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Protein

E-selectin

Gene

SELE

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

Functioni

Cell-surface glycoprotein having a role in immunoadhesion. Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with PSGL1/SELPLG. May have a role in capillary morphogenesis.1 Publication

GO - Molecular functioni

  • oligosaccharide binding Source: BHF-UCL
  • phospholipase binding Source: BHF-UCL
  • sialic acid binding Source: BHF-UCL
  • transmembrane signaling receptor activity Source: BHF-UCL

GO - Biological processi

  • actin filament-based process Source: BHF-UCL
  • activation of phospholipase C activity Source: BHF-UCL
  • calcium-mediated signaling Source: BHF-UCL
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: BHF-UCL
  • inflammatory response Source: ProtInc
  • leukocyte cell-cell adhesion Source: BHF-UCL
  • leukocyte migration Source: Reactome
  • leukocyte migration involved in inflammatory response Source: BHF-UCL
  • leukocyte tethering or rolling Source: BHF-UCL
  • positive regulation of receptor internalization Source: BHF-UCL
  • regulation of inflammatory response Source: BHF-UCL
  • response to interleukin-1 Source: BHF-UCL
  • response to lipopolysaccharide Source: BHF-UCL
  • response to tumor necrosis factor Source: BHF-UCL

Keywordsi

Biological processCell adhesion
LigandLectin

Enzyme and pathway databases

ReactomeiR-HSA-202733. Cell surface interactions at the vascular wall.
SIGNORiP16581.

Names & Taxonomyi

Protein namesi
Recommended name:
E-selectin
Alternative name(s):
CD62 antigen-like family member E
Endothelial leukocyte adhesion molecule 1
Short name:
ELAM-1
Leukocyte-endothelial cell adhesion molecule 2
Short name:
LECAM2
CD_antigen: CD62E
Gene namesi
Name:SELE
Synonyms:ELAM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000007908.15.
HGNCiHGNC:10718. SELE.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 556ExtracellularSequence analysisAdd BLAST535
Transmembranei557 – 578HelicalSequence analysisAdd BLAST22
Topological domaini579 – 610CytoplasmicSequence analysisAdd BLAST32

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi6401.
OpenTargetsiENSG00000007908.
Orphaneti34145. Berger disease.
PharmGKBiPA35640.

Chemistry databases

ChEMBLiCHEMBL3890.
DrugBankiDB01136. Carvedilol.
DB03721. N-acetyl-alpha-neuraminic acid.

Polymorphism and mutation databases

BioMutaiSELE.
DMDMi126180.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Add BLAST21
ChainiPRO_000001749222 – 610E-selectinAdd BLAST589

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi25N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi40 ↔ 1381 Publication
Disulfide bondi111 ↔ 1301 Publication
Disulfide bondi143 ↔ 1541 Publication
Glycosylationi145N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi148 ↔ 1631 Publication
Glycosylationi160N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi165 ↔ 1741 Publication
Glycosylationi179N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi180 ↔ 224By similarity
Glycosylationi199N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi203N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi210 ↔ 237By similarity
Disulfide bondi242 ↔ 286By similarity
Glycosylationi265N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi272 ↔ 299By similarity
Disulfide bondi304 ↔ 349By similarity
Glycosylationi312N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi332N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi335 ↔ 362By similarity
Disulfide bondi367 ↔ 412By similarity
Disulfide bondi398 ↔ 425By similarity
Disulfide bondi430 ↔ 475By similarity
Disulfide bondi461 ↔ 488By similarity
Disulfide bondi493 ↔ 534By similarity
Glycosylationi503N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi520 ↔ 547By similarity
Glycosylationi527N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP16581.
PaxDbiP16581.
PeptideAtlasiP16581.
PRIDEiP16581.

PTM databases

iPTMnetiP16581.
PhosphoSitePlusiP16581.

Expressioni

Gene expression databases

BgeeiENSG00000007908.
ExpressionAtlasiP16581. baseline and differential.
GenevisibleiP16581. HS.

Organism-specific databases

HPAiCAB002143.

Interactioni

Subunit structurei

Interacts with PSGL1/SELPLG and PODXL2 through the sialyl Lewis X epitope. PSGL1 sulfation appears not to be required for this interaction.2 Publications

GO - Molecular functioni

  • phospholipase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi112301. 16 interactors.
DIPiDIP-58639N.
IntActiP16581. 1 interactor.
MINTiMINT-8020220.
STRINGi9606.ENSP00000331736.

Chemistry databases

BindingDBiP16581.

Structurei

Secondary structure

1610
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 26Combined sources4
Helixi33 – 43Combined sources11
Beta strandi44 – 47Combined sources4
Helixi53 – 62Combined sources10
Beta strandi70 – 77Combined sources8
Beta strandi80 – 83Combined sources4
Turni84 – 86Combined sources3
Turni92 – 94Combined sources3
Beta strandi111 – 114Combined sources4
Beta strandi119 – 121Combined sources3
Beta strandi125 – 128Combined sources4
Beta strandi134 – 140Combined sources7
Helixi147 – 150Combined sources4
Beta strandi151 – 157Combined sources7
Beta strandi160 – 165Combined sources6
Beta strandi169 – 171Combined sources3
Beta strandi189 – 194Combined sources6
Beta strandi196 – 198Combined sources3
Beta strandi205 – 210Combined sources6
Beta strandi214 – 217Combined sources4
Beta strandi222 – 224Combined sources3
Beta strandi230 – 232Combined sources3
Beta strandi237 – 239Combined sources3
Beta strandi251 – 254Combined sources4
Beta strandi267 – 272Combined sources6
Beta strandi277 – 280Combined sources4
Beta strandi282 – 286Combined sources5
Beta strandi292 – 294Combined sources3
Beta strandi298 – 300Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ESLX-ray2.00A22-183[»]
1G1TX-ray1.50A22-178[»]
1KJAmodel-A22-141[»]
4C16X-ray1.93A/B22-301[»]
4CSYX-ray2.41A/B22-301[»]
ProteinModelPortaliP16581.
SMRiP16581.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16581.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 139C-type lectinPROSITE-ProRule annotationAdd BLAST118
Domaini140 – 175EGF-likePROSITE-ProRule annotationAdd BLAST36
Domaini178 – 239Sushi 1PROSITE-ProRule annotationAdd BLAST62
Domaini240 – 301Sushi 2PROSITE-ProRule annotationAdd BLAST62
Domaini303 – 364Sushi 3PROSITE-ProRule annotationAdd BLAST62
Domaini366 – 427Sushi 4PROSITE-ProRule annotationAdd BLAST62
Domaini429 – 490Sushi 5PROSITE-ProRule annotationAdd BLAST62
Domaini491 – 549Sushi 6PROSITE-ProRule annotationAdd BLAST59

Sequence similaritiesi

Belongs to the selectin/LECAM family.Curated

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00870000136398.
HOGENOMiHOG000236254.
HOVERGENiHBG052375.
InParanoidiP16581.
KOiK06494.
OMAiQGQWTQQ.
OrthoDBiEOG091G04KC.
PhylomeDBiP16581.
TreeFamiTF326910.

Family and domain databases

CDDicd00033. CCP. 6 hits.
cd03592. CLECT_selectins_like. 1 hit.
Gene3Di3.10.100.10. 1 hit.
InterProiView protein in InterPro
IPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_fold.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR033991. Selectin_CTLD.
IPR002396. Selectin_superfamily.
IPR000436. Sushi_SCR_CCP_dom.
PfamiView protein in Pfam
PF00008. EGF. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 6 hits.
PRINTSiPR00343. SELECTIN.
SMARTiView protein in SMART
SM00032. CCP. 6 hits.
SM00034. CLECT. 1 hit.
SM00181. EGF. 2 hits.
SUPFAMiSSF56436. SSF56436. 1 hit.
SSF57535. SSF57535. 6 hits.
PROSITEiView protein in 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. 6 hits.

Sequencei

Sequence statusi: Complete.

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

P16581-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIASQFLSAL TLVLLIKESG AWSYNTSTEA MTYDEASAYC QQRYTHLVAI
60 70 80 90 100
QNKEEIEYLN SILSYSPSYY WIGIRKVNNV WVWVGTQKPL TEEAKNWAPG
110 120 130 140 150
EPNNRQKDED CVEIYIKREK DVGMWNDERC SKKKLALCYT AACTNTSCSG
160 170 180 190 200
HGECVETINN YTCKCDPGFS GLKCEQIVNC TALESPEHGS LVCSHPLGNF
210 220 230 240 250
SYNSSCSISC DRGYLPSSME TMQCMSSGEW SAPIPACNVV ECDAVTNPAN
260 270 280 290 300
GFVECFQNPG SFPWNTTCTF DCEEGFELMG AQSLQCTSSG NWDNEKPTCK
310 320 330 340 350
AVTCRAVRQP QNGSVRCSHS PAGEFTFKSS CNFTCEEGFM LQGPAQVECT
360 370 380 390 400
TQGQWTQQIP VCEAFQCTAL SNPERGYMNC LPSASGSFRY GSSCEFSCEQ
410 420 430 440 450
GFVLKGSKRL QCGPTGEWDN EKPTCEAVRC DAVHQPPKGL VRCAHSPIGE
460 470 480 490 500
FTYKSSCAFS CEEGFELHGS TQLECTSQGQ WTEEVPSCQV VKCSSLAVPG
510 520 530 540 550
KINMSCSGEP VFGTVCKFAC PEGWTLNGSA ARTCGATGHW SGLLPTCEAP
560 570 580 590 600
TESNIPLVAG LSAAGLSLLT LAPFLLWLRK CLRKAKKFVP ASSCQSLESD
610
GSYQKPSYIL
Length:610
Mass (Da):66,655
Last modified:August 1, 1990 - v1
Checksum:i7D43E3C0D1229229
GO

Polymorphismi

A polymorphism in position 149 is associated with a higher risk of coronary artery disease (CAD). A significantly higher mutation frequency (Arg-149) is observed in patients with angiographically proven severe atherosclerosis compared with an unselected population (Ser-149).2 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01430021A → S1 PublicationCorresponds to variant dbSNP:rs3917407Ensembl.1
Natural variantiVAR_01430131M → I1 PublicationCorresponds to variant dbSNP:rs3917408Ensembl.1
Natural variantiVAR_011790130C → W. Corresponds to variant dbSNP:rs5360Ensembl.1
Natural variantiVAR_004191149S → R Polymorphism associated with coronary artery disease; no effect on ligand-specificity; may increase levels of rolling and adhesion of neutrophils and peripheral blood mononuclear cells to the endothelium; may induce constitutive stimulation of the MAPK signaling pathway, in the absence of leukocyte adhesion. 7 PublicationsCorresponds to variant dbSNP:rs5361Ensembl.1
Natural variantiVAR_014302257Q → P1 PublicationCorresponds to variant dbSNP:rs3917422Ensembl.1
Natural variantiVAR_011791295E → K1 PublicationCorresponds to variant dbSNP:rs5364Ensembl.1
Natural variantiVAR_011792421E → Q1 PublicationCorresponds to variant dbSNP:rs5366Ensembl.1
Natural variantiVAR_011793468H → Y2 PublicationsCorresponds to variant dbSNP:rs5368Ensembl.1
Natural variantiVAR_074189545P → L1 Publication1
Natural variantiVAR_014303550P → S1 PublicationCorresponds to variant dbSNP:rs3917429Ensembl.1
Natural variantiVAR_011794575L → F4 PublicationsCorresponds to variant dbSNP:rs5355Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30640 mRNA. Translation: AAA52377.1.
M61893
, M61895, M61887, M61888, M61890, M61891, M61892 Genomic DNA. Translation: AAA52375.1.
M24736 mRNA. Translation: AAA52376.1.
AF540378 Genomic DNA. Translation: AAN01237.1.
AL021940 Genomic DNA. No translation available.
CH471067 Genomic DNA. Translation: EAW90860.1.
BC131551 mRNA. Translation: AAI31552.1.
BC142677 mRNA. Translation: AAI42678.1.
BC142711 mRNA. Translation: AAI42712.1.
CCDSiCCDS1283.1.
PIRiA38615. A35046.
RefSeqiNP_000441.2. NM_000450.2.
UniGeneiHs.82848.

Genome annotation databases

EnsembliENST00000333360; ENSP00000331736; ENSG00000007908.
GeneIDi6401.
KEGGihsa:6401.
UCSCiuc001ggm.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiLYAM2_HUMAN
AccessioniPrimary (citable) accession number: P16581
Secondary accession number(s): A2RRD6, P16111
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: September 27, 2017
This is version 204 of the entry and version 1 of the sequence. See 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