dbPTM

TFR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TFR1_HUMAN
UniProt AC	P02786
Protein Name	Transferrin receptor protein 1
Gene Name	TFRC
Organism	Homo sapiens (Human).
Sequence Length	760
Subcellular Localization	Cell membrane Single-pass type II membrane protein . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Transferrin receptor protein 1, serum form: Secreted .
Protein Description	Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. Positively regulates T and B cell proliferation through iron uptake. [PubMed: 26642240; (Microbial infection) Acts as a receptor for new-world arenaviruses: Guanarito, Junin and Machupo virus.]
Protein Sequence	MMDQARSAFSNLFGGEPLSYTRFSLARQVDGDNSHVEMKLAVDEEENADNNTKANVTKPKRCSGSICYGTIAVIVFFLIGFMIGYLGYCKGVEPKTECERLAGTESPVREEPGEDFPAARRLYWDDLKRKLSEKLDSTDFTGTIKLLNENSYVPREAGSQKDENLALYVENQFREFKLSKVWRDQHFVKIQVKDSAQNSVIIVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTKKDFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHTQFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTDSTCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEPDHYVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDMVLKDGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFTYINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQFLYQDSNWASKVEKLTLDNAAFPFLAYSGIPAVSFCFCEDTDYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIKLTHDVELNLDYERYNSQLLSFVRDLNQYRADIKEMGLSLQWLYSARGDFFRATSRLTTDFGNAEKTDRFVMKKLNDRVMRVEYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRKQNNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNEF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MMDQARSAFSNLFG -CHHHHHHHHHHHHC	36.36	21945579
10	Phosphorylation	DQARSAFSNLFGGEP HHHHHHHHHHHCCCC	32.13	21945579
19	Phosphorylation	LFGGEPLSYTRFSLA HHCCCCCCEEEEEEE	34.86	21945579
20	Phosphorylation	FGGEPLSYTRFSLAR HCCCCCCEEEEEEEE	15.04	25159151
21	Phosphorylation	GGEPLSYTRFSLARQ CCCCCCEEEEEEEEE	23.12	21945579
24	Phosphorylation	PLSYTRFSLARQVDG CCCEEEEEEEEECCC	20.16	10531064
34	Phosphorylation	RQVDGDNSHVEMKLA EECCCCCCCEEEEEE	33.38	23401153
39	Ubiquitination	DNSHVEMKLAVDEEE CCCCEEEEEEECCHH	21.57	21906983
52	Phosphorylation	EENADNNTKANVTKP HHCCCCCCCCCCCCC	37.48	25159151
53	Acetylation	ENADNNTKANVTKPK HCCCCCCCCCCCCCC	39.84	7960211
53	Ubiquitination	ENADNNTKANVTKPK HCCCCCCCCCCCCCC	39.84	21906983
53	2-Hydroxyisobutyrylation	ENADNNTKANVTKPK HCCCCCCCCCCCCCC	39.84	-
58	Ubiquitination	NTKANVTKPKRCSGS CCCCCCCCCCCCCCC	44.23	21906983
60	Ubiquitination	KANVTKPKRCSGSIC CCCCCCCCCCCCCHH	68.54	-
62	S-palmitoylation	NVTKPKRCSGSICYG CCCCCCCCCCCHHHH	7.25	3582362
67	S-palmitoylation	KRCSGSICYGTIAVI CCCCCCHHHHHHHHH	2.48	2398066
95	Acetylation	YCKGVEPKTECERLA HHCCCCCCHHHHHHC	43.37	26051181
104	O-linked_Glycosylation	ECERLAGTESPVREE HHHHHCCCCCCCCCC	27.90	1421756
104	Phosphorylation	ECERLAGTESPVREE HHHHHCCCCCCCCCC	27.90	26434776
104	O-linked_Glycosylation	ECERLAGTESPVREE HHHHHCCCCCCCCCC	27.90	1421756
106	Phosphorylation	ERLAGTESPVREEPG HHHCCCCCCCCCCCC	28.65	25159151
106	O-linked_Glycosylation	ERLAGTESPVREEPG HHHCCCCCCCCCCCC	28.65	OGP
123	Phosphorylation	FPAARRLYWDDLKRK CHHHHHHCHHHHHHH	12.65	20068231
128	Acetylation	RLYWDDLKRKLSEKL HHCHHHHHHHHHHHC	55.25	27452117
128	Ubiquitination	RLYWDDLKRKLSEKL HHCHHHHHHHHHHHC	55.25	-
128	2-Hydroxyisobutyrylation	RLYWDDLKRKLSEKL HHCHHHHHHHHHHHC	55.25	-
128	Succinylation	RLYWDDLKRKLSEKL HHCHHHHHHHHHHHC	55.25	23954790
130	Ubiquitination	YWDDLKRKLSEKLDS CHHHHHHHHHHHCCC	55.57	-
132	Phosphorylation	DDLKRKLSEKLDSTD HHHHHHHHHHCCCCC	35.40	29457462
134	Ubiquitination	LKRKLSEKLDSTDFT HHHHHHHHCCCCCCC	54.97	-
134	2-Hydroxyisobutyrylation	LKRKLSEKLDSTDFT HHHHHHHHCCCCCCC	54.97	-
143	O-linked_Glycosylation	DSTDFTGTIKLLNEN CCCCCCCCEEECCCC	16.33	OGP
145	Ubiquitination	TDFTGTIKLLNENSY CCCCCCEEECCCCCC	46.92	21906983
145	2-Hydroxyisobutyrylation	TDFTGTIKLLNENSY CCCCCCEEECCCCCC	46.92	-
161	Ubiquitination	PREAGSQKDENLALY CCCCCCCCCCCHHHH	69.57	21906983
161	2-Hydroxyisobutyrylation	PREAGSQKDENLALY CCCCCCCCCCCHHHH	69.57	-
168	Phosphorylation	KDENLALYVENQFRE CCCCHHHHHHHHHHH	10.50	-
177	Ubiquitination	ENQFREFKLSKVWRD HHHHHHHHCHHHHCC	47.28	-
189	Ubiquitination	WRDQHFVKIQVKDSA HCCCCEEEEEECCCC	26.86	-
189	2-Hydroxyisobutyrylation	WRDQHFVKIQVKDSA HCCCCEEEEEECCCC	26.86	-
189	Acetylation	WRDQHFVKIQVKDSA HCCCCEEEEEECCCC	26.86	27452117
193	Ubiquitination	HFVKIQVKDSAQNSV CEEEEEECCCCCCEE	29.59	-
195	Phosphorylation	VKIQVKDSAQNSVII EEEEECCCCCCEEEE	26.49	21712546
199	Phosphorylation	VKDSAQNSVIIVDKN ECCCCCCEEEEEECC	11.56	21712546
205	Ubiquitination	NSVIIVDKNGRLVYL CEEEEEECCCCEEEE	50.86	21906983
205	2-Hydroxyisobutyrylation	NSVIIVDKNGRLVYL CEEEEEECCCCEEEE	50.86	-
211	Phosphorylation	DKNGRLVYLVENPGG ECCCCEEEEEECCCC	15.04	28152594
219	Phosphorylation	LVENPGGYVAYSKAA EEECCCCEEEECEEE	6.45	28152594
222	Phosphorylation	NPGGYVAYSKAATVT CCCCEEEECEEEEEE	10.72	28152594
223	Phosphorylation	PGGYVAYSKAATVTG CCCEEEECEEEEEEE	13.19	28152594
224	Ubiquitination	GGYVAYSKAATVTGK CCEEEECEEEEEEEC	29.39	21906983
231	Ubiquitination	KAATVTGKLVHANFG EEEEEEECEEECCCC	37.66	-
240	Ubiquitination	VHANFGTKKDFEDLY EECCCCCCCCHHHHC	51.21	-
240	2-Hydroxyisobutyrylation	VHANFGTKKDFEDLY EECCCCCCCCHHHHC	51.21	-
241	Ubiquitination	HANFGTKKDFEDLYT ECCCCCCCCHHHHCC	68.44	-
248	Phosphorylation	KDFEDLYTPVNGSIV CCHHHHCCCCCCEEE	28.23	21601212
251	N-linked_Glycosylation	EDLYTPVNGSIVIVR HHHCCCCCCEEEEEE	39.43	10531064
251	N-linked_Glycosylation	EDLYTPVNGSIVIVR HHHCCCCCCEEEEEE	39.43	10531064
261	Ubiquitination	IVIVRAGKITFAEKV EEEEECCEEEHHHHH	37.27	-
261	2-Hydroxyisobutyrylation	IVIVRAGKITFAEKV EEEEECCEEEHHHHH	37.27	-
282	Phosphorylation	NAIGVLIYMDQTKFP CEEEEEEEECCCCCC	7.17	-
286	Phosphorylation	VLIYMDQTKFPIVNA EEEEECCCCCCEECE	30.32	-
317	N-linked_Glycosylation	TPGFPSFNHTQFPPS CCCCCCCCCCCCCCC	41.45	10531064
317	N-linked_Glycosylation	TPGFPSFNHTQFPPS CCCCCCCCCCCCCCC	41.45	10531064
326	Phosphorylation	TQFPPSRSSGLPNIP CCCCCCCCCCCCCCC	32.85	23911959
327	Phosphorylation	QFPPSRSSGLPNIPV CCCCCCCCCCCCCCH	43.15	23911959
338	Phosphorylation	NIPVQTISRAAAEKL CCCHHHHCHHHHHHH	21.18	21712546
344	Ubiquitination	ISRAAAEKLFGNMEG HCHHHHHHHHCCCCC	44.37	-
344	2-Hydroxyisobutyrylation	ISRAAAEKLFGNMEG HCHHHHHHHHCCCCC	44.37	-
353	Glutathionylation	FGNMEGDCPSDWKTD HCCCCCCCCCCCCCC	5.23	22555962
358	Ubiquitination	GDCPSDWKTDSTCRM CCCCCCCCCCCCEEE	47.66	-
371	Ubiquitination	RMVTSESKNVKLTVS EEECCCCCCCEEEHH	62.80	-
374	Ubiquitination	TSESKNVKLTVSNVL CCCCCCCEEEHHHHH	48.08	-
376	Phosphorylation	ESKNVKLTVSNVLKE CCCCCEEEHHHHHHH	19.03	21955146
378	Phosphorylation	KNVKLTVSNVLKEIK CCCEEEHHHHHHHHH	18.91	21955146
382	Ubiquitination	LTVSNVLKEIKILNI EEHHHHHHHHHHHCH	53.78	21906983
382	Acetylation	LTVSNVLKEIKILNI EEHHHHHHHHHHHCH	53.78	27452117
385	Ubiquitination	SNVLKEIKILNIFGV HHHHHHHHHHCHHEH	42.08	-
394	Acetylation	LNIFGVIKGFVEPDH HCHHEHHCCCCCCCE	43.84	20167786
394	Ubiquitination	LNIFGVIKGFVEPDH HCHHEHHCCCCCCCE	43.84	-
402	Phosphorylation	GFVEPDHYVVVGAQR CCCCCCEEEEEEEEC	11.43	28152594
418	Acetylation	AWGPGAAKSGVGTAL CCCCCHHHCCHHHHH	47.40	20167786
418	Ubiquitination	AWGPGAAKSGVGTAL CCCCCHHHCCHHHHH	47.40	21906983
418	2-Hydroxyisobutyrylation	AWGPGAAKSGVGTAL CCCCCHHHCCHHHHH	47.40	-
419	Phosphorylation	WGPGAAKSGVGTALL CCCCHHHCCHHHHHH	33.70	21712546
432	Sulfoxidation	LLLKLAQMFSDMVLK HHHHHHHHHHHHHHC	2.63	21406390
439	2-Hydroxyisobutyrylation	MFSDMVLKDGFQPSR HHHHHHHCCCCCCCC	44.38	-
480	Phosphorylation	SLHLKAFTYINLDKA HCHHHEEEEEECCCH	28.49	23286773
481	Phosphorylation	LHLKAFTYINLDKAV CHHHEEEEEECCCHH	4.95	23286773
486	Ubiquitination	FTYINLDKAVLGTSN EEEEECCCHHHCCCC	43.49	-
486	2-Hydroxyisobutyrylation	FTYINLDKAVLGTSN EEEEECCCHHHCCCC	43.49	-
491	Phosphorylation	LDKAVLGTSNFKVSA CCCHHHCCCCCEECC	19.14	23286773
492	Phosphorylation	DKAVLGTSNFKVSAS CCHHHCCCCCEECCC	38.17	23286773
495	2-Hydroxyisobutyrylation	VLGTSNFKVSASPLL HHCCCCCEECCCHHH	39.26	-
497	Phosphorylation	GTSNFKVSASPLLYT CCCCCEECCCHHHHH	24.50	23286773
499	Phosphorylation	SNFKVSASPLLYTLI CCCEECCCHHHHHHH	14.47	20068231
503	Phosphorylation	VSASPLLYTLIEKTM ECCCHHHHHHHHHHH	13.74	20068231
504	Phosphorylation	SASPLLYTLIEKTMQ CCCHHHHHHHHHHHH	22.64	28060719
508	Ubiquitination	LLYTLIEKTMQNVKH HHHHHHHHHHHCCCC	42.16	-
509	Phosphorylation	LYTLIEKTMQNVKHP HHHHHHHHHHCCCCC	15.93	21601212
514	Ubiquitination	EKTMQNVKHPVTGQF HHHHHCCCCCCCCCE	50.14	-
514	2-Hydroxyisobutyrylation	EKTMQNVKHPVTGQF HHHHHCCCCCCCCCE	50.14	-
514	Acetylation	EKTMQNVKHPVTGQF HHHHHCCCCCCCCCE	50.14	21466224
518	O-linked_Glycosylation	QNVKHPVTGQFLYQD HCCCCCCCCCEEECC	29.71	OGP
523	Phosphorylation	PVTGQFLYQDSNWAS CCCCCEEECCCCHHH	16.15	28152594
531	Ubiquitination	QDSNWASKVEKLTLD CCCCHHHHEEEEECC	46.82	21906983
531	Acetylation	QDSNWASKVEKLTLD CCCCHHHHEEEEECC	46.82	27452117
534	Ubiquitination	NWASKVEKLTLDNAA CHHHHEEEEECCCCH	50.16	-
572	Phosphorylation	YLGTTMDTYKELIER CCCCCHHHHHHHHHH	26.18	-
573	Phosphorylation	LGTTMDTYKELIERI CCCCHHHHHHHHHHH	9.75	-
585	Ubiquitination	ERIPELNKVARAAAE HHHHHHHHHHHHHHH	50.31	-
585	2-Hydroxyisobutyrylation	ERIPELNKVARAAAE HHHHHHHHHHHHHHH	50.31	-
611	Phosphorylation	DVELNLDYERYNSQL CEEECCCHHHHHHHH	12.89	-
614	Phosphorylation	LNLDYERYNSQLLSF ECCCHHHHHHHHHHH	13.76	28152594
616	Phosphorylation	LDYERYNSQLLSFVR CCHHHHHHHHHHHHH	17.17	21712546
620	Phosphorylation	RYNSQLLSFVRDLNQ HHHHHHHHHHHHHHH	30.23	21712546
654	Phosphorylation	GDFFRATSRLTTDFG CCHHHHCCCEECCCC	25.06	21601212
658	Phosphorylation	RATSRLTTDFGNAEK HHCCCEECCCCCCHH	33.64	17081983
665	Ubiquitination	TDFGNAEKTDRFVMK CCCCCCHHHCHHHHH	54.00	21906983
665	2-Hydroxyisobutyrylation	TDFGNAEKTDRFVMK CCCCCCHHHCHHHHH	54.00	-
666	Phosphorylation	DFGNAEKTDRFVMKK CCCCCHHHCHHHHHH	24.74	21601212
683	Phosphorylation	DRVMRVEYHFLSPYV HCEEEEEEEECCCCC	8.60	28152594
687	Phosphorylation	RVEYHFLSPYVSPKE EEEEEECCCCCCCCC	17.16	28152594
689	Phosphorylation	EYHFLSPYVSPKESP EEEECCCCCCCCCCC	15.35	28152594
691	Phosphorylation	HFLSPYVSPKESPFR EECCCCCCCCCCCCC	25.14	26437602
693	Ubiquitination	LSPYVSPKESPFRHV CCCCCCCCCCCCCCC	64.42	2190698
693	2-Hydroxyisobutyrylation	LSPYVSPKESPFRHV CCCCCCCCCCCCCCC	64.42	-
717	Ubiquitination	PALLENLKLRKQNNG HHHHHHHHHHHHCCC	58.80	-
720	Ubiquitination	LENLKLRKQNNGAFN HHHHHHHHHCCCCCC	68.74	-
722	N-linked_Glycosylation	NLKLRKQNNGAFNET HHHHHHHCCCCCCHH	52.52	19349973
722	N-linked_Glycosylation	NLKLRKQNNGAFNET HHHHHHHCCCCCCHH	52.52	19349973
727	N-linked_Glycosylation	KQNNGAFNETLFRNQ HHCCCCCCHHHHHCH	40.59	10531064
727	N-linked_Glycosylation	KQNNGAFNETLFRNQ HHCCCCCCHHHHHCH	40.59	7780197

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
20	Y	Phosphorylation	Kinase	SRC	P12931	PSP
24	S	Phosphorylation	Kinase	KPCA	P17252	PhosphoELM
24	S	Phosphorylation	Kinase	PRKCA	P20444	GPS
24	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
24	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO6	Q9NRD1	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	MARCHF2	Q9P0N8	PMID:14722266
-	K	Ubiquitination	E3 ubiquitin ligase	MARCHF1	Q8TCQ1	PMID:14722266
-	K	Ubiquitination	E3 ubiquitin ligase	MARCHF8	Q5T0T0	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
62	C	Palmitoylation	3582362
Cys-62 seems to be the major site of palmitoylation.
62	C	Palmitoylation	3582362
Palmitoylated on both Cys-62 and Cys-67.
67	C	Palmitoylation	3582362
Palmitoylated on both Cys-62 and Cys-67.

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 TFR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HFE_HUMAN	HFE	physical	9465039
GBRAP_HUMAN	GABARAP	physical	11997026
AP2M_ARATH	AT5G46630	physical	17059402
TFR1_HUMAN	TFRC	physical	10531064
TRFE_HUMAN	TF	physical	11027676
HFE_HUMAN	HFE	physical	11027676
OPTN_HUMAN	OPTN	physical	20085643
HGS_HUMAN	HGS	physical	11988743
SH3B4_HUMAN	SH3BP4	physical	16325581
B4GT1_HUMAN	B4GALT1	physical	7744867
RANB9_HUMAN	RANBP9	physical	14722085
RAB8A_HUMAN	RAB8A	physical	22854040
ARFG1_HUMAN	ARFGAP1	physical	21499258
AP2B1_HUMAN	AP2B1	physical	21499258

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 TFR1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-251, AND MASSSPECTROMETRY.	19349973 [Abstract]
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-251 AND ASN-727, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-251, AND MASSSPECTROMETRY.	16335952 [Abstract]
O-linked Glycosylation
Reference	PubMed
"Identification of the O-linked glycosylation site of the humantransferrin receptor."; Hayes G.R., Enns C.A., Lucas J.J.; Glycobiology 2:355-359(1992). Cited for: GLYCOSYLATION AT THR-104.	1421757 [Abstract]
"Presence of O-linked oligosaccharide on a threonine residue in thehuman transferrin receptor."; Do S.-I., Cummings R.D.; Glycobiology 2:345-353(1992). Cited for: GLYCOSYLATION AT THR-104.	1421756 [Abstract]
Palmitoylation
Reference	PubMed
"Identification of the intermolecular disulfide bonds of the humantransferrin receptor and its lipid-attachment site."; Jing S., Trowbridge I.S.; EMBO J. 6:327-331(1987). Cited for: PALMITOYLATION AT CYS-62.	3582362 [Abstract]
Phosphorylation
Reference	PubMed
"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-21, AND MASSSPECTROMETRY.	18669648 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND MASSSPECTROMETRY.	17389395 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND MASSSPECTROMETRY.	15592455 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND MASSSPECTROMETRY.	15951569 [Abstract]

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