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P16109

- LYAM3_HUMAN

UniProt

P16109 - LYAM3_HUMAN

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Protein

P-selectin

Gene

SELP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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 via plasma membrane cell adhesion molecules 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini42 – 771730ExtracellularSequence AnalysisAdd
BLAST
Transmembranei772 – 79524HelicalSequence AnalysisAdd
BLAST
Topological domaini796 – 83035CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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 ↔ 174
Disulfide bondi168 ↔ 183
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

BgeeiP16109.
CleanExiHS_SELP.
ExpressionAtlasiP16109. baseline and differential.
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 – 464Combined sources
Helixi53 – 6311Combined sources
Beta strandi64 – 674Combined sources
Helixi73 – 8210Combined sources
Beta strandi90 – 978Combined sources
Beta strandi100 – 1034Combined sources
Turni104 – 1063Combined sources
Turni112 – 1143Combined sources
Beta strandi131 – 1344Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi145 – 1484Combined sources
Beta strandi154 – 1607Combined sources
Helixi167 – 1704Combined sources
Beta strandi171 – 1766Combined sources
Beta strandi178 – 1858Combined sources
Beta strandi189 – 1913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 42-763.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16109.

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

        10         20         30         40         50
MANCQIAILY QRFQRVVFGI SQLLCFSALI SELTNQKEVA AWTYHYSTKA
60 70 80 90 100
YSWNISRKYC QNRYTDLVAI QNKNEIDYLN KVLPYYSSYY WIGIRKNNKT
110 120 130 140 150
WTWVGTKKAL TNEAENWADN EPNNKRNNED CVEIYIKSPS APGKWNDEHC
160 170 180 190 200
LKKKHALCYT ASCQDMSCSK QGECLETIGN YTCSCYPGFY GPECEYVREC
210 220 230 240 250
GELELPQHVL MNCSHPLGNF SFNSQCSFHC TDGYQVNGPS KLECLASGIW
260 270 280 290 300
TNKPPQCLAA QCPPLKIPER GNMTCLHSAK AFQHQSSCSF SCEEGFALVG
310 320 330 340 350
PEVVQCTASG VWTAPAPVCK AVQCQHLEAP SEGTMDCVHP LTAFAYGSSC
360 370 380 390 400
KFECQPGYRV RGLDMLRCID SGHWSAPLPT CEAISCEPLE SPVHGSMDCS
410 420 430 440 450
PSLRAFQYDT NCSFRCAEGF MLRGADIVRC DNLGQWTAPA PVCQALQCQD
460 470 480 490 500
LPVPNEARVN CSHPFGAFRY QSVCSFTCNE GLLLVGASVL QCLATGNWNS
510 520 530 540 550
VPPECQAIPC TPLLSPQNGT MTCVQPLGSS SYKSTCQFIC DEGYSLSGPE
560 570 580 590 600
RLDCTRSGRW TDSPPMCEAI KCPELFAPEQ GSLDCSDTRG EFNVGSTCHF
610 620 630 640 650
SCDNGFKLEG PNNVECTTSG RWSATPPTCK GIASLPTPGL QCPALTTPGQ
660 670 680 690 700
GTMYCRHHPG TFGFNTTCYF GCNAGFTLIG DSTLSCRPSG QWTAVTPACR
710 720 730 740 750
AVKCSELHVN KPIAMNCSNL WGNFSYGSIC SFHCLEGQLL NGSAQTACQE
760 770 780 790 800
NGHWSTTVPT CQAGPLTIQE ALTYFGGAVA STIGLIMGGT LLALLRKRFR
810 820 830
QKDDGKCPLN PHSHLGTYGV FTNAAFDPSP
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 42-763.
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 DB06779. Dalteparin.
DB01109. Heparin.
DB08813. Nadroparin.

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

Bgeei P16109.
CleanExi HS_SELP.
ExpressionAtlasi P16109. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 182 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