dbPTM

RBM39_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBM39_HUMAN
UniProt AC	Q14498
Protein Name	RNA-binding protein 39
Gene Name	RBM39
Organism	Homo sapiens (Human).
Sequence Length	530
Subcellular Localization	Nucleus speckle. Concentrated in nuclear speckles. Colocalizes with the core spliceosomal snRNP proteins.
Protein Description	Transcriptional coactivator for steroid nuclear receptors ESR1/ER-alpha and ESR2/ER-beta, and JUN/AP-1 (By similarity). May be involved in pre-mRNA splicing process..
Protein Sequence	MADDIDIEAMLEAPYKKDENKLSSANGHEERSKKRKKSKSRSRSHERKRSKSKERKRSRDRERKKSKSRERKRSRSKERRRSRSRSRDRRFRGRYRSPYSGPKFNSAIRGKIGLPHSIKLSRRRSRSKSPFRKDKSPVREPIDNLTPEERDARTVFCMQLAARIRPRDLEEFFSTVGKVRDVRMISDRNSRRSKGIAYVEFVDVSSVPLAIGLTGQRVLGVPIIVQASQAEKNRAAAMANNLQKGSAGPMRLYVGSLHFNITEDMLRGIFEPFGRIESIQLMMDSETGRSKGYGFITFSDSECAKKALEQLNGFELAGRPMKVGHVTERTDASSASSFLDSDELERTGIDLGTTGRLQLMARLAEGTGLQIPPAAQQALQMSGSLAFGAVAEFSFVIDLQTRLSQQTEASALAAAASVQPLATQCFQLSNMFNPQTEEEVGWDTEIKDDVIEECNKHGGVIHIYVDKNSAQGNVYVKCPSIAAAIAAVNALHGRWFAGKMITAAYVPLPTYHNLFPDSMTATQLLVPSRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADDIDIEA ------CCCCCCHHH	24.15	22223895
15	Phosphorylation	EAMLEAPYKKDENKL HHHHCCCCCCCCCCC	37.40	20068231
15 (in isoform 2)	Phosphorylation	-	37.40	-
16	Sumoylation	AMLEAPYKKDENKLS HHHCCCCCCCCCCCC	53.33	-
16	Sumoylation	AMLEAPYKKDENKLS HHHCCCCCCCCCCCC	53.33	-
21	Sumoylation	PYKKDENKLSSANGH CCCCCCCCCCCCCCC	47.93	-
21	Sumoylation	PYKKDENKLSSANGH CCCCCCCCCCCCCCC	47.93	-
21	Acetylation	PYKKDENKLSSANGH CCCCCCCCCCCCCCC	47.93	26051181
23	Phosphorylation	KKDENKLSSANGHEE CCCCCCCCCCCCCHH	29.07	30108239
24	Phosphorylation	KDENKLSSANGHEER CCCCCCCCCCCCHHH	35.87	20363803
24 (in isoform 2)	Phosphorylation	-	35.87	-
40	Phosphorylation	KKRKKSKSRSRSHER HHHHHHHHHHHHHHH	42.45	29743597
40 (in isoform 2)	Phosphorylation	-	42.45	-
42	Phosphorylation	RKKSKSRSRSHERKR HHHHHHHHHHHHHHH	45.27	29743597
44	Phosphorylation	KSKSRSRSHERKRSK HHHHHHHHHHHHHHH	30.83	29743597
44 (in isoform 2)	Phosphorylation	-	30.83	-
50	Phosphorylation	RSHERKRSKSKERKR HHHHHHHHHHHHHHH	44.29	-
58	Phosphorylation	KSKERKRSRDRERKK HHHHHHHHHHHHHHH	41.38	20068231
84	Phosphorylation	KERRRSRSRSRDRRF HHHHHHHHHHHHHHH	35.54	20068231
86	Phosphorylation	RRRSRSRSRDRRFRG HHHHHHHHHHHHHHC	39.52	20068231
95	Phosphorylation	DRRFRGRYRSPYSGP HHHHHCCCCCCCCCC	20.47	25463755
95 (in isoform 2)	Phosphorylation	-	20.47	-
95 (in isoform 3)	Phosphorylation	-	20.47	26699800
96	Methylation	RRFRGRYRSPYSGPK HHHHCCCCCCCCCCC	29.78	115491475
97	Phosphorylation	RFRGRYRSPYSGPKF HHHCCCCCCCCCCCH	21.18	22167270
97 (in isoform 2)	Phosphorylation	-	21.18	-
97 (in isoform 1)	Phosphorylation	-	21.18	24719451
97 (in isoform 3)	Phosphorylation	-	21.18	28355574
99	Phosphorylation	RGRYRSPYSGPKFNS HCCCCCCCCCCCHHH	27.75	22167270
99 (in isoform 2)	Phosphorylation	-	27.75	-
100	Phosphorylation	GRYRSPYSGPKFNSA CCCCCCCCCCCHHHH	52.59	22167270
100 (in isoform 2)	Phosphorylation	-	52.59	-
103	Acetylation	RSPYSGPKFNSAIRG CCCCCCCCHHHHHHC	61.78	25953088
106	Phosphorylation	YSGPKFNSAIRGKIG CCCCCHHHHHHCCCC	28.36	25159151
109	Dimethylation	PKFNSAIRGKIGLPH CCHHHHHHCCCCCCC	39.82	-
109	Methylation	PKFNSAIRGKIGLPH CCHHHHHHCCCCCCC	39.82	12019201
111	Methylation	FNSAIRGKIGLPHSI HHHHHHCCCCCCCCH	24.61	23748837
111	Sumoylation	FNSAIRGKIGLPHSI HHHHHHCCCCCCCCH	24.61	28112733
117	Phosphorylation	GKIGLPHSIKLSRRR CCCCCCCCHHHHCCC	21.34	25159151
117 (in isoform 2)	Phosphorylation	-	21.34	-
119	Sumoylation	IGLPHSIKLSRRRSR CCCCCCHHHHCCCCC	43.34	-
119	Ubiquitination	IGLPHSIKLSRRRSR CCCCCCHHHHCCCCC	43.34	21890473
119	Sumoylation	IGLPHSIKLSRRRSR CCCCCCHHHHCCCCC	43.34	28112733
119	Ubiquitination	IGLPHSIKLSRRRSR CCCCCCHHHHCCCCC	43.34	21890473
119	Acetylation	IGLPHSIKLSRRRSR CCCCCCHHHHCCCCC	43.34	25953088
119 (in isoform 1)	Ubiquitination	-	43.34	21890473
119 (in isoform 2)	Ubiquitination	-	43.34	21890473
121	Phosphorylation	LPHSIKLSRRRSRSK CCCCHHHHCCCCCCC	20.81	26055452
122	Methylation	PHSIKLSRRRSRSKS CCCHHHHCCCCCCCC	48.76	24391431
123	Methylation	HSIKLSRRRSRSKSP CCHHHHCCCCCCCCC	37.23	24391441
124	Methylation	SIKLSRRRSRSKSPF CHHHHCCCCCCCCCC	35.00	24391451
125	Phosphorylation	IKLSRRRSRSKSPFR HHHHCCCCCCCCCCC	38.81	22167270
127	Phosphorylation	LSRRRSRSKSPFRKD HHCCCCCCCCCCCCC	38.44	30266825
127 (in isoform 2)	Phosphorylation	-	38.44	-
129	Phosphorylation	RRRSRSKSPFRKDKS CCCCCCCCCCCCCCC	30.43	30266825
129 (in isoform 2)	Phosphorylation	-	30.43	-
136	Phosphorylation	SPFRKDKSPVREPID CCCCCCCCCCCCCCC	38.47	29255136
136 (in isoform 2)	Phosphorylation	-	38.47	-
146	Phosphorylation	REPIDNLTPEERDAR CCCCCCCCHHHHHHH	34.60	25159151
146 (in isoform 2)	Phosphorylation	-	34.60	-
154	Phosphorylation	PEERDARTVFCMQLA HHHHHHHHHHHHHHH	21.47	20068231
154 (in isoform 2)	Phosphorylation	-	21.47	-
157	Glutathionylation	RDARTVFCMQLAARI HHHHHHHHHHHHHHC	1.15	22555962
174	Phosphorylation	RDLEEFFSTVGKVRD CCHHHHHHHCCCHHE	27.75	21712546
178	Ubiquitination	EFFSTVGKVRDVRMI HHHHHCCCHHEEEEE	29.75	22053931
178	2-Hydroxyisobutyrylation	EFFSTVGKVRDVRMI HHHHHCCCHHEEEEE	29.75	-
178	Ubiquitination	EFFSTVGKVRDVRMI HHHHHCCCHHEEEEE	29.75	21890473
178 (in isoform 1)	Ubiquitination	-	29.75	21890473
178 (in isoform 2)	Ubiquitination	-	29.75	21890473
183	Methylation	VGKVRDVRMISDRNS CCCHHEEEEECCCCC	22.47	115491467
186	Phosphorylation	VRDVRMISDRNSRRS HHEEEEECCCCCCCC	22.60	29449344
190	Phosphorylation	RMISDRNSRRSKGIA EEECCCCCCCCCCEE	29.93	28102081
193	Phosphorylation	SDRNSRRSKGIAYVE CCCCCCCCCCEEEEE	33.84	29496963
198	Phosphorylation	RRSKGIAYVEFVDVS CCCCCEEEEEEEECC	9.89	28122231
205	Phosphorylation	YVEFVDVSSVPLAIG EEEEEECCCCCEEEE	22.58	28122231
206	Phosphorylation	VEFVDVSSVPLAIGL EEEEECCCCCEEEEC	27.83	28122231
228	Phosphorylation	VPIIVQASQAEKNRA CCEEEECHHHHHHHH	16.90	21712546
232	Sumoylation	VQASQAEKNRAAAMA EECHHHHHHHHHHHH	55.54	-
232	Ubiquitination	VQASQAEKNRAAAMA EECHHHHHHHHHHHH	55.54	21906983
232	Sumoylation	VQASQAEKNRAAAMA EECHHHHHHHHHHHH	55.54	-
232	2-Hydroxyisobutyrylation	VQASQAEKNRAAAMA EECHHHHHHHHHHHH	55.54	-
232	Acetylation	VQASQAEKNRAAAMA EECHHHHHHHHHHHH	55.54	25953088
232 (in isoform 1)	Ubiquitination	-	55.54	21890473
232 (in isoform 2)	Ubiquitination	-	55.54	21890473
244	Ubiquitination	AMANNLQKGSAGPMR HHHHHHHCCCCCCCE	58.98	2190698
244	Sumoylation	AMANNLQKGSAGPMR HHHHHHHCCCCCCCE	58.98	28112733
244 (in isoform 1)	Ubiquitination	-	58.98	21890473
244 (in isoform 2)	Ubiquitination	-	58.98	21890473
253	Phosphorylation	SAGPMRLYVGSLHFN CCCCCEEEEEEEEEE	7.75	-
282	Sulfoxidation	RIESIQLMMDSETGR CEEEEEEEEECCCCC	1.28	21406390
291	Acetylation	DSETGRSKGYGFITF ECCCCCCCCCEEEEE	55.58	26051181
305	2-Hydroxyisobutyrylation	FSDSECAKKALEQLN ECCHHHHHHHHHHCC	50.68	-
305	Acetylation	FSDSECAKKALEQLN ECCHHHHHHHHHHCC	50.68	26051181
306	Ubiquitination	SDSECAKKALEQLNG CCHHHHHHHHHHCCC	39.41	-
322	Ubiquitination	ELAGRPMKVGHVTER EECCCCCCCCCCEEC	47.98	-
330	Phosphorylation	VGHVTERTDASSASS CCCCEECCCCCHHHH	29.68	30266825
330 (in isoform 2)	Phosphorylation	-	29.68	-
333	Phosphorylation	VTERTDASSASSFLD CEECCCCCHHHHHCC	29.28	23401153
334	Phosphorylation	TERTDASSASSFLDS EECCCCCHHHHHCCH	33.61	22617229
334 (in isoform 2)	Phosphorylation	-	33.61	-
336	Phosphorylation	RTDASSASSFLDSDE CCCCCHHHHHCCHHH	24.46	23401153
337	Phosphorylation	TDASSASSFLDSDEL CCCCHHHHHCCHHHH	29.55	30175587
337 (in isoform 2)	Phosphorylation	-	29.55	-
341	Phosphorylation	SASSFLDSDELERTG HHHHHCCHHHHHHHC	34.82	30266825
341 (in isoform 2)	Phosphorylation	-	34.82	-
346	Methylation	LDSDELERTGIDLGT CCHHHHHHHCCCCCH	51.37	115491459
347	Phosphorylation	DSDELERTGIDLGTT CHHHHHHHCCCCCHH	29.16	28450419
353	Phosphorylation	RTGIDLGTTGRLQLM HHCCCCCHHHHHHHH	33.12	23186163
354	Phosphorylation	TGIDLGTTGRLQLMA HCCCCCHHHHHHHHH	20.64	23917254
395 (in isoform 2)	Phosphorylation	-	7.29	-
469	Phosphorylation	HIYVDKNSAQGNVYV EEEECCCCCCCCEEE	27.92	20068231
475	Phosphorylation	NSAQGNVYVKCPSIA CCCCCCEEEECHHHH	9.74	20068231
477	Ubiquitination	AQGNVYVKCPSIAAA CCCCEEEECHHHHHH	23.81	-
477	Acetylation	AQGNVYVKCPSIAAA CCCCEEEECHHHHHH	23.81	26051181
478	S-nitrosocysteine	QGNVYVKCPSIAAAI CCCEEEECHHHHHHH	1.97	-
478	S-nitrosylation	QGNVYVKCPSIAAAI CCCEEEECHHHHHHH	1.97	22178444
505	Phosphorylation	GKMITAAYVPLPTYH CCCEEEEEECCCCCC	10.51	-

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
95	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
99	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	DCAF15	Q66K64	PMID:31819272

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RBM39_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 RBM39_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ESR2_HUMAN	ESR2	physical	11704680
ESR1_HUMAN	ESR1	physical	11704680
JUN_HUMAN	JUN	physical	11704680
SND1_HUMAN	SND1	physical	16051665
RS2_HUMAN	RPS2	physical	16051665
RS3_HUMAN	RPS3	physical	16051665
SRRM2_HUMAN	SRRM2	physical	16051665
ACINU_HUMAN	ACIN1	physical	16051665
U520_HUMAN	SNRNP200	physical	16051665
CDK12_HUMAN	CDK12	physical	16051665
SRRM1_HUMAN	SRRM1	physical	16051665
SF3B1_HUMAN	SF3B1	physical	16051665
RBM25_HUMAN	RBM25	physical	16051665
PININ_HUMAN	PNN	physical	16051665
U2AF2_HUMAN	U2AF2	physical	16051665
PCBP3_HUMAN	PCBP3	physical	16051665
TRA2B_HUMAN	TRA2B	physical	16051665
LC7L2_HUMAN	LUC7L2	physical	16051665
SRSF7_HUMAN	SRSF7	physical	16051665
SRSF1_HUMAN	SRSF1	physical	16051665
SAP18_HUMAN	SAP18	physical	16051665
SMD1_HUMAN	SNRPD1	physical	16051665
HNRPU_HUMAN	HNRNPU	physical	16051665
XRCC5_HUMAN	XRCC5	physical	16051665
XRCC6_HUMAN	XRCC6	physical	16051665
I2BP2_HUMAN	IRF2BP2	physical	16051665
RS13_HUMAN	RPS13	physical	16051665
RL27A_HUMAN	RPL27A	physical	16051665
I2BPL_HUMAN	IRF2BPL	physical	16051665
ESR1_HUMAN	ESR1	physical	15694343
PRGR_HUMAN	PGR	physical	15694343
A4_HUMAN	APP	physical	21832049
SMU1_HUMAN	SMU1	physical	22939629
SPF27_HUMAN	BCAS2	physical	22939629
SNUT2_HUMAN	USP39	physical	22939629
TOP1_HUMAN	TOP1	physical	22939629
RRP7A_HUMAN	RRP7A	physical	22939629
SEPT7_HUMAN	SEPT7	physical	22939629
TR112_HUMAN	TRMT112	physical	22939629
UT14A_HUMAN	UTP14A	physical	22939629
S10A9_HUMAN	S100A9	physical	22939629
RRS1_HUMAN	RRS1	physical	22939629
SEPT2_HUMAN	SEPT2	physical	22939629
VTNC_HUMAN	VTN	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
PR40A_HUMAN	PRPF40A	physical	22365833
RBM25_HUMAN	RBM25	physical	22365833
U2AF2_HUMAN	U2AF2	physical	22365833
CHERP_HUMAN	CHERP	physical	22365833
RBM23_HUMAN	RBM23	physical	22365833
PRPF3_HUMAN	PRPF3	physical	22365833
PR38A_HUMAN	PRPF38A	physical	22365833
SAP18_HUMAN	SAP18	physical	22365833
S30BP_HUMAN	SAP30BP	physical	22365833
HNRH2_HUMAN	HNRNPH2	physical	22365833
NKAP_HUMAN	NKAP	physical	22365833
TOE1_HUMAN	TOE1	physical	22365833
TTC14_HUMAN	TTC14	physical	22365833
ZCH10_HUMAN	ZCCHC10	physical	22365833
R113A_HUMAN	RNF113A	physical	22365833
SRPK2_HUMAN	SRPK2	physical	22365833
SF3B4_HUMAN	SF3B4	physical	25416956
SAP18_HUMAN	SAP18	physical	25416956
BLOM7_HUMAN	KIAA0907	physical	25416956
AR6P4_HUMAN	ARL6IP4	physical	25416956
ZCH10_HUMAN	ZCCHC10	physical	25416956
BANP_HUMAN	BANP	physical	25416956
THAP1_HUMAN	THAP1	physical	25416956
CK057_HUMAN	C11orf57	physical	25416956
PR40A_HUMAN	PRPF40A	physical	25416956
HOMEZ_HUMAN	HOMEZ	physical	25416956
KAD8_HUMAN	AK8	physical	25416956
F200A_HUMAN	FAM200A	physical	25416956
SR1IP_HUMAN	SREK1IP1	physical	25416956
KR122_HUMAN	KRTAP12-2	physical	25416956
PNISR_HUMAN	PNISR	physical	26344197
RBM14_HUMAN	RBM14	physical	26344197
RNPS1_HUMAN	RNPS1	physical	26344197
SON_HUMAN	SON	physical	26344197
SREK1_HUMAN	SREK1	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 RBM39_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-97, AND MASS SPECTROMETRY.	19413330 [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-136; SER-337 ANDSER-341, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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 SER-136, AND MASSSPECTROMETRY.	19369195 [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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-97, AND MASS 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 TYR-95; SER-97; SER-100;SER-117; SER-136; SER-334; SER-337 AND SER-341, 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 SER-97 AND SER-136, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND MASSSPECTROMETRY.	19367720 [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-136, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-136, AND MASSSPECTROMETRY.	18187866 [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-97 AND THR-146, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND MASSSPECTROMETRY.	17487921 [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-97; SER-127; SER-129 ANDSER-136, AND MASS SPECTROMETRY.	17081983 [Abstract]