dbPTM

CRTC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CRTC2_HUMAN
UniProt AC	Q53ET0
Protein Name	CREB-regulated transcription coactivator 2
Gene Name	CRTC2
Organism	Homo sapiens (Human).
Sequence Length	693
Subcellular Localization	Cytoplasm . Nucleus . Translocated from the nucleus to the cytoplasm on interaction of the phosphorylated form with 14-3-3 protein (PubMed:15454081). In response to cAMP levels and glucagon, relocated to the nucleus (PubMed:15454081).
Protein Description	Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates gluconeogenesis as a component of the LKB1/AMPK/TORC2 signaling pathway. Regulates the expression of specific genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR)..
Protein Sequence	MATSGANGPGSATASASNPRKFSEKIALQKQRQAEETAAFEEVMMDIGSTRLQAQKLRLAYTRSSHYGGSLPNVNQIGSGLAEFQSPLHSPLDSSRSTRHHGLVERVQRDPRRMVSPLRRYTRHIDSSPYSPAYLSPPPESSWRRTMAWGNFPAEKGQLFRLPSALNRTSSDSALHTSVMNPSPQDTYPGPTPPSILPSRRGGILDGEMDPKVPAIEENLLDDKHLLKPWDAKKLSSSSSRPRSCEVPGINIFPSPDQPANVPVLPPAMNTGGSLPDLTNLHFPPPLPTPLDPEETAYPSLSGGNSTSNLTHTMTHLGISRGMGLGPGYDAPGLHSPLSHPSLQSSLSNPNLQASLSSPQPQLQGSHSHPSLPASSLARHVLPTTSLGHPSLSAPALSSSSSSSSTSSPVLGAPSYPASTPGASPHHRRVPLSPLSLLAGPADARRSQQQLPKQFSPTMSPTLSSITQGVPLDTSKLSTDQRLPPYPYSSPSLVLPTQPHTPKSLQQPGLPSQSCSVQSSGGQPPGRQSHYGTPYPPGPSGHGQQSYHRPMSDFNLGNLEQFSMESPSASLVLDPPGFSEGPGFLGGEGPMGGPQDPHTFNHQNLTHCSRHGSGPNIILTGDSSPGFSKEIAAALAGVPGFEVSAAGLELGLGLEDELRMEPLGLEGLNMLSDPCALLPDPAVEESFRSDRLQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATSGANGP ------CCCCCCCCC	15.52	22814378
3	Phosphorylation	-----MATSGANGPG -----CCCCCCCCCC	26.79	20068231
4	Phosphorylation	----MATSGANGPGS ----CCCCCCCCCCC	26.77	20068231
11	Phosphorylation	SGANGPGSATASASN CCCCCCCCCCCCCCC	26.11	25159151
13	Phosphorylation	ANGPGSATASASNPR CCCCCCCCCCCCCHH	23.89	21406692
15	Phosphorylation	GPGSATASASNPRKF CCCCCCCCCCCHHHH	28.07	21406692
17	Phosphorylation	GSATASASNPRKFSE CCCCCCCCCHHHHHH	44.89	25159151
21	Acetylation	ASASNPRKFSEKIAL CCCCCHHHHHHHHHH	55.27	25953088
21	Sumoylation	ASASNPRKFSEKIAL CCCCCHHHHHHHHHH	55.27	-
23	Phosphorylation	ASNPRKFSEKIALQK CCCHHHHHHHHHHHH	40.80	24719451
25	Sumoylation	NPRKFSEKIALQKQR CHHHHHHHHHHHHHH	31.89	-
25	Acetylation	NPRKFSEKIALQKQR CHHHHHHHHHHHHHH	31.89	25953088
25	Sumoylation	NPRKFSEKIALQKQR CHHHHHHHHHHHHHH	31.89	-
25	Ubiquitination	NPRKFSEKIALQKQR CHHHHHHHHHHHHHH	31.89	29967540
30	Ubiquitination	SEKIALQKQRQAEET HHHHHHHHHHHHHHH	48.58	29967540
37	O-linked_Glycosylation	KQRQAEETAAFEEVM HHHHHHHHHHHHHHH	18.13	30059200
43	Ubiquitination	ETAAFEEVMMDIGST HHHHHHHHHHHHCCH	2.79	21890473
51	Asymmetric dimethylarginine	MMDIGSTRLQAQKLR HHHHCCHHHHHHHHH	26.88	-
51	Methylation	MMDIGSTRLQAQKLR HHHHCCHHHHHHHHH	26.88	-
64	Phosphorylation	LRLAYTRSSHYGGSL HHHHHHCCCCCCCCC	17.42	23401153
65	Phosphorylation	RLAYTRSSHYGGSLP HHHHHCCCCCCCCCC	19.89	23927012
67	Phosphorylation	AYTRSSHYGGSLPNV HHHCCCCCCCCCCCH	25.73	23927012
70	O-linked_Glycosylation	RSSHYGGSLPNVNQI CCCCCCCCCCCHHHC	35.97	30059200
70	Phosphorylation	RSSHYGGSLPNVNQI CCCCCCCCCCCHHHC	35.97	23927012
79	Phosphorylation	PNVNQIGSGLAEFQS CCHHHCCCCHHHCCC	32.06	23927012
86	Phosphorylation	SGLAEFQSPLHSPLD CCHHHCCCCCCCCCC	34.45	23927012
90	Phosphorylation	EFQSPLHSPLDSSRS HCCCCCCCCCCCCCC	34.54	15454081
94	Phosphorylation	PLHSPLDSSRSTRHH CCCCCCCCCCCCCCC	35.02	23927012
95	Phosphorylation	LHSPLDSSRSTRHHG CCCCCCCCCCCCCCC	29.89	23927012
99	Asymmetric dimethylarginine	LDSSRSTRHHGLVER CCCCCCCCCCCHHHH	22.50	-
99	Methylation	LDSSRSTRHHGLVER CCCCCCCCCCCHHHH	22.50	-
106	Methylation	RHHGLVERVQRDPRR CCCCHHHHHHCCHHH	23.53	115918757
116	Phosphorylation	RDPRRMVSPLRRYTR CCHHHHHHHHHHHHC	14.63	23898821
120	Asymmetric dimethylarginine	RMVSPLRRYTRHIDS HHHHHHHHHHCCCCC	44.87	-
120	Methylation	RMVSPLRRYTRHIDS HHHHHHHHHHCCCCC	44.87	-
123	Asymmetric dimethylarginine	SPLRRYTRHIDSSPY HHHHHHHCCCCCCCC	18.81	-
123	Methylation	SPLRRYTRHIDSSPY HHHHHHHCCCCCCCC	18.81	-
127	O-linked_Glycosylation	RYTRHIDSSPYSPAY HHHCCCCCCCCCCHH	32.39	30059200
127	Phosphorylation	RYTRHIDSSPYSPAY HHHCCCCCCCCCCHH	32.39	29978859
128	O-linked_Glycosylation	YTRHIDSSPYSPAYL HHCCCCCCCCCCHHC	24.90	30059200
128	Phosphorylation	YTRHIDSSPYSPAYL HHCCCCCCCCCCHHC	24.90	29978859
130	Phosphorylation	RHIDSSPYSPAYLSP CCCCCCCCCCHHCCC	29.27	21712546
131	Phosphorylation	HIDSSPYSPAYLSPP CCCCCCCCCHHCCCC	13.36	29978859
134	Phosphorylation	SSPYSPAYLSPPPES CCCCCCHHCCCCCCC	15.88	30108239
136	Phosphorylation	PYSPAYLSPPPESSW CCCCHHCCCCCCCCC	23.76	15454081
141	Phosphorylation	YLSPPPESSWRRTMA HCCCCCCCCCHHCCC	40.76	29978859
142	Phosphorylation	LSPPPESSWRRTMAW CCCCCCCCCHHCCCC	23.96	29978859
146	Phosphorylation	PESSWRRTMAWGNFP CCCCCHHCCCCCCCC	11.58	28555341
156	Sumoylation	WGNFPAEKGQLFRLP CCCCCCCCCCCEECC	54.80	-
156	Sumoylation	WGNFPAEKGQLFRLP CCCCCCCCCCCEECC	54.80	-
156	Ubiquitination	WGNFPAEKGQLFRLP CCCCCCCCCCCEECC	54.80	22817900
161	Asymmetric dimethylarginine	AEKGQLFRLPSALNR CCCCCCEECCHHHHC	55.04	-
161	Methylation	AEKGQLFRLPSALNR CCCCCCEECCHHHHC	55.04	80702691
164	Phosphorylation	GQLFRLPSALNRTSS CCCEECCHHHHCCCC	50.40	28857561
168	Asymmetric dimethylarginine	RLPSALNRTSSDSAL ECCHHHHCCCCCCCC	36.51	-
168	Methylation	RLPSALNRTSSDSAL ECCHHHHCCCCCCCC	36.51	-
169	Phosphorylation	LPSALNRTSSDSALH CCHHHHCCCCCCCCC	31.35	23401153
170	Phosphorylation	PSALNRTSSDSALHT CHHHHCCCCCCCCCC	28.98	30278072
171	Dephosphorylation	SALNRTSSDSALHTS HHHHCCCCCCCCCCC	34.66	15454081
171	O-linked_Glycosylation	SALNRTSSDSALHTS HHHHCCCCCCCCCCC	34.66	30059200
171	Phosphorylation	SALNRTSSDSALHTS HHHHCCCCCCCCCCC	34.66	23401153
173	O-linked_Glycosylation	LNRTSSDSALHTSVM HHCCCCCCCCCCCCC	34.38	30059200
173	Phosphorylation	LNRTSSDSALHTSVM HHCCCCCCCCCCCCC	34.38	30278072
177	Phosphorylation	SSDSALHTSVMNPSP CCCCCCCCCCCCCCC	24.70	30278072
178	Phosphorylation	SDSALHTSVMNPSPQ CCCCCCCCCCCCCCC	14.50	30278072
183	Phosphorylation	HTSVMNPSPQDTYPG CCCCCCCCCCCCCCC	30.13	30278072
187	Phosphorylation	MNPSPQDTYPGPTPP CCCCCCCCCCCCCCC	26.77	23927012
188	Phosphorylation	NPSPQDTYPGPTPPS CCCCCCCCCCCCCCC	17.93	23927012
192	Phosphorylation	QDTYPGPTPPSILPS CCCCCCCCCCCCCCC	54.47	23927012
195	Phosphorylation	YPGPTPPSILPSRRG CCCCCCCCCCCCCCC	37.65	23927012
199	Phosphorylation	TPPSILPSRRGGILD CCCCCCCCCCCCCCC	31.03	23927012
201	Methylation	PSILPSRRGGILDGE CCCCCCCCCCCCCCC	52.61	115918761
224	Sumoylation	EENLLDDKHLLKPWD HHCCCCCCCCCCCCC	35.50	-
224	Sumoylation	EENLLDDKHLLKPWD HHCCCCCCCCCCCCC	35.50	-
224	Ubiquitination	EENLLDDKHLLKPWD HHCCCCCCCCCCCCC	35.50	29967540
228	Sumoylation	LDDKHLLKPWDAKKL CCCCCCCCCCCHHHC	50.88	-
228	Acetylation	LDDKHLLKPWDAKKL CCCCCCCCCCCHHHC	50.88	19608861
228	Sumoylation	LDDKHLLKPWDAKKL CCCCCCCCCCCHHHC	50.88	19608861
228	Ubiquitination	LDDKHLLKPWDAKKL CCCCCCCCCCCHHHC	50.88	19608861
233	Ubiquitination	LLKPWDAKKLSSSSS CCCCCCHHHCCCCCC	52.34	29967540
234	Sumoylation	LKPWDAKKLSSSSSR CCCCCHHHCCCCCCC	56.15	28112733
271	Phosphorylation	VLPPAMNTGGSLPDL CCCCCCCCCCCCCCC	29.81	26074081
274	Phosphorylation	PAMNTGGSLPDLTNL CCCCCCCCCCCCCCC	37.77	26074081
306	Phosphorylation	PSLSGGNSTSNLTHT CCCCCCCCCCCCCCH	36.17	15454081
329	Phosphorylation	GMGLGPGYDAPGLHS CCCCCCCCCCCCCCC	16.44	28464451
336	Phosphorylation	YDAPGLHSPLSHPSL CCCCCCCCCCCCHHH	32.36	20068231
339	Phosphorylation	PGLHSPLSHPSLQSS CCCCCCCCCHHHHHH	36.41	20068231
342	Phosphorylation	HSPLSHPSLQSSLSN CCCCCCHHHHHHHCC	33.35	20068231
345	Phosphorylation	LSHPSLQSSLSNPNL CCCHHHHHHHCCCCH	38.24	26074081
346	Phosphorylation	SHPSLQSSLSNPNLQ CCHHHHHHHCCCCHH	23.90	26074081
348	Phosphorylation	PSLQSSLSNPNLQAS HHHHHHHCCCCHHHH	52.79	30576142
355	Phosphorylation	SNPNLQASLSSPQPQ CCCCHHHHHCCCCCC	18.80	20068231
357	Phosphorylation	PNLQASLSSPQPQLQ CCHHHHHCCCCCCCC	37.16	20068231
358	Phosphorylation	NLQASLSSPQPQLQG CHHHHHCCCCCCCCC	32.61	20068231
366	Phosphorylation	PQPQLQGSHSHPSLP CCCCCCCCCCCCCCC	14.62	20068231
368	Phosphorylation	PQLQGSHSHPSLPAS CCCCCCCCCCCCCHH	38.50	28464451
371	Phosphorylation	QGSHSHPSLPASSLA CCCCCCCCCCHHHHH	41.37	26074081
375	Phosphorylation	SHPSLPASSLARHVL CCCCCCHHHHHHHHC	24.76	20068231
376	Phosphorylation	HPSLPASSLARHVLP CCCCCHHHHHHHHCC	28.31	26074081
384	Phosphorylation	LARHVLPTTSLGHPS HHHHHCCCCCCCCCC	25.51	23401153
385	Phosphorylation	ARHVLPTTSLGHPSL HHHHCCCCCCCCCCC	21.73	26434776
386	Phosphorylation	RHVLPTTSLGHPSLS HHHCCCCCCCCCCCC	34.53	26434776
391	Phosphorylation	TTSLGHPSLSAPALS CCCCCCCCCCCCCCC	29.31	26434776
393	Phosphorylation	SLGHPSLSAPALSSS CCCCCCCCCCCCCCC	36.22	15454081
398	Phosphorylation	SLSAPALSSSSSSSS CCCCCCCCCCCCCCC	30.22	26434776
399	Phosphorylation	LSAPALSSSSSSSST CCCCCCCCCCCCCCC	34.78	30576142
400	Phosphorylation	SAPALSSSSSSSSTS CCCCCCCCCCCCCCC	30.75	23312004
401	Phosphorylation	APALSSSSSSSSTSS CCCCCCCCCCCCCCC	35.87	23312004
402	Phosphorylation	PALSSSSSSSSTSSP CCCCCCCCCCCCCCC	35.87	23312004
403	Phosphorylation	ALSSSSSSSSTSSPV CCCCCCCCCCCCCCC	30.20	23312004
404	Phosphorylation	LSSSSSSSSTSSPVL CCCCCCCCCCCCCCC	39.31	23312004
405	Phosphorylation	SSSSSSSSTSSPVLG CCCCCCCCCCCCCCC	33.97	23312004
406	Phosphorylation	SSSSSSSTSSPVLGA CCCCCCCCCCCCCCC	34.86	23312004
407	Phosphorylation	SSSSSSTSSPVLGAP CCCCCCCCCCCCCCC	34.29	28464451
408	Phosphorylation	SSSSSTSSPVLGAPS CCCCCCCCCCCCCCC	21.08	28464451
415	Phosphorylation	SPVLGAPSYPASTPG CCCCCCCCCCCCCCC	43.12	23312004
416	Phosphorylation	PVLGAPSYPASTPGA CCCCCCCCCCCCCCC	11.19	28464451
419	Phosphorylation	GAPSYPASTPGASPH CCCCCCCCCCCCCCC	30.54	23312004
420	Phosphorylation	APSYPASTPGASPHH CCCCCCCCCCCCCCC	28.04	27080861
424	Phosphorylation	PASTPGASPHHRRVP CCCCCCCCCCCCCCC	30.59	26055452
433	Phosphorylation	HHRRVPLSPLSLLAG CCCCCCCCHHHHHHC	20.09	29255136
436	Phosphorylation	RVPLSPLSLLAGPAD CCCCCHHHHHHCHHH	25.40	30266825
447	Phosphorylation	GPADARRSQQQLPKQ CHHHHHHHHHHCCCC	27.13	23312004
453	Sumoylation	RSQQQLPKQFSPTMS HHHHHCCCCCCCCCC	72.99	-
456	Phosphorylation	QQLPKQFSPTMSPTL HHCCCCCCCCCCCCH	19.57	28355574
458	Phosphorylation	LPKQFSPTMSPTLSS CCCCCCCCCCCCHHH	29.14	28355574
460	Phosphorylation	KQFSPTMSPTLSSIT CCCCCCCCCCHHHHC	19.74	30278072
462	Phosphorylation	FSPTMSPTLSSITQG CCCCCCCCHHHHCCC	31.78	30278072
464	Phosphorylation	PTMSPTLSSITQGVP CCCCCCHHHHCCCCC	23.36	30278072
465	Phosphorylation	TMSPTLSSITQGVPL CCCCCHHHHCCCCCC	32.54	30278072
467	Phosphorylation	SPTLSSITQGVPLDT CCCHHHHCCCCCCCC	22.63	23898821
474	Phosphorylation	TQGVPLDTSKLSTDQ CCCCCCCCCCCCCCC	35.13	23403867
475	Phosphorylation	QGVPLDTSKLSTDQR CCCCCCCCCCCCCCC	31.13	23403867
486	Phosphorylation	TDQRLPPYPYSSPSL CCCCCCCCCCCCCCE	16.92	25022875
488	Phosphorylation	QRLPPYPYSSPSLVL CCCCCCCCCCCCEEC	18.88	21712546
489	O-linked_Glycosylation	RLPPYPYSSPSLVLP CCCCCCCCCCCEECC	31.13	30059200
489	Phosphorylation	RLPPYPYSSPSLVLP CCCCCCCCCCCEECC	31.13	15454081
490	Phosphorylation	LPPYPYSSPSLVLPT CCCCCCCCCCEECCC	16.80	25159151
492	Phosphorylation	PYPYSSPSLVLPTQP CCCCCCCCEECCCCC	32.81	15454081
497	Phosphorylation	SPSLVLPTQPHTPKS CCCEECCCCCCCCCC	51.04	21712546
501	Phosphorylation	VLPTQPHTPKSLQQP ECCCCCCCCCCCCCC	38.81	25159151
504	O-linked_Glycosylation	TQPHTPKSLQQPGLP CCCCCCCCCCCCCCC	32.39	30059200
504	Phosphorylation	TQPHTPKSLQQPGLP CCCCCCCCCCCCCCC	32.39	25159151
512	Phosphorylation	LQQPGLPSQSCSVQS CCCCCCCCCCCEEEC	39.50	27080861
514	O-linked_Glycosylation	QPGLPSQSCSVQSSG CCCCCCCCCEEECCC	16.82	30059200
514	Phosphorylation	QPGLPSQSCSVQSSG CCCCCCCCCEEECCC	16.82	27080861
516	O-linked_Glycosylation	GLPSQSCSVQSSGGQ CCCCCCCEEECCCCC	28.56	30059200
516	Phosphorylation	GLPSQSCSVQSSGGQ CCCCCCCEEECCCCC	28.56	27080861
519	O-linked_Glycosylation	SQSCSVQSSGGQPPG CCCCEEECCCCCCCC	28.88	30059200
519	Phosphorylation	SQSCSVQSSGGQPPG CCCCEEECCCCCCCC	28.88	25159151
520	Phosphorylation	QSCSVQSSGGQPPGR CCCEEECCCCCCCCC	29.83	25159151
613	Phosphorylation	THCSRHGSGPNIILT CCCCCCCCCCEEEEE	44.97	25159151
620	Phosphorylation	SGPNIILTGDSSPGF CCCEEEEECCCCCCC	28.65	22167270
623	Phosphorylation	NIILTGDSSPGFSKE EEEEECCCCCCCCHH	39.51	29255136
624	Phosphorylation	IILTGDSSPGFSKEI EEEECCCCCCCCHHH	33.51	29255136
628	Phosphorylation	GDSSPGFSKEIAAAL CCCCCCCCHHHHHHH	34.98	29255136
629	Acetylation	DSSPGFSKEIAAALA CCCCCCCHHHHHHHH	51.37	18849969

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
171	S	Phosphorylation	Kinase	AMPK	Q9Y478	Uniprot
171	S	Phosphorylation	Kinase	MARK2	Q7KZI7	Uniprot
171	S	Phosphorylation	Kinase	SIK1	P57059	Uniprot
171	S	Phosphorylation	Kinase	SIK2	Q9H0K1	Uniprot
171	S	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
274	S	Phosphorylation	Kinase	MARK2	Q7KZI7	Uniprot
433	S	Phosphorylation	Kinase	CDK2	P24941	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	COP1	Q8NHY2	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	DET1	Q7L5Y6	PMID:17805301
-	K	Ubiquitination	E3 ubiquitin ligase	DET1#COP1	Q7L5Y6#Q8NHY2	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
171	S	Phosphorylation	15454081
Following adenylyl cyclase activation, dephosphorylated at Ser-171 by PPP3CA/calcineurin A resulting in CRTC2 dissociation from 14-3-3 proteins and PPP3CA (By similarity).
171	S	Phosphorylation	15454081
Phosphorylation/dephosphorylation states of Ser-171 are required for regulating transduction of CREB activity.
274	S	Phosphorylation	18626018
Phosphorylation at Ser-274 by MARK2 is induced under low glucose conditions and dephosphorylated in response to glucose influx.
274	S	Phosphorylation	18626018
Phosphorylation at Ser-274 promotes interaction with 14-3-3 proteins and translocation to the cytoplasm.

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 CRTC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SIK2_HUMAN	SIK2	physical	15454081
EP300_HUMAN	EP300	physical	17476304
PP2BA_HUMAN	PPP3CA	physical	27990298
PP2BC_HUMAN	PPP3CC	physical	28514442
CANB1_HUMAN	PPP3R1	physical	28514442
1433Z_HUMAN	YWHAZ	physical	28514442
1433G_HUMAN	YWHAG	physical	28514442
1433E_HUMAN	YWHAE	physical	28514442
PP2BB_HUMAN	PPP3CB	physical	28514442
CING_HUMAN	CGN	physical	27173435
STAT3_MOUSE	Stat3	physical	27362806
MDM2_HUMAN	MDM2	physical	27362806

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 CRTC2_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 THR-458; SER-460; SER-489 AND THR-497, AND MASSSPECTROMETRY.	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-228, 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-70; SER-86; SER-90;THR-192; SER-433; TYR-488; SER-490; SER-613 AND SER-624, 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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-458; SER-460; SER-489 AND THR-497, 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-70; SER-86; SER-90;TYR-130; SER-136; SER-433; SER-489; THR-501; SER-613 AND SER-624, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Glucose controls CREB activity in islet cells via regulatedphosphorylation of TORC2."; Jansson D., Ng A.C., Fu A., Depatie C., Al Azzabi M., Screaton R.A.; Proc. Natl. Acad. Sci. U.S.A. 105:10161-10166(2008). Cited for: PHOSPHORYLATION AT SER-171 AND SER-274, INTERACTION WITH 14-3-3, ANDMUTAGENESIS OF SER-171; SER-274 AND SER-368.	18626018 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-433, AND MASSSPECTROMETRY.	18220336 [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-433, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Silencing the constitutive active transcription factor CREB by theLKB1-SIK signaling cascade."; Katoh Y., Takemori H., Lin X.-Z., Tamura M., Muraoka M., Satoh T.,Tsuchiya Y., Min L., Doi J., Miyauchi A., Witters L.A., Nakamura H.,Okamoto M.; FEBS J. 273:2730-2748(2006). Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-171, ANDMUTAGENESIS OF SER-171.	16817901 [Abstract]
"The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitivecoincidence detector."; Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G.,Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H.,Okamoto M., Montminy M.; Cell 119:61-74(2004). Cited for: INTERACTION WITH CREB1; SIK2; PPP3CA; YWHAB AND YWHAG, TISSUESPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, PHOSPHORYLATION ATSER-70; SER-90; SER-136; SER-171; SER-306; SER-368; SER-393; SER-433;SER-456; SER-489; SER-492 AND SER-613, MASS SPECTROMETRY, ANDMUTAGENESIS OF SER-171 AND SER-368.	15454081 [Abstract]

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show

show