dbPTM

PECA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PECA1_HUMAN
UniProt AC	P16284
Protein Name	Platelet endothelial cell adhesion molecule
Gene Name	PECAM1
Organism	Homo sapiens (Human).
Sequence Length	738
Subcellular Localization	Cell membrane Single-pass type I membrane protein . Cell surface expression on neutrophils is down-regulated upon fMLP or CXCL8/IL8-mediated stimulation. Isoform Long: Cell membrane Single-pass type I membrane protein . Membrane raft . Cell junc
Protein Description	Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. [PubMed: 19342684]
Protein Sequence	MQPRWAQGATMWLGVLLTLLLCSSLEGQENSFTINSVDMKSLPDWTVQNGKNLTLQCFADVSTTSHVKPQHQMLFYKDDVLFYNISSMKSTESYFIPEVRIYDSGTYKCTVIVNNKEKTTAEYQVLVEGVPSPRVTLDKKEAIQGGIVRVNCSVPEEKAPIHFTIEKLELNEKMVKLKREKNSRDQNFVILEFPVEEQDRVLSFRCQARIISGIHMQTSESTKSELVTVTESFSTPKFHISPTGMIMEGAQLHIKCTIQVTHLAQEFPEIIIQKDKAIVAHNRHGNKAVYSVMAMVEHSGNYTCKVESSRISKVSSIVVNITELFSKPELESSFTHLDQGERLNLSCSIPGAPPANFTIQKEDTIVSQTQDFTKIASKSDSGTYICTAGIDKVVKKSNTVQIVVCEMLSQPRISYDAQFEVIKGQTIEVRCESISGTLPISYQLLKTSKVLENSTKNSNDPAVFKDNPTEDVEYQCVADNCHSHAKMLSEVLRVKVIAPVDEVQISILSSKVVESGEDIVLQCAVNEGSGPITYKFYREKEGKPFYQMTSNATQAFWTKQKASKEQEGEYYCTAFNRANHASSVPRSKILTVRVILAPWKKGLIAVVIIGVIIALLIIAAKCYFLRKAKAKQMPVEMSRPAVPLLNSNNEKMSDPNMEANSHYGHNDDVRNHAMKPINDNKEPLNSDVQYTEVQVSSAESHKDLGKKDTETVYSEVRKAVPDAVESRYSRTEGSLDGT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	PRWAQGATMWLGVLL CCHHHHHHHHHHHHH	18.72	24043423
18	Phosphorylation	MWLGVLLTLLLCSSL HHHHHHHHHHHHHHC	15.93	24043423
23	Phosphorylation	LLTLLLCSSLEGQEN HHHHHHHHHCCCCCC	37.62	24043423
24	Phosphorylation	LTLLLCSSLEGQENS HHHHHHHHCCCCCCE	29.46	24043423
31	Phosphorylation	SLEGQENSFTINSVD HCCCCCCEEEEEEEE	24.02	24043423
33	Phosphorylation	EGQENSFTINSVDMK CCCCCEEEEEEEEHH	21.04	24043423
36	Phosphorylation	ENSFTINSVDMKSLP CCEEEEEEEEHHHCC	18.68	24043423
52	N-linked_Glycosylation	WTVQNGKNLTLQCFA CEEECCCEEEEEEEE	39.39	26702061
84	N-linked_Glycosylation	KDDVLFYNISSMKST ECCEEEEECCCCCCC	21.97	17660510
108	Ubiquitination	IYDSGTYKCTVIVNN EEECCEEEEEEEECC	24.22	-
139	Ubiquitination	SPRVTLDKKEAIQGG CCCEEECHHHHHCCC	56.47	24816145
140	Ubiquitination	PRVTLDKKEAIQGGI CCEEECHHHHHCCCE	52.63	-
151	N-linked_Glycosylation	QGGIVRVNCSVPEEK CCCEEEEECCCCCHH	11.20	17660510
153	O-linked_Glycosylation	GIVRVNCSVPEEKAP CEEEEECCCCCHHCC	35.19	29351928
158 (in isoform 2)	Ubiquitination	-	58.77	-
158	Ubiquitination	NCSVPEEKAPIHFTI ECCCCCHHCCCEEEE	58.77	23503661
167 (in isoform 2)	Ubiquitination	-	43.33	-
167	Ubiquitination	PIHFTIEKLELNEKM CCEEEEEEHHHCHHH	43.33	23503661
173	Ubiquitination	EKLELNEKMVKLKRE EEHHHCHHHHHHHHH	48.17	23503661
203	Phosphorylation	EEQDRVLSFRCQARI HHCCCEEEEEEEEEE	14.05	24719451
276	Ubiquitination	EIIIQKDKAIVAHNR EEEEECCCEEEEECC	47.23	-
290	Phosphorylation	RHGNKAVYSVMAMVE CCCCCEEEEEEEEEE	10.62	18187866
301	N-linked_Glycosylation	AMVEHSGNYTCKVES EEEECCCCEEEEEEH	31.77	UniProtKB CARBOHYD
308	Phosphorylation	NYTCKVESSRISKVS CEEEEEEHHHHCEEE	28.09	18187866
309	Phosphorylation	YTCKVESSRISKVSS EEEEEEHHHHCEEEE	21.81	18187866
320	N-linked_Glycosylation	KVSSIVVNITELFSK EEEEEEEEHHHHCCC	25.27	19349973
326	Phosphorylation	VNITELFSKPELESS EEHHHHCCCHHHHCC	60.98	24719451
344	N-linked_Glycosylation	LDQGERLNLSCSIPG CCCCCCEEEEEECCC	35.81	17660510
356	N-linked_Glycosylation	IPGAPPANFTIQKED CCCCCCCCCEEECCC	40.13	17660510
374	Ubiquitination	SQTQDFTKIASKSDS EECCCCEECCCCCCC	35.95	29967540
378	Ubiquitination	DFTKIASKSDSGTYI CCEECCCCCCCCEEE	49.62	29967540
392	Ubiquitination	ICTAGIDKVVKKSNT EECCCCCCEECCCCE	47.19	29967540
409	Phosphorylation	IVVCEMLSQPRISYD EEEEECCCCCCEEEE	36.51	20068231
433	Phosphorylation	TIEVRCESISGTLPI EEEEEEEECCCCCCE	26.19	29083192
435	Phosphorylation	EVRCESISGTLPISY EEEEEECCCCCCEEE	34.70	29083192
437	Phosphorylation	RCESISGTLPISYQL EEEECCCCCCEEEHH	23.67	29083192
441	Phosphorylation	ISGTLPISYQLLKTS CCCCCCEEEHHHHHH	12.60	29083192
442	Phosphorylation	SGTLPISYQLLKTSK CCCCCEEEHHHHHHH	12.14	29759185
446	Ubiquitination	PISYQLLKTSKVLEN CEEEHHHHHHHHHHC	60.38	-
446	Acetylation	PISYQLLKTSKVLEN CEEEHHHHHHHHHHC	60.38	21669532
447	Phosphorylation	ISYQLLKTSKVLENS EEEHHHHHHHHHHCC	33.48	29759185
449	Acetylation	YQLLKTSKVLENSTK EHHHHHHHHHHCCCC	56.95	21669532
449	Ubiquitination	YQLLKTSKVLENSTK EHHHHHHHHHHCCCC	56.95	29967540
453	N-linked_Glycosylation	KTSKVLENSTKNSND HHHHHHHCCCCCCCC	51.31	17660510
456	Ubiquitination	KVLENSTKNSNDPAV HHHHCCCCCCCCCCC	59.19	29967540
495	Ubiquitination	LSEVLRVKVIAPVDE HHHHCCCEEEECCCE	22.84	-
551	N-linked_Glycosylation	PFYQMTSNATQAFWT CEEECCCCHHHHHHH	37.53	19349973
564	Ubiquitination	WTKQKASKEQEGEYY HHCCCCCHHHCCCEE	69.17	-
583	Phosphorylation	NRANHASSVPRSKIL CCCCCCCCCCHHHEE	36.60	16674116
587	Phosphorylation	HASSVPRSKILTVRV CCCCCCHHHEEEEEE	20.27	16674116
621	Acetylation	ALLIIAAKCYFLRKA HHHHHHHHHHHHHHH	22.05	21669532
622	S-palmitoylation	LLIIAAKCYFLRKAK HHHHHHHHHHHHHHH	2.20	17139370
623	Phosphorylation	LIIAAKCYFLRKAKA HHHHHHHHHHHHHHH	12.63	-
627	Acetylation	AKCYFLRKAKAKQMP HHHHHHHHHHHHCCC	57.28	21669532
631	Ubiquitination	FLRKAKAKQMPVEMS HHHHHHHHCCCCCCC	46.56	-
638	Phosphorylation	KQMPVEMSRPAVPLL HCCCCCCCCCCCCCC	22.93	26074081
647	Phosphorylation	PAVPLLNSNNEKMSD CCCCCCCCCCCCCCC	40.79	26846344
653	Phosphorylation	NSNNEKMSDPNMEAN CCCCCCCCCCCCCCC	62.07	26657352
661	Phosphorylation	DPNMEANSHYGHNDD CCCCCCCCCCCCCHH	25.74	28796482
663	Dephosphorylation	NMEANSHYGHNDDVR CCCCCCCCCCCHHHH	21.65	9774457
663	Phosphorylation	NMEANSHYGHNDDVR CCCCCCCCCCCHHHH	21.65	24702127
686	Phosphorylation	DNKEPLNSDVQYTEV CCCCCCCCCCCEEEE	47.01	28270605
690	Phosphorylation	PLNSDVQYTEVQVSS CCCCCCCEEEEEEEC	12.52	11927609
690	Dephosphorylation	PLNSDVQYTEVQVSS CCCCCCCEEEEEEEC	12.52	9774457
691	Phosphorylation	LNSDVQYTEVQVSSA CCCCCCEEEEEEECC	16.76	28060719
696	Phosphorylation	QYTEVQVSSAESHKD CEEEEEEECCHHCHH	13.52	28060719
697	Phosphorylation	YTEVQVSSAESHKDL EEEEEEECCHHCHHC	36.88	28060719
700	Phosphorylation	VQVSSAESHKDLGKK EEEECCHHCHHCCCC	35.24	15766557
709	Phosphorylation	KDLGKKDTETVYSEV HHCCCCCHHHHHHHH	42.30	28796482
711	Phosphorylation	LGKKDTETVYSEVRK CCCCCHHHHHHHHHH	27.17	28796482
713	Nitration	KKDTETVYSEVRKAV CCCHHHHHHHHHHHC	13.41	-
713	Dephosphorylation	KKDTETVYSEVRKAV CCCHHHHHHHHHHHC	13.41	9774457
713	Phosphorylation	KKDTETVYSEVRKAV CCCHHHHHHHHHHHC	13.41	11927609
714	Phosphorylation	KDTETVYSEVRKAVP CCHHHHHHHHHHHCC	25.86	23401153
726	Phosphorylation	AVPDAVESRYSRTEG HCCHHHHHCCCCCCC	29.89	23403867
728	Phosphorylation	PDAVESRYSRTEGSL CHHHHHCCCCCCCCC	16.28	23911959
729	Phosphorylation	DAVESRYSRTEGSLD HHHHHCCCCCCCCCC	31.45	23911959
731	Phosphorylation	VESRYSRTEGSLDGT HHHCCCCCCCCCCCC	38.46	23403867
734	Phosphorylation	RYSRTEGSLDGT--- CCCCCCCCCCCC---	19.63	28355574
738	Phosphorylation	TEGSLDGT------- CCCCCCCC-------	34.79	23403867

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
690	Y	Phosphorylation	Kinase	FER	P16591	Uniprot
690	Y	Phosphorylation	Kinase	FYN	P06241	PSP
713	Y	Phosphorylation	Kinase	FER	P16591	Uniprot
713	Y	Phosphorylation	Kinase	FYN	P06241	PSP
713	Y	Phosphorylation	Kinase	LCK	P06239	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:31489637
-	K	Ubiquitination	E3 ubiquitin ligase	K5	P90489	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
729	S	Phosphorylation	21464369
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.
734	S	Phosphorylation	21464369
Constitutively phosphorylated on Ser-734 in resting platelets.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PECA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XRCC6_HUMAN	XRCC6	physical	16169070
CTNB1_HUMAN	CTNNB1	physical	10801826
PTN11_HUMAN	PTPN11	physical	10801826
MK01_HUMAN	MAPK1	physical	10801826
DESP_HUMAN	DSP	physical	10801826
PLAK_HUMAN	JUP	physical	10801826
P85A_HUMAN	PIK3R1	physical	9774384
PTN11_HUMAN	PTPN11	physical	10350061
PLCG1_HUMAN	PLCG1	physical	10350061
SHIP1_HUMAN	INPP5D	physical	10350061
PTN6_HUMAN	PTPN6	physical	10350061
PTN11_HUMAN	PTPN11	physical	9774457
PTN6_HUMAN	PTPN6	physical	9774457
PECA1_HUMAN	PECAM1	physical	10425179
PTN11_HUMAN	PTPN11	physical	9054388
CTNB1_HUMAN	CTNNB1	physical	25241761
SRC_HUMAN	SRC	physical	12775720
2AAA_HUMAN	PPP2R1A	physical	12775720
LEG1_HUMAN	LGALS1	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PECA1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-320 AND ASN-551,AND MASS SPECTROMETRY.	19349973 [Abstract]
"Glycoproteomics analysis of human liver tissue by combination ofmultiple 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). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151; ASN-320 AND ASN-453,AND MASS SPECTROMETRY.	19159218 [Abstract]
Palmitoylation
Reference	PubMed
"Palmitoylation at Cys595 is essential for PECAM-1 localisation intomembrane microdomains and for efficient PECAM-1-mediatedcytoprotection."; 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). Cited for: PALMITOYLATION AT CYS-622, AND MUTAGENESIS OF CYS-622.	17139370 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-713, AND MASSSPECTROMETRY.	19690332 [Abstract]
"A novel and critical role for tyrosine 663 in platelet endothelialcell adhesion molecule-1 trafficking and transendothelial migration."; Dasgupta B., Dufour E., Mamdouh Z., Muller W.A.; J. Immunol. 182:5041-5051(2009). Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION ATTYR-690 AND TYR-713, MUTAGENESIS OF LYS-89; TYR-690 AND TYR-713, ANDINTERACTION WITH PTPN11.	19342684 [Abstract]
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-713, AND MASSSPECTROMETRY.	18088087 [Abstract]
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-290, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-713, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-713, AND MASSSPECTROMETRY.	15592455 [Abstract]
"Tyrosine residue in exon 14 of the cytoplasmic domain of plateletendothelial cell adhesion molecule-1 (PECAM-1/CD31) regulates ligandbinding specificity."; Famiglietti J., Sun J., DeLisser H.M., Albelda S.M.; J. Cell Biol. 138:1425-1435(1997). Cited for: PHOSPHORYLATION AT TYR-713.	9298995 [Abstract]

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