FOXK1_HUMAN - dbPTM
FOXK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOXK1_HUMAN
UniProt AC P85037
Protein Name Forkhead box protein K1
Gene Name FOXK1 {ECO:0000303|PubMed:15202027, ECO:0000303|PubMed:15289879}
Organism Homo sapiens (Human).
Sequence Length 733
Subcellular Localization Nucleus . Cytoplasm . (Microbial infection) Accumulates in the nucleus upon viral infection.
Protein Description Transcriptional regulator that binds to the upstream enhancer region (CCAC box) of myoglobin gene (By similarity). Important regulatory factor of the myogenic progenitor cell population (By similarity). Involved in the cell cycle process, promotes proliferation by repressing Foxo4 transcriptional activity and the cyclin-dependent kinase inhibitor, p21CIP, in the myogenic progenitor cells (By similarity). Represses myogenic differentiation by inhibiting MEFC acitivity (By similarity). Has a role in remodeling processes of adult muscles that occur in response to physiological stimuli (By similarity). Required to correct temporal orchestration of molecular and cellular events necessary for muscle repair (By similarity). Positively regulates Wnt/beta-catenin signaling by translocating DVL into the nucleus. [PubMed: 25805136 Reduces virus replication, probably by binding the interferon stimulated response element (ISRE) to promote antiviral gene expression]
Protein Sequence MAEVGEDSGARALLALRSAPCSPVLCAAAAAAAFPAAAPPPAPAQPQPPPGPPPPPPPPLPPGAIAGAGSSGGSSGVSGDSAVAGAAPALVAAAAASVRQSPGPALARLEGREFEFLMRQPSVTIGRNSSQGSVDLSMGLSSFISRRHLQLSFQEPHFYLRCLGKNGVFVDGAFQRRGAPALQLPKQCTFRFPSTAIKIQFTSLYHKEEAPASPLRPLYPQISPLKIHIPEPDLRSMVSPVPSPTGTISVPNSCPASPRGAGSSSYRFVQNVTSDLQLAAEFAAKAASEQQADTSGGDSPKDESKPPFSYAQLIVQAISSAQDRQLTLSGIYAHITKHYPYYRTADKGWQNSIRHNLSLNRYFIKVPRSQEEPGKGSFWRIDPASEAKLVEQAFRKRRQRGVSCFRTPFGPLSSRSAPASPTHPGLMSPRSGGLQTPECLSREGSPIPHDPEFGSKLASVPEYRYSQSAPGSPVSAQPVIMAVPPRPSSLVAKPVAYMPASIVTSQQPAGHAIHVVQQAPTVTMVRVVTTSANSANGYILTSQGAAGGSHDAAGAAVLDLGSEARGLEEKPTIAFATIPAAGGVIQTVASQMAPGVPGHTVTILQPATPVTLGQHHLPVRAVTQNGKHAVPTNSLAGNAYALTSPLQLLATQASSSAPVVVTRVCEVGPKEPAAAVAATATTTPATATTASASASSTGEPEVKRSRVEEPSGAVTTPAGVIAAAGPQGPGTGE
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------MAEVGEDSG
------CCCCCCCHH		21.8522814378
18PhosphorylationRALLALRSAPCSPVL
HHHHHHHCCCCHHHH		37.1026074081
22PhosphorylationALRSAPCSPVLCAAA
HHHCCCCHHHHHHHH		19.5826074081
101PhosphorylationAAASVRQSPGPALAR
HHHHHHCCCCCHHHH		22.6626846344
122PhosphorylationEFLMRQPSVTIGRNS
EEEECCCCEEECCCC		24.4524247654
124PhosphorylationLMRQPSVTIGRNSSQ
EECCCCEEECCCCCC		23.2724719451
130PhosphorylationVTIGRNSSQGSVDLS
EEECCCCCCCEEEHH		41.9522817900
145PhosphorylationMGLSSFISRRHLQLS
HHHHHHHHHHHHHHH		22.6624719451
161MethylationQEPHFYLRCLGKNGV
CCCCEEEEEECCCCE		11.3924129315
165AcetylationFYLRCLGKNGVFVDG
EEEEEECCCCEEECC		37.2626051181
165UbiquitinationFYLRCLGKNGVFVDG
EEEEEECCCCEEECC		37.26-
177MethylationVDGAFQRRGAPALQL
ECCCHHCCCCCCCCC		34.54-
186UbiquitinationAPALQLPKQCTFRFP
CCCCCCCCCCEEECC		67.6029967540
191MethylationLPKQCTFRFPSTAIK
CCCCCEEECCCCEEE		25.1424129315
202PhosphorylationTAIKIQFTSLYHKEE
CEEEEEEEECCCCCC		11.0528176443
202UbiquitinationTAIKIQFTSLYHKEE
CEEEEEEEECCCCCC		11.0527667366
203PhosphorylationAIKIQFTSLYHKEEA
EEEEEEEECCCCCCC		28.3728176443
205PhosphorylationKIQFTSLYHKEEAPA
EEEEEECCCCCCCCC		15.6028176443
213PhosphorylationHKEEAPASPLRPLYP
CCCCCCCCCCCCCCC		24.3329255136
219PhosphorylationASPLRPLYPQISPLK
CCCCCCCCCCCCCCE		8.8628176443
223PhosphorylationRPLYPQISPLKIHIP
CCCCCCCCCCEEECC		20.9429255136
226UbiquitinationYPQISPLKIHIPEPD
CCCCCCCEEECCCCC		35.3129967540
236PhosphorylationIPEPDLRSMVSPVPS
CCCCCHHHCCCCCCC		30.7330266825
239PhosphorylationPDLRSMVSPVPSPTG
CCHHHCCCCCCCCCC		16.1323927012
243PhosphorylationSMVSPVPSPTGTISV
HCCCCCCCCCCCEEC		35.0123927012
245PhosphorylationVSPVPSPTGTISVPN
CCCCCCCCCCEECCC		51.8223927012
247PhosphorylationPVPSPTGTISVPNSC
CCCCCCCCEECCCCC		16.7423927012
249PhosphorylationPSPTGTISVPNSCPA
CCCCCCEECCCCCCC		31.2130266825
253PhosphorylationGTISVPNSCPASPRG
CCEECCCCCCCCCCC		18.5330266825
257PhosphorylationVPNSCPASPRGAGSS
CCCCCCCCCCCCCCC		10.5625159151
263PhosphorylationASPRGAGSSSYRFVQ
CCCCCCCCCCEECCC		18.6423090842
264PhosphorylationSPRGAGSSSYRFVQN
CCCCCCCCCEECCCH		30.3923090842
265PhosphorylationPRGAGSSSYRFVQNV
CCCCCCCCEECCCHH		23.2523090842
266PhosphorylationRGAGSSSYRFVQNVT
CCCCCCCEECCCHHC		15.2623090842
273PhosphorylationYRFVQNVTSDLQLAA
EECCCHHCCHHHHHH		24.8722322096
274PhosphorylationRFVQNVTSDLQLAAE
ECCCHHCCHHHHHHH		31.8528348404
285UbiquitinationLAAEFAAKAASEQQA
HHHHHHHHHHHHHHC		40.8429967540
288PhosphorylationEFAAKAASEQQADTS
HHHHHHHHHHHCCCC		40.5819276368
294PhosphorylationASEQQADTSGGDSPK
HHHHHCCCCCCCCCC		32.0823927012
295PhosphorylationSEQQADTSGGDSPKD
HHHHCCCCCCCCCCC		41.1323927012
299PhosphorylationADTSGGDSPKDESKP
CCCCCCCCCCCCCCC		36.8029255136
304PhosphorylationGDSPKDESKPPFSYA
CCCCCCCCCCCCCHH		61.6725022875
309PhosphorylationDESKPPFSYAQLIVQ
CCCCCCCCHHHHHHH		25.9025022875
310PhosphorylationESKPPFSYAQLIVQA
CCCCCCCHHHHHHHH		9.9519276368
319PhosphorylationQLIVQAISSAQDRQL
HHHHHHHHCHHHHEE		23.7220873877
320PhosphorylationLIVQAISSAQDRQLT
HHHHHHHCHHHHEEE		24.6820068231
327O-linked_GlycosylationSAQDRQLTLSGIYAH
CHHHHEEEHHHHHHH		15.5623301498
327PhosphorylationSAQDRQLTLSGIYAH
CHHHHEEEHHHHHHH		15.5623186163
329PhosphorylationQDRQLTLSGIYAHIT
HHHEEEHHHHHHHHH		20.2223186163
336O-linked_GlycosylationSGIYAHITKHYPYYR
HHHHHHHHHCCCCEE		11.2523301498
339PhosphorylationYAHITKHYPYYRTAD
HHHHHHCCCCEECCC		8.42-
341PhosphorylationHITKHYPYYRTADKG
HHHHCCCCEECCCHH		9.83-
342PhosphorylationITKHYPYYRTADKGW
HHHCCCCEECCCHHH		9.29-
347AcetylationPYYRTADKGWQNSIR
CCEECCCHHHHHHHH		60.6325953088
347UbiquitinationPYYRTADKGWQNSIR
CCEECCCHHHHHHHH		60.6329967540
352PhosphorylationADKGWQNSIRHNLSL
CCHHHHHHHHHCCEE		13.1027067055
361MethylationRHNLSLNRYFIKVPR
HHCCEECCEEEECCC		32.79-
365MalonylationSLNRYFIKVPRSQEE
EECCEEEECCCCCCC		35.9726320211
365UbiquitinationSLNRYFIKVPRSQEE
EECCEEEECCCCCCC		35.9733845483
375SumoylationRSQEEPGKGSFWRID
CCCCCCCCCCCEECC		63.20-
375AcetylationRSQEEPGKGSFWRID
CCCCCCCCCCCEECC		63.2025953088
375SumoylationRSQEEPGKGSFWRID
CCCCCCCCCCCEECC		63.20-
375UbiquitinationRSQEEPGKGSFWRID
CCCCCCCCCCCEECC		63.2032015554
377PhosphorylationQEEPGKGSFWRIDPA
CCCCCCCCCEECCHH		25.7323917254
388UbiquitinationIDPASEAKLVEQAFR
CCHHHHHHHHHHHHH		49.3533845483
400MethylationAFRKRRQRGVSCFRT
HHHHHHHHCCCCCCC		45.74-
403PhosphorylationKRRQRGVSCFRTPFG
HHHHHCCCCCCCCCC		15.4622617229
407PhosphorylationRGVSCFRTPFGPLSS
HCCCCCCCCCCCCCC		11.6123927012
413PhosphorylationRTPFGPLSSRSAPAS
CCCCCCCCCCCCCCC		27.1723927012
414PhosphorylationTPFGPLSSRSAPASP
CCCCCCCCCCCCCCC		37.6323401153
416PhosphorylationFGPLSSRSAPASPTH
CCCCCCCCCCCCCCC		40.3229255136
420PhosphorylationSSRSAPASPTHPGLM
CCCCCCCCCCCCCCC		29.3129255136
422PhosphorylationRSAPASPTHPGLMSP
CCCCCCCCCCCCCCC		37.9029255136
428PhosphorylationPTHPGLMSPRSGGLQ
CCCCCCCCCCCCCCC		23.3929255136
431PhosphorylationPGLMSPRSGGLQTPE
CCCCCCCCCCCCCHH		40.3722167270
436PhosphorylationPRSGGLQTPECLSRE
CCCCCCCCHHHHCCC		26.5429255136
441PhosphorylationLQTPECLSREGSPIP
CCCHHHHCCCCCCCC		39.6929255136
445PhosphorylationECLSREGSPIPHDPE
HHHCCCCCCCCCCCC		18.2029255136
455PhosphorylationPHDPEFGSKLASVPE
CCCCCHHHHHCCCCC		29.8022167270
459PhosphorylationEFGSKLASVPEYRYS
CHHHHHCCCCCCCCC		48.9525159151
463PhosphorylationKLASVPEYRYSQSAP
HHCCCCCCCCCCCCC		14.5829514088
465PhosphorylationASVPEYRYSQSAPGS
CCCCCCCCCCCCCCC		15.3424043423
466PhosphorylationSVPEYRYSQSAPGSP
CCCCCCCCCCCCCCC		14.5226055452
468PhosphorylationPEYRYSQSAPGSPVS
CCCCCCCCCCCCCCC		30.4125159151
472PhosphorylationYSQSAPGSPVSAQPV
CCCCCCCCCCCCCCE		22.5225159151
475PhosphorylationSAPGSPVSAQPVIMA
CCCCCCCCCCCEEEE		25.2725159151
488PhosphorylationMAVPPRPSSLVAKPV
EECCCCCHHHCCCCE		37.2724043423
489PhosphorylationAVPPRPSSLVAKPVA
ECCCCCHHHCCCCEE		29.5524043423
497PhosphorylationLVAKPVAYMPASIVT
HCCCCEEECCHHEEE		12.1320068231
501PhosphorylationPVAYMPASIVTSQQP
CEEECCHHEEECCCC		16.2420068231
504PhosphorylationYMPASIVTSQQPAGH
ECCHHEEECCCCCCC		21.1020068231
505O-linked_GlycosylationMPASIVTSQQPAGHA
CCHHEEECCCCCCCC		18.8723301498
505PhosphorylationMPASIVTSQQPAGHA
CCHHEEECCCCCCCC		18.8720068231
521O-linked_GlycosylationHVVQQAPTVTMVRVV
EEEEECCEEEEEEEE		31.4623301498
521PhosphorylationHVVQQAPTVTMVRVV
EEEEECCEEEEEEEE		31.4620068231
523O-linked_GlycosylationVQQAPTVTMVRVVTT
EEECCEEEEEEEEEC		16.6623301498
523PhosphorylationVQQAPTVTMVRVVTT
EEECCEEEEEEEEEC		16.6620068231
529O-linked_GlycosylationVTMVRVVTTSANSAN
EEEEEEEECCCCCCC		16.5123301498
529PhosphorylationVTMVRVVTTSANSAN
EEEEEEEECCCCCCC		16.5122210691
530O-linked_GlycosylationTMVRVVTTSANSANG
EEEEEEECCCCCCCC		17.7723301498
531O-linked_GlycosylationMVRVVTTSANSANGY
EEEEEECCCCCCCCE		18.9823301498
534O-linked_GlycosylationVVTTSANSANGYILT
EEECCCCCCCCEEEE		23.8723301498
541O-linked_GlycosylationSANGYILTSQGAAGG
CCCCEEEECCCCCCC		14.9423301498
542O-linked_GlycosylationANGYILTSQGAAGGS
CCCEEEECCCCCCCC		24.1523301498
542PhosphorylationANGYILTSQGAAGGS
CCCEEEECCCCCCCC		24.1522210691
549O-linked_GlycosylationSQGAAGGSHDAAGAA
CCCCCCCCCCHHHEE		19.7823301498
562O-linked_GlycosylationAAVLDLGSEARGLEE
EEEEECCCCCCCCCC		35.0723301498
572O-linked_GlycosylationRGLEEKPTIAFATIP
CCCCCCCCEEEEECC		35.6923301498
587O-linked_GlycosylationAAGGVIQTVASQMAP
CCCHHHHHHHHHCCC		13.6023301498
590O-linked_GlycosylationGVIQTVASQMAPGVP
HHHHHHHHHCCCCCC		19.0223301498
600O-linked_GlycosylationAPGVPGHTVTILQPA
CCCCCCCEEEEECCC		25.8423301498
600PhosphorylationAPGVPGHTVTILQPA
CCCCCCCEEEEECCC		25.8427251275
602O-linked_GlycosylationGVPGHTVTILQPATP
CCCCCEEEEECCCCC		19.6823301498
602PhosphorylationGVPGHTVTILQPATP
CCCCCEEEEECCCCC		19.6827251275
608O-linked_GlycosylationVTILQPATPVTLGQH
EEEECCCCCCCCCCC		25.6023301498
608PhosphorylationVTILQPATPVTLGQH
EEEECCCCCCCCCCC		25.6027251275
611O-linked_GlycosylationLQPATPVTLGQHHLP
ECCCCCCCCCCCCCC		26.7823301498
632O-linked_GlycosylationNGKHAVPTNSLAGNA
CCCCCCCCCCCCCCH		30.7323301498
632PhosphorylationNGKHAVPTNSLAGNA
CCCCCCCCCCCCCCH		30.7328122231
634PhosphorylationKHAVPTNSLAGNAYA
CCCCCCCCCCCCHHH		23.2928122231
640PhosphorylationNSLAGNAYALTSPLQ
CCCCCCHHHCCCHHH		13.2228122231
643O-linked_GlycosylationAGNAYALTSPLQLLA
CCCHHHCCCHHHHHH		21.8123301498
643PhosphorylationAGNAYALTSPLQLLA
CCCHHHCCCHHHHHH		21.8128450419
644O-linked_GlycosylationGNAYALTSPLQLLAT
CCHHHCCCHHHHHHH		25.1823301498
644PhosphorylationGNAYALTSPLQLLAT
CCHHHCCCHHHHHHH		25.1825159151
651O-linked_GlycosylationSPLQLLATQASSSAP
CHHHHHHHHHCCCCC		25.3323301498
651PhosphorylationSPLQLLATQASSSAP
CHHHHHHHHHCCCCC		25.3328450419
654O-linked_GlycosylationQLLATQASSSAPVVV
HHHHHHHCCCCCEEE		18.2723301498
654PhosphorylationQLLATQASSSAPVVV
HHHHHHHCCCCCEEE		18.2728122231
655O-linked_GlycosylationLLATQASSSAPVVVT
HHHHHHCCCCCEEEE		33.2723301498
655PhosphorylationLLATQASSSAPVVVT
HHHHHHCCCCCEEEE		33.2728450419
656O-linked_GlycosylationLATQASSSAPVVVTR
HHHHHCCCCCEEEEE		33.8123301498
656PhosphorylationLATQASSSAPVVVTR
HHHHHCCCCCEEEEE		33.8128450419
662O-linked_GlycosylationSSAPVVVTRVCEVGP
CCCCEEEEEEEECCC		13.0323301498
662PhosphorylationSSAPVVVTRVCEVGP
CCCCEEEEEEEECCC		13.0320068231
679O-linked_GlycosylationPAAAVAATATTTPAT
CHHHHEEEEECCCCC		18.1423301498
682PhosphorylationAVAATATTTPATATT
HHEEEEECCCCCCCC		28.4630576142
683O-linked_GlycosylationVAATATTTPATATTA
HEEEEECCCCCCCCC		13.4323301498
683PhosphorylationVAATATTTPATATTA
HEEEEECCCCCCCCC		13.43-
686PhosphorylationTATTTPATATTASAS
EEECCCCCCCCCCCC		26.24-
691PhosphorylationPATATTASASASSTG
CCCCCCCCCCCCCCC		22.2130576142
693PhosphorylationTATTASASASSTGEP
CCCCCCCCCCCCCCC		26.6230576142
695PhosphorylationTTASASASSTGEPEV
CCCCCCCCCCCCCCC		26.41-
696PhosphorylationTASASASSTGEPEVK
CCCCCCCCCCCCCCH		39.90-
715PhosphorylationEEPSGAVTTPAGVIA
CCCCCCCCCCCCEEE		26.9125159151
716PhosphorylationEPSGAVTTPAGVIAA
CCCCCCCCCCCEEEE		12.4425159151
731PhosphorylationAGPQGPGTGE-----
CCCCCCCCCC-----		41.0725159151
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 FOXK1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOXK1_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 FOXK1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CMYA5_HUMANCMYA5physical
22863883
EF1D_HUMANEEF1Dphysical
22863883
GAPD1_HUMANGAPVD1physical
22863883
DPOD2_HUMANPOLD2physical
22863883
ANM5_HUMANPRMT5physical
22863883
UBP24_HUMANUSP24physical
22863883
VASP_HUMANVASPphysical
22863883
NAA10_HUMANNAA10physical
26344197
BAP1_HUMANBAP1physical
25451922
HCFC1_HUMANHCFC1physical
25451922
AP5Z1_HUMANAP5Z1physical
25609649
SIN3A_HUMANSIN3Aphysical
25609649
FOXK2_HUMANFOXK2physical
25609649
NCOR1_HUMANNCOR1physical
25609649
SDS3_HUMANSUDS3physical
25609649
TBL1R_HUMANTBL1XR1physical
25609649
ARI4A_HUMANARID4Aphysical
25609649
UBA7_HUMANUBA7physical
25609649
UBR4_HUMANUBR4physical
25609649
ARI4B_HUMANARID4Bphysical
25609649
E2AK3_HUMANEIF2AK3physical
25609649
CHK2_HUMANCHEK2physical
25609649
TP53B_HUMANTP53BP1physical
25609649
URFB1_HUMANUHRF1BP1physical
25609649
ANR52_HUMANANKRD52physical
25609649
KPB2_HUMANPHKA2physical
25609649
RBL1_HUMANRBL1physical
25609649
BAP1_HUMANBAP1physical
25609649
DVL2_HUMANDVL2physical
25609649
AGGF1_HUMANAGGF1physical
25609649
SP130_HUMANSAP130physical
25609649
UBP47_HUMANUSP47physical
25609649
BRM1L_HUMANBRMS1Lphysical
25609649
K0513_HUMANKIAA0513physical
25609649
RB_HUMANRB1physical
25609649
KANK2_HUMANKANK2physical
25609649
SCRIB_HUMANSCRIBphysical
25609649
SAHH_HUMANAHCYphysical
25609649
ANR28_HUMANANKRD28physical
25609649
BRMS1_HUMANBRMS1physical
25609649
PHKG2_HUMANPHKG2physical
25609649
RBL2_HUMANRBL2physical
25609649
SAP30_HUMANSAP30physical
25609649
TBCD4_HUMANTBC1D4physical
25609649
ABHDA_HUMANABHD10physical
25609649
CBPC1_HUMANAGTPBP1physical
25609649
GPS2_HUMANGPS2physical
25609649
HDAC2_HUMANHDAC2physical
25609649
ING2_HUMANING2physical
25609649
PP6R1_HUMANPPP6R1physical
25609649
P53_HUMANTP53physical
25609649
UBP28_HUMANUSP28physical
25609649
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 FOXK1_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-101; SER-213; SER-223; SER-236; SER-239;SER-243; SER-257; SER-416; SER-420; SER-428; THR-436 AND SER-441, ANDMASS 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-213 AND SER-223, 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-101; SER-213; SER-223; SER-236; SER-239;SER-243; SER-257; SER-416; SER-420; SER-428; THR-436 AND SER-441, 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-101; SER-213; SER-223;SER-239; SER-243; THR-247; SER-253; SER-257; SER-416; SER-420;THR-422; SER-428; SER-441; SER-445 AND SER-455, 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-213; SER-223; THR-245;THR-247; SER-416; SER-428 AND THR-436, AND MASS SPECTROMETRY.
"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-420; THR-422; THR-436AND SER-445, 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-213; SER-223 ANDSER-445, 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-213; SER-223; SER-416;SER-420; SER-428; THR-436; SER-441 AND SER-445, 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-416 AND SER-420, ANDMASS SPECTROMETRY.

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