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Protein Page:
PECAM-1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PECAM-1 a cell adhesion molecule expressed on platelets and at endothelial cell intercellular junctions. Plays a role in modulation of integrin-mediated cell adhesion, transendothelial migration, angiogenesis, apoptosis, cell migration, negative regulation of immune cell signaling, autoimmunity, macrophage phagocytosis, IgE-mediated anaphylaxis and thrombosis. Undergoes alternative splicing, generating multiple isoforms in vascular beds of various tissues. Note: This description may include information from UniProtKB.
Protein type: Cell adhesion; Membrane protein, integral
Chromosomal Location of Human Ortholog: 17q23.3
Cellular Component: cell junction; extracellular space; integral to membrane; lipid raft; plasma membrane; platelet alpha granule membrane
Molecular Function: protein binding
Biological Process: blood coagulation; cell adhesion; cell recognition; diapedesis; extracellular matrix organization and biogenesis; leukocyte migration; phagocytosis; platelet activation; platelet degranulation; signal transduction
Reference #:  P16284 (UniProtKB)
Alt. Names/Synonyms: adhesion molecule; CD31; CD31 antigen; CD31/EndoCAM; EndoCAM; FLJ58394; GPIIA'; PECA1; PECAM-1; PECAM-1, CD31/EndoCAM; PECAM1; Platelet endothelial cell adhesion molecule; platelet/endothelial cell adhesion molecule
Gene Symbols: PECAM1
Molecular weight: 82,536 Da
Basal Isoelectric point: 6.55  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PECAM-1

Protein Structure Not Found.


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Sites Implicated In
cell adhesion, altered: Y690‑p, Y713‑p
cell motility, altered: Y713‑p
cytoskeletal reorganization: Y690‑p, Y713‑p
endocytosis, induced: Y713‑p
activity, induced: Y690‑p, Y713‑p
intracellular localization: Y713‑p
molecular association, regulation: Y690‑p, S700‑p, Y713‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 K167 PIHFTIEKLELNEKM
0 1 Y290‑p RHGNKAVySVMAMVE
0 1 S409‑p IVVCEMLsQPRISYD
0 1 Q418 PRISYDAQFEVIKGQ
0 1 N467 DPAVFKDNPTEDVEY
0 1 S583‑p NRANHASsVPRsKIL
0 1 S587‑p HASsVPRsKILTVRV
0 1 Y623‑p LIIAAKCyFLRKAKA
0 1 S647‑p PAVPLLNsNNEKMsD
0 1 S653‑p NsNNEKMsDPNMEAN
0 9 Y663‑p NMEANSHyGHNDDVR
0 1 V669 HyGHNDDVRNHAMKP
1 3 S686‑p DNKEPLNsDVQytEV
8 43 Y690‑p PLNsDVQytEVQVSS
0 3 T691‑p LNsDVQytEVQVSSA
1 3 S700‑p VQVSSAEsHKDLGKK
0 8 T709‑p KDLGKKDtEtVysEV
0 16 T711‑p LGKKDtEtVysEVRK
11 790 Y713‑p KKDtEtVysEVRKAV
0 28 S714‑p KDtEtVysEVRKAVP
1 2 Y728‑p PDAVESRysRTEGsL
0 2 S729‑p DAVESRysRTEGsLD
0 2 S734‑p RysRTEGsLDGt___
0 1 T738‑p TEGsLDGt_______
  PECAM-1 iso2  
K167 PIHFTIEKLELNEKM
Y290 RHGNKAVYSVMAMVE
S409 IVVCEMLSQPRISYD
Q418 PRISYDAQFEVIKGQ
N467 DPAVFKDNPTEDVEY
S583 NRANHASSVPRSKIL
S587 HASSVPRSKILTVRV
Y623 LIIAAKCYFLRKAKA
S647 PAVPLLNSNNEKMSD
S653 NSNNEKMSDPNMEAN
Y663 NMEANSHYEPLNSDV
- gap
S668 SHYEPLNSDVQYTEV
Y672 PLNSDVQYTEVQVSS
T673 LNSDVQYTEVQVSSA
S682 VQVSSAESHKDLGKK
T691 KDLGKKDTETVYSEV
T693 LGKKDTETVYSEVRK
Y695 KKDTETVYSEVRKAV
S696 KDTETVYSEVRKAVP
Y710 PDAVESRYSRTEGSL
S711 DAVESRYSRTEGSLD
S716 RYSRTEGSLDGT___
T720 TEGSLDGT_______
  mouse

 
K157 PIFFKIEKLEVGTKF
Y279 KQSSEAVYSVMAMVE
S398 IQVCEMLSKPSIFHD
K407 PSIFHDAKSEIIKGH
K456 DPATFTDKPTRDMEY
S573 RASSMRTSPRSSTLA
S576 SMRTSPRSSTLAVRV
Y612 LIVAAKCYFLRKAKA
S636 PAAPLLNSNSEKISE
S642 NSNSEKISEPSVEAN
Y652 SVEANSHYGYDDVsG
S658‑p HYGYDDVsGNDAVKP
M675 QNKDPQNMDVEyTEV
Y679‑p PQNMDVEyTEVEVSS
T680 QNMDVEyTEVEVSSL
P689 VEVSSLEPHQALGTR
T698 QALGTRATETVysEI
T700 LGTRATETVysEIRK
Y702‑p TRATETVysEIRKVD
S703‑p RATETVysEIRKVDP
Y717‑p PNLMENRysRTEGSL
S718‑p NLMENRysRTEGSLN
S723 RysRTEGSLNGT___
T727 TEGSLNGT_______
  rat

 
K157‑ac PIYFKIEkVELGTKN
Y279 KQSKEAVYSVMALVE
S398 VQVCEMLSKPRIFHD
K407‑ac PRIFHDAkFEIIKGQ
K456‑ac DPVTFTDkPTRDMEY
S572 NRASIVTSLRSGPLT
S575 SIVTSLRSGPLTVRV
Y611 LIVAAKYYFLRKAKA
S635 PAVPLLNSNSEKVSE
S641 NSNSEKVSEPSVETN
Y651 SVETNSHYDSQNMDV
- gap
M656 SHYDSQNMDVEYTEV
Y660 SQNMDVEYTEVEVSS
T661 QNMDVEYTEVEVSSL
P670 VEVSSLEPHQENGRL
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
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