dbPTM

NUP50_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NUP50_HUMAN
UniProt AC	Q9UKX7
Protein Name	Nuclear pore complex protein Nup50
Gene Name	NUP50
Organism	Homo sapiens (Human).
Sequence Length	468
Subcellular Localization	Nucleus, nuclear pore complex . Nucleus membrane Peripheral membrane protein Nucleoplasmic side . Localizes to the nucleoplasmic fibrils of the nuclear pore complex (By similarity). Dissociates from the NPC structure early during prophase of mito
Protein Description	Component of the nuclear pore complex that has a direct role in nuclear protein import. [PubMed: 20016008 Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling]
Protein Sequence	MAKRNAEKELTDRNWDQEDEAEEVGTFSMASEEVLKNRAIKKAKRRNVGFESDTGGAFKGFKGLVVPSGGGRFSGFGSGAGGKPLEGLSNGNNITSAPPFASAKAAADPKVAFGSLAANGPTTLVDKVSNPKTNGDSQQPSSSGLASSKACVGNAYHKQLAALNCSVRDWIVKHVNTNPLCDLTPIFKDYEKYLANIEQQHGNSGRNSESESNKVAAETQSPSLFGSTKLQQESTFLFHGNKTEDTPDKKMEVASEKKTDPSSLGATSASFNFGKKVDSSVLGSLSSVPLTGFSFSPGNSSLFGKDTTQSKPVSSPFPTKPLEGQAEGDSGECKGGDEEENDEPPKVVVTEVKEEDAFYSKKCKLFYKKDNEFKEKGIGTLHLKPTANQKTQLLVRADTNLGNILLNVLIPPNMPCTRTGKNNVLIVCVPNPPIDEKNATMPVTMLIRVKTSEDADELHKILLEKKDA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2 (in isoform 2)	Acetylation	-	21.37	22814378
8	Acetylation	MAKRNAEKELTDRNW CCCCHHHHHHHCCCC	56.46	23749302
8	Ubiquitination	MAKRNAEKELTDRNW CCCCHHHHHHHCCCC	56.46	-
31	Ubiquitination	VGTFSMASEEVLKNR HCCCHHCCHHHHHHH	26.16	21890473
31	Phosphorylation	VGTFSMASEEVLKNR HCCCHHCCHHHHHHH	26.16	26670566
34	Ubiquitination	FSMASEEVLKNRAIK CHHCCHHHHHHHHHH	8.94	21890473
52	Phosphorylation	RRNVGFESDTGGAFK HCCCCCCCCCCCCCC	37.91	30266825
54	Phosphorylation	NVGFESDTGGAFKGF CCCCCCCCCCCCCCC	46.96	30266825
55	Ubiquitination	VGFESDTGGAFKGFK CCCCCCCCCCCCCCC	30.35	21890473
55	Acetylation	VGFESDTGGAFKGFK CCCCCCCCCCCCCCC	30.35	19608861
55	Ubiquitination	VGFESDTGGAFKGFK CCCCCCCCCCCCCCC	30.35	19608861
55 (in isoform 2)	Ubiquitination	-	30.35	-
59	Acetylation	SDTGGAFKGFKGLVV CCCCCCCCCCCEEEE	64.00	25953088
59	Methylation	SDTGGAFKGFKGLVV CCCCCCCCCCCEEEE	64.00	91125
59	Ubiquitination	SDTGGAFKGFKGLVV CCCCCCCCCCCEEEE	64.00	21890473
62	Acetylation	GGAFKGFKGLVVPSG CCCCCCCCEEEECCC	61.06	25953088
62	Methylation	GGAFKGFKGLVVPSG CCCCCCCCEEEECCC	61.06	44497529
62	Ubiquitination	GGAFKGFKGLVVPSG CCCCCCCCEEEECCC	61.06	21890473
68	Phosphorylation	FKGLVVPSGGGRFSG CCEEEECCCCCCCCC	38.16	25159151
74	Phosphorylation	PSGGGRFSGFGSGAG CCCCCCCCCCCCCCC	31.67	25159151
76 (in isoform 2)	Ubiquitination	-	7.34	-
78	Phosphorylation	GRFSGFGSGAGGKPL CCCCCCCCCCCCCCC	24.17	25159151
82 (in isoform 2)	Ubiquitination	-	28.07	-
83	Acetylation	FGSGAGGKPLEGLSN CCCCCCCCCCCCCCC	45.57	19608861
83	Ubiquitination	FGSGAGGKPLEGLSN CCCCCCCCCCCCCCC	45.57	21906983
99	Ubiquitination	NNITSAPPFASAKAA CCCCCCCCCCCCHHH	36.83	21890473
99 (in isoform 2)	Ubiquitination	-	36.83	-
104	Ubiquitination	APPFASAKAAADPKV CCCCCCCHHHCCCCE	35.74	21890473
110	Ubiquitination	AKAAADPKVAFGSLA CHHHCCCCEEEHHHH	46.90	21890473
115	Phosphorylation	DPKVAFGSLAANGPT CCCEEEHHHHCCCCC	14.37	19060867
122	Phosphorylation	SLAANGPTTLVDKVS HHHCCCCCEEEECCC	33.87	24972180
123	Phosphorylation	LAANGPTTLVDKVSN HHCCCCCEEEECCCC	28.11	24972180
127	Acetylation	GPTTLVDKVSNPKTN CCCEEEECCCCCCCC	39.83	25953088
127	Ubiquitination	GPTTLVDKVSNPKTN CCCEEEECCCCCCCC	39.83	21890473
132	Ubiquitination	VDKVSNPKTNGDSQQ EECCCCCCCCCCCCC	59.89	-
133	Phosphorylation	DKVSNPKTNGDSQQP ECCCCCCCCCCCCCC	45.77	20068231
137	Phosphorylation	NPKTNGDSQQPSSSG CCCCCCCCCCCCCCC	31.92	20068231
141	Phosphorylation	NGDSQQPSSSGLASS CCCCCCCCCCCCCCC	32.57	20068231
142	Phosphorylation	GDSQQPSSSGLASSK CCCCCCCCCCCCCCC	34.80	20068231
143	Phosphorylation	DSQQPSSSGLASSKA CCCCCCCCCCCCCCH	42.01	25159151
147	Phosphorylation	PSSSGLASSKACVGN CCCCCCCCCCHHHHH	37.10	20068231
148	Phosphorylation	SSSGLASSKACVGNA CCCCCCCCCHHHHHH	20.75	20068231
149	Acetylation	SSGLASSKACVGNAY CCCCCCCCHHHHHHH	43.22	26051181
158	Acetylation	CVGNAYHKQLAALNC HHHHHHHHHHHHHCC	34.04	23749302
158	Malonylation	CVGNAYHKQLAALNC HHHHHHHHHHHHHCC	34.04	26320211
158	Ubiquitination	CVGNAYHKQLAALNC HHHHHHHHHHHHHCC	34.04	-
164	Ubiquitination	HKQLAALNCSVRDWI HHHHHHHCCCHHHHH	15.99	21890473
164 (in isoform 2)	Ubiquitination	-	15.99	-
173	Acetylation	SVRDWIVKHVNTNPL CHHHHHHHHCCCCCC	32.47	23954790
173	Ubiquitination	SVRDWIVKHVNTNPL CHHHHHHHHCCCCCC	32.47	-
181	Glutathionylation	HVNTNPLCDLTPIFK HCCCCCCCCCCHHHC	4.20	22555962
184	Phosphorylation	TNPLCDLTPIFKDYE CCCCCCCCHHHCCHH	10.90	-
188	Acetylation	CDLTPIFKDYEKYLA CCCCHHHCCHHHHHH	61.18	26051181
188	Ubiquitination	CDLTPIFKDYEKYLA CCCCHHHCCHHHHHH	61.18	-
192	Acetylation	PIFKDYEKYLANIEQ HHHCCHHHHHHHHHH	39.06	25953088
192	Ubiquitination	PIFKDYEKYLANIEQ HHHCCHHHHHHHHHH	39.06	21890473
193	Phosphorylation	IFKDYEKYLANIEQQ HHCCHHHHHHHHHHH	10.10	26074081
201	Ubiquitination	LANIEQQHGNSGRNS HHHHHHHHCCCCCCC	36.78	21890473
204	Phosphorylation	IEQQHGNSGRNSESE HHHHHCCCCCCCHHH	43.66	25159151
208	Phosphorylation	HGNSGRNSESESNKV HCCCCCCCHHHHHHH	40.93	25159151
210	Phosphorylation	NSGRNSESESNKVAA CCCCCCHHHHHHHHH	46.26	28450419
212	Phosphorylation	GRNSESESNKVAAET CCCCHHHHHHHHHHC	51.75	28464451
214	Ubiquitination	NSESESNKVAAETQS CCHHHHHHHHHHCCC	42.40	-
219	Phosphorylation	SNKVAAETQSPSLFG HHHHHHHCCCCHHCC	29.62	30266825
221	Phosphorylation	KVAAETQSPSLFGST HHHHHCCCCHHCCCC	24.71	29255136
223	Phosphorylation	AAETQSPSLFGSTKL HHHCCCCHHCCCCCC	41.39	19664994
227	Phosphorylation	QSPSLFGSTKLQQES CCCHHCCCCCCEEEE	18.29	25159151
228	Phosphorylation	SPSLFGSTKLQQEST CCHHCCCCCCEEEEE	35.83	25159151
229	Acetylation	PSLFGSTKLQQESTF CHHCCCCCCEEEEEE	46.10	25953088
229	Ubiquitination	PSLFGSTKLQQESTF CHHCCCCCCEEEEEE	46.10	21890473
230	Ubiquitination	SLFGSTKLQQESTFL HHCCCCCCEEEEEEE	6.87	21890473
234	Phosphorylation	STKLQQESTFLFHGN CCCCEEEEEEEECCC	21.81	30576142
235	Phosphorylation	TKLQQESTFLFHGNK CCCEEEEEEEECCCC	24.49	28555341
242	Acetylation	TFLFHGNKTEDTPDK EEEECCCCCCCCCCC	58.86	26051181
242	Ubiquitination	TFLFHGNKTEDTPDK EEEECCCCCCCCCCC	58.86	-
243	Phosphorylation	FLFHGNKTEDTPDKK EEECCCCCCCCCCCC	42.99	30576142
246	Phosphorylation	HGNKTEDTPDKKMEV CCCCCCCCCCCCCCH	27.44	25159151
247	Acetylation	GNKTEDTPDKKMEVA CCCCCCCCCCCCCHH	64.84	19608861
247 (in isoform 2)	Ubiquitination	-	64.84	-
249	Acetylation	KTEDTPDKKMEVASE CCCCCCCCCCCHHHC	56.05	23749302
255	Phosphorylation	DKKMEVASEKKTDPS CCCCCHHHCCCCCHH	55.94	21815630
258	Ubiquitination	MEVASEKKTDPSSLG CCHHHCCCCCHHHCC	54.85	21890473
259	Phosphorylation	EVASEKKTDPSSLGA CHHHCCCCCHHHCCC	65.30	25159151
262	Phosphorylation	SEKKTDPSSLGATSA HCCCCCHHHCCCCEE	40.79	22199227
263	Phosphorylation	EKKTDPSSLGATSAS CCCCCHHHCCCCEEE	35.89	25159151
267	Phosphorylation	DPSSLGATSASFNFG CHHHCCCCEEEECCC	24.03	20068231
268	O-linked_Glycosylation	PSSLGATSASFNFGK HHHCCCCEEEECCCC	22.75	30059200
268	Phosphorylation	PSSLGATSASFNFGK HHHCCCCEEEECCCC	22.75	25159151
270	Phosphorylation	SLGATSASFNFGKKV HCCCCEEEECCCCCC	22.08	25159151
275	2-Hydroxyisobutyrylation	SASFNFGKKVDSSVL EEEECCCCCCCHHHH	45.55	-
275	Acetylation	SASFNFGKKVDSSVL EEEECCCCCCCHHHH	45.55	23954790
275	Methylation	SASFNFGKKVDSSVL EEEECCCCCCCHHHH	45.55	19608861
275	Ubiquitination	SASFNFGKKVDSSVL EEEECCCCCCCHHHH	45.55	19608861
279	Phosphorylation	NFGKKVDSSVLGSLS CCCCCCCHHHHHCCC	25.90	23090842
280	Phosphorylation	FGKKVDSSVLGSLSS CCCCCCHHHHHCCCC	19.52	23090842
284	O-linked_Glycosylation	VDSSVLGSLSSVPLT CCHHHHHCCCCCCCC	22.40	30059200
284	Phosphorylation	VDSSVLGSLSSVPLT CCHHHHHCCCCCCCC	22.40	23090842
286	Phosphorylation	SSVLGSLSSVPLTGF HHHHHCCCCCCCCEE	30.87	23090842
287	Phosphorylation	SVLGSLSSVPLTGFS HHHHCCCCCCCCEEE	32.80	23090842
291	Phosphorylation	SLSSVPLTGFSFSPG CCCCCCCCEEEECCC	30.06	28450419
294	Phosphorylation	SVPLTGFSFSPGNSS CCCCCEEEECCCCCC	26.59	22115753
296	Phosphorylation	PLTGFSFSPGNSSLF CCCEEEECCCCCCCC	30.60	25159151
300	Phosphorylation	FSFSPGNSSLFGKDT EEECCCCCCCCCCCC	34.04	22115753
301	Phosphorylation	SFSPGNSSLFGKDTT EECCCCCCCCCCCCC	31.55	28450419
305	Ubiquitination	GNSSLFGKDTTQSKP CCCCCCCCCCCCCCC	44.56	-
307	Phosphorylation	SSLFGKDTTQSKPVS CCCCCCCCCCCCCCC	30.16	30576142
308	Phosphorylation	SLFGKDTTQSKPVSS CCCCCCCCCCCCCCC	40.76	25394399
310	Phosphorylation	FGKDTTQSKPVSSPF CCCCCCCCCCCCCCC	36.51	30576142
311	Acetylation	GKDTTQSKPVSSPFP CCCCCCCCCCCCCCC	39.35	23954790
314	Phosphorylation	TTQSKPVSSPFPTKP CCCCCCCCCCCCCCC	40.60	29255136
315	Phosphorylation	TQSKPVSSPFPTKPL CCCCCCCCCCCCCCC	30.69	29255136
318 (in isoform 2)	Ubiquitination	-	42.78	-
319	Phosphorylation	PVSSPFPTKPLEGQA CCCCCCCCCCCCCCC	45.75	29255136
320	Acetylation	VSSPFPTKPLEGQAE CCCCCCCCCCCCCCC	48.09	26051181
320	Ubiquitination	VSSPFPTKPLEGQAE CCCCCCCCCCCCCCC	48.09	-
325 (in isoform 2)	Ubiquitination	-	27.19	-
330	Phosphorylation	EGQAEGDSGECKGGD CCCCCCCCCCCCCCC	47.55	29255136
346	Ubiquitination	EENDEPPKVVVTEVK CCCCCCCCEEEEEEC	59.38	21890473
353	Sumoylation	KVVVTEVKEEDAFYS CEEEEEECHHHHHHH	49.51	-
353	Sumoylation	KVVVTEVKEEDAFYS CEEEEEECHHHHHHH	49.51	28112733
353	Ubiquitination	KVVVTEVKEEDAFYS CEEEEEECHHHHHHH	49.51	21890473
364	Acetylation	AFYSKKCKLFYKKDN HHHHCCCEEEEECCC	50.97	26051181
376	Ubiquitination	KDNEFKEKGIGTLHL CCCCHHHCCCEEEEE	57.32	-
384	Acetylation	GIGTLHLKPTANQKT CCEEEEECCCCCCCE	29.58	25953088
399	Phosphorylation	QLLVRADTNLGNILL EEEEECCCCCCCHHH	31.21	20068231
432	Ubiquitination	LIVCVPNPPIDEKNA EEEECCCCCCCCCCC	22.58	21890473
450	Acetylation	VTMLIRVKTSEDADE EEEEEEEECCCCHHH	36.16	27452117
460	Acetylation	EDADELHKILLEKKD CCHHHHHHHHHHHHC	47.90	25953088
460	Ubiquitination	EDADELHKILLEKKD CCHHHHHHHHHHHHC	47.90	21890473

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
221	S	Phosphorylation	Kinase	CDK1	P06493	PSP
221	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
221	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
315	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
315	S	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NUP50_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 NUP50_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IMB1_HUMAN	KPNB1	physical	12176322
IMA1_HUMAN	KPNA2	physical	12176322
NU153_HUMAN	NUP153	physical	10891500
A4_HUMAN	APP	physical	21832049
UBAP2_HUMAN	UBAP2	physical	22939629
TOIP1_HUMAN	TOR1AIP1	physical	22939629
ACACA_HUMAN	ACACA	physical	22863883
E41L1_HUMAN	EPB41L1	physical	22863883
WASC4_HUMAN	KIAA1033	physical	22863883
KINH_HUMAN	KIF5B	physical	22863883
T22D1_HUMAN	TSC22D1	physical	22863883
TTI1_HUMAN	TTI1	physical	22863883
IMA7_HUMAN	KPNA6	physical	25416956
TP53B_HUMAN	TP53BP1	physical	26186194
PHF10_HUMAN	PHF10	physical	26186194
WDHD1_HUMAN	WDHD1	physical	26186194
SMRC2_HUMAN	SMARCC2	physical	26186194
BD1L1_HUMAN	BOD1L1	physical	26186194
ARID2_HUMAN	ARID2	physical	26186194
IMA6_HUMAN	KPNA5	physical	26186194
IMA7_HUMAN	KPNA6	physical	26186194
IMA5_HUMAN	KPNA1	physical	26186194
TAF4_HUMAN	TAF4	physical	26186194
RBP2_HUMAN	RANBP2	physical	26186194
KIFC1_HUMAN	KIFC1	physical	26186194
PB1_HUMAN	PBRM1	physical	26186194
SMRD3_HUMAN	SMARCD3	physical	26186194
SMRD2_HUMAN	SMARCD2	physical	26186194
SMRD1_HUMAN	SMARCD1	physical	26186194
KLHL7_HUMAN	KLHL7	physical	26186194
FBX28_HUMAN	FBXO28	physical	26186194
BRD7_HUMAN	BRD7	physical	26186194
IMA3_HUMAN	KPNA4	physical	26186194
NU153_HUMAN	NUP153	physical	26186194
BCL7B_HUMAN	BCL7B	physical	26186194
MCE1_HUMAN	RNGTT	physical	26186194
SET1A_HUMAN	SETD1A	physical	26186194
CDCA2_HUMAN	CDCA2	physical	26186194
SPOP_HUMAN	SPOP	physical	26186194
CXXC1_HUMAN	CXXC1	physical	26186194
MRGBP_HUMAN	MRGBP	physical	26186194
KI18B_HUMAN	KIF18B	physical	26186194
CCD22_HUMAN	CCDC22	physical	26344197
FLNB_HUMAN	FLNB	physical	26344197
GMFB_HUMAN	GMFB	physical	26344197
HPBP1_HUMAN	HSPBP1	physical	26344197
IMDH2_HUMAN	IMPDH2	physical	26344197
SYNC_HUMAN	NARS	physical	26344197
NU153_HUMAN	NUP153	physical	26344197
PAIP1_HUMAN	PAIP1	physical	26344197
PFD4_HUMAN	PFDN4	physical	26344197
PLEC_HUMAN	PLEC	physical	26344197
AAPK1_HUMAN	PRKAA1	physical	26344197
PSME3_HUMAN	PSME3	physical	26344197
RANG_HUMAN	RANBP1	physical	26344197
SBDS_HUMAN	SBDS	physical	26344197
STXB1_HUMAN	STXBP1	physical	26344197
KIFC1_HUMAN	KIFC1	physical	28514442
MCE1_HUMAN	RNGTT	physical	28514442
WDHD1_HUMAN	WDHD1	physical	28514442
BD1L1_HUMAN	BOD1L1	physical	28514442
KLHL7_HUMAN	KLHL7	physical	28514442
SPOP_HUMAN	SPOP	physical	28514442
ARID2_HUMAN	ARID2	physical	28514442
PB1_HUMAN	PBRM1	physical	28514442
CXXC1_HUMAN	CXXC1	physical	28514442
PHF10_HUMAN	PHF10	physical	28514442
NU153_HUMAN	NUP153	physical	28514442
CDCA2_HUMAN	CDCA2	physical	28514442
BCL7B_HUMAN	BCL7B	physical	28514442
BRD7_HUMAN	BRD7	physical	28514442
SET1A_HUMAN	SETD1A	physical	28514442
FBX28_HUMAN	FBXO28	physical	28514442
KI18B_HUMAN	KIF18B	physical	28514442
SMRD2_HUMAN	SMARCD2	physical	28514442
SMRC2_HUMAN	SMARCC2	physical	28514442
SMRD3_HUMAN	SMARCD3	physical	28514442
SMRD1_HUMAN	SMARCD1	physical	28514442
IMA3_HUMAN	KPNA4	physical	28514442
IMB1_HUMAN	KPNB1	physical	28514442
IMA7_HUMAN	KPNA6	physical	28514442
TP53B_HUMAN	TP53BP1	physical	28514442
IMA6_HUMAN	KPNA5	physical	28514442
IMA5_HUMAN	KPNA1	physical	28514442
MARF1_HUMAN	KIAA0430	physical	27173435
PAN2_HUMAN	PAN2	physical	27173435
NISCH_HUMAN	NISCH	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 NUP50_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-83, 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-221, 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-221, AND MASSSPECTROMETRY.	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 SER-221, AND MASSSPECTROMETRY.	18669648 [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-219 AND SER-221, ANDMASS SPECTROMETRY.	17287340 [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-221, AND MASSSPECTROMETRY.	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 SER-221, AND MASSSPECTROMETRY.	17081983 [Abstract]