DKC1_HUMAN - dbPTM
DKC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DKC1_HUMAN
UniProt AC O60832
Protein Name H/ACA ribonucleoprotein complex subunit DKC1
Gene Name DKC1 {ECO:0000312|HGNC:HGNC:2890}
Organism Homo sapiens (Human).
Sequence Length 514
Subcellular Localization Isoform 1: Nucleus, nucleolus . Nucleus, Cajal body . Also localized to Cajal bodies (coiled bodies).
Isoform 3: Cytoplasm .
Protein Description Isoform 1: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. [PubMed: 25219674 This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1]
Protein Sequence MADAEVIILPKKHKKKKERKSLPEEDVAEIQHAEEFLIKPESKVAKLDTSQWPLLLKNFDKLNVRTTHYTPLACGSNPLKREIGDYIRTGFINLDKPSNPSSHEVVAWIRRILRVEKTGHSGTLDPKVTGCLIVCIERATRLVKSQQSAGKEYVGIVRLHNAIEGGTQLSRALETLTGALFQRPPLIAAVKRQLRVRTIYESKMIEYDPERRLGIFWVSCEAGTYIRTLCVHLGLLLGVGGQMQELRRVRSGVMSEKDHMVTMHDVLDAQWLYDNHKDESYLRRVVYPLEKLLTSHKRLVMKDSAVNAICYGAKIMLPGVLRYEDGIEVNQEIVVITTKGEAICMAIALMTTAVISTCDHGIVAKIKRVIMERDTYPRKWGLGPKASQKKLMIKQGLLDKHGKPTDSTPATWKQEYVDYSESAKKEVVAEVVKAPQVVAEAAKTAKRKRESESESDETPPAAPQLIKKEKKKSKKDKKAKAGLESGAEPGDGDSDTTKKKKKKKKAKEVELVSE
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
2Acetylation------MADAEVIIL
------CCCCEEEEC		25.4022223895
112-HydroxyisobutyrylationAEVIILPKKHKKKKE
CEEEECCHHHCCHHH		65.15-
12AcetylationEVIILPKKHKKKKER
EEEECCHHHCCHHHH		59.7310534037
12UbiquitinationEVIILPKKHKKKKER
EEEECCHHHCCHHHH		59.73-
14AcetylationIILPKKHKKKKERKS
EECCHHHCCHHHHCC		75.1510534033
20SumoylationHKKKKERKSLPEEDV
HCCHHHHCCCCHHHH		58.3928112733
20UbiquitinationHKKKKERKSLPEEDV
HCCHHHHCCCCHHHH		58.3921906983
21PhosphorylationKKKKERKSLPEEDVA
CCHHHHCCCCHHHHH		56.2129255136
39SumoylationHAEEFLIKPESKVAK
HHHHHHCCCHHHCCC		44.90-
39AcetylationHAEEFLIKPESKVAK
HHHHHHCCCHHHCCC		44.9026051181
39SumoylationHAEEFLIKPESKVAK
HHHHHHCCCHHHCCC		44.9028112733
39UbiquitinationHAEEFLIKPESKVAK
HHHHHHCCCHHHCCC		44.9021906983
42PhosphorylationEFLIKPESKVAKLDT
HHHCCCHHHCCCCCC		40.7428387310
43SumoylationFLIKPESKVAKLDTS
HHCCCHHHCCCCCCC		44.54-
43SumoylationFLIKPESKVAKLDTS
HHCCCHHHCCCCCCC		44.5428112733
43UbiquitinationFLIKPESKVAKLDTS
HHCCCHHHCCCCCCC		44.5421963094
46AcetylationKPESKVAKLDTSQWP
CCHHHCCCCCCCCCC		50.3025953088
46UbiquitinationKPESKVAKLDTSQWP
CCHHHCCCCCCCCCC		50.3021906983
57UbiquitinationSQWPLLLKNFDKLNV
CCCCHHHHCCCCCCC		56.3821906983
61AcetylationLLLKNFDKLNVRTTH
HHHHCCCCCCCCCCC		37.5125953088
61UbiquitinationLLLKNFDKLNVRTTH
HHHHCCCCCCCCCCC		37.5123503661
66PhosphorylationFDKLNVRTTHYTPLA
CCCCCCCCCCCCCCC		17.4023312004
67PhosphorylationDKLNVRTTHYTPLAC
CCCCCCCCCCCCCCC		11.4328152594
69PhosphorylationLNVRTTHYTPLACGS
CCCCCCCCCCCCCCC		14.1428152594
70PhosphorylationNVRTTHYTPLACGSN
CCCCCCCCCCCCCCC		12.2928152594
802-HydroxyisobutyrylationACGSNPLKREIGDYI
CCCCCCCHHHHHHHH		49.60-
80AcetylationACGSNPLKREIGDYI
CCCCCCCHHHHHHHH		49.6025953088
80UbiquitinationACGSNPLKREIGDYI
CCCCCCCHHHHHHHH		49.6021963094
96AcetylationTGFINLDKPSNPSSH
HCCCCCCCCCCCCHH		54.2126051181
96UbiquitinationTGFINLDKPSNPSSH
HCCCCCCCCCCCCHH		54.21-
117UbiquitinationRRILRVEKTGHSGTL
HHHHCHHCCCCCCCC		57.88-
144UbiquitinationERATRLVKSQQSAGK
HHHHHHHHHHHHCCC		47.3327667366
1512-HydroxyisobutyrylationKSQQSAGKEYVGIVR
HHHHHCCCCEEEEEE		45.66-
151AcetylationKSQQSAGKEYVGIVR
HHHHHCCCCEEEEEE		45.6626051181
151UbiquitinationKSQQSAGKEYVGIVR
HHHHHCCCCEEEEEE		45.6621906983
153PhosphorylationQQSAGKEYVGIVRLH
HHHCCCCEEEEEEHH		13.88-
191AcetylationPPLIAAVKRQLRVRT
CHHHHHHHHHCCCCE		29.6925953088
191SumoylationPPLIAAVKRQLRVRT
CHHHHHHHHHCCCCE		29.6928112733
191UbiquitinationPPLIAAVKRQLRVRT
CHHHHHHHHHCCCCE		29.6923000965
198PhosphorylationKRQLRVRTIYESKMI
HHHCCCCEEEECCCC		25.6727732954
200PhosphorylationQLRVRTIYESKMIEY
HCCCCEEEECCCCEE		17.3427732954
202PhosphorylationRVRTIYESKMIEYDP
CCCEEEECCCCEECC		15.5627732954
203UbiquitinationVRTIYESKMIEYDPE
CCEEEECCCCEECCC		31.77-
255PhosphorylationRVRSGVMSEKDHMVT
HHHCCCCCCCCCEEE		38.8024719451
257UbiquitinationRSGVMSEKDHMVTMH
HCCCCCCCCCEEEHH		45.7021963094
277AcetylationQWLYDNHKDESYLRR
HHHHCCCCCHHHHHH		70.2419413330
287PhosphorylationSYLRRVVYPLEKLLT
HHHHHHHHHHHHHHH		10.15-
2912-HydroxyisobutyrylationRVVYPLEKLLTSHKR
HHHHHHHHHHHHCCC		57.38-
291AcetylationRVVYPLEKLLTSHKR
HHHHHHHHHHHHCCC		57.3825953088
2972-HydroxyisobutyrylationEKLLTSHKRLVMKDS
HHHHHHCCCHHCCHH		47.39-
297UbiquitinationEKLLTSHKRLVMKDS
HHHHHHCCCHHCCHH		47.3929967540
302AcetylationSHKRLVMKDSAVNAI
HCCCHHCCHHHHHHH		40.8426051181
302UbiquitinationSHKRLVMKDSAVNAI
HCCCHHCCHHHHHHH		40.8429967540
304PhosphorylationKRLVMKDSAVNAICY
CCHHCCHHHHHHHHH		28.7026074081
311PhosphorylationSAVNAICYGAKIMLP
HHHHHHHHCCEEECC		17.6326074081
314AcetylationNAICYGAKIMLPGVL
HHHHHCCEEECCCCE		25.0426051181
316SulfoxidationICYGAKIMLPGVLRY
HHHCCEEECCCCEEC		3.4921406390
323PhosphorylationMLPGVLRYEDGIEVN
ECCCCEECCCCEEEC		17.7626074081
337PhosphorylationNQEIVVITTKGEAIC
CCEEEEEEECHHHHH		15.7321902226
338PhosphorylationQEIVVITTKGEAICM
CEEEEEEECHHHHHH		26.4021902226
379AcetylationERDTYPRKWGLGPKA
CCCCCCCCCCCCCCH		40.9025953088
379UbiquitinationERDTYPRKWGLGPKA
CCCCCCCCCCCCCCH		40.9029967540
385UbiquitinationRKWGLGPKASQKKLM
CCCCCCCCHHHHHHH		59.8929967540
387PhosphorylationWGLGPKASQKKLMIK
CCCCCCHHHHHHHHH		48.9725159151
389UbiquitinationLGPKASQKKLMIKQG
CCCCHHHHHHHHHCC		45.4323000965
390UbiquitinationGPKASQKKLMIKQGL
CCCHHHHHHHHHCCC		35.3323000965
394SumoylationSQKKLMIKQGLLDKH
HHHHHHHHCCCHHCC		25.09-
3942-HydroxyisobutyrylationSQKKLMIKQGLLDKH
HHHHHHHHCCCHHCC		25.09-
394AcetylationSQKKLMIKQGLLDKH
HHHHHHHHCCCHHCC		25.0925953088
394SumoylationSQKKLMIKQGLLDKH
HHHHHHHHCCCHHCC		25.0928112733
394UbiquitinationSQKKLMIKQGLLDKH
HHHHHHHHCCCHHCC		25.0923000965
400AcetylationIKQGLLDKHGKPTDS
HHCCCHHCCCCCCCC		54.9825953088
400UbiquitinationIKQGLLDKHGKPTDS
HHCCCHHCCCCCCCC		54.9823000965
403AcetylationGLLDKHGKPTDSTPA
CCHHCCCCCCCCCCC		44.4526051181
403UbiquitinationGLLDKHGKPTDSTPA
CCHHCCCCCCCCCCC		44.4533845483
407PhosphorylationKHGKPTDSTPATWKQ
CCCCCCCCCCCCCCH		38.4828555341
408PhosphorylationHGKPTDSTPATWKQE
CCCCCCCCCCCCCHH		21.5428555341
411PhosphorylationPTDSTPATWKQEYVD
CCCCCCCCCCHHHCC		34.1027251275
413SumoylationDSTPATWKQEYVDYS
CCCCCCCCHHHCCCC		28.97-
413AcetylationDSTPATWKQEYVDYS
CCCCCCCCHHHCCCC		28.9726051181
413SumoylationDSTPATWKQEYVDYS
CCCCCCCCHHHCCCC		28.9725114211
413UbiquitinationDSTPATWKQEYVDYS
CCCCCCCCHHHCCCC		28.9732015554
416PhosphorylationPATWKQEYVDYSESA
CCCCCHHHCCCCHHH		8.9828152594
419PhosphorylationWKQEYVDYSESAKKE
CCHHHCCCCHHHCHH		12.3228152594
420PhosphorylationKQEYVDYSESAKKEV
CHHHCCCCHHHCHHH		22.1719691289
422PhosphorylationEYVDYSESAKKEVVA
HHCCCCHHHCHHHHH		39.1725159151
4242-HydroxyisobutyrylationVDYSESAKKEVVAEV
CCCCHHHCHHHHHHH		59.76-
424AcetylationVDYSESAKKEVVAEV
CCCCHHHCHHHHHHH		59.7626051181
424SumoylationVDYSESAKKEVVAEV
CCCCHHHCHHHHHHH		59.7628112733
424UbiquitinationVDYSESAKKEVVAEV
CCCCHHHCHHHHHHH		59.7633845483
4252-HydroxyisobutyrylationDYSESAKKEVVAEVV
CCCHHHCHHHHHHHH		56.30-
425UbiquitinationDYSESAKKEVVAEVV
CCCHHHCHHHHHHHH		56.3029967540
428UbiquitinationESAKKEVVAEVVKAP
HHHCHHHHHHHHCHH		3.8432015554
433AcetylationEVVAEVVKAPQVVAE
HHHHHHHCHHHHHHH		60.5726051181
433SumoylationEVVAEVVKAPQVVAE
HHHHHHHCHHHHHHH		60.5728112733
433UbiquitinationEVVAEVVKAPQVVAE
HHHHHHHCHHHHHHH		60.5732015554
438UbiquitinationVVKAPQVVAEAAKTA
HHCHHHHHHHHHHHH		3.1632015554
443AcetylationQVVAEAAKTAKRKRE
HHHHHHHHHHHHHHH		56.9425953088
443UbiquitinationQVVAEAAKTAKRKRE
HHHHHHHHHHHHHHH		56.9432015554
444PhosphorylationVVAEAAKTAKRKRES
HHHHHHHHHHHHHHC		32.4626074081
446AcetylationAEAAKTAKRKRESES
HHHHHHHHHHHHCCC		64.787676285
448PhosphorylationAAKTAKRKRESESES
HHHHHHHHHHCCCCC		60.8733259812
451PhosphorylationTAKRKRESESESDET
HHHHHHHCCCCCCCC		50.9129255136
453PhosphorylationKRKRESESESDETPP
HHHHHCCCCCCCCCC		52.2429255136
455PhosphorylationKRESESESDETPPAA
HHHCCCCCCCCCCCH		50.4529255136
458PhosphorylationSESESDETPPAAPQL
CCCCCCCCCCCHHHH		39.2929255136
467SumoylationPAAPQLIKKEKKKSK
CCHHHHHHHHHHCCH		64.5728112733
472AcetylationLIKKEKKKSKKDKKA
HHHHHHHCCHHHHHH		77.8069699
474AcetylationKKEKKKSKKDKKAKA
HHHHHCCHHHHHHHH		74.0969701
475AcetylationKEKKKSKKDKKAKAG
HHHHCCHHHHHHHHH		80.1769703
477AcetylationKKKSKKDKKAKAGLE
HHCCHHHHHHHHHHH		64.6169705
485PhosphorylationKAKAGLESGAEPGDG
HHHHHHHCCCCCCCC		48.6329255136
489PhosphorylationGLESGAEPGDGDSDT
HHHCCCCCCCCCCHH		45.7132142685
492PhosphorylationSGAEPGDGDSDTTKK
CCCCCCCCCCHHHHH		42.0932645325
494PhosphorylationAEPGDGDSDTTKKKK
CCCCCCCCHHHHHHH		42.2419664994
496PhosphorylationPGDGDSDTTKKKKKK
CCCCCCHHHHHHHHH		44.4629255136
497PhosphorylationGDGDSDTTKKKKKKK
CCCCCHHHHHHHHHH		45.9529255136
513PhosphorylationAKEVELVSE------
HHHCEECCC------		50.6529255136
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 DKC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DKC1_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 DKC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EF1G_HUMANEEF1Gphysical
16169070
SHQ1_HUMANSHQ1physical
22085966
NAF1_HUMANNAF1physical
19095616
NHP2_HUMANNHP2physical
19095616
NOP10_HUMANNOP10physical
19095616
FBRL_HUMANFBLphysical
19095616
NHP2_HUMANNHP2physical
22939629
GAR1_HUMANGAR1physical
22939629
NOP58_HUMANNOP58physical
22939629
TEBP_HUMANPTGES3physical
22939629
RBM28_HUMANRBM28physical
22939629
RSSA_HUMANRPSAphysical
22939629
RPAC1_HUMANPOLR1Cphysical
22939629
SRP14_HUMANSRP14physical
22939629
LSM2_HUMANLSM2physical
22939629
TERT_HUMANTERTphysical
18358808
RUVB1_HUMANRUVBL1physical
18358808
RUVB2_HUMANRUVBL2physical
18358808
DKC1_HUMANDKC1physical
21931644
NOP10_HUMANNOP10physical
26186194
RUVB1_HUMANRUVBL1physical
26186194
NAF1_HUMANNAF1physical
26186194
RUVB2_HUMANRUVBL2physical
26186194
SHQ1_HUMANSHQ1physical
26186194
DCAF4_HUMANDCAF4physical
26186194
BCCIP_HUMANBCCIPphysical
26344197
DDX56_HUMANDDX56physical
26344197
IF2P_HUMANEIF5Bphysical
26344197
FBRL_HUMANFBLphysical
26344197
NOG2_HUMANGNL2physical
26344197
GNL3_HUMANGNL3physical
26344197
NOG1_HUMANGTPBP4physical
26344197
NAF1_HUMANNAF1physical
26344197
NHP2_HUMANNHP2physical
26344197
MK67I_HUMANNIFKphysical
26344197
NMD3_HUMANNMD3physical
26344197
NOC2L_HUMANNOC2Lphysical
26344197
NOC4L_HUMANNOC4Lphysical
26344197
NOP56_HUMANNOP56physical
26344197
NOP58_HUMANNOP58physical
26344197
RPF2_HUMANRPF2physical
26344197
RS4X_HUMANRPS4Xphysical
26344197
TBL3_HUMANTBL3physical
26344197
QCR2_HUMANUQCRC2physical
26344197
WDR36_HUMANWDR36physical
26344197
DAXX_HUMANDAXXphysical
25416818
WAP53_HUMANWRAP53physical
25416818
SHQ1_HUMANSHQ1physical
28514442
NAF1_HUMANNAF1physical
28514442
NOP10_HUMANNOP10physical
28514442
RUVB2_HUMANRUVBL2physical
28514442
DCAF4_HUMANDCAF4physical
28514442
RL7_HUMANRPL7physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
305000Dyskeratosis congenita, X-linked (DKCX)
305000Hoyeraal-Hreidarsson syndrome (HHS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DKC1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-451; SER-453; SER-455; THR-458; SER-485;SER-494; THR-496; THR-497 AND SER-513, 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-21; SER-485; SER-494 ANDSER-513, 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-494 AND SER-513, ANDMASS 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-451; SER-453; SER-455; THR-458; SER-485;SER-494; THR-496; THR-497 AND SER-513, 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-494, 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-21; SER-451; SER-453;SER-455; THR-458; SER-485; SER-494 AND SER-513, 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-21, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, 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-422; SER-451; SER-453;SER-455; SER-494 AND SER-513, 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-451 AND SER-453, ANDMASS 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 SER-21, AND MASSSPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451 AND SER-455, ANDMASS 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-21 AND SER-513, 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-494 AND SER-513, 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-21; SER-451; SER-453;SER-455; THR-458 AND SER-513, 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-453 AND SER-455, ANDMASS SPECTROMETRY.
"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-494 AND SER-513, ANDMASS SPECTROMETRY.

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