CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004438
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Platelet endothelial cell adhesion molecule 
Protein Synonyms/Alias
 PECAM-1; EndoCAM; GPIIA'; PECA1; CD31 
Gene Name
 PECAM1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
158NCSVPEEKAPIHFTIubiquitination[1]
167PIHFTIEKLELNEKMubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
 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). 
Sequence Annotation
 DOMAIN 35 121 Ig-like C2-type 1.
 DOMAIN 145 233 Ig-like C2-type 2.
 DOMAIN 236 315 Ig-like C2-type 3.
 DOMAIN 328 401 Ig-like C2-type 4.
 DOMAIN 424 493 Ig-like C2-type 5.
 DOMAIN 499 591 Ig-like C2-type 6.
 REGION 721 738 May play a role in cytoprotective
 MOD_RES 690 690 Phosphotyrosine; by FER.
 MOD_RES 713 713 Phosphotyrosine; by FER.
 LIPID 622 622 S-palmitoyl cysteine.
 CARBOHYD 52 52 N-linked (GlcNAc...) (Potential).
 CARBOHYD 84 84 N-linked (GlcNAc...).
 CARBOHYD 151 151 N-linked (GlcNAc...).
 CARBOHYD 301 301 N-linked (GlcNAc...) (Potential).
 CARBOHYD 320 320 N-linked (GlcNAc...).
 CARBOHYD 344 344 N-linked (GlcNAc...) (Potential).
 CARBOHYD 356 356 N-linked (GlcNAc...) (Potential).
 CARBOHYD 453 453 N-linked (GlcNAc...).
 CARBOHYD 551 551 N-linked (GlcNAc...).
 DISULFID 57 109 Potential.
 DISULFID 152 206 Potential.
 DISULFID 256 304 Potential.
 DISULFID 347 386 Potential.
 DISULFID 431 476 Potential.
 DISULFID 523 572 Potential.  
Keyword
 3D-structure; Alternative splicing; Cell adhesion; Cell junction; Complete proteome; Disulfide bond; Glycoprotein; Immunoglobulin domain; Lipoprotein; Membrane; Palmitate; Phagocytosis; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 738 AA 
Protein Sequence
MQPRWAQGAT MWLGVLLTLL LCSSLEGQEN SFTINSVDMK SLPDWTVQNG KNLTLQCFAD 60
VSTTSHVKPQ HQMLFYKDDV LFYNISSMKS TESYFIPEVR IYDSGTYKCT VIVNNKEKTT 120
AEYQLLVEGV PSPRVTLDKK EAIQGGIVRV NCSVPEEKAP IHFTIEKLEL NEKMVKLKRE 180
KNSRDQNFVI LEFPVEEQDR VLSFRCQARI ISGIHMQTSE STKSELVTVT ESFSTPKFHI 240
SPTGMIMEGA QLHIKCTIQV THLAQEFPEI IIQKDKAIVA HNRHGNKAVY SVMAMVEHSG 300
NYTCKVESSR ISKVSSIVVN ITELFSKPEL ESSFTHLDQG ERLNLSCSIP GAPPANFTIQ 360
KEDTIVSQTQ DFTKIASKSD SGTYICTAGI DKVVKKSNTV QIVVCEMLSQ PRISYDAQFE 420
VIKGQTIEVR CESISGTLPI SYQLLKTSKV LENSTKNSND PAVFKDNPTE DVEYQCVADN 480
CHSHAKMLSE VLRVKVIAPV DEVQISILSS KVVESGEDIV LQCAVNEGSG PITYKFYREK 540
EGKPFYQMTS NATQAFWTKQ KASKEQEGEY YCTAFNRANH ASSVPRSKIL TVRVILAPWK 600
KGLIAVVIIG VIIALLIIAA KCYFLRKAKA KQMPVEMSRP AVPLLNSNNE KMSDPNMEAN 660
SHYEPLNSDV QYTEVQVSSA ESHKDLGKKD TETVYSEVRK AVPDAVESRY SRTEGSLDGT 720 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
 GO:0005615; C:extracellular space; IDA:BHF-UCL.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0008037; P:cell recognition; TAS:ProtInc.
 GO:0050904; P:diapedesis; IDA:UniProtKB.
 GO:0072011; P:glomerular endothelium development; IEP:UniProtKB.
 GO:0006909; P:phagocytosis; IDA:UniProtKB.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome.
 GO:0007165; P:signal transduction; TAS:ProtInc. 
Interpro
 IPR007110; Ig-like_dom.
 IPR013783; Ig-like_fold.
 IPR003599; Ig_sub. 
Pfam
  
SMART
 SM00409; IG 
PROSITE
 PS50835; IG_LIKE 
PRINTS