dbPTM

IF2B1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IF2B1_HUMAN
UniProt AC	Q9NZI8
Protein Name	Insulin-like growth factor 2 mRNA-binding protein 1
Gene Name	IGF2BP1
Organism	Homo sapiens (Human).
Sequence Length	577
Subcellular Localization	Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Cell projection, lamellipodium. Cell projection, dendrite. Cell projection, dendritic spine. Cell projection, growth cone. Cell projection, filopodium. Cell projection, axon. In the nucleus, located
Protein Description	RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to and stabilizes ABCB1/MDR-1 mRNA (By similarity). During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing (By similarity). Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence prevents MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD. Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to the oncofetal H19 transcript and to the neuron-specific TAU mRNA and regulates their localizations. Binds to and stabilizes BTRC/FBW1A mRNA. Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2. Promotes the directed movement of tumor-derived cells by fine-tuning intracellular signaling networks. Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN transcript open reading frame (ORF) and prevents mRNA decay. This combined action on MAPK4 (down-regulation) and PTEN (up-regulation) antagonizes HSPB1 phosphorylation, consequently it prevents G-actin sequestration by phosphorylated HSPB1, allowing F-actin polymerization. Hence enhances the velocity of cell migration and stimulates directed cell migration by PTEN-modulated polarization. Interacts with Hepatitis C virus (HCV) 5'-UTR and 3'-UTR and specifically enhances translation at the HCV IRES, but not 5'-cap-dependent translation, possibly by recruiting eIF3. Interacts with HIV-1 GAG protein and blocks the formation of infectious HIV-1 particles. Reduces HIV-1 assembly by inhibiting viral RNA packaging, as well as assembly and processing of GAG protein on cellular membranes. During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts..
Protein Sequence	MNKLYIGNLNESVTPADLEKVFAEHKISYSGQFLVKSGYAFVDCPDEHWAMKAIETFSGKVELQGKRLEIEHSVPKKQRSRKIQIRNIPPQLRWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYSNREQTRQAIMKLNGHQLENHALKVSYIPDEQIAQGPENGRRGGFGSRGQPRQGSPVAAGAPAKQQQVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKAISVHSTPEGCSSACKMILEIMHKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTLYNPERTITVKGAIENCCRAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSSAVPPPPSSVTGAAPYSSFMQAPEQEMVQVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVIITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENDQVIVKIIGHFYASQMAQRKIRDILAQVKQQHQKGQSNQAQARRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Ubiquitination	-----MNKLYIGNLN -----CCCEEECCCC	41.17	21890473
3	Ubiquitination	-----MNKLYIGNLN -----CCCEEECCCC	41.17	21890473
5	Phosphorylation	---MNKLYIGNLNES ---CCCEEECCCCCC	14.37	23186163
12	Phosphorylation	YIGNLNESVTPADLE EECCCCCCCCHHHHH	30.16	25159151
14	Phosphorylation	GNLNESVTPADLEKV CCCCCCCCHHHHHHH	23.26	23186163
20	Ubiquitination	VTPADLEKVFAEHKI CCHHHHHHHHHHCCC	50.37	21890473
20	Acetylation	VTPADLEKVFAEHKI CCHHHHHHHHHHCCC	50.37	26051181
20	Ubiquitination	VTPADLEKVFAEHKI CCHHHHHHHHHHCCC	50.37	22817900
26	Ubiquitination	EKVFAEHKISYSGQF HHHHHHCCCEECCEE	25.50	21890473
26	Ubiquitination	EKVFAEHKISYSGQF HHHHHHCCCEECCEE	25.50	22817900
30	Phosphorylation	AEHKISYSGQFLVKS HHCCCEECCEEEEEE	21.23	28555341
36	Ubiquitination	YSGQFLVKSGYAFVD ECCEEEEEECEEEEE	40.07	16196087
39	Phosphorylation	QFLVKSGYAFVDCPD EEEEEECEEEEECCC	12.17	20090780
44	Glutathionylation	SGYAFVDCPDEHWAM ECEEEEECCCHHHHH	3.73	22555962
52	Acetylation	PDEHWAMKAIETFSG CCHHHHHHHHHHCCC	38.17	26051181
52	Ubiquitination	PDEHWAMKAIETFSG CCHHHHHHHHHHCCC	38.17	32015554
60	Ubiquitination	AIETFSGKVELQGKR HHHHCCCEEEECCEE	31.19	32015554
66	Acetylation	GKVELQGKRLEIEHS CEEEECCEEEEEEEC	40.63	25953088
66	Ubiquitination	GKVELQGKRLEIEHS CEEEECCEEEEEEEC	40.63	29967540
73	Phosphorylation	KRLEIEHSVPKKQRS EEEEEEECCCCCCCC	27.59	25159151
76	Ubiquitination	EIEHSVPKKQRSRKI EEEECCCCCCCCCCC	60.42	29967540
77	Ubiquitination	IEHSVPKKQRSRKIQ EEECCCCCCCCCCCC	44.89	24816145
126	Ubiquitination	TAVVNVTYSNREQTR EEEEEEEECCHHHHH	10.32	21890473
138	Ubiquitination	QTRQAIMKLNGHQLE HHHHHHHHHCCHHHC	32.46	21890473
141	Ubiquitination	QAIMKLNGHQLENHA HHHHHHCCHHHCCCE	21.98	32142685
150	Ubiquitination	QLENHALKVSYIPDE HHCCCEEEEEECCHH	29.89	29967540
152	Phosphorylation	ENHALKVSYIPDEQI CCCEEEEEECCHHHH	18.76	26074081
153	Phosphorylation	NHALKVSYIPDEQIA CCEEEEEECCHHHHC	21.33	26074081
162	Ubiquitination	PDEQIAQGPENGRRG CHHHHCCCCCCCCCC	23.59	33845483
168	Methylation	QGPENGRRGGFGSRG CCCCCCCCCCCCCCC	51.49	115480207
173	Phosphorylation	GRRGGFGSRGQPRQG CCCCCCCCCCCCCCC	30.86	26074081
174	Methylation	RRGGFGSRGQPRQGS CCCCCCCCCCCCCCC	48.41	115480187
178	Ubiquitination	FGSRGQPRQGSPVAA CCCCCCCCCCCCCCC	45.67	23503661
181	Phosphorylation	RGQPRQGSPVAAGAP CCCCCCCCCCCCCCC	14.09	29255136
190	Neddylation	VAAGAPAKQQQVDIP CCCCCCCHHCCCCCC	47.80	32015554
190	Ubiquitination	VAAGAPAKQQQVDIP CCCCCCCHHCCCCCC	47.80	33845483
191	Ubiquitination	AAGAPAKQQQVDIPL CCCCCCHHCCCCCCH	40.83	32015554
201	Ubiquitination	VDIPLRLLVPTQYVG CCCCHHHCEECHHHH	3.33	22053931
207	Ubiquitination	LLVPTQYVGAIIGKE HCEECHHHHHHHCCC	2.76	24816145
211	Ubiquitination	TQYVGAIIGKEGATI CHHHHHHHCCCCCCH	6.81	22053931
213	Ubiquitination	YVGAIIGKEGATIRN HHHHHHCCCCCCHHH	42.43	21906983
216	Ubiquitination	AIIGKEGATIRNITK HHHCCCCCCHHHHCH	10.84	22817900
223	Neddylation	ATIRNITKQTQSKID CCHHHHCHHHHCCEE	47.77	32015554
223	Ubiquitination	ATIRNITKQTQSKID CCHHHHCHHHHCCEE	47.77	21906983
225	Phosphorylation	IRNITKQTQSKIDVH HHHHCHHHHCCEECC	36.04	20860994
228	Ubiquitination	ITKQTQSKIDVHRKE HCHHHHCCEECCHHH	32.86	22817900
234	Ubiquitination	SKIDVHRKENAGAAE CCEECCHHHCCCHHH	40.20	-
242	Acetylation	ENAGAAEKAISVHST HCCCHHHHCEECCCC	46.42	26051181
242	Ubiquitination	ENAGAAEKAISVHST HCCCHHHHCEECCCC	46.42	32015554
245	Phosphorylation	GAAEKAISVHSTPEG CHHHHCEECCCCCCC	20.73	26434776
246	Ubiquitination	AAEKAISVHSTPEGC HHHHCEECCCCCCCH	3.19	16196087
248	Phosphorylation	EKAISVHSTPEGCSS HHCEECCCCCCCHHH	43.43	25159151
249	Phosphorylation	KAISVHSTPEGCSSA HCEECCCCCCCHHHH	15.52	20873877
254	Phosphorylation	HSTPEGCSSACKMIL CCCCCCHHHHHHHHH	31.65	23312004
255	Phosphorylation	STPEGCSSACKMILE CCCCCHHHHHHHHHH	41.59	23312004
257	Glutathionylation	PEGCSSACKMILEIM CCCHHHHHHHHHHHH	3.12	22555962
258	Acetylation	EGCSSACKMILEIMH CCHHHHHHHHHHHHH	28.79	26051181
258	Ubiquitination	EGCSSACKMILEIMH CCHHHHHHHHHHHHH	28.79	16196087
266	Acetylation	MILEIMHKEAKDTKT HHHHHHHHHHCCCCC	41.82	25953088
272	Acetylation	HKEAKDTKTADEVPL HHHHCCCCCCCCCCC	52.42	26051181
272	Ubiquitination	HKEAKDTKTADEVPL HHHHCCCCCCCCCCC	52.42	33845483
273	Phosphorylation	KEAKDTKTADEVPLK HHHCCCCCCCCCCCC	41.24	21406692
280	Ubiquitination	TADEVPLKILAHNNF CCCCCCCCHHHCCCH	29.60	32015554
290	Ubiquitination	AHNNFVGRLIGKEGR HCCCHHHHHHCCCCC	20.17	29967540
294	Ubiquitination	FVGRLIGKEGRNLKK HHHHHHCCCCCCCCE	50.42	-
300	Acetylation	GKEGRNLKKVEQDTE CCCCCCCCEEECCCC	59.32	18586849
300	Ubiquitination	GKEGRNLKKVEQDTE CCCCCCCCEEECCCC	59.32	-
301	Ubiquitination	KEGRNLKKVEQDTET CCCCCCCEEECCCCC	54.92	21890473
301	Acetylation	KEGRNLKKVEQDTET CCCCCCCEEECCCCC	54.92	18586859
301	Ubiquitination	KEGRNLKKVEQDTET CCCCCCCEEECCCCC	54.92	22817900
306	Phosphorylation	LKKVEQDTETKITIS CCEEECCCCCCEEEE	45.29	25367160
309	Acetylation	VEQDTETKITISSLQ EECCCCCCEEEEECC	31.46	18586869
311	Ubiquitination	QDTETKITISSLQDL CCCCCCEEEEECCCC	19.16	21890473
311	Phosphorylation	QDTETKITISSLQDL CCCCCCEEEEECCCC	19.16	23403867
311	Ubiquitination	QDTETKITISSLQDL CCCCCCEEEEECCCC	19.16	20639865
313	Phosphorylation	TETKITISSLQDLTL CCCCEEEEECCCCCC	19.15	23403867
314	Phosphorylation	ETKITISSLQDLTLY CCCEEEEECCCCCCC	26.63	28464451
319	Phosphorylation	ISSLQDLTLYNPERT EEECCCCCCCCCCCE	35.17	23403867
321	Phosphorylation	SLQDLTLYNPERTIT ECCCCCCCCCCCEEE	24.36	23403867
326	Phosphorylation	TLYNPERTITVKGAI CCCCCCCEEEEHHHH	21.24	29209046
326	Ubiquitination	TLYNPERTITVKGAI CCCCCCCEEEEHHHH	21.24	22817900
328	Phosphorylation	YNPERTITVKGAIEN CCCCCEEEEHHHHHH	18.62	29209046
330	Ubiquitination	PERTITVKGAIENCC CCCEEEEHHHHHHHH	33.69	33845483
334	Ubiquitination	ITVKGAIENCCRAEQ EEEHHHHHHHHHHHH	43.62	22817900
336	Ubiquitination	VKGAIENCCRAEQEI EHHHHHHHHHHHHHH	0.78	21890473
336	Neddylation	VKGAIENCCRAEQEI EHHHHHHHHHHHHHH	0.78	32015554
336	Ubiquitination	VKGAIENCCRAEQEI EHHHHHHHHHHHHHH	0.78	33845483
344	Ubiquitination	CRAEQEIMKKVREAY HHHHHHHHHHHHHHH	3.19	32015554
346	Ubiquitination	AEQEIMKKVREAYEN HHHHHHHHHHHHHHC	29.19	24816145
366	Ubiquitination	SLQSHLIPGLNLAAV HHHHCCCCCCCEEEE	47.80	33845483
369	Ubiquitination	SHLIPGLNLAAVGLF HCCCCCCCEEEEEEC	33.28	32015554
399	Ubiquitination	GAAPYSSFMQAPEQE CCCCCCHHCCCCHHH	3.28	16196087
422	Ubiquitination	QAVGAIIGKKGQHIK HHHHHHHCCCCHHHH	21.36	32015554
427	Ubiquitination	IIGKKGQHIKQLSRF HHCCCCHHHHHHHHH	37.57	29967540
428	Ubiquitination	IGKKGQHIKQLSRFA HCCCCHHHHHHHHHH	2.03	21890473
429	Ubiquitination	GKKGQHIKQLSRFAS CCCCHHHHHHHHHHH	42.96	29967540
432	Phosphorylation	GQHIKQLSRFASASI CHHHHHHHHHHHCCE	23.90	-
436	Phosphorylation	KQLSRFASASIKIAP HHHHHHHHCCEEECC	21.60	28464451
438	Phosphorylation	LSRFASASIKIAPPE HHHHHHCCEEECCCC	23.17	28450419
438	Ubiquitination	LSRFASASIKIAPPE HHHHHHCCEEECCCC	23.17	20639865
439	Ubiquitination	SRFASASIKIAPPET HHHHHCCEEECCCCC	3.60	21890473
440	Ubiquitination	RFASASIKIAPPETP HHHHCCEEECCCCCC	30.25	22817900
446	Phosphorylation	IKIAPPETPDSKVRM EEECCCCCCCCCEEE	37.86	25159151
448	Ubiquitination	IAPPETPDSKVRMVI ECCCCCCCCCEEEEE	69.39	20639865
449	Phosphorylation	APPETPDSKVRMVII CCCCCCCCCEEEEEE	33.96	23403867
449	Ubiquitination	APPETPDSKVRMVII CCCCCCCCCEEEEEE	33.96	20639865
450	Ubiquitination	PPETPDSKVRMVIIT CCCCCCCCEEEEEEE	41.04	20639865
453	Ubiquitination	TPDSKVRMVIITGPP CCCCCEEEEEEECCC	2.58	21890473
461	Ubiquitination	VIITGPPEAQFKAQG EEEECCCHHHHHHHC	59.23	22817900
463	Ubiquitination	ITGPPEAQFKAQGRI EECCCHHHHHHHCCE	38.42	21890473
464	Ubiquitination	TGPPEAQFKAQGRIY ECCCHHHHHHHCCEE	10.24	21890473
465	Methylation	GPPEAQFKAQGRIYG CCCHHHHHHHCCEEE	27.93	24712003
465	Ubiquitination	GPPEAQFKAQGRIYG CCCHHHHHHHCCEEE	27.93	22817900
471	Ubiquitination	FKAQGRIYGKLKEEN HHHHCCEEEECCCCC	13.57	22817900
472	Ubiquitination	KAQGRIYGKLKEENF HHHCCEEEECCCCCC	26.84	22817900
473	Acetylation	AQGRIYGKLKEENFF HHCCEEEECCCCCCC	39.14	25953088
473	Ubiquitination	AQGRIYGKLKEENFF HHCCEEEECCCCCCC	39.14	21890473
474	Ubiquitination	QGRIYGKLKEENFFG HCCEEEECCCCCCCC	7.98	21890473
475	Sumoylation	GRIYGKLKEENFFGP CCEEEECCCCCCCCC	67.48	-
475	Neddylation	GRIYGKLKEENFFGP CCEEEECCCCCCCCC	67.48	32015554
475	Sumoylation	GRIYGKLKEENFFGP CCEEEECCCCCCCCC	67.48	-
475	Ubiquitination	GRIYGKLKEENFFGP CCEEEECCCCCCCCC	67.48	21906983
483	Ubiquitination	EENFFGPKEEVKLET CCCCCCCHHHEEEEE	67.87	32015554
490	Phosphorylation	KEEVKLETHIRVPAS HHHEEEEEEEECCHH	32.79	20860994
493	Methylation	VKLETHIRVPASAAG EEEEEEEECCHHHHC	22.29	115480197
493	Ubiquitination	VKLETHIRVPASAAG EEEEEEEECCHHHHC	22.29	23503661
496	Ubiquitination	ETHIRVPASAAGRVI EEEEECCHHHHCCEE	14.67	24816145
497	Phosphorylation	THIRVPASAAGRVIG EEEECCHHHHCCEEC	16.75	-
503	Ubiquitination	ASAAGRVIGKGGKTV HHHHCCEECCCCCCH	4.55	23503661
504	Ubiquitination	SAAGRVIGKGGKTVN HHHCCEECCCCCCHH	21.50	23503661
505	Ubiquitination	AAGRVIGKGGKTVNE HHCCEECCCCCCHHH	54.06	33845483
506	Ubiquitination	AGRVIGKGGKTVNEL HCCEECCCCCCHHHH	37.30	24816145
507	Ubiquitination	GRVIGKGGKTVNELQ CCEECCCCCCHHHHH	26.41	24816145
508	Ubiquitination	RVIGKGGKTVNELQN CEECCCCCCHHHHHH	58.95	32015554
517	Phosphorylation	VNELQNLTAAEVVVP HHHHHHCCCCEEEEC	31.22	-
526	Ubiquitination	AEVVVPRDQTPDEND CEEEECCCCCCCCCC	51.11	16196087
528	Phosphorylation	VVVPRDQTPDENDQV EEECCCCCCCCCCCE	36.68	25159151
536	Ubiquitination	PDENDQVIVKIIGHF CCCCCCEEHHHHHHH	1.86	16196087
537	Ubiquitination	DENDQVIVKIIGHFY CCCCCEEHHHHHHHH	3.70	16196087
538	Ubiquitination	ENDQVIVKIIGHFYA CCCCEEHHHHHHHHH	19.92	16196087
544	Phosphorylation	VKIIGHFYASQMAQR HHHHHHHHHHHHHHH	10.32	29496907
546	Phosphorylation	IIGHFYASQMAQRKI HHHHHHHHHHHHHHH	14.76	-
561	Ubiquitination	RDILAQVKQQHQKGQ HHHHHHHHHHHHHHH	31.96	33845483
566	Ubiquitination	QVKQQHQKGQSNQAQ HHHHHHHHHHCHHHH	57.71	29967540

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
Oops, there are no upstream regulatory protein records of IF2B1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IF2B1_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 IF2B1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FBW1A_HUMAN	BTRC	physical	16778892
STAU1_HUMAN	STAU1	physical	23125841
IF2B2_HUMAN	IGF2BP2	physical	26344197
IF2B3_HUMAN	IGF2BP3	physical	26344197
RAB2A_HUMAN	RAB2A	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
BIRC2_HUMAN	BIRC2	physical	24704827
MKRN1_HUMAN	MKRN1	physical	26265008
ELAV1_HUMAN	ELAVL1	physical	26265008

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 IF2B1_HUMAN

Related Literatures of Post-Translational Modification

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-181, 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-181 AND THR-446, ANDMASS 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-181, AND MASSSPECTROMETRY.	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-181, AND MASSSPECTROMETRY.	18691976 [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-181, AND MASSSPECTROMETRY.	19007248 [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-181, AND MASSSPECTROMETRY.	17287340 [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-181, AND MASSSPECTROMETRY.	17924679 [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-181, 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-181, AND MASSSPECTROMETRY.	17081983 [Abstract]