MAP1S_HUMAN - dbPTM
MAP1S_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAP1S_HUMAN
UniProt AC Q66K74
Protein Name Microtubule-associated protein 1S
Gene Name MAP1S
Organism Homo sapiens (Human).
Sequence Length 1059
Subcellular Localization Nucleus. Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Detected in filopodia-like protrusions and synapses (By similarity). Detected in perinuclear punctate network corresponding to mitochondrial aggregates and in the
Protein Description Microtubule-associated protein that mediates aggregation of mitochondria resulting in cell death and genomic destruction (MAGD). Plays a role in anchoring the microtubule organizing center to the centrosomes. Binds to DNA. Plays a role in apoptosis. Involved in the formation of microtubule bundles (By similarity)..
Protein Sequence MAAVAGSGAAAAPSSLLLVVGSEFGSPGLLTYVLEELERGIRSWDVDPGVCNLDEQLKVFVSRHSATFSSIVKGQRSLHHRGDNLETLVLLNPSDKSLYDELRNLLLDPASHKLLVLAGPCLEETGELLLQTGGFSPHHFLQVLKDREIRDILATTPPPVQPPILTITCPTFGDWAQLAPAVPGLQGALRLQLRLNPPAQLPNSEGLCEFLEYVAESLEPPSPFELLEPPTSGGFLRLGRPCCYIFPGGLGDAAFFAVNGFTVLVNGGSNPKSSFWKLVRHLDRVDAVLVTHPGADSLPGLNSLLRRKLAERSEVAAGGGSWDDRLRRLISPNLGVVFFNACEAASRLARGEDEAELALSLLAQLGITPLPLSRGPVPAKPTVLFEKMGVGRLDMYVLHPPSAGAERTLASVCALLVWHPAGPGEKVVRVLFPGCTPPACLLDGLVRLQHLRFLREPVVTPQDLEGPGRAESKESVGSRDSSKREGLLATHPRPGQERPGVARKEPARAEAPRKTEKEAKTPRELKKDPKPSVSRTQPREVRRAASSVPNLKKTNAQAAPKPRKAPSTSHSGFPPVANGPRSPPSLRCGEASPPSAACGSPASQLVATPSLELGPIPAGEEKALELPLAASSIPRPRTPSPESHRSPAEGSERLSLSPLRGGEAGPDASPTVTTPTVTTPSLPAEVGSPHSTEVDESLSVSFEQVLPPSAPTSEAGLSLPLRGPRARRSASPHDVDLCLVSPCEFEHRKAVPMAPAPASPGSSNDSSARSQERAGGLGAEETPPTSVSESLPTLSDSDPVPLAPGAADSDEDTEGFGVPRHDPLPDPLKVPPPLPDPSSICMVDPEMLPPKTARQTENVSRTRKPLARPNSRAAAPKATPVAAAKTKGLAGGDRASRPLSARSEPSEKGGRAPLSRKSSTPKTATRGPSGSASSRPGVSATPPKSPVYLDLAYLPSGSSAHLVDEEFFQRVRALCYVISGQDQRKEEGMRAVLDALLASKQHWDRDLQVTLIPTFDSVAMHTWYAETHARHQALGITVLGSNSMVSMQDDAFPACKVEF
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
15PhosphorylationGAAAAPSSLLLVVGS
HHHCCCCCEEEEECC
23.2128464451
22PhosphorylationSLLLVVGSEFGSPGL
CEEEEECCCCCCCHH
20.3828464451
26PhosphorylationVVGSEFGSPGLLTYV
EECCCCCCCHHHHHH
22.5528464451
31PhosphorylationFGSPGLLTYVLEELE
CCCCHHHHHHHHHHH
19.3428464451
32PhosphorylationGSPGLLTYVLEELER
CCCHHHHHHHHHHHH
11.7328464451
47UbiquitinationGIRSWDVDPGVCNLD
HHCCCCCCCCCCCHH
31.59-
47UbiquitinationGIRSWDVDPGVCNLD
HHCCCCCCCCCCCHH
31.5922505724
65PhosphorylationKVFVSRHSATFSSIV
HHHHHCCCCCHHHHH
28.0820873877
67PhosphorylationFVSRHSATFSSIVKG
HHHCCCCCHHHHHCC
27.3720068231
69PhosphorylationSRHSATFSSIVKGQR
HCCCCCHHHHHCCCC
18.1420068231
70UbiquitinationRHSATFSSIVKGQRS
CCCCCHHHHHCCCCC
27.49-
70PhosphorylationRHSATFSSIVKGQRS
CCCCCHHHHHCCCCC
27.4920068231
70UbiquitinationRHSATFSSIVKGQRS
CCCCCHHHHHCCCCC
27.4922817900
73AcetylationATFSSIVKGQRSLHH
CCHHHHHCCCCCCCC
47.897834091
73UbiquitinationATFSSIVKGQRSLHH
CCHHHHHCCCCCCCC
47.8922505724
96UbiquitinationVLLNPSDKSLYDELR
EEECCCCHHHHHHHH
46.8521906983
111PhosphorylationNLLLDPASHKLLVLA
HHHHCHHHCEEEEEE
26.92-
222PhosphorylationAESLEPPSPFELLEP
HHHCCCCCCCCCCCC
53.5922468782
251UbiquitinationYIFPGGLGDAAFFAV
EEECCCCCHHEEEEE
26.28-
277UbiquitinationNPKSSFWKLVRHLDR
CCCHHHHHHHHHHHC
34.78-
313PhosphorylationRRKLAERSEVAAGGG
HHHHHHHCCCCCCCC
28.1126552605
321PhosphorylationEVAAGGGSWDDRLRR
CCCCCCCCHHHHHHH
30.5230175587
354UbiquitinationRLARGEDEAELALSL
HHHCCCCHHHHHHHH
39.48-
354UbiquitinationRLARGEDEAELALSL
HHHCCCCHHHHHHHH
39.4830230243
361UbiquitinationEAELALSLLAQLGIT
HHHHHHHHHHHHCCC
4.83-
361UbiquitinationEAELALSLLAQLGIT
HHHHHHHHHHHHCCC
4.8322817900
380MalonylationSRGPVPAKPTVLFEK
CCCCCCCCCEEEEEE
34.8426320211
380UbiquitinationSRGPVPAKPTVLFEK
CCCCCCCCCEEEEEE
34.8427667366
387UbiquitinationKPTVLFEKMGVGRLD
CCEEEEEECCCCCEE
33.3521906983
446PhosphorylationACLLDGLVRLQHLRF
HHHHHHHHHHHHHHH
7.5932142685
447UbiquitinationCLLDGLVRLQHLRFL
HHHHHHHHHHHHHHH
33.4027667366
460PhosphorylationFLREPVVTPQDLEGP
HHCCCCCCHHHCCCC
18.5729449344
472PhosphorylationEGPGRAESKESVGSR
CCCCCCCCCCCCCCC
40.5123927012
473UbiquitinationGPGRAESKESVGSRD
CCCCCCCCCCCCCCC
45.5827667366
475PhosphorylationGRAESKESVGSRDSS
CCCCCCCCCCCCCCH
35.2023927012
478PhosphorylationESKESVGSRDSSKRE
CCCCCCCCCCCHHCC
30.6623927012
481PhosphorylationESVGSRDSSKREGLL
CCCCCCCCHHCCCCC
36.3330576142
482PhosphorylationSVGSRDSSKREGLLA
CCCCCCCHHCCCCCC
39.7726699800
490PhosphorylationKREGLLATHPRPGQE
HCCCCCCCCCCCCCC
32.1730576142
491UbiquitinationREGLLATHPRPGQER
CCCCCCCCCCCCCCC
15.6824816145
504UbiquitinationERPGVARKEPARAEA
CCCCCCCCCCCCCCC
59.3124816145
517UbiquitinationEAPRKTEKEAKTPRE
CCCCCCHHHCCCHHH
69.1024816145
520AcetylationRKTEKEAKTPRELKK
CCCHHHCCCHHHHCC
61.2221339330
521PhosphorylationKTEKEAKTPRELKKD
CCHHHCCCHHHHCCC
34.3332142685
527MethylationKTPRELKKDPKPSVS
CCHHHHCCCCCCCCC
86.1824129315
527UbiquitinationKTPRELKKDPKPSVS
CCHHHHCCCCCCCCC
86.1824816145
530UbiquitinationRELKKDPKPSVSRTQ
HHHCCCCCCCCCCCC
61.1224816145
534PhosphorylationKDPKPSVSRTQPREV
CCCCCCCCCCCHHHH
33.6728555341
546PhosphorylationREVRRAASSVPNLKK
HHHHHHHHCCCCHHH
30.7727273156
547PhosphorylationEVRRAASSVPNLKKT
HHHHHHHCCCCHHHH
36.5525849741
552MethylationASSVPNLKKTNAQAA
HHCCCCHHHHCCCCC
65.28-
553MethylationSSVPNLKKTNAQAAP
HCCCCHHHHCCCCCC
50.61-
553UbiquitinationSSVPNLKKTNAQAAP
HCCCCHHHHCCCCCC
50.6124816145
554PhosphorylationSVPNLKKTNAQAAPK
CCCCHHHHCCCCCCC
33.9129496963
556PhosphorylationPNLKKTNAQAAPKPR
CCHHHHCCCCCCCCC
12.9632142685
559PhosphorylationKKTNAQAAPKPRKAP
HHHCCCCCCCCCCCC
10.6832142685
567PhosphorylationPKPRKAPSTSHSGFP
CCCCCCCCCCCCCCC
47.6125159151
568PhosphorylationKPRKAPSTSHSGFPP
CCCCCCCCCCCCCCC
29.4223403867
569PhosphorylationPRKAPSTSHSGFPPV
CCCCCCCCCCCCCCC
21.7225159151
571PhosphorylationKAPSTSHSGFPPVAN
CCCCCCCCCCCCCCC
41.7327794612
582PhosphorylationPVANGPRSPPSLRCG
CCCCCCCCCCCCCCC
44.2723401153
585PhosphorylationNGPRSPPSLRCGEAS
CCCCCCCCCCCCCCC
31.6522167270
592PhosphorylationSLRCGEASPPSAACG
CCCCCCCCCCCCCCC
32.8030278072
595PhosphorylationCGEASPPSAACGSPA
CCCCCCCCCCCCCCH
31.7030278072
600PhosphorylationPPSAACGSPASQLVA
CCCCCCCCCHHHHCC
19.7130278072
603PhosphorylationAACGSPASQLVATPS
CCCCCCHHHHCCCCC
27.6830278072
605PhosphorylationCGSPASQLVATPSLE
CCCCHHHHCCCCCCC
2.3432142685
608PhosphorylationPASQLVATPSLELGP
CHHHHCCCCCCCCCC
13.1126657352
610PhosphorylationSQLVATPSLELGPIP
HHHCCCCCCCCCCCC
30.0723403867
612PhosphorylationLVATPSLELGPIPAG
HCCCCCCCCCCCCCC
56.8932142685
614PhosphorylationATPSLELGPIPAGEE
CCCCCCCCCCCCCHH
14.5532142685
631PhosphorylationLELPLAASSIPRPRT
CCCCCHHCCCCCCCC
24.1629255136
632PhosphorylationELPLAASSIPRPRTP
CCCCHHCCCCCCCCC
31.7029255136
638PhosphorylationSSIPRPRTPSPESHR
CCCCCCCCCCCCCCC
30.7029255136
640PhosphorylationIPRPRTPSPESHRSP
CCCCCCCCCCCCCCC
40.4629255136
643PhosphorylationPRTPSPESHRSPAEG
CCCCCCCCCCCCCCC
27.8229255136
646PhosphorylationPSPESHRSPAEGSER
CCCCCCCCCCCCCCC
24.0429255136
651PhosphorylationHRSPAEGSERLSLSP
CCCCCCCCCCCCCCC
15.8529255136
655PhosphorylationAEGSERLSLSPLRGG
CCCCCCCCCCCCCCC
32.7830278072
657PhosphorylationGSERLSLSPLRGGEA
CCCCCCCCCCCCCCC
20.6519664994
671PhosphorylationAGPDASPTVTTPTVT
CCCCCCCCCCCCCCC
28.1724275569
673PhosphorylationPDASPTVTTPTVTTP
CCCCCCCCCCCCCCC
29.5422468782
674PhosphorylationDASPTVTTPTVTTPS
CCCCCCCCCCCCCCC
16.7822468782
676PhosphorylationSPTVTTPTVTTPSLP
CCCCCCCCCCCCCCC
28.5229460479
688PhosphorylationSLPAEVGSPHSTEVD
CCCCCCCCCCCCCCC
25.3126074081
691PhosphorylationAEVGSPHSTEVDESL
CCCCCCCCCCCCCCC
29.6426074081
692PhosphorylationEVGSPHSTEVDESLS
CCCCCCCCCCCCCCE
36.6726074081
703PhosphorylationESLSVSFEQVLPPSA
CCCEEEEECCCCCCC
32.0732142685
705PhosphorylationLSVSFEQVLPPSAPT
CEEEEECCCCCCCCC
7.3432142685
715PhosphorylationPSAPTSEAGLSLPLR
CCCCCCCCCCCCCCC
24.8032142685
718PhosphorylationPTSEAGLSLPLRGPR
CCCCCCCCCCCCCCC
27.3324719451
729PhosphorylationRGPRARRSASPHDVD
CCCCHHCCCCCCCCC
27.7829255136
731PhosphorylationPRARRSASPHDVDLC
CCHHCCCCCCCCCEE
24.8229255136
733PhosphorylationARRSASPHDVDLCLV
HHCCCCCCCCCEEEE
45.2732645325
736PhosphorylationSASPHDVDLCLVSPC
CCCCCCCCEEEECCC
37.4132142685
741PhosphorylationDVDLCLVSPCEFEHR
CCCEEEECCCCCCCC
15.7529255136
753SulfoxidationEHRKAVPMAPAPASP
CCCCCCCCCCCCCCC
5.8421406390
759PhosphorylationPMAPAPASPGSSNDS
CCCCCCCCCCCCCCH
28.8319664994
762PhosphorylationPAPASPGSSNDSSAR
CCCCCCCCCCCHHHH
29.3822167270
763PhosphorylationAPASPGSSNDSSARS
CCCCCCCCCCHHHHH
51.0422167270
766PhosphorylationSPGSSNDSSARSQER
CCCCCCCHHHHHHHH
30.1030278072
767PhosphorylationPGSSNDSSARSQERA
CCCCCCHHHHHHHHH
30.4825159151
770PhosphorylationSNDSSARSQERAGGL
CCCHHHHHHHHHCCC
35.7923927012
782PhosphorylationGGLGAEETPPTSVSE
CCCCCCCCCCCCHHH
26.5225137130
785PhosphorylationGAEETPPTSVSESLP
CCCCCCCCCHHHCCC
42.8623927012
786PhosphorylationAEETPPTSVSESLPT
CCCCCCCCHHHCCCC
29.4423927012
788PhosphorylationETPPTSVSESLPTLS
CCCCCCHHHCCCCCC
22.6418669648
790PhosphorylationPPTSVSESLPTLSDS
CCCCHHHCCCCCCCC
31.9420873877
793PhosphorylationSVSESLPTLSDSDPV
CHHHCCCCCCCCCCC
44.1623927012
795PhosphorylationSESLPTLSDSDPVPL
HHCCCCCCCCCCCCC
37.2323927012
797PhosphorylationSLPTLSDSDPVPLAP
CCCCCCCCCCCCCCC
40.2023927012
809PhosphorylationLAPGAADSDEDTEGF
CCCCCCCCCCCCCCC
37.8728355574
813PhosphorylationAADSDEDTEGFGVPR
CCCCCCCCCCCCCCC
35.6423927012
838PhosphorylationPPPLPDPSSICMVDP
CCCCCCHHHCEEECH
39.4520068231
839PhosphorylationPPLPDPSSICMVDPE
CCCCCHHHCEEECHH
25.7920068231
851UbiquitinationDPEMLPPKTARQTEN
CHHHCCCCCHHCCCC
53.5324816145
852PhosphorylationPEMLPPKTARQTENV
HHHCCCCCHHCCCCC
32.61-
854MethylationMLPPKTARQTENVSR
HCCCCCHHCCCCCCC
49.54-
859UbiquitinationTARQTENVSRTRKPL
CHHCCCCCCCCCCCC
3.1427667366
861MethylationRQTENVSRTRKPLAR
HCCCCCCCCCCCCCC
33.98-
863MethylationTENVSRTRKPLARPN
CCCCCCCCCCCCCCC
37.17-
871PhosphorylationKPLARPNSRAAAPKA
CCCCCCCCCCCCCCC
26.4423312004
877UbiquitinationNSRAAAPKATPVAAA
CCCCCCCCCCCCHHH
61.2324816145
879PhosphorylationRAAAPKATPVAAAKT
CCCCCCCCCCHHHHC
25.1524719451
885UbiquitinationATPVAAAKTKGLAGG
CCCCHHHHCCCCCCC
46.1527667366
886PhosphorylationTPVAAAKTKGLAGGD
CCCHHHHCCCCCCCC
26.1423312004
887MethylationPVAAAKTKGLAGGDR
CCHHHHCCCCCCCCC
51.74-
894MethylationKGLAGGDRASRPLSA
CCCCCCCCCCCCCCC
37.42-
896PhosphorylationLAGGDRASRPLSARS
CCCCCCCCCCCCCCC
35.0124719451
896UbiquitinationLAGGDRASRPLSARS
CCCCCCCCCCCCCCC
35.0127667366
900PhosphorylationDRASRPLSARSEPSE
CCCCCCCCCCCCCCC
25.0730266825
903PhosphorylationSRPLSARSEPSEKGG
CCCCCCCCCCCCCCC
54.2823898821
906PhosphorylationLSARSEPSEKGGRAP
CCCCCCCCCCCCCCC
48.1418452278
915PhosphorylationKGGRAPLSRKSSTPK
CCCCCCCCCCCCCCC
36.2823882029
918PhosphorylationRAPLSRKSSTPKTAT
CCCCCCCCCCCCCCC
38.0326074081
919PhosphorylationAPLSRKSSTPKTATR
CCCCCCCCCCCCCCC
52.3326074081
920PhosphorylationPLSRKSSTPKTATRG
CCCCCCCCCCCCCCC
35.5820068231
922UbiquitinationSRKSSTPKTATRGPS
CCCCCCCCCCCCCCC
51.3727667366
923PhosphorylationRKSSTPKTATRGPSG
CCCCCCCCCCCCCCC
34.1720068231
925PhosphorylationSSTPKTATRGPSGSA
CCCCCCCCCCCCCCC
41.2020068231
926MethylationSTPKTATRGPSGSAS
CCCCCCCCCCCCCCC
53.19-
929PhosphorylationKTATRGPSGSASSRP
CCCCCCCCCCCCCCC
48.4825159151
931PhosphorylationATRGPSGSASSRPGV
CCCCCCCCCCCCCCC
29.3428985074
933PhosphorylationRGPSGSASSRPGVSA
CCCCCCCCCCCCCCC
28.6923312004
934PhosphorylationGPSGSASSRPGVSAT
CCCCCCCCCCCCCCC
42.0623312004
935MethylationPSGSASSRPGVSATP
CCCCCCCCCCCCCCC
29.51-
939PhosphorylationASSRPGVSATPPKSP
CCCCCCCCCCCCCCC
32.1323312004
941PhosphorylationSRPGVSATPPKSPVY
CCCCCCCCCCCCCEE
32.3925159151
945PhosphorylationVSATPPKSPVYLDLA
CCCCCCCCCEEEEEE
25.9327642862
948PhosphorylationTPPKSPVYLDLAYLP
CCCCCCEEEEEECCC
9.6227642862
974UbiquitinationFFQRVRALCYVISGQ
HHHHHHHHHHHHCCC
1.19-
974UbiquitinationFFQRVRALCYVISGQ
HHHHHHHHHHHHCCC
1.1921890473
976PhosphorylationQRVRALCYVISGQDQ
HHHHHHHHHHCCCHH
11.1529496907
999PhosphorylationVLDALLASKQHWDRD
HHHHHHHHHHHCCCC
32.58-
1000UbiquitinationLDALLASKQHWDRDL
HHHHHHHHHHCCCCC
40.3421890473
1000UbiquitinationLDALLASKQHWDRDL
HHHHHHHHHHCCCCC
40.3421890473

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
900SPhosphorylationKinaseCDKL2Q92772
PSP
900SPhosphorylationKinaseCDKL5O76039
PSP
-KUbiquitinationE3 ubiquitin ligaseGANQ9H2C0
PMID:18680552

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MAP1S_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 MAP1S_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RASF1_HUMANRASSF1physical
15753381
RASF1_MOUSERassf1physical
15753381
SOCS3_HUMANSOCS3physical
19027008
MLP3A_HUMANMAP1LC3Aphysical
21262964
ROA2_HUMANHNRNPA2B1physical
22863883
HNRPQ_HUMANSYNCRIPphysical
22863883
RASF5_HUMANRASSF5physical
25416956
ANXA1_HUMANANXA1physical
24366813
ANXA2_HUMANANXA2physical
24366813
B2MG_HUMANB2Mphysical
24366813
GELS_HUMANGSNphysical
24366813
MAP1B_HUMANMAP1Bphysical
24366813
STK4_HUMANSTK4physical
24366813
STK3_HUMANSTK3physical
24366813
RASF3_HUMANRASSF3physical
24366813
STIP1_HUMANSTIP1physical
24366813

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 MAP1S_HUMAN

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Related Literatures of Post-Translational Modification
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-638; SER-640; SER-759AND SER-762, 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 SER-759; SER-762 ANDTHR-813, 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-472; SER-475; THR-638;SER-640; SER-657; SER-729; SER-731; SER-741 AND SER-759, AND MASSSPECTROMETRY.
"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-657 AND SER-759, ANDMASS 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-731 AND SER-759, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-900, 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-472; SER-729 ANDSER-731, 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 THR-638; SER-640; SER-657AND SER-759, AND MASS SPECTROMETRY.

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