PECAM1
entrez
5175
canonical
uniprot
P16284
canonical
ensembl
ENSG00000261371
resolver
ensp
ENSP00000457421
resolver
ensp
ENSP00000574937
resolver
ensp
ENSP00000574938
resolver
ensp
ENSP00000574939
resolver
ensp
ENSP00000574943
resolver
ensp
ENSP00000645131
resolver
ensp
ENSP00000645132
resolver
ensp
ENSP00000724225
resolver
genesymbol
PECAM1
resolver
hgnc
HGNC:8823
resolver
uniprot
A0A075B738
resolver
uniprot
A8K3S7
resolver
uniprot
D3DU31
resolver
uniprot
Q6LDA9
resolver
uniprot
Q8TBH1
resolver
uniprot
Q96RF5
resolver
uniprot
Q96RF6
resolver
uniprot
Q9NP65
resolver
uniprot
Q9NPB7
resolver
uniprot
Q9NPG9
resolver
uniprot
Q9NQS9
resolver
uniprot
Q9NQT0
resolver
uniprot
Q9NQT1
resolver
uniprot
Q9NQT2
resolver
uniprot_entry
PECA1_HUMAN
resolver
uniprot_sec
A0A075B738
resolver
uniprot_sec
A8K3S7
resolver
uniprot_sec
D3DU31
resolver
uniprot_sec
Q6LDA9
resolver
uniprot_sec
Q8TBH1
resolver
uniprot_sec
Q96RF5
resolver
uniprot_sec
Q96RF6
resolver
uniprot_sec
Q9NP65
resolver
uniprot_sec
Q9NPB7
resolver
uniprot_sec
Q9NPG9
resolver
uniprot_sec
Q9NQS9
resolver
uniprot_sec
Q9NQT0
resolver
uniprot_sec
Q9NQT1
resolver
uniprot_sec
Q9NQT2
resolver
amino_acid_sequence
MQPRWAQGATMWLGVLLTLLLCSSLEGQENSFTINSVDMKSLPDWTVQNGKNLTLQCFADVSTTSHVKPQHQMLFYKDDVLFYNISSMKSTESYFIPEVRIYDSGTYKCTVIVNNKEKTTAEYQVLVEGVPSPRVTLDKKEAIQGGIVRVNCSVPEEKAPIHFTIEKLELNEKMVKLKREKNSRDQNFVILEFPVEEQDRVLSFRCQARIISGIHMQTSESTKSELVTVTESFSTPKFHISPTGMIMEGAQLHIKCTIQVTHLAQEFPEIIIQKDKAIVAHNRHGNKAVYSVMAMVEHSGNYTCKVESSRISKVSSIVVNITELFSKPELESSFTHLDQGERLNLSCSIPGAPPANFTIQKEDTIVSQTQDFTKIASKSDSGTYICTAGIDKVVKKSNTVQIVVCEMLSQPRISYDAQFEVIKGQTIEVRCESISGTLPISYQLLKTSKVLENSTKNSNDPAVFKDNPTEDVEYQCVADNCHSHAKMLSEVLRVKVIAPVDEVQISILSSKVVESGEDIVLQCAVNEGSGPITYKFYREKEGKPFYQMTSNATQAFWTKQKASKEQEGEYYCTAFNRANHASSVPRSKILTVRVILAPWKKGLIAVVIIGVIIALLIIAAKCYFLRKAKAKQMPVEMSRPAVPLLNSNNEKMSDPNMEANSHYGHNDDVRNHAMKPINDNKEPLNSDVQYTEVQVSSAESHKDLGKKDTETVYSEVRKAVPDAVESRYSRTEGSLDGT
uniprot
proteins
function
FUNCTION: Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions (PubMed:17580308, PubMed:19342684). 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). {ECO:0000250|UniProtKB:Q08481, ECO:0000269|PubMed:12110892, ECO:0000269|PubMed:17580308, ECO:0000269|PubMed:18672896, ECO:0000269|PubMed:19342684, ECO:0000269|PubMed:27958302}.; FUNCTION: [Isoform Delta15]: Does not protect against apoptosis. {ECO:0000269|PubMed:18388311}.
uniprot
proteins
mass_dalton
82522
uniprot
proteins
mutagenesis
MUTAGEN 52; /note="N->Q: Probable loss of N-glycosylation. No effect on homophilic cell adhesion; when associated with Q-84 and Q-151."; /evidence="ECO:0000269|PubMed:27958302"; MUTAGEN 74; /note="L->E: Reduced homophilic cell adhesion; when associated with E-112; E-188 and E-190."; /evidence="ECO:0000269|PubMed:27958302"; MUTAGEN 84; /note="N->Q: Probable loss of N-glycosylation. No effect on homophilic cell adhesion; when associated with Q-52 and Q-151."; /evidence="ECO:0000269|PubMed:27958302"; MUTAGEN 89; /note="K->A: Lacks homophilic binding ability and is distributed over the entire plasma membrane."; /evidence="ECO:0000269|PubMed:19342684"; MUTAGEN 112; /note="I->E: Reduced homophilic cell adhesion; when associated with E-74; E-188 and E-190."; /evidence="ECO:0000269|PubMed:27958302"; MUTAGEN 151; /note="N->Q: Probable loss of N-glycosylation. No effect on homophilic cell adhesion; when associated with Q-52 and Q-84."; /evidence="ECO:0000269|PubMed:27958302"; MUTAGEN 188; /note="F->E: Reduced homophilic cell adhesion; when associated with E-74; E-112 and E-190."; /evidence="ECO:0000269|PubMed:27958302"; MUTAGEN 190; /note="I->E: Reduced homophilic cell adhesion; when associated with E-74; E-112 and E-188."; /evidence="ECO:0000269|PubMed:27958302"; MUTAGEN 622; /note="C->A: 6-fold decrease in association with membrane microdomains."; /evidence="ECO:0000269|PubMed:17139370"; MUTAGEN 690; /note="Y->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."; /evidence="ECO:0000269|PubMed:18388311, ECO:0000269|PubMed:19342684, ECO:0000269|PubMed:21464369"; MUTAGEN 713; /note="Y->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."; /evidence="ECO:0000269|PubMed:18388311, ECO:0000269|PubMed:19342684, ECO:0000269|PubMed:21464369
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on Ser and Tyr residues after cellular activation by src kinases (PubMed:18710921, PubMed:19342684, PubMed:21464369, PubMed:9298995). 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). {ECO:0000250|UniProtKB:Q08481, ECO:0000269|PubMed:18710921, ECO:0000269|PubMed:19342684, ECO:0000269|PubMed:21464369, ECO:0000269|PubMed:9298995}.; PTM: Palmitoylation by ZDHHC21 is necessary for cell surface expression in endothelial cells and enrichment in membrane rafts. {ECO:0000269|PubMed:17139370, ECO:0000269|PubMed:22496122}.
uniprot
proteins
pubmed
11791967
uniprot
proteins
pubmed
12110892
uniprot
proteins
pubmed
12433657
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
1690453
uniprot
proteins
pubmed
1700999
uniprot
proteins
pubmed
17139370
uniprot
proteins
pubmed
17212705
uniprot
proteins
pubmed
17580308
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18388311
uniprot
proteins
pubmed
18672896
uniprot
proteins
pubmed
18710921
uniprot
proteins
pubmed
1874786
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19342684
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
21464369
uniprot
proteins
pubmed
22496122
uniprot
proteins
pubmed
2351935
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26702061
uniprot
proteins
pubmed
27958302
uniprot
proteins
pubmed
7994021
uniprot
proteins
pubmed
8226797
uniprot
proteins
pubmed
8532023
uniprot
proteins
pubmed
9298995
uniprot
proteins
sequence_length
738
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17580308}; Single-pass type I membrane protein {ECO:0000305}. Note=Cell surface expression on neutrophils is down-regulated upon fMLP or CXCL8/IL8-mediated stimulation. {ECO:0000269|PubMed:17580308}.; SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane {ECO:0000269|PubMed:18388311, ECO:0000269|PubMed:19342684}; Single-pass type I membrane protein {ECO:0000305|PubMed:18388311}. Membrane raft {ECO:0000269|PubMed:17139370, ECO:0000269|PubMed:22496122}. Cell junction {ECO:0000269|PubMed:18388311}. Note=Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells. {ECO:0000269|PubMed:19342684}.; SUBCELLULAR LOCATION: [Isoform Delta15]: Cell junction {ECO:0000269|PubMed:18388311}. Note=Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells.
uniprot
proteins
transmembrane_region
TRANSMEM 602..620; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins