dbPTM

PHF8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PHF8_HUMAN
UniProt AC	Q9UPP1
Protein Name	Histone lysine demethylase PHF8
Gene Name	PHF8
Organism	Homo sapiens (Human).
Sequence Length	1060
Subcellular Localization	Nucleus. Nucleus, nucleolus. Recruited to H3K4me3 sites on chromatin during interphase. Dissociates from chromatin when cells enter mitosis.
Protein Description	Histone lysine demethylase with selectivity for the di- and monomethyl states that plays a key role cell cycle progression, rDNA transcription and brain development. Demethylates mono- and dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks. Involved in cell cycle progression by being required to control G1-S transition. Acts as a coactivator of rDNA transcription, by activating polymerase I (pol I) mediated transcription of rRNA genes. Required for brain development, probably by regulating expression of neuron-specific genes. Only has activity toward H4K20Me1 when nucleosome is used as a substrate and when not histone octamer is used as substrate. May also have weak activity toward dimethylated H3 'Lys-36' (H3K36Me2), however, the relevance of this result remains unsure in vivo. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: has weak activity toward H3K9Me2 in absence of H3K4me3, while it has high activity toward H3K9me2 when binding H3K4me3..
Protein Sequence	MNRSRAIVQRGRVLPPPAPLDTTNLAGRRTLQGRAKMASVPVYCLCRLPYDVTRFMIECDMCQDWFHGSCVGVEEEKAADIDLYHCPNCEVLHGPSIMKKRRGSSKGHDTHKGKPVKTGSPTFVRELRSRTFDSSDEVILKPTGNQLTVEFLEENSFSVPILVLKKDGLGMTLPSPSFTVRDVEHYVGSDKEIDVIDVTRQADCKMKLGDFVKYYYSGKREKVLNVISLEFSDTRLSNLVETPKIVRKLSWVENLWPEECVFERPNVQKYCLMSVRDSYTDFHIDFGGTSVWYHVLKGEKIFYLIRPTNANLTLFECWSSSSNQNEMFFGDQVDKCYKCSVKQGQTLFIPTGWIHAVLTPVDCLAFGGNFLHSLNIEMQLKAYEIEKRLSTADLFRFPNFETICWYVGKHILDIFRGLRENRRHPASYLVHGGKALNLAFRAWTRKEALPDHEDEIPETVRTVQLIKDLAREIRLVEDIFQQNVGKTSNIFGLQRIFPAGSIPLTRPAHSTSVSMSRLSLPSKNGSKKKGLKPKELFKKAERKGKESSALGPAGQLSYNLMDTYSHQALKTGSFQKAKFNITGACLNDSDDDSPDLDLDGNESPLALLMSNGSTKRVKSLSKSRRTKIAKKVDKARLMAEQVMEDEFDLDSDDELQIDERLGKEKATLIIRPKFPRKLPRAKPCSDPNRVREPGEVEFDIEEDYTTDEDMVEGVEGKLGNGSGAGGILDLLKASRQVGGPDYAALTEAPASPSTQEAIQGMLCMANLQSSSSSPATSSLQAWWTGGQDRSSGSSSSGLGTVSNSPASQRTPGKRPIKRPAYWRTESEEEEENASLDEQDSLGACFKDAEYIYPSLESDDDDPALKSRPKKKKNSDDAPWSPKARVTPTLPKQDRPVREGTRVASIETGLAAAAAKLAQQELQKAQKKKYIKKKPLLKEVEQPRPQDSNLSLTVPAPTVAATPQLVTSSSPLPPPEPKQEALSGSLADHEYTARPNAFGMAQANRSTTPMAPGVFLTQRRPSVGSQSNQAGQGKRPKKGLATAKQRLGRILKIHRNGKLLL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
22	Phosphorylation	PPPAPLDTTNLAGRR CCCCCCCCCCCCCCC	25.85	-
23	Phosphorylation	PPAPLDTTNLAGRRT CCCCCCCCCCCCCCC	28.09	-
36	Acetylation	RTLQGRAKMASVPVY CCCCCCHHHCCCCEE	33.37	25953088
36	Ubiquitination	RTLQGRAKMASVPVY CCCCCCHHHCCCCEE	33.37	-
69	Phosphorylation	CQDWFHGSCVGVEEE CCHHHCCCCCCCCHH	9.32	20622854
84 (in isoform 2)	Phosphorylation	-	9.53	-
100	Ubiquitination	HGPSIMKKRRGSSKG CCCCHHCCCCCCCCC	29.92	-
104	Phosphorylation	IMKKRRGSSKGHDTH HHCCCCCCCCCCCCC	27.37	24260401
105	Phosphorylation	MKKRRGSSKGHDTHK HCCCCCCCCCCCCCC	45.54	-
117	Ubiquitination	THKGKPVKTGSPTFV CCCCCCCCCCCCCHH	56.55	-
118	Phosphorylation	HKGKPVKTGSPTFVR CCCCCCCCCCCCHHH	43.03	30266825
120	Phosphorylation	GKPVKTGSPTFVREL CCCCCCCCCCHHHHH	26.46	25159151
122	Phosphorylation	PVKTGSPTFVRELRS CCCCCCCCHHHHHHH	36.14	22199227
131	Phosphorylation	VRELRSRTFDSSDEV HHHHHHCCCCCCCCE	32.80	22468782
135	Phosphorylation	RSRTFDSSDEVILKP HHCCCCCCCCEEEEC	39.37	22468782
166	Ubiquitination	VPILVLKKDGLGMTL CEEEEEEECCCCCCC	53.52	-
175	Phosphorylation	GLGMTLPSPSFTVRD CCCCCCCCCCEECCE	35.97	28348404
179	Phosphorylation	TLPSPSFTVRDVEHY CCCCCCEECCEEHHH	20.97	24719451
191	Ubiquitination	EHYVGSDKEIDVIDV HHHCCCCCEEEEEEE	59.26	-
207	Ubiquitination	RQADCKMKLGDFVKY CCCCCCCCHHHHHHH	34.51	-
213	Ubiquitination	MKLGDFVKYYYSGKR CCHHHHHHHHHCCCH	27.77	-
214	Phosphorylation	KLGDFVKYYYSGKRE CHHHHHHHHHCCCHH	11.44	-
215	Phosphorylation	LGDFVKYYYSGKREK HHHHHHHHHCCCHHH	5.85	-
216	Phosphorylation	GDFVKYYYSGKREKV HHHHHHHHCCCHHHE	14.09	-
219	Acetylation	VKYYYSGKREKVLNV HHHHHCCCHHHEEEE	51.98	23749302
219	Ubiquitination	VKYYYSGKREKVLNV HHHHHCCCHHHEEEE	51.98	-
244	Methylation	SNLVETPKIVRKLSW HHHCCCHHHHHHHHH	62.34	-
248	Ubiquitination	ETPKIVRKLSWVENL CCHHHHHHHHHHHHH	35.66	-
303	Phosphorylation	LKGEKIFYLIRPTNA ECCCEEEEEECCCCC	12.51	22817900
359	Phosphorylation	GWIHAVLTPVDCLAF CHHHEEEEHHHHHHC	18.05	-
373	Phosphorylation	FGGNFLHSLNIEMQL CCCHHHHHCCHHHHH	25.84	-
383	Phosphorylation	IEMQLKAYEIEKRLS HHHHHHHHHHHHHHC	18.82	-
446	Ubiquitination	AFRAWTRKEALPDHE HHHHHHCHHHCCCCC	39.71	-
467	Ubiquitination	VRTVQLIKDLAREIR HHHHHHHHHHHHHHH	56.11	-
486	Ubiquitination	IFQQNVGKTSNIFGL HHHCCCCCCCCCCCC	44.49	-
486 (in isoform 2)	Phosphorylation	-	44.49	-
487	Phosphorylation	FQQNVGKTSNIFGLQ HHCCCCCCCCCCCCC	22.52	22210691
488	Phosphorylation	QQNVGKTSNIFGLQR HCCCCCCCCCCCCCE	31.26	22210691
505	Phosphorylation	PAGSIPLTRPAHSTS ECCCCCCCCCCCCCC	29.29	22210691
516	Phosphorylation	HSTSVSMSRLSLPSK CCCCCCCCCCCCCCC	23.67	26471730
519	Phosphorylation	SVSMSRLSLPSKNGS CCCCCCCCCCCCCCC	36.80	21815630
522	Phosphorylation	MSRLSLPSKNGSKKK CCCCCCCCCCCCCCC	44.01	20068231
523	Ubiquitination	SRLSLPSKNGSKKKG CCCCCCCCCCCCCCC	64.49	-
527	Ubiquitination	LPSKNGSKKKGLKPK CCCCCCCCCCCCCHH	60.96	-
528	Ubiquitination	PSKNGSKKKGLKPKE CCCCCCCCCCCCHHH	54.49	-
545	Ubiquitination	KKAERKGKESSALGP HHHHHCCCCCCCCCC	58.41	-
570	Ubiquitination	TYSHQALKTGSFQKA HCCCHHHHHCCCCEE	54.58	-
576	Ubiquitination	LKTGSFQKAKFNITG HHHCCCCEEEEEEEC	52.08	-
582	Phosphorylation	QKAKFNITGACLNDS CEEEEEEECEECCCC	21.60	22210691
589	Phosphorylation	TGACLNDSDDDSPDL ECEECCCCCCCCCCC	41.69	20873877
593	Phosphorylation	LNDSDDDSPDLDLDG CCCCCCCCCCCCCCC	27.58	24532841
603	Phosphorylation	LDLDGNESPLALLMS CCCCCCCCHHHHHHC	29.25	28102081
610	Phosphorylation	SPLALLMSNGSTKRV CHHHHHHCCCCCHHH	37.70	28102081
613	Phosphorylation	ALLMSNGSTKRVKSL HHHHCCCCCHHHHHC	34.70	20873877
614	Phosphorylation	LLMSNGSTKRVKSLS HHHCCCCCHHHHHCC	25.03	20873877
621	Phosphorylation	TKRVKSLSKSRRTKI CHHHHHCCHHHHHHH	35.36	18669648
651	Phosphorylation	EDEFDLDSDDELQID HCCCCCCCCCCCHHH	55.01	28102081
665	Ubiquitination	DERLGKEKATLIIRP HHHHCCCEEEEEECC	50.59	-
668 (in isoform 2)	Phosphorylation	-	3.51	-
669 (in isoform 2)	Phosphorylation	-	1.87	-
670 (in isoform 2)	Phosphorylation	-	7.49	-
685	Phosphorylation	LPRAKPCSDPNRVRE CCCCCCCCCCCCCCC	65.71	-
686 (in isoform 2)	Phosphorylation	-	51.73	-
704	Phosphorylation	EFDIEEDYTTDEDMV EEEECCCCCCCHHHH	18.15	24532841
705	Phosphorylation	FDIEEDYTTDEDMVE EEECCCCCCCHHHHC	39.84	28348404
706	Phosphorylation	DIEEDYTTDEDMVEG EECCCCCCCHHHHCC	31.03	28348404
722	Phosphorylation	EGKLGNGSGAGGILD CCCCCCCCCHHHHHH	29.48	22617229
732	Ubiquitination	GGILDLLKASRQVGG HHHHHHHHHHHCCCC	52.17	-
742	Phosphorylation	RQVGGPDYAALTEAP HCCCCCCHHHHCCCC	9.26	26074081
746	Phosphorylation	GPDYAALTEAPASPS CCCHHHHCCCCCCHH	25.94	26074081
751	Phosphorylation	ALTEAPASPSTQEAI HHCCCCCCHHHHHHH	20.51	26074081
753	Phosphorylation	TEAPASPSTQEAIQG CCCCCCHHHHHHHHH	39.98	18669648
754	Phosphorylation	EAPASPSTQEAIQGM CCCCCHHHHHHHHHH	33.54	26074081
768 (in isoform 2)	Phosphorylation	-	40.86	-
790	Phosphorylation	WTGGQDRSSGSSSSG ECCCCCCCCCCCCCC	47.54	23927012
790 (in isoform 2)	Phosphorylation	-	47.54	-
791	Phosphorylation	TGGQDRSSGSSSSGL CCCCCCCCCCCCCCC	43.52	23927012
793	Phosphorylation	GQDRSSGSSSSGLGT CCCCCCCCCCCCCCC	29.06	23927012
794	Phosphorylation	QDRSSGSSSSGLGTV CCCCCCCCCCCCCCC	31.86	23927012
795	Phosphorylation	DRSSGSSSSGLGTVS CCCCCCCCCCCCCCC	30.07	23927012
796	Phosphorylation	RSSGSSSSGLGTVSN CCCCCCCCCCCCCCC	39.73	23927012
800	Phosphorylation	SSSSGLGTVSNSPAS CCCCCCCCCCCCCHH	26.29	23927012
802	Phosphorylation	SSGLGTVSNSPASQR CCCCCCCCCCCHHHC	31.28	23927012
804	Phosphorylation	GLGTVSNSPASQRTP CCCCCCCCCHHHCCC	17.84	23401153
807	Phosphorylation	TVSNSPASQRTPGKR CCCCCCHHHCCCCCC	24.47	25159151
810	Phosphorylation	NSPASQRTPGKRPIK CCCHHHCCCCCCCCC	28.84	30576142
818 (in isoform 2)	Phosphorylation	-	23.08	-
821 (in isoform 2)	Phosphorylation	-	9.71	-
824	Phosphorylation	KRPAYWRTESEEEEE CCCCCCCCCCHHHHH	29.71	30266825
826	Phosphorylation	PAYWRTESEEEEENA CCCCCCCCHHHHHHC	50.09	30266825
834	Phosphorylation	EEEEENASLDEQDSL HHHHHHCCCCCCCHH	48.19	30266825
840	Phosphorylation	ASLDEQDSLGACFKD CCCCCCCHHHHHHCC	28.53	27732954
844 (in isoform 2)	Phosphorylation	-	4.06	-
850	Phosphorylation	ACFKDAEYIYPSLES HHHCCHHHHCCCCCC	13.89	23927012
852	Phosphorylation	FKDAEYIYPSLESDD HCCHHHHCCCCCCCC	5.95	23927012
854	Phosphorylation	DAEYIYPSLESDDDD CHHHHCCCCCCCCCC	28.00	22167270
857	Phosphorylation	YIYPSLESDDDDPAL HHCCCCCCCCCCHHH	52.19	19664994
866	Phosphorylation	DDDPALKSRPKKKKN CCCHHHHCCCCCCCC	55.45	23312004
874	Phosphorylation	RPKKKKNSDDAPWSP CCCCCCCCCCCCCCC	45.83	30576142
880	Phosphorylation	NSDDAPWSPKARVTP CCCCCCCCCCCCCCC	18.57	19664994
886	Phosphorylation	WSPKARVTPTLPKQD CCCCCCCCCCCCCCC	12.66	30266825
888	Phosphorylation	PKARVTPTLPKQDRP CCCCCCCCCCCCCCC	46.45	30266825
900	Phosphorylation	DRPVREGTRVASIET CCCCCCCCEEEEHHH	19.74	-
904	Phosphorylation	REGTRVASIETGLAA CCCCEEEEHHHHHHH	20.35	25159151
907	Phosphorylation	TRVASIETGLAAAAA CEEEEHHHHHHHHHH	35.51	29978859
915	Acetylation	GLAAAAAKLAQQELQ HHHHHHHHHHHHHHH	39.36	25953088
915	Ubiquitination	GLAAAAAKLAQQELQ HHHHHHHHHHHHHHH	39.36	-
923	Ubiquitination	LAQQELQKAQKKKYI HHHHHHHHHHHHHHH	66.46	-
947	Phosphorylation	EQPRPQDSNLSLTVP CCCCCCCCCCEEEEE	34.13	23312004
950	Phosphorylation	RPQDSNLSLTVPAPT CCCCCCCEEEEECCC	26.67	26074081
952	Phosphorylation	QDSNLSLTVPAPTVA CCCCCEEEEECCCEE	22.52	29978859
957	Phosphorylation	SLTVPAPTVAATPQL EEEEECCCEECCCCE	25.53	26657352
961	Phosphorylation	PAPTVAATPQLVTSS ECCCEECCCCEECCC	11.22	29116813
966	Phosphorylation	AATPQLVTSSSPLPP ECCCCEECCCCCCCC	31.33	30576142
967	Phosphorylation	ATPQLVTSSSPLPPP CCCCEECCCCCCCCC	22.72	30576142
968	Phosphorylation	TPQLVTSSSPLPPPE CCCEECCCCCCCCCC	26.98	29116813
969	Phosphorylation	PQLVTSSSPLPPPEP CCEECCCCCCCCCCC	30.17	30576142
1005	Phosphorylation	GMAQANRSTTPMAPG CCCCCCCCCCCCCCC	36.12	23684312
1006	Phosphorylation	MAQANRSTTPMAPGV CCCCCCCCCCCCCCE	31.51	21815630
1007	Phosphorylation	AQANRSTTPMAPGVF CCCCCCCCCCCCCEE	16.59	21815630
1021	Phosphorylation	FLTQRRPSVGSQSNQ EEEECCCCCCCCCCC	36.98	23401153
1024	Phosphorylation	QRRPSVGSQSNQAGQ ECCCCCCCCCCCCCC	28.42	28176443
1026	Phosphorylation	RPSVGSQSNQAGQGK CCCCCCCCCCCCCCC	32.38	28176443
1033	Acetylation	SNQAGQGKRPKKGLA CCCCCCCCCCCCCHH	58.60	25953088
1043	Sumoylation	KKGLATAKQRLGRIL CCCHHHHHHHHHHHH	31.43	-
1043	Sumoylation	KKGLATAKQRLGRIL CCCHHHHHHHHHHHH	31.43	-
1043	Ubiquitination	KKGLATAKQRLGRIL CCCHHHHHHHHHHHH	31.43	-
1051	Sumoylation	QRLGRILKIHRNGKL HHHHHHHHCCCCCEE	33.81	-
1051	Sumoylation	QRLGRILKIHRNGKL HHHHHHHHCCCCCEE	33.81	-

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
69	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
120	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
904	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	CDC20	Q12834	PMID:23979597

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
69	S	Phosphorylation	20622854
Phosphorylation at Ser-69 and Ser-120 are required for dissociation from chromatin and accumulation of H4K20Me1 levels during prophase.
120	S	Phosphorylation	20622854
Phosphorylation at Ser-69 and Ser-120 are required for dissociation from chromatin and accumulation of H4K20Me1 levels during prophase.

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 PHF8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WDR5_HUMAN	WDR5	physical	20208542
ASH2L_HUMAN	ASH2L	physical	20208542
H31_HUMAN	HIST1H3A	physical	20208542
HCFC1_HUMAN	HCFC1	physical	20622854
H31_HUMAN	HIST1H3A	physical	20346720
ZN711_HUMAN	ZNF711	physical	20346720
H31_HUMAN	HIST1H3A	physical	20622853
H31_HUMAN	HIST1H3A	physical	20548336
RARA_HUMAN	RARA	physical	20548336
H31_HUMAN	HIST1H3A	physical	20531378
H31_HUMAN	HIST1H3A	physical	20421419
RPB1_HUMAN	POLR2A	physical	20421419
RPB3_HUMAN	POLR2C	physical	20421419
TAF1_HUMAN	TAF1	physical	20421419
A4_HUMAN	APP	physical	21832049
SUH_HUMAN	RBPJ	physical	23022380
NOTC1_HUMAN	NOTCH1	physical	23022380
CDC27_HUMAN	CDC27	physical	23979597
CDC23_HUMAN	CDC23	physical	23979597
APC1_HUMAN	ANAPC1	physical	23979597
APC5_HUMAN	ANAPC5	physical	23979597
CDC26_HUMAN	CDC26	physical	23979597
APC4_HUMAN	ANAPC4	physical	23979597
CDC16_HUMAN	CDC16	physical	23979597
APC7_HUMAN	ANAPC7	physical	23979597
ANC2_HUMAN	ANAPC2	physical	23979597
CDC20_HUMAN	CDC20	physical	23979597
FZR1_HUMAN	FZR1	physical	23979597
CENPB_HUMAN	CENPB	physical	26496610
INCE_HUMAN	INCENP	physical	26496610
IF6_HUMAN	EIF6	physical	26496610
PLEC_HUMAN	PLEC	physical	26496610
XPC_HUMAN	XPC	physical	26496610
TRI26_HUMAN	TRIM26	physical	26496610
H2B2E_HUMAN	HIST2H2BE	physical	26496610
TRIPC_HUMAN	TRIP12	physical	26496610
H2AY_HUMAN	H2AFY	physical	26496610
RT27_HUMAN	MRPS27	physical	26496610
TDIF2_HUMAN	DNTTIP2	physical	26496610
NIP7_HUMAN	NIP7	physical	26496610
NOL8_HUMAN	NOL8	physical	26496610
RIF1_HUMAN	RIF1	physical	26496610
P4K2A_HUMAN	PI4K2A	physical	26496610
RCC2_HUMAN	RCC2	physical	26496610
THA11_HUMAN	THAP11	physical	26496610
RT35_HUMAN	MRPS35	physical	26496610
RT15_HUMAN	MRPS15	physical	26496610
REN3A_HUMAN	UPF3A	physical	26496610
CGAS_HUMAN	MB21D1	physical	26496610
LS14B_HUMAN	LSM14B	physical	26496610
BRAT1_HUMAN	BRAT1	physical	26496610
H3C_HUMAN	H3F3C	physical	26496610
BLM_HUMAN	BLM	physical	27183383
UBP7_HUMAN	USP7	physical	27183383
OGT1_HUMAN	OGT	physical	27183383
HSP7C_HUMAN	HSPA8	physical	27183383

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300263	Mental retardation, X-linked, syndromic, Siderius type (MRXSSD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PHF8_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"PHF8 mediates histone H4 lysine 20 demethylation events involved incell cycle progression."; Liu W., Tanasa B., Tyurina O.V., Zhou T.Y., Gassmann R., Liu W.T.,Ohgi K.A., Benner C., Garcia-Bassets I., Aggarwal A.K., Desai A.,Dorrestein P.C., Glass C.K., Rosenfeld M.G.; Nature 466:508-512(2010). Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN PHD-FINGER, INTERACTION WITHSETD1A; HCFC1 AND E2F1, CHARACTERIZATION OF VARIANT MRXSSD SER-315,PHOSPHORYLATION AT SER-69 AND SER-120, AND MUTAGENESIS OF SER-69;SER-120 AND HIS-283.	20622854 [Abstract]
"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-120; THR-705; THR-706;SER-804; SER-854; SER-857 AND SER-880, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-120; SER-804; SER-857AND SER-880, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-705; THR-706; SER-722;SER-854; SER-857 AND SER-880, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-857, AND MASSSPECTROMETRY.	17081983 [Abstract]
"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-120, AND MASSSPECTROMETRY.	15302935 [Abstract]

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