dbPTM

L1CAM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	L1CAM_HUMAN
UniProt AC	P32004
Protein Name	Neural cell adhesion molecule L1
Gene Name	L1CAM
Organism	Homo sapiens (Human).
Sequence Length	1257
Subcellular Localization	Cell membrane Single-pass type I membrane protein . Cell projection, growth cone . Cell projection, axon . Cell projection, dendrite. Colocalized with SHTN1 in close apposition with actin filaments in filopodia and lamellipodia of axonalne growth c
Protein Description	Neural cell adhesion molecule involved in the dynamics of cell adhesion and in the generation of transmembrane signals at tyrosine kinase receptors. During brain development, critical in multiple processes, including neuronal migration, axonal growth and fasciculation, and synaptogenesis. In the mature brain, plays a role in the dynamics of neuronal structure and function, including synaptic plasticity..
Protein Sequence	MVVALRYVWPLLLCSPCLLIQIPEEYEGHHVMEPPVITEQSPRRLVVFPTDDISLKCEASGKPEVQFRWTRDGVHFKPKEELGVTVYQSPHSGSFTITGNNSNFAQRFQGIYRCFASNKLGTAMSHEIRLMAEGAPKWPKETVKPVEVEEGESVVLPCNPPPSAEPLRIYWMNSKILHIKQDERVTMGQNGNLYFANVLTSDNHSDYICHAHFPGTRTIIQKEPIDLRVKATNSMIDRKPRLLFPTNSSSHLVALQGQPLVLECIAEGFPTPTIKWLRPSGPMPADRVTYQNHNKTLQLLKVGEEDDGEYRCLAENSLGSARHAYYVTVEAAPYWLHKPQSHLYGPGETARLDCQVQGRPQPEVTWRINGIPVEELAKDQKYRIQRGALILSNVQPSDTMVTQCEARNRHGLLLANAYIYVVQLPAKILTADNQTYMAVQGSTAYLLCKAFGAPVPSVQWLDEDGTTVLQDERFFPYANGTLGIRDLQANDTGRYFCLAANDQNNVTIMANLKVKDATQITQGPRSTIEKKGSRVTFTCQASFDPSLQPSITWRGDGRDLQELGDSDKYFIEDGRLVIHSLDYSDQGNYSCVASTELDVVESRAQLLVVGSPGPVPRLVLSDLHLLTQSQVRVSWSPAEDHNAPIEKYDIEFEDKEMAPEKWYSLGKVPGNQTSTTLKLSPYVHYTFRVTAINKYGPGEPSPVSETVVTPEAAPEKNPVDVKGEGNETTNMVITWKPLRWMDWNAPQVQYRVQWRPQGTRGPWQEQIVSDPFLVVSNTSTFVPYEIKVQAVNSQGKGPEPQVTIGYSGEDYPQAIPELEGIEILNSSAVLVKWRPVDLAQVKGHLRGYNVTYWREGSQRKHSKRHIHKDHVVVPANTTSVILSGLRPYSSYHLEVQAFNGRGSGPASEFTFSTPEGVPGHPEALHLECQSNTSLLLRWQPPLSHNGVLTGYVLSYHPLDEGGKGQLSFNLRDPELRTHNLTDLSPHLRYRFQLQATTKEGPGEAIVREGGTMALSGISDFGNISATAGENYSVVSWVPKEGQCNFRFHILFKALGEEKGGASLSPQYVSYNQSSYTQWDLQPDTDYEIHLFKERMFRHQMAVKTNGTGRVRLPPAGFATEGWFIGFVSAIILLLLVLLILCFIKRSKGGKYSVKDKEDTQVDSEARPMKDETFGEYRSLESDNEEKAFGSSQPSLNGDIKPLGSDDSLADYGGSVDVQFNEDGSFIGQYSGKKEKEAAGGNDSSGATSPINPAVALE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
51	Ubiquitination	RLVVFPTDDISLKCE EEEEEECCCCEEEEE	52.03	29967540
56	Ubiquitination	PTDDISLKCEASGKP ECCCCEEEEECCCCC	24.20	29967540
72	Ubiquitination	VQFRWTRDGVHFKPK EEEEEECCCCCCCCH	56.97	29967540
77	Ubiquitination	TRDGVHFKPKEELGV ECCCCCCCCHHHHCC	40.06	29967540
100	N-linked_Glycosylation	GSFTITGNNSNFAQR EEEEEECCCCCHHHH	39.86	UniProtKB CARBOHYD
135	Ubiquitination	IRLMAEGAPKWPKET HHHHHCCCCCCCCCC	8.26	29967540
139	Ubiquitination	AEGAPKWPKETVKPV HCCCCCCCCCCCCCE	30.63	21963094
140	Ubiquitination	EGAPKWPKETVKPVE CCCCCCCCCCCCCEE	65.97	29967540
144	Acetylation	KWPKETVKPVEVEEG CCCCCCCCCEEEECC	51.25	26051181
144	Ubiquitination	KWPKETVKPVEVEEG CCCCCCCCCEEEECC	51.25	21963094
153	Phosphorylation	VEVEEGESVVLPCNP EEEECCCEEEEECCC	28.51	-
163	Phosphorylation	LPCNPPPSAEPLRIY EECCCCCCCCCEEEE	51.54	-
175	Ubiquitination	RIYWMNSKILHIKQD EEEEECCCEEEEECC	44.26	21963094
180	Ubiquitination	NSKILHIKQDERVTM CCCEEEEECCCCEEE	40.73	21963094
203	N-linked_Glycosylation	ANVLTSDNHSDYICH EEEECCCCCCCEEEE	36.01	UniProtKB CARBOHYD
217	Ubiquitination	HAHFPGTRTIIQKEP EEECCCCEEEEECCC	29.82	29967540
222	Ubiquitination	GTRTIIQKEPIDLRV CCEEEEECCCCCEEE	55.86	29967540
225	Ubiquitination	TIIQKEPIDLRVKAT EEEECCCCCEEEEEC	9.04	29967540
230	Ubiquitination	EPIDLRVKATNSMID CCCCEEEEECCCCCC	42.96	29967540
247	N-linked_Glycosylation	PRLLFPTNSSSHLVA CCEEECCCCCCCEEE	39.88	UniProtKB CARBOHYD
290	Ubiquitination	MPADRVTYQNHNKTL CCCCCEEEECCCCEE	12.40	29967540
294	N-linked_Glycosylation	RVTYQNHNKTLQLLK CEEEECCCCEEEEEE	46.70	UniProtKB CARBOHYD
295	Ubiquitination	VTYQNHNKTLQLLKV EEEECCCCEEEEEEC	42.96	29967540
296	Ubiquitination	TYQNHNKTLQLLKVG EEECCCCEEEEEECC	25.67	21963094
301	Ubiquitination	NKTLQLLKVGEEDDG CCEEEEEECCCCCCC	57.71	21963094
333	Ubiquitination	YVTVEAAPYWLHKPQ EEEEEECCCEECCCC	28.07	29967540
338	Ubiquitination	AAPYWLHKPQSHLYG ECCCEECCCCHHCCC	42.45	29967540
373	Ubiquitination	WRINGIPVEELAKDQ EEECCEEHHHHHHCC	9.37	21963094
378	Ubiquitination	IPVEELAKDQKYRIQ EEHHHHHHCCCCEEE	73.62	21963094
397	Phosphorylation	ILSNVQPSDTMVTQC EECCCCCCCCEEECC	28.73	28122231
399	Phosphorylation	SNVQPSDTMVTQCEA CCCCCCCCEEECCHH	20.20	25099161
402	Phosphorylation	QPSDTMVTQCEARNR CCCCCEEECCHHHCC	19.38	25099161
418	Phosphorylation	GLLLANAYIYVVQLP CEEEECEEEEEEEEC	7.81	-
420	Phosphorylation	LLANAYIYVVQLPAK EEECEEEEEEEECCE	5.06	-
433	N-linked_Glycosylation	AKILTADNQTYMAVQ CEEECCCCCEEEEEC	33.36	UniProtKB CARBOHYD
479	N-linked_Glycosylation	ERFFPYANGTLGIRD CCEECCCCCCEEECE	37.83	UniProtKB CARBOHYD
481	O-linked_Glycosylation	FFPYANGTLGIRDLQ EECCCCCCEEECEEC	22.94	28657654
490	N-linked_Glycosylation	GIRDLQANDTGRYFC EECEECCCCCCCEEE	34.12	UniProtKB CARBOHYD
505	N-linked_Glycosylation	LAANDQNNVTIMANL EEEECCCCEEEEEEE	27.03	UniProtKB CARBOHYD
508	Ubiquitination	NDQNNVTIMANLKVK ECCCCEEEEEEEEEC	1.82	32015554
510	Ubiquitination	QNNVTIMANLKVKDA CCCEEEEEEEEECCC	17.85	29967540
513	Ubiquitination	VTIMANLKVKDATQI EEEEEEEEECCCCCC	47.23	32015554
515	Ubiquitination	IMANLKVKDATQITQ EEEEEEECCCCCCCC	39.81	29967540
518	Phosphorylation	NLKVKDATQITQGPR EEEECCCCCCCCCCC	30.55	20068231
521	Phosphorylation	VKDATQITQGPRSTI ECCCCCCCCCCCCEE	20.04	20068231
527	Phosphorylation	ITQGPRSTIEKKGSR CCCCCCCEEEECCCE	34.14	-
530	Acetylation	GPRSTIEKKGSRVTF CCCCEEEECCCEEEE	59.59	20167786
563	Ubiquitination	DGRDLQELGDSDKYF CCCCHHHHCCCCCEE	6.27	29967540
568	Ubiquitination	QELGDSDKYFIEDGR HHHCCCCCEEEECCC	46.11	29967540
583	Phosphorylation	LVIHSLDYSDQGNYS EEEEECCCCCCCCEE	21.31	23532336
588	N-linked_Glycosylation	LDYSDQGNYSCVAST CCCCCCCCEEEEEEC	21.66	UniProtKB CARBOHYD
589	Phosphorylation	DYSDQGNYSCVASTE CCCCCCCEEEEEECE	15.40	23532336
611	Phosphorylation	AQLLVVGSPGPVPRL EEEEEECCCCCCCCE	18.31	-
650	Ubiquitination	APIEKYDIEFEDKEM CCCCCCCCCCCCHHC	6.24	29967540
655	Ubiquitination	YDIEFEDKEMAPEKW CCCCCCCHHCCCHHE	42.04	29967540
656	Ubiquitination	DIEFEDKEMAPEKWY CCCCCCHHCCCHHEE	53.55	29967540
661	Ubiquitination	DKEMAPEKWYSLGKV CHHCCCHHEEECCCC	50.83	29967540
662	Ubiquitination	KEMAPEKWYSLGKVP HHCCCHHEEECCCCC	6.06	29967540
667	Ubiquitination	EKWYSLGKVPGNQTS HHEEECCCCCCCCCC	51.02	29967540
671	N-linked_Glycosylation	SLGKVPGNQTSTTLK ECCCCCCCCCCCEEE	35.57	16335952
682	Phosphorylation	TTLKLSPYVHYTFRV CEEEECCCEEEEEEE	9.11	24706070
685	Phosphorylation	KLSPYVHYTFRVTAI EECCCEEEEEEEEEE	9.49	24706070
689	Ubiquitination	YVHYTFRVTAINKYG CEEEEEEEEEEECCC	3.56	21963094
694	Acetylation	FRVTAINKYGPGEPS EEEEEEECCCCCCCC	45.53	27452117
694	Ubiquitination	FRVTAINKYGPGEPS EEEEEEECCCCCCCC	45.53	21963094
695	Phosphorylation	RVTAINKYGPGEPSP EEEEEECCCCCCCCC	24.86	20068231
701	Phosphorylation	KYGPGEPSPVSETVV CCCCCCCCCCCEEEE	33.36	20068231
704	Phosphorylation	PGEPSPVSETVVTPE CCCCCCCCEEEECCC	30.82	20068231
706	Phosphorylation	EPSPVSETVVTPEAA CCCCCCEEEECCCCC	16.87	20068231
709	Phosphorylation	PVSETVVTPEAAPEK CCCEEEECCCCCCCC	15.86	20068231
711	Ubiquitination	SETVVTPEAAPEKNP CEEEECCCCCCCCCC	48.36	29967540
716	Ubiquitination	TPEAAPEKNPVDVKG CCCCCCCCCCCCCCC	66.54	29967540
726	N-linked_Glycosylation	VDVKGEGNETTNMVI CCCCCCCCCCEEEEE	38.86	UniProtKB CARBOHYD
777	N-linked_Glycosylation	DPFLVVSNTSTFVPY CCEEEEECCCCEECE	26.83	UniProtKB CARBOHYD
784	Phosphorylation	NTSTFVPYEIKVQAV CCCCEECEEEEEEEE	25.61	-
793	Phosphorylation	IKVQAVNSQGKGPEP EEEEEECCCCCCCCC	33.44	24248375
806	Phosphorylation	EPQVTIGYSGEDYPQ CCCEEEEECCCCCCC	15.06	24248375
811	Phosphorylation	IGYSGEDYPQAIPEL EEECCCCCCCCCHHH	7.92	24248375
825	N-linked_Glycosylation	LEGIEILNSSAVLVK HCCEEEECCCEEEEE	39.31	UniProtKB CARBOHYD
837	Ubiquitination	LVKWRPVDLAQVKGH EEEEEECCHHHEECH	38.68	21963094
842	Ubiquitination	PVDLAQVKGHLRGYN ECCHHHEECHHCCCE	28.65	21963094
849	N-linked_Glycosylation	KGHLRGYNVTYWREG ECHHCCCEEEEECCC	23.60	UniProtKB CARBOHYD
876	N-linked_Glycosylation	DHVVVPANTTSVILS CEEEECCCCCEEEEC	37.51	UniProtKB CARBOHYD
883	Phosphorylation	NTTSVILSGLRPYSS CCCEEEECCCCCCCE	25.34	24719451
979	N-linked_Glycosylation	DPELRTHNLTDLSPH CHHHCCCCCCCCCHH	43.98	UniProtKB CARBOHYD
993	Ubiquitination	HLRYRFQLQATTKEG HHHHEEEEEEECCCC	3.26	21963094
998	Ubiquitination	FQLQATTKEGPGEAI EEEEEECCCCCCCEE	57.21	21963094
1022	N-linked_Glycosylation	SGISDFGNISATAGE CCCCCCCCEEECCCC	25.65	UniProtKB CARBOHYD
1030	N-linked_Glycosylation	ISATAGENYSVVSWV EEECCCCCEEEEEEC	33.20	UniProtKB CARBOHYD
1071	N-linked_Glycosylation	SPQYVSYNQSSYTQW CCEEEECCCCCCCCC	27.96	UniProtKB CARBOHYD
1105	N-linked_Glycosylation	HQMAVKTNGTGRVRL CEEEEEECCCCCEEC	40.07	UniProtKB CARBOHYD
1145	Ubiquitination	LILCFIKRSKGGKYS HHHHHHHHHCCCCCC	38.49	32142685
1146	Phosphorylation	ILCFIKRSKGGKYSV HHHHHHHHCCCCCCC	30.56	22210691
1149	Ubiquitination	FIKRSKGGKYSVKDK HHHHHCCCCCCCCCC	29.48	32142685
1150	Ubiquitination	IKRSKGGKYSVKDKE HHHHCCCCCCCCCCC	42.92	32142685
1151	Phosphorylation	KRSKGGKYSVKDKED HHHCCCCCCCCCCCC	23.21	19720049
1151	Ubiquitination	KRSKGGKYSVKDKED HHHCCCCCCCCCCCC	23.21	21963094
1152	Phosphorylation	RSKGGKYSVKDKEDT HHCCCCCCCCCCCCC	26.61	8663493
1154	Ubiquitination	KGGKYSVKDKEDTQV CCCCCCCCCCCCCCC	58.08	32142685
1154 (in isoform 3)	Phosphorylation	-	58.08	20068231
1156	Ubiquitination	GKYSVKDKEDTQVDS CCCCCCCCCCCCCCC	52.34	21963094
1156 (in isoform 2)	Ubiquitination	-	52.34	-
1158	Phosphorylation	YSVKDKEDTQVDSEA CCCCCCCCCCCCCCC	48.45	32142685
1158 (in isoform 3)	Phosphorylation	-	48.45	25849741
1159	Phosphorylation	SVKDKEDTQVDSEAR CCCCCCCCCCCCCCC	31.42	29116813
1159 (in isoform 2)	Phosphorylation	-	31.42	20068231
1163	Phosphorylation	KEDTQVDSEARPMKD CCCCCCCCCCCCCCC	34.01	20068231
1163 (in isoform 2)	Phosphorylation	-	34.01	25849741
1164	Ubiquitination	EDTQVDSEARPMKDE CCCCCCCCCCCCCCC	44.21	21963094
1167 (in isoform 3)	Phosphorylation	-	41.02	25159151
1169	Ubiquitination	DSEARPMKDETFGEY CCCCCCCCCCCCCCE	55.91	21963094
1169 (in isoform 2)	Ubiquitination	-	55.91	-
1171 (in isoform 3)	Phosphorylation	-	40.28	20201521
1172	Phosphorylation	ARPMKDETFGEYRSL CCCCCCCCCCCEECC	47.26	17081983
1172 (in isoform 2)	Phosphorylation	-	47.26	25159151
1172 (in isoform 3)	Phosphorylation	-	47.26	22167270
1176	Phosphorylation	KDETFGEYRSLESDN CCCCCCCEECCCCCC	13.09	26657352
1176 (in isoform 2)	Phosphorylation	-	13.09	20201521
1177	Ubiquitination	DETFGEYRSLESDNE CCCCCCEECCCCCCH	30.39	29967540
1177 (in isoform 2)	Phosphorylation	-	30.39	22167270
1178	Phosphorylation	ETFGEYRSLESDNEE CCCCCEECCCCCCHH	35.27	27732954
1181	Phosphorylation	GEYRSLESDNEEKAF CCEECCCCCCHHHHH	51.54	21955146
1181 (in isoform 3)	Phosphorylation	-	51.54	25849741
1182	Ubiquitination	EYRSLESDNEEKAFG CEECCCCCCHHHHHC	58.13	29967540
1182 (in isoform 3)	Phosphorylation	-	58.13	25159151
1185	Phosphorylation	SLESDNEEKAFGSSQ CCCCCCHHHHHCCCC	56.81	32142685
1185 (in isoform 3)	Phosphorylation	-	56.81	25849741
1186 (in isoform 2)	Phosphorylation	-	42.72	25849741
1187 (in isoform 2)	Phosphorylation	-	19.81	25159151
1190	Phosphorylation	NEEKAFGSSQPSLNG CHHHHHCCCCCCCCC	21.24	22617229
1190 (in isoform 2)	Phosphorylation	-	21.24	25849741
1191	Phosphorylation	EEKAFGSSQPSLNGD HHHHHCCCCCCCCCC	46.63	28102081
1194	Phosphorylation	AFGSSQPSLNGDIKP HHCCCCCCCCCCCCC	27.16	22617229
1204	Phosphorylation	GDIKPLGSDDSLADY CCCCCCCCCCCHHHC	46.02	10608864
1207	Phosphorylation	KPLGSDDSLADYGGS CCCCCCCCHHHCCCE	30.37	20068231
1211	Phosphorylation	SDDSLADYGGSVDVQ CCCCHHHCCCEEEEE	20.13	20068231
1214	Phosphorylation	SLADYGGSVDVQFNE CHHHCCCEEEEEECC	15.69	20068231
1224	Phosphorylation	VQFNEDGSFIGQYSG EEECCCCCCEEEECC	26.47	20068231
1226	Ubiquitination	FNEDGSFIGQYSGKK ECCCCCCEEEECCCC	3.44	29967540
1229	Phosphorylation	DGSFIGQYSGKKEKE CCCCEEEECCCCCCC	17.74	20068231
1230	Phosphorylation	GSFIGQYSGKKEKEA CCCEEEECCCCCCCC	35.93	20068231
1231	Ubiquitination	SFIGQYSGKKEKEAA CCEEEECCCCCCCCC	39.87	29967540
1235	Ubiquitination	QYSGKKEKEAAGGND EECCCCCCCCCCCCC	62.63	29967540
1239	Phosphorylation	KKEKEAAGGNDSSGA CCCCCCCCCCCCCCC	42.35	32142685
1240 (in isoform 2)	Phosphorylation	-	30.00	18669648
1243	Phosphorylation	EAAGGNDSSGATSPI CCCCCCCCCCCCCCC	34.37	30266825
1244	Phosphorylation	AAGGNDSSGATSPIN CCCCCCCCCCCCCCC	35.00	30266825
1247	Phosphorylation	GNDSSGATSPINPAV CCCCCCCCCCCCHHH	38.26	30266825
1248	Phosphorylation	NDSSGATSPINPAVA CCCCCCCCCCCHHHC	24.21	25159151

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
1172	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
1172	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
1176	Y	Phosphorylation	Kinase	SRC	P12931	PSP
1181	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
1181	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
1181	S	Phosphorylation	Kinase	CAMK2	-	Uniprot
1181	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
1204	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
1229	Y	Phosphorylation	Kinase	EPHB2	P29323	PSP
1248	S	Phosphorylation	Kinase	MAPK1	P28482	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of L1CAM_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 L1CAM_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AP2A1_HUMAN	AP2A1	physical	12942088
NUMB_HUMAN	NUMB	physical	12942088
PEA15_HUMAN	PEA15	physical	16169070
EZRI_HUMAN	EZR	physical	12070130
NCAN_HUMAN	NCAN	physical	7513709
ITA5_HUMAN	ITGA5	physical	10871287
ITAV_HUMAN	ITGAV	physical	10871287
CALX_HUMAN	CANX	physical	22222883
EZRI_HUMAN	EZR	physical	22846990
RABX5_HUMAN	RABGEF1	physical	23048039
NRP1_HUMAN	NRP1	physical	16377081
RANB9_HUMAN	RANBP9	physical	16000162
ANK3_RAT	Ank3	physical	11222639
EGFR_HUMAN	EGFR	physical	22815787
ERBB2_HUMAN	ERBB2	physical	22815787
ERBB3_HUMAN	ERBB3	physical	22815787
FGFR1_HUMAN	FGFR1	physical	23212305
FGFR1_HUMAN	FGFR1	physical	18222703

Drug and Disease Associations

Kegg Disease
H00266	Hereditary spastic paraplegia (SPG)
H00577	Syndromic X-linked mental retardation with epilepsy or seizures, including: West syndrome (WS); Part
H01034	L1 syndrome, including: ; X-linked hydrocephalus; MASA syndrome; X-linked complicated spastic parapl
OMIM Disease
307000	Hydrocephalus due to stenosis of the aqueduct of Sylvius (HSAS)
303350	Mental retardation, aphasia, shuffling gait, and adducted thumbs syndrome (MASA)
303350	Spastic paraplegia 1, X-linked (SPG1)
0000269\|PubMed	Note=Defects in L1CAM may contribute to Hirschsprung disease by modifying the effects of Hirschsprung disease-associated genes to cause intestinal aganglionosis. {ECO
304100
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of L1CAM_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-671, 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-671, AND MASSSPECTROMETRY.	16335952 [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 SER-1248, AND MASSSPECTROMETRY.	18669648 [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-1163; SER-1190; SER-1191AND SER-1194, AND MASS SPECTROMETRY.	17081983 [Abstract]