Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  P-selectin glycoprotein ligand 1  

UniProtKB / Swiss-Prot ID :  SELPL_HUMAN

Gene Name (Synonyms) : 
SELPLG  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Membrane; Single-pass type I membrane protein. 

Protein Function :  A SLe(x)-type glycan, 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. PSGL1 is critical for the initial leukocyte capture. 

Transmembrane Topology (topPTM) : SELPL_HUMAN 

Protein Sequence MPLQLLLLLILLGPGNSLQLWDTWADEAEKALGPLLARDRRQATEYEYLDYDFLPETEPPEMLRNSTDTT...
Predicted Secondary Structure CCHHHEEEEEEECCCCEEEEECCHHHHHHCCCCCEECCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
62M -> I (in dbSNP:rs2228315). VAR_019156
132Missing (in short form; not analternative splicing; dbSNP:rs63748999).
246P -> S (in dbSNP:rs8179142). VAR_019157
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
42Pyrrolidone carboxylic acid.RDRRQATEY
CCCCCCCCC
54.23UniProtKB
Link-
46SulfotyrosineQATEYEYLD
CCCCCCCCC
12.91HPRD
Link
46SulfotyrosineQATEYEYLD
CCCCCCCCC
12.91HPRD
Link
46SulfotyrosineQATEYEYLD
CCCCCCCCC
12.91HPRD
Link
46SulfotyrosineQATEYEYLD
CCCCCCCCC
12.91HPRD
Link
46Sulfotyrosine.QATEYEYLD
CCCCCCCCC
12.91UniProtKB
Link
48SulfotyrosineTEYEYLDYD
CCCCCCCCC
12.17HPRD
Link
48SulfotyrosineTEYEYLDYD
CCCCCCCCC
12.17HPRD
Link
48SulfotyrosineTEYEYLDYD
CCCCCCCCC
12.17HPRD
Link
48Sulfotyrosine.TEYEYLDYD
CCCCCCCCC
12.17UniProtKB
Link
51SulfotyrosineEYLDYDFLP
CCCCCCCCC
13.14HPRD
Link
51SulfotyrosineEYLDYDFLP
CCCCCCCCC
13.14HPRD
Link
51SulfotyrosineEYLDYDFLP
CCCCCCCCC
13.14HPRD
Link
51Sulfotyrosine.EYLDYDFLP
CCCCCCCCC
13.14UniProtKB
Link
57O-linked (GalNAc...)FLPETEPPE
CCCCCCCCC
52.42HPRD
Link
57O-linked (GalNAc...).FLPETEPPE
CCCCCCCCC
52.42UniProtKB
Link
389PhosphoserineSKAKSPGLT
CCCCCCCCC
29.12HPRD
Link-
389PhosphoserineSKAKSPGLT
CCCCCCCCC
29.12PhosphoELM
Link-
389PhosphoserineSKAKSPGLT
CCCCCCCCC
29.12Phosphositeplus
Link-
389PhosphoserineSKAKSPGLT
CCCCCCCCC
29.12SysPTM
Link-
389Phosphoserine.SKAKSPGLT
CCCCCCCCC
29.12UniProtKB
Link-
393PhosphothreonineSPGLTPEPR
CCCCCCCCC
31.36HPRD
Link-
393PhosphothreonineSPGLTPEPR
CCCCCCCCC
31.36PhosphoELM
Link-
393PhosphothreonineSPGLTPEPR
CCCCCCCCC
31.36Phosphositeplus
Link-
393PhosphothreonineSPGLTPEPR
CCCCCCCCC
31.36SysPTM
Link-
393Phosphothreonine.SPGLTPEPR
CCCCCCCCC
31.36UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
LYAM2_HUMANin vitro
in vivo
HPRD:02845HPRD8621728
9128259
LYAM3_HUMANin vitro
in vivo
HPRD:02845HPRD9128259
10713099
MOES_HUMANin vitro
in vivo
HPRD:02845HPRD12115638
SELPL_HUMANin vitroHPRD:02845HPRD10713099
CSPG2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:02845HPRD15522894
KSYK_HUMANin vitroHPRD:02845HPRD12387735
LYAM3_HUMANENSP00000228463STRING
LYAM2_HUMANENSP00000228463STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"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.
Phosphorylation
ReferencePubMed
"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.
"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.
Sulfation
ReferencePubMed
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures