dbPTM

TNAP3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TNAP3_HUMAN
UniProt AC	P21580
Protein Name	Tumor necrosis factor alpha-induced protein 3
Gene Name	TNFAIP3
Organism	Homo sapiens (Human).
Sequence Length	790
Subcellular Localization	Cytoplasm. Nucleus. Lysosome. A20p50: Cytoplasm.
Protein Description	Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquitinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquitinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system. Required for LPS-induced production of proinflammatory cytokines and IFN beta in LPS-tolerized macrophages..
Protein Sequence	MAEQVLPQALYLSNMRKAVKIRERTPEDIFKPTNGIIHHFKTMHRYTLEMFRTCQFCPQFREIIHKALIDRNIQATLESQKKLNWCREVRKLVALKTNGDGNCLMHATSQYMWGVQDTDLVLRKALFSTLKETDTRNFKFRWQLESLKSQEFVETGLCYDTRNWNDEWDNLIKMASTDTPMARSGLQYNSLEEIHIFVLCNILRRPIIVISDKMLRSLESGSNFAPLKVGGIYLPLHWPAQECYRYPIVLGYDSHHFVPLVTLKDSGPEIRAVPLVNRDRGRFEDLKVHFLTDPENEMKEKLLKEYLMVIEIPVQGWDHGTTHLINAAKLDEANLPKEINLVDDYFELVQHEYKKWQENSEQGRREGHAQNPMEPSVPQLSLMDVKCETPNCPFFMSVNTQPLCHECSERRQKNQNKLPKLNSKPGPEGLPGMALGASRGEAYEPLAWNPEESTGGPHSAPPTAPSPFLFSETTAMKCRSPGCPFTLNVQHNGFCERCHNARQLHASHAPDHTRHLDPGKCQACLQDVTRTFNGICSTCFKRTTAEASSSLSTSLPPSCHQRSKSDPSRLVRSPSPHSCHRAGNDAPAGCLSQAARTPGDRTGTSKCRKAGCVYFGTPENKGFCTLCFIEYRENKHFAAASGKVSPTASRFQNTIPCLGRECGTLGSTMFEGYCQKCFIEAQNQRFHEAKRTEEQLRSSQRRDVPRTTQSTSRPKCARASCKNILACRSEELCMECQHPNQRMGPGAHRGEPAPEDPPKQRCRAPACDHFGNAKCNGYCNECFQFKQMYG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEQVLPQA ------CHHCHHHHH	18.87	22814378
11	Phosphorylation	QVLPQALYLSNMRKA CHHHHHHHHHHHHHH	15.88	23401153
42	Phosphorylation	GIIHHFKTMHRYTLE CCHHHHHHHHHHHHH	19.78	30576142
53	Phosphorylation	YTLEMFRTCQFCPQF HHHHHHHHCCCCHHH	10.21	30576142
66	Ubiquitination	QFREIIHKALIDRNI HHHHHHHHHHHCCCH	34.18	-
76	Phosphorylation	IDRNIQATLESQKKL HCCCHHHHHHHHHHH	18.06	23403867
79	Phosphorylation	NIQATLESQKKLNWC CHHHHHHHHHHHHHH	50.87	23403867
81	Ubiquitination	QATLESQKKLNWCRE HHHHHHHHHHHHHHH	69.38	21906983
81	Acetylation	QATLESQKKLNWCRE HHHHHHHHHHHHHHH	69.38	129897
82	Ubiquitination	ATLESQKKLNWCREV HHHHHHHHHHHHHHH	39.14	22817900
108	Phosphorylation	GNCLMHATSQYMWGV CCCEEEECCCHHCCC	11.15	22617229
118	Phosphorylation	YMWGVQDTDLVLRKA HHCCCCCHHHHHHHH	17.72	22617229
124	Ubiquitination	DTDLVLRKALFSTLK CHHHHHHHHHHHHHH	45.33	25015289
128	Phosphorylation	VLRKALFSTLKETDT HHHHHHHHHHHHCCC	33.41	22617229
129	Phosphorylation	LRKALFSTLKETDTR HHHHHHHHHHHCCCC	34.22	22617229
131	Ubiquitination	KALFSTLKETDTRNF HHHHHHHHHCCCCCE	59.67	25015289
139	Ubiquitination	ETDTRNFKFRWQLES HCCCCCEEEEEEHHH	37.25	-
141	Ubiquitination	DTRNFKFRWQLESLK CCCCEEEEEEHHHCC	22.33	21963094
142	Ubiquitination	TRNFKFRWQLESLKS CCCEEEEEEHHHCCC	15.39	22817900
159	Phosphorylation	FVETGLCYDTRNWND HHHCCCCCCCCCCCH	25.95	27642862
161	Phosphorylation	ETGLCYDTRNWNDEW HCCCCCCCCCCCHHH	10.22	30108239
179	Phosphorylation	IKMASTDTPMARSGL HHHHCCCCCCCCCCC	18.30	-
217	Phosphorylation	ISDKMLRSLESGSNF ECHHHHHHCCCCCCC	32.31	30001349
220	Phosphorylation	KMLRSLESGSNFAPL HHHHHCCCCCCCCCE	53.46	23401153
222	Phosphorylation	LRSLESGSNFAPLKV HHHCCCCCCCCCEEE	37.75	30108239
287	Ubiquitination	RGRFEDLKVHFLTDP CCCHHCCEEEECCCC	46.08	29967540
299	Ubiquitination	TDPENEMKEKLLKEY CCCCHHHHHHHHHHH	45.58	29967540
301	Ubiquitination	PENEMKEKLLKEYLM CCHHHHHHHHHHHCC	54.31	-
306	Phosphorylation	KEKLLKEYLMVIEIP HHHHHHHHCCEEEEC	9.86	19413330
307	Ubiquitination	EKLLKEYLMVIEIPV HHHHHHHCCEEEECC	2.01	22817900
321	Phosphorylation	VQGWDHGTTHLINAA CCCCCCCHHHEEEHH	13.97	19413330
322	Phosphorylation	QGWDHGTTHLINAAK CCCCCCHHHEEEHHH	21.19	19413330
328	Ubiquitination	TTHLINAAKLDEANL HHHEEEHHHHCCCCC	14.41	22817900
337	Ubiquitination	LDEANLPKEINLVDD HCCCCCCCCCCCCHH	74.52	29967540
354	Ubiquitination	ELVQHEYKKWQENSE HHHHHHHHHHHHCCH	44.55	21963094
355	Ubiquitination	LVQHEYKKWQENSEQ HHHHHHHHHHHCCHH	53.89	22817900
376	Phosphorylation	AQNPMEPSVPQLSLM CCCCCCCCCCCEEEE	32.87	30108239
381	Phosphorylation	EPSVPQLSLMDVKCE CCCCCCEEEEEEEEC	19.19	21712546
397	Phosphorylation	PNCPFFMSVNTQPLC CCCCEEEEECCCCCC	13.68	30108239
400	Phosphorylation	PFFMSVNTQPLCHEC CEEEEECCCCCCHHH	29.43	30108239
420	Acetylation	KNQNKLPKLNSKPGP HHHCCCCCCCCCCCC	71.40	25953088
423	Phosphorylation	NKLPKLNSKPGPEGL CCCCCCCCCCCCCCC	51.14	30108239
424	Ubiquitination	KLPKLNSKPGPEGLP CCCCCCCCCCCCCCC	53.58	29967540
430	Ubiquitination	SKPGPEGLPGMALGA CCCCCCCCCCCCCCC	2.94	21963094
438	Phosphorylation	PGMALGASRGEAYEP CCCCCCCCCCCCCCC	38.73	28102081
443	Phosphorylation	GASRGEAYEPLAWNP CCCCCCCCCCCCCCC	17.49	22210691
453	Phosphorylation	LAWNPEESTGGPHSA CCCCCCCCCCCCCCC	30.59	26657352
454	Phosphorylation	AWNPEESTGGPHSAP CCCCCCCCCCCCCCC	49.81	30108239
459	Phosphorylation	ESTGGPHSAPPTAPS CCCCCCCCCCCCCCC	45.67	19276368
463	Phosphorylation	GPHSAPPTAPSPFLF CCCCCCCCCCCCCCC	50.57	30108239
466	Phosphorylation	SAPPTAPSPFLFSET CCCCCCCCCCCCCCC	26.31	30108239
471	Phosphorylation	APSPFLFSETTAMKC CCCCCCCCCCCEEEC	35.86	28634298
473	Phosphorylation	SPFLFSETTAMKCRS CCCCCCCCCEEECCC	20.75	28122231
474	Phosphorylation	PFLFSETTAMKCRSP CCCCCCCCEEECCCC	22.24	28122231
480	Phosphorylation	TTAMKCRSPGCPFTL CCEEECCCCCCCCEE	34.80	29214152
502	Ubiquitination	CERCHNARQLHASHA HHHCCCHHHHHHHCC	44.93	22817900
507	Phosphorylation	NARQLHASHAPDHTR CHHHHHHHCCCCCCC	14.94	28348404
509	Ubiquitination	RQLHASHAPDHTRHL HHHHHHCCCCCCCCC	14.55	23000965
520	Ubiquitination	TRHLDPGKCQACLQD CCCCCCCCHHHHHHH	28.67	21906983
537	Phosphorylation	RTFNGICSTCFKRTT HHHCCHHHHHHHHCC	26.70	30108239
538	Phosphorylation	TFNGICSTCFKRTTA HHCCHHHHHHHHCCH	19.97	30108239
541	Ubiquitination	GICSTCFKRTTAEAS CHHHHHHHHCCHHHH	51.48	21906983
548	Phosphorylation	KRTTAEASSSLSTSL HHCCHHHHHHHCCCC	16.38	30108239
549	Phosphorylation	RTTAEASSSLSTSLP HCCHHHHHHHCCCCC	42.20	30108239
550	Phosphorylation	TTAEASSSLSTSLPP CCHHHHHHHCCCCCC	24.68	30108239
552	Phosphorylation	AEASSSLSTSLPPSC HHHHHHHCCCCCCCH	20.21	30108239
553	Phosphorylation	EASSSLSTSLPPSCH HHHHHHCCCCCCCHH	39.31	30108239
554	Phosphorylation	ASSSLSTSLPPSCHQ HHHHHCCCCCCCHHC	35.19	30108239
563	Phosphorylation	PPSCHQRSKSDPSRL CCCHHCCCCCCHHHH	29.91	26699800
565	Phosphorylation	SCHQRSKSDPSRLVR CHHCCCCCCHHHHCC	56.87	25056879
568	Phosphorylation	QRSKSDPSRLVRSPS CCCCCCHHHHCCCCC	43.14	22817900
573	Phosphorylation	DPSRLVRSPSPHSCH CHHHHCCCCCHHCCC	23.42	23401153
575	Phosphorylation	SRLVRSPSPHSCHRA HHHCCCCCHHCCCCC	36.17	23401153
578	Phosphorylation	VRSPSPHSCHRAGND CCCCCHHCCCCCCCC	18.27	30108239
592	Phosphorylation	DAPAGCLSQAARTPG CCCCCHHHHHHCCCC	23.11	30108239
597	O-linked_Glycosylation	CLSQAARTPGDRTGT HHHHHHCCCCCCCCC	27.22	29351928
597	Phosphorylation	CLSQAARTPGDRTGT HHHHHHCCCCCCCCC	27.22	29214152
609	Ubiquitination	TGTSKCRKAGCVYFG CCCCCCCCCCEEEEC	59.61	29967540
614	Phosphorylation	CRKAGCVYFGTPENK CCCCCEEEECCCCCC	10.60	20090780
617	Phosphorylation	AGCVYFGTPENKGFC CCEEEECCCCCCCEE	19.96	29396449
621	Ubiquitination	YFGTPENKGFCTLCF EECCCCCCCEEEEEE	52.26	-
625	Phosphorylation	PENKGFCTLCFIEYR CCCCCEEEEEEEEEC	25.05	-
631	Phosphorylation	CTLCFIEYRENKHFA EEEEEEEECCCCCEE	20.57	20090780
635	Ubiquitination	FIEYRENKHFAAASG EEEECCCCCEEHHCC	35.03	-
641	Phosphorylation	NKHFAAASGKVSPTA CCCEEHHCCCCCCCH	34.13	23927012
643	Ubiquitination	HFAAASGKVSPTASR CEEHHCCCCCCCHHH	36.72	21963094
645	Phosphorylation	AAASGKVSPTASRFQ EHHCCCCCCCHHHHH	21.73	23927012
647	Phosphorylation	ASGKVSPTASRFQNT HCCCCCCCHHHHHCC	29.74	23927012
649	Phosphorylation	GKVSPTASRFQNTIP CCCCCCHHHHHCCCC	35.79	23927012
654	Phosphorylation	TASRFQNTIPCLGRE CHHHHHCCCCCCCCC	18.60	28555341
673	Phosphorylation	GSTMFEGYCQKCFIE CCHHCHHHHHHHHHH	5.63	20090780
676	Ubiquitination	MFEGYCQKCFIEAQN HCHHHHHHHHHHHHH	27.79	-
692	Phosphorylation	RFHEAKRTEEQLRSS HHHHHHHHHHHHHHH	43.07	29449344
698	Phosphorylation	RTEEQLRSSQRRDVP HHHHHHHHHHHCCCC	39.14	29449344
699	Phosphorylation	TEEQLRSSQRRDVPR HHHHHHHHHHCCCCC	22.67	29449344
715	Ubiquitination	TQSTSRPKCARASCK CCCCCCHHHHHHHHH	39.14	22817900
722	Acetylation	KCARASCKNILACRS HHHHHHHHHHEECCC	44.52	25953088
722	Ubiquitination	KCARASCKNILACRS HHHHHHHHHHEECCC	44.52	23000965
729	Phosphorylation	KNILACRSEELCMEC HHHEECCCHHHHHHC	34.99	30108239
778	Phosphorylation	GNAKCNGYCNECFQF CCCCCCCCHHHHHHH	4.33	20090780

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
381	S	Phosphorylation	Kinase	IKKB	O14920	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	TNFAIP3	P21580	PMID:21095585

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TNAP3_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 TNAP3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TAXB1_HUMAN	TAX1BP1	physical	10435631
TRAF1_HUMAN	TRAF1	physical	8692885
TRAF2_HUMAN	TRAF2	physical	8692885
TNAP3_HUMAN	TNFAIP3	physical	8692885
NEMO_HUMAN	IKBKG	physical	10755617
TNIP1_HUMAN	TNIP1	physical	10385526
1433Z_HUMAN	YWHAZ	physical	9299557
1433F_HUMAN	YWHAH	physical	9299557
1433B_HUMAN	YWHAB	physical	8702721
1433F_HUMAN	YWHAH	physical	8702721
1433Z_HUMAN	YWHAZ	physical	8702721
1433E_HUMAN	YWHAE	physical	8702721
IKKA_HUMAN	CHUK	physical	11594795
LAMP1_HUMAN	LAMP1	physical	18329387
AL9A1_HUMAN	ALDH9A1	physical	19615732
GCSP_HUMAN	GLDC	physical	19615732
KIF11_HUMAN	KIF11	physical	19615732
MCM6_HUMAN	MCM6	physical	19615732
NDUS1_HUMAN	NDUFS1	physical	19615732
2AAB_HUMAN	PPP2R1B	physical	19615732
RINI_HUMAN	RNH1	physical	19615732
1433B_HUMAN	YWHAB	physical	19615732
1433F_HUMAN	YWHAH	physical	19615732
CNKR2_HUMAN	CNKSR2	physical	19615732
FBX3_HUMAN	FBXO3	physical	19615732
TBK1_HUMAN	TBK1	physical	19615732
PP6R3_HUMAN	PPP6R3	physical	19615732
LRC47_HUMAN	LRRC47	physical	19615732
RIPK1_HUMAN	RIPK1	physical	15258597
UBC_HUMAN	UBC	physical	21095585
IRF7_HUMAN	IRF7	physical	20392859
M3K5_HUMAN	MAP3K5	physical	20448643
UBC_HUMAN	UBC	physical	20622874
TRAF6_HUMAN	TRAF6	physical	20622874
TBK1_HUMAN	TBK1	physical	21885437
TNAP3_HUMAN	TNFAIP3	physical	8797804
TNIP2_HUMAN	TNIP2	physical	11390377
LMP1_EBVB9	LMP1	physical	10544141
TRAF2_HUMAN	TRAF2	physical	10544141
TNIP3_HUMAN	TNIP3	physical	17088249
TNIP2_HUMAN	TNIP2	physical	21266526
LAPM5_HUMAN	LAPTM5	physical	22733818
CCD50_HUMAN	CCDC50	physical	18029035
1433B_HUMAN	YWHAB	physical	18029035
TNIP1_HUMAN	TNIP1	physical	18029035
TNIP2_HUMAN	TNIP2	physical	18029035
TNIP1_HUMAN	TNIP1	physical	11389905
TNIP2_HUMAN	TNIP2	physical	11389905
TNAP3_HUMAN	TNFAIP3	physical	11389905
TAXB1_HUMAN	TAX1BP1	physical	11389905
NEMO_HUMAN	IKBKG	physical	11389905
RNF11_HUMAN	RNF11	physical	23018911
TRAF6_HUMAN	TRAF6	physical	23018911
TAXB1_HUMAN	TAX1BP1	physical	23018911
TNIP1_HUMAN	TNIP1	physical	12586352
UBC_HUMAN	UBC	physical	23032187
HOIL1_HUMAN	RBCK1	physical	23032186
RNF31_HUMAN	RNF31	physical	23032186
SHRPN_HUMAN	SHARPIN	physical	23032186
NEMO_HUMAN	IKBKG	physical	23032186
UBC_HUMAN	UBC	physical	23032186
RIPK1_HUMAN	RIPK1	physical	22585859
UBE2N_HUMAN	UBE2N	physical	15258597
TRIM2_HUMAN	TRIM2	physical	23105109
RNF5_HUMAN	RNF5	physical	23105109
TRAF6_HUMAN	TRAF6	physical	23105109
RNF14_HUMAN	RNF14	physical	23105109
HOIL1_HUMAN	RBCK1	physical	23105109
RNF12_HUMAN	RLIM	physical	23105109
TRIM3_HUMAN	TRIM3	physical	23105109
TRIM8_HUMAN	TRIM8	physical	23105109
TRIM5_HUMAN	TRIM5	physical	23105109
P53_HUMAN	TP53	physical	23471665
AXIN1_HUMAN	AXIN1	physical	23671587
1433E_HUMAN	YWHAE	physical	21988832
1433Z_HUMAN	YWHAZ	physical	21988832
TNIP1_HUMAN	TNIP1	physical	21988832
TNAP3_HUMAN	TNFAIP3	physical	24008839
NFKB2_HUMAN	NFKB2	physical	24008839
BIRC3_HUMAN	BIRC3	physical	24008839
TRAF2_HUMAN	TRAF2	physical	24008839
P53_HUMAN	TP53	physical	24099634
OCLN_HUMAN	OCLN	physical	22031828
UBC_HUMAN	UBC	physical	23827681
TNAP3_HUMAN	TNFAIP3	physical	25165885
TNIP1_HUMAN	TNIP1	physical	25165885
1433T_HUMAN	YWHAQ	physical	25165885
RN114_HUMAN	RNF114	physical	25165885
TNAP3_HUMAN	TNFAIP3	physical	15258597
UB2D1_HUMAN	UBE2D1	physical	15258597
TNAP3_HUMAN	TNFAIP3	physical	25416956
TRAF2_HUMAN	TRAF2	physical	25416956
TNIP1_HUMAN	TNIP1	physical	25416956
ARRD3_HUMAN	ARRDC3	physical	25416956
TNIP3_HUMAN	TNIP3	physical	25416956
UBC_HUMAN	UBC	physical	19373254
UBC_HUMAN	UBC	physical	14748687
UBC_HUMAN	UBC	physical	22099304
UBC_HUMAN	UBC	physical	18029035
TRAF6_HUMAN	TRAF6	physical	18164316
TRAF6_HUMAN	TRAF6	physical	15334086
UBC_HUMAN	UBC	physical	15334086
MTOR_HUMAN	MTOR	physical	26043155
UBC_HUMAN	UBC	physical	27732584
OTUD5_HUMAN	OTUD5	physical	28514442
PCDB5_HUMAN	PCDHB5	physical	28514442
RN166_HUMAN	RNF166	physical	28514442
SHKB1_HUMAN	SHKBP1	physical	28514442
UBB_HUMAN	UBB	physical	28514442
AN13D_HUMAN	ANKRD13D	physical	28514442
TBC24_HUMAN	TBC1D24	physical	28514442
SRC_HUMAN	SRC	physical	28514442
BACD3_HUMAN	KCTD10	physical	28514442
AIDA_HUMAN	AIDA	physical	28514442
RN114_HUMAN	RNF114	physical	28514442
NED4L_HUMAN	NEDD4L	physical	28514442
ARI1_HUMAN	ARIH1	physical	28514442
TAXB1_HUMAN	TAX1BP1	physical	28514442
TRAF6_HUMAN	TRAF6	physical	28244869
TNAP3_HUMAN	TNFAIP3	physical	28244869
SNAI1_HUMAN	SNAI1	physical	28892081
UB2D1_HUMAN	UBE2D1	physical	28892081

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 TNAP3_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-459, AND MASSSPECTROMETRY.	19690332 [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-575, AND MASSSPECTROMETRY.	17081983 [Abstract]