dbPTM

MD1L1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MD1L1_HUMAN
UniProt AC	Q9Y6D9
Protein Name	Mitotic spindle assembly checkpoint protein MAD1
Gene Name	MAD1L1
Organism	Homo sapiens (Human).
Sequence Length	718
Subcellular Localization	Nucleus. Chromosome, centromere, kinetochore . Nucleus envelope . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole . Detected at the nucleus envelope during in
Protein Description	Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. May recruit MAD2L1 to unattached kinetochores. Has a role in the correct positioning of the septum. Required for anchoring MAD2L1 to the nuclear periphery. Binds to the TERT promoter and represses telomerase expression, possibly by interfering with MYC binding..
Protein Sequence	MEDLGENTMVLSTLRSLNNFISQRVEGGSGLDISTSAPGSLQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITTENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRRQDSIPAFLSSLTLELFSRQTVA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEDLGENT -------CCCCHHHH	9.02	22223895
8	Phosphorylation	MEDLGENTMVLSTLR CCCCHHHHHHHHHHH	12.35	20068231
12	Phosphorylation	GENTMVLSTLRSLNN HHHHHHHHHHHHHHH	17.62	22199227
13	Phosphorylation	ENTMVLSTLRSLNNF HHHHHHHHHHHHHHH	23.25	22199227
16	Phosphorylation	MVLSTLRSLNNFISQ HHHHHHHHHHHHHHH	38.26	25159151
22	Phosphorylation	RSLNNFISQRVEGGS HHHHHHHHHCCCCCC	14.06	24043423
29	Phosphorylation	SQRVEGGSGLDISTS HHCCCCCCCCCCCCC	47.22	18922800
55	Ubiquitination	SMQLEERAEQIRSKS HHHHHHHHHHHHCCH	19.14	29967540
61	Acetylation	RAEQIRSKSHLIQVE HHHHHHCCHHHHHHH	31.85	19608861
61	Sumoylation	RAEQIRSKSHLIQVE HHHHHHCCHHHHHHH	31.85	-
61	Ubiquitination	RAEQIRSKSHLIQVE HHHHHHCCHHHHHHH	31.85	19608861
61	Sumoylation	RAEQIRSKSHLIQVE HHHHHHCCHHHHHHH	31.85	28112733
62	Phosphorylation	AEQIRSKSHLIQVER HHHHHCCHHHHHHHH	25.44	28555341
68	Ubiquitination	KSHLIQVEREKMQME CHHHHHHHHHHHHHH	38.45	23000965
70	Ubiquitination	HLIQVEREKMQMELS HHHHHHHHHHHHHHH	39.10	29967540
71	Ubiquitination	LIQVEREKMQMELSH HHHHHHHHHHHHHHH	40.42	23000965
75	Ubiquitination	EREKMQMELSHKRAR HHHHHHHHHHHHHHH	30.17	29967540
76	Ubiquitination	REKMQMELSHKRARV HHHHHHHHHHHHHHH	5.65	24816145
77	Phosphorylation	EKMQMELSHKRARVE HHHHHHHHHHHHHHH	17.41	25159151
79	Ubiquitination	MQMELSHKRARVELE HHHHHHHHHHHHHHH	44.36	29967540
79	2-Hydroxyisobutyrylation	MQMELSHKRARVELE HHHHHHHHHHHHHHH	44.36	-
81	Ubiquitination	MELSHKRARVELERA HHHHHHHHHHHHHHH	25.36	21890473
90	Phosphorylation	VELERAASTSARNYE HHHHHHHHHCCHHHH	23.16	22067460
91	Phosphorylation	ELERAASTSARNYER HHHHHHHHCCHHHHH	22.98	22461510
92	Phosphorylation	LERAASTSARNYERE HHHHHHHCCHHHHHH	23.80	22067460
94	Ubiquitination	RAASTSARNYEREVD HHHHHCCHHHHHHHH	46.13	24816145
96	Phosphorylation	ASTSARNYEREVDRN HHHCCHHHHHHHHHH	15.71	22461510
115	Ubiquitination	TRIRQLQEREAGAEE HHHHHHHHHHHCHHH	62.17	29967540
123	Ubiquitination	REAGAEEKMQEQLER HHHCHHHHHHHHHHH	37.07	24816145
139	Ubiquitination	RQCQQNLDAASKRLR HHHHHHHHHHHHHHH	47.87	29967540
142	Phosphorylation	QQNLDAASKRLREKE HHHHHHHHHHHHHHH	21.74	24260401
143	Acetylation	QNLDAASKRLREKED HHHHHHHHHHHHHHH	51.21	25953088
143	Ubiquitination	QNLDAASKRLREKED HHHHHHHHHHHHHHH	51.21	29967540
143	2-Hydroxyisobutyrylation	QNLDAASKRLREKED HHHHHHHHHHHHHHH	51.21	-
148	Ubiquitination	ASKRLREKEDSLAQA HHHHHHHHHHHHHHH	61.46	29967540
156	Ubiquitination	EDSLAQAGETINALK HHHHHHHHHHHHHHH	22.09	23000965
159	Ubiquitination	LAQAGETINALKGRI HHHHHHHHHHHHHHH	2.18	23000965
163	Ubiquitination	GETINALKGRISELQ HHHHHHHHHHHHHHH	43.67	29967540
172	Phosphorylation	RISELQWSVMDQEMR HHHHHHHHHHCHHHH	8.46	26074081
182	Ubiquitination	DQEMRVKRLESEKQE CHHHHHHHHHHHHHH	40.61	24816145
185	Phosphorylation	MRVKRLESEKQELQE HHHHHHHHHHHHHHH	55.47	26074081
187	Ubiquitination	VKRLESEKQELQEQL HHHHHHHHHHHHHHH	59.35	24816145
207	Ubiquitination	KCQEANQKIQELQAS HHHHHHHHHHHHHHH	46.28	29967540
214	Phosphorylation	KIQELQASQEARADH HHHHHHHHHHHHHHH	18.65	17525332
215	Ubiquitination	IQELQASQEARADHE HHHHHHHHHHHHHHH	51.92	21890473
221	Ubiquitination	SQEARADHEQQIKDL HHHHHHHHHHHHHHH	33.51	29967540
221	Ubiquitination	SQEARADHEQQIKDL HHHHHHHHHHHHHHH	33.51	-
231	Ubiquitination	QIKDLEQKLSLQEQD HHHHHHHHHCHHHHH	30.57	29967540
233	Phosphorylation	KDLEQKLSLQEQDAA HHHHHHHCHHHHHHH	34.73	28555341
259	Ubiquitination	LPRLERELKQLREES HHHHHHHHHHHHHHH	5.54	24816145
266	Phosphorylation	LKQLREESAHLREMR HHHHHHHHHHHHHHH	19.08	27174698
303	Ubiquitination	MQETLVGLELENERL HHHHHHCHHHHCHHH	5.46	21890473
304	Ubiquitination	QETLVGLELENERLL HHHHHCHHHHCHHHH	48.38	24816145
313	Ubiquitination	ENERLLAKLQSWERL HCHHHHHHHHHHHHH	47.21	29967540
314	Ubiquitination	NERLLAKLQSWERLD CHHHHHHHHHHHHHH	3.97	23000965
323	Phosphorylation	SWERLDQTMGLSIRT HHHHHHHHCCCCCCC	16.93	20068231
324	Sulfoxidation	WERLDQTMGLSIRTP HHHHHHHCCCCCCCH	4.17	21406390
327	Phosphorylation	LDQTMGLSIRTPEDL HHHHCCCCCCCHHHH	12.32	20068231
336	Phosphorylation	RTPEDLSRFVVELQQ CCHHHHHHHHHHHHH	35.36	32142685
351	Ubiquitination	RELALKDKNSAVTSS HHHHHCCCCCHHHHH	51.74	24816145
358	Phosphorylation	KNSAVTSSARGLEKA CCCHHHHHHHHHHHH	16.78	26546556
359	Ubiquitination	NSAVTSSARGLEKAR CCHHHHHHHHHHHHH	14.88	23000965
375	Ubiquitination	QLQEELRQVSGQLLE HHHHHHHHHHHHHHH	46.48	29967540
377	Phosphorylation	QEELRQVSGQLLEER HHHHHHHHHHHHHHH	16.69	-
386	Ubiquitination	QLLEERKKRETHEAL HHHHHHHHHHHHHHH	62.78	23000965
389	Ubiquitination	EERKKRETHEALARR HHHHHHHHHHHHHHH	29.11	23000965
389	Ubiquitination	EERKKRETHEALARR HHHHHHHHHHHHHHH	29.11	-
406	Ubiquitination	KRVLLLTKERDGMRA HHHHHHCCCCCCHHH	51.20	23000965
406	2-Hydroxyisobutyrylation	KRVLLLTKERDGMRA HHHHHHCCCCCCHHH	51.20	-
412	Ubiquitination	TKERDGMRAILGSYD CCCCCCHHHHHCCCC	24.81	24816145
412	Ubiquitination	TKERDGMRAILGSYD CCCCCCHHHHHCCCC	24.81	-
415	Ubiquitination	RDGMRAILGSYDSEL CCCHHHHHCCCCCCC	3.49	24816145
417	Phosphorylation	GMRAILGSYDSELTP CHHHHHCCCCCCCCH	23.48	23403867
418	Phosphorylation	MRAILGSYDSELTPA HHHHHCCCCCCCCHH	22.99	30266825
420	Phosphorylation	AILGSYDSELTPAEY HHHCCCCCCCCHHHC	26.69	30266825
423	Phosphorylation	GSYDSELTPAEYSPQ CCCCCCCCHHHCCHH	19.19	30266825
427	Phosphorylation	SELTPAEYSPQLTRR CCCCHHHCCHHHHHH	27.97	30266825
428	Phosphorylation	ELTPAEYSPQLTRRM CCCHHHCCHHHHHHH	9.55	25159151
431	Ubiquitination	PAEYSPQLTRRMREA HHHCCHHHHHHHHHH	4.58	23000965
432	Phosphorylation	AEYSPQLTRRMREAE HHCCHHHHHHHHHHH	15.81	30266825
434	Ubiquitination	YSPQLTRRMREAEDM CCHHHHHHHHHHHHH	24.23	23000965
447	Phosphorylation	DMVQKVHSHSAEMEA HHHHHHHHCHHHHHH	23.33	23401153
449	Phosphorylation	VQKVHSHSAEMEAQL HHHHHHCHHHHHHHH	29.01	23532336
457	Ubiquitination	AEMEAQLSQALEELG HHHHHHHHHHHHHCC	11.00	24816145
457	Phosphorylation	AEMEAQLSQALEELG HHHHHHHHHHHHHCC	11.00	23532336
459	Ubiquitination	MEAQLSQALEELGGQ HHHHHHHHHHHCCCH	17.36	23000965
462	Ubiquitination	QLSQALEELGGQKQR HHHHHHHHCCCHHHH	54.27	23000965
467	Ubiquitination	LEELGGQKQRADMLE HHHCCCHHHHHHHHH	45.05	29967540
470	Ubiquitination	LGGQKQRADMLEMEL CCCHHHHHHHHHHHH	12.22	23000965
478	Acetylation	DMLEMELKMLKSQSS HHHHHHHHHHHCCCC	28.96	24887495
478	Ubiquitination	DMLEMELKMLKSQSS HHHHHHHHHHHCCCC	28.96	23000965
481	Ubiquitination	EMELKMLKSQSSSAE HHHHHHHHCCCCCHH	42.84	23000965
482	Phosphorylation	MELKMLKSQSSSAEQ HHHHHHHCCCCCHHH	31.19	20068231
484	Phosphorylation	LKMLKSQSSSAEQSF HHHHHCCCCCHHHHH	33.09	20068231
485	Phosphorylation	KMLKSQSSSAEQSFL HHHHCCCCCHHHHHH	26.40	20068231
485	Ubiquitination	KMLKSQSSSAEQSFL HHHHCCCCCHHHHHH	26.40	24816145
486	Phosphorylation	MLKSQSSSAEQSFLF HHHCCCCCHHHHHHH	40.86	20068231
490	Phosphorylation	QSSSAEQSFLFSREE CCCCHHHHHHHCHHH	18.54	19691289
494	Phosphorylation	AEQSFLFSREEADTL HHHHHHHCHHHHHHH	40.71	19691289
500	Phosphorylation	FSREEADTLRLKVEE HCHHHHHHHHHHHHH	22.33	-
504	Ubiquitination	EADTLRLKVEELEGE HHHHHHHHHHHHHCH	40.96	24816145
507	Ubiquitination	TLRLKVEELEGERSR HHHHHHHHHHCHHHH	55.92	29967540
507	Ubiquitination	TLRLKVEELEGERSR HHHHHHHHHHCHHHH	55.92	-
513	Phosphorylation	EELEGERSRLEEEKR HHHHCHHHHHHHHHH	36.59	22496350
522	Ubiquitination	LEEEKRMLEAQLERR HHHHHHHHHHHHHHH	5.99	29967540
522	Ubiquitination	LEEEKRMLEAQLERR HHHHHHHHHHHHHHH	5.99	-
527	Ubiquitination	RMLEAQLERRALQGD HHHHHHHHHHHHCCC	28.21	29967540
533	Ubiquitination	LERRALQGDYDQSRT HHHHHHCCCCCCCCC	35.97	21890473
533	Ubiquitination	LERRALQGDYDQSRT HHHHHHCCCCCCCCC	35.97	21890473
535	Phosphorylation	RRALQGDYDQSRTKV HHHHCCCCCCCCCEE	23.78	27642862
538	Phosphorylation	LQGDYDQSRTKVLHM HCCCCCCCCCEEEEE	38.73	21815630
542	Ubiquitination	YDQSRTKVLHMSLNP CCCCCCEEEEEECCH	4.36	23000965
545	Ubiquitination	SRTKVLHMSLNPTSV CCCEEEEEECCHHHH	4.22	23000965
546	Phosphorylation	RTKVLHMSLNPTSVA CCEEEEEECCHHHHH	17.78	20068231
550	Phosphorylation	LHMSLNPTSVARQRL EEEECCHHHHHHHHH	34.46	20068231
551	Phosphorylation	HMSLNPTSVARQRLR EEECCHHHHHHHHHH	18.29	20068231
562	Phosphorylation	QRLREDHSQLQAECE HHHHHCHHHHHHHHH	44.93	28555341
568	Ubiquitination	HSQLQAECERLRGLL HHHHHHHHHHHHHHH	4.06	24816145
578	Ubiquitination	LRGLLRAMERGGTVP HHHHHHHHHHCCCCC	2.66	21890473
583	Phosphorylation	RAMERGGTVPADLEA HHHHHCCCCCCCHHH	26.58	20068231
594	Phosphorylation	DLEAAAASLPSSKEV CHHHHHHCCCCHHHH	35.77	20068231
597	Phosphorylation	AAAASLPSSKEVAEL HHHHCCCCHHHHHHH	60.37	20068231
598	Phosphorylation	AAASLPSSKEVAELK HHHCCCCHHHHHHHH	30.78	20068231
599	Ubiquitination	AASLPSSKEVAELKK HHCCCCHHHHHHHHH	61.62	29967540
606	Ubiquitination	KEVAELKKQVESAEL HHHHHHHHHHHHHHH	72.67	21890473
610	Phosphorylation	ELKKQVESAELKNQR HHHHHHHHHHHHHHH	28.34	29162720
614	Ubiquitination	QVESAELKNQRLKEV HHHHHHHHHHHHHHH	42.41	29967540
614	Acetylation	QVESAELKNQRLKEV HHHHHHHHHHHHHHH	42.41	25953088
619	Ubiquitination	ELKNQRLKEVFQTKI HHHHHHHHHHHHHHH	54.76	29967540
619	Malonylation	ELKNQRLKEVFQTKI HHHHHHHHHHHHHHH	54.76	26320211
624	Phosphorylation	RLKEVFQTKIQEFRK HHHHHHHHHHHHHHH	20.74	-
625	Ubiquitination	LKEVFQTKIQEFRKA HHHHHHHHHHHHHHH	31.44	22817900
625	Acetylation	LKEVFQTKIQEFRKA HHHHHHHHHHHHHHH	31.44	25953088
634	Phosphorylation	QEFRKACYTLTGYQI HHHHHHHHHHCCCEE	15.05	29162720
649	Phosphorylation	DITTENQYRLTSLYA EEECCCCEEEEEEEC	21.12	18083107
666	Acetylation	PGDCLIFKATSPSGS CCCEEEEEEECCCCC	43.70	26051181
680	Phosphorylation	SKMQLLETEFSHTVG CHHHHEHHHHHCHHH	42.15	18922800
689	Ubiquitination	FSHTVGELIEVHLRR HHCHHHHHHHHHHCC	3.13	21890473
699	Phosphorylation	VHLRRQDSIPAFLSS HHHCCCCCHHHHHHH	23.33	18922800
708	Phosphorylation	PAFLSSLTLELFSRQ HHHHHHHHHHHHHHC	21.82	18922800
713	Phosphorylation	SLTLELFSRQTVA-- HHHHHHHHHCCCC--	35.78	20068231
716	Phosphorylation	LELFSRQTVA----- HHHHHHCCCC-----	19.79	29162720

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
8	T	Phosphorylation	Kinase	TTK	P33981	PSP
22	S	Phosphorylation	Kinase	PLK1	P53350	PSP
22	S	Phosphorylation	Kinase	TTK	P33981	PSP
29	S	Phosphorylation	Kinase	PLK1	P53350	PSP
62	S	Phosphorylation	Kinase	TTK	P33981	PSP
214	S	Phosphorylation	Kinase	ATM	Q13315	PSP
323	T	Phosphorylation	Kinase	TTK	P33981	PSP
598	S	Phosphorylation	Kinase	TTK	P33981	PSP
610	S	Phosphorylation	Kinase	TTK	P33981	PSP
624	T	Phosphorylation	Kinase	TTK	P33981	PSP
680	T	Phosphorylation	Kinase	PLK1	P53350	PSP
716	T	Phosphorylation	Kinase	TTK	P33981	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	BIRC2	Q13490	PMID:18082613

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MD1L1_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 MD1L1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TEX11_HUMAN	TEX11	physical	16189514
NINL_HUMAN	NINL	physical	16189514
F131C_HUMAN	FAM131C	physical	16189514
TRI29_HUMAN	TRIM29	physical	16189514
AMOL2_HUMAN	AMOTL2	physical	16189514
GCP4_HUMAN	TUBGCP4	physical	16189514
MD1L1_HUMAN	MAD1L1	physical	16189514
HDAC1_HUMAN	HDAC1	physical	15388328
HDAC2_HUMAN	HDAC2	physical	15388328
MD2L1_HUMAN	MAD2L1	physical	11707408
MD2L1_HUMAN	MAD2L1	physical	21525009
SIN3A_HUMAN	SIN3A	physical	22783022
MD2L1_HUMAN	MAD2L1	physical	21988832
ZZEF1_HUMAN	ZZEF1	physical	22863883
CDC20_HUMAN	CDC20	physical	24581499
MD2L1_HUMAN	MAD2L1	physical	24581499
MD2L1_HUMAN	MAD2L1	physical	25012665
PCH2_HUMAN	TRIP13	physical	25012665
RNF8_HUMAN	RNF8	physical	25416956
BAG5_HUMAN	BAG5	physical	25416956
SPAT2_HUMAN	SPATA2	physical	25416956
UBP15_HUMAN	USP15	physical	25416956
NEBL_HUMAN	NEBL	physical	25416956
TRI29_HUMAN	TRIM29	physical	25416956
LEGL_HUMAN	LGALSL	physical	25416956
CCHCR_HUMAN	CCHCR1	physical	25416956
ZSC32_HUMAN	ZSCAN32	physical	25416956
CCD94_HUMAN	CCDC94	physical	25416956
TSH3_HUMAN	TSHZ3	physical	25416956
HAUS1_HUMAN	HAUS1	physical	25416956
C19L2_HUMAN	CWF19L2	physical	25416956
NUDC_HUMAN	NUDC	physical	26344197
STK24_HUMAN	STK24	physical	26344197
MD2L1_HUMAN	MAD2L1	physical	18318601

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 MD1L1_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-61, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-428, AND MASSSPECTROMETRY.	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-16 AND SER-428, AND MASSSPECTROMETRY.	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 SER-428, AND MASSSPECTROMETRY.	18691976 [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-428, AND MASSSPECTROMETRY.	18220336 [Abstract]
"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-214, AND MASSSPECTROMETRY.	17525332 [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-428, 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-428, AND MASSSPECTROMETRY.	16964243 [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-428, AND MASSSPECTROMETRY.	15302935 [Abstract]