dbPTM

PRPF3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PRPF3_HUMAN
UniProt AC	O43395
Protein Name	U4/U6 small nuclear ribonucleoprotein Prp3
Gene Name	PRPF3
Organism	Homo sapiens (Human).
Sequence Length	683
Subcellular Localization	Nucleus speckle. Colocalizes with spliceosomal snRNPs.
Protein Description	Participates in pre-mRNA splicing. Part of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome..
Protein Sequence	MALSKRELDELKPWIEKTVKRVLGFSEPTVVTAALNCVGKGMDKKKAADHLKPFLDDSTLRFVDKLFEAVEEGRSSRHSKSSSDRSRKRELKEVFGDDSEISKESSGVKKRRIPRFEEVEEEPEVIPGPPSESPGMLTKLQIKQMMEAATRQIEERKKQLSFISPPTPQPKTPSSSQPERLPIGNTIQPSQAATFMNDAIEKARKAAELQARIQAQLALKPGLIGNANMVGLANLHAMGIAPPKVELKDQTKPTPLILDEQGRTVDATGKEIELTHRMPTLKANIRAVKREQFKQQLKEKPSEDMESNTFFDPRVSIAPSQRQRRTFKFHDKGKFEKIAQRLRTKAQLEKLQAEISQAARKTGIHTSTRLALIAPKKELKEGDIPEIEWWDSYIIPNGFDLTEENPKREDYFGITNLVEHPAQLNPPVDNDTPVTLGVYLTKKEQKKLRRQTRREAQKELQEKVRLGLMPPPEPKVRISNLMRVLGTEAVQDPTKVEAHVRAQMAKRQKAHEEANAARKLTAEQRKVKKIKKLKEDISQGVHISVYRVRNLSNPAKKFKIEANAGQLYLTGVVVLHKDVNVVVVEGGPKAQKKFKRLMLHRIKWDEQTSNTKGDDDEESDEEAVKKTNKCVLVWEGTAKDRSFGEMKFKQCPTENMAREHFKKHGAEHYWDLALSESVLESTD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Acetylation	KRELDELKPWIEKTV HHHHHHHHHHHHHHH	35.94	26051181
17	Ubiquitination	ELKPWIEKTVKRVLG HHHHHHHHHHHHHHC	49.86	29967540
17	Acetylation	ELKPWIEKTVKRVLG HHHHHHHHHHHHHHC	49.86	25953088
26	Phosphorylation	VKRVLGFSEPTVVTA HHHHHCCCCCHHHHH	40.65	24719451
27	Ubiquitination	KRVLGFSEPTVVTAA HHHHCCCCCHHHHHH	42.61	24816145
36	Ubiquitination	TVVTAALNCVGKGMD HHHHHHHHHHCCCCC	17.44	24816145
37	S-nitrosocysteine	VVTAALNCVGKGMDK HHHHHHHHHCCCCCH	4.43	-
37	Glutathionylation	VVTAALNCVGKGMDK HHHHHHHHHCCCCCH	4.43	22555962
37	S-nitrosylation	VVTAALNCVGKGMDK HHHHHHHHHCCCCCH	4.43	19483679
40	Ubiquitination	AALNCVGKGMDKKKA HHHHHHCCCCCHHHH	30.57	32015554
52	Ubiquitination	KKAADHLKPFLDDST HHHHHHHHHCCCHHH	30.24	22817900
52	Ubiquitination	KKAADHLKPFLDDST HHHHHHHHHCCCHHH	30.24	21890473
52	Acetylation	KKAADHLKPFLDDST HHHHHHHHHCCCHHH	30.24	26051181
52 (in isoform 1)	Ubiquitination	-	30.24	21890473
58	Phosphorylation	LKPFLDDSTLRFVDK HHHCCCHHHHHHHHH	29.07	27134283
59	Phosphorylation	KPFLDDSTLRFVDKL HHCCCHHHHHHHHHH	29.02	28555341
61	Methylation	FLDDSTLRFVDKLFE CCCHHHHHHHHHHHH	29.63	115488983
65	Ubiquitination	STLRFVDKLFEAVEE HHHHHHHHHHHHHHH	50.18	29967540
65	Acetylation	STLRFVDKLFEAVEE HHHHHHHHHHHHHHH	50.18	25953088
75	Phosphorylation	EAVEEGRSSRHSKSS HHHHHHCCCCCCCCC	42.45	28555341
76	Phosphorylation	AVEEGRSSRHSKSSS HHHHHCCCCCCCCCC	32.43	28555341
102	Phosphorylation	FGDDSEISKESSGVK HCCCCHHHHCCCCCC	26.73	20068231
103	Ubiquitination	GDDSEISKESSGVKK CCCCHHHHCCCCCCC	68.24	24816145
103	Acetylation	GDDSEISKESSGVKK CCCCHHHHCCCCCCC	68.24	26051181
105	Phosphorylation	DSEISKESSGVKKRR CCHHHHCCCCCCCCC	35.81	20068231
106	Phosphorylation	SEISKESSGVKKRRI CHHHHCCCCCCCCCC	49.01	18669648
117	Acetylation	KRRIPRFEEVEEEPE CCCCCCHHHCCCCCC	63.51	-
126	Ubiquitination	VEEEPEVIPGPPSES CCCCCCCCCCCCCCC	2.88	24816145
131	Phosphorylation	EVIPGPPSESPGMLT CCCCCCCCCCCCHHC	54.57	25159151
133	Phosphorylation	IPGPPSESPGMLTKL CCCCCCCCCCHHCHH	30.96	25159151
135	Ubiquitination	GPPSESPGMLTKLQI CCCCCCCCHHCHHHH	32.77	24816145
138	Phosphorylation	SESPGMLTKLQIKQM CCCCCHHCHHHHHHH	22.33	21712546
139	Sumoylation	ESPGMLTKLQIKQMM CCCCHHCHHHHHHHH	34.14	28112733
143	Ubiquitination	MLTKLQIKQMMEAAT HHCHHHHHHHHHHHH	21.12	29967540
150	Ubiquitination	KQMMEAATRQIEERK HHHHHHHHHHHHHHH	30.10	24816145
158	Ubiquitination	RQIEERKKQLSFISP HHHHHHHHHHCCCCC	63.79	29967540
159	Ubiquitination	QIEERKKQLSFISPP HHHHHHHHHCCCCCC	45.43	24816145
161	Phosphorylation	EERKKQLSFISPPTP HHHHHHHCCCCCCCC	20.31	21712546
163	Ubiquitination	RKKQLSFISPPTPQP HHHHHCCCCCCCCCC	5.62	-
164	Phosphorylation	KKQLSFISPPTPQPK HHHHCCCCCCCCCCC	23.86	25159151
167	Phosphorylation	LSFISPPTPQPKTPS HCCCCCCCCCCCCCC	37.63	25159151
171	Ubiquitination	SPPTPQPKTPSSSQP CCCCCCCCCCCCCCC	68.75	24816145
172	Phosphorylation	PPTPQPKTPSSSQPE CCCCCCCCCCCCCCC	34.78	25159151
172	O-linked_Glycosylation	PPTPQPKTPSSSQPE CCCCCCCCCCCCCCC	34.78	28510447
174	Phosphorylation	TPQPKTPSSSQPERL CCCCCCCCCCCCCCC	48.10	30576142
175	Phosphorylation	PQPKTPSSSQPERLP CCCCCCCCCCCCCCC	33.91	22199227
175	O-linked_Glycosylation	PQPKTPSSSQPERLP CCCCCCCCCCCCCCC	33.91	28510447
176	Phosphorylation	QPKTPSSSQPERLPI CCCCCCCCCCCCCCC	54.84	30576142
176	O-linked_Glycosylation	QPKTPSSSQPERLPI CCCCCCCCCCCCCCC	54.84	28510447
186	Phosphorylation	ERLPIGNTIQPSQAA CCCCCCCCCCHHHHH	18.77	30576142
190	Phosphorylation	IGNTIQPSQAATFMN CCCCCCHHHHHHHHH	18.97	26074081
194	Phosphorylation	IQPSQAATFMNDAIE CCHHHHHHHHHHHHH	26.82	26074081
220	Acetylation	IQAQLALKPGLIGNA HHHHHCCCCCCCCCC	31.28	26051181
244	Sumoylation	AMGIAPPKVELKDQT HCCCCCCCEECCCCC	47.48	28112733
251	Phosphorylation	KVELKDQTKPTPLIL CEECCCCCCCCCEEE	49.47	23403867
252	Sumoylation	VELKDQTKPTPLILD EECCCCCCCCCEEEC	41.06	-
252	Sumoylation	VELKDQTKPTPLILD EECCCCCCCCCEEEC	41.06	28112733
252	Ubiquitination	VELKDQTKPTPLILD EECCCCCCCCCEEEC	41.06	29967540
252	Acetylation	VELKDQTKPTPLILD EECCCCCCCCCEEEC	41.06	23236377
254	Phosphorylation	LKDQTKPTPLILDEQ CCCCCCCCCEEECCC	32.08	23403867
264	Phosphorylation	ILDEQGRTVDATGKE EECCCCCEECCCCCE	29.57	20068231
268	Phosphorylation	QGRTVDATGKEIELT CCCEECCCCCEEEEE	44.30	20068231
270	Ubiquitination	RTVDATGKEIELTHR CEECCCCCEEEEECC	51.68	33845483
270	2-Hydroxyisobutyrylation	RTVDATGKEIELTHR CEECCCCCEEEEECC	51.68	-
275	Phosphorylation	TGKEIELTHRMPTLK CCCEEEEECCCCCHH	8.47	20068231
280	Phosphorylation	ELTHRMPTLKANIRA EEECCCCCHHHHHHH	31.39	-
282	Acetylation	THRMPTLKANIRAVK ECCCCCHHHHHHHHH	41.69	25953088
294	Methylation	AVKREQFKQQLKEKP HHHHHHHHHHHHHCC	36.51	115975725
294	Ubiquitination	AVKREQFKQQLKEKP HHHHHHHHHHHHHCC	36.51	24816145
294	Acetylation	AVKREQFKQQLKEKP HHHHHHHHHHHHHCC	36.51	25953088
298	Ubiquitination	EQFKQQLKEKPSEDM HHHHHHHHHCCCHHC	60.39	-
307	Phosphorylation	KPSEDMESNTFFDPR CCCHHCCCCCCCCCC	34.24	28555341
316	Phosphorylation	TFFDPRVSIAPSQRQ CCCCCCCCCCCCHHH	17.82	28555341
319	Ubiquitination	DPRVSIAPSQRQRRT CCCCCCCCCHHHCCC	29.35	24816145
320	Phosphorylation	PRVSIAPSQRQRRTF CCCCCCCCHHHCCCE	29.04	26852163
328	Ubiquitination	QRQRRTFKFHDKGKF HHHCCCEECCCCHHH	40.97	24816145
331	Ubiquitination	RRTFKFHDKGKFEKI CCCEECCCCHHHHHH	65.62	24816145
340	Ubiquitination	GKFEKIAQRLRTKAQ HHHHHHHHHHHHHHH	48.71	24816145
345	2-Hydroxyisobutyrylation	IAQRLRTKAQLEKLQ HHHHHHHHHHHHHHH	27.92	-
350	Ubiquitination	RTKAQLEKLQAEISQ HHHHHHHHHHHHHHH	55.26	29967540
356	Phosphorylation	EKLQAEISQAARKTG HHHHHHHHHHHHHHC	12.79	17525332
376	Sumoylation	RLALIAPKKELKEGD HEEEEECHHHHCCCC	50.27	-
376	Sumoylation	RLALIAPKKELKEGD HEEEEECHHHHCCCC	50.27	-
411	Phosphorylation	ENPKREDYFGITNLV CCCCCCCCCCCCCCC	10.03	18452278
415	Phosphorylation	REDYFGITNLVEHPA CCCCCCCCCCCCCHH	23.91	18452278
432	Phosphorylation	NPPVDNDTPVTLGVY CCCCCCCCCCEEEEE	26.39	25159151
463	Ubiquitination	AQKELQEKVRLGLMP HHHHHHHHHHHCCCC	21.50	24816145
463	2-Hydroxyisobutyrylation	AQKELQEKVRLGLMP HHHHHHHHHHHCCCC	21.50	-
469	Sulfoxidation	EKVRLGLMPPPEPKV HHHHHCCCCCCCCCC	4.43	21406390
475	Ubiquitination	LMPPPEPKVRISNLM CCCCCCCCCCHHHHH	42.35	24816145
479	Phosphorylation	PEPKVRISNLMRVLG CCCCCCHHHHHHHHC	17.22	22817900
494	Phosphorylation	TEAVQDPTKVEAHVR CCHHCCCHHHHHHHH	56.88	22817900
495	Ubiquitination	EAVQDPTKVEAHVRA CHHCCCHHHHHHHHH	43.39	33845483
495	Acetylation	EAVQDPTKVEAHVRA CHHCCCHHHHHHHHH	43.39	26051181
503	Ubiquitination	VEAHVRAQMAKRQKA HHHHHHHHHHHHHHH	23.08	24816145
512	Ubiquitination	AKRQKAHEEANAARK HHHHHHHHHHHHHHH	64.76	24816145
552	Phosphorylation	VYRVRNLSNPAKKFK EEEECCCCCCHHHEE	44.29	29802988
608	Phosphorylation	RIKWDEQTSNTKGDD HHCCCHHCCCCCCCC	23.15	22167270
609	Phosphorylation	IKWDEQTSNTKGDDD HCCCHHCCCCCCCCC	42.04	22167270
611	Phosphorylation	WDEQTSNTKGDDDEE CCHHCCCCCCCCCHH	35.85	22167270
619	Phosphorylation	KGDDDEESDEEAVKK CCCCCHHCHHHHHHH	48.55	29255136
627	Phosphorylation	DEEAVKKTNKCVLVW HHHHHHHHCCEEEEE	33.90	26074081
637	Phosphorylation	CVLVWEGTAKDRSFG EEEEECCCCCCCCCC	21.01	26074081
647	Ubiquitination	DRSFGEMKFKQCPTE CCCCCCCCCCCCCCH	45.14	24816145
647	Acetylation	DRSFGEMKFKQCPTE CCCCCCCCCCCCCCH	45.14	26051181
649	Malonylation	SFGEMKFKQCPTENM CCCCCCCCCCCCHHH	45.53	26320211
651	Glutathionylation	GEMKFKQCPTENMAR CCCCCCCCCCHHHHH	4.67	22555962

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
161	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
167	T	Phosphorylation	Kinase	CDK2	P24941	PSP
494	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	PRPF19	Q9UMS4	PMID:20595234

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PRPF3_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 PRPF3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CC85B_HUMAN	CCDC85B	physical	16189514
GTPB3_HUMAN	GTPBP3	physical	16189514
DPY30_HUMAN	DPY30	physical	16189514
UBP4_HUMAN	USP4	physical	20595234
SART3_HUMAN	SART3	physical	20595234
PRP19_HUMAN	PRPF19	physical	20595234
NH2L1_HUMAN	NHP2L1	physical	16723661
PPIH_HUMAN	PPIH	physical	16723661
PRPF3_HUMAN	PRPF3	physical	16723661
PRP4_HUMAN	PRPF4	physical	16723661
PRP31_HUMAN	PRPF31	physical	16723661
SNUT1_HUMAN	SART1	physical	16723661
U2AF2_HUMAN	U2AF2	physical	22939629
SNUT1_HUMAN	SART1	physical	22939629
SF3A2_HUMAN	SF3A2	physical	22939629
SMD2_HUMAN	SNRPD2	physical	22939629
SF3A3_HUMAN	SF3A3	physical	22939629
SRSF5_HUMAN	SRSF5	physical	22939629
RU2A_HUMAN	SNRPA1	physical	22939629
SPF27_HUMAN	BCAS2	physical	22939629
SRRM2_HUMAN	SRRM2	physical	22939629
SRSF7_HUMAN	SRSF7	physical	22939629
RBM25_HUMAN	RBM25	physical	22939629
SF3A1_HUMAN	SF3A1	physical	22939629
RU1C_HUMAN	SNRPC	physical	22939629
SON_HUMAN	SON	physical	22939629
TR150_HUMAN	THRAP3	physical	22939629
RS10_HUMAN	RPS10	physical	22939629
SEPT2_HUMAN	SEPT2	physical	22939629
SP16H_HUMAN	SUPT16H	physical	22939629
SEPT7_HUMAN	SEPT7	physical	22939629
SF3B2_HUMAN	SF3B2	physical	22365833
SPF30_HUMAN	SMNDC1	physical	22365833
U2AF2_HUMAN	U2AF2	physical	22365833
RBM39_HUMAN	RBM39	physical	22365833
PRPF3_HUMAN	PRPF3	physical	22365833
CTBL1_HUMAN	CTNNBL1	physical	22365833
SNIP1_HUMAN	SNIP1	physical	22365833
MFAP1_HUMAN	MFAP1	physical	22365833
SLU7_HUMAN	SLU7	physical	22365833
F10C1_HUMAN	FRA10AC1	physical	22365833
PCBP1_HUMAN	PCBP1	physical	22365833
NKAP_HUMAN	NKAP	physical	22365833
ZCH10_HUMAN	ZCCHC10	physical	22365833
TRI39_HUMAN	TRIM39	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
BRCA1_HUMAN	BRCA1	physical	25184681
CD2B2_HUMAN	CD2BP2	physical	26344197
PLRG1_HUMAN	PLRG1	physical	26344197
PRP19_HUMAN	PRPF19	physical	26344197
PRP31_HUMAN	PRPF31	physical	26344197
PRP4_HUMAN	PRPF4	physical	26344197
RBM25_HUMAN	RBM25	physical	26344197
RBM26_HUMAN	RBM26	physical	26344197
RU17_HUMAN	SNRNP70	physical	26344197
SRRM1_HUMAN	SRRM1	physical	26344197
UTP20_HUMAN	UTP20	physical	26344197
SART3_HUMAN	SART3	physical	28514442
STPAP_HUMAN	TUT1	physical	28514442
PRP4_HUMAN	PRPF4	physical	28514442
AKA7A_HUMAN	AKAP7	physical	28514442
AKA7G_HUMAN	AKAP7	physical	28514442
CCD84_HUMAN	CCDC84	physical	28514442
SNR27_HUMAN	SNRNP27	physical	28514442
ZGPAT_HUMAN	ZGPAT	physical	28514442
MEPCE_HUMAN	MEPCE	physical	28514442
DDX23_HUMAN	DDX23	physical	28514442
PRP31_HUMAN	PRPF31	physical	28514442
TMOD3_HUMAN	TMOD3	physical	28514442
SNUT1_HUMAN	SART1	physical	28514442
SNR40_HUMAN	SNRNP40	physical	28514442
RBM42_HUMAN	RBM42	physical	28514442
LSM2_HUMAN	LSM2	physical	28514442
LSM4_HUMAN	LSM4	physical	28514442
RSMB_HUMAN	SNRPB	physical	28514442
PRP6_HUMAN	PRPF6	physical	28514442
NH2L1_HUMAN	NHP2L1	physical	28514442
LSM8_HUMAN	LSM8	physical	28514442
SMD2_HUMAN	SNRPD2	physical	28514442
SMD1_HUMAN	SNRPD1	physical	28514442
U520_HUMAN	SNRNP200	physical	28514442
LSM3_HUMAN	LSM3	physical	28514442
FBX11_HUMAN	FBXO11	physical	28514442
TXN4A_HUMAN	TXNL4A	physical	28514442
PRP4_HUMAN	PRPF4	physical	27173435
THOC4_HUMAN	ALYREF	physical	27173435
LSM4_HUMAN	LSM4	physical	27173435
LSM8_HUMAN	LSM8	physical	27173435
RL26L_HUMAN	RPL26L1	physical	27173435
SART3_HUMAN	SART3	physical	27173435
OLA1_HUMAN	OLA1	physical	27173435
RL32_HUMAN	RPL32	physical	27173435
LSM6_HUMAN	LSM6	physical	27173435
RINI_HUMAN	RNH1	physical	27173435
CHCH2_HUMAN	CHCHD2	physical	27173435
UBIM_HUMAN	FAU	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
601414	Retinitis pigmentosa 18 (RP18)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PRPF3_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-619, AND MASSSPECTROMETRY.	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-164 AND THR-167, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND MASSSPECTROMETRY.	18318008 [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-164; THR-167 ANDSER-619, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-619, ANDMASS SPECTROMETRY.	19007248 [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-356, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND MASSSPECTROMETRY.	17287340 [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-133, AND MASSSPECTROMETRY.	16565220 [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-619, AND MASSSPECTROMETRY.	17081983 [Abstract]