dbPTM

MED13_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MED13_HUMAN
UniProt AC	Q9UHV7
Protein Name	Mediator of RNA polymerase II transcription subunit 13
Gene Name	MED13
Organism	Homo sapiens (Human).
Sequence Length	2174
Subcellular Localization	Nucleus.
Protein Description	Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors..
Protein Sequence	MSASFVPNGASLEDCHCNLFCLADLTGIKWKKYVWQGPTSAPILFPVTEEDPILSSFSRCLKADVLGVWRRDQRPGRRELWIFWWGEDPSFADLIHHDLSEEEDGVWENGLSYECRTLLFKAVHNLLERCLMNRNFVRIGKWFVKPYEKDEKPINKSEHLSCSFTFFLHGDSNVCTSVEINQHQPVYLLSEEHITLAQQSNSPFQVILCPFGLNGTLTGQAFKMSDSATKKLIGEWKQFYPISCCLKEMSEEKQEDMDWEDDSLAAVEVLVAGVRMIYPACFVLVPQSDIPTPSPVGSTHCSSSCLGVHQVPASTRDPAMSSVTLTPPTSPEEVQTVDPQSVQKWVKFSSVSDGFNSDSTSHHGGKIPRKLANHVVDRVWQECNMNRAQNKRKYSASSGGLCEEATAAKVASWDFVEATQRTNCSCLRHKNLKSRNAGQQGQAPSLGQQQQILPKHKTNEKQEKSEKPQKRPLTPFHHRVSVSDDVGMDADSASQRLVISAPDSQVRFSNIRTNDVAKTPQMHGTEMANSPQPPPLSPHPCDVVDEGVTKTPSTPQSQHFYQMPTPDPLVPSKPMEDRIDSLSQSFPPQYQEAVEPTVYVGTAVNLEEDEANIAWKYYKFPKKKDVEFLPPQLPSDKFKDDPVGPFGQESVTSVTELMVQCKKPLKVSDELVQQYQIKNQCLSAIASDAEQEPKIDPYAFVEGDEEFLFPDKKDRQNSEREAGKKHKVEDGTSSVTVLSHEEDAMSLFSPSIKQDAPRPTSHARPPSTSLIYDSDLAVSYTDLDNLFNSDEDELTPGSKKSANGSDDKASCKESKTGNLDPLSCISTADLHKMYPTPPSLEQHIMGFSPMNMNNKEYGSMDTTPGGTVLEGNSSSIGAQFKIEVDEGFCSPKPSEIKDFSYVYKPENCQILVGCSMFAPLKTLPSQYLPPIKLPEECIYRQSWTVGKLELLSSGPSMPFIKEGDGSNMDQEYGTAYTPQTHTSFGMPPSSAPPSNSGAGILPSPSTPRFPTPRTPRTPRTPRGAGGPASAQGSVKYENSDLYSPASTPSTCRPLNSVEPATVPSIPEAHSLYVNLILSESVMNLFKDCNFDSCCICVCNMNIKGADVGVYIPDPTQEAQYRCTCGFSAVMNRKFGNNSGLFLEDELDIIGRNTDCGKEAEKRFEALRATSAEHVNGGLKESEKLSDDLILLLQDQCTNLFSPFGAADQDPFPKSGVISNWVRVEERDCCNDCYLALEHGRQFMDNMSGGKVDEALVKSSCLHPWSKRNDVSMQCSQDILRMLLSLQPVLQDAIQKKRTVRPWGVQGPLTWQQFHKMAGRGSYGTDESPEPLPIPTFLLGYDYDYLVLSPFALPYWERLMLEPYGSQRDIAYVVLCPENEALLNGAKSFFRDLTAIYESCRLGQHRPVSRLLTDGIMRVGSTASKKLSEKLVAEWFSQAADGNNEAFSKLKLYAQVCRYDLGPYLASLPLDSSLLSQPNLVAPTSQSLITPPQMTNTGNANTPSATLASAASSTMTVTSGVAISTSVATANSTLTTASTSSSSSSNLNSGVSSNKLPSFPPFGSMNSNAAGSMSTQANTVQSGQLGGQQTSALQTAGISGESSSLPTQPHPDVSESTMDRDKVGIPTDGDSHAVTYPPAIVVYIIDPFTYENTDESTNSSSVWTLGLLRCFLEMVQTLPPHIKSTVSVQIIPCQYLLQPVKHEDREIYPQHLKSLAFSAFTQCRRPLPTSTNVKTLTGFGPGLAMETALRSPDRPECIRLYAPPFILAPVKDKQTELGETFGEAGQKYNVLFVGYCLSHDQRWILASCTDLYGELLETCIINIDVPNRARRKKSSARKFGLQKLWEWCLGLVQMSSLPWRVVIGRLGRIGHGELKDWSCLLSRRNLQSLSKRLKDMCRMCGISAADSPSILSACLVAMEPQGSFVIMPDSVSTGSVFGRSTTLNMQTSQLNTPQDTSCTHILVFPTSASVQVASATYTTENLDLAFNPNNDGADGMGIFDLLDTGDDLDPDIINILPASPTGSPVHSPGSHYPHGGDAGKGQSTDRLLSTEPHEEVPNILQQPLALGYFVSTAKAGPLPDWFWSACPQAQYQCPLFLKASLHLHVPSVQSDELLHSKHSHPLDSNQTSDVLRFVLEQYNALSWLTCDPATQDRRSCLPIHFVVLNQLYNFIMNML

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
56	Phosphorylation	EEDPILSSFSRCLKA CCCCHHHHHHHHHHC	24.64	24945436
70	Methylation	ADVLGVWRRDQRPGR CHHHEEEECCCCCCC	29.86	54560319
225	O-linked_Glycosylation	TGQAFKMSDSATKKL CCCEEECCHHHHHHH	29.07	30379171
227	O-linked_Glycosylation	QAFKMSDSATKKLIG CEEECCHHHHHHHHH	30.45	30379171
229	O-linked_Glycosylation	FKMSDSATKKLIGEW EECCHHHHHHHHHHH	32.44	30379171
237	Acetylation	KKLIGEWKQFYPISC HHHHHHHHHHHHHHH	26.65	26051181
240	Phosphorylation	IGEWKQFYPISCCLK HHHHHHHHHHHHHHH	9.36	-
243	Phosphorylation	WKQFYPISCCLKEMS HHHHHHHHHHHHHCC	8.35	-
321	Phosphorylation	STRDPAMSSVTLTPP CCCCCCCCEEEECCC	24.62	30108239
322	Phosphorylation	TRDPAMSSVTLTPPT CCCCCCCEEEECCCC	13.16	30108239
324	Phosphorylation	DPAMSSVTLTPPTSP CCCCCEEEECCCCCH	27.19	30266825
326	Phosphorylation	AMSSVTLTPPTSPEE CCCEEEECCCCCHHH	20.18	30266825
329	Phosphorylation	SVTLTPPTSPEEVQT EEEECCCCCHHHHCC	59.11	30266825
330	Phosphorylation	VTLTPPTSPEEVQTV EEECCCCCHHHHCCC	35.77	30266825
336	Phosphorylation	TSPEEVQTVDPQSVQ CCHHHHCCCCHHHHH	31.86	30266825
341	Phosphorylation	VQTVDPQSVQKWVKF HCCCCHHHHHHHEEC	31.72	30108239
349	Phosphorylation	VQKWVKFSSVSDGFN HHHHEECCCCCCCCC	24.90	-
366	Acetylation	STSHHGGKIPRKLAN CCCCCCCCCCHHHHH	54.88	25953088
366	Ubiquitination	STSHHGGKIPRKLAN CCCCCCCCCCHHHHH	54.88	-
394	Phosphorylation	RAQNKRKYSASSGGL HHHHCCCCCCCCCCC	17.32	30266825
395	Phosphorylation	AQNKRKYSASSGGLC HHHCCCCCCCCCCCC	25.39	23401153
397	Phosphorylation	NKRKYSASSGGLCEE HCCCCCCCCCCCCHH	24.47	30266825
398	Phosphorylation	KRKYSASSGGLCEEA CCCCCCCCCCCCHHH	36.27	30266825
406	Phosphorylation	GGLCEEATAAKVASW CCCCHHHHHHHHHCC	30.35	23927012
445	Phosphorylation	GQQGQAPSLGQQQQI CCCCCCCCHHHHHHH	48.42	28555341
474	Phosphorylation	KPQKRPLTPFHHRVS CCCCCCCCCCCCCCC	26.96	30266825
481	Phosphorylation	TPFHHRVSVSDDVGM CCCCCCCCCCCCCCC	18.83	23911959
483	Phosphorylation	FHHRVSVSDDVGMDA CCCCCCCCCCCCCCC	22.16	25850435
494	Phosphorylation	GMDADSASQRLVISA CCCCCCHHCEEEEEC	21.56	27251275
500	Phosphorylation	ASQRLVISAPDSQVR HHCEEEEECCCCCEE	26.69	25159151
504	Phosphorylation	LVISAPDSQVRFSNI EEEECCCCCEEECCC	29.52	25159151
513	Phosphorylation	VRFSNIRTNDVAKTP EEECCCCCCCCCCCC	31.79	28985074
519	Phosphorylation	RTNDVAKTPQMHGTE CCCCCCCCCCCCCCC	14.71	23927012
525	Phosphorylation	KTPQMHGTEMANSPQ CCCCCCCCCCCCCCC	14.12	23927012
530	Phosphorylation	HGTEMANSPQPPPLS CCCCCCCCCCCCCCC	18.51	23401153
537	Phosphorylation	SPQPPPLSPHPCDVV CCCCCCCCCCCCCCC	27.26	23401153
549	Phosphorylation	DVVDEGVTKTPSTPQ CCCCCCCCCCCCCCC	39.80	23663014
551	Phosphorylation	VDEGVTKTPSTPQSQ CCCCCCCCCCCCCHH	17.07	25159151
553	Phosphorylation	EGVTKTPSTPQSQHF CCCCCCCCCCCHHCC	58.93	20068231
554	Phosphorylation	GVTKTPSTPQSQHFY CCCCCCCCCCHHCCC	26.93	25849741
557	Phosphorylation	KTPSTPQSQHFYQMP CCCCCCCHHCCCCCC	27.16	20068231
561	Phosphorylation	TPQSQHFYQMPTPDP CCCHHCCCCCCCCCC	11.19	20068231
565	Phosphorylation	QHFYQMPTPDPLVPS HCCCCCCCCCCCCCC	34.67	20068231
572	Phosphorylation	TPDPLVPSKPMEDRI CCCCCCCCCCHHHHH	41.74	20068231
635	Phosphorylation	FLPPQLPSDKFKDDP CCCCCCCCCCCCCCC	63.12	-
687	Phosphorylation	QCLSAIASDAEQEPK HHHHHHHCCCHHCCC	31.10	25159151
698	Phosphorylation	QEPKIDPYAFVEGDE HCCCCCCCCEECCCC	14.66	27642862
712	Acetylation	EEFLFPDKKDRQNSE CCCCCCCHHHCCCCH	57.73	23236377
733	Phosphorylation	HKVEDGTSSVTVLSH EECCCCCCCEEEECC	28.48	29759185
734	Phosphorylation	KVEDGTSSVTVLSHE ECCCCCCCEEEECCH	22.96	29759185
736	Phosphorylation	EDGTSSVTVLSHEED CCCCCCEEEECCHHH	20.06	29759185
739	Phosphorylation	TSSVTVLSHEEDAMS CCCEEEECCHHHHHH	25.23	29759185
749	Phosphorylation	EDAMSLFSPSIKQDA HHHHHHHCCCCCCCC	24.03	17192257
815	Ubiquitination	KASCKESKTGNLDPL CHHHHHCCCCCCCCC	62.64	-
816	Phosphorylation	ASCKESKTGNLDPLS HHHHHCCCCCCCCCC	40.35	23186163
823	Phosphorylation	TGNLDPLSCISTADL CCCCCCCCCEEHHHH	18.13	23186163
826	Phosphorylation	LDPLSCISTADLHKM CCCCCCEEHHHHHHH	23.13	25159151
827	Phosphorylation	DPLSCISTADLHKMY CCCCCEEHHHHHHHC	12.32	23186163
834	Phosphorylation	TADLHKMYPTPPSLE HHHHHHHCCCCCCHH	14.57	20068231
836	Phosphorylation	DLHKMYPTPPSLEQH HHHHHCCCCCCHHHH	30.28	20068231
839	Phosphorylation	KMYPTPPSLEQHIMG HHCCCCCCHHHHHCC	45.82	22496350
848	Phosphorylation	EQHIMGFSPMNMNNK HHHHCCCCCCCCCCC	19.94	20068231
857	Phosphorylation	MNMNNKEYGSMDTTP CCCCCCCCCCCCCCC	18.99	25627689
859	Phosphorylation	MNNKEYGSMDTTPGG CCCCCCCCCCCCCCC	16.75	25627689
862	Phosphorylation	KEYGSMDTTPGGTVL CCCCCCCCCCCCEEE	26.67	25159151
863	Phosphorylation	EYGSMDTTPGGTVLE CCCCCCCCCCCEEEE	18.70	17192257
867	Phosphorylation	MDTTPGGTVLEGNSS CCCCCCCEEEECCCC	28.03	28348404
890	Phosphorylation	EVDEGFCSPKPSEIK EECCCCCCCCHHHCC	33.43	29255136
892	Ubiquitination	DEGFCSPKPSEIKDF CCCCCCCCHHHCCCC	44.90	-
894	Phosphorylation	GFCSPKPSEIKDFSY CCCCCCHHHCCCCCE	59.07	30266825
901	Phosphorylation	SEIKDFSYVYKPENC HHCCCCCEEECCCCC	14.06	22210691
1005	Phosphorylation	AGILPSPSTPRFPTP CCCCCCCCCCCCCCC	56.21	21406692
1006	Phosphorylation	GILPSPSTPRFPTPR CCCCCCCCCCCCCCC	23.13	21406692
1011	Phosphorylation	PSTPRFPTPRTPRTP CCCCCCCCCCCCCCC	23.77	-
1014	Phosphorylation	PRFPTPRTPRTPRTP CCCCCCCCCCCCCCC	20.51	-
1017	Phosphorylation	PTPRTPRTPRTPRGA CCCCCCCCCCCCCCC	20.51	28985074
1020	Phosphorylation	RTPRTPRTPRGAGGP CCCCCCCCCCCCCCC	20.67	20068231
1022	Methylation	PRTPRTPRGAGGPAS CCCCCCCCCCCCCCC	47.16	115389153
1029	Phosphorylation	RGAGGPASAQGSVKY CCCCCCCCCCCCEEE	25.02	30266825
1033	Phosphorylation	GPASAQGSVKYENSD CCCCCCCCEEECCCC	11.89	30266825
1042	Phosphorylation	KYENSDLYSPASTPS EECCCCCCCCCCCCC	20.00	27732954
1043	Phosphorylation	YENSDLYSPASTPST ECCCCCCCCCCCCCC	22.68	27732954
1046	Phosphorylation	SDLYSPASTPSTCRP CCCCCCCCCCCCCCC	44.21	27732954
1047	Phosphorylation	DLYSPASTPSTCRPL CCCCCCCCCCCCCCC	24.30	27732954
1049	Phosphorylation	YSPASTPSTCRPLNS CCCCCCCCCCCCCCC	39.98	27732954
1050	Phosphorylation	SPASTPSTCRPLNSV CCCCCCCCCCCCCCC	17.46	27732954
1133	Sumoylation	FSAVMNRKFGNNSGL HHHHHCCCCCCCCCC	53.25	-
1138	Phosphorylation	NRKFGNNSGLFLEDE CCCCCCCCCCCEECH	40.65	-
1157	Sumoylation	GRNTDCGKEAEKRFE CCCCCCCHHHHHHHH	61.14	-
1247	Phosphorylation	RQFMDNMSGGKVDEA HHHHHHCCCCCCCHH	51.12	-
1363	Phosphorylation	ERLMLEPYGSQRDIA HHHCCCCCCCCCCEE	21.75	29083192
1365	Phosphorylation	LMLEPYGSQRDIAYV HCCCCCCCCCCEEEE	19.05	29083192
1387	Phosphorylation	ALLNGAKSFFRDLTA HHHHHHHHHHHHHHH	29.14	24719451
1393	Phosphorylation	KSFFRDLTAIYESCR HHHHHHHHHHHHHHC	18.46	20736484
1396	Phosphorylation	FRDLTAIYESCRLGQ HHHHHHHHHHHCCCC	10.18	20736484
1421	Phosphorylation	GIMRVGSTASKKLSE CCHHCCCHHHHHHHH	29.08	-
1423	Phosphorylation	MRVGSTASKKLSEKL HHCCCHHHHHHHHHH	30.34	-
1448	Ubiquitination	GNNEAFSKLKLYAQV CCCHHHHHHHHHHHH	43.09	21906983
1452	Phosphorylation	AFSKLKLYAQVCRYD HHHHHHHHHHHHCCC	8.06	20068231
1634	Phosphorylation	DGDSHAVTYPPAIVV CCCCCCCCCCCEEEE	30.97	-
1683	Phosphorylation	TLPPHIKSTVSVQII HCCCCCCCCEEEEEE	33.18	-
1684	Phosphorylation	LPPHIKSTVSVQIIP CCCCCCCCEEEEEEE	16.29	-
1686	Phosphorylation	PHIKSTVSVQIIPCQ CCCCCCEEEEEEECC	14.37	-
1694	Phosphorylation	VQIIPCQYLLQPVKH EEEEECCHHHCCCCC	18.98	-
1728	Phosphorylation	QCRRPLPTSTNVKTL CCCCCCCCCCCCEEC	56.73	20068231
1729	Phosphorylation	CRRPLPTSTNVKTLT CCCCCCCCCCCEECC	18.95	22210691
1730	Phosphorylation	RRPLPTSTNVKTLTG CCCCCCCCCCEECCC	46.65	20068231
1736	Phosphorylation	STNVKTLTGFGPGLA CCCCEECCCCCCCHH	35.38	22210691
1746	Phosphorylation	GPGLAMETALRSPDR CCCHHHHHHHHCCCC	20.22	25159151
1750	Phosphorylation	AMETALRSPDRPECI HHHHHHHCCCCCHHH	31.81	25159151
1772	Ubiquitination	ILAPVKDKQTELGET EEEECCCCCCHHHHH	54.09	-
1786	Ubiquitination	TFGEAGQKYNVLFVG HHHHHHHHEEEEEEE	37.56	-
1833	Phosphorylation	NRARRKKSSARKFGL CHHHHHHHHHHHHHH	32.06	24260401
1834	Phosphorylation	RARRKKSSARKFGLQ HHHHHHHHHHHHHHH	40.76	24260401
1837	Acetylation	RKKSSARKFGLQKLW HHHHHHHHHHHHHHH	43.42	30593069
1842	Acetylation	ARKFGLQKLWEWCLG HHHHHHHHHHHHHHH	61.69	30593075
1887	Phosphorylation	LSRRNLQSLSKRLKD HCHHHHHHHHHHHHH	37.46	21815630
1889	Phosphorylation	RRNLQSLSKRLKDMC HHHHHHHHHHHHHHH	22.45	23401153
1890	Ubiquitination	RNLQSLSKRLKDMCR HHHHHHHHHHHHHHH	68.02	-
2018	Phosphorylation	IINILPASPTGSPVH HHEECCCCCCCCCCC	22.51	26074081
2020	Phosphorylation	NILPASPTGSPVHSP EECCCCCCCCCCCCC	48.04	26074081
2022	Phosphorylation	LPASPTGSPVHSPGS CCCCCCCCCCCCCCC	26.65	26074081
2026	Phosphorylation	PTGSPVHSPGSHYPH CCCCCCCCCCCCCCC	31.06	26074081
2029	Phosphorylation	SPVHSPGSHYPHGGD CCCCCCCCCCCCCCC	24.19	26074081
2031	Phosphorylation	VHSPGSHYPHGGDAG CCCCCCCCCCCCCCC	9.91	26074081
2042	Phosphorylation	GDAGKGQSTDRLLST CCCCCCCCCCCCCCC	40.73	28450419
2043	Phosphorylation	DAGKGQSTDRLLSTE CCCCCCCCCCCCCCC	19.76	25627689
2048	Phosphorylation	QSTDRLLSTEPHEEV CCCCCCCCCCCCCCC	35.00	27273156
2049	Phosphorylation	STDRLLSTEPHEEVP CCCCCCCCCCCCCCC	54.21	28450419
2067	Phosphorylation	QQPLALGYFVSTAKA HCCHHHCHHHHCCCC	11.14	23186163
2070	Phosphorylation	LALGYFVSTAKAGPL HHHCHHHHCCCCCCC	16.85	23186163
2071	Phosphorylation	ALGYFVSTAKAGPLP HHCHHHHCCCCCCCC	27.20	23186163

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
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW7	Q969H0	PMID:23322298

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MED13_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 MED13_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MED29_HUMAN	MED29	physical	22939629
MED24_HUMAN	MED24	physical	22939629
MED4_HUMAN	MED4	physical	22939629
MED14_HUMAN	MED14	physical	22939629
MED16_HUMAN	MED16	physical	22939629
MED21_HUMAN	MED21	physical	22939629
MED1_HUMAN	MED1	physical	23563140
MED26_HUMAN	MED26	physical	23563140
MED19_HUMAN	MED19	physical	23563140
MED7_HUMAN	MED7	physical	23563140
U5S1_HUMAN	EFTUD2	physical	26344197
MED1_HUMAN	MED1	physical	26344197
MED10_HUMAN	MED10	physical	26344197
MED14_HUMAN	MED14	physical	26344197
MED16_HUMAN	MED16	physical	26344197
MED18_HUMAN	MED18	physical	26344197
MED19_HUMAN	MED19	physical	26344197
MED27_HUMAN	MED27	physical	26344197
MED6_HUMAN	MED6	physical	26344197
MED8_HUMAN	MED8	physical	26344197
RBP2_HUMAN	RANBP2	physical	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 MED13_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-326; THR-329; TYR-394;SER-395; SER-481; SER-530; SER-537; SER-890; SER-1029 AND SER-2048,AND MASS SPECTROMETRY.	19369195 [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 SER-504; THR-519 ANDSER-537, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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 THR-326; THR-336; SER-481;SER-500; THR-863; SER-890 AND SER-1029, AND MASS SPECTROMETRY.	18691976 [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-890, 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-1029, AND MASSSPECTROMETRY.	15302935 [Abstract]