dbPTM

MLH1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MLH1_HUMAN
UniProt AC	P40692
Protein Name	DNA mismatch repair protein Mlh1
Gene Name	MLH1
Organism	Homo sapiens (Human).
Sequence Length	756
Subcellular Localization	Nucleus .
Protein Description	Heterodimerizes with PMS2 to form MutL alpha, a component of the post-replicative DNA mismatch repair system (MMR). DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH6) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Heterodimerizes with MLH3 to form MutL gamma which plays a role in meiosis..
Protein Sequence	MSFVAGVIRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTSIQVIVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQSFEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLKAPPKPCAGNQGTQITVEDLFYNIATRRKALKNPSEEYGKILEVVGRYSVHNAGISFSVKKQGETVADVRTLPNASTVDNIRSIFGNAVSRELIEIGCEDKTLAFKMNGYISNANYSVKKCIFLLFINHRLVESTSLRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEMVKSTTSLTSSSTSGSSDKVYAHQMVRTDSREQKLDAFLQPLSKPLSSQPQAIVTEDKTDISSGRARQQDEEMLELPAPAEVAAKNQSLEGDTTKGTSEMSEKRGPTSSNPRKRHREDSDVEMVEDDSRKEMTAACTPRRRIINLTSVLSLQEEINEQGHEVLREMLHNHSFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEPAPLFDLAMLALDSPESGWTEEDGPKEGLAEYIVEFLKKKAEMLADYFSLEIDEEGNLIGLPLLIDNYVPPLEGLPIFILRLATEVNWDEEKECFESLSKECAMFYSIRKQYISEESTLSGQQSEVPGSIPNSWKWTVEHIVYKALRSHILPPKHFTEDGNILQLANLPDLYKVFERC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSFVAGVIR ------CCCHHHHHH	28.55	22223895
2	Phosphorylation	------MSFVAGVIR ------CCCHHHHHH	28.55	20860994
33	Ubiquitination	QRPANAIKEMIENCL CCHHHHHHHHHHHHH	38.53	-
35	Sulfoxidation	PANAIKEMIENCLDA HHHHHHHHHHHHHCC	3.85	21406390
57	Ubiquitination	IVKEGGLKLIQIQDN EEEECCEEEEEEEEC	46.98	-
70	Ubiquitination	DNGTGIRKEDLDIVC ECCCCCCHHHHHEEE	54.37	-
84	Ubiquitination	CERFTTSKLQSFEDL EEECCCCCCCCHHHH	48.75	-
87	Phosphorylation	FTTSKLQSFEDLASI CCCCCCCCHHHHHCC	40.83	28348404
123	Ubiquitination	TTKTADGKCAYRASY EEECCCCEEEEEEEC	19.08	-
134	Ubiquitination	RASYSDGKLKAPPKP EEECCCCCCCCCCCC	52.37	-
136	Ubiquitination	SYSDGKLKAPPKPCA ECCCCCCCCCCCCCC	63.43	-
140	Ubiquitination	GKLKAPPKPCAGNQG CCCCCCCCCCCCCCC	52.23	-
164	Ubiquitination	YNIATRRKALKNPSE HHHHHHHHHHCCHHH	55.57	-
167	Ubiquitination	ATRRKALKNPSEEYG HHHHHHHCCHHHHHH	72.22	-
175	Ubiquitination	NPSEEYGKILEVVGR CHHHHHHHHHHHHCC	43.12	-
183	Phosphorylation	ILEVVGRYSVHNAGI HHHHHCCCEEECCCE	14.76	20068231
184	Phosphorylation	LEVVGRYSVHNAGIS HHHHCCCEEECCCEE	18.62	20068231
191	Phosphorylation	SVHNAGISFSVKKQG EEECCCEEEEEEECC	15.56	20068231
193	Phosphorylation	HNAGISFSVKKQGET ECCCEEEEEEECCCE	26.66	20068231
195	Acetylation	AGISFSVKKQGETVA CCEEEEEEECCCEEE	37.87	25953088
196	Ubiquitination	GISFSVKKQGETVAD CEEEEEEECCCEEEE	62.47	-
200	Phosphorylation	SVKKQGETVADVRTL EEEECCCEEEEEECC	28.02	23403867
212	Phosphorylation	RTLPNASTVDNIRSI ECCCCCCCHHHHHHH	29.48	21857030
236	Acetylation	IEIGCEDKTLAFKMN HHHCCCCCCEEEECC	24.12	26051181
236	Ubiquitination	IEIGCEDKTLAFKMN HHHCCCCCCEEEECC	24.12	-
269	Phosphorylation	INHRLVESTSLRKAI HCCHHHCCHHHHHHH	18.80	20068231
270	Phosphorylation	NHRLVESTSLRKAIE CCHHHCCHHHHHHHH	20.48	20068231
271	Phosphorylation	HRLVESTSLRKAIET CHHHCCHHHHHHHHH	35.14	20068231
288	Phosphorylation	AAYLPKNTHPFLYLS HHHCCCCCCCEEEEE	36.73	19835603
293	Phosphorylation	KNTHPFLYLSLEISP CCCCCEEEEEEEECC	8.47	19835603
295	Phosphorylation	THPFLYLSLEISPQN CCCEEEEEEEECCCC	15.48	19835603
333	Ubiquitination	VQQHIESKLLGSNSS HHHHHHHHHCCCCCC	34.63	-
337	Phosphorylation	IESKLLGSNSSRMYF HHHHHCCCCCCCCEE	33.24	22210691
362	Phosphorylation	PSGEMVKSTTSLTSS CCCCEEEECCCCCCC	26.05	30576142
363	Phosphorylation	SGEMVKSTTSLTSSS CCCEEEECCCCCCCC	18.06	25137130
363	O-linked_Glycosylation	SGEMVKSTTSLTSSS CCCEEEECCCCCCCC	18.06	30379171
364	Phosphorylation	GEMVKSTTSLTSSST CCEEEECCCCCCCCC	28.91	28450419
365	Phosphorylation	EMVKSTTSLTSSSTS CEEEECCCCCCCCCC	29.73	28450419
367	Phosphorylation	VKSTTSLTSSSTSGS EEECCCCCCCCCCCC	26.74	30576142
368	Phosphorylation	KSTTSLTSSSTSGSS EECCCCCCCCCCCCC	27.82	28450419
369	Phosphorylation	STTSLTSSSTSGSSD ECCCCCCCCCCCCCC	32.19	28450419
370	Phosphorylation	TTSLTSSSTSGSSDK CCCCCCCCCCCCCCC	26.76	28450419
371	Phosphorylation	TSLTSSSTSGSSDKV CCCCCCCCCCCCCCE	38.77	28450419
372	Phosphorylation	SLTSSSTSGSSDKVY CCCCCCCCCCCCCEE	38.33	28450419
374	Phosphorylation	TSSSTSGSSDKVYAH CCCCCCCCCCCEEEE	34.82	25627689
375	Phosphorylation	SSSTSGSSDKVYAHQ CCCCCCCCCCEEEEE	45.00	28450419
377	Ubiquitination	STSGSSDKVYAHQMV CCCCCCCCEEEEEEE	38.81	-
377	Acetylation	STSGSSDKVYAHQMV CCCCCCCCEEEEEEE	38.81	25953088
379	Phosphorylation	SGSSDKVYAHQMVRT CCCCCCEEEEEEECC	12.24	27642862
386	Phosphorylation	YAHQMVRTDSREQKL EEEEEECCCCHHHHH	27.24	29514088
388	Phosphorylation	HQMVRTDSREQKLDA EEEECCCCHHHHHHH	36.78	29514088
392	Sumoylation	RTDSREQKLDAFLQP CCCCHHHHHHHHHHC	43.51	-
392	Sumoylation	RTDSREQKLDAFLQP CCCCHHHHHHHHHHC	43.51	-
392	Ubiquitination	RTDSREQKLDAFLQP CCCCHHHHHHHHHHC	43.51	-
401	Phosphorylation	DAFLQPLSKPLSSQP HHHHHCCCCCCCCCC	38.62	24719451
402	Ubiquitination	AFLQPLSKPLSSQPQ HHHHCCCCCCCCCCC	58.63	-
402	Acetylation	AFLQPLSKPLSSQPQ HHHHCCCCCCCCCCC	58.63	23236377
405	Phosphorylation	QPLSKPLSSQPQAIV HCCCCCCCCCCCEEE	35.14	29523821
406	Phosphorylation	PLSKPLSSQPQAIVT CCCCCCCCCCCEEEE	54.27	30576142
416	Sumoylation	QAIVTEDKTDISSGR CEEEECCCCCCCCCC	41.69	-
416	Ubiquitination	QAIVTEDKTDISSGR CEEEECCCCCCCCCC	41.69	-
416	Sumoylation	QAIVTEDKTDISSGR CEEEECCCCCCCCCC	41.69	-
443	Ubiquitination	APAEVAAKNQSLEGD CCHHHHHHCCCCCCC	45.87	-
443	Acetylation	APAEVAAKNQSLEGD CCHHHHHHCCCCCCC	45.87	23236377
446	Phosphorylation	EVAAKNQSLEGDTTK HHHHHCCCCCCCCCC	37.47	29396449
453	Ubiquitination	SLEGDTTKGTSEMSE CCCCCCCCCCHHHHH	63.38	-
455	Phosphorylation	EGDTTKGTSEMSEKR CCCCCCCCHHHHHHC	24.06	23403867
458	Sulfoxidation	TTKGTSEMSEKRGPT CCCCCHHHHHHCCCC	6.67	21406390
459	Phosphorylation	TKGTSEMSEKRGPTS CCCCHHHHHHCCCCC	35.59	27251275
461	Acetylation	GTSEMSEKRGPTSSN CCHHHHHHCCCCCCC	56.18	23749302
467	Phosphorylation	EKRGPTSSNPRKRHR HHCCCCCCCCCCCCC	54.02	26546556
477	Phosphorylation	RKRHREDSDVEMVED CCCCCCCCCCEECCC	38.51	9559627
486	Phosphorylation	VEMVEDDSRKEMTAA CEECCCCCHHHHHHH	58.54	25850435
488	Ubiquitination	MVEDDSRKEMTAACT ECCCCCHHHHHHHCC	56.65	-
491	Phosphorylation	DDSRKEMTAACTPRR CCCHHHHHHHCCCCH	16.52	29496963
495	Phosphorylation	KEMTAACTPRRRIIN HHHHHHCCCCHHHHH	18.33	21815630
508	Phosphorylation	INLTSVLSLQEEINE HHHHHHHHHHHHHHH	26.33	-
685	Phosphorylation	KECAMFYSIRKQYIS HHHHHHHHHHHHHCC	12.49	24719451
688	Ubiquitination	AMFYSIRKQYISEES HHHHHHHHHHCCCCC	45.87	-
690	Phosphorylation	FYSIRKQYISEESTL HHHHHHHHCCCCCCC	14.95	24043423
692	Phosphorylation	SIRKQYISEESTLSG HHHHHHCCCCCCCCC	30.31	24043423
695	Phosphorylation	KQYISEESTLSGQQS HHHCCCCCCCCCCCC	30.51	24043423
696	Phosphorylation	QYISEESTLSGQQSE HHCCCCCCCCCCCCC	28.37	24043423
698	Phosphorylation	ISEESTLSGQQSEVP CCCCCCCCCCCCCCC	34.34	24043423
702	Phosphorylation	STLSGQQSEVPGSIP CCCCCCCCCCCCCCC	32.45	24043423
707	Phosphorylation	QQSEVPGSIPNSWKW CCCCCCCCCCCCCCE	28.89	24043423
711	Phosphorylation	VPGSIPNSWKWTVEH CCCCCCCCCCEEHHH	25.36	24043423
732	Ubiquitination	RSHILPPKHFTEDGN HHCCCCCCCCCCCCC	49.78	-
751	Ubiquitination	ANLPDLYKVFERC-- HCCHHHHHHHHCC--	47.98	-

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
406	S	Phosphorylation	Kinase	ATM	Q13315	PSP
406	S	Phosphorylation	Kinase	ATR	Q13535	GPS
477	S	Phosphorylation	Kinase	CK2A1	P68400	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MLH1_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 MLH1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRI29_HUMAN	TRIM29	physical	16189514
ZC11A_HUMAN	ZC3H11A	physical	16189514
FRMD6_HUMAN	FRMD6	physical	16189514
RNF37_HUMAN	UBOX5	physical	16189514
BLM_HUMAN	BLM	physical	10783165
ATM_HUMAN	ATM	physical	10783165
RFC1_HUMAN	RFC1	physical	10783165
PMS2_HUMAN	PMS2	physical	12584560
MYC_HUMAN	MYC	physical	12584560
PMS2_HUMAN	PMS2	physical	11292842
MSH4_HUMAN	MSH4	physical	10928988
BLM_HUMAN	BLM	physical	11691925
MBD4_HUMAN	MBD4	physical	10097147
PMS2_HUMAN	PMS2	physical	10037723
EXO1_HUMAN	EXO1	physical	19015241
NTH2_YEAST	NTG2	physical	19015241
EXO1_YEAST	EXO1	physical	19015241
SGS1_YEAST	SGS1	physical	19015241
BLM_HUMAN	BLM	physical	19015241
PMS2_HUMAN	PMS2	physical	19015241
PMS2_HUMAN	PMS2	physical	17148452
PMS1_HUMAN	PMS1	physical	17148452
FANCJ_HUMAN	BRIP1	physical	17148452
MSH3_HUMAN	MSH3	physical	17148452
BRCA1_HUMAN	BRCA1	physical	17148452
SMC1A_HUMAN	SMC1A	physical	17148452
XRN1_HUMAN	XRN1	physical	17148452
PSD3_HUMAN	PSD3	physical	17148452
UBC_HUMAN	UBC	physical	17148452
UBP2L_HUMAN	UBAP2L	physical	17148452
YLPM1_HUMAN	YLPM1	physical	17148452
EXO1_HUMAN	EXO1	physical	17148452
PRKDC_HUMAN	PRKDC	physical	17148452
IMA1_HUMAN	KPNA2	physical	17148452
IMB1_HUMAN	KPNB1	physical	17148452
RUVB1_HUMAN	RUVBL1	physical	17148452
RUVB2_HUMAN	RUVBL2	physical	17148452
FAN1_HUMAN	FAN1	physical	17148452
2AAA_HUMAN	PPP2R1A	physical	17148452
2ABA_HUMAN	PPP2R2A	physical	17148452
2ABB_HUMAN	PPP2R2B	physical	17148452
PP2BB_HUMAN	PPP3CB	physical	17148452
PP2BC_HUMAN	PPP3CC	physical	17148452
2ABD_HUMAN	PPP2R2D	physical	17148452
AIFM1_HUMAN	AIFM1	physical	17148452
P3C2A_HUMAN	PIK3C2A	physical	17148452
AMOT_HUMAN	AMOT	physical	17148452
ATD3A_HUMAN	ATAD3A	physical	17148452
DOCK7_HUMAN	DOCK7	physical	17148452
PYGB_HUMAN	PYGB	physical	17148452
ATPA_HUMAN	ATP5A1	physical	17148452
ATD3B_HUMAN	ATAD3B	physical	17148452
WDR61_HUMAN	WDR61	physical	17148452
PMS1_HUMAN	PMS1	physical	20004149
PMS2_HUMAN	PMS2	physical	20978114
FANCJ_HUMAN	BRIP1	physical	20978114
FAN1_HUMAN	FAN1	physical	20603073
EXO1_HUMAN	EXO1	physical	21533173
PMS2_HUMAN	PMS2	physical	17581638
FANCJ_HUMAN	BRIP1	physical	17581638
EXO1_HUMAN	EXO1	physical	22222486
MSH2_HUMAN	MSH2	physical	10748159
MSH6_HUMAN	MSH6	physical	10748159
PMS2_HUMAN	PMS2	physical	10748159
PMS1_HUMAN	PMS1	physical	10748159
POLH_HUMAN	POLH	physical	19703417
PMS2_HUMAN	PMS2	physical	12799449
MSH2_HUMAN	MSH2	physical	12799449
MSH6_HUMAN	MSH6	physical	12799449
PMS2_HUMAN	PMS2	physical	22939629
PMS2_HUMAN	PMS2	physical	20706999
DDX47_HUMAN	DDX47	physical	20706999
TRI23_HUMAN	TRIM23	physical	20706999
PAR12_HUMAN	PARP12	physical	20706999
RD23B_HUMAN	RAD23B	physical	20706999
RPGFL_HUMAN	RAPGEFL1	physical	20706999
AIFM1_HUMAN	AIFM1	physical	20706999
ANXA6_HUMAN	ANXA6	physical	20706999
ARAF_HUMAN	ARAF	physical	20706999
CAN5_HUMAN	CAPN5	physical	20706999
CATB_HUMAN	CTSB	physical	20706999
GBRAP_HUMAN	GABARAP	physical	20706999
MP2K6_HUMAN	MAP2K6	physical	20706999
NDRG1_HUMAN	NDRG1	physical	20706999
STAP2_HUMAN	STAP2	physical	20706999
THIOM_HUMAN	TXN2	physical	20706999
ZER1_HUMAN	ZER1	physical	20706999
FLNB_HUMAN	FLNB	physical	20706999
ACTG_HUMAN	ACTG1	physical	20706999
ACTH_HUMAN	ACTG2	physical	20706999
ANXA2_HUMAN	ANXA2	physical	20706999
CKAP4_HUMAN	CKAP4	physical	20706999
DESM_HUMAN	DES	physical	20706999
MYL6_HUMAN	MYL6	physical	20706999
PARVA_HUMAN	PARVA	physical	20706999
SPTN1_HUMAN	SPTAN1	physical	20706999
TYB4_HUMAN	TMSB4X	physical	20706999
FBX32_HUMAN	FBXO32	physical	20706999
SQSTM_HUMAN	SQSTM1	physical	20706999
EIF2A_HUMAN	EIF2A	physical	20706999
EF1G_HUMAN	EEF1G	physical	20706999
EF2_HUMAN	EEF2	physical	20706999
5NT3B_HUMAN	NT5C3B	physical	20706999
APT_HUMAN	APRT	physical	20706999
LEG4_HUMAN	LGALS4	physical	20706999
MUC2_HUMAN	MUC2	physical	20706999
FCGBP_HUMAN	FCGBP	physical	20706999
ABHGA_HUMAN	ABHD16A	physical	20706999
MRP3_HUMAN	ABCC3	physical	20706999
AGR2_HUMAN	AGR2	physical	20706999
ALDOA_HUMAN	ALDOA	physical	20706999
ASSY_HUMAN	ASS1	physical	20706999
ELP6_HUMAN	ELP6	physical	20706999
CB39L_HUMAN	CAB39L	physical	20706999
KCRB_HUMAN	CKB	physical	20706999
EXOC3_HUMAN	EXOC3	physical	20706999
GSTP1_HUMAN	GSTP1	physical	20706999
ACER3_HUMAN	ACER3	physical	20706999
PTGDS_HUMAN	PTGDS	physical	20706999
S61A1_HUMAN	SEC61A1	physical	20706999
SBP1_HUMAN	SELENBP1	physical	20706999
PEDF_HUMAN	SERPINF1	physical	20706999
VAMP8_HUMAN	VAMP8	physical	20706999
ZC11A_HUMAN	ZC3H11A	physical	19060904
PMS2_HUMAN	PMS2	physical	15225546
PCNA_HUMAN	PCNA	physical	15225546
PMS2_HUMAN	PMS2	physical	11429708
EXO1_HUMAN	EXO1	physical	11429708
THIO_HUMAN	TXN	physical	21988832
ORC4_HUMAN	ORC4	physical	21988832
MLH3_HUMAN	MLH3	physical	24443562
MSH3_HUMAN	MSH3	physical	25416956
MYOG_HUMAN	MYOG	physical	25416956
PSA1_HUMAN	PSMA1	physical	25416956
CX057_HUMAN	CXorf57	physical	25416956
SPERT_HUMAN	SPERT	physical	25416956
API5_HUMAN	API5	physical	26344197
SPTN1_HUMAN	SPTAN1	physical	26344197
SPTN2_HUMAN	SPTBN2	physical	26344197
UBP5_HUMAN	USP5	physical	26344197
ZN224_HUMAN	ZNF224	physical	26344197
PMS2_HUMAN	PMS2	physical	18206974
CX057_HUMAN	CXorf57	physical	21516116
CAZA2_HUMAN	CAPZA2	physical	26496610
LYST_HUMAN	LYST	physical	26496610
SRC8_HUMAN	CTTN	physical	26496610
VIGLN_HUMAN	HDLBP	physical	26496610
PMS1_HUMAN	PMS1	physical	26496610
TXTP_HUMAN	SLC25A1	physical	26496610
PSMD6_HUMAN	PSMD6	physical	26496610
FKBP8_HUMAN	FKBP8	physical	26496610
INO80_HUMAN	INO80	physical	26496610
PLXA3_HUMAN	PLXNA3	physical	26496610
ELMO2_HUMAN	ELMO2	physical	26496610
NANP_HUMAN	NANP	physical	26496610
AES_HUMAN	AES	physical	27229929
CCD33_HUMAN	CCDC33	physical	27229929
CDA7L_HUMAN	CDCA7L	physical	27229929
CEP76_HUMAN	CEP76	physical	27229929
CX057_HUMAN	CXorf57	physical	27229929
CE126_HUMAN	KIAA1377	physical	27229929
LY96_HUMAN	LY96	physical	27229929
MAGA8_HUMAN	MAGEA8	physical	27229929
MLH3_HUMAN	MLH3	physical	27229929
RNF37_HUMAN	UBOX5	physical	27229929
ZBED1_HUMAN	ZBED1	physical	27229929
ZC11A_HUMAN	ZC3H11A	physical	27229929
MCM9_HUMAN	MCM9	physical	26300262

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609310	Hereditary non-polyposis colorectal cancer 2 (HNPCC2)
276300	Mismatch repair cancer syndrome (MMRCS)
158320	Muir-Torre syndrome (MRTES)
	Note=Defects in MLH1 may contribute to lobular carcinoma in situ (LCIS), a non-invasive neoplastic disease of the breast.
608089
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MLH1_HUMAN

Related Literatures of Post-Translational Modification

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-477, AND MASSSPECTROMETRY.	19690332 [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-477, AND MASSSPECTROMETRY.	18669648 [Abstract]