RRP12_HUMAN - dbPTM
RRP12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RRP12_HUMAN
UniProt AC Q5JTH9
Protein Name RRP12-like protein
Gene Name RRP12
Organism Homo sapiens (Human).
Sequence Length 1297
Subcellular Localization Nucleus, nucleolus . Nucleus membrane
Single-pass membrane protein .
Protein Description
Protein Sequence MGRSGKLPSGVSAKLKRWKKGHSSDSNPAICRHRQAARSRFFSRPSGRSDLTVDAVKLHNELQSGSLRLGKSEAPETPMEEEAELVLTEKSSGTFLSGLSDCTNVTFSKVQRFWESNSAAHKEICAVLAAVTEVIRSQGGKETETEYFAALMTTMEAVESPESLAAVAYLLNLVLKRVPSPVLIKKFSDTSKAFMDIMSAQASSGSTSVLRWVLSCLATLLRKQDLEAWGYPVTLQVYHGLLSFTVHPKPKIRKAAQHGVCSVLKGSEFMFEKAPAHHPAAISTAKFCIQEIEKSGGSKEATTTLHMLTLLKDLLPCFPEGLVKSCSETLLRVMTLSHVLVTACAMQAFHSLFHARPGLSTLSAELNAQIITALYDYVPSENDLQPLLAWLKVMEKAHINLVRLQWDLGLGHLPRFFGTAVTCLLSPHSQVLTAATQSLKEILKECVAPHMADIGSVTSSASGPAQSVAKMFRAVEEGLTYKFHAAWSSVLQLLCVFFEACGRQAHPVMRKCLQSLCDLRLSPHFPHTAALDQAVGAAVTSMGPEVVLQAVPLEIDGSEETLDFPRSWLLPVIRDHVQETRLGFFTTYFLPLANTLKSKAMDLAQAGSTVESKIYDTLQWQMWTLLPGFCTRPTDVAISFKGLARTLGMAISERPDLRVTVCQALRTLITKGCQAEADRAEVSRFAKNFLPILFNLYGQPVAAGDTPAPRRAVLETIRTYLTITDTQLVNSLLEKASEKVLDPASSDFTRLSVLDLVVALAPCADEAAISKLYSTIRPYLESKAHGVQKKAYRVLEEVCASPQGPGALFVQSHLEDLKKTLLDSLRSTSSPAKRPRLKCLLHIVRKLSAEHKEFITALIPEVILCTKEVSVGARKNAFALLVEMGHAFLRFGSNQEEALQCYLVLIYPGLVGAVTMVSCSILALTHLLFEFKGLMGTSTVEQLLENVCLLLASRTRDVVKSALGFIKVAVTVMDVAHLAKHVQLVMEAIGKLSDDMRRHFRMKLRNLFTKFIRKFGFELVKRLLPEEYHRVLVNIRKAEARAKRHRALSQAAVEEEEEEEEEEEPAQGKGDSIEEILADSEDEEDNEEEERSRGKEQRKLARQRSRAWLKEGGGDEPLNFLDPKVAQRVLATQPGPGRGRKKDHGFKVSADGRLIIREEADGNKMEEEEGAKGEDEEMADPMEDVIIRNKKHQKLKHQKEAEEEELEIPPQYQAGGSGIHRPVAKKAMPGAEYKAKKAKGDVKKKGRPDPYAYIPLNRSKLNRRKKMKLQGQFKGLVKAARRGSQVGHKNRRKDRRP
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
4Phosphorylation----MGRSGKLPSGV
----CCCCCCCCCCH
51.6620068231
6Acetylation--MGRSGKLPSGVSA
--CCCCCCCCCCHHH
59.4825953088
6Ubiquitination--MGRSGKLPSGVSA
--CCCCCCCCCCHHH
59.48-
9PhosphorylationGRSGKLPSGVSAKLK
CCCCCCCCCHHHHHH
63.3620068231
12PhosphorylationGKLPSGVSAKLKRWK
CCCCCCHHHHHHHHH
24.1820068231
14AcetylationLPSGVSAKLKRWKKG
CCCCHHHHHHHHHCC
47.2223954790
14UbiquitinationLPSGVSAKLKRWKKG
CCCCHHHHHHHHHCC
47.22-
23PhosphorylationKRWKKGHSSDSNPAI
HHHHCCCCCCCCHHH
44.5026434776
24PhosphorylationRWKKGHSSDSNPAIC
HHHCCCCCCCCHHHH
39.1126434776
26PhosphorylationKKGHSSDSNPAICRH
HCCCCCCCCHHHHHH
46.8126434776
39PhosphorylationRHRQAARSRFFSRPS
HHHHHHHHHHCCCCC
28.8128555341
46PhosphorylationSRFFSRPSGRSDLTV
HHHCCCCCCCCCCEE
45.8120860994
49PhosphorylationFSRPSGRSDLTVDAV
CCCCCCCCCCEEEHH
40.2619060867
52PhosphorylationPSGRSDLTVDAVKLH
CCCCCCCEEEHHHHH
22.7221815630
572-HydroxyisobutyrylationDLTVDAVKLHNELQS
CCEEEHHHHHHHHHH
45.83-
57AcetylationDLTVDAVKLHNELQS
CCEEEHHHHHHHHHH
45.8326051181
57UbiquitinationDLTVDAVKLHNELQS
CCEEEHHHHHHHHHH
45.83-
64PhosphorylationKLHNELQSGSLRLGK
HHHHHHHHCCCEECC
42.8730266825
66PhosphorylationHNELQSGSLRLGKSE
HHHHHHCCCEECCCC
18.6330266825
71AcetylationSGSLRLGKSEAPETP
HCCCEECCCCCCCCC
50.1126051181
71SumoylationSGSLRLGKSEAPETP
HCCCEECCCCCCCCC
50.1125114211
71UbiquitinationSGSLRLGKSEAPETP
HCCCEECCCCCCCCC
50.1121906983
71 (in isoform 1)Ubiquitination-50.1121906983
71 (in isoform 2)Ubiquitination-50.1121906983
72PhosphorylationGSLRLGKSEAPETPM
CCCEECCCCCCCCCC
36.8725159151
77PhosphorylationGKSEAPETPMEEEAE
CCCCCCCCCCHHHCE
27.2025159151
88PhosphorylationEEAELVLTEKSSGTF
HHCEEEEEECCCCCC
33.6119664994
91PhosphorylationELVLTEKSSGTFLSG
EEEEEECCCCCCCCC
27.9729743597
92PhosphorylationLVLTEKSSGTFLSGL
EEEEECCCCCCCCCC
53.5829743597
94PhosphorylationLTEKSSGTFLSGLSD
EEECCCCCCCCCCCC
24.2925159151
97PhosphorylationKSSGTFLSGLSDCTN
CCCCCCCCCCCCCCC
33.2325159151
100PhosphorylationGTFLSGLSDCTNVTF
CCCCCCCCCCCCCCH
33.8818691976
103PhosphorylationLSGLSDCTNVTFSKV
CCCCCCCCCCCHHHH
37.4025159151
106PhosphorylationLSDCTNVTFSKVQRF
CCCCCCCCHHHHHHH
25.0225159151
109AcetylationCTNVTFSKVQRFWES
CCCCCHHHHHHHHHC
37.8926051181
109UbiquitinationCTNVTFSKVQRFWES
CCCCCHHHHHHHHHC
37.89-
116PhosphorylationKVQRFWESNSAAHKE
HHHHHHHCCHHHHHH
27.0427732954
118PhosphorylationQRFWESNSAAHKEIC
HHHHHCCHHHHHHHH
35.7925159151
132PhosphorylationCAVLAAVTEVIRSQG
HHHHHHHHHHHHHCC
21.5821601212
137PhosphorylationAVTEVIRSQGGKETE
HHHHHHHHCCCCCCC
23.2721601212
180PhosphorylationLVLKRVPSPVLIKKF
HHHHCCCCCCEEEEC
25.4527499020
1852-HydroxyisobutyrylationVPSPVLIKKFSDTSK
CCCCCEEEECCCCCH
43.54-
185UbiquitinationVPSPVLIKKFSDTSK
CCCCCEEEECCCCCH
43.54-
191PhosphorylationIKKFSDTSKAFMDIM
EEECCCCCHHHHHHH
27.2922210691
199PhosphorylationKAFMDIMSAQASSGS
HHHHHHHHHHCCCCC
19.9825072903
203PhosphorylationDIMSAQASSGSTSVL
HHHHHHCCCCCHHHH
24.1325072903
204PhosphorylationIMSAQASSGSTSVLR
HHHHHCCCCCHHHHH
39.5222210691
206PhosphorylationSAQASSGSTSVLRWV
HHHCCCCCHHHHHHH
21.3225072903
207PhosphorylationAQASSGSTSVLRWVL
HHCCCCCHHHHHHHH
26.7825072903
208PhosphorylationQASSGSTSVLRWVLS
HCCCCCHHHHHHHHH
22.3525072903
212 (in isoform 2)Ubiquitination-7.4021906983
219PhosphorylationWVLSCLATLLRKQDL
HHHHHHHHHHHHCCH
17.2424260401
231PhosphorylationQDLEAWGYPVTLQVY
CCHHHHCCCEEEEEE
5.4824043423
234PhosphorylationEAWGYPVTLQVYHGL
HHHCCCEEEEEEEHH
13.6324043423
238PhosphorylationYPVTLQVYHGLLSFT
CCEEEEEEEHHHCCC
4.1724043423
243PhosphorylationQVYHGLLSFTVHPKP
EEEEHHHCCCCCCCH
24.7424043423
245PhosphorylationYHGLLSFTVHPKPKI
EEHHHCCCCCCCHHH
17.9624043423
254UbiquitinationHPKPKIRKAAQHGVC
CCCHHHHHHHHHCCH
52.09-
262PhosphorylationAAQHGVCSVLKGSEF
HHHHCCHHHHCCCHH
28.25-
265AcetylationHGVCSVLKGSEFMFE
HCCHHHHCCCHHHHC
59.2325953088
265UbiquitinationHGVCSVLKGSEFMFE
HCCHHHHCCCHHHHC
59.23-
273AcetylationGSEFMFEKAPAHHPA
CCHHHHCCCCCCCHH
48.7025953088
273UbiquitinationGSEFMFEKAPAHHPA
CCHHHHCCCCCCCHH
48.7021906983
273 (in isoform 1)Ubiquitination-48.7021906983
286AcetylationPAAISTAKFCIQEIE
HHHHHHHHHHHHHHH
40.6425953088
286UbiquitinationPAAISTAKFCIQEIE
HHHHHHHHHHHHHHH
40.64-
288GlutathionylationAISTAKFCIQEIEKS
HHHHHHHHHHHHHHC
2.8622555962
2942-HydroxyisobutyrylationFCIQEIEKSGGSKEA
HHHHHHHHCCCCHHH
61.12-
294AcetylationFCIQEIEKSGGSKEA
HHHHHHHHCCCCHHH
61.1226051181
294UbiquitinationFCIQEIEKSGGSKEA
HHHHHHHHCCCCHHH
61.12-
299AcetylationIEKSGGSKEATTTLH
HHHCCCCHHHHHHHH
55.4326051181
309PhosphorylationTTTLHMLTLLKDLLP
HHHHHHHHHHHHHHC
23.5918767875
317S-nitrosocysteineLLKDLLPCFPEGLVK
HHHHHHCCCCHHHHH
10.04-
317S-nitrosylationLLKDLLPCFPEGLVK
HHHHHHCCCCHHHHH
10.0419483679
325PhosphorylationFPEGLVKSCSETLLR
CCHHHHHHHHHHHHH
18.5220860994
327PhosphorylationEGLVKSCSETLLRVM
HHHHHHHHHHHHHHH
40.4820860994
329PhosphorylationLVKSCSETLLRVMTL
HHHHHHHHHHHHHHH
18.1320860994
396UbiquitinationAWLKVMEKAHINLVR
HHHHHHHHHCCCEEE
27.46-
444AcetylationQSLKEILKECVAPHM
HHHHHHHHHHCCHHH
55.5226051181
444UbiquitinationQSLKEILKECVAPHM
HHHHHHHHHHCCHHH
55.52-
458PhosphorylationMADIGSVTSSASGPA
HHCCCCCCCCCCCCH
20.7525599653
459PhosphorylationADIGSVTSSASGPAQ
HCCCCCCCCCCCCHH
23.0428348404
460PhosphorylationDIGSVTSSASGPAQS
CCCCCCCCCCCCHHH
19.6525159151
462PhosphorylationGSVTSSASGPAQSVA
CCCCCCCCCCHHHHH
47.4625599653
467PhosphorylationSASGPAQSVAKMFRA
CCCCCHHHHHHHHHH
26.5827251275
470AcetylationGPAQSVAKMFRAVEE
CCHHHHHHHHHHHHC
36.0926051181
5112-HydroxyisobutyrylationQAHPVMRKCLQSLCD
CCCHHHHHHHHHHHH
22.62-
511AcetylationQAHPVMRKCLQSLCD
CCCHHHHHHHHHHHH
22.6226051181
511MalonylationQAHPVMRKCLQSLCD
CCCHHHHHHHHHHHH
22.6226320211
511UbiquitinationQAHPVMRKCLQSLCD
CCCHHHHHHHHHHHH
22.62-
536 (in isoform 2)Ubiquitination-15.7221906983
538 (in isoform 2)Ubiquitination-10.1321906983
597UbiquitinationLPLANTLKSKAMDLA
HHHHHHHHHHHHHHH
48.1221906983
597 (in isoform 1)Ubiquitination-48.1221906983
598PhosphorylationPLANTLKSKAMDLAQ
HHHHHHHHHHHHHHH
28.8520860994
5992-HydroxyisobutyrylationLANTLKSKAMDLAQA
HHHHHHHHHHHHHHC
46.25-
599AcetylationLANTLKSKAMDLAQA
HHHHHHHHHHHHHHC
46.2527452117
599UbiquitinationLANTLKSKAMDLAQA
HHHHHHHHHHHHHHC
46.2521906983
599 (in isoform 1)Ubiquitination-46.2521906983
601SulfoxidationNTLKSKAMDLAQAGS
HHHHHHHHHHHHCCC
5.0821406390
608PhosphorylationMDLAQAGSTVESKIY
HHHHHCCCCHHHHHH
32.0920860994
610 (in isoform 2)Ubiquitination-9.2921906983
626 (in isoform 2)Ubiquitination-2.8121906983
639PhosphorylationRPTDVAISFKGLART
CCCCEEEHHHHHHHH
15.9224719451
646O-linked_GlycosylationSFKGLARTLGMAISE
HHHHHHHHHCHHHHC
23.2730379171
646PhosphorylationSFKGLARTLGMAISE
HHHHHHHHHCHHHHC
23.27-
652PhosphorylationRTLGMAISERPDLRV
HHHCHHHHCCCCHHH
20.29-
6712-HydroxyisobutyrylationALRTLITKGCQAEAD
HHHHHHHCCCHHHHH
51.17-
671AcetylationALRTLITKGCQAEAD
HHHHHHHCCCHHHHH
51.1726051181
671MalonylationALRTLITKGCQAEAD
HHHHHHHCCCHHHHH
51.1726320211
671UbiquitinationALRTLITKGCQAEAD
HHHHHHHCCCHHHHH
51.17-
671 (in isoform 1)Ubiquitination-51.1721906983
679MethylationGCQAEADRAEVSRFA
CCHHHHHHHHHHHHH
39.43115492917
687AcetylationAEVSRFAKNFLPILF
HHHHHHHHHHHHHHH
45.5826051181
687UbiquitinationAEVSRFAKNFLPILF
HHHHHHHHHHHHHHH
45.582190698
687 (in isoform 1)Ubiquitination-45.5821906983
706PhosphorylationQPVAAGDTPAPRRAV
CCCCCCCCCCCHHHH
22.0422199227
716PhosphorylationPRRAVLETIRTYLTI
CHHHHHHHHHHHCCC
16.1720068231
731PhosphorylationTDTQLVNSLLEKASE
CCHHHHHHHHHHHHH
27.1824719451
735UbiquitinationLVNSLLEKASEKVLD
HHHHHHHHHHHHCCC
58.12-
737PhosphorylationNSLLEKASEKVLDPA
HHHHHHHHHHCCCCC
49.3626074081
7392-HydroxyisobutyrylationLLEKASEKVLDPASS
HHHHHHHHCCCCCCC
45.67-
739AcetylationLLEKASEKVLDPASS
HHHHHHHHCCCCCCC
45.6726051181
739UbiquitinationLLEKASEKVLDPASS
HHHHHHHHCCCCCCC
45.67-
745PhosphorylationEKVLDPASSDFTRLS
HHCCCCCCCCCCHHH
35.5126074081
746PhosphorylationKVLDPASSDFTRLSV
HCCCCCCCCCCHHHH
38.5626074081
7832-HydroxyisobutyrylationIRPYLESKAHGVQKK
HHHHHHHHCCCCHHH
34.72-
783UbiquitinationIRPYLESKAHGVQKK
HHHHHHHHCCCCHHH
34.72-
801PhosphorylationVLEEVCASPQGPGAL
HHHHHHCCCCCCCCE
16.7820873877
818AcetylationQSHLEDLKKTLLDSL
HHHHHHHHHHHHHHH
56.9126051181
818UbiquitinationQSHLEDLKKTLLDSL
HHHHHHHHHHHHHHH
56.91-
819UbiquitinationSHLEDLKKTLLDSLR
HHHHHHHHHHHHHHH
52.26-
820PhosphorylationHLEDLKKTLLDSLRS
HHHHHHHHHHHHHHC
30.8530206219
824PhosphorylationLKKTLLDSLRSTSSP
HHHHHHHHHHCCCCC
26.1730206219
827PhosphorylationTLLDSLRSTSSPAKR
HHHHHHHCCCCCCCC
37.6230206219
828PhosphorylationLLDSLRSTSSPAKRP
HHHHHHCCCCCCCCH
27.1330206219
829PhosphorylationLDSLRSTSSPAKRPR
HHHHHCCCCCCCCHH
35.2530206219
830PhosphorylationDSLRSTSSPAKRPRL
HHHHCCCCCCCCHHH
29.0330206219
838UbiquitinationPAKRPRLKCLLHIVR
CCCCHHHHHHHHHHH
24.90-
846UbiquitinationCLLHIVRKLSAEHKE
HHHHHHHHHCHHHHH
35.58-
852AcetylationRKLSAEHKEFITALI
HHHCHHHHHHHHHHH
45.9126051181
937PhosphorylationEFKGLMGTSTVEQLL
HCCCCCCCHHHHHHH
13.7829978859
938PhosphorylationFKGLMGTSTVEQLLE
CCCCCCCHHHHHHHH
25.4029978859
939PhosphorylationKGLMGTSTVEQLLEN
CCCCCCHHHHHHHHH
28.0929978859
953PhosphorylationNVCLLLASRTRDVVK
HHHHHHHHCCHHHHH
33.8729978859
9602-HydroxyisobutyrylationSRTRDVVKSALGFIK
HCCHHHHHHHHHHHH
29.84-
1010AcetylationKLRNLFTKFIRKFGF
HHHHHHHHHHHHHCH
31.3126051181
1014AcetylationLFTKFIRKFGFELVK
HHHHHHHHHCHHHHH
45.0526051181
1021AcetylationKFGFELVKRLLPEEY
HHCHHHHHHHCCHHH
50.3726051181
1049PhosphorylationAKRHRALSQAAVEEE
HHHHHHHHHHHHHHH
19.4525159151
1072PhosphorylationPAQGKGDSIEEILAD
CCCCCCCCHHHHHCC
40.3422167270
1080PhosphorylationIEEILADSEDEEDNE
HHHHHCCCCCCCCCH
41.1429255136
1092PhosphorylationDNEEEERSRGKEQRK
CCHHHHHHHHHHHHH
48.9830576142
1105PhosphorylationRKLARQRSRAWLKEG
HHHHHHHHHHHHHCC
20.2930624053
1110MethylationQRSRAWLKEGGGDEP
HHHHHHHHCCCCCCC
43.54115977399
1110UbiquitinationQRSRAWLKEGGGDEP
HHHHHHHHCCCCCCC
43.54-
1124UbiquitinationPLNFLDPKVAQRVLA
CCCCCCHHHHHHHHH
50.28-
1132PhosphorylationVAQRVLATQPGPGRG
HHHHHHHCCCCCCCC
31.0028555341
1138MethylationATQPGPGRGRKKDHG
HCCCCCCCCCCCCCC
44.8912019387
1140MethylationQPGPGRGRKKDHGFK
CCCCCCCCCCCCCEE
41.30115492923
1142MethylationGPGRGRKKDHGFKVS
CCCCCCCCCCCEEEC
54.30116252851
1147MethylationRKKDHGFKVSADGRL
CCCCCCEEECCCCEE
39.61115977405
1149PhosphorylationKDHGFKVSADGRLII
CCCCEEECCCCEEEE
22.6425159151
1212PhosphorylationELEIPPQYQAGGSGI
HCCCCCCCCCCCCCC
13.2028555341
1217PhosphorylationPQYQAGGSGIHRPVA
CCCCCCCCCCCCCHH
33.3928985074
1225UbiquitinationGIHRPVAKKAMPGAE
CCCCCHHHHCCCCHH
41.10-
1226UbiquitinationIHRPVAKKAMPGAEY
CCCCHHHHCCCCHHH
39.93-
1237AcetylationGAEYKAKKAKGDVKK
CHHHCHHHCCCCCCC
61.2611791429
1239AcetylationEYKAKKAKGDVKKKG
HHCHHHCCCCCCCCC
65.609854453
1243AcetylationKKAKGDVKKKGRPDP
HHCCCCCCCCCCCCC
54.2111791439
1251PhosphorylationKKGRPDPYAYIPLNR
CCCCCCCCCCCCCCH
21.2928442448
1253PhosphorylationGRPDPYAYIPLNRSK
CCCCCCCCCCCCHHH
9.3822461510
1268UbiquitinationLNRRKKMKLQGQFKG
CCHHHHHHHHHHHHH
46.68-
1284PhosphorylationVKAARRGSQVGHKNR
HHHHHHCCCCCCCCC
21.6330576142

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
1049SPhosphorylationKinaseCHEK1O14757
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RRP12_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 RRP12_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP2M1_HUMANAP2M1physical
12421765
BRX1_HUMANBRIX1physical
26344197
DDX24_HUMANDDX24physical
26344197
EIF2A_HUMANEIF2Aphysical
26344197
IF2P_HUMANEIF5Bphysical
26344197
H1X_HUMANH1FXphysical
26344197
MK67I_HUMANNIFKphysical
26344197
NOC2L_HUMANNOC2Lphysical
26344197
RBM19_HUMANRBM19physical
26344197
RL1D1_HUMANRSL1D1physical
26344197
TSR1_HUMANTSR1physical
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 RRP12_HUMAN

loading...

Related Literatures of Post-Translational Modification
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-72; THR-77 AND SER-1080,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-1080, AND MASSSPECTROMETRY.
"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-1049 AND SER-1080, 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-1072 AND SER-1080, ANDMASS SPECTROMETRY.
"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-49; THR-52 AND SER-1080,AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1080, 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-1049, 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-1080, AND MASSSPECTROMETRY.

TOP