROAA_HUMANHNRNPABphysical
17643375
EXOS2_HUMANEXOSC2physical
17643375
YRDC_HUMANYRDCphysical
17643375
UBC12_HUMANUBE2Mphysical
17643375
SDE2_HUMANSDE2physical
17643375
T2FA_HUMANGTF2F1physical
17643375
TBC15_HUMANTBC1D15physical
17643375
PURA_HUMANPURAphysical
17643375
RL38_HUMANRPL38physical
17643375
UE2NL_HUMANUBE2NLphysical
17643375
KTHY_HUMANDTYMKphysical
17643375
KIF11_HUMANKIF11physical
17643375
SRSF3_HUMANSRSF3physical
17643375
CDC73_HUMANCDC73physical
17643375
RS14_HUMANRPS14physical
17643375
RS9_HUMANRPS9physical
17643375
HSP76_HUMANHSPA6physical
17643375
PRP19_HUMANPRPF19physical
22863883
RUXG_HUMANSNRPGphysical
24778252
BGAL_HUMANGLB1physical
24778252
PRPF3_HUMANPRPF3physical
24778252
RSMB_HUMANSNRPBphysical
24778252
RU2B_HUMANSNRPB2physical
24778252
PPGB_HUMANCTSAphysical
24778252
LARP7_HUMANLARP7physical
24778252
RUXF_HUMANSNRPFphysical
24778252
SART3_HUMANSART3physical
24778252
CHMP3_HUMANCHMP3physical
26186194
ROA1_HUMANHNRNPA1physical
26186194
CHMP3_HUMANCHMP3physical
28514442
ROA1_HUMANHNRNPA1physical
28514442

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 MEPCE_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-60; THR-213; SER-216; SER-217 AND THR-291, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-213; SER-216 ANDSER-254, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-60; THR-213; SER-216; SER-217 AND THR-291, 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-60; SER-69; THR-213;SER-216; SER-217 AND SER-254, 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 SER-57; SER-60; SER-69;SER-101; SER-152; SER-175; SER-216; SER-217; SER-254; SER-330 ANDSER-390, 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-69; SER-175 AND SER-179,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 THR-213 AND SER-217, ANDMASS SPECTROMETRY.
"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-60, 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 SER-69 AND SER-175, AND MASSSPECTROMETRY.
"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-213, 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-661, AND MASSSPECTROMETRY.

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