VIR_HUMAN - dbPTM
VIR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VIR_HUMAN
UniProt AC Q69YN4
Protein Name Protein virilizer homolog {ECO:0000305}
Gene Name VIRMA {ECO:0000312|HGNC:HGNC:24500}
Organism Homo sapiens (Human).
Sequence Length 1812
Subcellular Localization Nucleus speckle . Nucleus, nucleoplasm . Cytoplasm . Mainly nuclear with some fraction located in the cytoplasm. ZC3H13 is required to anchor component of the MACOM subcomplex, such as VIRMA, in the nucleus.
Protein Description Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. [PubMed: 24981863]
Protein Sequence MAVDSAMELLFLDTFKHPSAEQSSHIDVVRFPCVVYINEVRVIPPGVRAHSSLPDNRAYGETSPHTFQLDLFFNNVSKPSAPVFDRLGSLEYDENTSIIFRPNSKVNTDGLVLRGWYNCLTLAIYGSVDRVISHDRDSPPPPPPPPPPPQPQPSLKRNPKHADGEKEDQFNGSPPRPQPRGPRTPPGPPPPDDDEDDPVPLPVSGDKEEDAPHREDYFEPISPDRNSVPQEGQYSDEGEVEEEQQEEGEEDEDDVDVEEEEDEDEDDRRTVDSIPEEEEEDEEEEGEEDEEGEGDDGYEQISSDEDGIADLERETFKYPNFDVEYTAEDLASVPPMTYDPYDRELVPLLYFSCPYKTTFEIEISRMKDQGPDKENSGAIEASVKLTELLDLYREDRGAKWVTALEEIPSLIIKGLSYLQLKNTKQDSLGQLVDWTMQALNLQVALRQPIALNVRQLKAGTKLVSSLAECGAQGVTGLLQAGVISGLFELLFADHVSSSLKLNAFKALDSVISMTEGMEAFLRGRQNEKSGYQKLLELILLDQTVRVVTAGSAILQKCHFYEVLSEIKRLGDHLAEKTSSLPNHSEPDHDTDAGLERTNPEYENEVEASMDMDLLESSNISEGEIERLINLLEEVFHLMETAPHTMIQQPVKSFPTMARITGPPERDDPYPVLFRYLHSHHFLELVTLLLSIPVTSAHPGVLQATKDVLKFLAQSQKGLLFFMSEYEATNLLIRALCHFYDQDEEEGLQSDGVIDDAFALWLQDSTQTLQCITELFSHFQRCTASEETDHSDLLGTLHNLYLITFNPVGRSAVGHVFSLEKNLQSLITLMEYYSKEALGDSKSKKSVAYNYACILILVVVQSSSDVQMLEQHAASLLKLCKADENNAKLQELGKWLEPLKNLRFEINCIPNLIEYVKQNIDNLMTPEGVGLTTALRVLCNVACPPPPVEGQQKDLKWNLAVIQLFSAEGMDTFIRVLQKLNSILTQPWRLHVNMGTTLHRVTTISMARCTLTLLKTMLTELLRGGSFEFKDMRVPSALVTLHMLLCSIPLSGRLDSDEQKIQNDIIDILLTFTQGVNEKLTISEETLANNTWSLMLKEVLSSILKVPEGFFSGLILLSELLPLPLPMQTTQVIEPHDISVALNTRKLWSMHLHVQAKLLQEIVRSFSGTTCQPIQHMLRRICVQLCDLASPTALLIMRTVLDLIVEDLQSTSEDKEKQYTSQTTRLLALLDALASHKACKLAILHLINGTIKGDERYAEIFQDLLALVRSPGDSVIRQQCVEYVTSILQSLCDQDIALILPSSSEGSISELEQLSNSLPNKELMTSICDCLLATLANSESSYNCLLTCVRTMMFLAEHDYGLFHLKSSLRKNSSALHSLLKRVVSTFSKDTGELASSFLEFMRQILNSDTIGCCGDDNGLMEVEGAHTSRTMSINAAELKQLLQSKEESPENLFLELEKLVLEHSKDDDNLDSLLDSVVGLKQMLESSGDPLPLSDQDVEPVLSAPESLQNLFNNRTAYVLADVMDDQLKSMWFTPFQAEEIDTDLDLVKVDLIELSEKCCSDFDLHSELERSFLSEPSSPGRTKTTKGFKLGKHKHETFITSSGKSEYIEPAKRAHVVPPPRGRGRGGFGQGIRPHDIFRQRKQNTSRPPSMHVDDFVAAESKEVVPQDGIPPPKRPLKVSQKISSRGGFSGNRGGRGAFHSQNRFFTPPASKGNYSRREGTRGSSWSAQNTPRGNYNESRGGQSNFNRGPLPPLRPLSSTGYRPSPRDRASRGRGGLGPSWASANSGSGGSRGKFVSGGSGRGRHVRSFTR
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------MAVDSAMEL
------CCHHHHHHH
25.7319413330
5Phosphorylation---MAVDSAMELLFL
---CCHHHHHHHHHH
23.9426852163
14PhosphorylationMELLFLDTFKHPSAE
HHHHHHHCCCCCCHH
36.4126852163
16UbiquitinationLLFLDTFKHPSAEQS
HHHHHCCCCCCHHHC
57.6133845483
36PhosphorylationVRFPCVVYINEVRVI
EEECEEEEECEEEEC
4.2419664994
36 (in isoform 1)Phosphorylation-4.24-
38UbiquitinationFPCVVYINEVRVIPP
ECEEEEECEEEECCC
24.8322817900
59PhosphorylationSLPDNRAYGETSPHT
CCCCCCCCCCCCCCE
16.5622617229
62PhosphorylationDNRAYGETSPHTFQL
CCCCCCCCCCCEEEE
43.1028450419
63PhosphorylationNRAYGETSPHTFQLD
CCCCCCCCCCEEEEE
15.4728450419
64UbiquitinationRAYGETSPHTFQLDL
CCCCCCCCCEEEEEE
37.6523503661
66PhosphorylationYGETSPHTFQLDLFF
CCCCCCCEEEEEEEE
19.2328450419
89PhosphorylationPVFDRLGSLEYDENT
CCCCCCCCEECCCCC
23.71-
97PhosphorylationLEYDENTSIIFRPNS
EECCCCCEEEECCCC
25.85-
104PhosphorylationSIIFRPNSKVNTDGL
EEEECCCCCCCCCCE
40.4320068231
105UbiquitinationIIFRPNSKVNTDGLV
EEECCCCCCCCCCEE
46.2621906983
105 (in isoform 2)Ubiquitination-46.2621890473
105 (in isoform 1)Ubiquitination-46.2621890473
105 (in isoform 3)Ubiquitination-46.2621890473
105 (in isoform 4)Ubiquitination-46.2621890473
108PhosphorylationRPNSKVNTDGLVLRG
CCCCCCCCCCEEECH
34.1420068231
108 (in isoform 1)Phosphorylation-34.14-
133PhosphorylationGSVDRVISHDRDSPP
CCCCCHHCCCCCCCC
19.2429255136
133 (in isoform 1)Phosphorylation-19.24-
138PhosphorylationVISHDRDSPPPPPPP
HHCCCCCCCCCCCCC
39.9529255136
138 (in isoform 1)Phosphorylation-39.95-
154PhosphorylationPPPQPQPSLKRNPKH
CCCCCCCCCCCCCCC
41.0723927012
166AcetylationPKHADGEKEDQFNGS
CCCCCCCCCCCCCCC
72.6091089
173PhosphorylationKEDQFNGSPPRPQPR
CCCCCCCCCCCCCCC
32.6029255136
173 (in isoform 1)Phosphorylation-32.60-
184PhosphorylationPQPRGPRTPPGPPPP
CCCCCCCCCCCCCCC
36.6529255136
184 (in isoform 1)Phosphorylation-36.65-
193UbiquitinationPGPPPPDDDEDDPVP
CCCCCCCCCCCCCCC
67.9627667366
204PhosphorylationDPVPLPVSGDKEEDA
CCCCCCCCCCCCCCC
39.0623927012
217PhosphorylationDAPHREDYFEPISPD
CCCCCCCCCCCCCCC
12.7023927012
222PhosphorylationEDYFEPISPDRNSVP
CCCCCCCCCCCCCCC
31.3119664994
222 (in isoform 1)Phosphorylation-31.31-
235PhosphorylationVPQEGQYSDEGEVEE
CCCCCCCCCCCCCCH
22.6918452278
235 (in isoform 1)Phosphorylation-22.69-
241UbiquitinationYSDEGEVEEEQQEEG
CCCCCCCCHHHHHCC
52.0621963094
302PhosphorylationDDGYEQISSDEDGIA
CCCCHHCCCCCCCHH
31.2818452278
302 (in isoform 1)Phosphorylation-31.28-
303PhosphorylationDGYEQISSDEDGIAD
CCCHHCCCCCCCHHH
46.8018452278
303 (in isoform 1)Phosphorylation-46.80-
315PhosphorylationIADLERETFKYPNFD
HHHHHHHHCCCCCCC
31.4828787133
355PhosphorylationLLYFSCPYKTTFEIE
EEEEECCCCEEEEEE
25.87-
357PhosphorylationYFSCPYKTTFEIEIS
EEECCCCEEEEEEEE
30.76-
367UbiquitinationEIEISRMKDQGPDKE
EEEEECCHHCCCCCC
45.87-
373UbiquitinationMKDQGPDKENSGAIE
CHHCCCCCCCCCHHH
63.0321906983
373AcetylationMKDQGPDKENSGAIE
CHHCCCCCCCCCHHH
63.0325953088
373 (in isoform 1)Ubiquitination-63.0321890473
373 (in isoform 2)Ubiquitination-63.0321890473
373 (in isoform 3)Ubiquitination-63.0321890473
373 (in isoform 4)Ubiquitination-63.0321890473
399UbiquitinationYREDRGAKWVTALEE
HHHCCCCCHHHHHHH
45.0523503661
399 (in isoform 2)Ubiquitination-45.05-
402PhosphorylationDRGAKWVTALEEIPS
CCCCCHHHHHHHCHH
25.1420068231
409PhosphorylationTALEEIPSLIIKGLS
HHHHHCHHHHHHHCC
37.5520068231
416PhosphorylationSLIIKGLSYLQLKNT
HHHHHHCCCEEECCC
32.25-
506UbiquitinationLKLNAFKALDSVISM
CCHHHHHHHHHHHHH
15.3327667366
528UbiquitinationLRGRQNEKSGYQKLL
HHHCCCCCCHHHHHH
57.6527667366
552UbiquitinationRVVTAGSAILQKCHF
EEEECCHHHHHHCCH
12.9522817900
556UbiquitinationAGSAILQKCHFYEVL
CCHHHHHHCCHHHHH
26.65-
558UbiquitinationSAILQKCHFYEVLSE
HHHHHHCCHHHHHHH
35.0521963094
564UbiquitinationCHFYEVLSEIKRLGD
CCHHHHHHHHHHHHH
42.3121890473
576UbiquitinationLGDHLAEKTSSLPNH
HHHHHHHHCCCCCCC
48.3721906983
576 (in isoform 2)Ubiquitination-48.3721890473
576 (in isoform 1)Ubiquitination-48.3721890473
576 (in isoform 3)Ubiquitination-48.3721890473
576 (in isoform 4)Ubiquitination-48.3721890473
584PhosphorylationTSSLPNHSEPDHDTD
CCCCCCCCCCCCCCC
58.4225849741
590PhosphorylationHSEPDHDTDAGLERT
CCCCCCCCCCCCCCC
25.08-
660PhosphorylationFPTMARITGPPERDD
CCCCCCCCCCCCCCC
37.7721712546
694UbiquitinationLLLSIPVTSAHPGVL
HHHHCCCCCCCCCHH
18.1622817900
841UbiquitinationKEALGDSKSKKSVAY
HHHHCCCCCCHHHHH
71.6627667366
843AcetylationALGDSKSKKSVAYNY
HHCCCCCCHHHHHHH
53.457707055
874PhosphorylationMLEQHAASLLKLCKA
HHHHHHHHHHHHHHC
34.7124719451
880UbiquitinationASLLKLCKADENNAK
HHHHHHHHCCCCCHH
70.1233845483
887UbiquitinationKADENNAKLQELGKW
HCCCCCHHHHHHHHH
53.4821906983
887AcetylationKADENNAKLQELGKW
HCCCCCHHHHHHHHH
53.4825953088
887 (in isoform 1)Ubiquitination-53.4821890473
887 (in isoform 2)Ubiquitination-53.4821890473
887 (in isoform 3)Ubiquitination-53.4821890473
887 (in isoform 4)Ubiquitination-53.4821890473
893UbiquitinationAKLQELGKWLEPLKN
HHHHHHHHHHHHHHH
62.3221963094
899UbiquitinationGKWLEPLKNLRFEIN
HHHHHHHHHCCEEEE
65.7321890473
899 (in isoform 1)Ubiquitination-65.7321890473
899 (in isoform 2)Ubiquitination-65.7321890473
899 (in isoform 3)Ubiquitination-65.7321890473
899 (in isoform 4)Ubiquitination-65.7321890473
914PhosphorylationCIPNLIEYVKQNIDN
CHHHHHHHHHHHHHH
13.1222817900
924PhosphorylationQNIDNLMTPEGVGLT
HHHHHCCCCCCCCHH
22.73-
981PhosphorylationRVLQKLNSILTQPWR
HHHHHHHHHHHCCEE
29.4320068231
1029UbiquitinationRGGSFEFKDMRVPSA
CCCCCCCCCCCCCHH
43.3422817900
1029 (in isoform 1)Ubiquitination-43.3421890473
1029 (in isoform 2)Ubiquitination-43.3421890473
1029 (in isoform 3)Ubiquitination-43.3421890473
1029 (in isoform 4)Ubiquitination-43.3421890473
1080PhosphorylationQGVNEKLTISEETLA
CCCCCCCCCCHHHHH
33.26-
1100PhosphorylationLMLKEVLSSILKVPE
HHHHHHHHHHHCCCC
22.1021406692
1101PhosphorylationMLKEVLSSILKVPEG
HHHHHHHHHHCCCCC
27.9824719451
1252UbiquitinationLINGTIKGDERYAEI
HHCCCCCCCHHHHHH
37.8527667366
1377PhosphorylationKNSSALHSLLKRVVS
CCHHHHHHHHHHHHH
35.9324719451
1380UbiquitinationSALHSLLKRVVSTFS
HHHHHHHHHHHHHHC
48.7329967540
1430PhosphorylationEGAHTSRTMSINAAE
ECCCCCCCEECCHHH
18.2923403867
1432PhosphorylationAHTSRTMSINAAELK
CCCCCCEECCHHHHH
16.4523403867
1444PhosphorylationELKQLLQSKEESPEN
HHHHHHHCCCCCCCH
41.8423186163
1445UbiquitinationLKQLLQSKEESPENL
HHHHHHCCCCCCCHH
53.1729967540
1448PhosphorylationLLQSKEESPENLFLE
HHHCCCCCCCHHHHH
38.3127732954
1458UbiquitinationNLFLELEKLVLEHSK
HHHHHHHHHHHHCCC
57.4229967540
1464PhosphorylationEKLVLEHSKDDDNLD
HHHHHHCCCCCCCHH
28.5320068231
1465UbiquitinationKLVLEHSKDDDNLDS
HHHHHCCCCCCCHHH
68.0629967540
1472PhosphorylationKDDDNLDSLLDSVVG
CCCCCHHHHHHHHHH
33.7220068231
1476PhosphorylationNLDSLLDSVVGLKQM
CHHHHHHHHHHHHHH
20.7620068231
1494PhosphorylationSGDPLPLSDQDVEPV
CCCCCCCCCCCCHHH
31.1425332170
1503PhosphorylationQDVEPVLSAPESLQN
CCCHHHHCCCHHHHH
41.8525332170
1507PhosphorylationPVLSAPESLQNLFNN
HHHCCCHHHHHHCCC
33.9125332170
1518PhosphorylationLFNNRTAYVLADVMD
HCCCCHHHHHHHHCC
8.7220068231
1561PhosphorylationELSEKCCSDFDLHSE
HHHHHHCCCCCCCHH
51.2727251275
1572PhosphorylationLHSELERSFLSEPSS
CCHHHHHHHHCCCCC
22.5923927012
1575PhosphorylationELERSFLSEPSSPGR
HHHHHHHCCCCCCCC
45.5125463755
1578PhosphorylationRSFLSEPSSPGRTKT
HHHHCCCCCCCCCCC
45.1522167270
1579PhosphorylationSFLSEPSSPGRTKTT
HHHCCCCCCCCCCCC
41.9329255136
1583PhosphorylationEPSSPGRTKTTKGFK
CCCCCCCCCCCCCEE
38.3625159151
1587UbiquitinationPGRTKTTKGFKLGKH
CCCCCCCCCEECCCC
68.5327667366
1595UbiquitinationGFKLGKHKHETFITS
CEECCCCCCCEEECC
46.7729967540
1602PhosphorylationKHETFITSSGKSEYI
CCCEEECCCCCCCCC
32.0728555341
1603PhosphorylationHETFITSSGKSEYIE
CCEEECCCCCCCCCC
41.4025627689
1605AcetylationTFITSSGKSEYIEPA
EEECCCCCCCCCCCC
41.9026051181
1608PhosphorylationTSSGKSEYIEPAKRA
CCCCCCCCCCCCCCC
20.0628796482
1613UbiquitinationSEYIEPAKRAHVVPP
CCCCCCCCCCCCCCC
61.9133845483
1613AcetylationSEYIEPAKRAHVVPP
CCCCCCCCCCCCCCC
61.9125953088
1626MethylationPPPRGRGRGGFGQGI
CCCCCCCCCCCCCCC
40.47115481053
1634MethylationGGFGQGIRPHDIFRQ
CCCCCCCCHHHHHHH
29.35115481061
1646PhosphorylationFRQRKQNTSRPPSMH
HHHHHCCCCCCCCCC
24.5020068231
1647PhosphorylationRQRKQNTSRPPSMHV
HHHHCCCCCCCCCCH
50.7920068231
1651PhosphorylationQNTSRPPSMHVDDFV
CCCCCCCCCCHHHHH
24.9730576142
1663AcetylationDFVAAESKEVVPQDG
HHHHHCCCCCCCCCC
46.147370215
1687DimethylationVSQKISSRGGFSGNR
CCHHHHHCCCCCCCC
42.32-
1687MethylationVSQKISSRGGFSGNR
CCHHHHHCCCCCCCC
42.3224395707
1694DimethylationRGGFSGNRGGRGAFH
CCCCCCCCCCCCCCC
53.09-
1694MethylationRGGFSGNRGGRGAFH
CCCCCCCCCCCCCCC
53.0924395717
1697DimethylationFSGNRGGRGAFHSQN
CCCCCCCCCCCCCCC
35.77-
1697MethylationFSGNRGGRGAFHSQN
CCCCCCCCCCCCCCC
35.7754561481
1702PhosphorylationGGRGAFHSQNRFFTP
CCCCCCCCCCCCCCC
23.7728509920
1708PhosphorylationHSQNRFFTPPASKGN
CCCCCCCCCCCCCCC
26.1721712546
1712PhosphorylationRFFTPPASKGNYSRR
CCCCCCCCCCCCCCC
47.0420068231
1719MethylationSKGNYSRREGTRGSS
CCCCCCCCCCCCCCC
40.53115481077
1723DimethylationYSRREGTRGSSWSAQ
CCCCCCCCCCCCCCC
54.58-
1723MethylationYSRREGTRGSSWSAQ
CCCCCCCCCCCCCCC
54.5824129315
1728PhosphorylationGTRGSSWSAQNTPRG
CCCCCCCCCCCCCCC
23.1722199227
1732PhosphorylationSSWSAQNTPRGNYNE
CCCCCCCCCCCCCCC
11.4121712546
1734MethylationWSAQNTPRGNYNESR
CCCCCCCCCCCCCCC
43.90115382751
1741Asymmetric dimethylarginineRGNYNESRGGQSNFN
CCCCCCCCCCCCCCC
47.27-
1741MethylationRGNYNESRGGQSNFN
CCCCCCCCCCCCCCC
47.2724395727
1749MethylationGGQSNFNRGPLPPLR
CCCCCCCCCCCCCCC
43.92115481045
1759PhosphorylationLPPLRPLSSTGYRPS
CCCCCCCCCCCCCCC
28.6526657352
1760PhosphorylationPPLRPLSSTGYRPSP
CCCCCCCCCCCCCCH
33.2728152594
1761PhosphorylationPLRPLSSTGYRPSPR
CCCCCCCCCCCCCHH
34.5528152594
1763PhosphorylationRPLSSTGYRPSPRDR
CCCCCCCCCCCHHCC
21.3126074081
1766PhosphorylationSSTGYRPSPRDRASR
CCCCCCCCHHCCCCC
24.4626055452
1773Asymmetric dimethylarginineSPRDRASRGRGGLGP
CHHCCCCCCCCCCCC
37.53-
1773MethylationSPRDRASRGRGGLGP
CHHCCCCCCCCCCCC
37.5324129315
1775Asymmetric dimethylarginineRDRASRGRGGLGPSW
HCCCCCCCCCCCCCH
34.59-
1775MethylationRDRASRGRGGLGPSW
HCCCCCCCCCCCCCH
34.5924129315
1793Asymmetric dimethylarginineNSGSGGSRGKFVSGG
CCCCCCCCCCCCCCC
56.44-
1793MethylationNSGSGGSRGKFVSGG
CCCCCCCCCCCCCCC
56.4424129315
1798PhosphorylationGSRGKFVSGGSGRGR
CCCCCCCCCCCCCCC
40.3420068231
1801PhosphorylationGKFVSGGSGRGRHVR
CCCCCCCCCCCCCCC
28.9220068231
1808MethylationSGRGRHVRSFTR---
CCCCCCCCCCCC---
21.6754557005
1812MethylationRHVRSFTR-------
CCCCCCCC-------
42.40115481069

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 VIR_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VIR_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 VIR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BPTF_HUMANBPTFphysical
26344197
ZC3HD_HUMANZC3H13physical
26344197

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 VIR_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-1579, 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-138 AND SER-1579, ANDMASS 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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-1579, 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-1579 AND THR-1708, 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-1579, 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-173; THR-184 ANDSER-222, AND MASS 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-222 AND SER-1579, ANDMASS SPECTROMETRY.

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