PAIRB_HUMAN - dbPTM
PAIRB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAIRB_HUMAN
UniProt AC Q8NC51
Protein Name Plasminogen activator inhibitor 1 RNA-binding protein
Gene Name SERBP1
Organism Homo sapiens (Human).
Sequence Length 408
Subcellular Localization Cytoplasm . Nucleus . Cytoplasm, perinuclear region . Also found in perinuclear regions.
Protein Description May play a role in the regulation of mRNA stability. Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay..
Protein Sequence MPGHLQEGFGCVVTNRFDQLFDDESDPFEVLKAAENKKKEAGGGGVGGPGAKSAAQAAAQTNSNAAGKQLRKESQKDRKNPLPPSVGVVDKKEETQPPVALKKEGIRRVGRRPDQQLQGEGKIIDRRPERRPPRERRFEKPLEEKGEGGEFSVDRPIIDRPIRGRGGLGRGRGGRGRGMGRGDGFDSRGKREFDRHSGSDRSSFSHYSGLKHEDKRGGSGSHNWGTVKDELTESPKYIQKQISYNYSDLDQSNVTEETPEGEEHHPVADTENKENEVEEVKEEGPKEMTLDEWKAIQNKDRAKVEFNIRKPNEGADGQWKKGFVLHKSKSEEAHAEDSVMDHHFRKPANDITSQLEINFGDLGRPGRGGRGGRGGRGRGGRPNRGSRTDKSSASAPDVDDPEAFPALA
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
11S-nitrosocysteineHLQEGFGCVVTNRFD
CCCCCCCEEEECCHH		1.76-
11GlutathionylationHLQEGFGCVVTNRFD
CCCCCCCEEEECCHH		1.7622555962
11S-nitrosylationHLQEGFGCVVTNRFD
CCCCCCCEEEECCHH		1.7619483679
25PhosphorylationDQLFDDESDPFEVLK
HHHCCCCCCHHHHHH		58.5419664994
25 (in isoform 3)Phosphorylation-58.5418669648
32AcetylationSDPFEVLKAAENKKK
CCHHHHHHHHHHHCC		51.2126051181
32UbiquitinationSDPFEVLKAAENKKK
CCHHHHHHHHHHHCC		51.2121906983
32 (in isoform 1)Ubiquitination-51.2121890473
32 (in isoform 2)Ubiquitination-51.2121890473
32 (in isoform 3)Ubiquitination-51.2121890473
32 (in isoform 4)Ubiquitination-51.2121890473
37UbiquitinationVLKAAENKKKEAGGG
HHHHHHHHCCCCCCC		57.6422053931
37 (in isoform 1)Ubiquitination-57.6421890473
392-HydroxyisobutyrylationKAAENKKKEAGGGGV
HHHHHHCCCCCCCCC		55.17-
39UbiquitinationKAAENKKKEAGGGGV
HHHHHHCCCCCCCCC		55.17-
52AcetylationGVGGPGAKSAAQAAA
CCCCHHHHHHHHHHH		46.6826051181
52SumoylationGVGGPGAKSAAQAAA
CCCCHHHHHHHHHHH		46.6825114211
52UbiquitinationGVGGPGAKSAAQAAA
CCCCHHHHHHHHHHH		46.6821906983
52 (in isoform 1)Ubiquitination-46.6821890473
52 (in isoform 2)Ubiquitination-46.6821890473
52 (in isoform 3)Ubiquitination-46.6821890473
52 (in isoform 4)Ubiquitination-46.6821890473
53PhosphorylationVGGPGAKSAAQAAAQ
CCCHHHHHHHHHHHH		28.4425159151
61O-linked_GlycosylationAAQAAAQTNSNAAGK
HHHHHHHCCCCHHHH		35.5723301498
61PhosphorylationAAQAAAQTNSNAAGK
HHHHHHHCCCCHHHH		35.5725159151
63PhosphorylationQAAAQTNSNAAGKQL
HHHHHCCCCHHHHHH		31.1025159151
682-HydroxyisobutyrylationTNSNAAGKQLRKESQ
CCCCHHHHHHHHHHH		41.24-
68AcetylationTNSNAAGKQLRKESQ
CCCCHHHHHHHHHHH		41.2419608861
68UbiquitinationTNSNAAGKQLRKESQ
CCCCHHHHHHHHHHH		41.2421890473
68 (in isoform 1)Ubiquitination-41.2421890473
68 (in isoform 2)Ubiquitination-41.2421890473
68 (in isoform 3)Ubiquitination-41.2421890473
68 (in isoform 4)Ubiquitination-41.2421890473
72UbiquitinationAAGKQLRKESQKDRK
HHHHHHHHHHHHHCC		71.02-
74PhosphorylationGKQLRKESQKDRKNP
HHHHHHHHHHHCCCC		45.6326699800
79MalonylationKESQKDRKNPLPPSV
HHHHHHCCCCCCCCC		73.4026320211
85PhosphorylationRKNPLPPSVGVVDKK
CCCCCCCCCCCCCCC		29.5725159151
912-HydroxyisobutyrylationPSVGVVDKKEETQPP
CCCCCCCCCCCCCCC		50.94-
91AcetylationPSVGVVDKKEETQPP
CCCCCCCCCCCCCCC		50.9426051181
92AcetylationSVGVVDKKEETQPPV
CCCCCCCCCCCCCCC		57.2123236377
92UbiquitinationSVGVVDKKEETQPPV
CCCCCCCCCCCCCCC		57.21-
95PhosphorylationVVDKKEETQPPVALK
CCCCCCCCCCCCCCC		47.6825159151
102SumoylationTQPPVALKKEGIRRV
CCCCCCCCHHHHCCC		38.76-
1022-HydroxyisobutyrylationTQPPVALKKEGIRRV
CCCCCCCCHHHHCCC		38.76-
102AcetylationTQPPVALKKEGIRRV
CCCCCCCCHHHHCCC		38.7625953088
102SuccinylationTQPPVALKKEGIRRV
CCCCCCCCHHHHCCC		38.7623954790
102SumoylationTQPPVALKKEGIRRV
CCCCCCCCHHHHCCC		38.7628112733
102UbiquitinationTQPPVALKKEGIRRV
CCCCCCCCHHHHCCC		38.76-
1222-HydroxyisobutyrylationQQLQGEGKIIDRRPE
HHHCCCCCCCCCCCC		31.99-
122AcetylationQQLQGEGKIIDRRPE
HHHCCCCCCCCCCCC		31.9919608861
122MalonylationQQLQGEGKIIDRRPE
HHHCCCCCCCCCCCC		31.9926320211
122UbiquitinationQQLQGEGKIIDRRPE
HHHCCCCCCCCCCCC		31.9921890473
122 (in isoform 1)Ubiquitination-31.9921890473
122 (in isoform 2)Ubiquitination-31.9921890473
122 (in isoform 3)Ubiquitination-31.9921890473
122 (in isoform 4)Ubiquitination-31.9921890473
126MethylationGEGKIIDRRPERRPP
CCCCCCCCCCCCCCC		45.72115486343
140AcetylationPRERRFEKPLEEKGE
CCHHHCCCCCHHCCC		52.7919608861
140MalonylationPRERRFEKPLEEKGE
CCHHHCCCCCHHCCC		52.7926320211
140UbiquitinationPRERRFEKPLEEKGE
CCHHHCCCCCHHCCC		52.79-
1452-HydroxyisobutyrylationFEKPLEEKGEGGEFS
CCCCCHHCCCCCCCC		53.54-
152PhosphorylationKGEGGEFSVDRPIID
CCCCCCCCCCCCCCC		20.8529255136
155MethylationGGEFSVDRPIIDRPI
CCCCCCCCCCCCCCC		23.3558858761
160MethylationVDRPIIDRPIRGRGG
CCCCCCCCCCCCCCC		20.3824384579
163DimethylationPIIDRPIRGRGGLGR
CCCCCCCCCCCCCCC		31.29-
163MethylationPIIDRPIRGRGGLGR
CCCCCCCCCCCCCCC		31.2912019671
165MethylationIDRPIRGRGGLGRGR
CCCCCCCCCCCCCCC		26.5912019683
177DimethylationRGRGGRGRGMGRGDG
CCCCCCCCCCCCCCC		30.48-
177MethylationRGRGGRGRGMGRGDG
CCCCCCCCCCCCCCC		30.4812019695
181DimethylationGRGRGMGRGDGFDSR
CCCCCCCCCCCCCCC		31.01-
181MethylationGRGRGMGRGDGFDSR
CCCCCCCCCCCCCCC		31.0112019707
188MethylationRGDGFDSRGKREFDR
CCCCCCCCCCCCCCC		57.4054557871
195MethylationRGKREFDRHSGSDRS
CCCCCCCCCCCCCCH		31.0680701133
197PhosphorylationKREFDRHSGSDRSSF
CCCCCCCCCCCCHHH		40.6729255136
197 (in isoform 2)Phosphorylation-40.6729743597
197 (in isoform 4)Phosphorylation-40.6729743597
199PhosphorylationEFDRHSGSDRSSFSH
CCCCCCCCCCHHHCC		32.6323401153
199 (in isoform 2)Phosphorylation-32.6317081983
199 (in isoform 4)Phosphorylation-32.6317081983
201MethylationDRHSGSDRSSFSHYS
CCCCCCCCHHHCCCC		35.5854557863
202PhosphorylationRHSGSDRSSFSHYSG
CCCCCCCHHHCCCCC		40.5023401153
202 (in isoform 3)Phosphorylation-40.5018220336
203PhosphorylationHSGSDRSSFSHYSGL
CCCCCCHHHCCCCCC		31.4922167270
205PhosphorylationGSDRSSFSHYSGLKH
CCCCHHHCCCCCCCC		24.3821945579
207PhosphorylationDRSSFSHYSGLKHED
CCHHHCCCCCCCCCC		11.8421945579
208PhosphorylationRSSFSHYSGLKHEDK
CHHHCCCCCCCCCCC		32.0223401153
211AcetylationFSHYSGLKHEDKRGG
HCCCCCCCCCCCCCC		48.7719608861
211SumoylationFSHYSGLKHEDKRGG
HCCCCCCCCCCCCCC		48.7728112733
211UbiquitinationFSHYSGLKHEDKRGG
HCCCCCCCCCCCCCC		48.7719608861
211 (in isoform 3)Ubiquitination-48.77-
213 (in isoform 4)Phosphorylation-64.7424144214
215 (in isoform 4)Phosphorylation-50.3824144214
216DimethylationGLKHEDKRGGSGSHN
CCCCCCCCCCCCCCC		68.01-
216MethylationGLKHEDKRGGSGSHN
CCCCCCCCCCCCCCC		68.0124129315
219PhosphorylationHEDKRGGSGSHNWGT
CCCCCCCCCCCCCCC		39.6923401153
219 (in isoform 3)Phosphorylation-39.6925849741
220 (in isoform 4)Phosphorylation-35.8824144214
221PhosphorylationDKRGGSGSHNWGTVK
CCCCCCCCCCCCCCC		18.4923401153
221 (in isoform 3)Phosphorylation-18.4924144214
226PhosphorylationSGSHNWGTVKDELTE
CCCCCCCCCCCHHHC		18.9223927012
226 (in isoform 3)Phosphorylation-18.9224144214
226 (in isoform 4)Phosphorylation-18.9225159151
228SumoylationSHNWGTVKDELTESP
CCCCCCCCCHHHCCH		45.37-
228AcetylationSHNWGTVKDELTESP
CCCCCCCCCHHHCCH		45.3726051181
228SumoylationSHNWGTVKDELTESP
CCCCCCCCCHHHCCH		45.3725114211
228UbiquitinationSHNWGTVKDELTESP
CCCCCCCCCHHHCCH		45.37-
230 (in isoform 2)Ubiquitination-52.4521890473
231 (in isoform 4)Phosphorylation-10.3826503892
232PhosphorylationGTVKDELTESPKYIQ
CCCCCHHHCCHHHHH		32.1622167270
232 (in isoform 3)Phosphorylation-32.1625159151
234PhosphorylationVKDELTESPKYIQKQ
CCCHHHCCHHHHHHH		22.8129255136
234 (in isoform 2)Ubiquitination-22.81-
234 (in isoform 4)Phosphorylation-22.8126503892
2362-HydroxyisobutyrylationDELTESPKYIQKQIS
CHHHCCHHHHHHHHC		65.35-
236AcetylationDELTESPKYIQKQIS
CHHHCCHHHHHHHHC		65.3523236377
236UbiquitinationDELTESPKYIQKQIS
CHHHCCHHHHHHHHC		65.3521890473
236 (in isoform 1)Ubiquitination-65.3521890473
237PhosphorylationELTESPKYIQKQISY
HHHCCHHHHHHHHCC		16.3923927012
237 (in isoform 3)Phosphorylation-16.3926503892
237 (in isoform 4)Phosphorylation-16.3925159151
240AcetylationESPKYIQKQISYNYS
CCHHHHHHHHCCCCH		39.7926051181
240UbiquitinationESPKYIQKQISYNYS
CCHHHHHHHHCCCCH		39.79-
240 (in isoform 3)Phosphorylation-39.7926503892
243PhosphorylationKYIQKQISYNYSDLD
HHHHHHHCCCCHHCC		12.5821945579
243 (in isoform 3)Phosphorylation-12.5825159151
244PhosphorylationYIQKQISYNYSDLDQ
HHHHHHCCCCHHCCC		21.5421945579
246PhosphorylationQKQISYNYSDLDQSN
HHHHCCCCHHCCCCC		8.7021945579
247PhosphorylationKQISYNYSDLDQSNV
HHHCCCCHHCCCCCC		28.2321945579
249 (in isoform 4)Phosphorylation-5.4720873877
252PhosphorylationNYSDLDQSNVTEETP
CCHHCCCCCCCCCCC		32.6921945579
255PhosphorylationDLDQSNVTEETPEGE
HCCCCCCCCCCCCCC		32.1421945579
255 (in isoform 3)Phosphorylation-32.1420873877
258PhosphorylationQSNVTEETPEGEEHH
CCCCCCCCCCCCCCC		22.0221945579
270PhosphorylationEHHPVADTENKENEV
CCCCCCCCCCCCCCH		31.5521945579
273AcetylationPVADTENKENEVEEV
CCCCCCCCCCCHHHH		56.5426051181
273 (in isoform 4)Ubiquitination-56.5421890473
279 (in isoform 3)Ubiquitination-65.1521890473
281SumoylationENEVEEVKEEGPKEM
CCCHHHHHHHCCCCC		54.02-
281AcetylationENEVEEVKEEGPKEM
CCCHHHHHHHCCCCC		54.0226051181
281SumoylationENEVEEVKEEGPKEM
CCCHHHHHHHCCCCC		54.0228112733
281UbiquitinationENEVEEVKEEGPKEM
CCCHHHHHHHCCCCC		54.02-
286UbiquitinationEVKEEGPKEMTLDEW
HHHHHCCCCCCHHHH		71.61-
288 (in isoform 2)Ubiquitination-5.8721890473
2942-HydroxyisobutyrylationEMTLDEWKAIQNKDR
CCCHHHHHHHHCCCC		33.30-
294AcetylationEMTLDEWKAIQNKDR
CCCHHHHHHHHCCCC		33.3026822725
294UbiquitinationEMTLDEWKAIQNKDR
CCCHHHHHHHHCCCC		33.3021890473
294 (in isoform 1)Ubiquitination-33.3021890473
2992-HydroxyisobutyrylationEWKAIQNKDRAKVEF
HHHHHHCCCCCEEEE		32.01-
299 (in isoform 4)Ubiquitination-32.0121890473
303AcetylationIQNKDRAKVEFNIRK
HHCCCCCEEEEEECC		43.1026051181
303UbiquitinationIQNKDRAKVEFNIRK
HHCCCCCEEEEEECC		43.10-
305 (in isoform 3)Ubiquitination-32.0621890473
310AcetylationKVEFNIRKPNEGADG
EEEEEECCCCCCCCC		48.6926051181
310UbiquitinationKVEFNIRKPNEGADG
EEEEEECCCCCCCCC		48.69-
314 (in isoform 2)Ubiquitination-35.2921890473
3202-HydroxyisobutyrylationEGADGQWKKGFVLHK
CCCCCCEEEEEEEEC		34.82-
320AcetylationEGADGQWKKGFVLHK
CCCCCCEEEEEEEEC		34.8225953088
320UbiquitinationEGADGQWKKGFVLHK
CCCCCCEEEEEEEEC		34.8221906983
320 (in isoform 1)Ubiquitination-34.8221890473
3212-HydroxyisobutyrylationGADGQWKKGFVLHKS
CCCCCEEEEEEEECC		55.40-
321AcetylationGADGQWKKGFVLHKS
CCCCCEEEEEEEECC		55.4026051181
321UbiquitinationGADGQWKKGFVLHKS
CCCCCEEEEEEEECC		55.40-
3272-HydroxyisobutyrylationKKGFVLHKSKSEEAH
EEEEEEECCCCCHHH		56.25-
327AcetylationKKGFVLHKSKSEEAH
EEEEEEECCCCCHHH		56.2525953088
327MethylationKKGFVLHKSKSEEAH
EEEEEEECCCCCHHH		56.25115974577
327UbiquitinationKKGFVLHKSKSEEAH
EEEEEEECCCCCHHH		56.25-
328PhosphorylationKGFVLHKSKSEEAHA
EEEEEECCCCCHHHH		30.5722167270
3292-HydroxyisobutyrylationGFVLHKSKSEEAHAE
EEEEECCCCCHHHHH		67.69-
329AcetylationGFVLHKSKSEEAHAE
EEEEECCCCCHHHHH		67.6926822725
329UbiquitinationGFVLHKSKSEEAHAE
EEEEECCCCCHHHHH		67.69-
330PhosphorylationFVLHKSKSEEAHAED
EEEECCCCCHHHHHH		48.0022167270
338PhosphorylationEEAHAEDSVMDHHFR
CHHHHHHHHHHHHCC		15.7330266825
340SulfoxidationAHAEDSVMDHHFRKP
HHHHHHHHHHHCCCC		4.7421406390
346UbiquitinationVMDHHFRKPANDITS
HHHHHCCCCHHHHCC		47.76-
352PhosphorylationRKPANDITSQLEINF
CCCHHHHCCCCEEEC		17.1823663014
353PhosphorylationKPANDITSQLEINFG
CCHHHHCCCCEEECC		32.8523663014
364MethylationINFGDLGRPGRGGRG
EECCCCCCCCCCCCC		37.4824129315
367MethylationGDLGRPGRGGRGGRG
CCCCCCCCCCCCCCC		47.2624129315
369 (in isoform 4)Ubiquitination-24.5721890473
370MethylationGRPGRGGRGGRGGRG
CCCCCCCCCCCCCCC		47.4124129315
373MethylationGRGGRGGRGGRGRGG
CCCCCCCCCCCCCCC		47.4124396625
375 (in isoform 3)Ubiquitination-27.7521890473
384 (in isoform 2)Ubiquitination-47.3421890473
386PhosphorylationGGRPNRGSRTDKSSA
CCCCCCCCCCCCCCC		28.8618669648
388PhosphorylationRPNRGSRTDKSSASA
CCCCCCCCCCCCCCC		49.8530266825
390AcetylationNRGSRTDKSSASAPD
CCCCCCCCCCCCCCC		45.7725953088
390UbiquitinationNRGSRTDKSSASAPD
CCCCCCCCCCCCCCC		45.772190698
390 (in isoform 1)Ubiquitination-45.7721890473
391PhosphorylationRGSRTDKSSASAPDV
CCCCCCCCCCCCCCC		33.6725159151
392PhosphorylationGSRTDKSSASAPDVD
CCCCCCCCCCCCCCC		31.8025159151
394PhosphorylationRTDKSSASAPDVDDP
CCCCCCCCCCCCCCH		42.1325159151
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 PAIRB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAIRB_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 PAIRB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHD3_HUMANCHD3physical
12505151
FXYD3_HUMANFXYD3physical
16169070
CHD3_HUMANCHD3physical
16169070
VIME_HUMANVIMphysical
16169070
P53_HUMANTP53physical
16455055
TIP_HUMANITFG1physical
21900206
DAXX_HUMANDAXXphysical
16679534
TOPRS_HUMANTOPORSphysical
16679534
SAE2_HUMANUBA2physical
16679534
TDG_HUMANTDGphysical
16679534
PIAS1_HUMANPIAS1physical
16679534
PIAS3_HUMANPIAS3physical
16679534
PIAS4_HUMANPIAS4physical
16679534
A4_HUMANAPPphysical
21832049
RL4_HUMANRPL4physical
22939629
ANM8_HUMANPRMT8physical
23455924
DYHC1_HUMANDYNC1H1physical
22863883
DC1I2_HUMANDYNC1I2physical
22863883
RS24_HUMANRPS24physical
22863883
RS26_HUMANRPS26physical
22863883
RS3_HUMANRPS3physical
22863883
RS6_HUMANRPS6physical
22863883
TSR1_HUMANTSR1physical
22863883
PAIRB_HUMANSERBP1physical
25416956
BASP1_HUMANBASP1physical
26344197
UBIM_HUMANFAUphysical
26344197
OTUB1_HUMANOTUB1physical
26344197
RL37A_HUMANRPL37Aphysical
26344197
WDR5_HUMANWDR5physical
26344197
TBCE_HUMANTBCEphysical
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 PAIRB_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-122; LYS-140 ANDLYS-211, 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-25; SER-234; SER-392 ANDSER-394, 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-234 AND SER-394, 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-25; SER-234; SER-252;THR-255; SER-330 AND SER-394, 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-234, AND MASSSPECTROMETRY.
"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 THR-232 AND SER-252, 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 THR-61; SER-85; SER-197;SER-203; SER-221; SER-234; SER-328 AND SER-330, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232; SER-234; SER-328AND SER-330, AND MASS 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-234, 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-197; SER-234; SER-252AND SER-330, AND MASS SPECTROMETRY.

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