dbPTM

TE2IP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TE2IP_HUMAN
UniProt AC	Q9NYB0
Protein Name	Telomeric repeat-binding factor 2-interacting protein 1
Gene Name	TERF2IP
Organism	Homo sapiens (Human).
Sequence Length	399
Subcellular Localization	Nucleus . Cytoplasm . Chromosome . Chromosome, telomere . Associates with chromosomes, both at telomeres and in extratelomeric sites. Also exists as a cytoplasmic form, where it associates with the IKK complex.
Protein Description	Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes..
Protein Sequence	MAEAMDLGKDPNGPTHSSTLFVRDDGSSMSFYVRPSPAKRRLSTLILHGGGTVCRVQEPGAVLLAQPGEALAEASGDFISTQYILDCVERNERLELEAYRLGPASAADTGSEAKPGALAEGAAEPEPQRHAGRIAFTDADDVAILTYVKENARSPSSVTGNALWKAMEKSSLTQHSWQSLKDRYLKHLRGQEHKYLLGDAPVSPSSQKLKRKAEEDPEAADSGEPQNKRTPDLPEEEYVKEEIQENEEAVKKMLVEATREFEEVVVDESPPDFEIHITMCDDDPPTPEEDSETQPDEEEEEEEEKVSQPEVGAAIKIIRQLMEKFNLDLSTVTQAFLKNSGELEATSAFLASGQRADGYPIWSRQDDIDLQKDDEDTREALVKKFGAQNVARRIEFRKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEAMDLGK ------CCCCCCCCC	17.16	19413330
15	Phosphorylation	GKDPNGPTHSSTLFV CCCCCCCCCCCEEEE	35.47	-
27	Phosphorylation	LFVRDDGSSMSFYVR EEEECCCCEEEEEEC	29.84	23403867
28	Phosphorylation	FVRDDGSSMSFYVRP EEECCCCEEEEEECC	24.79	23403867
30	Phosphorylation	RDDGSSMSFYVRPSP ECCCCEEEEEECCCC	18.51	27794612
32	Phosphorylation	DGSSMSFYVRPSPAK CCCEEEEEECCCCCH	6.56	21712546
36	Phosphorylation	MSFYVRPSPAKRRLS EEEEECCCCCHHCCE	27.25	25159151
39	Acetylation	YVRPSPAKRRLSTLI EECCCCCHHCCEEEE	41.24	25953088
39	Ubiquitination	YVRPSPAKRRLSTLI EECCCCCHHCCEEEE	41.24	24816145
43	Phosphorylation	SPAKRRLSTLILHGG CCCHHCCEEEEECCC	21.25	27273156
44	Phosphorylation	PAKRRLSTLILHGGG CCHHCCEEEEECCCC	23.55	27273156
52	O-linked_Glycosylation	LILHGGGTVCRVQEP EEECCCCCEEEECCC	21.51	23301498
52	Phosphorylation	LILHGGGTVCRVQEP EEECCCCCEEEECCC	21.51	23927012
54	S-nitrosylation	LHGGGTVCRVQEPGA ECCCCCEEEECCCCC	3.37	24105792
105	Phosphorylation	AYRLGPASAADTGSE EEECCCCCCCCCCCC	27.42	24719451
109	Phosphorylation	GPASAADTGSEAKPG CCCCCCCCCCCCCCC	37.57	25850435
111	Phosphorylation	ASAADTGSEAKPGAL CCCCCCCCCCCCCHH	36.15	26714015
114	Acetylation	ADTGSEAKPGALAEG CCCCCCCCCCHHCCC	39.68	26051181
114	Sumoylation	ADTGSEAKPGALAEG CCCCCCCCCCHHCCC	39.68	28112733
114	Ubiquitination	ADTGSEAKPGALAEG CCCCCCCCCCHHCCC	39.68	21906983
146	Phosphorylation	ADDVAILTYVKENAR HHHEEEEEEHHHHCC	21.84	26074081
147	Phosphorylation	DDVAILTYVKENARS HHEEEEEEHHHHCCC	13.18	26074081
149	Ubiquitination	VAILTYVKENARSPS EEEEEEHHHHCCCCC	34.53	32015554
154	Phosphorylation	YVKENARSPSSVTGN EHHHHCCCCCCHHHH	27.07	22167270
156	Phosphorylation	KENARSPSSVTGNAL HHHCCCCCCHHHHHH	38.39	30266825
157	Phosphorylation	ENARSPSSVTGNALW HHCCCCCCHHHHHHH	27.38	30266825
159	Phosphorylation	ARSPSSVTGNALWKA CCCCCCHHHHHHHHH	27.02	30266825
169	Ubiquitination	ALWKAMEKSSLTQHS HHHHHHHHCCCCHHH	32.06	29967540
170	Phosphorylation	LWKAMEKSSLTQHSW HHHHHHHCCCCHHHH	19.78	20873877
171	Phosphorylation	WKAMEKSSLTQHSWQ HHHHHHCCCCHHHHH	46.64	26434776
173	Phosphorylation	AMEKSSLTQHSWQSL HHHHCCCCHHHHHHH	26.61	26434776
176	Phosphorylation	KSSLTQHSWQSLKDR HCCCCHHHHHHHHHH	19.59	30108239
179	Phosphorylation	LTQHSWQSLKDRYLK CCHHHHHHHHHHHHH	31.00	28464451
194	Ubiquitination	HLRGQEHKYLLGDAP HHCCCCCHHHCCCCC	36.52	21890473
194	Ubiquitination	HLRGQEHKYLLGDAP HHCCCCCHHHCCCCC	36.52	21906983
194	Ubiquitination	HLRGQEHKYLLGDAP HHCCCCCHHHCCCCC	36.52	21890473
194	Sumoylation	HLRGQEHKYLLGDAP HHCCCCCHHHCCCCC	36.52	28112733
195	Phosphorylation	LRGQEHKYLLGDAPV HCCCCCHHHCCCCCC	14.74	30266825
203	Phosphorylation	LLGDAPVSPSSQKLK HCCCCCCCCCHHHHH	20.29	19664994
205	Phosphorylation	GDAPVSPSSQKLKRK CCCCCCCCHHHHHHH	37.58	29255136
206	Phosphorylation	DAPVSPSSQKLKRKA CCCCCCCHHHHHHHH	34.42	22167270
208	Ubiquitination	PVSPSSQKLKRKAEE CCCCCHHHHHHHHHH	58.90	32015554
208	Acetylation	PVSPSSQKLKRKAEE CCCCCHHHHHHHHHH	58.90	25953088
208	Sumoylation	PVSPSSQKLKRKAEE CCCCCHHHHHHHHHH	58.90	28112733
212	Sumoylation	SSQKLKRKAEEDPEA CHHHHHHHHHHCHHH	59.57	28112733
222	Phosphorylation	EDPEAADSGEPQNKR HCHHHHHCCCCCCCC	40.09	21815630
228	Ubiquitination	DSGEPQNKRTPDLPE HCCCCCCCCCCCCCH	53.02	33845483
230	Phosphorylation	GEPQNKRTPDLPEEE CCCCCCCCCCCCHHH	23.82	25159151
238	Phosphorylation	PDLPEEEYVKEEIQE CCCCHHHHHHHHHHH	21.80	27642862
240	Sumoylation	LPEEEYVKEEIQENE CCHHHHHHHHHHHCH	49.04	28112733
240	Sumoylation	LPEEEYVKEEIQENE CCHHHHHHHHHHHCH	49.04	-
240	Ubiquitination	LPEEEYVKEEIQENE CCHHHHHHHHHHHCH	49.04	21906983
251	Ubiquitination	QENEEAVKKMLVEAT HHCHHHHHHHHHHHH	39.24	21906983
251	Acetylation	QENEEAVKKMLVEAT HHCHHHHHHHHHHHH	39.24	25953088
252	Ubiquitination	ENEEAVKKMLVEATR HCHHHHHHHHHHHHH	30.76	22817900
269	Phosphorylation	EEVVVDESPPDFEIH EEEECCCCCCCCEEE	36.95	28348404
278	Phosphorylation	PDFEIHITMCDDDPP CCCEEEEEECCCCCC	9.51	28348404
286	Phosphorylation	MCDDDPPTPEEDSET ECCCCCCCCCCCCCC	49.04	22817901
291	Phosphorylation	PPTPEEDSETQPDEE CCCCCCCCCCCCCHH	45.91	28348404
293	Phosphorylation	TPEEDSETQPDEEEE CCCCCCCCCCCHHHH	49.72	28348404
316	Ubiquitination	PEVGAAIKIIRQLME HHHHHHHHHHHHHHH	27.62	22817900
316	Ubiquitination	PEVGAAIKIIRQLME HHHHHHHHHHHHHHH	27.62	21890473
316	Ubiquitination	PEVGAAIKIIRQLME HHHHHHHHHHHHHHH	27.62	21890473
338	Ubiquitination	TVTQAFLKNSGELEA HHHHHHHHCCCCCEE	42.48	32015554
363	Phosphorylation	ADGYPIWSRQDDIDL CCCCCCCCCCCCCCC	22.30	24905233
372	Ubiquitination	QDDIDLQKDDEDTRE CCCCCCCCCCHHHHH	74.56	24816145
372	Sumoylation	QDDIDLQKDDEDTRE CCCCCCCCCCHHHHH	74.56	28112733
377	Phosphorylation	LQKDDEDTREALVKK CCCCCHHHHHHHHHH	28.50	25849741
383	Ubiquitination	DTREALVKKFGAQNV HHHHHHHHHHCHHHH	43.14	24816145
384	Ubiquitination	TREALVKKFGAQNVA HHHHHHHHHCHHHHH	41.36	29967540
384	Acetylation	TREALVKKFGAQNVA HHHHHHHHHCHHHHH	41.36	25953088

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
203	S	Phosphorylation	Kinase	CDK2	P24941	PSP
205	S	Phosphorylation	Kinase	P90RSK	Q15418	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TE2IP_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 TE2IP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAD50_HUMAN	RAD50	physical	15100233
XRCC5_HUMAN	XRCC5	physical	15100233
TERF2_HUMAN	TERF2	physical	15100233
PARP1_HUMAN	PARP1	physical	15100233
MRE11_HUMAN	MRE11A	physical	15100233
XRCC6_HUMAN	XRCC6	physical	15100233
TE2IP_HUMAN	TERF2IP	physical	10850490
TERF2_HUMAN	TERF2	physical	10850490
TERF2_HUMAN	TERF2	physical	21217703
RAD50_HUMAN	RAD50	physical	15383534
XRCC5_HUMAN	XRCC5	physical	15383534
MRE11_HUMAN	MRE11A	physical	15383534
HSP74_HUMAN	HSPA4	physical	15383534
TERF2_HUMAN	TERF2	physical	15383534
TINF2_HUMAN	TINF2	physical	15383534
POTE1_HUMAN	POT1	physical	15383534
RAD51_HUMAN	RAD51	physical	15316005
POTE1_HUMAN	POT1	physical	15316005
TERF2_HUMAN	TERF2	physical	15316005
ACD_HUMAN	ACD	physical	15316005
TERF1_HUMAN	TERF1	physical	15316005
TINF2_HUMAN	TINF2	physical	15316005
VGLL4_HUMAN	VGLL4	physical	21044950
CHM2B_HUMAN	CHMP2B	physical	21044950
ES8L1_HUMAN	EPS8L1	physical	21044950
MT3_HUMAN	MT3	physical	21044950
DPOD1_HUMAN	POLD1	physical	21044950
TBCA_HUMAN	TBCA	physical	21044950
ENAH_HUMAN	ENAH	physical	21044950
TSSC4_HUMAN	TSSC4	physical	21044950
SCLY_HUMAN	SCLY	physical	21044950
ARK73_HUMAN	AKR7A3	physical	21044950
F122A_HUMAN	FAM122A	physical	21044950
RBBP9_HUMAN	RBBP9	physical	21044950
GPKOW_HUMAN	GPKOW	physical	21044950
HDGR3_HUMAN	HDGFRP3	physical	21044950
PCNP_HUMAN	PCNP	physical	21044950
3MG_HUMAN	MPG	physical	21044950
CA174_HUMAN	C1orf174	physical	21044950
ZN414_HUMAN	ZNF414	physical	21044950
HMGB3_HUMAN	HMGB3	physical	21044950
WDR5_HUMAN	WDR5	physical	21044950
AK1BA_HUMAN	AKR1B10	physical	21044950
BABA1_HUMAN	BABAM1	physical	21044950
DNM3A_HUMAN	DNMT3A	physical	21044950
TLS1_HUMAN	C9orf78	physical	21044950
AIMP2_HUMAN	AIMP2	physical	21044950
S100P_HUMAN	S100P	physical	21044950
FABPI_HUMAN	FABP2	physical	21044950
PRP16_HUMAN	DHX38	physical	21044950
CPNE2_HUMAN	CPNE2	physical	21044950
XPO1_HUMAN	XPO1	physical	21044950
NUD18_HUMAN	NUDT18	physical	21044950
PML_HUMAN	PML	physical	21044950
EPAS1_HUMAN	EPAS1	physical	21044950
GAGE5_HUMAN	GAGE5	physical	21044950
RPP25_HUMAN	RPP25	physical	21044950
CALL3_HUMAN	CALML3	physical	21044950
AKT1_HUMAN	AKT1	physical	21044950
PRAX_HUMAN	PRX	physical	21044950
HNRPK_HUMAN	HNRNPK	physical	21044950
MSS4_HUMAN	RABIF	physical	21044950
PACN3_HUMAN	PACSIN3	physical	21044950
GLO2_HUMAN	HAGH	physical	21044950
I23O1_HUMAN	IDO1	physical	21044950
MRT4_HUMAN	MRTO4	physical	21044950
RGMA_HUMAN	RGMA	physical	21044950
COTL1_HUMAN	COTL1	physical	21044950
PEA15_HUMAN	PEA15	physical	21044950
MDHC_HUMAN	MDH1	physical	21044950
PRDX6_HUMAN	PRDX6	physical	21044950
SMRC2_HUMAN	SMARCC2	physical	21044950
CRBB1_HUMAN	CRYBB1	physical	21044950
MCM2_HUMAN	MCM2	physical	21044950
DDX23_HUMAN	DDX23	physical	21044950
PNMT_HUMAN	PNMT	physical	21044950
PA1B3_HUMAN	PAFAH1B3	physical	21044950
AK1A1_HUMAN	AKR1A1	physical	21044950
NUD14_HUMAN	NUDT14	physical	21044950
ARP21_HUMAN	ARPP21	physical	21044950
H11_HUMAN	HIST1H1A	physical	21044950
OGFR_HUMAN	OGFR	physical	21044950
BCL7B_HUMAN	BCL7B	physical	21044950
NASP_HUMAN	NASP	physical	21044950
XRCC6_HUMAN	XRCC6	physical	21044950
HMGB1_HUMAN	HMGB1	physical	21044950
NAIF1_HUMAN	NAIF1	physical	21044950
CTBP1_HUMAN	CTBP1	physical	21044950
TERF2_HUMAN	TERF2	physical	21044950
LANC2_HUMAN	LANCL2	physical	21044950
MGN2_HUMAN	MAGOHB	physical	21044950
BANP_HUMAN	BANP	physical	21044950
TOIP1_HUMAN	TOR1AIP1	physical	21044950
XAGE2_HUMAN	XAGE2	physical	21044950
CRK_HUMAN	CRK	physical	21044950
UCHL1_HUMAN	UCHL1	physical	21044950
TWF2_HUMAN	TWF2	physical	21044950
ADA_HUMAN	ADA	physical	21044950
PP6R3_HUMAN	PPP6R3	physical	21044950
IL1RA_HUMAN	IL1RN	physical	21044950
RPAP1_HUMAN	RPAP1	physical	21044950
SCRN2_HUMAN	SCRN2	physical	21044950
IPP2_HUMAN	PPP1R2	physical	21044950
WIPI2_HUMAN	WIPI2	physical	21044950
3HAO_HUMAN	HAAO	physical	21044950
SET_HUMAN	SET	physical	21044950
PTMA_HUMAN	PTMA	physical	21044950
PACN2_HUMAN	PACSIN2	physical	21044950
TALDO_HUMAN	TALDO1	physical	21044950
APEX1_HUMAN	APEX1	physical	21044950
DDX24_HUMAN	DDX24	physical	21044950
6PGL_HUMAN	PGLS	physical	21044950
GAMT_HUMAN	GAMT	physical	21044950
OCM2_HUMAN	OCM2	physical	21044950
PPM1G_HUMAN	PPM1G	physical	21044950
HMGN4_HUMAN	HMGN4	physical	21044950
SYUG_HUMAN	SNCG	physical	21044950
TB10A_HUMAN	TBC1D10A	physical	21044950
SP100_HUMAN	SP100	physical	21044950
NUMA1_HUMAN	NUMA1	physical	21044950
TYB4Y_HUMAN	TMSB4Y	physical	21044950
MT1X_HUMAN	MT1X	physical	21044950
KAD1_HUMAN	AK1	physical	21044950
HMGN3_HUMAN	HMGN3	physical	21044950
DX39A_HUMAN	DDX39A	physical	21044950
PCP4_HUMAN	PCP4	physical	21044950
LEGL_HUMAN	LGALSL	physical	21044950
CRBS_HUMAN	CRYGS	physical	21044950
RECQ4_HUMAN	RECQL4	physical	21044950
DPP3_HUMAN	DPP3	physical	21044950
ANXA5_HUMAN	ANXA5	physical	21044950
DBNL_HUMAN	DBNL	physical	21044950
PGM1_HUMAN	PGM1	physical	21044950
NOL3_HUMAN	NOL3	physical	21044950
AXA81_HUMAN	ANXA8L1	physical	21044950
TYB10_HUMAN	TMSB10	physical	21044950
SBDS_HUMAN	SBDS	physical	21044950
NXNL1_HUMAN	NXNL1	physical	21044950
CPNE3_HUMAN	CPNE3	physical	21044950
GNMT_HUMAN	GNMT	physical	21044950
TERF2_HUMAN	TERF2	physical	19164295
TERF2_HUMAN	TERF2	physical	22939629
PANK4_HUMAN	PANK4	physical	22863883
2A5E_HUMAN	PPP2R5E	physical	22863883
TERF2_HUMAN	TERF2	physical	23307557
VKGC_HUMAN	GGCX	physical	26496610
PP1RA_HUMAN	PPP1R10	physical	26496610
TERF2_HUMAN	TERF2	physical	26496610
MOT4_HUMAN	SLC16A3	physical	26496610
WDFY3_HUMAN	WDFY3	physical	26496610
POTE1_HUMAN	POT1	physical	26496610
TINF2_HUMAN	TINF2	physical	26496610
P33MX_HUMAN	KIAA1191	physical	26496610
DCR1B_HUMAN	DCLRE1B	physical	26496610
ACD_HUMAN	ACD	physical	26496610
TERF2_HUMAN	TERF2	physical	28082411

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 TE2IP_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-203 AND SER-205, 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-154 AND SER-203, ANDMASS SPECTROMETRY.	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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-203 AND SER-205, 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 SER-36; SER-154 AND SER-203,AND MASS SPECTROMETRY.	18669648 [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-203, AND MASSSPECTROMETRY.	18187866 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-206, ANDMASS SPECTROMETRY.	17525332 [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-203, AND MASSSPECTROMETRY.	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-154; SER-156 ANDSER-203, AND MASS SPECTROMETRY.	16964243 [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-154, AND MASSSPECTROMETRY.	15302935 [Abstract]