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Protein

Platelet endothelial cell adhesion molecule

Gene

PECAM1

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

Functioni

Induces susceptibility to atherosclerosis (By similarity). Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-690 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Isoform Delta15 is unable to protect against apoptosis. Modulates BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in human umbilical cord vein cells (HUVEC).By similarity2 Publications

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • cell recognition Source: ProtInc
  • diapedesis Source: UniProtKB
  • extracellular matrix organization Source: Reactome
  • glomerular endothelium development Source: UniProtKB
  • leukocyte migration Source: Reactome
  • phagocytosis Source: UniProtKB
  • platelet degranulation Source: Reactome
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Phagocytosis

Enzyme and pathway databases

BioCyciZFISH:G66-32708-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-210990. PECAM1 interactions.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-432142. Platelet sensitization by LDL.
R-HSA-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet endothelial cell adhesion molecule
Short name:
PECAM-1
Alternative name(s):
EndoCAM
GPIIA'
PECA1
CD_antigen: CD31
Gene namesi
Name:PECAM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:8823. PECAM1.

Subcellular locationi

Isoform Long :
  • Cell membrane 2 Publications; Single-pass type I membrane protein 1 Publication
  • Membrane raft 2 Publications
  • Cell junction 1 Publication

  • Note: Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells.1 Publication
Isoform Delta15 :
  • Cell junction 1 Publication

  • Note: Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells.

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini28 – 601ExtracellularSequence analysisAdd BLAST574
Transmembranei602 – 620HelicalSequence analysisAdd BLAST19
Topological domaini621 – 738CytoplasmicSequence analysisAdd BLAST118

GO - Cellular componenti

  • cell junction Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: BHF-UCL
  • integral component of membrane Source: UniProtKB-KW
  • membrane raft Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • platelet alpha granule membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi89K → A: Lacks homophilic binding ability and is distributed over the entire plasma membrane. 1 Publication1
Mutagenesisi622C → A: 6-fold decrease in association with membrane microdomains. 1 Publication1
Mutagenesisi690Y → F: Inhibits targeted recycling of PECAM1 from the lateral border recycling compartment (LBRC) around transmigrating monocytes. Decreases phosphorylation. No effect on interaction with PTPN11. Loss of phosphorylation and loss of binding to PTPN11; when associated with F-713. 2 Publications1
Mutagenesisi713Y → F: Does not inhibit targeted recycling of PECAM1 from the lateral border recycling compartment (LBRC) around transmigrating monocytes. Decreases phosphorylation. Loss of interaction with PTPN11. Loss of phosphorylation and loss of binding to PTPN11; when associated with F-690. 2 Publications1

Organism-specific databases

DisGeNETi5175.
PharmGKBiPA33167.

Polymorphism and mutation databases

DMDMi129747.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Add BLAST27
ChainiPRO_000001489528 – 738Platelet endothelial cell adhesion moleculeAdd BLAST711

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi52N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi57 ↔ 109PROSITE-ProRule annotation
Glycosylationi84N-linked (GlcNAc...)1 Publication1
Glycosylationi151N-linked (GlcNAc...)1 Publication1
Disulfide bondi152 ↔ 206PROSITE-ProRule annotation
Disulfide bondi256 ↔ 304PROSITE-ProRule annotation
Glycosylationi301N-linked (GlcNAc...)Sequence analysis1
Glycosylationi320N-linked (GlcNAc...)2 Publications1
Glycosylationi344N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi347 ↔ 386PROSITE-ProRule annotation
Glycosylationi356N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi431 ↔ 476PROSITE-ProRule annotation
Glycosylationi453N-linked (GlcNAc...)1 Publication1
Disulfide bondi523 ↔ 572PROSITE-ProRule annotation
Glycosylationi551N-linked (GlcNAc...)1 Publication1
Lipidationi622S-palmitoyl cysteine1 Publication1
Modified residuei690Phosphotyrosine; by FER1 Publication1
Modified residuei713Phosphotyrosine; by FER2 Publications1

Post-translational modificationi

Phosphorylated on Ser and Tyr residues after cellular activation. Phosphorylated on tyrosine residues by FER and FES in response to FCER1 activation (By similarity). In endothelial cells Fyn mediates mechanical-force (stretch or pull) induced tyrosine phosphorylation.By similarity3 Publications
Palmitoylation by ZDHHC21 is necessary for cell surface expression in endothelial cells and enrichment in membrane rafts.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDiP16284.
MaxQBiP16284.
PeptideAtlasiP16284.
PRIDEiP16284.
TopDownProteomicsiP16284-1. [P16284-1]

2D gel databases

UCD-2DPAGEP16284.

PTM databases

iPTMnetiP16284.
PhosphoSitePlusiP16284.
SwissPalmiP16284.

Miscellaneous databases

PMAP-CutDBP16284.

Expressioni

Tissue specificityi

Expressed on platelets and leukocytes and is primarily concentrated at the borders between endothelial cells. Isoform Long predominates in all tissues examined. Isoform Delta12 is detected only in trachea. Isoform Delta14-15 is only detected in lung. Isoform Delta14 is detected in all tissues examined with the strongest expression in heart. Isoform Delta15 is expressed in brain, testis, ovary, cell surface of platelets, human umbilical vein endothelial cells (HUVECs), Jurkat T-cell leukemia, human erythroleukemia (HEL) and U-937 histiocytic lymphoma cell lines (at protein level).2 Publications

Organism-specific databases

HPAiHPA004690.

Interactioni

Subunit structurei

Interacts with PTPN11; Tyr-713 is critical for PTPN11 recruitment. Forms a complex with BDKRB2 and GNAQ. Interacts with BDKRB2 and GNAQ.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P352223EBI-716404,EBI-491549
JUPP149237EBI-716404,EBI-702484
PTPN11Q061247EBI-716404,EBI-297779
PTPN6P293504EBI-716404,EBI-78260
SRCP129313EBI-716404,EBI-621482

Protein-protein interaction databases

BioGridi111201. 21 interactors.
IntActiP16284. 20 interactors.
MINTiMINT-1198729.

Structurei

Secondary structure

1738
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 43Combined sources12
Beta strandi45 – 48Combined sources4
Beta strandi53 – 64Combined sources12
Beta strandi71 – 77Combined sources7
Beta strandi80 – 98Combined sources19
Helixi101 – 103Combined sources3
Beta strandi105 – 115Combined sources11
Beta strandi117 – 119Combined sources3
Beta strandi123 – 128Combined sources6
Beta strandi134 – 138Combined sources5
Beta strandi147 – 153Combined sources7
Beta strandi161 – 169Combined sources9
Beta strandi174 – 182Combined sources9
Beta strandi184 – 194Combined sources11
Beta strandi200 – 218Combined sources19
Helixi709 – 728Combined sources20
Beta strandi731 – 733Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KY5NMR-A686-738[»]
5C14X-ray2.80A/B28-229[»]
ProteinModelPortaliP16284.
SMRiP16284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16284.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 121Ig-like C2-type 1Add BLAST87
Domaini145 – 233Ig-like C2-type 2Add BLAST89
Domaini236 – 315Ig-like C2-type 3Add BLAST80
Domaini328 – 401Ig-like C2-type 4Add BLAST74
Domaini424 – 493Ig-like C2-type 5Add BLAST70
Domaini499 – 591Ig-like C2-type 6Add BLAST93

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni721 – 738May play a role in cytoprotective signalingAdd BLAST18

Domaini

The Ig-like C2-type domains 2 and 3 contribute to formation of the complex with BDKRB2 and in regulation of its activity.

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG059434.
InParanoidiP16284.
KOiK06471.
PhylomeDBiP16284.

Family and domain databases

Gene3Di2.60.40.10. 6 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF13895. Ig_2. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 5 hits.
SM00408. IGc2. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 5 hits.
PROSITEiPS50835. IG_LIKE. 4 hits.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P16284-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQPRWAQGAT MWLGVLLTLL LCSSLEGQEN SFTINSVDMK SLPDWTVQNG
60 70 80 90 100
KNLTLQCFAD VSTTSHVKPQ HQMLFYKDDV LFYNISSMKS TESYFIPEVR
110 120 130 140 150
IYDSGTYKCT VIVNNKEKTT AEYQLLVEGV PSPRVTLDKK EAIQGGIVRV
160 170 180 190 200
NCSVPEEKAP IHFTIEKLEL NEKMVKLKRE KNSRDQNFVI LEFPVEEQDR
210 220 230 240 250
VLSFRCQARI ISGIHMQTSE STKSELVTVT ESFSTPKFHI SPTGMIMEGA
260 270 280 290 300
QLHIKCTIQV THLAQEFPEI IIQKDKAIVA HNRHGNKAVY SVMAMVEHSG
310 320 330 340 350
NYTCKVESSR ISKVSSIVVN ITELFSKPEL ESSFTHLDQG ERLNLSCSIP
360 370 380 390 400
GAPPANFTIQ KEDTIVSQTQ DFTKIASKSD SGTYICTAGI DKVVKKSNTV
410 420 430 440 450
QIVVCEMLSQ PRISYDAQFE VIKGQTIEVR CESISGTLPI SYQLLKTSKV
460 470 480 490 500
LENSTKNSND PAVFKDNPTE DVEYQCVADN CHSHAKMLSE VLRVKVIAPV
510 520 530 540 550
DEVQISILSS KVVESGEDIV LQCAVNEGSG PITYKFYREK EGKPFYQMTS
560 570 580 590 600
NATQAFWTKQ KASKEQEGEY YCTAFNRANH ASSVPRSKIL TVRVILAPWK
610 620 630 640 650
KGLIAVVIIG VIIALLIIAA KCYFLRKAKA KQMPVEMSRP AVPLLNSNNE
660 670 680 690 700
KMSDPNMEAN SHYGHNDDVR NHAMKPINDN KEPLNSDVQY TEVQVSSAES
710 720 730
HKDLGKKDTE TVYSEVRKAV PDAVESRYSR TEGSLDGT
Length:738
Mass (Da):82,536
Last modified:April 1, 1990 - v1
Checksum:iC57BBFA200A407A6
GO
Isoform Delta12 (identifier: P16284-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     664-681: Missing.

Show »
Length:720
Mass (Da):80,479
Checksum:iAAD7D2166EE7137B
GO
Isoform Delta13 (identifier: P16284-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     682-702: Missing.

Show »
Length:717
Mass (Da):80,207
Checksum:i84A04E34A9EF7619
GO
Isoform Delta14 (identifier: P16284-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     703-721: Missing.

Show »
Length:719
Mass (Da):80,419
Checksum:i41B823F2ACEEE3AB
GO
Isoform Delta14-15 (identifier: P16284-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     703-729: Missing.
     730-738: RTEGSLDGT → ENGRLP

Show »
Length:708
Mass (Da):79,261
Checksum:i9245FAAEFDFCF5E2
GO
Isoform Delta15 (identifier: P16284-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     722-729: Missing.
     730-738: RTEGSLDGT → ENGRLP

Show »
Length:727
Mass (Da):81,378
Checksum:i50DEEBC45F1864E9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti6A → T in BAF83381 (PubMed:14702039).Curated1
Sequence conflicti8 – 12GATMW → ADV (PubMed:2351935).Curated5
Sequence conflicti80V → M in AAK84009 (Ref. 11) Curated1
Sequence conflicti97P → L in AAK84011 (Ref. 11) Curated1
Sequence conflicti329E → K in AAF91460 (Ref. 11) Curated1
Sequence conflicti430R → H in AAF91451 (Ref. 11) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013145125L → V.8 PublicationsCorresponds to variant rs668dbSNPEnsembl.1
Natural variantiVAR_059402304C → Y.Corresponds to variant rs7209607dbSNPEnsembl.1
Natural variantiVAR_059403563S → I.Corresponds to variant rs12953dbSNPEnsembl.1
Natural variantiVAR_059404563S → N.7 PublicationsCorresponds to variant rs12953dbSNPEnsembl.1
Natural variantiVAR_059405670R → G.6 PublicationsCorresponds to variant rs1131012dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_011806664 – 681Missing in isoform Delta12. CuratedAdd BLAST18
Alternative sequenceiVSP_011807682 – 702Missing in isoform Delta13. CuratedAdd BLAST21
Alternative sequenceiVSP_011808703 – 729Missing in isoform Delta14-15. CuratedAdd BLAST27
Alternative sequenceiVSP_011809703 – 721Missing in isoform Delta14. CuratedAdd BLAST19
Alternative sequenceiVSP_011810722 – 729Missing in isoform Delta15. Curated8
Alternative sequenceiVSP_011811730 – 738RTEGSLDGT → ENGRLP in isoform Delta14-15 and isoform Delta15. Curated9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37780 mRNA. Translation: AAA36186.1.
M28526 mRNA. Translation: AAA36429.1.
L34657
, L34631, L34637, L34638, L34639, L34640, L34641, L34642, L34644, L34645, L34649, L34655 Genomic DNA. Translation: AAA60057.1.
JQ287500 mRNA. Translation: AFA36630.1.
AK290692 mRNA. Translation: BAF83381.1.
AC016489 Genomic DNA. No translation available.
AC138744 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94207.1.
CH471109 Genomic DNA. Translation: EAW94208.1.
BC022512 mRNA. Translation: AAH22512.1.
BC051822 mRNA. Translation: AAH51822.1.
AF281287 mRNA. Translation: AAF91446.1.
AF281288 mRNA. Translation: AAF91447.1.
AF281289 mRNA. Translation: AAF91448.1.
AF281290 mRNA. Translation: AAF91449.1.
AF281291 mRNA. Translation: AAF91450.1.
AF281292 mRNA. Translation: AAF91451.1.
AF281293 mRNA. Translation: AAF91452.1.
AF281294 mRNA. Translation: AAF91453.1.
AF281295 mRNA. Translation: AAF91454.1.
AF281296 mRNA. Translation: AAF91455.1.
AF281297 mRNA. Translation: AAF91456.1.
AF281298 mRNA. Translation: AAF91457.1.
AF281299 mRNA. Translation: AAF91458.1.
AF281300 mRNA. Translation: AAF91459.1.
AF281301 mRNA. Translation: AAF91460.1.
AF393676 mRNA. Translation: AAK84009.1.
AF393677 mRNA. Translation: AAK84010.1.
AF393678 mRNA. Translation: AAK84011.1.
S66450 mRNA. Translation: AAB28645.1.
CCDSiCCDS74132.1. [P16284-1]
PIRiA40096.
RefSeqiNP_000433.4. NM_000442.4.
UniGeneiHs.376675.
Hs.514412.
Hs.722648.

Genome annotation databases

GeneIDi5175.
KEGGihsa:5175.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

CD31 entry

Functional Glycomics Gateway - Glycan Binding

PECAM-1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37780 mRNA. Translation: AAA36186.1.
M28526 mRNA. Translation: AAA36429.1.
L34657
, L34631, L34637, L34638, L34639, L34640, L34641, L34642, L34644, L34645, L34649, L34655 Genomic DNA. Translation: AAA60057.1.
JQ287500 mRNA. Translation: AFA36630.1.
AK290692 mRNA. Translation: BAF83381.1.
AC016489 Genomic DNA. No translation available.
AC138744 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94207.1.
CH471109 Genomic DNA. Translation: EAW94208.1.
BC022512 mRNA. Translation: AAH22512.1.
BC051822 mRNA. Translation: AAH51822.1.
AF281287 mRNA. Translation: AAF91446.1.
AF281288 mRNA. Translation: AAF91447.1.
AF281289 mRNA. Translation: AAF91448.1.
AF281290 mRNA. Translation: AAF91449.1.
AF281291 mRNA. Translation: AAF91450.1.
AF281292 mRNA. Translation: AAF91451.1.
AF281293 mRNA. Translation: AAF91452.1.
AF281294 mRNA. Translation: AAF91453.1.
AF281295 mRNA. Translation: AAF91454.1.
AF281296 mRNA. Translation: AAF91455.1.
AF281297 mRNA. Translation: AAF91456.1.
AF281298 mRNA. Translation: AAF91457.1.
AF281299 mRNA. Translation: AAF91458.1.
AF281300 mRNA. Translation: AAF91459.1.
AF281301 mRNA. Translation: AAF91460.1.
AF393676 mRNA. Translation: AAK84009.1.
AF393677 mRNA. Translation: AAK84010.1.
AF393678 mRNA. Translation: AAK84011.1.
S66450 mRNA. Translation: AAB28645.1.
CCDSiCCDS74132.1. [P16284-1]
PIRiA40096.
RefSeqiNP_000433.4. NM_000442.4.
UniGeneiHs.376675.
Hs.514412.
Hs.722648.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KY5NMR-A686-738[»]
5C14X-ray2.80A/B28-229[»]
ProteinModelPortaliP16284.
SMRiP16284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111201. 21 interactors.
IntActiP16284. 20 interactors.
MINTiMINT-1198729.

PTM databases

iPTMnetiP16284.
PhosphoSitePlusiP16284.
SwissPalmiP16284.

Polymorphism and mutation databases

DMDMi129747.

2D gel databases

UCD-2DPAGEP16284.

Proteomic databases

EPDiP16284.
MaxQBiP16284.
PeptideAtlasiP16284.
PRIDEiP16284.
TopDownProteomicsiP16284-1. [P16284-1]

Protocols and materials databases

DNASUi5175.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5175.
KEGGihsa:5175.

Organism-specific databases

CTDi5175.
DisGeNETi5175.
GeneCardsiPECAM1.
HGNCiHGNC:8823. PECAM1.
HPAiHPA004690.
MIMi173445. gene.
neXtProtiNX_P16284.
PharmGKBiPA33167.
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG059434.
InParanoidiP16284.
KOiK06471.
PhylomeDBiP16284.

Enzyme and pathway databases

BioCyciZFISH:G66-32708-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-210990. PECAM1 interactions.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-432142. Platelet sensitization by LDL.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiPECAM1. human.
EvolutionaryTraceiP16284.
GeneWikiiCD31.
GenomeRNAii5175.
PMAP-CutDBP16284.
PROiP16284.
SOURCEiSearch...

Family and domain databases

Gene3Di2.60.40.10. 6 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF13895. Ig_2. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 5 hits.
SM00408. IGc2. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 5 hits.
PROSITEiPS50835. IG_LIKE. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPECA1_HUMAN
AccessioniPrimary (citable) accession number: P16284
Secondary accession number(s): A8K3S7
, D3DU31, Q6LDA9, Q8TBH1, Q96RF5, Q96RF6, Q9NP65, Q9NPB7, Q9NPG9, Q9NQS9, Q9NQT0, Q9NQT1, Q9NQT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 30, 2016
This is version 193 of the entry and version 1 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 17
    Human chromosome 17: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.