P16284 (PECA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Platelet endothelial cell adhesion molecule
Short name=PECAM-1

Alternative name(s):
EndoCAM
GPIIA'
PECA1
CD_antigen=CD31

Gene names

Name:

PECAM1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	738 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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). Ref.11 Ref.19 Ref.21
Subunit structure	Interacts with PTPN11; Tyr-713 is critical for PTPN11 recruitment. Forms a complex with BDKRB2 and GNAQ. Interacts with BDKRB2 and GNAQ. Ref.17 Ref.19 Ref.21
Subcellular location	Isoform Long: Membrane; Single-pass type I membrane protein. Cell junction. Note: Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells. Ref.19 Ref.21 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. Ref.19 Ref.21
Tissue specificity	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 U937 histiocytic lymphoma cell lines (at protein level). Ref.12 Ref.21
Domain	The Ig-like C2-type domains 2 and 3 contribute to formation of the complex with BDKRB2 and in regulation of its activity.
Post-translational modification	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. Ref.10 Ref.13 Ref.15 Ref.16 Ref.18 Ref.20 Ref.21 Ref.24
Sequence similarities	Contains 6 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
Biological process	Cell adhesion Phagocytosis
Cellular component	Cell junction Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cell recognition Traceable author statement. Source: ProtInc diapedesis Inferred from direct assay Ref.21. Source: UniProtKB phagocytosis Inferred from direct assay Ref.11. Source: UniProtKB platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome signal transduction Traceable author statement. Source: ProtInc
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space Inferred from direct assay. Source: BHF-UCL integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement. Source: Reactome platelet alpha granule membrane Traceable author statement. Source: Reactome
Molecular function	protein binding Inferred from physical interaction Ref.17. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
JUP	P14923	7	EBI-716404,EBI-702484

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P16284-1)

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.

Isoform Delta12 (identifier: P16284-2)

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

Isoform Delta13 (identifier: P16284-3)

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

Isoform Delta14 (identifier: P16284-4)

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

Isoform Delta14-15 (identifier: P16284-5)

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

Isoform Delta15 (identifier: P16284-6)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Chain

28 – 738

711

Platelet endothelial cell adhesion molecule

PRO_0000014895

Regions

Topological domain

28 – 601

574

Extracellular Potential

Transmembrane

602 – 620

19

Helical; Potential

Topological domain

621 – 738

118

Cytoplasmic Potential

Domain

35 – 121

87

Ig-like C2-type 1

Domain

145 – 233

89

Ig-like C2-type 2

Domain

236 – 315

80

Ig-like C2-type 3

Domain

328 – 401

74

Ig-like C2-type 4

Domain

424 – 493

70

Ig-like C2-type 5

Domain

499 – 591

93

Ig-like C2-type 6

Region

721 – 738

18

May play a role in cytoprotective signaling

Amino acid modifications

Modified residue

290

1

Phosphotyrosine Ref.16

Modified residue

690

1

Phosphotyrosine; by FER Ref.21

Modified residue

713

1

Phosphotyrosine; by FER Ref.10 Ref.13 Ref.15 Ref.20 Ref.21 Ref.24

Lipidation

622

1

S-palmitoyl cysteine Ref.14

Glycosylation

52

1

N-linked (GlcNAc...) Potential

Glycosylation

84

1

N-linked (GlcNAc...) Ref.23

Glycosylation

151

1

N-linked (GlcNAc...) Ref.22

Glycosylation

301

1

N-linked (GlcNAc...) Potential

Glycosylation

320

1

N-linked (GlcNAc...) Ref.22 Ref.23

Glycosylation

344

1

N-linked (GlcNAc...) Potential

Glycosylation

356

1

N-linked (GlcNAc...) Potential

Glycosylation

453

1

N-linked (GlcNAc...) Ref.22

Glycosylation

551

1

N-linked (GlcNAc...) Ref.23

Disulfide bond

57 ↔ 109

Potential

Disulfide bond

152 ↔ 206

Potential

Disulfide bond

256 ↔ 304

Potential

Disulfide bond

347 ↔ 386

Potential

Disulfide bond

431 ↔ 476

Potential

Disulfide bond

523 ↔ 572

Potential

Natural variations

Alternative sequence

664 – 681

18

Missing in isoform Delta12.

VSP_011806

Alternative sequence

682 – 702

21

Missing in isoform Delta13.

VSP_011807

Alternative sequence

703 – 729

27

Missing in isoform Delta14-15.

VSP_011808

Alternative sequence

703 – 721

19

Missing in isoform Delta14.

VSP_011809

Alternative sequence

722 – 729

8

Missing in isoform Delta15.

VSP_011810

Alternative sequence

730 – 738

9

RTEGSLDGT → ENGRLP in isoform Delta14-15 and isoform Delta15.

VSP_011811

Natural variant

125

1

L → V. Ref.2 Ref.7 Ref.8 Ref.25 Ref.26
Corresponds to variant rs668 [ dbSNP | Ensembl ].

VAR_013145

Natural variant

304

1

C → Y.
Corresponds to variant rs7209607 [ dbSNP | Ensembl ].

VAR_059402

Natural variant

563

1

S → I.
Corresponds to variant rs12953 [ dbSNP | Ensembl ].

VAR_059403

Natural variant

563

1

S → N. Ref.2 Ref.5 Ref.7 Ref.8
Corresponds to variant rs12953 [ dbSNP | Ensembl ].

VAR_059404

Natural variant

670

1

R → G. Ref.2 Ref.7 Ref.8
Corresponds to variant rs1131012 [ dbSNP | Ensembl ].

VAR_059405

Experimental info

Mutagenesis

89

1

K → A: Lacks homophilic binding ability and is distributed over the entire plasma membrane. Ref.21

Mutagenesis

622

1

C → A: 6-fold decrease in association with membrane microdomains. Ref.14

Mutagenesis

690

1

Y → 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. Ref.19 Ref.21

Mutagenesis

713

1

Y → 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. Ref.19 Ref.21

Sequence conflict

8 – 12

5

GATMW → ADV Ref.1

Sequence conflict

80

1

V → M in AAK84009. Ref.8

Sequence conflict

97

1

P → L in AAK84011. Ref.8

Sequence conflict

329

1

E → K in AAF91460. Ref.8

Sequence conflict

430

1

R → H in AAF91451. Ref.8

Secondary structure

1

.

.

.

738

Helix Strand Turn

Details...

Helix

709 – 728

20

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified April 1, 1990. Version 1. Checksum: C57BBFA200A407A6	FASTA	738	82,536
	10 20 30 40 50 60 MQPRWAQGAT MWLGVLLTLL LCSSLEGQEN SFTINSVDMK SLPDWTVQNG KNLTLQCFAD 70 80 90 100 110 120 VSTTSHVKPQ HQMLFYKDDV LFYNISSMKS TESYFIPEVR IYDSGTYKCT VIVNNKEKTT 130 140 150 160 170 180 AEYQLLVEGV PSPRVTLDKK EAIQGGIVRV NCSVPEEKAP IHFTIEKLEL NEKMVKLKRE 190 200 210 220 230 240 KNSRDQNFVI LEFPVEEQDR VLSFRCQARI ISGIHMQTSE STKSELVTVT ESFSTPKFHI 250 260 270 280 290 300 SPTGMIMEGA QLHIKCTIQV THLAQEFPEI IIQKDKAIVA HNRHGNKAVY SVMAMVEHSG 310 320 330 340 350 360 NYTCKVESSR ISKVSSIVVN ITELFSKPEL ESSFTHLDQG ERLNLSCSIP GAPPANFTIQ 370 380 390 400 410 420 KEDTIVSQTQ DFTKIASKSD SGTYICTAGI DKVVKKSNTV QIVVCEMLSQ PRISYDAQFE 430 440 450 460 470 480 VIKGQTIEVR CESISGTLPI SYQLLKTSKV LENSTKNSND PAVFKDNPTE DVEYQCVADN 490 500 510 520 530 540 CHSHAKMLSE VLRVKVIAPV DEVQISILSS KVVESGEDIV LQCAVNEGSG PITYKFYREK 550 560 570 580 590 600 EGKPFYQMTS NATQAFWTKQ KASKEQEGEY YCTAFNRANH ASSVPRSKIL TVRVILAPWK 610 620 630 640 650 660 KGLIAVVIIG VIIALLIIAA KCYFLRKAKA KQMPVEMSRP AVPLLNSNNE KMSDPNMEAN 670 680 690 700 710 720 SHYGHNDDVR NHAMKPINDN KEPLNSDVQY TEVQVSSAES HKDLGKKDTE TVYSEVRKAV 730 PDAVESRYSR TEGSLDGT
	Isoform Delta12 [UniParc]. Checksum: AAD7D2166EE7137B	FASTA	720	80,479
	10 20 30 40 50 60 MQPRWAQGAT MWLGVLLTLL LCSSLEGQEN SFTINSVDMK SLPDWTVQNG KNLTLQCFAD 70 80 90 100 110 120 VSTTSHVKPQ HQMLFYKDDV LFYNISSMKS TESYFIPEVR IYDSGTYKCT VIVNNKEKTT 130 140 150 160 170 180 AEYQLLVEGV PSPRVTLDKK EAIQGGIVRV NCSVPEEKAP IHFTIEKLEL NEKMVKLKRE 190 200 210 220 230 240 KNSRDQNFVI LEFPVEEQDR VLSFRCQARI ISGIHMQTSE STKSELVTVT ESFSTPKFHI 250 260 270 280 290 300 SPTGMIMEGA QLHIKCTIQV THLAQEFPEI IIQKDKAIVA HNRHGNKAVY SVMAMVEHSG 310 320 330 340 350 360 NYTCKVESSR ISKVSSIVVN ITELFSKPEL ESSFTHLDQG ERLNLSCSIP GAPPANFTIQ 370 380 390 400 410 420 KEDTIVSQTQ DFTKIASKSD SGTYICTAGI DKVVKKSNTV QIVVCEMLSQ PRISYDAQFE 430 440 450 460 470 480 VIKGQTIEVR CESISGTLPI SYQLLKTSKV LENSTKNSND PAVFKDNPTE DVEYQCVADN 490 500 510 520 530 540 CHSHAKMLSE VLRVKVIAPV DEVQISILSS KVVESGEDIV LQCAVNEGSG PITYKFYREK 550 560 570 580 590 600 EGKPFYQMTS NATQAFWTKQ KASKEQEGEY YCTAFNRANH ASSVPRSKIL TVRVILAPWK 610 620 630 640 650 660 KGLIAVVIIG VIIALLIIAA KCYFLRKAKA KQMPVEMSRP AVPLLNSNNE KMSDPNMEAN 670 680 690 700 710 720 SHYEPLNSDV QYTEVQVSSA ESHKDLGKKD TETVYSEVRK AVPDAVESRY SRTEGSLDGT
	Isoform Delta13 [UniParc]. Checksum: 84A04E34A9EF7619	FASTA	717	80,207
	10 20 30 40 50 60 MQPRWAQGAT MWLGVLLTLL LCSSLEGQEN SFTINSVDMK SLPDWTVQNG KNLTLQCFAD 70 80 90 100 110 120 VSTTSHVKPQ HQMLFYKDDV LFYNISSMKS TESYFIPEVR IYDSGTYKCT VIVNNKEKTT 130 140 150 160 170 180 AEYQLLVEGV PSPRVTLDKK EAIQGGIVRV NCSVPEEKAP IHFTIEKLEL NEKMVKLKRE 190 200 210 220 230 240 KNSRDQNFVI LEFPVEEQDR VLSFRCQARI ISGIHMQTSE STKSELVTVT ESFSTPKFHI 250 260 270 280 290 300 SPTGMIMEGA QLHIKCTIQV THLAQEFPEI IIQKDKAIVA HNRHGNKAVY SVMAMVEHSG 310 320 330 340 350 360 NYTCKVESSR ISKVSSIVVN ITELFSKPEL ESSFTHLDQG ERLNLSCSIP GAPPANFTIQ 370 380 390 400 410 420 KEDTIVSQTQ DFTKIASKSD SGTYICTAGI DKVVKKSNTV QIVVCEMLSQ PRISYDAQFE 430 440 450 460 470 480 VIKGQTIEVR CESISGTLPI SYQLLKTSKV LENSTKNSND PAVFKDNPTE DVEYQCVADN 490 500 510 520 530 540 CHSHAKMLSE VLRVKVIAPV DEVQISILSS KVVESGEDIV LQCAVNEGSG PITYKFYREK 550 560 570 580 590 600 EGKPFYQMTS NATQAFWTKQ KASKEQEGEY YCTAFNRANH ASSVPRSKIL TVRVILAPWK 610 620 630 640 650 660 KGLIAVVIIG VIIALLIIAA KCYFLRKAKA KQMPVEMSRP AVPLLNSNNE KMSDPNMEAN 670 680 690 700 710 SHYGHNDDVR NHAMKPINDN KDLGKKDTET VYSEVRKAVP DAVESRYSRT EGSLDGT
	Isoform Delta14 [UniParc]. Checksum: 41B823F2ACEEE3AB	FASTA	719	80,419
	10 20 30 40 50 60 MQPRWAQGAT MWLGVLLTLL LCSSLEGQEN SFTINSVDMK SLPDWTVQNG KNLTLQCFAD 70 80 90 100 110 120 VSTTSHVKPQ HQMLFYKDDV LFYNISSMKS TESYFIPEVR IYDSGTYKCT VIVNNKEKTT 130 140 150 160 170 180 AEYQLLVEGV PSPRVTLDKK EAIQGGIVRV NCSVPEEKAP IHFTIEKLEL NEKMVKLKRE 190 200 210 220 230 240 KNSRDQNFVI LEFPVEEQDR VLSFRCQARI ISGIHMQTSE STKSELVTVT ESFSTPKFHI 250 260 270 280 290 300 SPTGMIMEGA QLHIKCTIQV THLAQEFPEI IIQKDKAIVA HNRHGNKAVY SVMAMVEHSG 310 320 330 340 350 360 NYTCKVESSR ISKVSSIVVN ITELFSKPEL ESSFTHLDQG ERLNLSCSIP GAPPANFTIQ 370 380 390 400 410 420 KEDTIVSQTQ DFTKIASKSD SGTYICTAGI DKVVKKSNTV QIVVCEMLSQ PRISYDAQFE 430 440 450 460 470 480 VIKGQTIEVR CESISGTLPI SYQLLKTSKV LENSTKNSND PAVFKDNPTE DVEYQCVADN 490 500 510 520 530 540 CHSHAKMLSE VLRVKVIAPV DEVQISILSS KVVESGEDIV LQCAVNEGSG PITYKFYREK 550 560 570 580 590 600 EGKPFYQMTS NATQAFWTKQ KASKEQEGEY YCTAFNRANH ASSVPRSKIL TVRVILAPWK 610 620 630 640 650 660 KGLIAVVIIG VIIALLIIAA KCYFLRKAKA KQMPVEMSRP AVPLLNSNNE KMSDPNMEAN 670 680 690 700 710 SHYGHNDDVR NHAMKPINDN KEPLNSDVQY TEVQVSSAES HKDAVESRYS RTEGSLDGT
	Isoform Delta14-15 [UniParc]. Checksum: 9245FAAEFDFCF5E2	FASTA	708	79,261
	10 20 30 40 50 60 MQPRWAQGAT MWLGVLLTLL LCSSLEGQEN SFTINSVDMK SLPDWTVQNG KNLTLQCFAD 70 80 90 100 110 120 VSTTSHVKPQ HQMLFYKDDV LFYNISSMKS TESYFIPEVR IYDSGTYKCT VIVNNKEKTT 130 140 150 160 170 180 AEYQLLVEGV PSPRVTLDKK EAIQGGIVRV NCSVPEEKAP IHFTIEKLEL NEKMVKLKRE 190 200 210 220 230 240 KNSRDQNFVI LEFPVEEQDR VLSFRCQARI ISGIHMQTSE STKSELVTVT ESFSTPKFHI 250 260 270 280 290 300 SPTGMIMEGA QLHIKCTIQV THLAQEFPEI IIQKDKAIVA HNRHGNKAVY SVMAMVEHSG 310 320 330 340 350 360 NYTCKVESSR ISKVSSIVVN ITELFSKPEL ESSFTHLDQG ERLNLSCSIP GAPPANFTIQ 370 380 390 400 410 420 KEDTIVSQTQ DFTKIASKSD SGTYICTAGI DKVVKKSNTV QIVVCEMLSQ PRISYDAQFE 430 440 450 460 470 480 VIKGQTIEVR CESISGTLPI SYQLLKTSKV LENSTKNSND PAVFKDNPTE DVEYQCVADN 490 500 510 520 530 540 CHSHAKMLSE VLRVKVIAPV DEVQISILSS KVVESGEDIV LQCAVNEGSG PITYKFYREK 550 560 570 580 590 600 EGKPFYQMTS NATQAFWTKQ KASKEQEGEY YCTAFNRANH ASSVPRSKIL TVRVILAPWK 610 620 630 640 650 660 KGLIAVVIIG VIIALLIIAA KCYFLRKAKA KQMPVEMSRP AVPLLNSNNE KMSDPNMEAN 670 680 690 700 SHYGHNDDVR NHAMKPINDN KEPLNSDVQY TEVQVSSAES HKENGRLP
	Isoform Delta15 [UniParc]. Checksum: 50DEEBC45F1864E9	FASTA	727	81,378
	10 20 30 40 50 60 MQPRWAQGAT MWLGVLLTLL LCSSLEGQEN SFTINSVDMK SLPDWTVQNG KNLTLQCFAD 70 80 90 100 110 120 VSTTSHVKPQ HQMLFYKDDV LFYNISSMKS TESYFIPEVR IYDSGTYKCT VIVNNKEKTT 130 140 150 160 170 180 AEYQLLVEGV PSPRVTLDKK EAIQGGIVRV NCSVPEEKAP IHFTIEKLEL NEKMVKLKRE 190 200 210 220 230 240 KNSRDQNFVI LEFPVEEQDR VLSFRCQARI ISGIHMQTSE STKSELVTVT ESFSTPKFHI 250 260 270 280 290 300 SPTGMIMEGA QLHIKCTIQV THLAQEFPEI IIQKDKAIVA HNRHGNKAVY SVMAMVEHSG 310 320 330 340 350 360 NYTCKVESSR ISKVSSIVVN ITELFSKPEL ESSFTHLDQG ERLNLSCSIP GAPPANFTIQ 370 380 390 400 410 420 KEDTIVSQTQ DFTKIASKSD SGTYICTAGI DKVVKKSNTV QIVVCEMLSQ PRISYDAQFE 430 440 450 460 470 480 VIKGQTIEVR CESISGTLPI SYQLLKTSKV LENSTKNSND PAVFKDNPTE DVEYQCVADN 490 500 510 520 530 540 CHSHAKMLSE VLRVKVIAPV DEVQISILSS KVVESGEDIV LQCAVNEGSG PITYKFYREK 550 560 570 580 590 600 EGKPFYQMTS NATQAFWTKQ KASKEQEGEY YCTAFNRANH ASSVPRSKIL TVRVILAPWK 610 620 630 640 650 660 KGLIAVVIIG VIIALLIIAA KCYFLRKAKA KQMPVEMSRP AVPLLNSNNE KMSDPNMEAN 670 680 690 700 710 720 SHYGHNDDVR NHAMKPINDN KEPLNSDVQY TEVQVSSAES HKDLGKKDTE TVYSEVRKAV PENGRLP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2351935] [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: 1700999] [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: 1690453] [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: 1874786] [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: 7994021] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG), VARIANT ASN-563.
[6]	"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: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANTS VAL-125; ASN-563 AND GLY-670. Tissue: Brain.
[8]	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.
[9]	"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: 8226797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 507-584.
[10]	"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: 9298995] [Abstract] Cited for: PHOSPHORYLATION AT TYR-713.
[11]	"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: 12110892] [Abstract] Cited for: FUNCTION.
[12]	"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: 12433657] [Abstract] Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[13]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-713, MASS SPECTROMETRY.
[14]	"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: 17139370] [Abstract] Cited for: PALMITOYLATION AT CYS-622, MUTAGENESIS OF CYS-622.
[15]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-713, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[16]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-290, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 18672896] [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: 18710921] [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: 18388311] [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]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-713, MASS SPECTROMETRY. 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: 19342684] [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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151; ASN-320 AND ASN-453, MASS SPECTROMETRY. 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: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-320 AND ASN-551, MASS SPECTROMETRY. 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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-713, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"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: 8532023] [Abstract] Cited for: VARIANT VAL-125.
[26]	"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: 11791967] [Abstract] Cited for: VARIANT VAL-125.
+	Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

CD31 entry

Functional Glycomics Gateway - Glycan Binding

PECAM-1

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
AC016489 Genomic DNA. No translation available.
AC138744 Genomic DNA. No translation available.
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.

IPI

IPI00295618.
IPI00470719.
IPI00470720.
IPI00871352.
IPI00914041.
IPI01010172.

PIR

A40096.

RefSeq

NP_000433.4. NM_000442.4.

UniGene

Hs.376675.
Hs.514412.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KY5	NMR	-	A	686-738	[»]

ProteinModelPortal

P16284.

SMR

P16284. Positions 44-169, 244-484, 501-583, 704-738.

ModBase

Search...

Protein-protein interaction databases

IntAct

P16284. 8 interactions.

MINT

MINT-1198729.

PTM databases

PhosphoSite

P16284.

2D gel databases

UCD-2DPAGE

P16284.

Proteomic databases

PRIDE

P16284.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

5175.

KEGG

hsa:5175.

UCSC

uc002jeg.1. human.

Organism-specific databases

CTD

5175.

GeneCards

GC17M062399.

H-InvDB

HIX0059654.

HGNC

HGNC:8823. PECAM1.

MIM

173445. gene.

neXtProt

NX_P16284.

PharmGKB

PA33167.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07057.

HOVERGEN

HBG059434.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

Genevestigator

P16284.

GermOnline

ENSG00000198802. Homo sapiens.

Family and domain databases

InterPro

IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 5 hits.

KO

K06471.

SMART

SM00409. IG. 3 hits.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

20032.

PMAP-CutDB

P16284.

SOURCE

Search...

Entry information

Entry name

PECA1_HUMAN

Accession

Primary (citable) accession number: P16284
Secondary accession number(s): Q6LDA9 , Q8TBH1, Q96RF5, Q96RF6, Q9NP65, Q9NPB7, Q9NPG9, Q9NQS9, Q9NQT0, Q9NQT1, Q9NQT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	January 25, 2012
This is version 147 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.