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Protein

Platelet endothelial cell adhesion molecule

Gene

PECAM1

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

Functioni

Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions (PubMed:19342684, PubMed:17580308). 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 (PubMed:19342684). Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions (PubMed:27958302). Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils (PubMed:17580308). Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal (PubMed:12110892). Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes (PubMed:12110892). Modulates bradykinin receptor BDKRB2 activation (PubMed:18672896). Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells (PubMed:18672896). Induces susceptibility to atherosclerosis (By similarity).By similarity5 Publications
Isoform Delta15: Does not protect against apoptosis.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

Keywordsi

Biological processCell adhesion, Phagocytosis

Enzyme and pathway databases

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: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000261371.5
HGNCiHGNC:8823 PECAM1
MIMi173445 gene
neXtProtiNX_P16284

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 domaini28 – 601ExtracellularSequence analysisAdd BLAST574
Transmembranei602 – 620HelicalSequence analysisAdd BLAST19
Topological domaini621 – 738CytoplasmicSequence analysisAdd BLAST118

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi52N → Q: Probable loss of N-glycosylation. No effect on homophilic cell adhesion; when associated with Q-84 and Q-151. 1 Publication1
Mutagenesisi74L → E: Reduced homophilic cell adhesion; when associated with E-112; E-188 and E-190. 1 Publication1
Mutagenesisi84N → Q: Probable loss of N-glycosylation. No effect on homophilic cell adhesion; when associated with Q-52 and Q-151. 1 Publication1
Mutagenesisi89K → A: Lacks homophilic binding ability and is distributed over the entire plasma membrane. 1 Publication1
Mutagenesisi112I → E: Reduced homophilic cell adhesion; when associated with E-74; E-188 and E-190. 1 Publication1
Mutagenesisi151N → Q: Probable loss of N-glycosylation. No effect on homophilic cell adhesion; when associated with Q-52 and Q-84. 1 Publication1
Mutagenesisi188F → E: Reduced homophilic cell adhesion; when associated with E-74; E-112 and E-190. 1 Publication1
Mutagenesisi190I → E: Reduced homophilic cell adhesion; when associated with E-74; E-112 and E-188. 1 Publication1
Mutagenesisi622C → A: 6-fold decrease in association with membrane microdomains. 1 Publication1
Mutagenesisi690Y → F: No effect on Tyr-713 phosphorylation. 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. 3 Publications1
Mutagenesisi713Y → F: Loss of Tyr-690 phosphorylation. 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. 3 Publications1

Organism-specific databases

DisGeNETi5175
OpenTargetsiENSG00000261371
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...) asparagineCombined sources1 Publication1
Disulfide bondi57 ↔ 109PROSITE-ProRule annotationCombined sources2 Publications
Glycosylationi84N-linked (GlcNAc...) asparagineCombined sources2 Publications1
Glycosylationi151N-linked (GlcNAc...) asparagineCombined sources2 Publications1
Disulfide bondi152 ↔ 206PROSITE-ProRule annotationCombined sources2 Publications
Disulfide bondi256 ↔ 304PROSITE-ProRule annotation
Glycosylationi301N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi320N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi344N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi347 ↔ 386PROSITE-ProRule annotation
Glycosylationi356N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi431 ↔ 476PROSITE-ProRule annotation
Glycosylationi453N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi523 ↔ 572PROSITE-ProRule annotation
Glycosylationi551N-linked (GlcNAc...) asparagine1 Publication1
Lipidationi622S-palmitoyl cysteine1 Publication1
Modified residuei690Phosphotyrosine; by FER2 Publications1
Modified residuei713Phosphotyrosine; by FER3 Publications1
Modified residuei729Phosphoserine1 Publication1
Modified residuei734Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylated on Ser and Tyr residues after cellular activation by src kinases (PubMed:21464369, PubMed:9298995, PubMed:19342684, PubMed:18710921). Upon activation, phosphorylated on Ser-729 which probably initiates the dissociation of the membrane-interaction segment (residues 709-729) from the cell membrane allowing the sequential phosphorylation of Tyr-713 and Tyr-690 (PubMed:21464369). Constitutively phosphorylated on Ser-734 in resting platelets (PubMed:21464369). 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 (PubMed:18710921).By similarity4 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
PeptideAtlasiP16284
PRIDEiP16284
ProteomicsDBi53335
53336 [P16284-2]
53337 [P16284-3]
53338 [P16284-4]
53339 [P16284-5]
53340 [P16284-6]
TopDownProteomicsiP16284-1 [P16284-1]

2D gel databases

UCD-2DPAGEiP16284

PTM databases

GlyConnecti1610
iPTMnetiP16284
PhosphoSitePlusiP16284
SwissPalmiP16284

Miscellaneous databases

PMAP-CutDBiP16284

Expressioni

Tissue specificityi

Expressed on platelets and leukocytes and is primarily concentrated at the borders between endothelial cells (PubMed:18388311, PubMed:21464369). Expressed in human umbilical vein endothelial cells (HUVECs) (at protein level) (PubMed:19342684, PubMed:17580308). Expressed on neutrophils (at protein level) (PubMed:17580308). Isoform Long predominates in all tissues examined (PubMed:12433657). Isoform Delta12 is detected only in trachea (PubMed:12433657). Isoform Delta14-15 is only detected in lung (PubMed:12433657). Isoform Delta14 is detected in all tissues examined with the strongest expression in heart (PubMed:12433657). 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) (PubMed:12433657, PubMed:18388311).5 Publications

Gene expression databases

BgeeiENSG00000261371 Expressed in 238 organ(s), highest expression level in tendon of biceps brachii

Organism-specific databases

HPAiHPA004690

Interactioni

Subunit structurei

Trans-homodimer (via Ig-like C2-type 1 and Ig-like C2-type 2 domains); trans-homodimerization is required for cell-cell interaction (PubMed:26702061, PubMed:27958302). Forms a complex with BDKRB2 and GNAQ (PubMed:18672896). Interacts with BDKRB2 and GNAQ (PubMed:18672896).Interacts with PTPN11; Tyr-713 is critical for PTPN11 recruitment (PubMed:18388311, PubMed:19342684). Interacts with FER (By similarity). Interacts (via Ig-like C2-type domain 6) with CD177; the interaction is Ca2+-dependent; the interaction is direct (PubMed:17580308).By similarity6 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi111201, 22 interactors
IntActiP16284, 20 interactors
MINTiP16284

Structurei

Secondary structure

1738
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
Regioni709 – 729Membrane-bound segment which detaches upon phosphorylation1 PublicationAdd BLAST21
Regioni721 – 738May play a role in cytoprotective signalingAdd BLAST18

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi688 – 693ITIM motif 11 Publication6
Motifi711 – 716ITIM motif 21 Publication6

Domaini

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

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00440000034155
HOVERGENiHBG059434
InParanoidiP16284
KOiK06471
OMAiYTCKVEA
OrthoDBiEOG091G033M
PhylomeDBiP16284

Family and domain databases

Gene3Di2.60.40.10, 4 hits
InterProiView protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR003598 Ig_sub2
PfamiView protein in Pfam
PF13895 Ig_2, 1 hit
SMARTiView protein in SMART
SM00409 IG, 5 hits
SM00408 IGc2, 3 hits
SUPFAMiSSF48726 SSF48726, 5 hits
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 4 hits

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

This entry has 6 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

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 AEYQVLVEGV 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):82,522
Last modified:March 28, 2018 - v2
Checksum:i9D531D2DDCCB7F92
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):80,465
Checksum:iA87B2E6BF8844823
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):80,193
Checksum:iD9362D6FF1EC2AD7
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):80,405
Checksum:i3D445E64CFB5BBA8
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):79,247
Checksum:i9C3615328E16C7E4
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):81,364
Checksum:iB50CE0F2A7B04E6B
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A075B727A0A075B727_HUMAN
Platelet endothelial cell adhesion ...
PECAM1
230Annotation score:
A0A075B737A0A075B737_HUMAN
Platelet endothelial cell adhesion ...
PECAM1
134Annotation score:
A0A075B728A0A075B728_HUMAN
Platelet endothelial cell adhesion ...
PECAM1
183Annotation score:

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 (PubMed:17212705).Curated1
Sequence conflicti97P → L in AAK84011 (PubMed:17212705).Curated1
Sequence conflicti329E → K in AAF91460 (PubMed:17212705).Curated1
Sequence conflicti430R → H in AAF91451 (PubMed:17212705).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013145125V → L4 PublicationsCorresponds to variant dbSNP:rs281865545EnsemblClinVar.1
Natural variantiVAR_059402304C → Y. Corresponds to variant dbSNP:rs7209607Ensembl.1
Natural variantiVAR_059403563S → I. Corresponds to variant dbSNP:rs12953Ensembl.1
Natural variantiVAR_059404563S → N7 PublicationsCorresponds to variant dbSNP:rs12953Ensembl.1
Natural variantiVAR_059405670R → G6 PublicationsCorresponds to variant dbSNP:rs1131012Ensembl.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.
AC234063 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 [P16284-1]
XP_005276937.1, XM_005276880.1 [P16284-6]
XP_005276938.1, XM_005276881.1 [P16284-4]
XP_005276939.1, XM_005276882.1 [P16284-3]
XP_011523191.1, XM_011524889.2 [P16284-1]
XP_011523192.1, XM_011524890.1 [P16284-1]
XP_016880227.1, XM_017024738.1 [P16284-1]
XP_016880228.1, XM_017024739.1 [P16284-2]
XP_016880229.1, XM_017024740.1 [P16284-4]
UniGeneiHs.376675
Hs.514412
Hs.722648

Genome annotation databases

EnsembliENST00000563924; ENSP00000457421; ENSG00000261371 [P16284-1]
GeneIDi5175
KEGGihsa:5175

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

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.
AC234063 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 [P16284-1]
XP_005276937.1, XM_005276880.1 [P16284-6]
XP_005276938.1, XM_005276881.1 [P16284-4]
XP_005276939.1, XM_005276882.1 [P16284-3]
XP_011523191.1, XM_011524889.2 [P16284-1]
XP_011523192.1, XM_011524890.1 [P16284-1]
XP_016880227.1, XM_017024738.1 [P16284-1]
XP_016880228.1, XM_017024739.1 [P16284-2]
XP_016880229.1, XM_017024740.1 [P16284-4]
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[»]
5GNIX-ray3.01A/B28-232[»]
ProteinModelPortaliP16284
SMRiP16284
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111201, 22 interactors
IntActiP16284, 20 interactors
MINTiP16284

PTM databases

GlyConnecti1610
iPTMnetiP16284
PhosphoSitePlusiP16284
SwissPalmiP16284

Polymorphism and mutation databases

DMDMi129747

2D gel databases

UCD-2DPAGEiP16284

Proteomic databases

EPDiP16284
PeptideAtlasiP16284
PRIDEiP16284
ProteomicsDBi53335
53336 [P16284-2]
53337 [P16284-3]
53338 [P16284-4]
53339 [P16284-5]
53340 [P16284-6]
TopDownProteomicsiP16284-1 [P16284-1]

Protocols and materials databases

DNASUi5175
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000563924; ENSP00000457421; ENSG00000261371 [P16284-1]
GeneIDi5175
KEGGihsa:5175

Organism-specific databases

CTDi5175
DisGeNETi5175
EuPathDBiHostDB:ENSG00000261371.5
GeneCardsiPECAM1
HGNCiHGNC:8823 PECAM1
HPAiHPA004690
MIMi173445 gene
neXtProtiNX_P16284
OpenTargetsiENSG00000261371
PharmGKBiPA33167
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00440000034155
HOVERGENiHBG059434
InParanoidiP16284
KOiK06471
OMAiYTCKVEA
OrthoDBiEOG091G033M
PhylomeDBiP16284

Enzyme and pathway databases

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-CutDBiP16284
PROiPR:P16284
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000261371 Expressed in 238 organ(s), highest expression level in tendon of biceps brachii

Family and domain databases

Gene3Di2.60.40.10, 4 hits
InterProiView protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR003598 Ig_sub2
PfamiView protein in Pfam
PF13895 Ig_2, 1 hit
SMARTiView protein in SMART
SM00409 IG, 5 hits
SM00408 IGc2, 3 hits
SUPFAMiSSF48726 SSF48726, 5 hits
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 4 hits
ProtoNetiSearch...

Entry informationi

Entry nameiPECA1_HUMAN
AccessioniPrimary (citable) accession number: P16284
Secondary accession number(s): A0A075B738
, A8K3S7, D3DU31, Q6LDA9, Q8TBH1, Q96RF5, Q96RF6, Q9NP65, Q9NPB7, Q9NPG9, Q9NQS9, Q9NQT0, Q9NQT1, Q9NQT2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: March 28, 2018
Last modified: November 7, 2018
This is version 210 of the entry and version 2 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 entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
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