dbPTM

RS3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS3_HUMAN
UniProt AC	P23396
Protein Name	40S ribosomal protein S3
Gene Name	RPS3
Organism	Homo sapiens (Human).
Sequence Length	243
Subcellular Localization	Cytoplasm . Nucleus . Nucleus, nucleolus . Mitochondrion inner membrane Peripheral membrane protein . Cytoplasm, cytoskeleton, spindle . In normal cells, located mainly in the cytoplasm with small amounts in the nucleus but translocates to the nucl
Protein Description	Involved in translation as a component of the 40S small ribosomal subunit. [PubMed: 8706699 Has endonuclease activity and plays a role in repair of damaged DNA]
Protein Sequence	MAVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPTGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAVQISKKR ------CCCCCCCCC	11.26	25944712
6	Phosphorylation	--MAVQISKKRKFVA --CCCCCCCCCCCCC	18.29	19059439
6	Ubiquitination	--MAVQISKKRKFVA --CCCCCCCCCCCCC	18.29	22817900
7	Ubiquitination	-MAVQISKKRKFVAD -CCCCCCCCCCCCCC	59.22	23000965
7	Acetylation	-MAVQISKKRKFVAD -CCCCCCCCCCCCCC	59.22	25953088
8	Ubiquitination	MAVQISKKRKFVADG CCCCCCCCCCCCCCC	54.77	23000965
10	Ubiquitination	VQISKKRKFVADGIF CCCCCCCCCCCCCCH	53.74	23000965
10	Acetylation	VQISKKRKFVADGIF CCCCCCCCCCCCCCH	53.74	25953088
15	Ubiquitination	KRKFVADGIFKAELN CCCCCCCCCHHHHHH	19.93	23000965
18	Sumoylation	FVADGIFKAELNEFL CCCCCCHHHHHHHHH	38.74	-
18	Ubiquitination	FVADGIFKAELNEFL CCCCCCHHHHHHHHH	38.74	1890473
18	Sumoylation	FVADGIFKAELNEFL CCCCCCHHHHHHHHH	38.74	-
18	Acetylation	FVADGIFKAELNEFL CCCCCCHHHHHHHHH	38.74	26051181
22	Ubiquitination	GIFKAELNEFLTREL CCHHHHHHHHHHHHH	29.49	23000965
25	Ubiquitination	KAELNEFLTRELAED HHHHHHHHHHHHHHC	3.44	23000965
27	Methylation	ELNEFLTRELAEDGY HHHHHHHHHHHHCCC	38.79	115492683
34	Phosphorylation	RELAEDGYSGVEVRV HHHHHCCCCCEEEEE	17.99	28152594
35	Phosphorylation	ELAEDGYSGVEVRVT HHHHCCCCCEEEEEC	41.72	28152594
42	Phosphorylation	SGVEVRVTPTRTEII CCEEEEECCCCCEEE	14.37	22817900
46	Phosphorylation	VRVTPTRTEIIILAT EEECCCCCEEEEEEE	33.73	21712546
59	Ubiquitination	ATRTQNVLGEKGRRI EECCCCCCCCHHHHH	10.86	23000965
61	Ubiquitination	RTQNVLGEKGRRIRE CCCCCCCCHHHHHHH	48.45	23000965
62	Acetylation	TQNVLGEKGRRIREL CCCCCCCHHHHHHHH	56.79	19608861
62	Ubiquitination	TQNVLGEKGRRIREL CCCCCCCHHHHHHHH	56.79	27667366
62	Malonylation	TQNVLGEKGRRIREL CCCCCCCHHHHHHHH	56.79	26320211
64	Asymmetric dimethylarginine	NVLGEKGRRIRELTA CCCCCHHHHHHHHHH	41.75	-
64	Methylation	NVLGEKGRRIRELTA CCCCCHHHHHHHHHH	41.75	19460357
65	Asymmetric dimethylarginine	VLGEKGRRIRELTAV CCCCHHHHHHHHHHH	40.77	-
65	Methylation	VLGEKGRRIRELTAV CCCCHHHHHHHHHHH	40.77	19460357
67	Asymmetric dimethylarginine	GEKGRRIRELTAVVQ CCHHHHHHHHHHHHH	30.94	-
67	Methylation	GEKGRRIRELTAVVQ CCHHHHHHHHHHHHH	30.94	19460357
70	Phosphorylation	GRRIRELTAVVQKRF HHHHHHHHHHHHHHH	16.80	22817900
71	Ubiquitination	RRIRELTAVVQKRFG HHHHHHHHHHHHHHC	16.47	23000965
71	Neddylation	RRIRELTAVVQKRFG HHHHHHHHHHHHHHC	16.47	32015554
75	Acetylation	ELTAVVQKRFGFPEG HHHHHHHHHHCCCCC	37.78	25953088
75	Ubiquitination	ELTAVVQKRFGFPEG HHHHHHHHHHCCCCC	37.78	21906983
76	Ubiquitination	LTAVVQKRFGFPEGS HHHHHHHHHCCCCCC	21.60	23000965
83	Phosphorylation	RFGFPEGSVELYAEK HHCCCCCCCHHHHHH	15.68	28152594
87	Phosphorylation	PEGSVELYAEKVATR CCCCCHHHHHHHHHH	10.14	28152594
88	Ubiquitination	EGSVELYAEKVATRG CCCCHHHHHHHHHHH	23.82	23000965
90	Ubiquitination	SVELYAEKVATRGLC CCHHHHHHHHHHHHH	29.06	27667366
90	Malonylation	SVELYAEKVATRGLC CCHHHHHHHHHHHHH	29.06	26320211
90	Acetylation	SVELYAEKVATRGLC CCHHHHHHHHHHHHH	29.06	23236377
95	Phosphorylation	AEKVATRGLCAIAQA HHHHHHHHHHHHHCH	22.28	32645325
97	S-nitrosocysteine	KVATRGLCAIAQAES HHHHHHHHHHHCHHH	2.61	-
97	Glutathionylation	KVATRGLCAIAQAES HHHHHHHHHHHCHHH	2.61	22555962
97	S-nitrosylation	KVATRGLCAIAQAES HHHHHHHHHHHCHHH	2.61	22178444
97	S-palmitoylation	KVATRGLCAIAQAES HHHHHHHHHHHCHHH	2.61	29575903
101	Ubiquitination	RGLCAIAQAESLRYK HHHHHHHCHHHHHHH	39.28	23000965
104	Phosphorylation	CAIAQAESLRYKLLG HHHHCHHHHHHHHHH	22.59	29255136
104	Ubiquitination	CAIAQAESLRYKLLG HHHHCHHHHHHHHHH	22.59	23000965
104	Neddylation	CAIAQAESLRYKLLG HHHHCHHHHHHHHHH	22.59	32015554
107	Phosphorylation	AQAESLRYKLLGGLA HCHHHHHHHHHHHHH	15.98	28152594
108	Acetylation	QAESLRYKLLGGLAV CHHHHHHHHHHHHHH	30.70	23749302
108	Ubiquitination	QAESLRYKLLGGLAV CHHHHHHHHHHHHHH	30.70	23000965
108	Malonylation	QAESLRYKLLGGLAV CHHHHHHHHHHHHHH	30.70	26320211
119	Glutathionylation	GLAVRRACYGVLRFI HHHHHHHHHHHHHHH	2.63	22555962
119	S-palmitoylation	GLAVRRACYGVLRFI HHHHHHHHHHHHHHH	2.63	29575903
120	Phosphorylation	LAVRRACYGVLRFIM HHHHHHHHHHHHHHH	14.86	28152594
124	Ubiquitination	RACYGVLRFIMESGA HHHHHHHHHHHHCCC	19.35	23000965
132	Succinylation	FIMESGAKGCEVVVS HHHHCCCCCCEEEEC	68.56	-
132	Ubiquitination	FIMESGAKGCEVVVS HHHHCCCCCCEEEEC	68.56	21963094
132	Succinylation	FIMESGAKGCEVVVS HHHHCCCCCCEEEEC	68.56	-
132	Acetylation	FIMESGAKGCEVVVS HHHHCCCCCCEEEEC	68.56	26051181
134	Glutathionylation	MESGAKGCEVVVSGK HHCCCCCCEEEECCC	3.37	22555962
134	S-nitrosylation	MESGAKGCEVVVSGK HHCCCCCCEEEECCC	3.37	2212679
134	S-palmitoylation	MESGAKGCEVVVSGK HHCCCCCCEEEECCC	3.37	26865113
139	Phosphorylation	KGCEVVVSGKLRGQR CCCEEEECCCCCCCC	20.71	21712546
141	Sumoylation	CEVVVSGKLRGQRAK CEEEECCCCCCCCCC	27.75	-
141	Ubiquitination	CEVVVSGKLRGQRAK CEEEECCCCCCCCCC	27.75	23000965
141	Sumoylation	CEVVVSGKLRGQRAK CEEEECCCCCCCCCC	27.75	-
141	Acetylation	CEVVVSGKLRGQRAK CEEEECCCCCCCCCC	27.75	25953088
148	Ubiquitination	KLRGQRAKSMKFVDG CCCCCCCCCCEEECE	53.95	23000965
149	Phosphorylation	LRGQRAKSMKFVDGL CCCCCCCCCEEECEE	26.64	27362937
151	Ubiquitination	GQRAKSMKFVDGLMI CCCCCCCEEECEEEE	49.69	23000965
151	Acetylation	GQRAKSMKFVDGLMI CCCCCCCEEECEEEE	49.69	26051181
157	Sulfoxidation	MKFVDGLMIHSGDPV CEEECEEEEECCCCC	2.95	30846556
157	Ubiquitination	MKFVDGLMIHSGDPV CEEECEEEEECCCCC	2.95	23000965
160	Phosphorylation	VDGLMIHSGDPVNYY ECEEEEECCCCCHHH	33.69	27362937
164	Ubiquitination	MIHSGDPVNYYVDTA EEECCCCCHHHHHHH	9.53	23000965
166	Phosphorylation	HSGDPVNYYVDTAVR ECCCCCHHHHHHHHH	12.71	19534553
167	Phosphorylation	SGDPVNYYVDTAVRH CCCCCHHHHHHHHHH	6.14	21552520
167	Ubiquitination	SGDPVNYYVDTAVRH CCCCCHHHHHHHHHH	6.14	23000965
170	Phosphorylation	PVNYYVDTAVRHVLL CCHHHHHHHHHHHHH	19.60	27362937
185	Ubiquitination	RQGVLGIKVKIMLPW HCCCCEEEEEEEECC	35.36	23000965
187	Ubiquitination	GVLGIKVKIMLPWDP CCCEEEEEEEECCCC	19.86	23000965
187	Acetylation	GVLGIKVKIMLPWDP CCCEEEEEEEECCCC	19.86	26051181
189	Sulfoxidation	LGIKVKIMLPWDPTG CEEEEEEEECCCCCC	2.81	30846556
195	Phosphorylation	IMLPWDPTGKIGPKK EEECCCCCCCCCCCC	48.94	21601212
197	Acetylation	LPWDPTGKIGPKKPL ECCCCCCCCCCCCCC	47.14	23749302
197	Ubiquitination	LPWDPTGKIGPKKPL ECCCCCCCCCCCCCC	47.14	23000965
197	Neddylation	LPWDPTGKIGPKKPL ECCCCCCCCCCCCCC	47.14	32015554
201	Ubiquitination	PTGKIGPKKPLPDHV CCCCCCCCCCCCCCE	62.91	23000965
202	Ubiquitination	TGKIGPKKPLPDHVS CCCCCCCCCCCCCEE	55.72	23000965
202	Malonylation	TGKIGPKKPLPDHVS CCCCCCCCCCCCCEE	55.72	26320211
202	Acetylation	TGKIGPKKPLPDHVS CCCCCCCCCCCCCEE	55.72	26051181
203	Ubiquitination	GKIGPKKPLPDHVSI CCCCCCCCCCCCEEE	56.08	23000965
209	Phosphorylation	KPLPDHVSIVEPKDE CCCCCCEEECCCCCC	19.93	30266825
213	Ubiquitination	DHVSIVEPKDEILPT CCEEECCCCCCCCCC	38.20	23000965
213	Neddylation	DHVSIVEPKDEILPT CCEEECCCCCCCCCC	38.20	32015554
214	Acetylation	HVSIVEPKDEILPTT CEEECCCCCCCCCCC	55.26	23236377
214	Sumoylation	HVSIVEPKDEILPTT CEEECCCCCCCCCCC	55.26	-
214	Ubiquitination	HVSIVEPKDEILPTT CEEECCCCCCCCCCC	55.26	25015289
214	Sumoylation	HVSIVEPKDEILPTT CEEECCCCCCCCCCC	55.26	-
214	Malonylation	HVSIVEPKDEILPTT CEEECCCCCCCCCCC	55.26	26320211
217	Ubiquitination	IVEPKDEILPTTPIS ECCCCCCCCCCCCCC	8.83	23000965
218	Ubiquitination	VEPKDEILPTTPISE CCCCCCCCCCCCCCC	2.65	23000965
220	Phosphorylation	PKDEILPTTPISEQK CCCCCCCCCCCCCCC	41.58	19664994
221	Phosphorylation	KDEILPTTPISEQKG CCCCCCCCCCCCCCC	19.38	19664994
224	Phosphorylation	ILPTTPISEQKGGKP CCCCCCCCCCCCCCC	34.87	22167270
227	Ubiquitination	TTPISEQKGGKPEPP CCCCCCCCCCCCCCC	66.63	23000965
227	Acetylation	TTPISEQKGGKPEPP CCCCCCCCCCCCCCC	66.63	26051181
230	Sumoylation	ISEQKGGKPEPPAMP CCCCCCCCCCCCCCC	55.68	-
230	Ubiquitination	ISEQKGGKPEPPAMP CCCCCCCCCCCCCCC	55.68	21906983
230	Sumoylation	ISEQKGGKPEPPAMP CCCCCCCCCCCCCCC	55.68	28112733
230	Neddylation	ISEQKGGKPEPPAMP CCCCCCCCCCCCCCC	55.68	32015554
230	Acetylation	ISEQKGGKPEPPAMP CCCCCCCCCCCCCCC	55.68	26051181
236	Sulfoxidation	GKPEPPAMPQPVPTA CCCCCCCCCCCCCCC	3.80	21406390
237	Phosphorylation	KPEPPAMPQPVPTA- CCCCCCCCCCCCCC-	37.11	32645325
242	Phosphorylation	AMPQPVPTA------ CCCCCCCCC------	45.28	29255136
243	Ubiquitination	MPQPVPTA------- CCCCCCCC-------	16.02	23000965
246	Ubiquitination	PVPTA---------- CCCCC----------		23000965
246	Neddylation	PVPTA---------- CCCCC----------		32015554
258	Phosphorylation	---------------------- ----------------------		27251275

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
6	S	Phosphorylation	Kinase	PKCD	Q05655	PSP
42	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
42	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
42	T	Phosphorylation	Kinase	MAPK	-	Uniprot
70	T	Phosphorylation	Kinase	AKT1	P31749	PSP
70	T	Phosphorylation	Kinase	AKT1	P47196	PSP
209	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
221	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
221	T	Phosphorylation	Kinase	PKCD	Q05655	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
18	K	Sumoylation	21968017
Sumoylation occurs at one or more of the three consensus sites, Lys-18, Lys-214 and Lys-230.
209	S	Phosphorylation	21399639
Phosphorylated on Ser-209 by IKKB in response to activation of the NF-kappa-B p65-p50 complex which enhances the association of RPS3 with importin-alpha and mediates the nuclear translocation of RPS3.
214	K	Sumoylation	21968017
Sumoylation occurs at one or more of the three consensus sites, Lys-18, Lys-214 and Lys-230.
214	K	ubiquitylation	21968017
Monoubiquitinated at Lys-214 by ZNF598 when a ribosome has stalled during translation of poly(A) sequences, leading to preclude synthesis of a long poly-lysine tail and initiate the ribosome quality control (RQC) pathway to degrade the potentially detrimental aberrant nascent polypeptide.
221	T	Phosphorylation
Phosphorylation at Thr-221 by CDK1 occurs mainly in G2/M phase.
230	K	Sumoylation	21968017
Sumoylation occurs at one or more of the three consensus sites, Lys-18, Lys-214 and Lys-230.

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 RS3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HS90A_HUMAN	HSP90AA1	physical	16314389
HSP74_HUMAN	HSPA4	physical	16314389
TF65_HUMAN	RELA	physical	18045535
NFKB1_HUMAN	NFKB1	physical	18045535
IKBA_HUMAN	NFKBIA	physical	18045535
MDM2_HUMAN	MDM2	physical	19656744
P53_HUMAN	TP53	physical	19656744
SUMO1_HUMAN	SUMO1	physical	21968017
RS9_HUMAN	RPS9	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RL40_HUMAN	UBA52	physical	22939629
TCPA_HUMAN	TCP1	physical	22939629
SND1_HUMAN	SND1	physical	22939629
TPM1_HUMAN	TPM1	physical	22939629
IL7RA_HUMAN	IL7R	physical	23151878
VHL_HUMAN	VHL	physical	23612971
RS2_HUMAN	RPS2	physical	23612971
EIF3A_HUMAN	EIF3A	physical	22863883
EIF3E_HUMAN	EIF3E	physical	22863883
RSSA_HUMAN	RPSA	physical	22863883
LARP1_HUMAN	LARP1	physical	22863883
RS10_HUMAN	RPS10	physical	22863883
RS12_HUMAN	RPS12	physical	22863883
RS24_HUMAN	RPS24	physical	22863883
RS2_HUMAN	RPS2	physical	22863883
RS3A_HUMAN	RPS3A	physical	22863883
RS5_HUMAN	RPS5	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS7_HUMAN	RPS7	physical	22863883
RS9_HUMAN	RPS9	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
TRAF2_HUMAN	TRAF2	physical	23188828
TF65_HUMAN	RELA	physical	23188828
NFKB1_HUMAN	NFKB1	physical	23188828
RM03_HUMAN	MRPL3	physical	26344197
RT12_HUMAN	MRPS12	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13_HUMAN	RPL13	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL18_HUMAN	RPL18	physical	26344197
RL18A_HUMAN	RPL18A	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL26_HUMAN	RPL26	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL31_HUMAN	RPL31	physical	26344197
RL32_HUMAN	RPL32	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL36_HUMAN	RPL36	physical	26344197
RL37_HUMAN	RPL37	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL8_HUMAN	RPL8	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA0_HUMAN	RPLP0	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS15_HUMAN	RPS15	physical	26344197
RS15A_HUMAN	RPS15A	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS19_HUMAN	RPS19	physical	26344197
RS20_HUMAN	RPS20	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS29_HUMAN	RPS29	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS5_HUMAN	RPS5	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS9_HUMAN	RPS9	physical	26344197
RSSA_HUMAN	RPSA	physical	26344197
ACOD_HUMAN	SCD	physical	26344197
LA_HUMAN	SSB	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 RS3_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 THR-220 AND THR-221, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-62, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 THR-221; SER-224 ANDTHR-242, AND MASS SPECTROMETRY.	18691976 [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 THR-220; THR-221 ANDSER-224, AND MASS SPECTROMETRY.	18187866 [Abstract]
"Phosphoproteomic analysis of the human pituitary."; Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.; Pituitary 9:109-120(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND MASSSPECTROMETRY.	16807684 [Abstract]
"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 THR-221, 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 THR-220 AND THR-221, ANDMASS SPECTROMETRY.	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 THR-220 AND THR-221, 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 THR-221 AND THR-242, ANDMASS 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 THR-221, 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 THR-221, 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 THR-221, 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 THR-221, AND MASSSPECTROMETRY.	16565220 [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 THR-221, AND MASSSPECTROMETRY.	15302935 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-166, AND MASSSPECTROMETRY.	19534553 [Abstract]
Ubiquitylation
Reference	PubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-90 AND LYS-202, AND MASSSPECTROMETRY.	18781797 [Abstract]

show

show

show

show

show

show