P16109 (LYAM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	830 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	EGF-like domain Repeat Signal Sushi Transmembrane Transmembrane helix
Ligand	Lectin
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	defense response to Gram-negative bacterium Inferred by curator PubMed 16514062. Source: BHF-UCL heterophilic cell-cell adhesion Inferred from electronic annotation. Source: Compara inflammatory response Inferred from electronic annotation. Source: Compara 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: Compara platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome positive regulation of leukocyte migration Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase cascade 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_component	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 to plasma membrane Traceable author statement PubMed 1701178. Source: ProtInc nucleus Inferred from direct assay. Source: HPA platelet alpha granule membrane Inferred from direct assay PubMed 15297306. Source: MGI platelet dense granule membrane Traceable author statement. Source: Reactome
Molecular_function	fucose 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 sialic acid binding Inferred from direct assay PubMed 7680663. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 41

41

Chain

42 – 830

789

P-selectin

PRO_0000017498

Regions

Topological domain

42 – 771

730

Extracellular Potential

Transmembrane

772 – 795

24

Helical; Potential

Topological domain

796 – 830

35

Cytoplasmic Potential

Domain

58 – 158

101

C-type lectin

Domain

159 – 195

37

EGF-like

Domain

198 – 259

62

Sushi 1

Domain

260 – 321

62

Sushi 2

Domain

322 – 383

62

Sushi 3

Domain

384 – 445

62

Sushi 4

Domain

446 – 507

62

Sushi 5

Domain

508 – 569

62

Sushi 6

Domain

570 – 631

62

Sushi 7

Domain

640 – 701

62

Sushi 8

Domain

702 – 763

62

Sushi 9

Region

821 – 830

10

Interaction with SNX17

Motif

818 – 821

4

Endocytosis signal Probable

Amino acid modifications

Lipidation

807

1

S-palmitoyl cysteine; alternate Ref.5

Lipidation

807

1

S-stearoyl cysteine; alternate

Glycosylation

54

1

N-linked (GlcNAc...) Ref.11

Glycosylation

98

1

N-linked (GlcNAc...) Potential

Glycosylation

180

1

N-linked (GlcNAc...) Potential

Glycosylation

212

1

N-linked (GlcNAc...) Potential

Glycosylation

219

1

N-linked (GlcNAc...) Potential

Glycosylation

411

1

N-linked (GlcNAc...) Potential

Glycosylation

460

1

N-linked (GlcNAc...) Potential

Glycosylation

518

1

N-linked (GlcNAc...) Potential

Glycosylation

665

1

N-linked (GlcNAc...) Potential

Glycosylation

716

1

N-linked (GlcNAc...) Potential

Glycosylation

723

1

N-linked (GlcNAc...) Potential

Glycosylation

741

1

N-linked (GlcNAc...) Potential

Disulfide bond

60 ↔ 158

By similarity

Disulfide bond

131 ↔ 150

By similarity

Disulfide bond

163 ↔ 174

Disulfide bond

168 ↔ 183

Disulfide bond

185 ↔ 194

Disulfide bond

200 ↔ 244

By similarity

Disulfide bond

230 ↔ 257

By similarity

Disulfide bond

262 ↔ 306

By similarity

Disulfide bond

292 ↔ 319

By similarity

Disulfide bond

324 ↔ 368

By similarity

Disulfide bond

354 ↔ 381

By similarity

Disulfide bond

386 ↔ 430

By similarity

Disulfide bond

416 ↔ 443

By similarity

Disulfide bond

448 ↔ 492

By similarity

Disulfide bond

478 ↔ 505

By similarity

Disulfide bond

510 ↔ 554

By similarity

Disulfide bond

540 ↔ 567

By similarity

Disulfide bond

572 ↔ 616

By similarity

Disulfide bond

602 ↔ 629

By similarity

Disulfide bond

642 ↔ 686

By similarity

Disulfide bond

672 ↔ 699

By similarity

Disulfide bond

704 ↔ 748

By similarity

Disulfide bond

734 ↔ 761

By similarity

Natural variations

Natural variant

179

1

G → R. Ref.2
Corresponds to variant rs3917718 [ dbSNP | Ensembl ].

VAR_019381

Natural variant

209

1

V → M. Ref.2 Ref.18
Corresponds to variant rs6125 [ dbSNP | Ensembl ].

VAR_013910

Natural variant

230

1

C → F. Ref.2
Corresponds to variant rs3917869 [ dbSNP | Ensembl ].

VAR_019382

Natural variant

274

1

T → I. Ref.1 Ref.2
Corresponds to variant rs3917724 [ dbSNP | Ensembl ].

VAR_019383

Natural variant

301

1

P → L. Ref.18
Corresponds to variant rs6124 [ dbSNP | Ensembl ].

VAR_013911

Natural variant

331

1

S → N. Ref.2 Ref.17 Ref.18
Corresponds to variant rs6131 [ dbSNP | Ensembl ].

VAR_004192

Natural variant

365

1

M → V. Ref.18
Corresponds to variant rs6134 [ dbSNP | Ensembl ].

VAR_013912

Natural variant

385

1

S → L. Ref.2
Corresponds to variant rs3917742 [ dbSNP | Ensembl ].

VAR_019384

Natural variant

500

1

S → F. Ref.18
Corresponds to variant rs6130 [ dbSNP | Ensembl ].

VAR_013913

Natural variant

542

1

E → K. Ref.2
Corresponds to variant rs3917769 [ dbSNP | Ensembl ].

VAR_019385

Natural variant

603

1

D → N. Ref.1 Ref.2 Ref.17 Ref.18
Corresponds to variant rs6127 [ dbSNP | Ensembl ].

VAR_004193

Natural variant

619

1

S → A. Ref.2
Corresponds to variant rs2228672 [ dbSNP | Ensembl ].

VAR_019386

Natural variant

631

1

G → V. Ref.2
Corresponds to variant rs3917812 [ dbSNP | Ensembl ].

VAR_019387

Natural variant

640

1

L → 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 variant

661

1

T → N. Ref.2
Corresponds to variant rs3917814 [ dbSNP | Ensembl ].

VAR_019388

Natural variant

673

1

N → S. Ref.2
Corresponds to variant rs3917815 [ dbSNP | Ensembl ].

VAR_019389

Natural variant

756

1

T → P Reduced frequency in patients with myocardial infarction. Ref.2 Ref.17 Ref.18
Corresponds to variant rs6136 [ dbSNP | Ensembl ].

VAR_004195

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

830

Helix Strand Turn

Details...

Beta strand

43 – 46

4

Helix

53 – 63

11

Beta strand

64 – 67

4

Helix

73 – 82

10

Beta strand

90 – 97

8

Beta strand

100 – 103

4

Turn

104 – 106

3

Turn

112 – 114

3

Beta strand

131 – 134

4

Beta strand

139 – 141

3

Beta strand

145 – 148

4

Beta strand

154 – 160

7

Helix

167 – 170

4

Beta strand

171 – 176

6

Beta strand

178 – 185

8

Beta strand

189 – 191

3

Sequences

	Sequence		Length	Mass (Da)
	P16109 [UniParc]. Last modified November 25, 2008. Version 3. Checksum: F53BC476AB6F70AC	FASTA	830	90,834
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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.

Web resources

SeattleSNPs

Functional Glycomics Gateway - Glycan Binding

P-selectin

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M60234 , 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.

IPI

IPI00295339.

PIR

A30359.

RefSeq

NP_002996.2. NM_003005.3.

UniGene

Hs.73800.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FSB	NMR	-	A	160-199	[»]
1G1Q	X-ray	2.40	A/B/C/D	42-198	[»]
1G1R	X-ray	3.40	A/B/C/D	42-198	[»]
1G1S	X-ray	1.90	A/B	42-198	[»]
1HES	X-ray	3.00	P	813-830	[»]
1KJD	model	-	A	42-161	[»]

ProteinModelPortal

P16109.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37667N.

IntAct

P16109. 1 interaction.

STRING

9606.ENSP00000263686.

PTM databases

PhosphoSite

P16109.

Polymorphism databases

DMDM

215274139.

Proteomic databases

PaxDb

P16109.

PRIDE

P16109.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263686; ENSP00000263686; ENSG00000174175.
ENST00000367790; ENSP00000356764; ENSG00000174175.

GeneID

6403.

KEGG

hsa:6403.

Organism-specific databases

CTD

6403.

GeneCards

GC01M169558.

HGNC

HGNC:10721. SELP.

HPA

CAB002145.
HPA002655.
HPA005990.

MIM

173610. gene+phenotype.
601367. phenotype.

neXtProt

NX_P16109.

PharmGKB

PA35643.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG242963.

HOGENOM

HOG000236254.

HOVERGEN

HBG052375.

InParanoid

P16109.

KO

K06496.

Enzyme and pathway databases

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.
il4_2pathway. IL4-mediated signaling events.

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P16109.

Bgee

P16109.

CleanEx

HS_SELP.

Genevestigator

P16109.

GermOnline

ENSG00000174175. Homo sapiens.

Family and domain databases

Gene3D

3.10.100.10. 1 hit.

InterPro

IPR001304. 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]

Pfam

PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 9 hits.
[Graphical view]

PRINTS

PR00343. SELECTIN.

SMART

SM00032. CCP. 9 hits.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 1 hit.
SSF57535. Complement_control_module. 9 hits.

PROSITE

PS00615. 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]

ProtoNet

Search...

Other

BindingDB

P16109.

ChEMBL

CHEMBL5378.

DrugBank

DB00758. Clopidogrel.
DB01109. Heparin.
DB00775. Tirofiban.

EvolutionaryTrace

P16109.

GenomeRNAi

6403.

NextBio

24878.

SOURCE

Search...

Entry information

Entry name

LYAM3_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 167 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.