dbPTM

MORC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MORC2_HUMAN
UniProt AC	Q9Y6X9
Protein Name	MORC family CW-type zinc finger protein 2
Gene Name	MORC2
Organism	Homo sapiens (Human).
Sequence Length	1032
Subcellular Localization	Nucleus . Cytoplasm, cytosol . Mainly located in the nucleus.
Protein Description	Exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY, possibly preventing its dephosphorylation. [PubMed: 24286864 May act as a transcriptional repressor]
Protein Sequence	MAFTNYSSLNRAQLTFEYLHTNSTTHEFLFGALAELVDNARDADATRIDIYAERREDLRGGFMLCFLDDGAGMDPSDAASVIQFGKSAKRTPESTQIGQYGNGLKSGSMRIGKDFILFTKKEDTMTCLFLSRTFHEEEGIDEVIVPLPTWNARTREPVTDNVEKFAIETELIYKYSPFRTEEEVMTQFMKIPGDSGTLVIIFNLKLMDNGEPELDIISNPRDIQMAETSPEGTKPERRSFRAYAAVLYIDPRMRIFIHGHKVQTKRLSCCLYKPRMYKYTSSRFKTRAEQEVKKAEHVARIAEEKAREAESKARTLEVRLGGDLTRDSRVMLRQVQNRAITLRREADVKKRIKEAKQRALKEPKELNFVFGVNIEHRDLDGMFIYNCSRLIKMYEKVGPQLEGGMACGGVVGVVDVPYLVLEPTHNKQDFADAKEYRHLLRAMGEHLAQYWKDIAIAQRGIIKFWDEFGYLSANWNQPPSSELRYKRRRAMEIPTTIQCDLCLKWRTLPFQLSSVEKDYPDTWVCSMNPDPEQDRCEASEQKQKVPLGTFRKDMKTQEEKQKQLTEKIRQQQEKLEALQKTTPIRSQADLKKLPLEVTTRPSTEEPVRRPQRPRSPPLPAVIRNAPSRPPSLPTPRPASQPRKAPVISSTPKLPALAAREEASTSRLLQPPEAPRKPANTLVKTASRPAPLVQQLSPSLLPNSKSPREVPSPKVIKTPVVKKTESPIKLSPATPSRKRSVAVSDEEEVEEEAERRKERCKRGRFVVKEEKKDSNELSDSAGEEDSADLKRAQKDKGLHVEVRVNREWYTGRVTAVEVGKHVVRWKVKFDYVPTDTTPRDRWVEKGSEDVRLMKPPSPEHQSLDTQQEGGEEEVGPVAQQAIAVAEPSTSECLRIEPDTTALSTNHETIDLLVQILRNCLRYFLPPSFPISKKQLSAMNSDELISFPLKEYFKQYEVGLQNLCNSYQSRADSRAKASEESLRTSERKLRETEEKLQKLRTNIVALLQKVQEDIDINTDDELDAYIEDLITKGD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAFTNYSSL ------CCCCCHHHC	31.13	22223895
4	Phosphorylation	----MAFTNYSSLNR ----CCCCCHHHCCH	40.06	20860994
7	Phosphorylation	-MAFTNYSSLNRAQL -CCCCCHHHCCHHHE	30.34	23186163
8	Phosphorylation	MAFTNYSSLNRAQLT CCCCCHHHCCHHHEE	21.21	23186163
43	Ubiquitination	LVDNARDADATRIDI HHHHHCCCCCCEEEE	11.64	21963094
91	Phosphorylation	FGKSAKRTPESTQIG CCCCCCCCCCCCCCC	30.60	25159151
100	Phosphorylation	ESTQIGQYGNGLKSG CCCCCCCCCCCCCCC	13.82	21214269
105	Ubiquitination	GQYGNGLKSGSMRIG CCCCCCCCCCCEEEC	54.92	21906983
107	Phosphorylation	YGNGLKSGSMRIGKD CCCCCCCCCEEECCC	24.71	24719451
110	Ubiquitination	GLKSGSMRIGKDFIL CCCCCCEEECCCEEE	35.88	21963094
113	Ubiquitination	SGSMRIGKDFILFTK CCCEEECCCEEEEEC	47.28	-
169	Phosphorylation	VEKFAIETELIYKYS HHHHEEEEEEEEECC	29.94	24719451
175	Phosphorylation	ETELIYKYSPFRTEE EEEEEEECCCCCCHH	12.47	23663014
176	Phosphorylation	TELIYKYSPFRTEEE EEEEEECCCCCCHHH	17.26	23663014
180	Phosphorylation	YKYSPFRTEEEVMTQ EECCCCCCHHHHHHH	48.40	23663014
228	Phosphorylation	RDIQMAETSPEGTKP HHCCCCCCCCCCCCC	39.79	28985074
231	Ubiquitination	QMAETSPEGTKPERR CCCCCCCCCCCCHHH	78.31	24816145
234	Ubiquitination	ETSPEGTKPERRSFR CCCCCCCCCHHHHHH	56.59	-
268	Phosphorylation	KVQTKRLSCCLYKPR CCCCCCEECEEECHH	13.55	22617229
273	Acetylation	RLSCCLYKPRMYKYT CEECEEECHHHHHHC	17.13	26051181
279	Phosphorylation	YKPRMYKYTSSRFKT ECHHHHHHCHHHHHH	8.38	20860994
281	Phosphorylation	PRMYKYTSSRFKTRA HHHHHHCHHHHHHHH	19.20	20860994
293	Ubiquitination	TRAEQEVKKAEHVAR HHHHHHHHHHHHHHH	45.58	24816145
298	Ubiquitination	EVKKAEHVARIAEEK HHHHHHHHHHHHHHH	2.63	24816145
372	Ubiquitination	ELNFVFGVNIEHRDL HHCEEEEECCCCCCC	4.41	29967540
434	Ubiquitination	KQDFADAKEYRHLLR CCCCCCHHHHHHHHH	56.69	29967540
507	Phosphorylation	DLCLKWRTLPFQLSS CCCEEECCCCEEHHH	37.35	21406692
512	Ubiquitination	WRTLPFQLSSVEKDY ECCCCEEHHHCCCCC	4.16	29967540
513	Phosphorylation	RTLPFQLSSVEKDYP CCCCEEHHHCCCCCC	22.89	21406692
514	Phosphorylation	TLPFQLSSVEKDYPD CCCEEHHHCCCCCCC	42.77	21406692
518	Ubiquitination	QLSSVEKDYPDTWVC EHHHCCCCCCCCEEE	46.84	33845483
540	Phosphorylation	QDRCEASEQKQKVPL HHHHHHHHHHHCCCC	69.69	24719451
553	Phosphorylation	PLGTFRKDMKTQEEK CCCHHCHHCCCHHHH	39.28	24719451
569	Phosphorylation	KQLTEKIRQQQEKLE HHHHHHHHHHHHHHH	39.05	24719451
572	Phosphorylation	TEKIRQQQEKLEALQ HHHHHHHHHHHHHHH	41.26	24719451
574	Ubiquitination	KIRQQQEKLEALQKT HHHHHHHHHHHHHHC	47.49	29967540
580	Ubiquitination	EKLEALQKTTPIRSQ HHHHHHHHCCCCCCH	56.04	33845483
581	Phosphorylation	KLEALQKTTPIRSQA HHHHHHHCCCCCCHH	25.50	28985074
582	Phosphorylation	LEALQKTTPIRSQAD HHHHHHCCCCCCHHH	24.61	25159151
588	Phosphorylation	TTPIRSQADLKKLPL CCCCCCHHHHHCCCC	25.91	24719451
590	Ubiquitination	PIRSQADLKKLPLEV CCCCHHHHHCCCCEE	6.21	24816145
598	Phosphorylation	KKLPLEVTTRPSTEE HCCCCEEECCCCCCC	14.01	23186163
599	Phosphorylation	KLPLEVTTRPSTEEP CCCCEEECCCCCCCC	45.84	23186163
602	Phosphorylation	LEVTTRPSTEEPVRR CEEECCCCCCCCCCC	45.20	22817900
603	Phosphorylation	EVTTRPSTEEPVRRP EEECCCCCCCCCCCC	47.23	22817900
615	Phosphorylation	RRPQRPRSPPLPAVI CCCCCCCCCCCCCHH	33.29	19664994
621	Ubiquitination	RSPPLPAVIRNAPSR CCCCCCCHHCCCCCC	3.89	24816145
624	Phosphorylation	PLPAVIRNAPSRPPS CCCCHHCCCCCCCCC	45.11	24719451
627	Phosphorylation	AVIRNAPSRPPSLPT CHHCCCCCCCCCCCC	55.82	23312004
631	O-linked_Glycosylation	NAPSRPPSLPTPRPA CCCCCCCCCCCCCCC	50.06	30379171
631	Phosphorylation	NAPSRPPSLPTPRPA CCCCCCCCCCCCCCC	50.06	23312004
634	Phosphorylation	SRPPSLPTPRPASQP CCCCCCCCCCCCCCC	36.90	18669648
636	Phosphorylation	PPSLPTPRPASQPRK CCCCCCCCCCCCCCC	41.73	24719451
639	Phosphorylation	LPTPRPASQPRKAPV CCCCCCCCCCCCCCC	43.32	28555341
641	Phosphorylation	TPRPASQPRKAPVIS CCCCCCCCCCCCCCC	36.93	24719451
643	Phosphorylation	RPASQPRKAPVISST CCCCCCCCCCCCCCC	64.82	24719451
648	Phosphorylation	PRKAPVISSTPKLPA CCCCCCCCCCCCCCH	28.52	29214152
649	Phosphorylation	RKAPVISSTPKLPAL CCCCCCCCCCCCCHH	37.29	25278378
650	Phosphorylation	KAPVISSTPKLPALA CCCCCCCCCCCCHHH	20.04	21815630
652	Sumoylation	PVISSTPKLPALAAR CCCCCCCCCCHHHHC	68.16	28112733
652	Ubiquitination	PVISSTPKLPALAAR CCCCCCCCCCHHHHC	68.16	24816145
655	Phosphorylation	SSTPKLPALAAREEA CCCCCCCHHHHCHHH	21.92	24719451
657	Ubiquitination	TPKLPALAAREEAST CCCCCHHHHCHHHCC	13.43	24816145
663	Phosphorylation	LAAREEASTSRLLQP HHHCHHHCCCHHCCC	30.14	17081983
664	Phosphorylation	AAREEASTSRLLQPP HHCHHHCCCHHCCCC	25.55	28555341
668	Phosphorylation	EASTSRLLQPPEAPR HHCCCHHCCCCCCCC	7.54	24719451
671	Phosphorylation	TSRLLQPPEAPRKPA CCHHCCCCCCCCCCC	37.10	24719451
677	Phosphorylation	PPEAPRKPANTLVKT CCCCCCCCCCCCEEC	31.83	24719451
681	Phosphorylation	PRKPANTLVKTASRP CCCCCCCCEECCCCC	3.59	24719451
683	Methylation	KPANTLVKTASRPAP CCCCCCEECCCCCCC	41.30	116254073
683	Ubiquitination	KPANTLVKTASRPAP CCCCCCEECCCCCCC	41.30	24816145
684	Phosphorylation	PANTLVKTASRPAPL CCCCCEECCCCCCCH	23.53	24732914
686	Phosphorylation	NTLVKTASRPAPLVQ CCCEECCCCCCCHHH	43.99	24732914
688	Ubiquitination	LVKTASRPAPLVQQL CEECCCCCCCHHHHC	35.42	24816145
696	Phosphorylation	APLVQQLSPSLLPNS CCHHHHCCHHHCCCC	14.22	25159151
698	Phosphorylation	LVQQLSPSLLPNSKS HHHHCCHHHCCCCCC	38.88	23927012
703	Phosphorylation	SPSLLPNSKSPREVP CHHHCCCCCCCCCCC	32.35	23927012
704	Sumoylation	PSLLPNSKSPREVPS HHHCCCCCCCCCCCC	71.73	28112733
705	Acetylation	SLLPNSKSPREVPSP HHCCCCCCCCCCCCC	29.07	19608861
705	Phosphorylation	SLLPNSKSPREVPSP HHCCCCCCCCCCCCC	29.07	23927012
711	Phosphorylation	KSPREVPSPKVIKTP CCCCCCCCCCEECCC	42.39	30576142
713	Acetylation	PREVPSPKVIKTPVV CCCCCCCCEECCCCC	62.01	19830023
715	Phosphorylation	EVPSPKVIKTPVVKK CCCCCCEECCCCCCC	5.26	24719451
716	Sumoylation	VPSPKVIKTPVVKKT CCCCCEECCCCCCCC	50.17	28112733
717	O-linked_Glycosylation	PSPKVIKTPVVKKTE CCCCEECCCCCCCCC	15.36	30379171
717	Phosphorylation	PSPKVIKTPVVKKTE CCCCEECCCCCCCCC	15.36	23911959
723	Phosphorylation	KTPVVKKTESPIKLS CCCCCCCCCCCCCCC	35.66	22167270
725	Phosphorylation	PVVKKTESPIKLSPA CCCCCCCCCCCCCCC	36.84	22167270
730	Phosphorylation	TESPIKLSPATPSRK CCCCCCCCCCCCCCC	13.90	22167270
733	Phosphorylation	PIKLSPATPSRKRSV CCCCCCCCCCCCCCE	25.77	22167270
735	Phosphorylation	KLSPATPSRKRSVAV CCCCCCCCCCCCEEC	46.19	30266825
739	Phosphorylation	ATPSRKRSVAVSDEE CCCCCCCCEECCCHH	19.91	29255136
743	Phosphorylation	RKRSVAVSDEEEVEE CCCCEECCCHHHHHH	29.57	19664994
757	Ubiquitination	EEAERRKERCKRGRF HHHHHHHHHHHHCCE	62.59	33845483
763	Ubiquitination	KERCKRGRFVVKEEK HHHHHHCCEEECCCC	25.81	22817900
765	Ubiquitination	RCKRGRFVVKEEKKD HHHHCCEEECCCCCC	6.07	21890473
765	Ubiquitination	RCKRGRFVVKEEKKD HHHHCCEEECCCCCC	6.07	21890473
767	Sumoylation	KRGRFVVKEEKKDSN HHCCEEECCCCCCCC	55.65	-
767	Acetylation	KRGRFVVKEEKKDSN HHCCEEECCCCCCCC	55.65	19608861
767	Sumoylation	KRGRFVVKEEKKDSN HHCCEEECCCCCCCC	55.65	28112733
773	Phosphorylation	VKEEKKDSNELSDSA ECCCCCCCCCCCCCC	40.87	23401153
774	Phosphorylation	KEEKKDSNELSDSAG CCCCCCCCCCCCCCC	65.45	27251275
777	Phosphorylation	KKDSNELSDSAGEED CCCCCCCCCCCCCCC	24.28	29255136
779	Phosphorylation	DSNELSDSAGEEDSA CCCCCCCCCCCCCHH	34.49	29255136
785	Phosphorylation	DSAGEEDSADLKRAQ CCCCCCCHHHHHHHH	27.28	22167270
794	Phosphorylation	DLKRAQKDKGLHVEV HHHHHHHHCCCEEEE	37.87	27251275
813	Phosphorylation	EWYTGRVTAVEVGKH EEECCCEEEEEECCE	24.51	-
819	Acetylation	VTAVEVGKHVVRWKV EEEEEECCEEEEEEE	38.10	30590443
819	Sumoylation	VTAVEVGKHVVRWKV EEEEEECCEEEEEEE	38.10	28112733
819	Ubiquitination	VTAVEVGKHVVRWKV EEEEEECCEEEEEEE	38.10	33845483
825	Ubiquitination	GKHVVRWKVKFDYVP CCEEEEEEEEEECCC	25.61	22817900
827	Ubiquitination	HVVRWKVKFDYVPTD EEEEEEEEEECCCCC	28.88	21906983
830	Ubiquitination	RWKVKFDYVPTDTTP EEEEEEECCCCCCCC	16.09	22817900
832	Ubiquitination	KVKFDYVPTDTTPRD EEEEECCCCCCCCCH	20.51	21890473
833	Phosphorylation	VKFDYVPTDTTPRDR EEEECCCCCCCCCHH	35.61	29396449
835	Phosphorylation	FDYVPTDTTPRDRWV EECCCCCCCCCHHCC	40.97	28387310
836	Phosphorylation	DYVPTDTTPRDRWVE ECCCCCCCCCHHCCC	21.09	25159151
856	Phosphorylation	VRLMKPPSPEHQSLD CEECCCCCHHHCCCC	51.99	22167270
861	Phosphorylation	PPSPEHQSLDTQQEG CCCHHHCCCCCCCCC	30.07	22167270
864	Phosphorylation	PEHQSLDTQQEGGEE HHHCCCCCCCCCCCC	37.13	22167270
869	Ubiquitination	LDTQQEGGEEEVGPV CCCCCCCCCCCCHHH	38.09	23000965
870	Ubiquitination	DTQQEGGEEEVGPVA CCCCCCCCCCCHHHH	62.94	21890473
870	Ubiquitination	DTQQEGGEEEVGPVA CCCCCCCCCCCHHHH	62.94	21890473
887	Phosphorylation	AIAVAEPSTSECLRI HHEEECCCCHHCEEC	35.75	23927012
888	Phosphorylation	IAVAEPSTSECLRIE HEEECCCCHHCEECC	38.98	23927012
889	Phosphorylation	AVAEPSTSECLRIEP EEECCCCHHCEECCC	30.56	23927012
921	Phosphorylation	ILRNCLRYFLPPSFP HHHHHHHHHCCCCCC	9.12	26657352
926	Phosphorylation	LRYFLPPSFPISKKQ HHHHCCCCCCCCHHH	41.54	26657352
930	Phosphorylation	LPPSFPISKKQLSAM CCCCCCCCHHHHHCC	33.76	26657352
931	Ubiquitination	PPSFPISKKQLSAMN CCCCCCCHHHHHCCC	45.30	23000965
932	Sumoylation	PSFPISKKQLSAMNS CCCCCCHHHHHCCCH	50.08	28112733
932	Ubiquitination	PSFPISKKQLSAMNS CCCCCCHHHHHCCCH	50.08	23000965
935	Phosphorylation	PISKKQLSAMNSDEL CCCHHHHHCCCHHHC	23.99	20068231
936	Ubiquitination	ISKKQLSAMNSDELI CCHHHHHCCCHHHCE	15.12	23000965
937	Ubiquitination	SKKQLSAMNSDELIS CHHHHHCCCHHHCEE	4.42	21890473
939	Phosphorylation	KQLSAMNSDELISFP HHHHCCCHHHCEECH	21.27	20068231
944	Phosphorylation	MNSDELISFPLKEYF CCHHHCEECHHHHHH	33.17	20068231
950	Phosphorylation	ISFPLKEYFKQYEVG EECHHHHHHHHHHHH	17.94	20068231
967	Phosphorylation	NLCNSYQSRADSRAK HHHHHHHHHHHHHHH	22.62	-
971	Phosphorylation	SYQSRADSRAKASEE HHHHHHHHHHHHCHH	32.90	-
974	Ubiquitination	SRADSRAKASEESLR HHHHHHHHHCHHHHH	51.87	-
983	Phosphorylation	SEESLRTSERKLRET CHHHHHHHHHHHHHH	29.04	22210691
993	Acetylation	KLRETEEKLQKLRTN HHHHHHHHHHHHHHH	50.41	26051181
993	Ubiquitination	KLRETEEKLQKLRTN HHHHHHHHHHHHHHH	50.41	24816145
998	Ubiquitination	EEKLQKLRTNIVALL HHHHHHHHHHHHHHH	32.53	24816145
1016	Phosphorylation	QEDIDINTDDELDAY HHCCCCCCCHHHHHH	45.20	28387310

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
582	T	Phosphorylation	Kinase	PKACA	P17612	PSP
739	S	Phosphorylation	Kinase	PAK1	Q13153	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
739	S	Phosphorylation		19690332
Phosphorylated by PAK1 at Ser-739 upon DNA damage.

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 MORC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
HDAC4_HUMAN	HDAC4	physical	20110259

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 MORC2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-767, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-739 AND SER-743, ANDMASS 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-615 AND SER-743, ANDMASS 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 SER-615; SER-696; SER-705;THR-717; SER-725; SER-730; THR-733; SER-739; SER-743; SER-777 ANDSER-779, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-615; SER-725; SER-730AND SER-735, AND MASS SPECTROMETRY.	18220336 [Abstract]
"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-615, AND MASSSPECTROMETRY.	16565220 [Abstract]
"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-615, AND MASSSPECTROMETRY.	16964243 [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-615; SER-777 ANDSER-779, AND MASS SPECTROMETRY.	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-615 AND SER-743, ANDMASS SPECTROMETRY.	15302935 [Abstract]

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