LYAM3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LYAM3_HUMAN
• UniProt AC: P16109
• Protein Name: P-selectin
• Gene Name: SELP
• Organism: Homo sapiens (Human).
• Sequence Length: 830
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein .
• Protein Description: Ca(2+)-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with SELPLG..
• Protein Sequence: MANCQIAILYQRFQRVVFGISQLLCFSALISELTNQKEVAAWTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYYSSYYWIGIRKNNKTWTWVGTKKALTNEAENWADNEPNNKRNNEDCVEIYIKSPSAPGKWNDEHCLKKKHALCYTASCQDMSCSKQGECLETIGNYTCSCYPGFYGPECEYVRECGELELPQHVLMNCSHPLGNFSFNSQCSFHCTDGYQVNGPSKLECLASGIWTNKPPQCLAAQCPPLKIPERGNMTCLHSAKAFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVCKAVQCQHLEAPSEGTMDCVHPLTAFAYGSSCKFECQPGYRVRGLDMLRCIDSGHWSAPLPTCEAISCEPLESPVHGSMDCSPSLRAFQYDTNCSFRCAEGFMLRGADIVRCDNLGQWTAPAPVCQALQCQDLPVPNEARVNCSHPFGAFRYQSVCSFTCNEGLLLVGASVLQCLATGNWNSVPPECQAIPCTPLLSPQNGTMTCVQPLGSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMCEAIKCPELFAPEQGSLDCSDTRGEFNVGSTCHFSCDNGFKLEGPNNVECTTSGRWSATPPTCKGIASLPTPGLQCPALTTPGQGTMYCRHHPGTFGFNTTCYFGCNAGFTLIGDSTLSCRPSGQWTAVTPACRAVKCSELHVNKPIAMNCSNLWGNFSYGSICSFHCLEGQLLNGSAQTACQENGHWSTTVPTCQAGPLTIQEALTYFGGAVASTIGLIMGGTLLALLRKRFRQKDDGKCPLNPHSHLGTYGVFTNAAFDPSP

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
54	N-linked_Glycosylation	STKAYSWNISRKYCQ CCCEECCCCCHHHHH	19.20	16263699
58	Acetylation	YSWNISRKYCQNRYT ECCCCCHHHHHCCCC	43.52	12431295
98	N-linked_Glycosylation	WIGIRKNNKTWTWVG EEEEECCCEEEEEEE	46.28	UniProtKB CARBOHYD
180	N-linked_Glycosylation	ECLETIGNYTCSCYP CEEEHHCCEECCCCC	25.70	UniProtKB CARBOHYD
212	N-linked_Glycosylation	LPQHVLMNCSHPLGN CCCEEEECCCCCCCC	21.70	UniProtKB CARBOHYD
219	N-linked_Glycosylation	NCSHPLGNFSFNSQC CCCCCCCCCCCCCCC	36.75	UniProtKB CARBOHYD
411	N-linked_Glycosylation	RAFQYDTNCSFRCAE CEEECCCCCCCEECC	19.28	17660510
460	N-linked_Glycosylation	VPNEARVNCSHPFGA CCCCCCCCCCCCCCC	18.93	UniProtKB CARBOHYD
518	N-linked_Glycosylation	TPLLSPQNGTMTCVQ CCCCCCCCCCEEEEE	51.81	UniProtKB CARBOHYD
617	Phosphorylation	GPNNVECTTSGRWSA CCCCEEECCCCCCCC	15.53	28270605
618	Phosphorylation	PNNVECTTSGRWSAT CCCEEECCCCCCCCC	40.62	28270605
619	Phosphorylation	NNVECTTSGRWSATP CCEEECCCCCCCCCC	14.28	28270605
623	Phosphorylation	CTTSGRWSATPPTCK ECCCCCCCCCCCCCC	22.39	28060719
625	Phosphorylation	TSGRWSATPPTCKGI CCCCCCCCCCCCCCC	25.04	28060719
628	Phosphorylation	RWSATPPTCKGIASL CCCCCCCCCCCCCCC	28.22	28060719
634	Phosphorylation	PTCKGIASLPTPGLQ CCCCCCCCCCCCCCC	32.72	28060719
637	Phosphorylation	KGIASLPTPGLQCPA CCCCCCCCCCCCCCC	34.97	28060719
665	N-linked_Glycosylation	HPGTFGFNTTCYFGC CCCCCCCCCEEECCC	34.55	UniProtKB CARBOHYD
716	N-linked_Glycosylation	VNKPIAMNCSNLWGN CCCCEEEECCCCCCC	19.62	UniProtKB CARBOHYD
723	N-linked_Glycosylation	NCSNLWGNFSYGSIC ECCCCCCCCCCCCCE	15.88	UniProtKB CARBOHYD
741	N-linked_Glycosylation	CLEGQLLNGSAQTAC ECCCCEECCCCCCHH	51.47	UniProtKB CARBOHYD
807	S-palmitoylation	RQKDDGKCPLNPHSH HCCCCCCCCCCCCCC	5.91	7684381
807	Stearoylation	RQKDDGKCPLNPHSH HCCCCCCCCCCCCCC	5.91	7684381
812	Phosphorylation	GKCPLNPHSHLGTYG CCCCCCCCCCCCCEE	27.12	-
813	Phosphorylation	KCPLNPHSHLGTYGV CCCCCCCCCCCCEEE	22.97	28060719
814	Phosphorylation	CPLNPHSHLGTYGVF CCCCCCCCCCCEEEE	25.83	-
817	Phosphorylation	NPHSHLGTYGVFTNA CCCCCCCCEEEEECC	24.38	28060719
818	Phosphorylation	PHSHLGTYGVFTNAA CCCCCCCEEEEECCC	14.97	28060719
822	Phosphorylation	LGTYGVFTNAAFDPS CCCEEEEECCCCCCC	22.88	7691235
829	Phosphorylation	TNAAFDPSP------ ECCCCCCCC------	45.12	28060719

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of LYAM3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LYAM3_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of LYAM3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AP1M1_HUMAN	AP1M1	physical	11247301
CSPG2_HUMAN	VCAN	physical	10950950
SNX17_HUMAN	SNX17	physical	23382219
SNX27_HUMAN	SNX27	physical	23382219

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 601367: Ischemic stroke (ISCHSTR)
• Kegg Drug
• D10356: Inclacumab (USAN/INN)
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-54, AND MASS SPECTROMETRY.
PubMed: 16263699

Palmitoylation

"P-selectin is acylated with palmitic acid and stearic acid atcysteine 766 through a thioester linkage.";
Fujimoto T., Stroud E., Whatley R.E., Prescott S.M., Muszbek L.,Laposata M., McEver R.P.;
J. Biol. Chem. 268:11394-11400(1993).
Cited for: PALMITOYLATION AT CYS-807, AND STEAROYLATION AT CYS-807.
PubMed: 7684381