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P16109

- LYAM3_HUMAN

UniProt

P16109 - LYAM3_HUMAN

Protein

P-selectin

Gene

SELP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    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 PSGL1.1 Publication

    GO - Molecular functioni

    1. fucose binding Source: BHF-UCL
    2. glycosphingolipid binding Source: BHF-UCL
    3. heparin binding Source: BHF-UCL
    4. lipopolysaccharide binding Source: BHF-UCL
    5. oligosaccharide binding Source: BHF-UCL
    6. protein binding Source: UniProtKB
    7. sialic acid binding Source: BHF-UCL

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cell adhesion Source: ProtInc
    3. defense response to Gram-negative bacterium Source: BHF-UCL
    4. heterophilic cell-cell adhesion Source: Ensembl
    5. inflammatory response Source: Ensembl
    6. leukocyte cell-cell adhesion Source: BHF-UCL
    7. leukocyte migration Source: Reactome
    8. leukocyte tethering or rolling Source: Ensembl
    9. platelet activation Source: Reactome
    10. platelet degranulation Source: Reactome
    11. positive regulation of leukocyte migration Source: Ensembl
    12. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    13. positive regulation of platelet activation Source: BHF-UCL
    14. regulation of integrin activation Source: UniProtKB
    15. response to lipopolysaccharide Source: BHF-UCL

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Lectin

    Enzyme and pathway databases

    ReactomeiREACT_12051. Cell surface interactions at the vascular wall.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:SELP
    Synonyms:GMRP, GRMP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10721. SELP.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. external side of plasma membrane Source: BHF-UCL
    3. extracellular space Source: BHF-UCL
    4. integral component of plasma membrane Source: ProtInc
    5. nucleus Source: HPA
    6. plasma membrane Source: Reactome
    7. platelet alpha granule membrane Source: MGI
    8. platelet dense granule membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi173610. gene+phenotype.
    601367. phenotype.
    PharmGKBiPA35643.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4141Add
    BLAST
    Chaini42 – 830789P-selectinPRO_0000017498Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi54 – 541N-linked (GlcNAc...)1 Publication
    Disulfide bondi60 ↔ 158By similarity
    Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi131 ↔ 150By similarity
    Disulfide bondi163 ↔ 1741 Publication
    Disulfide bondi168 ↔ 1831 Publication
    Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi185 ↔ 1941 Publication
    Disulfide bondi200 ↔ 244By similarity
    Glycosylationi212 – 2121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi230 ↔ 257By similarity
    Disulfide bondi262 ↔ 306By similarity
    Disulfide bondi292 ↔ 319By similarity
    Disulfide bondi324 ↔ 368By similarity
    Disulfide bondi354 ↔ 381By similarity
    Disulfide bondi386 ↔ 430By similarity
    Glycosylationi411 – 4111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi416 ↔ 443By similarity
    Disulfide bondi448 ↔ 492By similarity
    Glycosylationi460 – 4601N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi478 ↔ 505By similarity
    Disulfide bondi510 ↔ 554By similarity
    Glycosylationi518 – 5181N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi540 ↔ 567By similarity
    Disulfide bondi572 ↔ 616By similarity
    Disulfide bondi602 ↔ 629By similarity
    Disulfide bondi642 ↔ 686By similarity
    Glycosylationi665 – 6651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi672 ↔ 699By similarity
    Disulfide bondi704 ↔ 748By similarity
    Glycosylationi716 – 7161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi723 – 7231N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi734 ↔ 761By similarity
    Glycosylationi741 – 7411N-linked (GlcNAc...)Sequence Analysis
    Lipidationi807 – 8071S-palmitoyl cysteine; alternate1 Publication
    Lipidationi807 – 8071S-stearoyl cysteine; alternate1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Proteomic databases

    PaxDbiP16109.
    PRIDEiP16109.

    PTM databases

    PhosphoSiteiP16109.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    ArrayExpressiP16109.
    BgeeiP16109.
    CleanExiHS_SELP.
    GenevestigatoriP16109.

    Organism-specific databases

    HPAiCAB002145.
    HPA002655.
    HPA005990.

    Interactioni

    Subunit structurei

    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 PSGL1.7 Publications

    Protein-protein interaction databases

    BioGridi112303. 8 interactions.
    DIPiDIP-37667N.
    IntActiP16109. 1 interaction.
    STRINGi9606.ENSP00000263686.

    Structurei

    Secondary structure

    1
    830
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi43 – 464
    Helixi53 – 6311
    Beta strandi64 – 674
    Helixi73 – 8210
    Beta strandi90 – 978
    Beta strandi100 – 1034
    Turni104 – 1063
    Turni112 – 1143
    Beta strandi131 – 1344
    Beta strandi139 – 1413
    Beta strandi145 – 1484
    Beta strandi154 – 1607
    Helixi167 – 1704
    Beta strandi171 – 1766
    Beta strandi178 – 1858
    Beta strandi189 – 1913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP16109.
    SMRiP16109. Positions 42-764.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16109.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini42 – 771730ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini796 – 83035CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei772 – 79524HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 158101C-type lectinPROSITE-ProRule annotationAdd
    BLAST
    Domaini159 – 19537EGF-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini198 – 25962Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini260 – 32162Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini322 – 38362Sushi 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini384 – 44562Sushi 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini446 – 50762Sushi 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini508 – 56962Sushi 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini570 – 63162Sushi 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini640 – 70162Sushi 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini702 – 76362Sushi 9PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni821 – 83010Interaction with SNX17

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi818 – 8214Endocytosis signalCurated

    Sequence similaritiesi

    Belongs to the selectin/LECAM family.Curated
    Contains 1 C-type lectin domain.PROSITE-ProRule annotation
    Contains 1 EGF-like domain.PROSITE-ProRule annotation
    Contains 9 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Sushi, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG242963.
    HOGENOMiHOG000236254.
    HOVERGENiHBG052375.
    InParanoidiP16109.
    KOiK06496.
    PhylomeDBiP16109.
    TreeFamiTF326910.

    Family and domain databases

    Gene3Di3.10.100.10. 1 hit.
    InterProiIPR001304. 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]
    PfamiPF00059. Lectin_C. 1 hit.
    PF00084. Sushi. 9 hits.
    [Graphical view]
    PRINTSiPR00343. SELECTIN.
    SMARTiSM00032. CCP. 9 hits.
    SM00034. CLECT. 1 hit.
    SM00181. EGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 1 hit.
    SSF57535. SSF57535. 9 hits.
    PROSITEiPS00615. 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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P16109-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANCQIAILY QRFQRVVFGI SQLLCFSALI SELTNQKEVA AWTYHYSTKA    50
    YSWNISRKYC QNRYTDLVAI QNKNEIDYLN KVLPYYSSYY WIGIRKNNKT 100
    WTWVGTKKAL TNEAENWADN EPNNKRNNED CVEIYIKSPS APGKWNDEHC 150
    LKKKHALCYT ASCQDMSCSK QGECLETIGN YTCSCYPGFY GPECEYVREC 200
    GELELPQHVL MNCSHPLGNF SFNSQCSFHC TDGYQVNGPS KLECLASGIW 250
    TNKPPQCLAA QCPPLKIPER GNMTCLHSAK AFQHQSSCSF SCEEGFALVG 300
    PEVVQCTASG VWTAPAPVCK AVQCQHLEAP SEGTMDCVHP LTAFAYGSSC 350
    KFECQPGYRV RGLDMLRCID SGHWSAPLPT CEAISCEPLE SPVHGSMDCS 400
    PSLRAFQYDT NCSFRCAEGF MLRGADIVRC DNLGQWTAPA PVCQALQCQD 450
    LPVPNEARVN CSHPFGAFRY QSVCSFTCNE GLLLVGASVL QCLATGNWNS 500
    VPPECQAIPC TPLLSPQNGT MTCVQPLGSS SYKSTCQFIC DEGYSLSGPE 550
    RLDCTRSGRW TDSPPMCEAI KCPELFAPEQ GSLDCSDTRG EFNVGSTCHF 600
    SCDNGFKLEG PNNVECTTSG RWSATPPTCK GIASLPTPGL QCPALTTPGQ 650
    GTMYCRHHPG TFGFNTTCYF GCNAGFTLIG DSTLSCRPSG QWTAVTPACR 700
    AVKCSELHVN KPIAMNCSNL WGNFSYGSIC SFHCLEGQLL NGSAQTACQE 750
    NGHWSTTVPT CQAGPLTIQE ALTYFGGAVA STIGLIMGGT LLALLRKRFR 800
    QKDDGKCPLN PHSHLGTYGV FTNAAFDPSP 830
    Length:830
    Mass (Da):90,834
    Last modified:November 25, 2008 - v3
    Checksum:iF53BC476AB6F70AC
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti179 – 1791G → R.1 Publication
    Corresponds to variant rs3917718 [ dbSNP | Ensembl ].
    VAR_019381
    Natural varianti209 – 2091V → M.2 Publications
    Corresponds to variant rs6125 [ dbSNP | Ensembl ].
    VAR_013910
    Natural varianti230 – 2301C → F.1 Publication
    Corresponds to variant rs3917869 [ dbSNP | Ensembl ].
    VAR_019382
    Natural varianti274 – 2741T → I.2 Publications
    Corresponds to variant rs3917724 [ dbSNP | Ensembl ].
    VAR_019383
    Natural varianti301 – 3011P → L.1 Publication
    Corresponds to variant rs6124 [ dbSNP | Ensembl ].
    VAR_013911
    Natural varianti331 – 3311S → N.3 Publications
    Corresponds to variant rs6131 [ dbSNP | Ensembl ].
    VAR_004192
    Natural varianti365 – 3651M → V.1 Publication
    Corresponds to variant rs6134 [ dbSNP | Ensembl ].
    VAR_013912
    Natural varianti385 – 3851S → L.1 Publication
    Corresponds to variant rs3917742 [ dbSNP | Ensembl ].
    VAR_019384
    Natural varianti500 – 5001S → F.1 Publication
    Corresponds to variant rs6130 [ dbSNP | Ensembl ].
    VAR_013913
    Natural varianti542 – 5421E → K.1 Publication
    Corresponds to variant rs3917769 [ dbSNP | Ensembl ].
    VAR_019385
    Natural varianti603 – 6031D → N.4 Publications
    Corresponds to variant rs6127 [ dbSNP | Ensembl ].
    VAR_004193
    Natural varianti619 – 6191S → A.1 Publication
    Corresponds to variant rs2228672 [ dbSNP | Ensembl ].
    VAR_019386
    Natural varianti631 – 6311G → V.1 Publication
    Corresponds to variant rs3917812 [ dbSNP | Ensembl ].
    VAR_019387
    Natural varianti640 – 6401L → V Associated with susceptibility to ischemic stroke. 5 Publications
    Corresponds to variant rs6133 [ dbSNP | Ensembl ].
    VAR_004194
    Natural varianti661 – 6611T → N.1 Publication
    Corresponds to variant rs3917814 [ dbSNP | Ensembl ].
    VAR_019388
    Natural varianti673 – 6731N → S.1 Publication
    Corresponds to variant rs3917815 [ dbSNP | Ensembl ].
    VAR_019389
    Natural varianti756 – 7561T → P Reduced frequency in patients with myocardial infarction. 3 Publications
    Corresponds to variant rs6136 [ dbSNP | Ensembl ].
    VAR_004195

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1282.1.
    PIRiA30359.
    RefSeqiNP_002996.2. NM_003005.3.
    XP_005245492.1. XM_005245435.1.
    XP_005245493.1. XM_005245436.1.
    UniGeneiHs.73800.

    Genome annotation databases

    EnsembliENST00000263686; ENSP00000263686; ENSG00000174175.
    GeneIDi6403.
    KEGGihsa:6403.

    Polymorphism databases

    DMDMi215274139.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs
    Functional Glycomics Gateway - Glycan Binding

    P-selectin

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS1282.1.
    PIRi A30359.
    RefSeqi NP_002996.2. NM_003005.3.
    XP_005245492.1. XM_005245435.1.
    XP_005245493.1. XM_005245436.1.
    UniGenei Hs.73800.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P16109.
    SMRi P16109. Positions 42-764.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112303. 8 interactions.
    DIPi DIP-37667N.
    IntActi P16109. 1 interaction.
    STRINGi 9606.ENSP00000263686.

    Chemistry

    BindingDBi P16109.
    ChEMBLi CHEMBL5378.
    DrugBanki DB00758. Clopidogrel.
    DB01109. Heparin.
    DB00775. Tirofiban.

    PTM databases

    PhosphoSitei P16109.

    Polymorphism databases

    DMDMi 215274139.

    Proteomic databases

    PaxDbi P16109.
    PRIDEi P16109.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263686 ; ENSP00000263686 ; ENSG00000174175 .
    GeneIDi 6403.
    KEGGi hsa:6403.

    Organism-specific databases

    CTDi 6403.
    GeneCardsi GC01M169558.
    HGNCi HGNC:10721. SELP.
    HPAi CAB002145.
    HPA002655.
    HPA005990.
    MIMi 173610. gene+phenotype.
    601367. phenotype.
    neXtProti NX_P16109.
    PharmGKBi PA35643.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG242963.
    HOGENOMi HOG000236254.
    HOVERGENi HBG052375.
    InParanoidi P16109.
    KOi K06496.
    PhylomeDBi P16109.
    TreeFami TF326910.

    Enzyme and pathway databases

    Reactomei REACT_12051. Cell surface interactions at the vascular wall.

    Miscellaneous databases

    EvolutionaryTracei P16109.
    GeneWikii P-selectin.
    GenomeRNAii 6403.
    NextBioi 24878.
    PROi P16109.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16109.
    Bgeei P16109.
    CleanExi HS_SELP.
    Genevestigatori P16109.

    Family and domain databases

    Gene3Di 3.10.100.10. 1 hit.
    InterProi 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 ]
    Pfami PF00059. Lectin_C. 1 hit.
    PF00084. Sushi. 9 hits.
    [Graphical view ]
    PRINTSi PR00343. SELECTIN.
    SMARTi SM00032. CCP. 9 hits.
    SM00034. CLECT. 1 hit.
    SM00181. EGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 1 hit.
    SSF57535. SSF57535. 9 hits.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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. 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. Cited for: VARIANTS MET-209; LEU-301; ASN-331; VAL-365; PHE-500; ASN-603; VAL-640 AND PRO-756.
    19. "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.

    Entry informationi

    Entry nameiLYAM3_HUMAN
    AccessioniPrimary (citable) accession number: P16109
    Secondary accession number(s): Q5R344, Q8IVD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 180 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3