dbPTM

MAVS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MAVS_HUMAN
UniProt AC	Q7Z434
Protein Name	Mitochondrial antiviral-signaling protein {ECO:0000305}
Gene Name	MAVS {ECO:0000312\|HGNC:HGNC:29233}
Organism	Homo sapiens (Human).
Sequence Length	540
Subcellular Localization	Mitochondrion outer membrane . Mitochondrion . Peroxisome .
Protein Description	Required for innate immune defense against viruses. Acts downstream of DHX33, DDX58/RIG-I and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFN-beta and RANTES (CCL5). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state. Upon viral infection, peroxisomal MAVS induces the rapid interferon-independent expression of defense factors that provide short-term protection, whereas mitochondrial MAVS activates an interferon-dependent signaling pathway with delayed kinetics, which amplifies and stabilizes the antiviral response. May activate the same pathways following detection of extracellular dsRNA by TLR3. May protect cells from apoptosis..
Protein Sequence	MPFAEDKTYKYICRNFSNFCNVDVVEILPYLPCLTARDQDRLRATCTLSGNRDTLWHLFNTLQRRPGWVEYFIAALRGCELVDLADEVASVYQSYQPRTSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYNSCREKEPSYPMPVQETQAPESPGENSEQALQTLSPRAIPRNPDGGPLESSSDLAALSPLTSSGHQEQDTELGSTHTAGATSSLTPSRGPVSPSVSFQPLARSTPRASRLPGPTGSVVSTGTSFSSSSPGLASAGAAEGKQGAESDQAEPIICSSGAEAPANSLPSKVPTTLMPVNTVALKVPANPASVSTVPSKLPTSSKPPGAVPSNALTNPAPSKLPINSTRAGMVPSKVPTSMVLTKVSASTVPTDGSSRNEETPAAPTPAGATGGSSAWLDSSSENRGLGSELSKPGVLASQVDSPFSGCFEDLAISASTSLGMGPCHGPEENEYKSEGTFGIHVAENPSIQLLEGNPGPPADPDGGPRPQADRKFQEREVPCHRPSPGALWLQVAVTGVLVVTLLVVLYRRRLH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Malonylation	-MPFAEDKTYKYICR -CCCCCCHHHHHHHH	45.30	26320211
7	Ubiquitination	-MPFAEDKTYKYICR -CCCCCCHHHHHHHH	45.30	29967540
8	Phosphorylation	MPFAEDKTYKYICRN CCCCCCHHHHHHHHC	37.25	29496907
9	Phosphorylation	PFAEDKTYKYICRNF CCCCCHHHHHHHHCC	13.92	27642862
10	Acetylation	FAEDKTYKYICRNFS CCCCHHHHHHHHCCC	33.11	27452117
10	Malonylation	FAEDKTYKYICRNFS CCCCHHHHHHHHCCC	33.11	26320211
10	Ubiquitination	FAEDKTYKYICRNFS CCCCHHHHHHHHCCC	33.11	-
11	Phosphorylation	AEDKTYKYICRNFSN CCCHHHHHHHHCCCC	8.54	27642862
11 (in isoform 4)	Phosphorylation	-	8.54	25849741
22	Phosphorylation	NFSNFCNVDVVEILP CCCCCCCCCCEEHHH	6.59	32142685
30	Phosphorylation	DVVEILPYLPCLTAR CCEEHHHCCCCCCCC	21.60	-
45	Phosphorylation	DQDRLRATCTLSGNR CHHHHEEEEEECCCH	10.29	-
71	Phosphorylation	RRPGWVEYFIAALRG CCCCHHHHHHHHHHC	7.23	-
81	Phosphorylation	AALRGCELVDLADEV HHHHCCEEEHHHHHH	4.17	32142685
90	Phosphorylation	DLADEVASVYQSYQP HHHHHHHHHHHHCCC	26.91	26552605
92	Phosphorylation	ADEVASVYQSYQPRT HHHHHHHHHHCCCCC	6.83	28796482
94	Phosphorylation	EVASVYQSYQPRTSD HHHHHHHHCCCCCCC	14.19	26552605
95	Phosphorylation	VASVYQSYQPRTSDR HHHHHHHCCCCCCCC	13.65	26552605
99	Phosphorylation	YQSYQPRTSDRPPDP HHHCCCCCCCCCCCC	41.48	23312004
100	Phosphorylation	QSYQPRTSDRPPDPL HHCCCCCCCCCCCCC	32.66	23312004
111	Phosphorylation	PDPLEPPSLPAERPG CCCCCCCCCCCCCCC	58.67	24173317
121	Phosphorylation	AERPGPPTPAAAHSI CCCCCCCCCCHHHCC	28.79	28348404
139	Phosphorylation	SCREKEPSYPMPVQE CCCCCCCCCCCCCCC	42.85	23927012
140	Phosphorylation	CREKEPSYPMPVQET CCCCCCCCCCCCCCC	17.79	23927012
147	Phosphorylation	YPMPVQETQAPESPG CCCCCCCCCCCCCCC	16.97	23927012
152	Phosphorylation	QETQAPESPGENSEQ CCCCCCCCCCCCHHH	36.83	25159151
157	Phosphorylation	PESPGENSEQALQTL CCCCCCCHHHHHHHC	27.12	23927012
163	Phosphorylation	NSEQALQTLSPRAIP CHHHHHHHCCCCCCC	30.01	30266825
165	Phosphorylation	EQALQTLSPRAIPRN HHHHHHCCCCCCCCC	18.74	25159151
180	Phosphorylation	PDGGPLESSSDLAAL CCCCCCCCHHHHHHH	42.71	26074081
181	Phosphorylation	DGGPLESSSDLAALS CCCCCCCHHHHHHHC	20.63	26074081
182	Phosphorylation	GGPLESSSDLAALSP CCCCCCHHHHHHHCC	46.02	26074081
188	Phosphorylation	SSDLAALSPLTSSGH HHHHHHHCCCCCCCC	17.09	26074081
191	Phosphorylation	LAALSPLTSSGHQEQ HHHHCCCCCCCCHHC	25.00	26074081
192	Phosphorylation	AALSPLTSSGHQEQD HHHCCCCCCCCHHCC	41.84	26074081
193	Phosphorylation	ALSPLTSSGHQEQDT HHCCCCCCCCHHCCC	34.75	26074081
200	Phosphorylation	SGHQEQDTELGSTHT CCCHHCCCCCCCCCC	32.57	26714015
204	Phosphorylation	EQDTELGSTHTAGAT HCCCCCCCCCCCCCC	29.64	26714015
205	Phosphorylation	QDTELGSTHTAGATS CCCCCCCCCCCCCCC	22.80	26714015
207	Phosphorylation	TELGSTHTAGATSSL CCCCCCCCCCCCCCC	27.20	25002506
207	Ubiquitination	TELGSTHTAGATSSL CCCCCCCCCCCCCCC	27.20	32015554
211	Phosphorylation	STHTAGATSSLTPSR CCCCCCCCCCCCCCC	20.24	25002506
212	Phosphorylation	THTAGATSSLTPSRG CCCCCCCCCCCCCCC	23.86	25002506
213	Phosphorylation	HTAGATSSLTPSRGP CCCCCCCCCCCCCCC	31.72	25002506
215	Phosphorylation	AGATSSLTPSRGPVS CCCCCCCCCCCCCCC	22.59	26074081
217	Phosphorylation	ATSSLTPSRGPVSPS CCCCCCCCCCCCCCC	44.63	26074081
221	Ubiquitination	LTPSRGPVSPSVSFQ CCCCCCCCCCCCCCC	17.08	32015554
222	Phosphorylation	TPSRGPVSPSVSFQP CCCCCCCCCCCCCCC	18.00	19664994
224	Phosphorylation	SRGPVSPSVSFQPLA CCCCCCCCCCCCCCC	23.92	30266825
226	Phosphorylation	GPVSPSVSFQPLARS CCCCCCCCCCCCCCC	23.62	30266825
230	Ubiquitination	PSVSFQPLARSTPRA CCCCCCCCCCCCCCH	4.26	32015554
232	Methylation	VSFQPLARSTPRASR CCCCCCCCCCCCHHH	49.06	115482703
233	Phosphorylation	SFQPLARSTPRASRL CCCCCCCCCCCHHHC	36.84	25159151
234	Phosphorylation	FQPLARSTPRASRLP CCCCCCCCCCHHHCC	15.96	25159151
236	Asymmetric dimethylarginine	PLARSTPRASRLPGP CCCCCCCCHHHCCCC	45.33	-
236	Methylation	PLARSTPRASRLPGP CCCCCCCCHHHCCCC	45.33	-
238	Phosphorylation	ARSTPRASRLPGPTG CCCCCCHHHCCCCCC	35.31	23090842
239	Methylation	RSTPRASRLPGPTGS CCCCCHHHCCCCCCC	43.87	82955043
244	Phosphorylation	ASRLPGPTGSVVSTG HHHCCCCCCCEEEEC	48.26	30278072
246	Phosphorylation	RLPGPTGSVVSTGTS HCCCCCCCEEEECCC	23.09	30278072
249	Phosphorylation	GPTGSVVSTGTSFSS CCCCCEEEECCCCCC	20.97	30278072
250	Phosphorylation	PTGSVVSTGTSFSSS CCCCEEEECCCCCCC	32.63	25159151
252	Phosphorylation	GSVVSTGTSFSSSSP CCEEEECCCCCCCCC	27.04	25159151
253	Phosphorylation	SVVSTGTSFSSSSPG CEEEECCCCCCCCCC	25.19	30278072
255	Phosphorylation	VSTGTSFSSSSPGLA EEECCCCCCCCCCHH	29.13	30278072
256	Phosphorylation	STGTSFSSSSPGLAS EECCCCCCCCCCHHH	32.59	30278072
257	Phosphorylation	TGTSFSSSSPGLASA ECCCCCCCCCCHHHC	39.08	30278072
258	Phosphorylation	GTSFSSSSPGLASAG CCCCCCCCCCHHHCC	25.57	30278072
263	Phosphorylation	SSSPGLASAGAAEGK CCCCCHHHCCHHCCC	32.07	30278072
275	Phosphorylation	EGKQGAESDQAEPII CCCCCCCCCCCCCEE	34.19	22199227
284	Phosphorylation	QAEPIICSSGAEAPA CCCCEEECCCCCCCC	22.77	25627689
296	Phosphorylation	APANSLPSKVPTTLM CCCCCCCCCCCCCEE	52.13	24719451
300	Phosphorylation	SLPSKVPTTLMPVNT CCCCCCCCCEECCCE	35.23	-
301	O-linked_Glycosylation	LPSKVPTTLMPVNTV CCCCCCCCEECCCEE	18.26	30059200
301	Phosphorylation	LPSKVPTTLMPVNTV CCCCCCCCEECCCEE	18.26	-
303	Sulfoxidation	SKVPTTLMPVNTVAL CCCCCCEECCCEEEE	3.06	21406390
307	O-linked_Glycosylation	TTLMPVNTVALKVPA CCEECCCEEEEECCC	13.85	30059200
307	Phosphorylation	TTLMPVNTVALKVPA CCEECCCEEEEECCC	13.85	-
311	Ubiquitination	PVNTVALKVPANPAS CCCEEEEECCCCCCC	36.11	-
318	Phosphorylation	KVPANPASVSTVPSK ECCCCCCCCCCCCCC	20.18	25159151
328	O-linked_Glycosylation	TVPSKLPTSSKPPGA CCCCCCCCCCCCCCC	56.95	30059200
329	O-linked_Glycosylation	VPSKLPTSSKPPGAV CCCCCCCCCCCCCCC	34.13	30059200
330	O-linked_Glycosylation	PSKLPTSSKPPGAVP CCCCCCCCCCCCCCC	52.22	30059200
338	O-linked_Glycosylation	KPPGAVPSNALTNPA CCCCCCCCCCCCCCC	28.30	30059200
342	O-linked_Glycosylation	AVPSNALTNPAPSKL CCCCCCCCCCCCCCC	36.42	30059200
347	O-linked_Glycosylation	ALTNPAPSKLPINST CCCCCCCCCCCCCCC	49.26	30059200
348	Ubiquitination	LTNPAPSKLPINSTR CCCCCCCCCCCCCCC	58.17	32015554
354	Phosphorylation	SKLPINSTRAGMVPS CCCCCCCCCCCCCCC	21.76	29759185
361	Phosphorylation	TRAGMVPSKVPTSMV CCCCCCCCCCCCCCE	34.57	-
362	Acetylation	RAGMVPSKVPTSMVL CCCCCCCCCCCCCEE	46.28	25953088
362	Ubiquitination	RAGMVPSKVPTSMVL CCCCCCCCCCCCCEE	46.28	20483786
365	O-linked_Glycosylation	MVPSKVPTSMVLTKV CCCCCCCCCCEEEEE	32.23	30059200
365	Phosphorylation	MVPSKVPTSMVLTKV CCCCCCCCCCEEEEE	32.23	-
366	O-linked_Glycosylation	VPSKVPTSMVLTKVS CCCCCCCCCEEEEEE	10.79	30059200
366	Phosphorylation	VPSKVPTSMVLTKVS CCCCCCCCCEEEEEE	10.79	19060867
370	O-linked_Glycosylation	VPTSMVLTKVSASTV CCCCCEEEEEEECCC	20.28	30059200
370	Phosphorylation	VPTSMVLTKVSASTV CCCCCEEEEEEECCC	20.28	22210691
371	Ubiquitination	PTSMVLTKVSASTVP CCCCEEEEEEECCCC	29.99	32015554
373	Phosphorylation	SMVLTKVSASTVPTD CCEEEEEEECCCCCC	20.32	30108239
375	Phosphorylation	VLTKVSASTVPTDGS EEEEEEECCCCCCCC	23.56	30108239
376	O-linked_Glycosylation	LTKVSASTVPTDGSS EEEEEECCCCCCCCC	30.16	OGP
376	Phosphorylation	LTKVSASTVPTDGSS EEEEEECCCCCCCCC	30.16	30108239
379	Phosphorylation	VSASTVPTDGSSRNE EEECCCCCCCCCCCC	48.97	22210691
383	Phosphorylation	TVPTDGSSRNEETPA CCCCCCCCCCCCCCC	44.66	21815630
388	Phosphorylation	GSSRNEETPAAPTPA CCCCCCCCCCCCCCC	16.43	20068231
393	Phosphorylation	EETPAAPTPAGATGG CCCCCCCCCCCCCCC	22.50	30108239
398	Phosphorylation	APTPAGATGGSSAWL CCCCCCCCCCCCCCC	40.95	21082442
401	Phosphorylation	PAGATGGSSAWLDSS CCCCCCCCCCCCCCC	20.44	30108239
402	Phosphorylation	AGATGGSSAWLDSSS CCCCCCCCCCCCCCC	27.09	30576142
407	Phosphorylation	GSSAWLDSSSENRGL CCCCCCCCCCCCCCC	33.33	30108239
408	Phosphorylation	SSAWLDSSSENRGLG CCCCCCCCCCCCCCC	41.14	21815630
409	Phosphorylation	SAWLDSSSENRGLGS CCCCCCCCCCCCCCC	42.73	21815630
416	Phosphorylation	SENRGLGSELSKPGV CCCCCCCCCCCCCCC	40.17	25159151
419	Phosphorylation	RGLGSELSKPGVLAS CCCCCCCCCCCCCHH	32.52	28355574
426	Phosphorylation	SKPGVLASQVDSPFS CCCCCCHHHCCCCCC	26.95	26074081
430	Phosphorylation	VLASQVDSPFSGCFE CCHHHCCCCCCCHHH	29.05	25159151
433	Phosphorylation	SQVDSPFSGCFEDLA HHCCCCCCCHHHHHH	37.73	26074081
442	Phosphorylation	CFEDLAISASTSLGM HHHHHHHHCCCCCCC	15.57	27302953
461	Ubiquitination	GPEENEYKSEGTFGI CCCCCCCCCCCCEEE	35.53	20483786
475	Phosphorylation	IHVAENPSIQLLEGN EEEECCCCEEEECCC	34.25	24173317
500	Ubiquitination	PRPQADRKFQEREVP CCCHHHHHHHCCCCC	52.53	1938049

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
9	Y	Phosphorylation	Kinase	ABL	P00519	PSP
30	Y	Phosphorylation	Kinase	ABL	P00519	PSP
71	Y	Phosphorylation	Kinase	ABL	P00519	PSP
442	S	Phosphorylation	Kinase	IKKB	O14920	PSP
442	S	Phosphorylation	Kinase	TBK1	Q9UHD2	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	RNF5	Q99942	PMID:20483786
-	K	Ubiquitination	E3 ubiquitin ligase	RNF125	Q96EQ8	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:23087404
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:19881509
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM25	Q14258	PMID:22626058

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
442	S	Phosphorylation		25636800
Following activation, phosphorylated by TBK1 at Ser-442 in the pLxIS motif.

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 MAVS_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MARH5_HUMAN	MARCH5	physical	21625535
BIRC2_HUMAN	BIRC2	physical	20097753
BIRC3_HUMAN	BIRC3	physical	20097753
HRSL4_HUMAN	RARRES3	physical	21203974
IKKE_HUMAN	IKBKE	physical	19380491
DDX58_HUMAN	DDX58	physical	16127453
IFIH1_HUMAN	IFIH1	physical	16127453
FADD_HUMAN	FADD	physical	16127453
KRR1_HUMAN	KRR1	physical	16127453
TRAF5_HUMAN	TRAF5	physical	20161788
NEMO_HUMAN	IKBKG	physical	20161788
DDX58_HUMAN	DDX58	physical	21903422
RIPK2_HUMAN	RIPK2	physical	21903422
BAG6_HUMAN	BAG6	physical	21903422
HECD3_HUMAN	HECTD3	physical	21903422
OAS3_HUMAN	OAS3	physical	21903422
PDS5A_HUMAN	PDS5A	physical	21903422
STAT1_HUMAN	STAT1	physical	21903422
TRAF2_HUMAN	TRAF2	physical	21903422
TRAF6_HUMAN	TRAF6	physical	21903422
UBE4A_HUMAN	UBE4A	physical	21903422
DDX58_HUMAN	DDX58	physical	22022264
E2AK2_HUMAN	EIF2AK2	physical	22022264
TRAF3_HUMAN	TRAF3	physical	22022264
PSA7_HUMAN	PSMA7	physical	19734229
IFIH1_HUMAN	IFIH1	physical	19881509
PCBP2_HUMAN	PCBP2	physical	19881509
ITCH_HUMAN	ITCH	physical	19881509
TRAF3_HUMAN	TRAF3	physical	21200404
IKKE_HUMAN	IKBKE	physical	21200404
HRSL4_HUMAN	RARRES3	physical	21200404
TSN6_HUMAN	TSPAN6	physical	22908223
TRAF3_HUMAN	TRAF3	physical	16858409
SRC_HUMAN	SRC	physical	19419966
NEMO_HUMAN	IKBKG	physical	23028469
TBK1_HUMAN	TBK1	physical	23028469
NFIP1_HUMAN	NDFIP1	physical	23087404
MUL1_HUMAN	MUL1	physical	23399697
DDX58_HUMAN	DDX58	physical	20434986
TOM70_HUMAN	TOMM70A	physical	20628368
MFN1_HUMAN	MFN1	physical	20661427
MFN2_HUMAN	MFN2	physical	20661427
TRAF3_HUMAN	TRAF3	physical	22901541
STING_HUMAN	TMEM173	physical	24622840
SMUF2_HUMAN	SMURF2	physical	24729608
UBXN1_HUMAN	UBXN1	physical	23545497
TRAF6_HUMAN	TRAF6	physical	23545497
TRAF3_HUMAN	TRAF3	physical	23545497
MIB2_HUMAN	MIB2	physical	25142606
ABL1_HUMAN	ABL1	physical	19914245
IFIT3_HUMAN	IFIT3	physical	21813773
TBK1_HUMAN	TBK1	physical	21813773
TRAF2_HUMAN	TRAF2	physical	21516116
TRAF1_HUMAN	TRAF1	physical	26221961
TRAF2_HUMAN	TRAF2	physical	26221961
TRAF3_HUMAN	TRAF3	physical	26221961
TRAF5_HUMAN	TRAF5	physical	26221961
TRAF6_HUMAN	TRAF6	physical	26221961
MAVS_HUMAN	MAVS	physical	26221961
TRI14_HUMAN	TRIM14	physical	24379373
NEMO_HUMAN	IKBKG	physical	24379373
IRF3_HUMAN	IRF3	physical	24379373
KC1E_HUMAN	CSNK1E	physical	26928339
TRI31_HUMAN	TRIM31	physical	27992402
RN114_HUMAN	RNF114	physical	28625874
PRKN_HUMAN	PARK2	physical	27348524
RNF31_HUMAN	RNF31	physical	27348524
TRAF3_HUMAN	TRAF3	physical	27348524
TRAF2_HUMAN	TRAF2	physical	27348524
TRAF5_HUMAN	TRAF5	physical	27348524
TRAF6_HUMAN	TRAF6	physical	27348524
TBK1_HUMAN	TBK1	physical	29125880
IKKE_HUMAN	IKBKE	physical	29125880
TRAF2_HUMAN	TRAF2	physical	29125880
TRAF3_HUMAN	TRAF3	physical	29125880
TRAF6_HUMAN	TRAF6	physical	29125880
HRSL4_HUMAN	RARRES3	physical	27312109
IFIH1_HUMAN	IFIH1	physical	27312109
TBK1_HUMAN	TBK1	physical	28346439
MAVS_HUMAN	MAVS	physical	28934360

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 MAVS_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-152; SER-165 ANDSER-222, AND MASS 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, 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-152; SER-157; THR-163;SER-165; SER-222; SER-233; THR-234; SER-253 AND SER-258, 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-152; SER-165 ANDSER-222, AND MASS SPECTROMETRY.	18691976 [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-222, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND MASSSPECTROMETRY.	18088087 [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-222, AND MASSSPECTROMETRY.	16964243 [Abstract]

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