dbPTM

KS6A3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KS6A3_HUMAN
UniProt AC	P51812
Protein Name	Ribosomal protein S6 kinase alpha-3
Gene Name	RPS6KA3
Organism	Homo sapiens (Human).
Sequence Length	740
Subcellular Localization	Nucleus. Cytoplasm.
Protein Description	Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3. Negatively regulates EGF-induced MAPK1/3 phosphorylation via phosphorylation of SOS1. Phosphorylates SOS1 at 'Ser-1134' and 'Ser-1161' that create YWHAB and YWHAE binding sites and which contribute to the negative regulation of MAPK1/3 phosphorylation (By similarity). Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration. [PubMed: 26158630]
Protein Sequence	MPLAQLADPWQKMAVESPSDSAENGQQIMDEPMGEEEINPQTEEVSIKEIAITHHVKEGHEKADPSQFELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRLGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQLFRGFSFVAITSDDESQAMQTVGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTLAQRRGIKKITSTAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
17	Phosphorylation	WQKMAVESPSDSAEN HHHHCCCCCCCCHHH	24.09	25159151
19	Phosphorylation	KMAVESPSDSAENGQ HHCCCCCCCCHHHCC	54.18	25159151
21	Phosphorylation	AVESPSDSAENGQQI CCCCCCCCHHHCCCC	41.65	30576142
57	Ubiquitination	IAITHHVKEGHEKAD HHHHHHHHCCCCCCC	54.33	-
62	Acetylation	HVKEGHEKADPSQFE HHHCCCCCCCHHHHH	53.03	25953088
62	Ubiquitination	HVKEGHEKADPSQFE HHHCCCCCCCHHHHH	53.03	-
66	Phosphorylation	GHEKADPSQFELLKV CCCCCCHHHHHHHHH	48.31	20068231
72	Ubiquitination	PSQFELLKVLGQGSF HHHHHHHHHHCCCCC	48.30	21890473
78	Phosphorylation	LKVLGQGSFGKVFLV HHHHCCCCCCEEEEE	23.96	20068231
81	Ubiquitination	LGQGSFGKVFLVKKI HCCCCCCEEEEEEEC	28.01	21890473
81	Acetylation	LGQGSFGKVFLVKKI HCCCCCCEEEEEEEC	28.01	89713
100	Acetylation	ARQLYAMKVLKKATL HHHHHHHHHHHHHCH	35.92	7987735
103	Acetylation	LYAMKVLKKATLKVR HHHHHHHHHHCHHHH	43.26	7987747
144	Phosphorylation	FQTEGKLYLILDFLR EECCCEEEEEEHHHH	8.65	-
160	Phosphorylation	GDLFTRLSKEVMFTE CCHHHHHCCCCCCCH	24.39	12618428
164	Sulfoxidation	TRLSKEVMFTEEDVK HHHCCCCCCCHHHHH	3.45	21406390
166	Phosphorylation	LSKEVMFTEEDVKFY HCCCCCCCHHHHHHH	21.99	22210691
195	Ubiquitination	GIIYRDLKPENILLD CCEECCCCHHHEEEC	55.35	-
210	Phosphorylation	EEGHIKLTDFGLSKE CCCCEEECCCCCCHH	25.04	21082442
215	Phosphorylation	KLTDFGLSKESIDHE EECCCCCCHHHCCCC	34.45	28857561
216	Ubiquitination	LTDFGLSKESIDHEK ECCCCCCHHHCCCCH	61.60	-
218	Phosphorylation	DFGLSKESIDHEKKA CCCCCHHHCCCCHHH	36.73	28857561
226	Phosphorylation	IDHEKKAYSFCGTVE CCCCHHHHHCCCCHH	15.91	22322096
227	Phosphorylation	DHEKKAYSFCGTVEY CCCHHHHHCCCCHHH	20.94	22322096
231	Phosphorylation	KAYSFCGTVEYMAPE HHHHCCCCHHHHCHH	16.02	22322096
234	Phosphorylation	SFCGTVEYMAPEVVN HCCCCHHHHCHHHHC	8.34	23927012
274	Ubiquitination	PFQGKDRKETMTMIL CCCCCCHHHHHHHHH	68.61	-
276	Phosphorylation	QGKDRKETMTMILKA CCCCHHHHHHHHHHH	22.45	23612710
278	Phosphorylation	KDRKETMTMILKAKL CCHHHHHHHHHHHHH	14.42	29457462
297	Phosphorylation	FLSPEAQSLLRMLFK CCCHHHHHHHHHHHH	36.10	24719451
322	Ubiquitination	PDGVEEIKRHSFFST CCCHHHHHHHCCCCC	47.54	-
325	Phosphorylation	VEEIKRHSFFSTIDW HHHHHHHCCCCCCCH	31.83	20873877
328	Phosphorylation	IKRHSFFSTIDWNKL HHHHCCCCCCCHHHH	23.57	29083192
329	Phosphorylation	KRHSFFSTIDWNKLY HHHCCCCCCCHHHHH	20.14	20873877
336	Phosphorylation	TIDWNKLYRREIHPP CCCHHHHHHCCCCCC	14.83	29083192
345	Ubiquitination	REIHPPFKPATGRPE CCCCCCCCCCCCCCC	39.24	-
348	Phosphorylation	HPPFKPATGRPEDTF CCCCCCCCCCCCCCE	42.10	28555341
354	Phosphorylation	ATGRPEDTFYFDPEF CCCCCCCCEECCHHH	20.69	19060867
356	Phosphorylation	GRPEDTFYFDPEFTA CCCCCCEECCHHHCC	14.79	26074081
362	Phosphorylation	FYFDPEFTAKTPKDS EECCHHHCCCCCCCC	26.11	30576142
364	Acetylation	FDPEFTAKTPKDSPG CCHHHCCCCCCCCCC	63.40	20167786
364	Ubiquitination	FDPEFTAKTPKDSPG CCHHHCCCCCCCCCC	63.40	-
365	Phosphorylation	DPEFTAKTPKDSPGI CHHHCCCCCCCCCCC	32.86	22167270
369	Phosphorylation	TAKTPKDSPGIPPSA CCCCCCCCCCCCCCC	31.02	29255136
375	Phosphorylation	DSPGIPPSANAHQLF CCCCCCCCCCHHHHH	28.88	29255136
386	Phosphorylation	HQLFRGFSFVAITSD HHHHCCCEEEEEECC	22.95	18156174
391	Phosphorylation	GFSFVAITSDDESQA CCEEEEEECCCHHHH	19.16	22199227
392	Phosphorylation	FSFVAITSDDESQAM CEEEEEECCCHHHHH	36.63	22199227
396	Phosphorylation	AITSDDESQAMQTVG EEECCCHHHHHHHHC	30.18	22199227
406	Phosphorylation	MQTVGVHSIVQQLHR HHHHCHHHHHHHHHH	23.27	27080861
415	Phosphorylation	VQQLHRNSIQFTDGY HHHHHHCCCCCCCCC	20.09	29255136
419	Phosphorylation	HRNSIQFTDGYEVKE HHCCCCCCCCCEECC	16.49	29691806
422	Phosphorylation	SIQFTDGYEVKEDIG CCCCCCCCEECCCCC	21.99	23927012
433	Phosphorylation	EDIGVGSYSVCKRCI CCCCCCCHHHHHHHH	10.13	-
437	Ubiquitination	VGSYSVCKRCIHKAT CCCHHHHHHHHHHHH	48.42	-
470	Phosphorylation	EIEILLRYGQHPNII HHHHHHHHCCCCCEE	22.55	18156174
478	Phosphorylation	GQHPNIITLKDVYDD CCCCCEEEEEEECCC	24.77	20071362
480	Ubiquitination	HPNIITLKDVYDDGK CCCEEEEEEECCCCC	36.18	-
483	Phosphorylation	IITLKDVYDDGKYVY EEEEEEECCCCCEEE	20.60	18156174
488	Phosphorylation	DVYDDGKYVYVVTEL EECCCCCEEEEEEEC	11.53	18156174
493	Phosphorylation	GKYVYVVTELMKGGE CCEEEEEEECHHCCH	17.23	22817900
504	Ubiquitination	KGGELLDKILRQKFF HCCHHHHHHHHHHCC	43.54	-
509	Ubiquitination	LDKILRQKFFSEREA HHHHHHHHCCCHHHH	41.78	-
517	Phosphorylation	FFSEREASAVLFTIT CCCHHHHHHHEEEHH	17.73	-
529	Phosphorylation	TITKTVEYLHAQGVV EHHHHHHHHHHCCCC	10.23	18156174
541	Ubiquitination	GVVHRDLKPSNILYV CCCCCCCCHHHEEEE	51.17	-
541	Acetylation	GVVHRDLKPSNILYV CCCCCCCCHHHEEEE	51.17	26051181
556	Phosphorylation	DESGNPESIRICDFG CCCCCCCCEEECCHH	20.58	17192257
556	O-linked_Glycosylation	DESGNPESIRICDFG CCCCCCCCEEECCHH	20.58	29351928
566	Acetylation	ICDFGFAKQLRAENG ECCHHHHHHHHHHCC	47.83	25953088
566	Ubiquitination	ICDFGFAKQLRAENG ECCHHHHHHHHHHCC	47.83	-
577	Phosphorylation	AENGLLMTPCYTANF HHCCCEECCCEECCC	15.35	21945579
580	Phosphorylation	GLLMTPCYTANFVAP CCEECCCEECCCCCH	15.30	21945579
581	Phosphorylation	LLMTPCYTANFVAPE CEECCCEECCCCCHH	23.11	21945579
591	Ubiquitination	FVAPEVLKRQGYDAA CCCHHHHHHCCCCHH	48.10	-
591	Acetylation	FVAPEVLKRQGYDAA CCCHHHHHHCCCCHH	48.10	25953088
625	Phosphorylation	FANGPDDTPEEILAR CCCCCCCCHHHHHHH	39.72	-
641	Phosphorylation	GSGKFSLSGGYWNSV CCCCEEECCCCCCCH	29.04	21082442
644	Phosphorylation	KFSLSGGYWNSVSDT CEEECCCCCCCHHHH	12.63	18156174
651	Phosphorylation	YWNSVSDTAKDLVSK CCCCHHHHHHHHHHH	28.27	30576142
658	Ubiquitination	TAKDLVSKMLHVDPH HHHHHHHHHCCCCHH	37.69	-
688	Phosphorylation	HWDQLPQYQLNRQDA CHHHCCHHCCCCCCC	17.02	27642862
706	Phosphorylation	VKGAMAATYSALNRN HHHHHHHHHHHHHCC	14.42	21945579
707	Phosphorylation	KGAMAATYSALNRNQ HHHHHHHHHHHHCCC	6.29	21945579
708	Phosphorylation	GAMAATYSALNRNQS HHHHHHHHHHHCCCC	23.17	21945579
715	Phosphorylation	SALNRNQSPVLEPVG HHHHCCCCCCCCCCC	22.11	19664994
723	Methylation	PVLEPVGRSTLAQRR CCCCCCCHHHHHHHH	27.05	97804695
724	Phosphorylation	VLEPVGRSTLAQRRG CCCCCCHHHHHHHHC	23.11	28555341
725	Phosphorylation	LEPVGRSTLAQRRGI CCCCCHHHHHHHHCC	25.42	28555341
736	Phosphorylation	RRGIKKITSTAL--- HHCCCHHHHCCC---	28.98	29978859
737	Phosphorylation	RGIKKITSTAL---- HCCCHHHHCCC----	18.37	30576142
737	O-linked_Glycosylation	RGIKKITSTAL---- HCCCHHHHCCC----	18.37	29351928
738	Phosphorylation	GIKKITSTAL----- CCCHHHHCCC-----	24.27	30576142

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
227	S	Phosphorylation	Kinase	PDPK1	O15530	Uniprot
386	S	Phosphorylation	Kinase	MAPKAPK2	P49137	Uniprot
386	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
470	Y	Phosphorylation	Kinase	SRC	P12931	PSP
470	Y	Phosphorylation	Kinase	FYN	P06241	PSP
483	Y	Phosphorylation	Kinase	FYN	P06241	PSP
483	Y	Phosphorylation	Kinase	SRC	P12931	PSP
488	Y	Phosphorylation	Kinase	MAPK1	P28482	GPS
488	Y	Phosphorylation	Kinase	FGFR_GROUP	-	PhosphoELM
488	Y	Phosphorylation	Kinase	FGFR-FAMILY	-	GPS
488	Y	Phosphorylation	Kinase	SRC	P12931	PSP
488	Y	Phosphorylation	Kinase	FYN	P06241	PSP
488	Y	Phosphorylation	Kinase	FGFR3	P22607	PSP
529	Y	Phosphorylation	Kinase	MAPK1	P28482	GPS
529	Y	Phosphorylation	Kinase	SRC	P12931	PSP
529	Y	Phosphorylation	Kinase	FYN	P06241	PSP
529	Y	Phosphorylation	Kinase	FGFR3	P22607	Uniprot
577	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
580	Y	Phosphorylation	Kinase	FYN	P06241	PSP
580	Y	Phosphorylation	Kinase	SRC	P12931	PSP
644	Y	Phosphorylation	Kinase	FYN	P06241	PSP
644	Y	Phosphorylation	Kinase	SRC	P12931	PSP
707	Y	Phosphorylation	Kinase	FGFR1	P11362	PhosphoELM
707	Y	Phosphorylation	Kinase	SRC	P12931	PSP
707	Y	Phosphorylation	Kinase	FYN	P06241	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
227	S	Phosphorylation	-
Activated by phosphorylation at Ser-227 by PDPK1.
365	T	Phosphorylation	18691976
May be phosphorylated at Thr-365 and Ser-369 by MAPK1/ERK2 and MAPK3/ERK1.
369	S	Phosphorylation	18691976
May be phosphorylated at Thr-365 and Ser-369 by MAPK1/ERK2 and MAPK3/ERK1.
386	S	Phosphorylation	18691976
Autophosphorylated on Ser-386, as part of the activation process.
386	S	Phosphorylation	18691976
Can also be activated via phosphorylation at Ser-386 by MAPKAPK2.

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 KS6A3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PEA15_HUMAN	PEA15	physical	12796492
CBP_HUMAN	CREBBP	physical	11564891
MK01_HUMAN	MAPK1	physical	8939914
MK03_HUMAN	MAPK3	physical	8939914
PDPK1_HUMAN	PDPK1	physical	10856237
MK01_HUMAN	MAPK1	physical	9915826
H2AX_HUMAN	H2AFX	physical	21224359
EIF3C_HUMAN	EIF3C	physical	21900206
ATP5J_HUMAN	ATP5J	physical	21900206
BARX1_HUMAN	BARX1	physical	21900206
MASP1_HUMAN	MASP1	physical	21900206
SPSY_HUMAN	SMS	physical	21900206
ESR1_HUMAN	ESR1	physical	11432835
YBOX1_HUMAN	YBX1	physical	19036157
IKBA_HUMAN	NFKBIA	physical	22685297
TRAF2_HUMAN	TRAF2	physical	22685297
TAU_HUMAN	MAPT	physical	17512525
H31_HUMAN	HIST1H3A	physical	10436156
HMGN1_HUMAN	HMGN1	physical	11438671
FGFR1_HUMAN	FGFR1	physical	24141780
DFFA_HUMAN	DFFA	physical	22863883
HSP7C_HUMAN	HSPA8	physical	22863883
PNCB_HUMAN	NAPRT	physical	22863883
RASL1_HUMAN	RASAL1	physical	22863883
NHRF1_HUMAN	SLC9A3R1	physical	22863883
MK01_HUMAN	MAPK1	physical	12016217
MK01_HUMAN	MAPK1	physical	25241761
PDPK1_HUMAN	PDPK1	physical	25241761

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
303600	Coffin-Lowry syndrome (CLS)
300844	Mental retardation, X-linked 19 (MRX19)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00945	Acetylsalicylic acid

Regulatory Network of KS6A3_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-415 AND SER-715, ANDMASS SPECTROMETRY.	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 SER-17; SER-19; TYR-226;SER-227; THR-365; SER-369; SER-375; SER-386; THR-391; SER-415; SER-715AND SER-737, AND MASS SPECTROMETRY.	19369195 [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-365; SER-369; SER-375AND SER-715, 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-227; THR-365; SER-369;SER-375; SER-386; SER-415; SER-556 AND SER-715, AND MASS SPECTROMETRY.	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-715, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; THR-231; THR-365;SER-369 AND SER-715, AND MASS SPECTROMETRY.	17192257 [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-715, 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-715, 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 THR-365 AND SER-369, ANDMASS SPECTROMETRY.	17081983 [Abstract]

show

show

show

show

show