LSR_HUMAN - dbPTM
LSR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LSR_HUMAN
UniProt AC Q86X29
Protein Name Lipolysis-stimulated lipoprotein receptor
Gene Name LSR
Organism Homo sapiens (Human).
Sequence Length 649
Subcellular Localization Cell membrane
Single-pass membrane protein .
Protein Description Probable role in the clearance of triglyceride-rich lipoprotein from blood. Binds chylomicrons, LDL and VLDL in presence of free fatty acids and allows their subsequent uptake in the cells (By similarity)..
Protein Sequence MQQDGLGVGTRNGSGKGRSVHPSWPWCAPRPLRYFGRDARARRAQTAAMALLAGGLSRGLGSHPAAAGRDAVVFVWLLLSTWCTAPARAIQVTVSNPYHVVILFQPVTLPCTYQMTSTPTQPIVIWKYKSFCRDRIADAFSPASVDNQLNAQLAAGNPGYNPYVECQDSVRTVRVVATKQGNAVTLGDYYQGRRITITGNADLTFDQTAWGDSGVYYCSVVSAQDLQGNNEAYAELIVLGRTSGVAELLPGFQAGPIEDWLFVVVVCLAAFLIFLLLGICWCQCCPHTCCCYVRCPCCPDKCCCPEALYAAGKAATSGVPSIYAPSTYAHLSPAKTPPPPAMIPMGPAYNGYPGGYPGDVDRSSSAGGQGSYVPLLRDTDSSVASEVRSGYRIQASQQDDSMRVLYYMEKELANFDPSRPGPPSGRVERAMSEVTSLHEDDWRSRPSRGPALTPIRDEEWGGHSPRSPRGWDQEPAREQAGGGWRARRPRARSVDALDDLTPPSTAESGSRSPTSNGGRSRAYMPPRSRSRDDLYDQDDSRDFPRSRDPHYDDFRSRERPPADPRSHHHRTRDPRDNGSRSGDLPYDGRLLEEAVRKKGSEERRRPHKEEEEEAYYPPAPPPYSETDSQASRERRLKKNLALSRESLVV
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
10PhosphorylationQDGLGVGTRNGSGKG
CCCCCCCCCCCCCCC
20.6820068231
14PhosphorylationGVGTRNGSGKGRSVH
CCCCCCCCCCCCCCC
40.6620068231
23PhosphorylationKGRSVHPSWPWCAPR
CCCCCCCCCCCCCCC
30.7824719451
46PhosphorylationARARRAQTAAMALLA
HHHHHHHHHHHHHHH
18.5225884760
57PhosphorylationALLAGGLSRGLGSHP
HHHHHHHHHCCCCCH
27.8125884760
116PhosphorylationLPCTYQMTSTPTQPI
ECCEEECCCCCCCCE
17.5829083192
117PhosphorylationPCTYQMTSTPTQPIV
CCEEECCCCCCCCEE
27.3529083192
118PhosphorylationCTYQMTSTPTQPIVI
CEEECCCCCCCCEEE
22.6129083192
120PhosphorylationYQMTSTPTQPIVIWK
EECCCCCCCCEEEEE
47.2529083192
131UbiquitinationVIWKYKSFCRDRIAD
EEEEEHHHHCHHHHH
3.2821890473
141O-linked_GlycosylationDRIADAFSPASVDNQ
HHHHHCCCHHHHHHH
22.68OGP
142 (in isoform 2)Ubiquitination-23.3121890473
144PhosphorylationADAFSPASVDNQLNA
HHCCCHHHHHHHHHH
33.1326657352
150 (in isoform 6)Phosphorylation-18.8429514088
153 (in isoform 6)Phosphorylation-3.0729514088
179UbiquitinationTVRVVATKQGNAVTL
EEEEEEECCCCEEEE
46.61-
179UbiquitinationTVRVVATKQGNAVTL
EEEEEEECCCCEEEE
46.6121906983
179 (in isoform 1)Ubiquitination-46.6121890473
179 (in isoform 3)Ubiquitination-46.6121890473
185O-linked_GlycosylationTKQGNAVTLGDYYQG
ECCCCEEEECCEECC
23.71171669
185PhosphorylationTKQGNAVTLGDYYQG
ECCCCEEEECCEECC
23.7121082442
189PhosphorylationNAVTLGDYYQGRRIT
CEEEECCEECCCEEE
8.90-
190PhosphorylationAVTLGDYYQGRRITI
EEEECCEECCCEEEE
14.83-
216PhosphorylationAWGDSGVYYCSVVSA
CCCCCCEEEEEEEEH
11.4132142685
227UbiquitinationVVSAQDLQGNNEAYA
EEEHHHCCCCCHHEE
61.9423503661
254UbiquitinationELLPGFQAGPIEDWL
HHCCCCCCCCHHHHH
24.3821890473
267UbiquitinationWLFVVVVCLAAFLIF
HHHHHHHHHHHHHHH
1.1323503661
286UbiquitinationICWCQCCPHTCCCYV
HHHHHHCCCCCEEEE
33.1923503661
290PhosphorylationQCCPHTCCCYVRCPC
HHCCCCCEEEEECCC
1.65-
293UbiquitinationPHTCCCYVRCPCCPD
CCCCEEEEECCCCCC
2.9529901268
298 (in isoform 2)Ubiquitination-2.70-
302UbiquitinationCPCCPDKCCCPEALY
CCCCCCCCCCHHHHH
3.6323000965
304PhosphorylationCCPDKCCCPEALYAA
CCCCCCCCHHHHHHH
4.84-
307PhosphorylationDKCCCPEALYAAGKA
CCCCCHHHHHHHHHH
7.33-
309PhosphorylationCCCPEALYAAGKAAT
CCCHHHHHHHHHHHH
11.0621945579
313PhosphorylationEALYAAGKAATSGVP
HHHHHHHHHHHCCCC
30.07-
313UbiquitinationEALYAAGKAATSGVP
HHHHHHHHHHHCCCC
30.07-
316O-linked_GlycosylationYAAGKAATSGVPSIY
HHHHHHHHCCCCCEE
30.7655821201
316PhosphorylationYAAGKAATSGVPSIY
HHHHHHHHCCCCCEE
30.7621945579
316UbiquitinationYAAGKAATSGVPSIY
HHHHHHHHCCCCCEE
30.7623503661
317O-linked_GlycosylationAAGKAATSGVPSIYA
HHHHHHHCCCCCEEC
32.8255821207
317PhosphorylationAAGKAATSGVPSIYA
HHHHHHHCCCCCEEC
32.8221945579
321PhosphorylationAATSGVPSIYAPSTY
HHHCCCCCEECCCCC
26.3121945579
323PhosphorylationTSGVPSIYAPSTYAH
HCCCCCEECCCCCCC
19.4621945579
326O-linked_GlycosylationVPSIYAPSTYAHLSP
CCCEECCCCCCCCCC
26.3619901323
326PhosphorylationVPSIYAPSTYAHLSP
CCCEECCCCCCCCCC
26.3621945579
327O-linked_GlycosylationPSIYAPSTYAHLSPA
CCEECCCCCCCCCCC
24.5424870719
327PhosphorylationPSIYAPSTYAHLSPA
CCEECCCCCCCCCCC
24.5421945579
328PhosphorylationSIYAPSTYAHLSPAK
CEECCCCCCCCCCCC
9.0721945579
332O-linked_GlycosylationPSTYAHLSPAKTPPP
CCCCCCCCCCCCCCC
16.9714643711
332PhosphorylationPSTYAHLSPAKTPPP
CCCCCCCCCCCCCCC
16.9721945579
335UbiquitinationYAHLSPAKTPPPPAM
CCCCCCCCCCCCCCC
66.0223503661
336PhosphorylationAHLSPAKTPPPPAMI
CCCCCCCCCCCCCCC
43.0421945579
341UbiquitinationAKTPPPPAMIPMGPA
CCCCCCCCCCCCCCC
17.8223000965
342UbiquitinationKTPPPPAMIPMGPAY
CCCCCCCCCCCCCCC
4.3323000965
347PhosphorylationPAMIPMGPAYNGYPG
CCCCCCCCCCCCCCC
25.8932142685
349PhosphorylationMIPMGPAYNGYPGGY
CCCCCCCCCCCCCCC
16.5621945579
352PhosphorylationMGPAYNGYPGGYPGD
CCCCCCCCCCCCCCC
8.6121945579
352 (in isoform 2)Ubiquitination-8.6121890473
353PhosphorylationGPAYNGYPGGYPGDV
CCCCCCCCCCCCCCC
31.00-
356PhosphorylationYNGYPGGYPGDVDRS
CCCCCCCCCCCCCCC
15.2321945579
361UbiquitinationGGYPGDVDRSSSAGG
CCCCCCCCCCCCCCC
49.8623000965
362 (in isoform 3)Phosphorylation-37.9828348404
363O-linked_GlycosylationYPGDVDRSSSAGGQG
CCCCCCCCCCCCCCC
24.96OGP
363PhosphorylationYPGDVDRSSSAGGQG
CCCCCCCCCCCCCCC
24.9621945579
363 (in isoform 3)Phosphorylation-24.9625262027
364PhosphorylationPGDVDRSSSAGGQGS
CCCCCCCCCCCCCCC
25.7121945579
365PhosphorylationGDVDRSSSAGGQGSY
CCCCCCCCCCCCCCE
31.9821945579
366 (in isoform 3)Phosphorylation-28.2525262027
371O-linked_GlycosylationSSAGGQGSYVPLLRD
CCCCCCCCEEEEECC
18.319543037
371PhosphorylationSSAGGQGSYVPLLRD
CCCCCCCCEEEEECC
18.3121945579
372PhosphorylationSAGGQGSYVPLLRDT
CCCCCCCEEEEECCC
16.9521945579
379PhosphorylationYVPLLRDTDSSVASE
EEEEECCCCCHHHHH
31.2021406692
381PhosphorylationPLLRDTDSSVASEVR
EEECCCCCHHHHHHH
28.8921406692
382PhosphorylationLLRDTDSSVASEVRS
EECCCCCHHHHHHHC
25.2221406692
385PhosphorylationDTDSSVASEVRSGYR
CCCCHHHHHHHCCCE
34.1725849741
387PhosphorylationDSSVASEVRSGYRIQ
CCHHHHHHHCCCEEE
5.67-
388PhosphorylationSSVASEVRSGYRIQA
CHHHHHHHCCCEEEE
21.95-
389PhosphorylationSVASEVRSGYRIQAS
HHHHHHHCCCEEEEE
45.4025849741
390UbiquitinationVASEVRSGYRIQASQ
HHHHHHCCCEEEEEC
12.7423000965
390UbiquitinationVASEVRSGYRIQASQ
HHHHHHCCCEEEEEC
12.7421890473
390UbiquitinationVASEVRSGYRIQASQ
HHHHHHCCCEEEEEC
12.7421890473
391PhosphorylationASEVRSGYRIQASQQ
HHHHHCCCEEEEECC
13.0421945579
391UbiquitinationASEVRSGYRIQASQQ
HHHHHCCCEEEEECC
13.0423000965
391 (in isoform 3)Ubiquitination-13.0421890473
396PhosphorylationSGYRIQASQQDDSMR
CCCEEEEECCCCHHH
16.4021945579
401PhosphorylationQASQQDDSMRVLYYM
EEECCCCHHHHHHHH
19.4421945579
406PhosphorylationDDSMRVLYYMEKELA
CCHHHHHHHHHHHHH
9.6325159151
407PhosphorylationDSMRVLYYMEKELAN
CHHHHHHHHHHHHHC
8.4728102081
409UbiquitinationMRVLYYMEKELANFD
HHHHHHHHHHHHCCC
27.5323000965
410UbiquitinationRVLYYMEKELANFDP
HHHHHHHHHHHCCCC
41.3123000965
410 (in isoform 1)Ubiquitination-41.3121890473
413PhosphorylationYYMEKELANFDPSRP
HHHHHHHHCCCCCCC
18.7432645325
417PhosphorylationKELANFDPSRPGPPS
HHHHCCCCCCCCCCC
28.27-
418O-linked_GlycosylationELANFDPSRPGPPSG
HHHCCCCCCCCCCCC
53.61317667069
418PhosphorylationELANFDPSRPGPPSG
HHHCCCCCCCCCCCC
53.6123312004
424O-linked_GlycosylationPSRPGPPSGRVERAM
CCCCCCCCCHHHHHH
42.2254904091
424PhosphorylationPSRPGPPSGRVERAM
CCCCCCCCCHHHHHH
42.2225849741
432O-linked_GlycosylationGRVERAMSEVTSLHE
CHHHHHHHHHHHHCC
28.1220068231
432PhosphorylationGRVERAMSEVTSLHE
CHHHHHHHHHHHHCC
28.1223401153
435O-linked_GlycosylationERAMSEVTSLHEDDW
HHHHHHHHHHCCCCC
22.8655821261
435PhosphorylationERAMSEVTSLHEDDW
HHHHHHHHHHCCCCC
22.8630266825
436O-linked_GlycosylationRAMSEVTSLHEDDWR
HHHHHHHHHCCCCCC
32.679543097
436PhosphorylationRAMSEVTSLHEDDWR
HHHHHHHHHCCCCCC
32.6730266825
444O-linked_GlycosylationLHEDDWRSRPSRGPA
HCCCCCCCCCCCCCC
44.2755821461
445PhosphorylationHEDDWRSRPSRGPAL
CCCCCCCCCCCCCCC
25.33-
447O-linked_GlycosylationDDWRSRPSRGPALTP
CCCCCCCCCCCCCCC
49.0855821467
447PhosphorylationDDWRSRPSRGPALTP
CCCCCCCCCCCCCCC
49.08-
452UbiquitinationRPSRGPALTPIRDEE
CCCCCCCCCCCCCCC
7.05-
453O-linked_GlycosylationPSRGPALTPIRDEEW
CCCCCCCCCCCCCCC
20.839543109
453PhosphorylationPSRGPALTPIRDEEW
CCCCCCCCCCCCCCC
20.8323927012
464O-linked_GlycosylationDEEWGGHSPRSPRGW
CCCCCCCCCCCCCCC
25.8619651622
464PhosphorylationDEEWGGHSPRSPRGW
CCCCCCCCCCCCCCC
25.8623927012
467PhosphorylationWGGHSPRSPRGWDQE
CCCCCCCCCCCCCCC
23.4921955146
474PhosphorylationSPRGWDQEPAREQAG
CCCCCCCCHHHHHCC
38.15-
482PhosphorylationPAREQAGGGWRARRP
HHHHHCCCCHHCCCC
35.19-
491UbiquitinationWRARRPRARSVDALD
HHCCCCCCCCCCCHH
15.6932015554
493PhosphorylationARRPRARSVDALDDL
CCCCCCCCCCCHHHC
24.3019664994
495PhosphorylationRPRARSVDALDDLTP
CCCCCCCCCHHHCCC
42.53-
500UbiquitinationSVDALDDLTPPSTAE
CCCCHHHCCCCCCCC
8.4823503661
501PhosphorylationVDALDDLTPPSTAES
CCCHHHCCCCCCCCC
39.9019664994
504PhosphorylationLDDLTPPSTAESGSR
HHHCCCCCCCCCCCC
41.2623401153
505O-linked_GlycosylationDDLTPPSTAESGSRS
HHCCCCCCCCCCCCC
39.97OGP
505PhosphorylationDDLTPPSTAESGSRS
HHCCCCCCCCCCCCC
39.9730266825
508PhosphorylationTPPSTAESGSRSPTS
CCCCCCCCCCCCCCC
39.3430266825
509PhosphorylationPPSTAESGSRSPTSN
CCCCCCCCCCCCCCC
20.70-
510PhosphorylationPSTAESGSRSPTSNG
CCCCCCCCCCCCCCC
38.5730266825
511PhosphorylationSTAESGSRSPTSNGG
CCCCCCCCCCCCCCC
50.62-
512PhosphorylationTAESGSRSPTSNGGR
CCCCCCCCCCCCCCC
33.9430266825
514PhosphorylationESGSRSPTSNGGRSR
CCCCCCCCCCCCCCC
35.7530266825
515PhosphorylationSGSRSPTSNGGRSRA
CCCCCCCCCCCCCCC
36.5430266825
516PhosphorylationGSRSPTSNGGRSRAY
CCCCCCCCCCCCCCC
60.46-
520PhosphorylationPTSNGGRSRAYMPPR
CCCCCCCCCCCCCCC
25.2523403867
521PhosphorylationTSNGGRSRAYMPPRS
CCCCCCCCCCCCCCC
28.51-
523PhosphorylationNGGRSRAYMPPRSRS
CCCCCCCCCCCCCCC
14.7227259358
528PhosphorylationRAYMPPRSRSRDDLY
CCCCCCCCCCCCCCC
40.1423401153
530PhosphorylationYMPPRSRSRDDLYDQ
CCCCCCCCCCCCCCC
41.1123927012
532PhosphorylationPPRSRSRDDLYDQDD
CCCCCCCCCCCCCCC
52.0617389395
535PhosphorylationSRSRDDLYDQDDSRD
CCCCCCCCCCCCCCC
20.6727273156
539UbiquitinationDDLYDQDDSRDFPRS
CCCCCCCCCCCCCHH
39.6823503661
540PhosphorylationDLYDQDDSRDFPRSR
CCCCCCCCCCCCHHC
41.8823927012
540UbiquitinationDLYDQDDSRDFPRSR
CCCCCCCCCCCCHHC
41.8823503661
546O-linked_GlycosylationDSRDFPRSRDPHYDD
CCCCCCHHCCCCHHC
41.0746243171
546PhosphorylationDSRDFPRSRDPHYDD
CCCCCCHHCCCCHHC
41.0721945579
550PhosphorylationFPRSRDPHYDDFRSR
CCHHCCCCHHCHHCC
42.8317016520
550 (in isoform 2)Ubiquitination-42.83-
551PhosphorylationPRSRDPHYDDFRSRE
CHHCCCCHHCHHCCC
23.6921945579
556PhosphorylationPHYDDFRSRERPPAD
CCHHCHHCCCCCCCC
38.1921945579
559UbiquitinationDDFRSRERPPADPRS
HCHHCCCCCCCCCCC
41.2023503661
562PhosphorylationRSRERPPADPRSHHH
HCCCCCCCCCCCCCC
41.97-
567PhosphorylationPPADPRSHHHRTRDP
CCCCCCCCCCCCCCC
23.2717389395
579PhosphorylationRDPRDNGSRSGDLPY
CCCCCCCCCCCCCCC
29.5423401153
581PhosphorylationPRDNGSRSGDLPYDG
CCCCCCCCCCCCCCC
38.0519664994
586PhosphorylationSRSGDLPYDGRLLEE
CCCCCCCCCCHHHHH
38.0227273156
588UbiquitinationSGDLPYDGRLLEEAV
CCCCCCCCHHHHHHH
19.1123503661
589UbiquitinationGDLPYDGRLLEEAVR
CCCCCCCHHHHHHHH
32.9523503661
596PhosphorylationRLLEEAVRKKGSEER
HHHHHHHHHCCCHHH
41.85-
597PhosphorylationLLEEAVRKKGSEERR
HHHHHHHHCCCHHHC
55.69-
604PhosphorylationKKGSEERRRPHKEEE
HCCCHHHCCCCHHHH
60.81-
607UbiquitinationSEERRRPHKEEEEEA
CHHHCCCCHHHHHHH
48.6323503661
608UbiquitinationEERRRPHKEEEEEAY
HHHCCCCHHHHHHHC
70.2923503661
615PhosphorylationKEEEEEAYYPPAPPP
HHHHHHHCCCCCCCC
21.5621945579
616PhosphorylationEEEEEAYYPPAPPPY
HHHHHHCCCCCCCCC
15.1321945579
623PhosphorylationYPPAPPPYSETDSQA
CCCCCCCCCCCCCHH
25.5526657352
624PhosphorylationPPAPPPYSETDSQAS
CCCCCCCCCCCCHHH
39.5321945579
626PhosphorylationAPPPYSETDSQASRE
CCCCCCCCCCHHHHH
34.7021945579
627PhosphorylationPPPYSETDSQASRER
CCCCCCCCCHHHHHH
34.40-
628PhosphorylationPPYSETDSQASRERR
CCCCCCCCHHHHHHH
34.7621945579
631PhosphorylationSETDSQASRERRLKK
CCCCCHHHHHHHHHH
27.3421945579
638UbiquitinationSRERRLKKNLALSRE
HHHHHHHHHHCCCHH
62.88-
643PhosphorylationLKKNLALSRESLVV-
HHHHHCCCHHHCCC-
28.5226846344
646PhosphorylationNLALSRESLVV----
HHCCCHHHCCC----
25.9226846344

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 LSR_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LSR_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 LSR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RARG_HUMANRARGphysical
21988832
MAPK5_HUMANMAPKAPK5physical
21988832
STON2_HUMANSTON2physical
28514442
EPS15_HUMANEPS15physical
28514442
RBP1_HUMANRALBP1physical
28514442
EP15R_HUMANEPS15L1physical
28514442
SMAD5_HUMANSMAD5physical
28514442
REPS1_HUMANREPS1physical
28514442
ITSN1_HUMANITSN1physical
28514442
AP1B1_HUMANAP1B1physical
28514442
AP2A2_HUMANAP2A2physical
28514442
VPS45_HUMANVPS45physical
28514442
AP2A1_HUMANAP2A1physical
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 LSR_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 SER-643, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643 AND SER-646, ANDMASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, AND MASSSPECTROMETRY.
"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-493, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-530, ANDMASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-372 AND TYR-406, ANDMASS SPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-551 AND TYR-586, ANDMASS SPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309; TYR-328; TYR-406;TYR-535; TYR-551; TYR-586 AND TYR-615, AND MASS SPECTROMETRY.

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