dbPTM

RL1D1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL1D1_HUMAN
UniProt AC	O76021
Protein Name	Ribosomal L1 domain-containing protein 1
Gene Name	RSL1D1
Organism	Homo sapiens (Human).
Sequence Length	490
Subcellular Localization	Nucleus, nucleolus . Colocalizes with ING1 in the nucleolus after UV stress.
Protein Description	Regulates cellular senescence through inhibition of PTEN translation. Acts as a pro-apoptotic regulator in response to DNA damage..
Protein Sequence	MEDSASASLSSAAATGTSTSTPAAPTARKQLDKEQVRKAVDALLTHCKSRKNNYGLLLNENESLFLMVVLWKIPSKELRVRLTLPHSIRSDSEDICLFTKDEPNSTPEKTEQFYRKLLNKHGIKTVSQIISLQTLKKEYKSYEAKLRLLSSFDFFLTDARIRRLLPSLIGRHFYQRKKVPVSVNLLSKNLSREINDCIGGTVLNISKSGSCSAIRIGHVGMQIEHIIENIVAVTKGLSEKLPEKWESVKLLFVKTEKSAALPIFSSFVSNWDEATKRSLLNKKKKEARRKRRERNFEKQKERKKKRQQARKTASVLSKDDVAPESGDTTVKKPESKKEQTPEHGKKKRGRGKAQVKATNESEDEIPQLVPIGKKTPANEKVEIQKHATGKKSPAKSPNPSTPRGKKRKALPASETPKAAESETPGKSPEKKPKIKEEAVKEKSPSLGKKDARQTPKKPEAKFFTTPSKSVRKASHTPKKWPKKPKVPQST

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEDSASAS -------CCCCHHHH	13.41	22223895
4	Phosphorylation	----MEDSASASLSS ----CCCCHHHHHHH	15.71	20860994
6	Phosphorylation	--MEDSASASLSSAA --CCCCHHHHHHHHH	23.49	18491316
8	Phosphorylation	MEDSASASLSSAAAT CCCCHHHHHHHHHHH	26.70	21406692
10	Phosphorylation	DSASASLSSAAATGT CCHHHHHHHHHHHCC	18.55	21406692
11	Phosphorylation	SASASLSSAAATGTS CHHHHHHHHHHHCCC	27.50	21406692
15	Phosphorylation	SLSSAAATGTSTSTP HHHHHHHHCCCCCCC	35.94	25159151
17	Phosphorylation	SSAAATGTSTSTPAA HHHHHHCCCCCCCCC	25.20	21406692
18	Phosphorylation	SAAATGTSTSTPAAP HHHHHCCCCCCCCCC	23.00	21406692
19	Phosphorylation	AAATGTSTSTPAAPT HHHHCCCCCCCCCCC	36.14	25159151
20	Phosphorylation	AATGTSTSTPAAPTA HHHCCCCCCCCCCCH	31.96	25159151
21	Phosphorylation	ATGTSTSTPAAPTAR HHCCCCCCCCCCCHH	19.62	25159151
26	Phosphorylation	TSTPAAPTARKQLDK CCCCCCCCHHHHCCH	34.07	22210691
29	Ubiquitination	PAAPTARKQLDKEQV CCCCCHHHHCCHHHH	53.39	24816145
33	2-Hydroxyisobutyrylation	TARKQLDKEQVRKAV CHHHHCCHHHHHHHH	59.65	-
33	Acetylation	TARKQLDKEQVRKAV CHHHHCCHHHHHHHH	59.65	26051181
33	Ubiquitination	TARKQLDKEQVRKAV CHHHHCCHHHHHHHH	59.65	29967540
38	Acetylation	LDKEQVRKAVDALLT CCHHHHHHHHHHHHH	54.64	26051181
38	Ubiquitination	LDKEQVRKAVDALLT CCHHHHHHHHHHHHH	54.64	29967540
45	Phosphorylation	KAVDALLTHCKSRKN HHHHHHHHHHHHCCC	26.52	24114839
47	Glutathionylation	VDALLTHCKSRKNNY HHHHHHHHHHCCCCC	3.45	22555962
48	2-Hydroxyisobutyrylation	DALLTHCKSRKNNYG HHHHHHHHHCCCCCE	45.77	-
48	Acetylation	DALLTHCKSRKNNYG HHHHHHHHHCCCCCE	45.77	25953088
48	Ubiquitination	DALLTHCKSRKNNYG HHHHHHHHHCCCCCE	45.77	23000965
51	Ubiquitination	LTHCKSRKNNYGLLL HHHHHHCCCCCEEEE	57.55	23000965
54	Phosphorylation	CKSRKNNYGLLLNEN HHHCCCCCEEEECCC	20.67	-
75	Phosphorylation	VVLWKIPSKELRVRL EEEECCCCHHHEEEE	42.08	24719451
76	2-Hydroxyisobutyrylation	VLWKIPSKELRVRLT EEECCCCHHHEEEEE	56.25	-
87	Phosphorylation	VRLTLPHSIRSDSED EEEECCCCCCCCCCC	20.11	21406692
90	Phosphorylation	TLPHSIRSDSEDICL ECCCCCCCCCCCEEE	43.76	23663014
92	Phosphorylation	PHSIRSDSEDICLFT CCCCCCCCCCEEEEE	38.11	30266825
96	Glutathionylation	RSDSEDICLFTKDEP CCCCCCEEEEECCCC	3.85	22555962
98	Acetylation	DSEDICLFTKDEPNS CCCCEEEEECCCCCC	7.46	-
99	Phosphorylation	SEDICLFTKDEPNST CCCEEEEECCCCCCC	25.33	30266825
100	Acetylation	EDICLFTKDEPNSTP CCEEEEECCCCCCCH	53.40	25825284
100	Ubiquitination	EDICLFTKDEPNSTP CCEEEEECCCCCCCH	53.40	32015554
105	Phosphorylation	FTKDEPNSTPEKTEQ EECCCCCCCHHHHHH	56.93	24732914
106	Phosphorylation	TKDEPNSTPEKTEQF ECCCCCCCHHHHHHH	41.95	24732914
109	2-Hydroxyisobutyrylation	EPNSTPEKTEQFYRK CCCCCHHHHHHHHHH	59.57	-
109	Acetylation	EPNSTPEKTEQFYRK CCCCCHHHHHHHHHH	59.57	23236377
109	Succinylation	EPNSTPEKTEQFYRK CCCCCHHHHHHHHHH	59.57	23954790
109	Ubiquitination	EPNSTPEKTEQFYRK CCCCCHHHHHHHHHH	59.57	32015554
116	Methylation	KTEQFYRKLLNKHGI HHHHHHHHHHHHCCC	46.04	23644510
120	Sumoylation	FYRKLLNKHGIKTVS HHHHHHHHCCCCHHH	43.08	-
120	2-Hydroxyisobutyrylation	FYRKLLNKHGIKTVS HHHHHHHHCCCCHHH	43.08	-
120	Acetylation	FYRKLLNKHGIKTVS HHHHHHHHCCCCHHH	43.08	25825284
120	Methylation	FYRKLLNKHGIKTVS HHHHHHHHCCCCHHH	43.08	23644510
120	Sumoylation	FYRKLLNKHGIKTVS HHHHHHHHCCCCHHH	43.08	28112733
120	Ubiquitination	FYRKLLNKHGIKTVS HHHHHHHHCCCCHHH	43.08	29967540
124	Acetylation	LLNKHGIKTVSQIIS HHHHCCCCHHHHHHH	47.68	26051181
124	Methylation	LLNKHGIKTVSQIIS HHHHCCCCHHHHHHH	47.68	23644510
125	Phosphorylation	LNKHGIKTVSQIISL HHHCCCCHHHHHHHH	24.38	21406692
127	Phosphorylation	KHGIKTVSQIISLQT HCCCCHHHHHHHHHH	22.39	29396449
131	Phosphorylation	KTVSQIISLQTLKKE CHHHHHHHHHHHHHH	18.96	21406692
134	Phosphorylation	SQIISLQTLKKEYKS HHHHHHHHHHHHHCC	45.93	21406692
136	2-Hydroxyisobutyrylation	IISLQTLKKEYKSYE HHHHHHHHHHHCCHH	47.12	-
136	Acetylation	IISLQTLKKEYKSYE HHHHHHHHHHHCCHH	47.12	26051181
139	Phosphorylation	LQTLKKEYKSYEAKL HHHHHHHHCCHHHHH	17.70	-
140	2-Hydroxyisobutyrylation	QTLKKEYKSYEAKLR HHHHHHHCCHHHHHH	47.88	-
140	Acetylation	QTLKKEYKSYEAKLR HHHHHHHCCHHHHHH	47.88	27452117
140	Succinylation	QTLKKEYKSYEAKLR HHHHHHHCCHHHHHH	47.88	23954790
141	Phosphorylation	TLKKEYKSYEAKLRL HHHHHHCCHHHHHHH	27.57	29457462
142	Phosphorylation	LKKEYKSYEAKLRLL HHHHHCCHHHHHHHH	18.76	-
145	2-Hydroxyisobutyrylation	EYKSYEAKLRLLSSF HHCCHHHHHHHHHHC	23.38	-
145	Acetylation	EYKSYEAKLRLLSSF HHCCHHHHHHHHHHC	23.38	26051181
150	Phosphorylation	EAKLRLLSSFDFFLT HHHHHHHHHCHHHHC	33.28	-
160	Acetylation	DFFLTDARIRRLLPS HHHHCHHHHHHHHHH	26.25	-
160	Methylation	DFFLTDARIRRLLPS HHHHCHHHHHHHHHH	26.25	-
167	Phosphorylation	RIRRLLPSLIGRHFY HHHHHHHHHHHHHHH	32.37	-
174	Phosphorylation	SLIGRHFYQRKKVPV HHHHHHHHHCCCCCC	10.98	22817900
182	Phosphorylation	QRKKVPVSVNLLSKN HCCCCCCCHHHHCCC	10.14	21601212
188	Ubiquitination	VSVNLLSKNLSREIN CCHHHHCCCCCHHHH	62.97	21890473
188	Acetylation	VSVNLLSKNLSREIN CCHHHHCCCCCHHHH	62.97	25825284
188	Ubiquitination	VSVNLLSKNLSREIN CCHHHHCCCCCHHHH	62.97	23000965
197	S-nitrosocysteine	LSREINDCIGGTVLN CCHHHHHHCCCEEEE	2.42	-
197	Glutathionylation	LSREINDCIGGTVLN CCHHHHHHCCCEEEE	2.42	22555962
197	S-nitrosylation	LSREINDCIGGTVLN CCHHHHHHCCCEEEE	2.42	19483679
201	Phosphorylation	INDCIGGTVLNISKS HHHHCCCEEEEEECC	19.33	21406692
206	Phosphorylation	GGTVLNISKSGSCSA CCEEEEEECCCCCCE	21.50	21406692
207	Acetylation	GTVLNISKSGSCSAI CEEEEEECCCCCCEE	55.85	26051181
221	Sulfoxidation	IRIGHVGMQIEHIIE EEECCHHHHHHHHHH	3.36	28183972
240	2-Hydroxyisobutyrylation	VTKGLSEKLPEKWES HHCCHHHHCCHHHCC	67.00	-
244	Acetylation	LSEKLPEKWESVKLL HHHHCCHHHCCCEEE	55.08	25825284
244	Ubiquitination	LSEKLPEKWESVKLL HHHHCCHHHCCCEEE	55.08	29967540
249	2-Hydroxyisobutyrylation	PEKWESVKLLFVKTE CHHHCCCEEEEEECC	49.07	-
249	Acetylation	PEKWESVKLLFVKTE CHHHCCCEEEEEECC	49.07	26051181
254	2-Hydroxyisobutyrylation	SVKLLFVKTEKSAAL CCEEEEEECCHHHCH	43.56	-
254	Acetylation	SVKLLFVKTEKSAAL CCEEEEEECCHHHCH	43.56	25825284
254	Sumoylation	SVKLLFVKTEKSAAL CCEEEEEECCHHHCH	43.56	28112733
257	2-Hydroxyisobutyrylation	LLFVKTEKSAALPIF EEEEECCHHHCHHHH	51.10	-
258	Phosphorylation	LFVKTEKSAALPIFS EEEECCHHHCHHHHH	16.73	20068231
266	Phosphorylation	AALPIFSSFVSNWDE HCHHHHHHHHCCCCH	20.93	-
275	Phosphorylation	VSNWDEATKRSLLNK HCCCCHHHHHHHHHH	25.58	-
276	Acetylation	SNWDEATKRSLLNKK CCCCHHHHHHHHHHH	47.22	26051181
278	Phosphorylation	WDEATKRSLLNKKKK CCHHHHHHHHHHHHH	38.47	24719451
285	Ubiquitination	SLLNKKKKEARRKRR HHHHHHHHHHHHHHH	66.54	24816145
300	Ubiquitination	ERNFEKQKERKKKRQ HHHHHHHHHHHHHHH	71.23	24816145
311	Ubiquitination	KKRQQARKTASVLSK HHHHHHHHHHHHHCC	52.00	29967540
312	Phosphorylation	KRQQARKTASVLSKD HHHHHHHHHHHHCCC	20.72	20873877
314	Phosphorylation	QQARKTASVLSKDDV HHHHHHHHHHCCCCC	28.90	20873877
317	Phosphorylation	RKTASVLSKDDVAPE HHHHHHHCCCCCCCC	31.70	27050516
318	Acetylation	KTASVLSKDDVAPES HHHHHHCCCCCCCCC	54.51	23236377
318	Malonylation	KTASVLSKDDVAPES HHHHHHCCCCCCCCC	54.51	32601280
318	Neddylation	KTASVLSKDDVAPES HHHHHHCCCCCCCCC	54.51	32015554
318	Ubiquitination	KTASVLSKDDVAPES HHHHHHCCCCCCCCC	54.51	32015554
325	Phosphorylation	KDDVAPESGDTTVKK CCCCCCCCCCCCCCC	40.69	25159151
328	Phosphorylation	VAPESGDTTVKKPES CCCCCCCCCCCCCCC	36.69	19691289
329	Phosphorylation	APESGDTTVKKPESK CCCCCCCCCCCCCCC	34.76	19691289
331	Acetylation	ESGDTTVKKPESKKE CCCCCCCCCCCCCCC	61.59	25953088
331	Ubiquitination	ESGDTTVKKPESKKE CCCCCCCCCCCCCCC	61.59	32015554
332	Ubiquitination	SGDTTVKKPESKKEQ CCCCCCCCCCCCCCC	50.08	33845483
335	Phosphorylation	TTVKKPESKKEQTPE CCCCCCCCCCCCCCC	58.52	26074081
337	Acetylation	VKKPESKKEQTPEHG CCCCCCCCCCCCCCC	65.42	30585397
340	Phosphorylation	PESKKEQTPEHGKKK CCCCCCCCCCCCCCC	31.56	28176443
345	Acetylation	EQTPEHGKKKRGRGK CCCCCCCCCCCCCCC	57.96	6589853
358	Phosphorylation	GKAQVKATNESEDEI CCCCEECCCCCCCCC	33.53	29255136
361	Phosphorylation	QVKATNESEDEIPQL CEECCCCCCCCCCCC	53.03	19664994
373	Acetylation	PQLVPIGKKTPANEK CCCEECCCCCCCCCC	54.94	25953088
373	Ubiquitination	PQLVPIGKKTPANEK CCCEECCCCCCCCCC	54.94	33845483
374	Acetylation	QLVPIGKKTPANEKV CCEECCCCCCCCCCE	55.30	27452117
375	Phosphorylation	LVPIGKKTPANEKVE CEECCCCCCCCCCEE	30.99	25159151
380	2-Hydroxyisobutyrylation	KKTPANEKVEIQKHA CCCCCCCCEEEEECC	45.00	-
380	Acetylation	KKTPANEKVEIQKHA CCCCCCCCEEEEECC	45.00	25953088
380	Sumoylation	KKTPANEKVEIQKHA CCCCCCCCEEEEECC	45.00	28112733
380	Ubiquitination	KKTPANEKVEIQKHA CCCCCCCCEEEEECC	45.00	33845483
385	2-Hydroxyisobutyrylation	NEKVEIQKHATGKKS CCCEEEEECCCCCCC	40.65	-
385	Acetylation	NEKVEIQKHATGKKS CCCEEEEECCCCCCC	40.65	25953088
385	Ubiquitination	NEKVEIQKHATGKKS CCCEEEEECCCCCCC	40.65	33845483
388	Phosphorylation	VEIQKHATGKKSPAK EEEEECCCCCCCCCC	49.61	24732914
391	Acetylation	QKHATGKKSPAKSPN EECCCCCCCCCCCCC	64.12	25953088
392	Phosphorylation	KHATGKKSPAKSPNP ECCCCCCCCCCCCCC	33.31	22167270
395	Acetylation	TGKKSPAKSPNPSTP CCCCCCCCCCCCCCC	70.59	25953088
395	Methylation	TGKKSPAKSPNPSTP CCCCCCCCCCCCCCC	70.59	-
396	Phosphorylation	GKKSPAKSPNPSTPR CCCCCCCCCCCCCCC	31.83	29255136
400	Phosphorylation	PAKSPNPSTPRGKKR CCCCCCCCCCCCCCC	58.65	27273156
401	Phosphorylation	AKSPNPSTPRGKKRK CCCCCCCCCCCCCCC	20.47	22167270
413	Phosphorylation	KRKALPASETPKAAE CCCCCCCCCCCHHHH	39.81	23401153
415	Phosphorylation	KALPASETPKAAESE CCCCCCCCCHHHHCC	27.82	30266825
417	Ubiquitination	LPASETPKAAESETP CCCCCCCHHHHCCCC	68.59	33845483
421	Phosphorylation	ETPKAAESETPGKSP CCCHHHHCCCCCCCC	41.88	29255136
423	Phosphorylation	PKAAESETPGKSPEK CHHHHCCCCCCCCCC	46.77	29255136
426	Acetylation	AESETPGKSPEKKPK HHCCCCCCCCCCCCC	65.13	25953088
426	Ubiquitination	AESETPGKSPEKKPK HHCCCCCCCCCCCCC	65.13	33845483
427	Phosphorylation	ESETPGKSPEKKPKI HCCCCCCCCCCCCCC	44.18	29255136
435	Sumoylation	PEKKPKIKEEAVKEK CCCCCCCCHHHHHHH	56.48	-
435	Acetylation	PEKKPKIKEEAVKEK CCCCCCCCHHHHHHH	56.48	26051181
435	Sumoylation	PEKKPKIKEEAVKEK CCCCCCCCHHHHHHH	56.48	25218447
435	Ubiquitination	PEKKPKIKEEAVKEK CCCCCCCCHHHHHHH	56.48	33845483
443	Phosphorylation	EEAVKEKSPSLGKKD HHHHHHHCCCCCHHC	22.32	29255136
445	Phosphorylation	AVKEKSPSLGKKDAR HHHHHCCCCCHHCCC	57.77	30266825
448	2-Hydroxyisobutyrylation	EKSPSLGKKDARQTP HHCCCCCHHCCCCCC	53.42	-
448	Acetylation	EKSPSLGKKDARQTP HHCCCCCHHCCCCCC	53.42	25953088
449	"N6,N6-dimethyllysine"	KSPSLGKKDARQTPK HCCCCCHHCCCCCCC	55.62	-
449	Methylation	KSPSLGKKDARQTPK HCCCCCHHCCCCCCC	55.62	-
454	Phosphorylation	GKKDARQTPKKPEAK CHHCCCCCCCCCCCC	31.36	21955146
457	Acetylation	DARQTPKKPEAKFFT CCCCCCCCCCCCCCC	49.66	25953088
461	Acetylation	TPKKPEAKFFTTPSK CCCCCCCCCCCCCCH	39.07	25953088
461	Sumoylation	TPKKPEAKFFTTPSK CCCCCCCCCCCCCCH	39.07	28112733
461	Ubiquitination	TPKKPEAKFFTTPSK CCCCCCCCCCCCCCH	39.07	24816145
464	Phosphorylation	KPEAKFFTTPSKSVR CCCCCCCCCCCHHHH	40.71	30266825
465	Phosphorylation	PEAKFFTTPSKSVRK CCCCCCCCCCHHHHH	22.02	29255136
467	Phosphorylation	AKFFTTPSKSVRKAS CCCCCCCCHHHHHHC	35.16	30266825
468	Acetylation	KFFTTPSKSVRKASH CCCCCCCHHHHHHCC	54.92	19608861
469	Phosphorylation	FFTTPSKSVRKASHT CCCCCCHHHHHHCCC	31.34	23401153
474	Phosphorylation	SKSVRKASHTPKKWP CHHHHHHCCCCCCCC	30.81	28152594
476	Phosphorylation	SVRKASHTPKKWPKK HHHHHCCCCCCCCCC	34.02	24719451
489	Phosphorylation	KKPKVPQST------ CCCCCCCCC------	29.98	24732914
490	Phosphorylation	KPKVPQST------- CCCCCCCC-------	37.06	24732914

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
312	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	LNX1	Q8TBB1	PMID:22889411

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL1D1_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 RL1D1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RS13_HUMAN	RPS13	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RPC3_HUMAN	POLR3C	physical	22939629
RRS1_HUMAN	RRS1	physical	22939629
RPC6_HUMAN	POLR3F	physical	22939629
IL7RA_HUMAN	IL7R	physical	23151878
H1X_HUMAN	H1FX	physical	26344197
MDM2_HUMAN	MDM2	physical	27811966

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 RL1D1_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-361 AND THR-465, 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-468, 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-361, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-361 AND THR-465, 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-358; SER-361; THR-375;SER-392; SER-396; THR-401; THR-415; THR-423; SER-427; SER-443;THR-465; SER-467 AND SER-469, 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-361; SER-427 ANDTHR-465, 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 SER-361, 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-325; THR-328; THR-358;SER-361; SER-392; SER-396; THR-401; SER-421; THR-423; SER-427; SER-443AND SER-445, AND MASS SPECTROMETRY.	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-358; SER-361; THR-465AND SER-467, AND MASS SPECTROMETRY.	17924679 [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-358; SER-361; SER-427AND THR-465, AND MASS SPECTROMETRY.	16565220 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; SER-396; THR-401;THR-423; SER-427 AND THR-465, AND MASS SPECTROMETRY.	16964243 [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 THR-340; SER-361; SER-392;SER-427 AND SER-443, AND MASS SPECTROMETRY.	17081983 [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 SER-361, AND MASSSPECTROMETRY.	15302935 [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 THR-358 AND THR-465, ANDMASS SPECTROMETRY.	16083285 [Abstract]