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P16284

- PECA1_HUMAN

UniProt

P16284 - PECA1_HUMAN

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Protein

Platelet endothelial cell adhesion molecule

Gene
PECAM1
Organism
Homo sapiens (Human)
Status
Reviewed - 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).3 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cell adhesion Source: UniProtKB-KW
  3. cell recognition Source: ProtInc
  4. diapedesis Source: UniProtKB
  5. extracellular matrix organization Source: Reactome
  6. glomerular endothelium development Source: UniProtKB
  7. leukocyte migration Source: Reactome
  8. phagocytosis Source: UniProtKB
  9. platelet activation Source: Reactome
  10. platelet degranulation Source: Reactome
  11. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Phagocytosis

Enzyme and pathway databases

ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
REACT_12519. PECAM1 interactions.
REACT_13552. Integrin cell surface interactions.
REACT_23879. Platelet sensitization by LDL.

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
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:8823. PECAM1.

Subcellular locationi

Isoform Long : Cell membrane; Single-pass type I membrane protein. Cell membrane; Lipid-anchor. Cell junction
Note: Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells.3 Publications
Isoform Delta15 : Cell junction
Note: Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells.3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 601574Extracellular Reviewed predictionAdd
BLAST
Transmembranei602 – 62019Helical; Reviewed predictionAdd
BLAST
Topological domaini621 – 738118Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. cell junction Source: UniProtKB-SubCell
  2. extracellular space Source: BHF-UCL
  3. extracellular vesicular exosome Source: UniProt
  4. integral component of membrane Source: UniProtKB-KW
  5. plasma membrane Source: UniProtKB
  6. platelet alpha granule membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi89 – 891K → A: Lacks homophilic binding ability and is distributed over the entire plasma membrane. 1 Publication
Mutagenesisi622 – 6221C → A: 6-fold decrease in association with membrane microdomains. 1 Publication
Mutagenesisi690 – 6901Y → 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 Publications
Mutagenesisi713 – 7131Y → 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 Publications

Organism-specific databases

PharmGKBiPA33167.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Add
BLAST
Chaini28 – 738711Platelet endothelial cell adhesion moleculePRO_0000014895Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi52 – 521N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi57 ↔ 109 Reviewed prediction
Glycosylationi84 – 841N-linked (GlcNAc...)1 Publication
Glycosylationi151 – 1511N-linked (GlcNAc...)1 Publication
Disulfide bondi152 ↔ 206 Reviewed prediction
Disulfide bondi256 ↔ 304 Reviewed prediction
Glycosylationi301 – 3011N-linked (GlcNAc...) Reviewed prediction
Glycosylationi320 – 3201N-linked (GlcNAc...)2 Publications
Glycosylationi344 – 3441N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi347 ↔ 386 Reviewed prediction
Glycosylationi356 – 3561N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi431 ↔ 476 Reviewed prediction
Glycosylationi453 – 4531N-linked (GlcNAc...)1 Publication
Disulfide bondi523 ↔ 572 Reviewed prediction
Glycosylationi551 – 5511N-linked (GlcNAc...)1 Publication
Lipidationi622 – 6221S-palmitoyl cysteine2 Publications
Modified residuei690 – 6901Phosphotyrosine; by FER1 Publication
Modified residuei713 – 7131Phosphotyrosine; by FER2 Publications

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.3 Publications
Palmitoylation by ZDHHC21 is necessary for cell surface expression in endothelial cells.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP16284.
PRIDEiP16284.

2D gel databases

UCD-2DPAGEP16284.

PTM databases

PhosphoSiteiP16284.

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

Gene expression databases

GenevestigatoriP16284.

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
JUPP149237EBI-716404,EBI-702484
PTPN11Q061247EBI-716404,EBI-297779
PTPN6P293504EBI-716404,EBI-78260
SRCP129313EBI-716404,EBI-621482

Protein-protein interaction databases

BioGridi111201. 20 interactions.
IntActiP16284. 14 interactions.
MINTiMINT-1198729.

Structurei

Secondary structure

1
738
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi709 – 72820
Beta strandi731 – 7333

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KY5NMR-A686-738[»]
ProteinModelPortaliP16284.
SMRiP16284. Positions 704-738.

Miscellaneous databases

EvolutionaryTraceiP16284.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 12187Ig-like C2-type 1Add
BLAST
Domaini145 – 23389Ig-like C2-type 2Add
BLAST
Domaini236 – 31580Ig-like C2-type 3Add
BLAST
Domaini328 – 40174Ig-like C2-type 4Add
BLAST
Domaini424 – 49370Ig-like C2-type 5Add
BLAST
Domaini499 – 59193Ig-like C2-type 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni721 – 73818May play a role in cytoprotective signalingAdd
BLAST

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.
KOiK06471.
PhylomeDBiP16284.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTiSM00409. IG. 3 hits.
[Graphical view]
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. Align

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

MQPRWAQGAT MWLGVLLTLL LCSSLEGQEN SFTINSVDMK SLPDWTVQNG    50
KNLTLQCFAD VSTTSHVKPQ HQMLFYKDDV LFYNISSMKS TESYFIPEVR 100
IYDSGTYKCT VIVNNKEKTT AEYQLLVEGV PSPRVTLDKK EAIQGGIVRV 150
NCSVPEEKAP IHFTIEKLEL NEKMVKLKRE KNSRDQNFVI LEFPVEEQDR 200
VLSFRCQARI ISGIHMQTSE STKSELVTVT ESFSTPKFHI SPTGMIMEGA 250
QLHIKCTIQV THLAQEFPEI IIQKDKAIVA HNRHGNKAVY SVMAMVEHSG 300
NYTCKVESSR ISKVSSIVVN ITELFSKPEL ESSFTHLDQG ERLNLSCSIP 350
GAPPANFTIQ KEDTIVSQTQ DFTKIASKSD SGTYICTAGI DKVVKKSNTV 400
QIVVCEMLSQ PRISYDAQFE VIKGQTIEVR CESISGTLPI SYQLLKTSKV 450
LENSTKNSND PAVFKDNPTE DVEYQCVADN CHSHAKMLSE VLRVKVIAPV 500
DEVQISILSS KVVESGEDIV LQCAVNEGSG PITYKFYREK EGKPFYQMTS 550
NATQAFWTKQ KASKEQEGEY YCTAFNRANH ASSVPRSKIL TVRVILAPWK 600
KGLIAVVIIG VIIALLIIAA KCYFLRKAKA KQMPVEMSRP AVPLLNSNNE 650
KMSDPNMEAN SHYGHNDDVR NHAMKPINDN KEPLNSDVQY TEVQVSSAES 700
HKDLGKKDTE TVYSEVRKAV PDAVESRYSR TEGSLDGT 738
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti125 – 1251L → V.8 Publications
Corresponds to variant rs668 [ dbSNP | Ensembl ].
VAR_013145
Natural varianti304 – 3041C → Y.
Corresponds to variant rs7209607 [ dbSNP | Ensembl ].
VAR_059402
Natural varianti563 – 5631S → I.
Corresponds to variant rs12953 [ dbSNP | Ensembl ].
VAR_059403
Natural varianti563 – 5631S → N.7 Publications
Corresponds to variant rs12953 [ dbSNP | Ensembl ].
VAR_059404
Natural varianti670 – 6701R → G.6 Publications
Corresponds to variant rs1131012 [ dbSNP | Ensembl ].
VAR_059405

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei664 – 68118Missing in isoform Delta12. VSP_011806Add
BLAST
Alternative sequencei682 – 70221Missing in isoform Delta13. VSP_011807Add
BLAST
Alternative sequencei703 – 72927Missing in isoform Delta14-15. VSP_011808Add
BLAST
Alternative sequencei703 – 72119Missing in isoform Delta14. VSP_011809Add
BLAST
Alternative sequencei722 – 7298Missing in isoform Delta15. VSP_011810
Alternative sequencei730 – 7389RTEGSLDGT → ENGRLP in isoform Delta14-15 and isoform Delta15. VSP_011811

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61A → T in BAF83381. 1 Publication
Sequence conflicti8 – 125GATMW → ADV1 Publication
Sequence conflicti80 – 801V → M in AAK84009. 1 Publication
Sequence conflicti97 – 971P → L in AAK84011. 1 Publication
Sequence conflicti329 – 3291E → K in AAF91460. 1 Publication
Sequence conflicti430 – 4301R → H in AAF91451. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
PIRiA40096.
RefSeqiNP_000433.4. NM_000442.4.
UniGeneiHs.376675.
Hs.514412.

Genome annotation databases

GeneIDi5175.
KEGGihsa:5175.

Polymorphism databases

DMDMi129747.

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:
EMBL
GenBank
DDBJ
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 .
PIRi A40096.
RefSeqi NP_000433.4. NM_000442.4.
UniGenei Hs.376675.
Hs.514412.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KY5 NMR - A 686-738 [» ]
ProteinModelPortali P16284.
SMRi P16284. Positions 704-738.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111201. 20 interactions.
IntActi P16284. 14 interactions.
MINTi MINT-1198729.

PTM databases

PhosphoSitei P16284.

Polymorphism databases

DMDMi 129747.

2D gel databases

UCD-2DPAGE P16284.

Proteomic databases

MaxQBi P16284.
PRIDEi P16284.

Protocols and materials databases

DNASUi 5175.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5175.
KEGGi hsa:5175.

Organism-specific databases

CTDi 5175.
GeneCardsi GC17M062399.
HGNCi HGNC:8823. PECAM1.
MIMi 173445. gene.
neXtProti NX_P16284.
PharmGKBi PA33167.
GenAtlasi Search...

Phylogenomic databases

HOVERGENi HBG059434.
KOi K06471.
PhylomeDBi P16284.

Enzyme and pathway databases

Reactomei REACT_12051. Cell surface interactions at the vascular wall.
REACT_12519. PECAM1 interactions.
REACT_13552. Integrin cell surface interactions.
REACT_23879. Platelet sensitization by LDL.

Miscellaneous databases

EvolutionaryTracei P16284.
GeneWikii CD31.
GenomeRNAii 5175.
NextBioi 20032.
PMAP-CutDB P16284.
PROi P16284.
SOURCEi Search...

Gene expression databases

Genevestigatori P16284.

Family and domain databases

Gene3Di 2.60.40.10. 5 hits.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view ]
SMARTi SM00409. IG. 3 hits.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of CD31, a putative intercellular adhesion molecule closely related to carcinoembryonic antigen."
    Simmons D.L., Walker C., Power C., Pigott R.
    J. Exp. Med. 171:2147-2152(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
  2. "Molecular characterization and functional analysis of the leukocyte surface protein CD31."
    Stockinger H., Gadd S.J., Eher R., Majdic O., Kasinrek W., Schreiber W., Strass B., Schnabl E., Knapp W.
    J. Immunol. 145:3889-3897(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANTS VAL-125; ASN-563 AND GLY-670.
  3. "PECAM-1 (CD31) cloning and relation to adhesion molecules of the immunoglobulin gene superfamily."
    Newman P.J., Berndt M.C., Gorski J., White J.C. II, Lyman S., Paddock C., Muller W.A.
    Science 247:1219-1222(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
  4. "Molecular and cellular properties of PECAM-1 (endoCAM/CD31): a novel vascular cell-cell adhesion molecule."
    Albelda S.M., Muller W.A., Buck C.A., Newman P.J.
    J. Cell Biol. 114:1059-1068(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
  5. "Organization of the gene for human platelet/endothelial cell adhesion molecule-1 shows alternatively spliced isoforms and a functionally complex cytoplasmic domain."
    Kirschbaum N.E., Gumina R.J., Newman P.J.
    Blood 84:4028-4037(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG), VARIANT ASN-563.
  6. "Gene cloning and sequence analysis of human nasopharyngeal carcinoma resistance cells CNE1/R platelet/endothelial cell adhesion molecule."
    Wang R.-Y., Lun Y.-Z., Jiang Z.-X., Li X.
    Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANTS VAL-125; ASN-563 AND GLY-670.
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANTS VAL-125; ASN-563 AND GLY-670.
    Tissue: Lung.
  8. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS VAL-125; ASN-563 AND GLY-670.
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANTS VAL-125; ASN-563 AND GLY-670.
    Tissue: Brain.
  11. Robbins F.-M.Y., Yao H., Hurley C.K., Hartzman R.J.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-734 (ISOFORM LONG), VARIANTS VAL-125; ASN-563 AND GLY-670.
  12. "Identification of PECAM-1 in solid tumor cells and its potential involvement in tumor cell adhesion to endothelium."
    Tang D.G., Chen Y.Q., Newman P.J., Shi L., Gao X., Diglio C.A., Honn K.V.
    J. Biol. Chem. 268:22883-22894(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 507-584.
  13. "Tyrosine residue in exon 14 of the cytoplasmic domain of platelet endothelial cell adhesion molecule-1 (PECAM-1/CD31) regulates ligand binding specificity."
    Famiglietti J., Sun J., DeLisser H.M., Albelda S.M.
    J. Cell Biol. 138:1425-1435(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-713.
  14. "Apoptosis disables CD31-mediated cell detachment from phagocytes promoting binding and engulfment."
    Brown S., Heinisch I., Ross E., Shaw K., Buckley C.D., Savill J.
    Nature 418:200-203(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Tissue-specific distributions of alternatively spliced human PECAM-1 isoforms."
    Wang Y., Su X., Sorenson C.M., Sheibani N.
    Am. J. Physiol. 284:H1008-H1017(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  16. "Palmitoylation at Cys595 is essential for PECAM-1 localisation into membrane microdomains and for efficient PECAM-1-mediated cytoprotection."
    Sardjono C.T., Harbour S.N., Yip J.C., Paddock C., Tridandapani S., Newman P.J., Jackson D.E.
    Thromb. Haemost. 96:756-766(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-622, MUTAGENESIS OF CYS-622.
  17. "Regulation of G protein-coupled receptor activities by the platelet-endothelial cell adhesion molecule, PECAM-1."
    Yeh J.C., Otte L.A., Frangos J.A.
    Biochemistry 47:9029-9039(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BDKRB2 AND GNAQ.
  18. "Mechanotransduction in an extracted cell model: Fyn drives stretch- and flow-elicited PECAM-1 phosphorylation."
    Chiu Y.J., McBeath E., Fujiwara K.
    J. Cell Biol. 182:753-763(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  19. "An alternatively spliced isoform of PECAM-1 is expressed at high levels in human and murine tissues, and suggests a novel role for the C-terminus of PECAM-1 in cytoprotective signaling."
    Bergom C., Paddock C., Gao C., Holyst T., Newman D.K., Newman P.J.
    J. Cell Sci. 121:1235-1242(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS DELTA14-15 AND DELTA15), FUNCTION (ISOFORM DELTA15), SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-690 AND TYR-713, INTERACTION WITH PTPN11.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  21. "A novel and critical role for tyrosine 663 in platelet endothelial cell adhesion molecule-1 trafficking and transendothelial migration."
    Dasgupta B., Dufour E., Mamdouh Z., Muller W.A.
    J. Immunol. 182:5041-5051(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT TYR-690 AND TYR-713, MUTAGENESIS OF LYS-89; TYR-690 AND TYR-713, INTERACTION WITH PTPN11.
  22. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151; ASN-320 AND ASN-453.
    Tissue: Liver.
  23. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-320 AND ASN-551.
    Tissue: Leukemic T-cell.
  24. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  25. "Endothelial cell palmitoylproteomic identifies novel lipid-modified targets and potential substrates for protein acyl transferases."
    Marin E.P., Derakhshan B., Lam T.T., Davalos A., Sessa W.C.
    Circ. Res. 110:1336-1344(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION BY ZDHHC21, SUBCELLULAR LOCATION.
  26. "Polymorphism of adhesion molecule CD31 and its role in acute graft-versus-host disease."
    Behar E., Chao N.J., Hiraki D.D., Krishnaswamy S., Brown B.W., Zehnder J.L., Grumet F.C.
    N. Engl. J. Med. 334:286-291(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VAL-125.
  27. "Codon 125 polymorphism of CD31 and susceptibility to malaria."
    Casals-Pascual C., Allen S., Allen A., Kai O., Lowe B., Pain A., Roberts D.J.
    Am. J. Trop. Med. Hyg. 65:736-737(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VAL-125.

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: September 3, 2014
This is version 169 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

External Data

Dasty 3

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