LAP2B_HUMAN - dbPTM
LAP2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LAP2B_HUMAN
UniProt AC P42167
Protein Name Lamina-associated polypeptide 2, isoforms beta/gamma
Gene Name TMPO
Organism Homo sapiens (Human).
Sequence Length 454
Subcellular Localization Nucleus inner membrane
Single-pass type II membrane protein. Tightly associated with the nuclear lamina.
Isoform Zeta: Cytoplasm .
Protein Description May help direct the assembly of the nuclear lamina and thereby help maintain the structural organization of the nuclear envelope. Possible receptor for attachment of lamin filaments to the inner nuclear membrane. May be involved in the control of initiation of DNA replication through its interaction with NAKAP95.; Thymopoietin (TP) and Thymopentin (TP5) may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide..
Protein Sequence MPEFLEDPSVLTKDKLKSELVANNVTLPAGEQRKDVYVQLYLQHLTARNRPPLPAGTNSKGPPDFSSDEEREPTPVLGSGAAAAGRSRAAVGRKATKKTDKPRQEDKDDLDVTELTNEDLLDQLVKYGVNPGPIVGTTRKLYEKKLLKLREQGTESRSSTPLPTISSSAENTRQNGSNDSDRYSDNEEDSKIELKLEKREPLKGRAKTPVTLKQRRVEHNQSYSQAGITETEWTSGSSKGGPLQALTRESTRGSRRTPRKRVETSEHFRIDGPVISESTPIAETIMASSNESLVVNRVTGNFKHASPILPITEFSDIPRRAPKKPLTRAEVGEKTEERRVERDILKEMFPYEASTPTGISASCRRPIKGAAGRPLELSDFRMEESFSSKYVPKYVPLADVKSEKTKKGRSIPVWIKILLFVVVAVFLFLVYQAMETNQVNPFSNFLHVDPRKSN
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
9PhosphorylationPEFLEDPSVLTKDKL
CCCCCCCCCCCHHHH		41.9220068231
12PhosphorylationLEDPSVLTKDKLKSE
CCCCCCCCHHHHHHH		34.7320068231
13SumoylationEDPSVLTKDKLKSEL
CCCCCCCHHHHHHHH		49.02-
17SumoylationVLTKDKLKSELVANN
CCCHHHHHHHHHHCC		47.85-
18PhosphorylationLTKDKLKSELVANNV
CCHHHHHHHHHHCCC		46.75-
26PhosphorylationELVANNVTLPAGEQR
HHHHCCCEECCCCCH		29.19-
50MethylationQHLTARNRPPLPAGT
HHHHHCCCCCCCCCC		28.76115918653
57PhosphorylationRPPLPAGTNSKGPPD
CCCCCCCCCCCCCCC		38.1218669648
59PhosphorylationPLPAGTNSKGPPDFS
CCCCCCCCCCCCCCC		38.5421406692
60UbiquitinationLPAGTNSKGPPDFSS
CCCCCCCCCCCCCCC		76.99-
60AcetylationLPAGTNSKGPPDFSS
CCCCCCCCCCCCCCC		76.9919809475
60UbiquitinationLPAGTNSKGPPDFSS
CCCCCCCCCCCCCCC		76.9921906983
60 (in isoform 1)Ubiquitination-76.9921890473
60 (in isoform 2)Ubiquitination-76.9921890473
66PhosphorylationSKGPPDFSSDEEREP
CCCCCCCCCCCCCCC		44.2318669648
67PhosphorylationKGPPDFSSDEEREPT
CCCCCCCCCCCCCCC		49.3818669648
74PhosphorylationSDEEREPTPVLGSGA
CCCCCCCCCCCCCHH		22.6718691976
79PhosphorylationEPTPVLGSGAAAAGR
CCCCCCCCHHHHHCC		22.5418669648
86MethylationSGAAAAGRSRAAVGR
CHHHHHCCCHHHHCC		20.4515231555
87PhosphorylationGAAAAGRSRAAVGRK
HHHHHCCCHHHHCCC		25.9217287340
88MethylationAAAAGRSRAAVGRKA
HHHHCCCHHHHCCCC		25.79-
96PhosphorylationAAVGRKATKKTDKPR
HHHCCCCCCCCCCCC		35.7917287340
99PhosphorylationGRKATKKTDKPRQED
CCCCCCCCCCCCCCC		51.3017287340
107UbiquitinationDKPRQEDKDDLDVTE
CCCCCCCCCCCCHHH		53.00-
107UbiquitinationDKPRQEDKDDLDVTE
CCCCCCCCCCCCHHH		53.0021906983
107 (in isoform 1)Ubiquitination-53.0021890473
107 (in isoform 2)Ubiquitination-53.0021890473
113PhosphorylationDKDDLDVTELTNEDL
CCCCCCHHHHCCHHH		25.5824719451
116PhosphorylationDLDVTELTNEDLLDQ
CCCHHHHCCHHHHHH		30.26-
126UbiquitinationDLLDQLVKYGVNPGP
HHHHHHHHCCCCCCC		44.90-
127PhosphorylationLLDQLVKYGVNPGPI
HHHHHHHCCCCCCCC		20.87-
137PhosphorylationNPGPIVGTTRKLYEK
CCCCCCCHHHHHHHH		16.7217287340
154PhosphorylationLKLREQGTESRSSTP
HHHHHCCCCCCCCCC		30.4024719451
156PhosphorylationLREQGTESRSSTPLP
HHHCCCCCCCCCCCC		36.9820068231
158PhosphorylationEQGTESRSSTPLPTI
HCCCCCCCCCCCCCC		48.0921406692
158 (in isoform 2)Phosphorylation-48.0921406692
158 (in isoform 3)Phosphorylation-48.0921406692
159PhosphorylationQGTESRSSTPLPTIS
CCCCCCCCCCCCCCC		32.6917081983
159 (in isoform 2)Phosphorylation-32.6921406692
159 (in isoform 3)Phosphorylation-32.6921406692
160PhosphorylationGTESRSSTPLPTISS
CCCCCCCCCCCCCCC		30.0518669648
160 (in isoform 2)Phosphorylation-30.0521406692
160 (in isoform 3)Phosphorylation-30.0521406692
164PhosphorylationRSSTPLPTISSSAEN
CCCCCCCCCCCCCCC		40.9718669648
164 (in isoform 2)Phosphorylation-40.9721406692
164 (in isoform 3)Phosphorylation-40.9721406692
166PhosphorylationSTPLPTISSSAENTR
CCCCCCCCCCCCCCC		22.2518669648
166 (in isoform 2)Phosphorylation-22.2521406692
166 (in isoform 3)Phosphorylation-22.2521406692
167PhosphorylationTPLPTISSSAENTRQ
CCCCCCCCCCCCCCC		29.7121406692
167 (in isoform 2)Phosphorylation-29.7121406692
167 (in isoform 3)Phosphorylation-29.7121406692
168PhosphorylationPLPTISSSAENTRQN
CCCCCCCCCCCCCCC		32.5821406692
168 (in isoform 2)Phosphorylation-32.5821406692
168 (in isoform 3)Phosphorylation-32.5821406692
172PhosphorylationISSSAENTRQNGSND
CCCCCCCCCCCCCCC		25.7418669648
172 (in isoform 2)Phosphorylation-25.7421406692
172 (in isoform 3)Phosphorylation-25.7421406692
177PhosphorylationENTRQNGSNDSDRYS
CCCCCCCCCCCCCCC		45.0422167270
177 (in isoform 2)Phosphorylation-45.0422167270
177 (in isoform 3)Phosphorylation-45.0422167270
180PhosphorylationRQNGSNDSDRYSDNE
CCCCCCCCCCCCCCH		28.3922167270
180 (in isoform 2)Phosphorylation-28.3922167270
180 (in isoform 3)Phosphorylation-28.3922167270
183PhosphorylationGSNDSDRYSDNEEDS
CCCCCCCCCCCHHHC		25.9322167270
183 (in isoform 2)Phosphorylation-25.9322167270
183 (in isoform 3)Phosphorylation-25.9322167270
184PhosphorylationSNDSDRYSDNEEDSK
CCCCCCCCCCHHHCC		34.5522167270
184 (in isoform 2)Phosphorylation-34.5522167270
184 (in isoform 3)Phosphorylation-34.5522167270
190PhosphorylationYSDNEEDSKIELKLE
CCCCHHHCCEEHEEE		38.5222167270
190 (in isoform 2)Phosphorylation-38.5222167270
190 (in isoform 3)Phosphorylation-38.5222167270
207AcetylationEPLKGRAKTPVTLKQ
CCCCCCCCCCCEEHH		52.59-
207AcetylationEPLKGRAKTPVTLKQ
CCCCCCCCCCCEEHH		52.5923749302
207MethylationEPLKGRAKTPVTLKQ
CCCCCCCCCCCEEHH		52.5922647053
208PhosphorylationPLKGRAKTPVTLKQR
CCCCCCCCCCEEHHH		23.2322167270
208 (in isoform 2)Phosphorylation-23.2322167270
208 (in isoform 3)Phosphorylation-23.2322167270
211PhosphorylationGRAKTPVTLKQRRVE
CCCCCCCEEHHHHHH		29.4630266825
211 (in isoform 2)Phosphorylation-29.4630266825
211 (in isoform 3)Phosphorylation-29.4630266825
213UbiquitinationAKTPVTLKQRRVEHN
CCCCCEEHHHHHHCC		32.18-
213UbiquitinationAKTPVTLKQRRVEHN
CCCCCEEHHHHHHCC		32.18-
222PhosphorylationRRVEHNQSYSQAGIT
HHHHCCCCCCCCCCC		31.8825159151
223PhosphorylationRVEHNQSYSQAGITE
HHHCCCCCCCCCCCE		8.6121955146
224PhosphorylationVEHNQSYSQAGITET
HHCCCCCCCCCCCEE		20.8525159151
225 (in isoform 2)Ubiquitination-35.06-
226 (in isoform 2)Phosphorylation-12.8624719451
229PhosphorylationSYSQAGITETEWTSG
CCCCCCCCEEEEECC		35.6223663014
231PhosphorylationSQAGITETEWTSGSS
CCCCCCEEEEECCCC		28.3323663014
234PhosphorylationGITETEWTSGSSKGG
CCCEEEEECCCCCCC		19.5826356563
235PhosphorylationITETEWTSGSSKGGP
CCEEEEECCCCCCCC		37.4425159151
237PhosphorylationETEWTSGSSKGGPLQ
EEEEECCCCCCCCCH		28.7526356563
237 (in isoform 2)Ubiquitination-28.7521890473
238PhosphorylationTEWTSGSSKGGPLQA
EEEECCCCCCCCCHH		38.5526356563
242 (in isoform 2)Phosphorylation-29.9325159151
245 (in isoform 2)Phosphorylation-20.7023401153
246 (in isoform 2)Phosphorylation-2.7520201521
247PhosphorylationGGPLQALTRESTRGS
CCCCHHHCCCCCCCC		35.0923401153
248 (in isoform 2)Phosphorylation-36.4023401153
250PhosphorylationLQALTRESTRGSRRT
CHHHCCCCCCCCCCC		21.8023401153
251PhosphorylationQALTRESTRGSRRTP
HHHCCCCCCCCCCCC		34.0123401153
251 (in isoform 2)Phosphorylation-34.0125159151
253 (in isoform 2)Phosphorylation-26.1225159151
254PhosphorylationTRESTRGSRRTPRKR
CCCCCCCCCCCCCCC		18.4623917254
257PhosphorylationSTRGSRRTPRKRVET
CCCCCCCCCCCCEEC		26.7423882029
259 (in isoform 2)Ubiquitination-38.5121890473
264O-linked_GlycosylationTPRKRVETSEHFRID
CCCCCEECCCCCEEC		36.2423301498
264PhosphorylationTPRKRVETSEHFRID
CCCCCEECCCCCEEC		36.2423401153
265O-linked_GlycosylationPRKRVETSEHFRIDG
CCCCEECCCCCEECC		18.6323301498
265PhosphorylationPRKRVETSEHFRIDG
CCCCEECCCCCEECC		18.6327794612
269 (in isoform 2)Phosphorylation-28.1719664994
276PhosphorylationRIDGPVISESTPIAE
EECCCEECCCCCHHH		26.2330108239
276 (in isoform 2)Phosphorylation-26.2322167270
278PhosphorylationDGPVISESTPIAETI
CCCEECCCCCHHHHH		32.4730108239
278 (in isoform 2)Phosphorylation-32.4723401153
279PhosphorylationGPVISESTPIAETIM
CCEECCCCCHHHHHH		18.0525159151
279 (in isoform 2)Phosphorylation-18.0522167270
280 (in isoform 2)Ubiquitination-32.8321890473
281 (in isoform 2)Phosphorylation-5.6830108239
284PhosphorylationESTPIAETIMASSNE
CCCCHHHHHHHCCCC		13.6630108239
284 (in isoform 2)Ubiquitination-13.6621890473
285 (in isoform 2)Phosphorylation-1.3128796482
288PhosphorylationIAETIMASSNESLVV
HHHHHHHCCCCCEEE		19.1330108239
289PhosphorylationAETIMASSNESLVVN
HHHHHHCCCCCEEEE		34.7730108239
292PhosphorylationIMASSNESLVVNRVT
HHHCCCCCEEEEEEE		30.6225159151
292 (in isoform 2)Ubiquitination-30.6221890473
293 (in isoform 2)Phosphorylation-3.9823401153
299PhosphorylationSLVVNRVTGNFKHAS
CEEEEEEECCCCCCC		24.1424732914
303MethylationNRVTGNFKHASPILP
EEEECCCCCCCCCCC		42.1124791321
303UbiquitinationNRVTGNFKHASPILP
EEEECCCCCCCCCCC		42.1121890473
303 (in isoform 1)Ubiquitination-42.1121890473
306PhosphorylationTGNFKHASPILPITE
ECCCCCCCCCCCCCC		16.5222167270
312PhosphorylationASPILPITEFSDIPR
CCCCCCCCCCCCCCC		29.1023927012
315PhosphorylationILPITEFSDIPRRAP
CCCCCCCCCCCCCCC		28.5325159151
320CitrullinationEFSDIPRRAPKKPLT
CCCCCCCCCCCCCCC		50.30-
320CitrullinationEFSDIPRRAPKKPLT
CCCCCCCCCCCCCCC		50.30-
323UbiquitinationDIPRRAPKKPLTRAE
CCCCCCCCCCCCHHH		67.07-
324UbiquitinationIPRRAPKKPLTRAEV
CCCCCCCCCCCHHHC		44.17-
334AcetylationTRAEVGEKTEERRVE
CHHHCCCHHHHHHHH		56.1470721
334UbiquitinationTRAEVGEKTEERRVE
CHHHCCCHHHHHHHH		56.1421906983
334 (in isoform 1)Ubiquitination-56.1421890473
335PhosphorylationRAEVGEKTEERRVER
HHHCCCHHHHHHHHH		38.4828985074
346UbiquitinationRVERDILKEMFPYEA
HHHHHHHHHHCCCCC		47.6821890473
346 (in isoform 1)Ubiquitination-47.6821890473
348SulfoxidationERDILKEMFPYEAST
HHHHHHHHCCCCCCC		3.8121406390
351PhosphorylationILKEMFPYEASTPTG
HHHHHCCCCCCCCCC		16.9225159151
354PhosphorylationEMFPYEASTPTGISA
HHCCCCCCCCCCCCH		23.9923401153
355PhosphorylationMFPYEASTPTGISAS
HCCCCCCCCCCCCHH		31.7320201521
357PhosphorylationPYEASTPTGISASCR
CCCCCCCCCCCHHHC		47.4323401153
360PhosphorylationASTPTGISASCRRPI
CCCCCCCCHHHCCCC		18.5725159151
362PhosphorylationTPTGISASCRRPIKG
CCCCCCHHHCCCCCC		11.0225159151
363GlutathionylationPTGISASCRRPIKGA
CCCCCHHHCCCCCCC		4.2322555962
368UbiquitinationASCRRPIKGAAGRPL
HHHCCCCCCCCCCCC		45.2221906983
368 (in isoform 1)Ubiquitination-45.2221890473
378PhosphorylationAGRPLELSDFRMEES
CCCCCCHHHHCCCHH		25.9019664994
385PhosphorylationSDFRMEESFSSKYVP
HHHCCCHHHCCCCCC		19.6822167270
387PhosphorylationFRMEESFSSKYVPKY
HCCCHHHCCCCCCCC		34.8923401153
388PhosphorylationRMEESFSSKYVPKYV
CCCHHHCCCCCCCCC		26.4522167270
389AcetylationMEESFSSKYVPKYVP
CCHHHCCCCCCCCCC		49.41-
389UbiquitinationMEESFSSKYVPKYVP
CCHHHCCCCCCCCCC		49.4121890473
389 (in isoform 1)Ubiquitination-49.4121890473
390PhosphorylationEESFSSKYVPKYVPL
CHHHCCCCCCCCCCH		24.7530108239
393AcetylationFSSKYVPKYVPLADV
HCCCCCCCCCCHHHC		49.1623236377
393UbiquitinationFSSKYVPKYVPLADV
HCCCCCCCCCCHHHC		49.1621890473
393 (in isoform 1)Ubiquitination-49.1621890473
394PhosphorylationSSKYVPKYVPLADVK
CCCCCCCCCCHHHCC		10.9628796482
401SumoylationYVPLADVKSEKTKKG
CCCHHHCCCCCCCCC		54.1428112733
401UbiquitinationYVPLADVKSEKTKKG
CCCHHHCCCCCCCCC		54.1421890473
401 (in isoform 1)Ubiquitination-54.1421890473
402PhosphorylationVPLADVKSEKTKKGR
CCHHHCCCCCCCCCC		44.1423401153
404UbiquitinationLADVKSEKTKKGRSI
HHHCCCCCCCCCCCH		73.13-
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 LAP2B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAP2B_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 LAP2B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RB_HUMANRB1physical
12475961
LMNA_HUMANLMNAphysical
12475961
LMNA_HUMANLMNAphysical
10984438
AKP8L_HUMANAKAP8Lphysical
12538639
BAF_HUMANBANF1physical
10393804
LMNB1_HUMANLMNB1physical
9490046
LMNB2_HUMANLMNB2physical
9490046
LMNB1_HUMANLMNB1physical
8324822
HDAC3_HUMANHDAC3physical
16129885
MS18B_HUMANOIP5physical
17284516
PCGF2_HUMANPCGF2physical
19727227
LMNA_HUMANLMNAphysical
19727227
MRE11_HUMANMRE11Aphysical
22939629
SYLC_HUMANLARSphysical
26344197
ATRX_HUMANATRXphysical
26496610
BST2_HUMANBST2physical
26496610
CHD1_HUMANCHD1physical
26496610
STOM_HUMANSTOMphysical
26496610
PGBM_HUMANHSPG2physical
26496610
DNLI3_HUMANLIG3physical
26496610
LMNA_HUMANLMNAphysical
26496610
LMNB1_HUMANLMNB1physical
26496610
PHB_HUMANPHBphysical
26496610
RRBP1_HUMANRRBP1physical
26496610
SDC2_HUMANSDC2physical
26496610
SPT6H_HUMANSUPT6Hphysical
26496610
TBG1_HUMANTUBG1physical
26496610
UBF1_HUMANUBTFphysical
26496610
SYVC_HUMANVARSphysical
26496610
AF10_HUMANMLLT10physical
26496610
HIRP3_HUMANHIRIP3physical
26496610
VA0D1_HUMANATP6V0D1physical
26496610
NOLC1_HUMANNOLC1physical
26496610
KAT7_HUMANKAT7physical
26496610
RL35_HUMANRPL35physical
26496610
PHB2_HUMANPHB2physical
26496610
EXOS8_HUMANEXOSC8physical
26496610
BRD1_HUMANBRD1physical
26496610
NUSAP_HUMANNUSAP1physical
26496610
PHIP_HUMANPHIPphysical
26496610
JADE1_HUMANJADE1physical
26496610
CAVN3_HUMANPRKCDBPphysical
26496610
SMS2_HUMANSGMS2physical
26496610
Drug and Disease Associations
Kegg Disease
H00294 Dilated cardiomyopathy (DCM)
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 LAP2B_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-207, 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-292 AND SER-306, 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-57; SER-66; SER-67;THR-74; SER-79; SER-156; THR-160; THR-164; SER-177; SER-180; THR-208;THR-211; SER-306; SER-315; SER-354; SER-362; SER-378 AND SER-385, ANDMASS 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-66; SER-67; THR-74 ANDSER-306, AND MASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 AND SER-184, 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-66; SER-67; THR-74;THR-137; SER-306; SER-315 AND SER-378, AND MASS 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-66; SER-67; SER-79;THR-96; THR-99; THR-137; SER-159 AND THR-160, AND MASS SPECTROMETRY.
"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-306, 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 THR-208; SER-306 ANDSER-378, AND MASS 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-184; SER-306 ANDSER-378, 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 THR-355, AND MASSSPECTROMETRY.

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