dbPTM

LA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LA_HUMAN
UniProt AC	P05455
Protein Name	Lupus La protein
Gene Name	SSB
Organism	Homo sapiens (Human).
Sequence Length	408
Subcellular Localization	Nucleus .
Protein Description	Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation. [PubMed: 3192525]
Protein Sequence	MAENGDNEKMAALEAKICHQIEYYFGDFNLPRDKFLKEQIKLDEGWVPLEIMIKFNRLNRLTTDFNVIVEALSKSKAELMEISEDKTKIRRSPSKPLPEVTDEYKNDVKNRSVYIKGFPTDATLDDIKEWLEDKGQVLNIQMRRTLHKAFKGSIFVVFDSIESAKKFVETPGQKYKETDLLILFKDDYFAKKNEERKQNKVEAKLRAKQEQEAKQKLEEDAEMKSLEEKIGCLLKFSGDLDDQTCREDLHILFSNHGEIKWIDFVRGAKEGIILFKEKAKEALGKAKDANNGNLQLRNKEVTWEVLEGEVEKEALKKIIEDQQESLNKWKSKGRRFKGKGKGNKAAQPGSGKGKVQFQGKKTKFASDDEHDEHDENGATGPVKRAREETDKEEPASKQQKTENGAGDQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Ubiquitination	AENGDNEKMAALEAK CCCCCHHHHHHHHHH	39.84	22817900
9	2-Hydroxyisobutyrylation	AENGDNEKMAALEAK CCCCCHHHHHHHHHH	39.84	-
9	Ubiquitination	AENGDNEKMAALEAK CCCCCHHHHHHHHHH	39.84	21890473
9	Ubiquitination	AENGDNEKMAALEAK CCCCCHHHHHHHHHH	39.84	21890473
16	Ubiquitination	KMAALEAKICHQIEY HHHHHHHHHHHHHHH	36.17	32015554
23	Phosphorylation	KICHQIEYYFGDFNL HHHHHHHHHHCCCCC	13.01	17360941
24	Phosphorylation	ICHQIEYYFGDFNLP HHHHHHHHHCCCCCC	6.57	20090780
37	Ubiquitination	LPRDKFLKEQIKLDE CCHHHHHHHHHCCCC	51.19	21906983
37	2-Hydroxyisobutyrylation	LPRDKFLKEQIKLDE CCHHHHHHHHHCCCC	51.19	-
37	Acetylation	LPRDKFLKEQIKLDE CCHHHHHHHHHCCCC	51.19	26822725
37	Ubiquitination	LPRDKFLKEQIKLDE CCHHHHHHHHHCCCC	51.19	21890473
37	Ubiquitination	LPRDKFLKEQIKLDE CCHHHHHHHHHCCCC	51.19	21890473
41	Sumoylation	KFLKEQIKLDEGWVP HHHHHHHCCCCCCEE	49.97	-
41	Ubiquitination	KFLKEQIKLDEGWVP HHHHHHHCCCCCCEE	49.97	32015554
41	Sumoylation	KFLKEQIKLDEGWVP HHHHHHHCCCCCCEE	49.97	-
52	Sulfoxidation	GWVPLEIMIKFNRLN CCEEHHHEEHHHHHC	1.67	30846556
54	Ubiquitination	VPLEIMIKFNRLNRL EEHHHEEHHHHHCCC	21.14	32015554
73	Phosphorylation	NVIVEALSKSKAELM HHHHHHHHHCHHHHH	41.76	21601212
74	Ubiquitination	VIVEALSKSKAELME HHHHHHHHCHHHHHH	57.75	22817900
75	Phosphorylation	IVEALSKSKAELMEI HHHHHHHCHHHHHHH	33.45	21406692
76	Ubiquitination	VEALSKSKAELMEIS HHHHHHCHHHHHHHC	50.01	21906983
76	Sumoylation	VEALSKSKAELMEIS HHHHHHCHHHHHHHC	50.01	-
76	2-Hydroxyisobutyrylation	VEALSKSKAELMEIS HHHHHHCHHHHHHHC	50.01	-
76	Ubiquitination	VEALSKSKAELMEIS HHHHHHCHHHHHHHC	50.01	21890473
76	Ubiquitination	VEALSKSKAELMEIS HHHHHHCHHHHHHHC	50.01	21890473
80	Sulfoxidation	SKSKAELMEISEDKT HHCHHHHHHHCCCCH	3.02	21406390
83	Phosphorylation	KAELMEISEDKTKIR HHHHHHHCCCCHHHC	26.83	24719451
86	Sumoylation	LMEISEDKTKIRRSP HHHHCCCCHHHCCCC	47.90	-
86	Sumoylation	LMEISEDKTKIRRSP HHHHCCCCHHHCCCC	47.90	-
86	Ubiquitination	LMEISEDKTKIRRSP HHHHCCCCHHHCCCC	47.90	33845483
86	2-Hydroxyisobutyrylation	LMEISEDKTKIRRSP HHHHCCCCHHHCCCC	47.90	-
87	Phosphorylation	MEISEDKTKIRRSPS HHHCCCCHHHCCCCC	43.98	26074081
92	Phosphorylation	DKTKIRRSPSKPLPE CCHHHCCCCCCCCCC	24.55	29255136
94	Phosphorylation	TKIRRSPSKPLPEVT HHHCCCCCCCCCCCC	48.42	29255136
95	Acetylation	KIRRSPSKPLPEVTD HHCCCCCCCCCCCCH	54.69	23236377
95	Ubiquitination	KIRRSPSKPLPEVTD HHCCCCCCCCCCCCH	54.69	22817900
95	Ubiquitination	KIRRSPSKPLPEVTD HHCCCCCCCCCCCCH	54.69	21890473
95	Ubiquitination	KIRRSPSKPLPEVTD HHCCCCCCCCCCCCH	54.69	21890473
101	Phosphorylation	SKPLPEVTDEYKNDV CCCCCCCCHHHHHCC	22.81	29255136
104	Phosphorylation	LPEVTDEYKNDVKNR CCCCCHHHHHCCCCC	20.22	24732914
105	Ubiquitination	PEVTDEYKNDVKNRS CCCCHHHHHCCCCCE	44.62	33845483
105	Sumoylation	PEVTDEYKNDVKNRS CCCCHHHHHCCCCCE	44.62	-
105	2-Hydroxyisobutyrylation	PEVTDEYKNDVKNRS CCCCHHHHHCCCCCE	44.62	-
105	Malonylation	PEVTDEYKNDVKNRS CCCCHHHHHCCCCCE	44.62	26320211
105	Acetylation	PEVTDEYKNDVKNRS CCCCHHHHHCCCCCE	44.62	26051181
109	Ubiquitination	DEYKNDVKNRSVYIK HHHHHCCCCCEEEEE	49.89	24816145
116	Acetylation	KNRSVYIKGFPTDAT CCCEEEEECCCCCCC	36.49	19608861
116	Ubiquitination	KNRSVYIKGFPTDAT CCCEEEEECCCCCCC	36.49	23000965
116	Sumoylation	KNRSVYIKGFPTDAT CCCEEEEECCCCCCC	36.49	19608861
116	Succinylation	KNRSVYIKGFPTDAT CCCEEEEECCCCCCC	36.49	23954790
116	Ubiquitination	KNRSVYIKGFPTDAT CCCEEEEECCCCCCC	36.49	21890473
116	Ubiquitination	KNRSVYIKGFPTDAT CCCEEEEECCCCCCC	36.49	21890473
120	Phosphorylation	VYIKGFPTDATLDDI EEEECCCCCCCHHHH	35.68	23917254
128	Acetylation	DATLDDIKEWLEDKG CCCHHHHHHHHHHHC	50.24	19608861
128	Ubiquitination	DATLDDIKEWLEDKG CCCHHHHHHHHHHHC	50.24	32015554
134	Ubiquitination	IKEWLEDKGQVLNIQ HHHHHHHHCCEEEHH	41.70	-
142	Sulfoxidation	GQVLNIQMRRTLHKA CCEEEHHHHHHHHHH	2.51	21406390
148	2-Hydroxyisobutyrylation	QMRRTLHKAFKGSIF HHHHHHHHHHCCCEE	59.64	-
153	Phosphorylation	LHKAFKGSIFVVFDS HHHHHCCCEEEEEEC	17.28	23401153
165	Acetylation	FDSIESAKKFVETPG EECHHHHHHHHCCCC	56.90	24846101
165	Ubiquitination	FDSIESAKKFVETPG EECHHHHHHHHCCCC	56.90	21906983
166	Ubiquitination	DSIESAKKFVETPGQ ECHHHHHHHHCCCCC	55.12	22817900
166	2-Hydroxyisobutyrylation	DSIESAKKFVETPGQ ECHHHHHHHHCCCCC	55.12	-
174	Ubiquitination	FVETPGQKYKETDLL HHCCCCCCCEECCEE	65.29	23000965
174	Acetylation	FVETPGQKYKETDLL HHCCCCCCCEECCEE	65.29	27452117
176	Ubiquitination	ETPGQKYKETDLLIL CCCCCCCEECCEEEE	62.26	23000965
176	2-Hydroxyisobutyrylation	ETPGQKYKETDLLIL CCCCCCCEECCEEEE	62.26	-
176	Ubiquitination	ETPGQKYKETDLLIL CCCCCCCEECCEEEE	62.26	21890473
176	Ubiquitination	ETPGQKYKETDLLIL CCCCCCCEECCEEEE	62.26	21890473
178	Phosphorylation	PGQKYKETDLLILFK CCCCCEECCEEEEEC	28.00	20068231
185	Acetylation	TDLLILFKDDYFAKK CCEEEEECHHHHHHC	46.36	30583871
185	Sumoylation	TDLLILFKDDYFAKK CCEEEEECHHHHHHC	46.36	-
185	Sumoylation	TDLLILFKDDYFAKK CCEEEEECHHHHHHC	46.36	-
188	Phosphorylation	LILFKDDYFAKKNEE EEEECHHHHHHCCHH	18.64	-
191	Methylation	FKDDYFAKKNEERKQ ECHHHHHHCCHHHHH	46.35	115980481
191	Ubiquitination	FKDDYFAKKNEERKQ ECHHHHHHCCHHHHH	46.35	33845483
197	Ubiquitination	AKKNEERKQNKVEAK HHCCHHHHHHHHHHH	62.60	24816145
200	Sumoylation	NEERKQNKVEAKLRA CHHHHHHHHHHHHHH	38.67	-
200	Sumoylation	NEERKQNKVEAKLRA CHHHHHHHHHHHHHH	38.67	-
204	Acetylation	KQNKVEAKLRAKQEQ HHHHHHHHHHHHHHH	25.63	25953088
208	Sumoylation	VEAKLRAKQEQEAKQ HHHHHHHHHHHHHHH	48.19	-
208	Sumoylation	VEAKLRAKQEQEAKQ HHHHHHHHHHHHHHH	48.19	-
208	Ubiquitination	VEAKLRAKQEQEAKQ HHHHHHHHHHHHHHH	48.19	29967540
214	Ubiquitination	AKQEQEAKQKLEEDA HHHHHHHHHHHHHHH	47.41	22817900
216	Acetylation	QEQEAKQKLEEDAEM HHHHHHHHHHHHHHH	58.10	23749302
216	Ubiquitination	QEQEAKQKLEEDAEM HHHHHHHHHHHHHHH	58.10	21906983
224	Ubiquitination	LEEDAEMKSLEEKIG HHHHHHHHHHHHHHH	43.31	22817900
224	Ubiquitination	LEEDAEMKSLEEKIG HHHHHHHHHHHHHHH	43.31	21890473
224	Ubiquitination	LEEDAEMKSLEEKIG HHHHHHHHHHHHHHH	43.31	21890473
225	Phosphorylation	EEDAEMKSLEEKIGC HHHHHHHHHHHHHHH	39.44	26462736
229	Ubiquitination	EMKSLEEKIGCLLKF HHHHHHHHHHHHHHC	34.72	22817900
229	2-Hydroxyisobutyrylation	EMKSLEEKIGCLLKF HHHHHHHHHHHHHHC	34.72	-
229	Acetylation	EMKSLEEKIGCLLKF HHHHHHHHHHHHHHC	34.72	25953088
229	Ubiquitination	EMKSLEEKIGCLLKF HHHHHHHHHHHHHHC	34.72	21890473
229	Ubiquitination	EMKSLEEKIGCLLKF HHHHHHHHHHHHHHC	34.72	21890473
232	S-nitrosocysteine	SLEEKIGCLLKFSGD HHHHHHHHHHHCCCC	4.60	-
232	S-nitrosylation	SLEEKIGCLLKFSGD HHHHHHHHHHHCCCC	4.60	19483679
235	Ubiquitination	EKIGCLLKFSGDLDD HHHHHHHHCCCCCCC	25.24	32015554
235	2-Hydroxyisobutyrylation	EKIGCLLKFSGDLDD HHHHHHHHCCCCCCC	25.24	-
266	Methylation	IKWIDFVRGAKEGII EEEEEECCCCCCEEE	39.07	115917865
269	Ubiquitination	IDFVRGAKEGIILFK EEECCCCCCEEEEEH	60.33	33845483
269	2-Hydroxyisobutyrylation	IDFVRGAKEGIILFK EEECCCCCCEEEEEH	60.33	-
276	Ubiquitination	KEGIILFKEKAKEAL CCEEEEEHHHHHHHH	55.66	33845483
280	Acetylation	ILFKEKAKEALGKAK EEEHHHHHHHHHCCC	55.37	7693029
280	2-Hydroxyisobutyrylation	ILFKEKAKEALGKAK EEEHHHHHHHHHCCC	55.37	-
285	Acetylation	KAKEALGKAKDANNG HHHHHHHCCCCCCCC	53.78	24884075
285	Ubiquitination	KAKEALGKAKDANNG HHHHHHHCCCCCCCC	53.78	22817900
287	Ubiquitination	KEALGKAKDANNGNL HHHHHCCCCCCCCCC	61.94	22817900
287	2-Hydroxyisobutyrylation	KEALGKAKDANNGNL HHHHHCCCCCCCCCC	61.94	-
287	Ubiquitination	KEALGKAKDANNGNL HHHHHCCCCCCCCCC	61.94	21890473
287	Ubiquitination	KEALGKAKDANNGNL HHHHHCCCCCCCCCC	61.94	21890473
299	Ubiquitination	GNLQLRNKEVTWEVL CCCEECCEEEEHHHH	47.32	29967540
299	2-Hydroxyisobutyrylation	GNLQLRNKEVTWEVL CCCEECCEEEEHHHH	47.32	-
302	Phosphorylation	QLRNKEVTWEVLEGE EECCEEEEHHHHCCH	19.59	22817900
312	Ubiquitination	VLEGEVEKEALKKII HHCCHHHHHHHHHHH	54.16	21906983
312	2-Hydroxyisobutyrylation	VLEGEVEKEALKKII HHCCHHHHHHHHHHH	54.16	-
312	Ubiquitination	VLEGEVEKEALKKII HHCCHHHHHHHHHHH	54.16	21890473
312	Ubiquitination	VLEGEVEKEALKKII HHCCHHHHHHHHHHH	54.16	21890473
316	Ubiquitination	EVEKEALKKIIEDQQ HHHHHHHHHHHHHHH	49.31	23503661
317	Ubiquitination	VEKEALKKIIEDQQE HHHHHHHHHHHHHHH	50.17	33845483
317	2-Hydroxyisobutyrylation	VEKEALKKIIEDQQE HHHHHHHHHHHHHHH	50.17	-
325	Phosphorylation	IIEDQQESLNKWKSK HHHHHHHHHHHHHHC	32.67	21815630
328	Acetylation	DQQESLNKWKSKGRR HHHHHHHHHHHCCCC	62.38	19608861
328	Ubiquitination	DQQESLNKWKSKGRR HHHHHHHHHHHCCCC	62.38	23000965
328	Neddylation	DQQESLNKWKSKGRR HHHHHHHHHHHCCCC	62.38	32015554
328	Ubiquitination	DQQESLNKWKSKGRR HHHHHHHHHHHCCCC	62.38	21890473
328	Ubiquitination	DQQESLNKWKSKGRR HHHHHHHHHHHCCCC	62.38	21890473
330	Ubiquitination	QESLNKWKSKGRRFK HHHHHHHHHCCCCCC	43.85	23000965
332	Ubiquitination	SLNKWKSKGRRFKGK HHHHHHHCCCCCCCC	53.35	23000965
341	Acetylation	RRFKGKGKGNKAAQP CCCCCCCCCCCCCCC	63.90	-
350	Phosphorylation	NKAAQPGSGKGKVQF CCCCCCCCCCCEEEE	43.97	26546556
352	Acetylation	AAQPGSGKGKVQFQG CCCCCCCCCEEEECC	58.20	26051181
352	Ubiquitination	AAQPGSGKGKVQFQG CCCCCCCCCEEEECC	58.20	29967540
354	Acetylation	QPGSGKGKVQFQGKK CCCCCCCEEEECCEE	36.03	23749302
354	Ubiquitination	QPGSGKGKVQFQGKK CCCCCCCEEEECCEE	36.03	27667366
360	Acetylation	GKVQFQGKKTKFASD CEEEECCEEEECCCC	46.62	19608861
360	Ubiquitination	GKVQFQGKKTKFASD CEEEECCEEEECCCC	46.62	33845483
361	Acetylation	KVQFQGKKTKFASDD EEEECCEEEECCCCC	64.87	12439017
362	Phosphorylation	VQFQGKKTKFASDDE EEECCEEEECCCCCC	34.58	23927012
366	Phosphorylation	GKKTKFASDDEHDEH CEEEECCCCCCCCCC	49.04	29255136
379	Phosphorylation	EHDENGATGPVKRAR CCCCCCCCCHHHHHH	43.34	22167270
383	Ubiquitination	NGATGPVKRAREETD CCCCCHHHHHHHHCC	43.40	32015554
383	Acetylation	NGATGPVKRAREETD CCCCCHHHHHHHHCC	43.40	25953088
389	Phosphorylation	VKRAREETDKEEPAS HHHHHHHCCCCCCHH	47.84	27273156
391	Acetylation	RAREETDKEEPASKQ HHHHHCCCCCCHHHH	71.98	23749302
397	Ubiquitination	DKEEPASKQQKTENG CCCCCHHHHHCCCCC	59.87	22817900
400	Ubiquitination	EPASKQQKTENGAGD CCHHHHHCCCCCCCC	56.14	33845483

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
366	S	Phosphorylation	Kinase	CSK21	P68400	PhosphoELM
366	S	Phosphorylation	Kinase	CSNK2A1	P19139	GPS
366	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
366	S	Phosphorylation	Kinase	CK2	-	Uniprot
366	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
389	T	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NUCL_HUMAN	NCL	physical	12096904
RO60_HUMAN	TROVE2	physical	10785401
A4_HUMAN	APP	physical	21832049
IL7RA_HUMAN	IL7R	physical	23151878
HMGA1_HUMAN	HMGA1	physical	18850631
SRC8_HUMAN	CTTN	physical	22863883
SYK_HUMAN	KARS	physical	22863883
PP2AA_HUMAN	PPP2CA	physical	22863883
ANKY2_HUMAN	ANKMY2	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
LARP7_HUMAN	LARP7	physical	26344197
NAT10_HUMAN	NAT10	physical	26344197
MK67I_HUMAN	NIFK	physical	26344197
DPOE1_HUMAN	POLE	physical	26344197
RPAC1_HUMAN	POLR1C	physical	26344197
RBM34_HUMAN	RBM34	physical	26344197
SMC3_HUMAN	SMC3	physical	26344197
TPM2_HUMAN	TPM2	physical	26344197
TRM6_HUMAN	TRMT6	physical	26344197
WDR74_HUMAN	WDR74	physical	26344197
ZN593_HUMAN	ZNF593	physical	26344197
PRP31_HUMAN	PRPF31	physical	27173435

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 LA_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-116; LYS-128; LYS-328 ANDLYS-360, 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-366, AND MASSSPECTROMETRY.	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-366, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-362 AND SER-366, ANDMASS SPECTROMETRY.	19413330 [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-366, AND MASSSPECTROMETRY.	18691976 [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-366, 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-366, AND MASSSPECTROMETRY.	18669648 [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-366, AND MASSSPECTROMETRY.	19367720 [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-366, AND MASSSPECTROMETRY.	17924679 [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-366, AND MASSSPECTROMETRY.	17287340 [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-366, 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-366, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASSSPECTROMETRY.	16083285 [Abstract]
"Phosphorylation of the human La antigen on serine 366 can regulaterecycling of RNA polymerase III transcription complexes."; Fan H., Sakulich A.L., Goodier J.L., Zhang X., Qin J., Maraie R.J.; Cell 88:707-715(1997). Cited for: PHOSPHORYLATION AT SER-366.	9054510 [Abstract]