dbPTM

LYAM1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LYAM1_HUMAN
UniProt AC	P14151
Protein Name	L-selectin
Gene Name	SELL
Organism	Homo sapiens (Human).
Sequence Length	372
Subcellular Localization	Cell membrane Single-pass type I membrane protein .
Protein Description	Calcium-dependent lectin that mediates cell adhesion by binding to glycoproteins on neighboring cells. [PubMed: 12403782]
Protein Sequence	MIFPWKCQSTQRDLWNIFKLWGWTMLCCDFLAHHGTDCWTYHYSEKPMNWQRARRFCRDNYTDLVAIQNKAEIEYLEKTLPFSRSYYWIGIRKIGGIWTWVGTNKSLTEEAENWGDGEPNNKKNKEDCVEIYIKRNKDAGKWNDDACHKLKAALCYTASCQPWSCSGHGECVEIINNYTCNCDVGYYGPQCQFVIQCEPLEAPELGTMDCTHPLGNFSFSSQCAFSCSEGTNLTGIEETTCGPFGNWSSPEPTCQVIQCEPLSAPDLGIMNCSHPLASFSFTSACTFICSEGTELIGKKKTICESSGIWSNPSPICQKLDKSFSMIKEGDYNPLFIPVAVMVTAFSGLAFIIWLARRLKKGKKSKRSMNDPY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
60	N-linked_Glycosylation	ARRFCRDNYTDLVAI HHHHHHCCHHHEEEE	23.42	28011641
73	N-linked_Glycosylation	AIQNKAEIEYLEKTL EECCHHHHHHHHHHC	5.15	16335952
78	Ubiquitination	AEIEYLEKTLPFSRS HHHHHHHHHCCCCCC	53.41	-
79	Phosphorylation	EIEYLEKTLPFSRSY HHHHHHHHCCCCCCE	30.23	23882029
91	Ubiquitination	RSYYWIGIRKIGGIW CCEEEEEEEEECCEE	2.74	-
91 (in isoform 2)	Ubiquitination	-	2.74	-
93	Ubiquitination	YYWIGIRKIGGIWTW EEEEEEEEECCEEEE	43.72	-
104	N-linked_Glycosylation	IWTWVGTNKSLTEEA EEEECCCCHHHHHHH	26.45	28011641
105	Ubiquitination	WTWVGTNKSLTEEAE EEECCCCHHHHHHHH	46.83	-
106	Ubiquitination	TWVGTNKSLTEEAEN EECCCCHHHHHHHHH	42.46	-
106 (in isoform 2)	Ubiquitination	-	42.46	-
117	N-linked_Glycosylation	EAENWGDGEPNNKKN HHHHCCCCCCCCCCC	48.61	28489325
118 (in isoform 2)	Ubiquitination	-	49.98	-
118	Ubiquitination	AENWGDGEPNNKKNK HHHCCCCCCCCCCCH	49.98	-
122	Ubiquitination	GDGEPNNKKNKEDCV CCCCCCCCCCHHHHE	65.45	-
123	Ubiquitination	DGEPNNKKNKEDCVE CCCCCCCCCHHHHEE	75.32	-
125	Ubiquitination	EPNNKKNKEDCVEIY CCCCCCCHHHHEEEE	64.90	-
132	Phosphorylation	KEDCVEIYIKRNKDA HHHHEEEEEECCCCC	6.20	-
134	Ubiquitination	DCVEIYIKRNKDAGK HHEEEEEECCCCCCC	32.71	-
135	Ubiquitination	CVEIYIKRNKDAGKW HEEEEEECCCCCCCC	45.96	22505724
136 (in isoform 2)	Ubiquitination	-	41.37	-
137	Ubiquitination	EIYIKRNKDAGKWND EEEEECCCCCCCCCH	53.65	-
138	Ubiquitination	IYIKRNKDAGKWNDD EEEECCCCCCCCCHH	65.19	-
138 (in isoform 2)	Ubiquitination	-	65.19	-
141	Ubiquitination	KRNKDAGKWNDDACH ECCCCCCCCCHHHHH	44.54	-
147	Ubiquitination	GKWNDDACHKLKAAL CCCCHHHHHHHHHHH	3.60	-
147 (in isoform 2)	Ubiquitination	-	3.60	-
149	Ubiquitination	WNDDACHKLKAALCY CCHHHHHHHHHHHHE	52.12	-
150 (in isoform 2)	Ubiquitination	-	1.71	-
150	Ubiquitination	NDDACHKLKAALCYT CHHHHHHHHHHHHEE	1.71	-
154	Ubiquitination	CHKLKAALCYTASCQ HHHHHHHHHEECCCC	2.47	-
154 (in isoform 2)	Ubiquitination	-	2.47	-
162 (in isoform 2)	Ubiquitination	-	29.31	-
162	Ubiquitination	CYTASCQPWSCSGHG HEECCCCCCCCCCCC	29.31	-
177	N-linked_Glycosylation	ECVEIINNYTCNCDV CEEEEECCEECCCCC	24.07	28489325
232	N-linked_Glycosylation	FSCSEGTNLTGIEET EECCCCCCCCCCEEE	46.60	UniProtKB CARBOHYD
246	N-linked_Glycosylation	TTCGPFGNWSSPEPT EECCCCCCCCCCCCE	35.52	UniProtKB CARBOHYD
271	N-linked_Glycosylation	APDLGIMNCSHPLAS CCCCEECCCCCCCCC	23.40	UniProtKB CARBOHYD
299	Ubiquitination	GTELIGKKKTICESS CCEEECCCCEEECCC	50.35	-
300	Ubiquitination	TELIGKKKTICESSG CEEECCCCEEECCCC	46.75	-
311	N-linked_Glycosylation	ESSGIWSNPSPICQK CCCCCCCCCCHHHHH	26.52	UniProtKB CARBOHYD
312 (in isoform 2)	Ubiquitination	-	35.65	-
313 (in isoform 2)	Ubiquitination	-	31.02	-
313	Ubiquitination	SGIWSNPSPICQKLD CCCCCCCCHHHHHHH	31.02	-
321	Ubiquitination	PICQKLDKSFSMIKE HHHHHHHHHHHCCCC	64.93	-
324	Phosphorylation	QKLDKSFSMIKEGDY HHHHHHHHCCCCCCC	27.04	25907765
331	Ubiquitination	SMIKEGDYNPLFIPV HCCCCCCCCCCHHHH	29.54	-
334 (in isoform 2)	Ubiquitination	-	5.60	-
334	Ubiquitination	KEGDYNPLFIPVAVM CCCCCCCCHHHHHHH	5.60	-
364	Phosphorylation	RLKKGKKSKRSMNDP HHHCCCCHHCCCCCC	36.47	-
367	Phosphorylation	KGKKSKRSMNDPY-- CCCCHHCCCCCCC--	26.19	-
377	Phosphorylation	DPY------------ CCC------------		-
380	Phosphorylation	--------------- ---------------		-

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
372	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LYAM1_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 LYAM1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MUCEN_HUMAN	EMCN	physical	15249540
PODXL_HUMAN	PODXL	physical	9625756
CFAH_HUMAN	CFH	physical	10377245
GRB2_HUMAN	GRB2	physical	8986819
MUC7_HUMAN	MUC7	physical	9538010
CSPG2_HUMAN	VCAN	physical	10950950
MOES_HUMAN	MSN	physical	11706008
EZRI_HUMAN	EZR	physical	11706008
LYAM2_HUMAN	SELE	physical	9024699
KPCA_HUMAN	PRKCA	physical	15192100
KPCT_HUMAN	PRKCQ	physical	15192100

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 LYAM1_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-60 AND ASN-104, AND MASSSPECTROMETRY.	19349973 [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-60, AND MASS SPECTROMETRY.	16335952 [Abstract]