TIF1A_HUMAN - dbPTM
TIF1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TIF1A_HUMAN
UniProt AC O15164
Protein Name Transcription intermediary factor 1-alpha
Gene Name TRIM24
Organism Homo sapiens (Human).
Sequence Length 1050
Subcellular Localization Nucleus . Cytoplasm . Colocalizes with sites of active transcription. Detected both in nucleus and cytoplasm in some breast cancer samples. Predominantly nuclear.
Protein Description Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has E3 protein-ubiquitin ligase activity. Promotes ubiquitination and proteasomal degradation of p53/TP53. Plays a role in the regulation of cell proliferation and apoptosis, at least in part via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, including RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes (By similarity)..
Protein Sequence MEVAVEKAVAAAAAASAAASGGPSAAPSGENEAESRQGPDSERGGEAARLNLLDTCAVCHQNIQSRAPKLLPCLHSFCQRCLPAPQRYLMLPAPMLGSAETPPPVPAPGSPVSGSSPFATQVGVIRCPVCSQECAERHIIDNFFVKDTTEVPSSTVEKSNQVCTSCEDNAEANGFCVECVEWLCKTCIRAHQRVKFTKDHTVRQKEEVSPEAVGVTSQRPVFCPFHKKEQLKLYCETCDKLTCRDCQLLEHKEHRYQFIEEAFQNQKVIIDTLITKLMEKTKYIKFTGNQIQNRIIEVNQNQKQVEQDIKVAIFTLMVEINKKGKALLHQLESLAKDHRMKLMQQQQEVAGLSKQLEHVMHFSKWAVSSGSSTALLYSKRLITYRLRHLLRARCDASPVTNNTIQFHCDPSFWAQNIINLGSLVIEDKESQPQMPKQNPVVEQNSQPPSGLSSNQLSKFPTQISLAQLRLQHMQQQVMAQRQQVQRRPAPVGLPNPRMQGPIQQPSISHQQPPPRLINFQNHSPKPNGPVLPPHPQQLRYPPNQNIPRQAIKPNPLQMAFLAQQAIKQWQISSGQGTPSTTNSTSSTPSSPTITSAAGYDGKAFGSPMIDLSSPVGGSYNLPSLPDIDCSSTIMLDNIVRKDTNIDHGQPRPPSNRTVQSPNSSVPSPGLAGPVTMTSVHPPIRSPSASSVGSRGSSGSSSKPAGADSTHKVPVVMLEPIRIKQENSGPPENYDFPVVIVKQESDEESRPQNANYPRSILTSLLLNSSQSSTSEETVLRSDAPDSTGDQPGLHQDNSSNGKSEWLDPSQKSPLHVGETRKEDDPNEDWCAVCQNGGELLCCEKCPKVFHLSCHVPTLTNFPSGEWICTFCRDLSKPEVEYDCDAPSHNSEKKKTEGLVKLTPIDKRKCERLLLFLYCHEMSLAFQDPVPLTVPDYYKIIKNPMDLSTIKKRLQEDYSMYSKPEDFVADFRLIFQNCAEFNEPDSEVANAGIKLENYFEELLKNLYPEKRFPKPEFRNESEDNKFSDDSDDDFVQPRKKRLKSIEERQLLK
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
7Sumoylation-MEVAVEKAVAAAAA
-CCHHHHHHHHHHHH		41.3828112733
16PhosphorylationVAAAAAASAAASGGP
HHHHHHHHHHHHCCC		17.4526261332
20PhosphorylationAAASAAASGGPSAAP
HHHHHHHHCCCCCCC		39.2926261332
24PhosphorylationAAASGGPSAAPSGEN
HHHHCCCCCCCCCCC		40.1026261332
28PhosphorylationGGPSAAPSGENEAES
CCCCCCCCCCCHHHH		54.7526261332
35PhosphorylationSGENEAESRQGPDSE
CCCCHHHHCCCCCCC		36.6326261332
41PhosphorylationESRQGPDSERGGEAA
HHCCCCCCCCCHHHH		32.1226261332
76PhosphorylationKLLPCLHSFCQRCLP
HHHHHHHHHHHHHCC		18.1227080861
98PhosphorylationLPAPMLGSAETPPPV
CCCCCCCCCCCCCCC		20.9722199227
101PhosphorylationPMLGSAETPPPVPAP
CCCCCCCCCCCCCCC		40.5922199227
101 (in isoform 2)Phosphorylation-40.59-
110PhosphorylationPPVPAPGSPVSGSSP
CCCCCCCCCCCCCCC		22.5221082442
110 (in isoform 2)Phosphorylation-22.52-
113PhosphorylationPAPGSPVSGSSPFAT
CCCCCCCCCCCCCCC		36.0228450419
115PhosphorylationPGSPVSGSSPFATQV
CCCCCCCCCCCCCEE		27.6028450419
116PhosphorylationGSPVSGSSPFATQVG
CCCCCCCCCCCCEEC		27.8028450419
120PhosphorylationSGSSPFATQVGVIRC
CCCCCCCCEECEEEC		24.9429523821
148PhosphorylationDNFFVKDTTEVPSST
CCEEECCCCCCCCHH		21.09-
153PhosphorylationKDTTEVPSSTVEKSN
CCCCCCCCHHHCCCC		43.76-
154PhosphorylationDTTEVPSSTVEKSNQ
CCCCCCCHHHCCCCC		30.33-
185AcetylationECVEWLCKTCIRAHQ
HHHHHHHHHHHHHHH		44.2419413330
185 (in isoform 2)Acetylation-44.24-
205SumoylationKDHTVRQKEEVSPEA
CCCCCCCCCCCCHHH		45.3228112733
209PhosphorylationVRQKEEVSPEAVGVT
CCCCCCCCHHHCCCC		21.9425159151
216PhosphorylationSPEAVGVTSQRPVFC
CHHHCCCCCCCCCCC		17.1424732914
217PhosphorylationPEAVGVTSQRPVFCP
HHHCCCCCCCCCCCC		23.0624732914
234PhosphorylationKKEQLKLYCETCDKL
CHHHHHHHHHHCCCE		6.15-
240AcetylationLYCETCDKLTCRDCQ
HHHHHCCCEECCCCC		48.0926051181
252UbiquitinationDCQLLEHKEHRYQFI
CCCHHCCHHHHHHHH		45.93-
276SumoylationIIDTLITKLMEKTKY
HHHHHHHHHHHHCCC		38.5528112733
285UbiquitinationMEKTKYIKFTGNQIQ
HHHCCCEEECCHHHH		33.51-
303UbiquitinationIEVNQNQKQVEQDIK
EECCCCHHHHHHHHH		64.9521906983
303 (in isoform 1)Ubiquitination-64.9521890473
303 (in isoform 2)Ubiquitination-64.9521890473
325UbiquitinationVEINKKGKALLHQLE
HHHHHHHHHHHHHHH		44.7521890473
325UbiquitinationVEINKKGKALLHQLE
HHHHHHHHHHHHHHH		44.7521890473
325UbiquitinationVEINKKGKALLHQLE
HHHHHHHHHHHHHHH		44.7521890473
325 (in isoform 1)Ubiquitination-44.7521890473
325 (in isoform 2)Ubiquitination-44.7521890473
336UbiquitinationHQLESLAKDHRMKLM
HHHHHHHHHHHHHHH		60.40-
341UbiquitinationLAKDHRMKLMQQQQE
HHHHHHHHHHHHHHH		40.5421890473
341UbiquitinationLAKDHRMKLMQQQQE
HHHHHHHHHHHHHHH		40.5421890473
341UbiquitinationLAKDHRMKLMQQQQE
HHHHHHHHHHHHHHH		40.5421890473
341 (in isoform 1)Ubiquitination-40.5421890473
341 (in isoform 2)Ubiquitination-40.5421890473
343SulfoxidationKDHRMKLMQQQQEVA
HHHHHHHHHHHHHHH		2.5621406390
436SumoylationESQPQMPKQNPVVEQ
CCCCCCCCCCCCCCC		58.3228112733
445PhosphorylationNPVVEQNSQPPSGLS
CCCCCCCCCCCCCCC		43.7030257219
449PhosphorylationEQNSQPPSGLSSNQL
CCCCCCCCCCCHHHH		60.0822210691
452PhosphorylationSQPPSGLSSNQLSKF
CCCCCCCCHHHHHHC		30.6722210691
458UbiquitinationLSSNQLSKFPTQISL
CCHHHHHHCCHHHHH		65.0521890473
458UbiquitinationLSSNQLSKFPTQISL
CCHHHHHHCCHHHHH		65.0521890473
458SumoylationLSSNQLSKFPTQISL
CCHHHHHHCCHHHHH		65.0528112733
458UbiquitinationLSSNQLSKFPTQISL
CCHHHHHHCCHHHHH		65.0521890473
458 (in isoform 1)Ubiquitination-65.0521890473
458 (in isoform 2)Ubiquitination-65.0521890473
461PhosphorylationNQLSKFPTQISLAQL
HHHHHCCHHHHHHHH		41.4928555341
469MethylationQISLAQLRLQHMQQQ
HHHHHHHHHHHHHHH		21.8824411089
481MethylationQQQVMAQRQQVQRRP
HHHHHHHHHHHHHCC		21.25115918953
552SumoylationNIPRQAIKPNPLQMA
CCCCCCCCCCHHHHH		41.5828112733
580O-linked_GlycosylationSGQGTPSTTNSTSST
CCCCCCCCCCCCCCC		31.0630620550
589PhosphorylationNSTSSTPSSPTITSA
CCCCCCCCCCCCCCC		49.3823186163
590PhosphorylationSTSSTPSSPTITSAA
CCCCCCCCCCCCCCC		27.5423917254
592PhosphorylationSSTPSSPTITSAAGY
CCCCCCCCCCCCCCC		38.5423186163
606PhosphorylationYDGKAFGSPMIDLSS
CCCCCCCCCCEECCC		12.5825159151
612PhosphorylationGSPMIDLSSPVGGSY
CCCCEECCCCCCCCC		28.9325627689
626 (in isoform 2)Phosphorylation-55.43-
633 (in isoform 2)Phosphorylation-2.52-
641SumoylationMLDNIVRKDTNIDHG
EECHHHCCCCCCCCC		58.9928112733
641UbiquitinationMLDNIVRKDTNIDHG
EECHHHCCCCCCCCC		58.99-
643PhosphorylationDNIVRKDTNIDHGQP
CHHHCCCCCCCCCCC		36.7923403867
651 (in isoform 2)Phosphorylation-48.12-
653 (in isoform 2)Phosphorylation-45.58-
654PhosphorylationHGQPRPPSNRTVQSP
CCCCCCCCCCCCCCC		41.4423401153
657PhosphorylationPRPPSNRTVQSPNSS
CCCCCCCCCCCCCCC		27.4423401153
660PhosphorylationPSNRTVQSPNSSVPS
CCCCCCCCCCCCCCC		23.0123401153
663PhosphorylationRTVQSPNSSVPSPGL
CCCCCCCCCCCCCCC		35.7823927012
664PhosphorylationTVQSPNSSVPSPGLA
CCCCCCCCCCCCCCC		44.6923927012
667PhosphorylationSPNSSVPSPGLAGPV
CCCCCCCCCCCCCCE		29.4623401153
675PhosphorylationPGLAGPVTMTSVHPP
CCCCCCEEEEECCCC		20.1928450419
677PhosphorylationLAGPVTMTSVHPPIR
CCCCEEEEECCCCCC		20.4528450419
678PhosphorylationAGPVTMTSVHPPIRS
CCCEEEEECCCCCCC		13.9628450419
685PhosphorylationSVHPPIRSPSASSVG
ECCCCCCCCCCCCCC		24.7526055452
687PhosphorylationHPPIRSPSASSVGSR
CCCCCCCCCCCCCCC		41.8723401153
689PhosphorylationPIRSPSASSVGSRGS
CCCCCCCCCCCCCCC		29.8721406692
689 (in isoform 2)Sumoylation-29.87-
690PhosphorylationIRSPSASSVGSRGSS
CCCCCCCCCCCCCCC		30.1630576142
693PhosphorylationPSASSVGSRGSSGSS
CCCCCCCCCCCCCCC		31.1725627689
696PhosphorylationSSVGSRGSSGSSSKP
CCCCCCCCCCCCCCC		30.3425159151
697PhosphorylationSVGSRGSSGSSSKPA
CCCCCCCCCCCCCCC		45.5825627689
699PhosphorylationGSRGSSGSSSKPAGA
CCCCCCCCCCCCCCC		33.1325627689
700PhosphorylationSRGSSGSSSKPAGAD
CCCCCCCCCCCCCCC		46.0025627689
701PhosphorylationRGSSGSSSKPAGADS
CCCCCCCCCCCCCCC		44.3429214152
702SumoylationGSSGSSSKPAGADST
CCCCCCCCCCCCCCC		40.61-
702SumoylationGSSGSSSKPAGADST
CCCCCCCCCCCCCCC		40.6128112733
707 (in isoform 2)Sumoylation-53.82-
708PhosphorylationSKPAGADSTHKVPVV
CCCCCCCCCCCCCEE		31.7021712546
709PhosphorylationKPAGADSTHKVPVVM
CCCCCCCCCCCCEEE		26.6821712546
711SumoylationAGADSTHKVPVVMLE
CCCCCCCCCCEEEEE		48.61-
711SumoylationAGADSTHKVPVVMLE
CCCCCCCCCCEEEEE		48.6128112733
723SumoylationMLEPIRIKQENSGPP
EEEEEEEECCCCCCC		41.53-
723SumoylationMLEPIRIKQENSGPP
EEEEEEEECCCCCCC		41.5325114211
727PhosphorylationIRIKQENSGPPENYD
EEEECCCCCCCCCCC		52.5021945579
733PhosphorylationNSGPPENYDFPVVIV
CCCCCCCCCCCEEEE		19.8021945579
734 (in isoform 2)Phosphorylation-53.61-
737 (in isoform 2)Phosphorylation-4.66-
738 (in isoform 2)Phosphorylation-4.19-
739 (in isoform 2)Phosphorylation-3.05-
741SumoylationDFPVVIVKQESDEES
CCCEEEEECCCCCCC		36.9028112733
744PhosphorylationVVIVKQESDEESRPQ
EEEEECCCCCCCCCC		48.0723401153
748PhosphorylationKQESDEESRPQNANY
ECCCCCCCCCCCCCC		47.4120363803
755PhosphorylationSRPQNANYPRSILTS
CCCCCCCCCHHHHHH		9.5230266825
758PhosphorylationQNANYPRSILTSLLL
CCCCCCHHHHHHHHH		19.9024732914
761PhosphorylationNYPRSILTSLLLNSS
CCCHHHHHHHHHCCC		18.6924732914
762PhosphorylationYPRSILTSLLLNSSQ
CCHHHHHHHHHCCCC		17.3625159151
767PhosphorylationLTSLLLNSSQSSTSE
HHHHHHCCCCCCCCC		29.7123663014
768PhosphorylationTSLLLNSSQSSTSEE
HHHHHCCCCCCCCCC		32.7717525332
770PhosphorylationLLLNSSQSSTSEETV
HHHCCCCCCCCCCEE		37.2223663014
771PhosphorylationLLNSSQSSTSEETVL
HHCCCCCCCCCCEEE		28.4630278072
772PhosphorylationLNSSQSSTSEETVLR
HCCCCCCCCCCEEEC		45.4620044836
773PhosphorylationNSSQSSTSEETVLRS
CCCCCCCCCCEEECC		35.0728102081
774 (in isoform 2)Phosphorylation-58.75-
776PhosphorylationQSSTSEETVLRSDAP
CCCCCCCEEECCCCC		22.3124732914
777 (in isoform 2)Phosphorylation-4.77-
780PhosphorylationSEETVLRSDAPDSTG
CCCEEECCCCCCCCC		33.6821406692
784 (in isoform 2)Phosphorylation-61.63-
785PhosphorylationLRSDAPDSTGDQPGL
ECCCCCCCCCCCCCC		32.9821406692
786PhosphorylationRSDAPDSTGDQPGLH
CCCCCCCCCCCCCCC		52.7528450419
797PhosphorylationPGLHQDNSSNGKSEW
CCCCCCCCCCCCCCC		33.2125849741
798PhosphorylationGLHQDNSSNGKSEWL
CCCCCCCCCCCCCCC		56.7223663014
801SumoylationQDNSSNGKSEWLDPS
CCCCCCCCCCCCCCH		49.83-
801AcetylationQDNSSNGKSEWLDPS
CCCCCCCCCCCCCCH		49.8326051181
801SumoylationQDNSSNGKSEWLDPS
CCCCCCCCCCCCCCH		49.8328112733
802PhosphorylationDNSSNGKSEWLDPSQ
CCCCCCCCCCCCCHH		35.0923927012
808PhosphorylationKSEWLDPSQKSPLHV
CCCCCCCHHCCCCCC		50.3223927012
810SumoylationEWLDPSQKSPLHVGE
CCCCCHHCCCCCCCC		59.3828112733
811PhosphorylationWLDPSQKSPLHVGET
CCCCHHCCCCCCCCC		25.6729255136
818PhosphorylationSPLHVGETRKEDDPN
CCCCCCCCCCCCCCC		40.9023927012
820AcetylationLHVGETRKEDDPNED
CCCCCCCCCCCCCCC		73.2826051181
874PhosphorylationCTFCRDLSKPEVEYD
ECCCCHHCCCCCEEC		50.91-
875AcetylationTFCRDLSKPEVEYDC
CCCCHHCCCCCEECC		53.1226051181
875SumoylationTFCRDLSKPEVEYDC
CCCCHHCCCCCEECC		53.1228112733
889PhosphorylationCDAPSHNSEKKKTEG
CCCCCCCCCCCCCCC		45.4228555341
891AcetylationAPSHNSEKKKTEGLV
CCCCCCCCCCCCCCC		60.4326051181
916PhosphorylationERLLLFLYCHEMSLA
HHHHHHHHHHHHHHH		5.61-
936PhosphorylationPLTVPDYYKIIKNPM
CCCCCCHHHHHCCCC		11.77-
940SumoylationPDYYKIIKNPMDLST
CCHHHHHCCCCCHHH		59.48-
940SumoylationPDYYKIIKNPMDLST
CCHHHHHCCCCCHHH		59.48-
949SumoylationPMDLSTIKKRLQEDY
CCCHHHHHHHHHHCH		31.74-
949SumoylationPMDLSTIKKRLQEDY
CCCHHHHHHHHHHCH		31.7425218447
960PhosphorylationQEDYSMYSKPEDFVA
HHCHHCCCCCHHHHH		32.8524719451
985 (in isoform 2)Phosphorylation-53.69-
991 (in isoform 2)Phosphorylation-4.23-
992SumoylationEVANAGIKLENYFEE
HHHHHCCCHHHHHHH		49.1628112733
994 (in isoform 2)Phosphorylation-44.90-
996PhosphorylationAGIKLENYFEELLKN
HCCCHHHHHHHHHHH		11.73-
1002UbiquitinationNYFEELLKNLYPEKR
HHHHHHHHHHCCCCC		58.49-
1008 (in isoform 2)Phosphorylation-55.63-
1019PhosphorylationKPEFRNESEDNKFSD
CHHHCCCCCCCCCCC		54.5229255136
1025PhosphorylationESEDNKFSDDSDDDF
CCCCCCCCCCCCCCC		41.9629255136
1028PhosphorylationDNKFSDDSDDDFVQP
CCCCCCCCCCCCCCH		48.1829255136
1041SumoylationQPRKKRLKSIEERQL
CHHHHHHHHHHHHHH		54.1125772364
1042PhosphorylationPRKKRLKSIEERQLL
HHHHHHHHHHHHHHC		39.5623401153
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
768SPhosphorylationKinaseATMQ13315
PSP
-KUbiquitinationE3 ubiquitin ligaseSPOPO43791
PMID:25278611
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TIF1A_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 TIF1A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TIF1A_HUMANTRIM24physical
12684500
PML_HUMANPMLphysical
10610177
TIF1A_HUMANTRIM24physical
11331580
MCR_HUMANNR3C2physical
11518808
ESR1_HUMANESR1physical
9115274
THA_HUMANTHRAphysical
9115274
RARA_HUMANRARAphysical
9115274
RXRA_HUMANRXRAphysical
9115274
GCR_HUMANNR3C1physical
9115274
MCR_HUMANNR3C2physical
9115274
ANDR_HUMANARphysical
9115274
TIF1A_HUMANTRIM24physical
12096914
TRI33_HUMANTRIM33physical
12096914
T2EA_HUMANGTF2E1physical
9632676
TAF7_HUMANTAF7physical
9632676
TAF11_HUMANTAF11physical
9632676
ESR1_HUMANESR1physical
10598587
RARA_HUMANRARAphysical
12503607
P53_HUMANTP53physical
19556538
ANDR_HUMANARphysical
19909775
BRD7_HUMANBRD7physical
19909775
P53_HUMANTP53physical
22389628
H31_HUMANHIST1H3Aphysical
21164480
H4_HUMANHIST1H4Iphysical
21164480
RN141_HUMANRNF141physical
22493164
RN181_HUMANRNF181physical
22493164
TRIM8_HUMANTRIM8physical
22493164
TRI33_HUMANTRIM33physical
24820418
P53_HUMANTP53physical
24820418
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
188550Thyroid papillary carcinoma (TPC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TIF1A_HUMAN

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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-1025 AND SER-1028, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-687; SER-1025 ANDSER-1028, AND MASS 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-660; SER-667; SER-768;SER-808; SER-811; SER-1019; SER-1025 AND SER-1028, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-768, 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-811, AND MASSSPECTROMETRY.

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