dbPTM

SELPL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SELPL_HUMAN
UniProt AC	Q14242
Protein Name	P-selectin glycoprotein ligand 1
Gene Name	SELPLG
Organism	Homo sapiens (Human).
Sequence Length	412
Subcellular Localization	Membrane Single-pass type I membrane protein.
Protein Description	A SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E-, P- and L-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture.; (Microbial infection) Acts as a receptor for enterovirus 71..
Protein Sequence	MPLQLLLLLILLGPGNSLQLWDTWADEAEKALGPLLARDRRQATEYEYLDYDFLPETEPPEMLRNSTDTTPLTGPGTPESTTVEPAARRSTGLDAGGAVTELTTELANMGNLSTDSAAMEIQTTQPAATEAQTTQPVPTEAQTTPLAATEAQTTRLTATEAQTTPLAATEAQTTPPAATEAQTTQPTGLEAQTTAPAAMEAQTTAPAAMEAQTTPPAAMEAQTTQTTAMEAQTTAPEATEAQTTQPTATEAQTTPLAAMEALSTEPSATEALSMEPTTKRGLFIPFSVSSVTHKGIPMAASNLSVNYPVGAPDHISVKQCLLAILILALVATIFFVCTVVLAVRLSRKGHMYPVRNYSPTEMVCISSLLPDGGEGPSATANGGLSKAKSPGLTPEPREDREGDDLTLHSFLP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
42	Pyrrolidone_carboxylic_acid	LLARDRRQATEYEYL HHHHHHHHCCEEEEC	54.23	-
42	Pyrrolidone_carboxylic_acid	LLARDRRQATEYEYL HHHHHHHHCCEEEEC	54.23	11081633
42	Pyrrolidone_carboxylic_acid	LLARDRRQATEYEYL HHHHHHHHCCEEEEC	54.23	11081633
46	Sulfation	DRRQATEYEYLDYDF HHHHCCEEEECCCCC	12.91	-
46	Sulfation	DRRQATEYEYLDYDF HHHHCCEEEECCCCC	12.91	11081633
48	Sulfation	RQATEYEYLDYDFLP HHCCEEEECCCCCCC	12.17	-
48	Sulfation	RQATEYEYLDYDFLP HHCCEEEECCCCCCC	12.17	11081633
51	Sulfation	TEYEYLDYDFLPETE CEEEECCCCCCCCCC	13.14	-
51	Sulfation	TEYEYLDYDFLPETE CEEEECCCCCCCCCC	13.14	11081633
57	O-linked_Glycosylation	DYDFLPETEPPEMLR CCCCCCCCCCHHHHC	52.42	11081633
65	N-linked_Glycosylation	EPPEMLRNSTDTTPL CCHHHHCCCCCCCCC	45.35	UniProtKB CARBOHYD
67	Phosphorylation	PEMLRNSTDTTPLTG HHHHCCCCCCCCCCC	40.70	-
69	Phosphorylation	MLRNSTDTTPLTGPG HHCCCCCCCCCCCCC	30.33	-
73	Phosphorylation	STDTTPLTGPGTPES CCCCCCCCCCCCCCC	42.40	-
81	Phosphorylation	GPGTPESTTVEPAAR CCCCCCCCCCCCHHH	32.95	-
82	Phosphorylation	PGTPESTTVEPAARR CCCCCCCCCCCHHHH	31.95	-
111	N-linked_Glycosylation	TELANMGNLSTDSAA HHHHHCCCCCCCCHH	21.76	UniProtKB CARBOHYD
143	O-linked_Glycosylation	PVPTEAQTTPLAATE CCCCCCCCCCCCCCC	37.11	OGP
157	Phosphorylation	EAQTTRLTATEAQTT CCHHCCEECCCCCCC	28.39	-
159	Phosphorylation	QTTRLTATEAQTTPL HHCCEECCCCCCCCC	26.98	-
264	O-linked_Glycosylation	AAMEALSTEPSATEA HHHHHHCCCCCHHHH	53.41	OGP
287	O-linked_Glycosylation	RGLFIPFSVSSVTHK CCEEECEECCCEECC	18.74	55824305
289	O-linked_Glycosylation	LFIPFSVSSVTHKGI EEECEECCCEECCCC	20.21	55824309
290	O-linked_Glycosylation	FIPFSVSSVTHKGIP EECEECCCEECCCCC	28.95	55824313
292	O-linked_Glycosylation	PFSVSSVTHKGIPMA CEECCCEECCCCCCC	21.59	55824319
302	N-linked_Glycosylation	GIPMAASNLSVNYPV CCCCCCCCEEECCCC	31.44	UniProtKB CARBOHYD
357	Phosphorylation	HMYPVRNYSPTEMVC CCEECCCCCCCCEEE	12.88	28464451
358	Phosphorylation	MYPVRNYSPTEMVCI CEECCCCCCCCEEEE	28.97	28464451
360	Phosphorylation	PVRNYSPTEMVCISS ECCCCCCCCEEEEEC	30.67	26657352
366	Phosphorylation	PTEMVCISSLLPDGG CCCEEEEECCCCCCC	15.14	28450419
367	Phosphorylation	TEMVCISSLLPDGGE CCEEEEECCCCCCCC	17.64	28464451
376	Phosphorylation	LPDGGEGPSATANGG CCCCCCCCCCCCCCC	19.25	27251275
377	Phosphorylation	PDGGEGPSATANGGL CCCCCCCCCCCCCCC	49.46	26074081
379	Phosphorylation	GGEGPSATANGGLSK CCCCCCCCCCCCCCC	25.62	27080861
385	Phosphorylation	ATANGGLSKAKSPGL CCCCCCCCCCCCCCC	33.57	26074081
388	Ubiquitination	NGGLSKAKSPGLTPE CCCCCCCCCCCCCCC	62.00	29967540
389	Phosphorylation	GGLSKAKSPGLTPEP CCCCCCCCCCCCCCC	29.12	25159151
393	Phosphorylation	KAKSPGLTPEPREDR CCCCCCCCCCCCCCC	31.36	23401153
404	Ubiquitination	REDREGDDLTLHSFL CCCCCCCCCCCHHCC	53.03	29967540
405	Phosphorylation	EDREGDDLTLHSFLP CCCCCCCCCCHHCCC	6.98	27251275
406	Phosphorylation	DREGDDLTLHSFLP- CCCCCCCCCHHCCC-	29.44	28122231
409	Phosphorylation	GDDLTLHSFLP---- CCCCCCHHCCC----	31.43	23401153
422	Phosphorylation	----------------- -----------------		24719451
425	Phosphorylation	-------------------- --------------------		27251275

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

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SELPL_HUMAN	SELPLG	physical	10713099
LYAM3_HUMAN	SELP	physical	10713099
MOES_HUMAN	MSN	physical	12115638
TNIP1_HUMAN	TNIP1	physical	17632516
P85A_HUMAN	PIK3R1	physical	17632516

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 SELPL_HUMAN

Related Literatures of Post-Translational Modification

O-linked Glycosylation
Reference	PubMed
"Insights into the molecular basis of leukocyte tethering and rollingrevealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1."; Somers W.S., Tang J., Shaw G.D., Camphausen R.T.; Cell 103:467-479(2000). Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-68 IN COMPLEX WITH SELEAND SELP LECTIN/EGF DOMAINS, SULFATION AT TYR-46; TYR-48 AND TYR-51,GLYCOSYLATION AT THR-57, AND PYROGLUTAMATE FORMATION AT GLN-42.	11081633 [Abstract]
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-389 AND THR-393, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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-389 AND THR-393, ANDMASS SPECTROMETRY.	18669648 [Abstract]
Sulfation
Reference	PubMed
"Insights into the molecular basis of leukocyte tethering and rollingrevealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1."; Somers W.S., Tang J., Shaw G.D., Camphausen R.T.; Cell 103:467-479(2000). Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-68 IN COMPLEX WITH SELEAND SELP LECTIN/EGF DOMAINS, SULFATION AT TYR-46; TYR-48 AND TYR-51,GLYCOSYLATION AT THR-57, AND PYROGLUTAMATE FORMATION AT GLN-42.	11081633 [Abstract]