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P16109 (LYAM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 178. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
P-selectin
Alternative name(s):
CD62 antigen-like family member P
Granule membrane protein 140
Short name=GMP-140
Leukocyte-endothelial cell adhesion molecule 3
Short name=LECAM3
Platelet activation dependent granule-external membrane protein
Short name=PADGEM
CD_antigen=CD62P
Gene names
Name:SELP
Synonyms:GMRP, GRMP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length830 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ca2+-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 PSGL1. Ref.7

Subunit structure

Interacts with SNX17. Interacts with PSGL1/SEPL and PODXL2 and mediates neutrophil adhesion and leukocyte rolling. This interaction requires the sialyl-Lewis X epitope of PSGL1 and PODXL2, and specific tyrosine sulfation on PSGL1. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.15

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. Upon cell activation by agonists, P-selectin is transported rapidly to the cell surface.

Involvement in disease

Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.20

Sequence similarities

Belongs to the selectin/LECAM family.

Contains 1 C-type lectin domain.

Contains 1 EGF-like domain.

Contains 9 Sushi (CCP/SCR) domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainEGF-like domain
Repeat
Signal
Sushi
Transmembrane
Transmembrane helix
   LigandLectin
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

cell adhesion

Traceable author statement Ref.1. Source: ProtInc

defense response to Gram-negative bacterium

Inferred by curator PubMed 16514062. Source: BHF-UCL

heterophilic cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: Ensembl

leukocyte cell-cell adhesion

Inferred from direct assay PubMed 7680663. Source: BHF-UCL

leukocyte migration

Traceable author statement. Source: Reactome

leukocyte tethering or rolling

Inferred from electronic annotation. Source: Ensembl

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of leukocyte migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from direct assay PubMed 17632516. Source: UniProtKB

positive regulation of platelet activation

Inferred from sequence or structural similarity PubMed 16514062. Source: BHF-UCL

regulation of integrin activation

Inferred from mutant phenotype PubMed 17632516. Source: UniProtKB

response to lipopolysaccharide

Inferred by curator PubMed 16514062. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

external side of plasma membrane

Inferred from direct assay PubMed 16514062. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 9290466. Source: BHF-UCL

integral component of plasma membrane

Traceable author statement PubMed 1701178. Source: ProtInc

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Traceable author statement. Source: Reactome

platelet alpha granule membrane

Inferred from direct assay PubMed 15297306. Source: MGI

platelet dense granule membrane

Traceable author statement. Source: Reactome

   Molecular_functionfucose binding

Inferred from direct assay PubMed 7680663. Source: BHF-UCL

glycosphingolipid binding

Traceable author statement PubMed 7680663. Source: BHF-UCL

heparin binding

Inferred from direct assay PubMed 7680663. Source: BHF-UCL

lipopolysaccharide binding

Inferred from mutant phenotype PubMed 16514062. Source: BHF-UCL

oligosaccharide binding

Inferred from direct assay PubMed 7680663. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.9PubMed 15633604Ref.12PubMed 9129046. Source: UniProtKB

sialic acid binding

Inferred from direct assay PubMed 7680663. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141
Chain42 – 830789P-selectin
PRO_0000017498

Regions

Topological domain42 – 771730Extracellular Potential
Transmembrane772 – 79524Helical; Potential
Topological domain796 – 83035Cytoplasmic Potential
Domain58 – 158101C-type lectin
Domain159 – 19537EGF-like
Domain198 – 25962Sushi 1
Domain260 – 32162Sushi 2
Domain322 – 38362Sushi 3
Domain384 – 44562Sushi 4
Domain446 – 50762Sushi 5
Domain508 – 56962Sushi 6
Domain570 – 63162Sushi 7
Domain640 – 70162Sushi 8
Domain702 – 76362Sushi 9
Region821 – 83010Interaction with SNX17
Motif818 – 8214Endocytosis signal Probable

Amino acid modifications

Lipidation8071S-palmitoyl cysteine; alternate Ref.5
Lipidation8071S-stearoyl cysteine; alternate
Glycosylation541N-linked (GlcNAc...) Ref.11
Glycosylation981N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation4111N-linked (GlcNAc...) Potential
Glycosylation4601N-linked (GlcNAc...) Potential
Glycosylation5181N-linked (GlcNAc...) Potential
Glycosylation6651N-linked (GlcNAc...) Potential
Glycosylation7161N-linked (GlcNAc...) Potential
Glycosylation7231N-linked (GlcNAc...) Potential
Glycosylation7411N-linked (GlcNAc...) Potential
Disulfide bond60 ↔ 158 By similarity
Disulfide bond131 ↔ 150 By similarity
Disulfide bond163 ↔ 174
Disulfide bond168 ↔ 183
Disulfide bond185 ↔ 194
Disulfide bond200 ↔ 244 By similarity
Disulfide bond230 ↔ 257 By similarity
Disulfide bond262 ↔ 306 By similarity
Disulfide bond292 ↔ 319 By similarity
Disulfide bond324 ↔ 368 By similarity
Disulfide bond354 ↔ 381 By similarity
Disulfide bond386 ↔ 430 By similarity
Disulfide bond416 ↔ 443 By similarity
Disulfide bond448 ↔ 492 By similarity
Disulfide bond478 ↔ 505 By similarity
Disulfide bond510 ↔ 554 By similarity
Disulfide bond540 ↔ 567 By similarity
Disulfide bond572 ↔ 616 By similarity
Disulfide bond602 ↔ 629 By similarity
Disulfide bond642 ↔ 686 By similarity
Disulfide bond672 ↔ 699 By similarity
Disulfide bond704 ↔ 748 By similarity
Disulfide bond734 ↔ 761 By similarity

Natural variations

Natural variant1791G → R. Ref.2
Corresponds to variant rs3917718 [ dbSNP | Ensembl ].
VAR_019381
Natural variant2091V → M. Ref.2 Ref.18
Corresponds to variant rs6125 [ dbSNP | Ensembl ].
VAR_013910
Natural variant2301C → F. Ref.2
Corresponds to variant rs3917869 [ dbSNP | Ensembl ].
VAR_019382
Natural variant2741T → I. Ref.1 Ref.2
Corresponds to variant rs3917724 [ dbSNP | Ensembl ].
VAR_019383
Natural variant3011P → L. Ref.18
Corresponds to variant rs6124 [ dbSNP | Ensembl ].
VAR_013911
Natural variant3311S → N. Ref.2 Ref.17 Ref.18
Corresponds to variant rs6131 [ dbSNP | Ensembl ].
VAR_004192
Natural variant3651M → V. Ref.18
Corresponds to variant rs6134 [ dbSNP | Ensembl ].
VAR_013912
Natural variant3851S → L. Ref.2
Corresponds to variant rs3917742 [ dbSNP | Ensembl ].
VAR_019384
Natural variant5001S → F. Ref.18
Corresponds to variant rs6130 [ dbSNP | Ensembl ].
VAR_013913
Natural variant5421E → K. Ref.2
Corresponds to variant rs3917769 [ dbSNP | Ensembl ].
VAR_019385
Natural variant6031D → N. Ref.1 Ref.2 Ref.17 Ref.18
Corresponds to variant rs6127 [ dbSNP | Ensembl ].
VAR_004193
Natural variant6191S → A. Ref.2
Corresponds to variant rs2228672 [ dbSNP | Ensembl ].
VAR_019386
Natural variant6311G → V. Ref.2
Corresponds to variant rs3917812 [ dbSNP | Ensembl ].
VAR_019387
Natural variant6401L → V Associated with susceptibility to ischemic stroke. Ref.2 Ref.3 Ref.4 Ref.17 Ref.18 Ref.20
Corresponds to variant rs6133 [ dbSNP | Ensembl ].
VAR_004194
Natural variant6611T → N. Ref.2
Corresponds to variant rs3917814 [ dbSNP | Ensembl ].
VAR_019388
Natural variant6731N → S. Ref.2
Corresponds to variant rs3917815 [ dbSNP | Ensembl ].
VAR_019389
Natural variant7561T → P Reduced frequency in patients with myocardial infarction. Ref.2 Ref.17 Ref.18
Corresponds to variant rs6136 [ dbSNP | Ensembl ].
VAR_004195

Secondary structure

.............................. 830
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16109 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: F53BC476AB6F70AC

FASTA83090,834
        10         20         30         40         50         60 
MANCQIAILY QRFQRVVFGI SQLLCFSALI SELTNQKEVA AWTYHYSTKA YSWNISRKYC 

        70         80         90        100        110        120 
QNRYTDLVAI QNKNEIDYLN KVLPYYSSYY WIGIRKNNKT WTWVGTKKAL TNEAENWADN 

       130        140        150        160        170        180 
EPNNKRNNED CVEIYIKSPS APGKWNDEHC LKKKHALCYT ASCQDMSCSK QGECLETIGN 

       190        200        210        220        230        240 
YTCSCYPGFY GPECEYVREC GELELPQHVL MNCSHPLGNF SFNSQCSFHC TDGYQVNGPS 

       250        260        270        280        290        300 
KLECLASGIW TNKPPQCLAA QCPPLKIPER GNMTCLHSAK AFQHQSSCSF SCEEGFALVG 

       310        320        330        340        350        360 
PEVVQCTASG VWTAPAPVCK AVQCQHLEAP SEGTMDCVHP LTAFAYGSSC KFECQPGYRV 

       370        380        390        400        410        420 
RGLDMLRCID SGHWSAPLPT CEAISCEPLE SPVHGSMDCS PSLRAFQYDT NCSFRCAEGF 

       430        440        450        460        470        480 
MLRGADIVRC DNLGQWTAPA PVCQALQCQD LPVPNEARVN CSHPFGAFRY QSVCSFTCNE 

       490        500        510        520        530        540 
GLLLVGASVL QCLATGNWNS VPPECQAIPC TPLLSPQNGT MTCVQPLGSS SYKSTCQFIC 

       550        560        570        580        590        600 
DEGYSLSGPE RLDCTRSGRW TDSPPMCEAI KCPELFAPEQ GSLDCSDTRG EFNVGSTCHF 

       610        620        630        640        650        660 
SCDNGFKLEG PNNVECTTSG RWSATPPTCK GIASLPTPGL QCPALTTPGQ GTMYCRHHPG 

       670        680        690        700        710        720 
TFGFNTTCYF GCNAGFTLIG DSTLSCRPSG QWTAVTPACR AVKCSELHVN KPIAMNCSNL 

       730        740        750        760        770        780 
WGNFSYGSIC SFHCLEGQLL NGSAQTACQE NGHWSTTVPT CQAGPLTIQE ALTYFGGAVA 

       790        800        810        820        830 
STIGLIMGGT LLALLRKRFR QKDDGKCPLN PHSHLGTYGV FTNAAFDPSP 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of GMP-140, a granule membrane protein of platelets and endothelium: sequence similarity to proteins involved in cell adhesion and inflammation."
Johnston G.I., Cook R.G., McEver R.P.
Cell 56:1033-1044(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS ILE-274 AND ASN-603.
[2]SeattleSNPs variation discovery resource
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-179; MET-209; PHE-230; ILE-274; ASN-331; LEU-385; LYS-542; ASN-603; ALA-619; VAL-631; VAL-640; ASN-661; SER-673 AND PRO-756.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-640.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-640.
[5]"P-selectin is acylated with palmitic acid and stearic acid at cysteine 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-807, STEAROYLATION AT CYS-807.
[6]"A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding."
Sako D., Comess K.M., Barone K.M., Camphausen R.T., Cumming D.A., Shaw G.D.
Cell 83:323-331(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SELPLG.
[7]"PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus."
Pouyani T., Seed B.
Cell 83:333-343(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SELPLG, FUNCTION.
[8]"Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin."
Wilkins P.P., Moore K.L., McEver R.P., Cummings R.D.
J. Biol. Chem. 270:22677-22680(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SELPLG.
[9]"A new member of the sorting nexin family interacts with the C-terminus of P-selectin."
Florian V., Schlueter T., Bohnensack R.
Biochem. Biophys. Res. Commun. 281:1045-1050(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX17.
[10]"Functions of sorting nexin 17 domains and recognition motif for P-selectin trafficking."
Knauth P., Schlueter T., Czubayko M., Kirsch C., Florian V., Schreckenberger S., Hahn H., Bohnensack R.
J. Mol. Biol. 347:813-825(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX17.
[11]"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
Lewandrowski U., Moebius J., Walter U., Sickmann A.
Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-54.
Tissue: Platelet.
[12]"Endoglycan, a member of the CD34 family of sialomucins, is a ligand for the vascular selectins."
Kerr S.C., Fieger C.B., Snapp K.R., Rosen S.D.
J. Immunol. 181:1480-1490(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PODXL2.
[13]"Structure and function of the epidermal growth factor domain of P-selectin."
Freedman S.J., Sanford D.G., Bachovchin W.W., Furie B.C., Baleja J.D., Furie B.
Biochemistry 35:13733-13744(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 160-199.
[14]"Knowledge-based model building of proteins: concepts and examples."
Bajorath J., Stenkamp R., Aruffo A.
Protein Sci. 2:1798-1810(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 42-161.
[15]"Insights into the molecular basis of leukocyte tethering and rolling revealed 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) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-198 IN COMPLEX WITH CALCIUM IONS AND SELPLG, SUBUNIT, DISULFIDE BONDS AT 60-CYS--CYS-158; 131-CYS--CYS-150; 163-CYS--CYS-183 AND 185-CYS--CYS-194.
[16]Erratum
Somers W.S., Tang J., Shaw G.D., Camphausen R.T.
Cell 105:971-971(2001)
[17]"The P-selectin gene is highly polymorphic: reduced frequency of the Pro715 allele carriers in patients with myocardial infarction."
Herrmann S.M., Ricard S., Nicaud V., Mallet C., Evans A., Ruidavets J.B., Arveiler D., Luc G., Cambien F.
Hum. Mol. Genet. 7:1277-1284(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASN-331; ASN-603; VAL-640 AND PRO-756.
[18]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MET-209; LEU-301; ASN-331; VAL-365; PHE-500; ASN-603; VAL-640 AND PRO-756.
[19]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[20]"Polymorphism in the P-selectin and interleukin-4 genes as determinants of stroke: a population-based, prospective genetic analysis."
Zee R.Y.L., Cook N.R., Cheng S., Reynolds R., Erlich H.A., Lindpaintner K., Ridker P.M.
Hum. Mol. Genet. 13:389-396(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION OF VARIANT VAL-640 WITH SUSCEPTIBILITY TO ISCHSTR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60234 expand/collapse EMBL AC list , M60217, M60218, M60219, M60222, M60223, M60224, M60225, M60226, M60227, M60228, M60229, M60231, M60232, M60233 Genomic DNA. Translation: AAA35910.1.
M25322 mRNA. Translation: AAA35911.1.
AF542391 Genomic DNA. Translation: AAN06828.1.
AL022146, Z99572 Genomic DNA. Translation: CAI22753.1.
Z99572, AL022146 Genomic DNA. Translation: CAI23058.1.
CH471067 Genomic DNA. Translation: EAW90851.1.
CCDSCCDS1282.1.
PIRA30359.
RefSeqNP_002996.2. NM_003005.3.
XP_005245492.1. XM_005245435.1.
XP_005245493.1. XM_005245436.1.
UniGeneHs.73800.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FSBNMR-A160-199[»]
1G1QX-ray2.40A/B/C/D42-198[»]
1G1RX-ray3.40A/B/C/D42-198[»]
1G1SX-ray1.90A/B42-198[»]
1HESX-ray3.00P813-830[»]
1KJDmodel-A42-161[»]
ProteinModelPortalP16109.
SMRP16109. Positions 42-764.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112303. 8 interactions.
DIPDIP-37667N.
IntActP16109. 1 interaction.
STRING9606.ENSP00000263686.

Chemistry

BindingDBP16109.
ChEMBLCHEMBL5378.
DrugBankDB00758. Clopidogrel.
DB01109. Heparin.
DB00775. Tirofiban.

PTM databases

PhosphoSiteP16109.

Polymorphism databases

DMDM215274139.

Proteomic databases

PaxDbP16109.
PRIDEP16109.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263686; ENSP00000263686; ENSG00000174175.
GeneID6403.
KEGGhsa:6403.

Organism-specific databases

CTD6403.
GeneCardsGC01M169558.
HGNCHGNC:10721. SELP.
HPACAB002145.
HPA002655.
HPA005990.
MIM173610. gene+phenotype.
601367. phenotype.
neXtProtNX_P16109.
PharmGKBPA35643.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG242963.
HOGENOMHOG000236254.
HOVERGENHBG052375.
InParanoidP16109.
KOK06496.
PhylomeDBP16109.
TreeFamTF326910.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP16109.
BgeeP16109.
CleanExHS_SELP.
GenevestigatorP16109.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002396. Selectin_superfamily.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00059. Lectin_C. 1 hit.
PF00084. Sushi. 9 hits.
[Graphical view]
PRINTSPR00343. SELECTIN.
SMARTSM00032. CCP. 9 hits.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
SSF57535. SSF57535. 9 hits.
PROSITEPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS50923. SUSHI. 9 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16109.
GeneWikiP-selectin.
GenomeRNAi6403.
NextBio24878.
PROP16109.
SOURCESearch...

Entry information

Entry nameLYAM3_HUMAN
AccessionPrimary (citable) accession number: P16109
Secondary accession number(s): Q5R344, Q8IVD1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 178 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries