XRN2_HUMAN - dbPTM
XRN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XRN2_HUMAN
UniProt AC Q9H0D6
Protein Name 5'-3' exoribonuclease 2
Gene Name XRN2
Organism Homo sapiens (Human).
Sequence Length 950
Subcellular Localization Nucleus, nucleolus .
Protein Description Possesses 5'->3' exoribonuclease activity (By similarity). May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5' fragment which is subsequently processed to form the mature mRNA and a 3' fragment which remains attached to the elongating polymerase. The processive degradation of this 3' fragment by this protein may promote termination of transcription. Binds to RNA polymerase II (RNAp II) transcription termination R-loops formed by G-rich pause sites. [PubMed: 21700224]
Protein Sequence MGVPAFFRWLSRKYPSIIVNCVEEKPKECNGVKIPVDASKPNPNDVEFDNLYLDMNGIIHPCTHPEDKPAPKNEDEMMVAIFEYIDRLFSIVRPRRLLYMAIDGVAPRAKMNQQRSRRFRASKEGMEAAVEKQRVREEILAKGGFLPPEEIKERFDSNCITPGTEFMDNLAKCLRYYIADRLNNDPGWKNLTVILSDASAPGEGEHKIMDYIRRQRAQPNHDPNTHHCLCGADADLIMLGLATHEPNFTIIREEFKPNKPKPCGLCNQFGHEVKDCEGLPREKKGKHDELADSLPCAEGEFIFLRLNVLREYLERELTMASLPFTFDVERSIDDWVFMCFFVGNDFLPHLPSLEIRENAIDRLVNIYKNVVHKTGGYLTESGYVNLQRVQMIMLAVGEVEDSIFKKRKDDEDSFRRRQKEKRKRMKRDQPAFTPSGILTPHALGSRNSPGSQVASNPRQAAYEMRMQNNSSPSISPNTSFTSDGSPSPLGGIKRKAEDSDSEPEPEDNVRLWEAGWKQRYYKNKFDVDAADEKFRRKVVQSYVEGLCWVLRYYYQGCASWKWYYPFHYAPFASDFEGIADMPSDFEKGTKPFKPLEQLMGVFPAASGNFLPPSWRKLMSDPDSSIIDFYPEDFAIDLNGKKYAWQGVALLPFVDERRLRAALEEVYPDLTPEETRRNSLGGDVLFVGKHHPLHDFILELYQTGSTEPVEVPPELCHGIQGKFSLDEEAILPDQIVCSPVPMLRDLTQNTVVSINFKDPQFAEDYIFKAVMLPGARKPAAVLKPSDWEKSSNGRQWKPQLGFNRDRRPVHLDQAAFRTLGHVMPRGSGTGIYSNAAPPPVTYQGNLYRPLLRGQAQIPKLMSNMRPQDSWRGPPPLFQQQRFDRGVGAEPLLPWNRMLQTQNAAFQPNQYQMLAGPGGYPPRRDDRGGRQGYPREGRKYPLPPPSGRYNWN
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
13AcetylationFFRWLSRKYPSIIVN
HHHHHHHHCCEEEEE		59.1326051181
14PhosphorylationFRWLSRKYPSIIVNC
HHHHHHHCCEEEEEC		10.9128152594
16PhosphorylationWLSRKYPSIIVNCVE
HHHHHCCEEEEECCC		23.1228152594
25AcetylationIVNCVEEKPKECNGV
EEECCCCCCCCCCCE		48.1325953088
27AcetylationNCVEEKPKECNGVKI
ECCCCCCCCCCCEEC		82.8426051181
40UbiquitinationKIPVDASKPNPNDVE
ECCCCCCCCCCCCCC		51.00-
40AcetylationKIPVDASKPNPNDVE
ECCCCCCCCCCCCCC		51.0026051181
56 (in isoform 2)Ubiquitination-37.8721890473
68AcetylationPCTHPEDKPAPKNED
CCCCCCCCCCCCCCH		41.2225953088
99PhosphorylationVRPRRLLYMAIDGVA
HCHHHHHHHHHCCCC		6.78-
113 (in isoform 2)Ubiquitination-36.2421890473
120DimethylationQQRSRRFRASKEGME
HHHHHHHHHCHHHHH		35.82-
120MethylationQQRSRRFRASKEGME
HHHHHHHHHCHHHHH		35.8224390299
123UbiquitinationSRRFRASKEGMEAAV
HHHHHHCHHHHHHHH		58.25-
132SumoylationGMEAAVEKQRVREEI
HHHHHHHHHHHHHHH		36.48-
132UbiquitinationGMEAAVEKQRVREEI
HHHHHHHHHHHHHHH		36.4821906983
132SumoylationGMEAAVEKQRVREEI
HHHHHHHHHHHHHHH		36.48-
132 (in isoform 1)Ubiquitination-36.4821890473
142UbiquitinationVREEILAKGGFLPPE
HHHHHHHCCCCCCHH		57.00-
152UbiquitinationFLPPEEIKERFDSNC
CCCHHHHHHHHHCCC		46.23-
159GlutathionylationKERFDSNCITPGTEF
HHHHHCCCCCCCHHH		4.1922555962
172UbiquitinationEFMDNLAKCLRYYIA
HHHHHHHHHHHHHHH		36.65-
176PhosphorylationNLAKCLRYYIADRLN
HHHHHHHHHHHHHHC		6.0522817900
177PhosphorylationLAKCLRYYIADRLNN
HHHHHHHHHHHHHCC		5.3422817900
189UbiquitinationLNNDPGWKNLTVILS
HCCCCCCCCEEEEEE		48.2521906983
189 (in isoform 1)Ubiquitination-48.2521890473
192PhosphorylationDPGWKNLTVILSDAS
CCCCCCEEEEEECCC		18.2020068231
196PhosphorylationKNLTVILSDASAPGE
CCEEEEEECCCCCCC		21.7320068231
207UbiquitinationAPGEGEHKIMDYIRR
CCCCCHHHHHHHHHH		35.11-
284UbiquitinationEGLPREKKGKHDELA
CCCCCCCCCCCCHHH		69.32-
284AcetylationEGLPREKKGKHDELA
CCCCCCCCCCCCHHH		69.3226051181
286AcetylationLPREKKGKHDELADS
CCCCCCCCCCHHHHH		57.6826051181
286UbiquitinationLPREKKGKHDELADS
CCCCCCCCCCHHHHH		57.68-
296GlutathionylationELADSLPCAEGEFIF
HHHHHCCCCCCCEEH		6.9822555962
297 (in isoform 2)Ubiquitination-26.37-
319SulfoxidationYLERELTMASLPFTF
HHHHHCHHCCCCEEE		3.5921406390
352PhosphorylationDFLPHLPSLEIRENA
CCCCCCCCHHHHHHH		45.0224719451
368UbiquitinationDRLVNIYKNVVHKTG
HHHHHHHHHCHHHCC		39.20-
373UbiquitinationIYKNVVHKTGGYLTE
HHHHCHHHCCCCCCC		36.94-
373AcetylationIYKNVVHKTGGYLTE
HHHHCHHHCCCCCCC		36.9426051181
374PhosphorylationYKNVVHKTGGYLTES
HHHCHHHCCCCCCCC		22.44-
379PhosphorylationHKTGGYLTESGYVNL
HHCCCCCCCCCCCCH		21.44-
402PhosphorylationAVGEVEDSIFKKRKD
HHCCCCHHHHHHCCC		19.2024719451
417 (in isoform 2)Ubiquitination-47.9021890473
433PhosphorylationKRDQPAFTPSGILTP
CCCCCCCCCCCCCCC		20.7423927012
435PhosphorylationDQPAFTPSGILTPHA
CCCCCCCCCCCCCCC		35.0930266825
439PhosphorylationFTPSGILTPHALGSR
CCCCCCCCCCCCCCC		15.8823927012
445PhosphorylationLTPHALGSRNSPGSQ
CCCCCCCCCCCCCCC		29.1923927012
448PhosphorylationHALGSRNSPGSQVAS
CCCCCCCCCCCCCCC		29.5429255136
448 (in isoform 2)Ubiquitination-29.5421890473
451PhosphorylationGSRNSPGSQVASNPR
CCCCCCCCCCCCCHH		25.5122167270
455PhosphorylationSPGSQVASNPRQAAY
CCCCCCCCCHHHHHH		48.8125159151
457 (in isoform 2)Ubiquitination-27.5421890473
458MethylationSQVASNPRQAAYEMR
CCCCCCHHHHHHHHH		42.91115920133
462PhosphorylationSNPRQAAYEMRMQNN
CCHHHHHHHHHHHCC		17.1826074081
470PhosphorylationEMRMQNNSSPSISPN
HHHHHCCCCCCCCCC		51.6929255136
471PhosphorylationMRMQNNSSPSISPNT
HHHHCCCCCCCCCCC		25.4529255136
473PhosphorylationMQNNSSPSISPNTSF
HHCCCCCCCCCCCCC		37.3329255136
475PhosphorylationNNSSPSISPNTSFTS
CCCCCCCCCCCCCCC		19.2129255136
478PhosphorylationSPSISPNTSFTSDGS
CCCCCCCCCCCCCCC		28.7129255136
479PhosphorylationPSISPNTSFTSDGSP
CCCCCCCCCCCCCCC		32.9229255136
481PhosphorylationISPNTSFTSDGSPSP
CCCCCCCCCCCCCCC		26.1930266825
482PhosphorylationSPNTSFTSDGSPSPL
CCCCCCCCCCCCCCC		37.6530266825
485PhosphorylationTSFTSDGSPSPLGGI
CCCCCCCCCCCCCCC		27.4823401153
487PhosphorylationFTSDGSPSPLGGIKR
CCCCCCCCCCCCCCC		34.1629255136
493UbiquitinationPSPLGGIKRKAEDSD
CCCCCCCCCCCCCCC		51.6321906983
493AcetylationPSPLGGIKRKAEDSD
CCCCCCCCCCCCCCC		51.6325953088
493 (in isoform 1)Ubiquitination-51.6321890473
499PhosphorylationIKRKAEDSDSEPEPE
CCCCCCCCCCCCCCH		34.2429255136
501PhosphorylationRKAEDSDSEPEPEDN
CCCCCCCCCCCCHHH		60.0329255136
517UbiquitinationRLWEAGWKQRYYKNK
HHHHHHHHHHHHCCC		24.79-
522UbiquitinationGWKQRYYKNKFDVDA
HHHHHHHCCCCCCHH		44.73-
524MethylationKQRYYKNKFDVDAAD
HHHHHCCCCCCHHHC		38.5042377321
524UbiquitinationKQRYYKNKFDVDAAD
HHHHHCCCCCCHHHC		38.5021906983
524AcetylationKQRYYKNKFDVDAAD
HHHHHCCCCCCHHHC		38.5026051181
524 (in isoform 1)Ubiquitination-38.5021890473
533UbiquitinationDVDAADEKFRRKVVQ
CCHHHCHHHHHHHHH		44.7221890473
5332-HydroxyisobutyrylationDVDAADEKFRRKVVQ
CCHHHCHHHHHHHHH		44.72-
533AcetylationDVDAADEKFRRKVVQ
CCHHHCHHHHHHHHH		44.7226051181
533 (in isoform 1)Ubiquitination-44.7221890473
537UbiquitinationADEKFRRKVVQSYVE
HCHHHHHHHHHHHHH		42.37-
559PhosphorylationYYYQGCASWKWYYPF
HHHCCCCCCEEECCC		33.0124719451
564 (in isoform 2)Ubiquitination-9.7921890473
613PhosphorylationSGNFLPPSWRKLMSD
CCCCCCHHHHHHHCC		37.2626091039
616UbiquitinationFLPPSWRKLMSDPDS
CCCHHHHHHHCCCCC		42.13-
640AcetylationFAIDLNGKKYAWQGV
EEEECCCCEEEEEEE		41.3523954790
640UbiquitinationFAIDLNGKKYAWQGV
EEEECCCCEEEEEEE		41.3521906983
640 (in isoform 1)Ubiquitination-41.3521890473
641UbiquitinationAIDLNGKKYAWQGVA
EEECCCCEEEEEEEE		41.41-
641AcetylationAIDLNGKKYAWQGVA
EEECCCCEEEEEEEE		41.4126051181
666PhosphorylationRAALEEVYPDLTPEE
HHHHHHHCCCCCHHH		8.3623312004
670PhosphorylationEEVYPDLTPEETRRN
HHHCCCCCHHHHHHH		35.7128348404
674PhosphorylationPDLTPEETRRNSLGG
CCCCHHHHHHHCCCC		33.0123312004
678PhosphorylationPEETRRNSLGGDVLF
HHHHHHHCCCCCEEE		26.9523401153
680 (in isoform 2)Ubiquitination-30.0321890473
691 (in isoform 2)Ubiquitination-30.9821890473
756UbiquitinationTVVSINFKDPQFAED
EEEEEEECCHHHHHH		65.1021906983
756 (in isoform 1)Ubiquitination-65.1021890473
764PhosphorylationDPQFAEDYIFKAVML
CHHHHHHHHHEEEEC		10.36-
764NitrationDPQFAEDYIFKAVML
CHHHHHHHHHEEEEC		10.36-
767UbiquitinationFAEDYIFKAVMLPGA
HHHHHHHEEEECCCC		30.432190698
767 (in isoform 1)Ubiquitination-30.4321890473
776UbiquitinationVMLPGARKPAAVLKP
EECCCCCCCCEECCH		38.17-
782UbiquitinationRKPAAVLKPSDWEKS
CCCCEECCHHHHCCC		35.56-
782AcetylationRKPAAVLKPSDWEKS
CCCCEECCHHHHCCC		35.5626051181
789PhosphorylationKPSDWEKSSNGRQWK
CHHHHCCCCCCCCCC		19.95-
790PhosphorylationPSDWEKSSNGRQWKP
HHHHCCCCCCCCCCC		55.14-
796AcetylationSSNGRQWKPQLGFNR
CCCCCCCCCCCCCCC		17.9723954790
796UbiquitinationSSNGRQWKPQLGFNR
CCCCCCCCCCCCCCC		17.9719608861
806MethylationLGFNRDRRPVHLDQA
CCCCCCCCCCCHHHH		41.71115920137
816MethylationHLDQAAFRTLGHVMP
CHHHHHHHHHCCCCC		25.0654560631
817PhosphorylationLDQAAFRTLGHVMPR
HHHHHHHHHCCCCCC		30.5527174698
824Asymmetric dimethylarginineTLGHVMPRGSGTGIY
HHCCCCCCCCCCCCC		33.54-
824MethylationTLGHVMPRGSGTGIY
HHCCCCCCCCCCCCC		33.5424129315
826PhosphorylationGHVMPRGSGTGIYSN
CCCCCCCCCCCCCCC		34.1727174698
828PhosphorylationVMPRGSGTGIYSNAA
CCCCCCCCCCCCCCC		23.3127174698
831PhosphorylationRGSGTGIYSNAAPPP
CCCCCCCCCCCCCCC		9.3827174698
832PhosphorylationGSGTGIYSNAAPPPV
CCCCCCCCCCCCCCE		20.3327174698
840PhosphorylationNAAPPPVTYQGNLYR
CCCCCCEEECCCCCH		18.8527174698
841PhosphorylationAAPPPVTYQGNLYRP
CCCCCEEECCCCCHH		18.0427174698
846PhosphorylationVTYQGNLYRPLLRGQ
EEECCCCCHHHHHCC		17.7427174698
847Asymmetric dimethylarginineTYQGNLYRPLLRGQA
EECCCCCHHHHHCCC		20.68-
847MethylationTYQGNLYRPLLRGQA
EECCCCCHHHHHCCC		20.6824129315
851Asymmetric dimethylarginineNLYRPLLRGQAQIPK
CCCHHHHHCCCCCCH		42.75-
851MethylationNLYRPLLRGQAQIPK
CCCHHHHHCCCCCCH		42.7524129315
858MethylationRGQAQIPKLMSNMRP
HCCCCCCHHHHCCCC		59.45115920129
861PhosphorylationAQIPKLMSNMRPQDS
CCCCHHHHCCCCCCC		37.6020068231
864DimethylationPKLMSNMRPQDSWRG
CHHHHCCCCCCCCCC		29.94-
864MethylationPKLMSNMRPQDSWRG
CHHHHCCCCCCCCCC		29.9454560639
870DimethylationMRPQDSWRGPPPLFQ
CCCCCCCCCCCCCHH		52.25-
870MethylationMRPQDSWRGPPPLFQ
CCCCCCCCCCCCCHH		52.2554560655
880Asymmetric dimethylargininePPLFQQQRFDRGVGA
CCCHHHHCCCCCCCC		30.97-
880MethylationPPLFQQQRFDRGVGA
CCCHHHHCCCCCCCC		30.9754560671
883Asymmetric dimethylarginineFQQQRFDRGVGAEPL
HHHHCCCCCCCCCCC		38.70-
883MethylationFQQQRFDRGVGAEPL
HHHHCCCCCCCCCCC		38.7024129315
895MethylationEPLLPWNRMLQTQNA
CCCCCHHHHHHHCCC		24.2624129315
921DimethylationGPGGYPPRRDDRGGR
CCCCCCCCCCCCCCC		50.59-
921MethylationGPGGYPPRRDDRGGR
CCCCCCCCCCCCCCC		50.5926494099
922DimethylationPGGYPPRRDDRGGRQ
CCCCCCCCCCCCCCC		56.83-
922MethylationPGGYPPRRDDRGGRQ
CCCCCCCCCCCCCCC		56.8330761565
925DimethylationYPPRRDDRGGRQGYP
CCCCCCCCCCCCCCC		54.47-
925MethylationYPPRRDDRGGRQGYP
CCCCCCCCCCCCCCC		54.4781121143
928DimethylationRRDDRGGRQGYPREG
CCCCCCCCCCCCCCC		29.58-
928MethylationRRDDRGGRQGYPREG
CCCCCCCCCCCCCCC		29.5880700641
931PhosphorylationDRGGRQGYPREGRKY
CCCCCCCCCCCCCCC		7.2622461510
933MethylationGGRQGYPREGRKYPL
CCCCCCCCCCCCCCC		50.9854560623
944PhosphorylationKYPLPPPSGRYNWN-
CCCCCCCCCCCCCC-		41.5028555341
946Asymmetric dimethylargininePLPPPSGRYNWN---
CCCCCCCCCCCC---		26.42-
946MethylationPLPPPSGRYNWN---
CCCCCCCCCCCC---		26.4224129315
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
439TPhosphorylationKinaseCDK7P50613
PSP
439TPhosphorylationKinaseCDK9P50750
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of XRN2_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 XRN2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOLIP_HUMANTOLLIPphysical
15231747
EIF3L_HUMANEIF3Lphysical
15231747
EF1A1_HUMANEEF1A1physical
15231747
ATRN_HUMANATRNphysical
15231747
CATC_HUMANCTSCphysical
15231747
IF6_HUMANEIF6physical
15231747
IF5A1_HUMANEIF5Aphysical
15231747
PARPT_HUMANTIPARPphysical
15231747
COMT_HUMANCOMTphysical
15231747
MOCS3_HUMANMOCS3physical
15231747
AL1B1_HUMANALDH1B1physical
15231747
PRAME_HUMANPRAMEphysical
15231747
RT10_HUMANMRPS10physical
15231747
RM04_HUMANMRPL4physical
15231747
DXO_HUMANDXOphysical
15231747
EXOS8_HUMANEXOSC8physical
15231747
EXOSX_HUMANEXOSC10physical
15231747
PSA3_HUMANPSMA3physical
15231747
TADBP_HUMANTARDBPphysical
15231747
C2AIL_HUMANCDKN2AIPNLphysical
24778252
IMA7_HUMANKPNA6physical
24778252
DHX8_HUMANDHX8physical
24778252
RPB1_HUMANPOLR2Aphysical
24778252
IMA5_HUMANKPNA1physical
24778252
NKRF_HUMANNKRFphysical
24778252
CARF_HUMANCDKN2AIPphysical
24778252
RPB2_HUMANPOLR2Bphysical
24778252
CFA58_HUMANCFAP58physical
26344197
MCFD2_HUMANMCFD2physical
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 XRN2_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-796, 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-448; SER-471; SER-473;SER-475; SER-499 AND SER-501, AND MASS SPECTROMETRY.
"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-448; SER-499 ANDSER-501, 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-448; SER-473; SER-475;SER-499 AND SER-501, AND MASS 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-499 AND SER-501, 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 THR-439; SER-448; SER-499AND SER-501, 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-448, 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 SER-448, AND MASSSPECTROMETRY.
"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 SER-448, AND MASSSPECTROMETRY.
"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-448 AND SER-455, ANDMASS SPECTROMETRY.
"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-448; SER-499 ANDSER-501, AND MASS 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-501, AND MASSSPECTROMETRY.
"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-448; SER-499 ANDSER-501, AND MASS SPECTROMETRY.

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