Q08481 (PECA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Platelet endothelial cell adhesion molecule
Short name=PECAM-1

Alternative name(s):
CD_antigen=CD31

Gene names

Name:	Pecam1
Synonyms:	Pecam, Pecam-1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	727 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-679 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). Modulates BDKRB2 activation By similarity. Induces susceptibility to atherosclerosis. Ref.9
Subunit structure	Interacts with PTPN11; Tyr-702 is critical for PTPN11 recruitment. Forms a complex with BDKRB2 and GNAQ. Interacts with BDKRB2 and GNAQ By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein. Cell junction By similarity. Note: Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells By similarity.
Tissue specificity	Isoform 1 and isoform 3 are expressed in lung and platelets. Ref.10
Domain	The Ig-like C2-type domains 2 and 3 contribute to formation of the complex with BDKRB2 and in regulation of its activity By similarity.
Post-translational modification	Phosphorylated on Ser and Tyr residues after cellular activation. In endothelial cells Fyn mediates mechanical-force (stretch or pull) induced tyrosine phosphorylation By similarity. Phosphorylated on tyrosine residues by FER and FES in response to FCER1 activation. Ref.7
Disruption phenotype	Mice show reduced atherosclerotic lesions. There is down-regulation of ICAM-1 in endothelial cells at the lesion periphery, and reduced disruption of Cx43 junctional staining at arterial branch points and in the descending aorta. Ref.9
Sequence similarities	Contains 6 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Membrane
Coding sequence diversity	Alternative splicing
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Rho protein signal transduction Inferred from mutant phenotype PubMed 12890700. Source: MGI cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cellular component movement Inferred from electronic annotation. Source: Compara positive regulation of leukocyte migration Inferred from electronic annotation. Source: Compara positive regulation of tyrosine phosphorylation of Stat5 protein Inferred from direct assay PubMed 11254359. Source: MGI regulation of cell migration Inferred from mutant phenotype PubMed 12890700. Source: MGI response to cytokine stimulus Inferred from electronic annotation. Source: Compara wound healing Inferred from mutant phenotype PubMed 12890700. Source: MGI
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-SubCell external side of plasma membrane Inferred from direct assay PubMed 20620994. Source: BHF-UCL integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane raft Inferred from direct assay PubMed 12890700. Source: MGI smooth muscle contractile fiber Inferred from direct assay PubMed 18332105. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q08481-1)

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.

Isoform 2 (identifier: Q08481-2)

The sequence of this isoform differs from the canonical sequence as follows:
     692-727: ALGTRATETVYSEIRKVDPNLMENRYSRTEGSLNGT → ENGRLP

Isoform 3 (identifier: Q08481-3)

The sequence of this isoform differs from the canonical sequence as follows:
     711-727: NLMENRYSRTEGSLNGT → KNGRLP

Isoform 4 (identifier: Q08481-4)

The sequence of this isoform differs from the canonical sequence as follows:
     119-219: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Ref.6
	Chain	18 – 727	710	Platelet endothelial cell adhesion molecule		PRO_0000014896
Regions
	Topological domain	18 – 590	573	Extracellular Potential
	Transmembrane	591 – 609	19	Helical; Potential
	Topological domain	610 – 727	118	Cytoplasmic Potential
	Domain	40 – 126	87	Ig-like C2-type 1
	Domain	135 – 213	79	Ig-like C2-type 2
	Domain	225 – 309	85	Ig-like C2-type 3
	Domain	315 – 391	77	Ig-like C2-type 4
	Domain	413 – 472	60	Ig-like C2-type 5
	Domain	488 – 578	91	Ig-like C2-type 6
	Region	710 – 727	18	May play a role in cytoprotective signaling By similarity
Amino acid modifications
	Modified residue	679	1	Phosphotyrosine; by FER Probable
	Modified residue	702	1	Phosphotyrosine; by FER Ref.7 Ref.8
	Lipidation	611	1	S-palmitoyl cysteine By similarity
	Glycosylation	74	1	N-linked (GlcNAc...) Ref.11
	Glycosylation	141	1	N-linked (GlcNAc...) Ref.11
	Glycosylation	309	1	N-linked (GlcNAc...) Potential
	Glycosylation	345	1	N-linked (GlcNAc...) Potential
	Glycosylation	360	1	N-linked (GlcNAc...) Ref.11
	Glycosylation	424	1	N-linked (GlcNAc...) Ref.11
	Glycosylation	540	1	N-linked (GlcNAc...) Ref.11
	Disulfide bond	47 ↔ 99		Potential
	Disulfide bond	142 ↔ 195		Potential
	Disulfide bond	245 ↔ 293		Potential
	Disulfide bond	336 ↔ 375		Potential
	Disulfide bond	420 ↔ 465		Potential
	Disulfide bond	512 ↔ 561		Potential
Natural variations
	Alternative sequence	119 – 219	101	Missing in isoform 4.		VSP_038723
	Alternative sequence	692 – 727	36	ALGTR…SLNGT → ENGRLP in isoform 2.		VSP_038724
	Alternative sequence	711 – 727	17	NLMEN…SLNGT → KNGRLP in isoform 3.		VSP_038725
Experimental info
	Mutagenesis	679	1	Y → F: Reduces tyrosine phosphorylation by FER by about 60%. Ref.7
	Mutagenesis	702	1	Y → F: Reduces tyrosine phosphorylation by FER by about 60%. Ref.7
	Mutagenesis	717	1	Y → F: No significant effect on phosphorylation by FER. Ref.7
	Sequence conflict	18	1	E → T AA sequence Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 34C04752D199BAA5	FASTA	727	81,263
	10 20 30 40 50 60 MLLALGLTLV LYASLQAEEN SFTINSIHME SLPSWEVMNG QQLTLECLVD ISTTSKSRSQ 70 80 90 100 110 120 HRVLFYKDDA MVYNVTSREH TESYVIPQAR VFHSGKYKCT VMLNNKEKTT IEYEVKVHGV 130 140 150 160 170 180 SKPKVTLDKK EVTEGGVVTV NCSLQEEKPP IFFKIEKLEV GTKFVKRRID KTSNENFVLM 190 200 210 220 230 240 EFPIEAQDHV LVFRCQAGIL SGFKLQESEP IRSEYVTVQE SFSTPKFEIK PPGMIIEGDQ 250 260 270 280 290 300 LHIRCIVQVT HLVQEFTEII IQKDKAIVAT SKQSSEAVYS VMAMVEYSGH YTCKVESNRI 310 320 330 340 350 360 SKASSIMVNI TELFPKPKLE FSSSRLDQGE LLDLSCSVSG TPVANFTIQK EETVLSQYQN 370 380 390 400 410 420 FSKIAEESDS GEYSCTAGIG KVVKRSGLVP IQVCEMLSKP SIFHDAKSEI IKGHAIGISC 430 440 450 460 470 480 QSENGTAPIT YHLMKAKSDF QTLEVTSNDP ATFTDKPTRD MEYQCRADNC HSHPAVFSEI 490 500 510 520 530 540 LRVRVIAPVD EVVISILSSN EVQSGSEMVL RCSVKEGTSP ITFQFYKEKE DRPFHQAVVN 550 560 570 580 590 600 DTQAFWHNKQ ASKKQEGQYY CTASNRASSM RTSPRSSTLA VRVFLAPWKK GLIAVVVIGV 610 620 630 640 650 660 VIATLIVAAK CYFLRKAKAK QKPVEMSRPA APLLNSNSEK ISEPSVEANS HYGYDDVSGN 670 680 690 700 710 720 DAVKPINQNK DPQNMDVEYT EVEVSSLEPH QALGTRATET VYSEIRKVDP NLMENRYSRT EGSLNGT
	Isoform 2 [UniParc]. Checksum: EF8538025C1AB55F	FASTA	697	77,917
	10 20 30 40 50 60 MLLALGLTLV LYASLQAEEN SFTINSIHME SLPSWEVMNG QQLTLECLVD ISTTSKSRSQ 70 80 90 100 110 120 HRVLFYKDDA MVYNVTSREH TESYVIPQAR VFHSGKYKCT VMLNNKEKTT IEYEVKVHGV 130 140 150 160 170 180 SKPKVTLDKK EVTEGGVVTV NCSLQEEKPP IFFKIEKLEV GTKFVKRRID KTSNENFVLM 190 200 210 220 230 240 EFPIEAQDHV LVFRCQAGIL SGFKLQESEP IRSEYVTVQE SFSTPKFEIK PPGMIIEGDQ 250 260 270 280 290 300 LHIRCIVQVT HLVQEFTEII IQKDKAIVAT SKQSSEAVYS VMAMVEYSGH YTCKVESNRI 310 320 330 340 350 360 SKASSIMVNI TELFPKPKLE FSSSRLDQGE LLDLSCSVSG TPVANFTIQK EETVLSQYQN 370 380 390 400 410 420 FSKIAEESDS GEYSCTAGIG KVVKRSGLVP IQVCEMLSKP SIFHDAKSEI IKGHAIGISC 430 440 450 460 470 480 QSENGTAPIT YHLMKAKSDF QTLEVTSNDP ATFTDKPTRD MEYQCRADNC HSHPAVFSEI 490 500 510 520 530 540 LRVRVIAPVD EVVISILSSN EVQSGSEMVL RCSVKEGTSP ITFQFYKEKE DRPFHQAVVN 550 560 570 580 590 600 DTQAFWHNKQ ASKKQEGQYY CTASNRASSM RTSPRSSTLA VRVFLAPWKK GLIAVVVIGV 610 620 630 640 650 660 VIATLIVAAK CYFLRKAKAK QKPVEMSRPA APLLNSNSEK ISEPSVEANS HYGYDDVSGN 670 680 690 DAVKPINQNK DPQNMDVEYT EVEVSSLEPH QENGRLP
	Isoform 3 [UniParc]. Checksum: E4D281B5523017B6	FASTA	716	80,004
	10 20 30 40 50 60 MLLALGLTLV LYASLQAEEN SFTINSIHME SLPSWEVMNG QQLTLECLVD ISTTSKSRSQ 70 80 90 100 110 120 HRVLFYKDDA MVYNVTSREH TESYVIPQAR VFHSGKYKCT VMLNNKEKTT IEYEVKVHGV 130 140 150 160 170 180 SKPKVTLDKK EVTEGGVVTV NCSLQEEKPP IFFKIEKLEV GTKFVKRRID KTSNENFVLM 190 200 210 220 230 240 EFPIEAQDHV LVFRCQAGIL SGFKLQESEP IRSEYVTVQE SFSTPKFEIK PPGMIIEGDQ 250 260 270 280 290 300 LHIRCIVQVT HLVQEFTEII IQKDKAIVAT SKQSSEAVYS VMAMVEYSGH YTCKVESNRI 310 320 330 340 350 360 SKASSIMVNI TELFPKPKLE FSSSRLDQGE LLDLSCSVSG TPVANFTIQK EETVLSQYQN 370 380 390 400 410 420 FSKIAEESDS GEYSCTAGIG KVVKRSGLVP IQVCEMLSKP SIFHDAKSEI IKGHAIGISC 430 440 450 460 470 480 QSENGTAPIT YHLMKAKSDF QTLEVTSNDP ATFTDKPTRD MEYQCRADNC HSHPAVFSEI 490 500 510 520 530 540 LRVRVIAPVD EVVISILSSN EVQSGSEMVL RCSVKEGTSP ITFQFYKEKE DRPFHQAVVN 550 560 570 580 590 600 DTQAFWHNKQ ASKKQEGQYY CTASNRASSM RTSPRSSTLA VRVFLAPWKK GLIAVVVIGV 610 620 630 640 650 660 VIATLIVAAK CYFLRKAKAK QKPVEMSRPA APLLNSNSEK ISEPSVEANS HYGYDDVSGN 670 680 690 700 710 DAVKPINQNK DPQNMDVEYT EVEVSSLEPH QALGTRATET VYSEIRKVDP KNGRLP
	Isoform 4 [UniParc]. Checksum: 0CF4D64C49CE468B	FASTA	626	69,823
	10 20 30 40 50 60 MLLALGLTLV LYASLQAEEN SFTINSIHME SLPSWEVMNG QQLTLECLVD ISTTSKSRSQ 70 80 90 100 110 120 HRVLFYKDDA MVYNVTSREH TESYVIPQAR VFHSGKYKCT VMLNNKEKTT IEYEVKVHES 130 140 150 160 170 180 FSTPKFEIKP PGMIIEGDQL HIRCIVQVTH LVQEFTEIII QKDKAIVATS KQSSEAVYSV 190 200 210 220 230 240 MAMVEYSGHY TCKVESNRIS KASSIMVNIT ELFPKPKLEF SSSRLDQGEL LDLSCSVSGT 250 260 270 280 290 300 PVANFTIQKE ETVLSQYQNF SKIAEESDSG EYSCTAGIGK VVKRSGLVPI QVCEMLSKPS 310 320 330 340 350 360 IFHDAKSEII KGHAIGISCQ SENGTAPITY HLMKAKSDFQ TLEVTSNDPA TFTDKPTRDM 370 380 390 400 410 420 EYQCRADNCH SHPAVFSEIL RVRVIAPVDE VVISILSSNE VQSGSEMVLR CSVKEGTSPI 430 440 450 460 470 480 TFQFYKEKED RPFHQAVVND TQAFWHNKQA SKKQEGQYYC TASNRASSMR TSPRSSTLAV 490 500 510 520 530 540 RVFLAPWKKG LIAVVVIGVV IATLIVAAKC YFLRKAKAKQ KPVEMSRPAA PLLNSNSEKI 550 560 570 580 590 600 SEPSVEANSH YGYDDVSGND AVKPINQNKD PQNMDVEYTE VEVSSLEPHQ ALGTRATETV 610 620 YSEIRKVDPN LMENRYSRTE GSLNGT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and adhesive properties of murine platelet/endothelial cell adhesion molecule 1." Xie Y., Muller W.A. Proc. Natl. Acad. Sci. U.S.A. 90:5569-5573(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: BALB/c. Tissue: Lung.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Strain: C57BL/6J. Tissue: Stomach.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6 and FVB/N. Tissue: Mammary tumor.
[6]	"Association of murine CD31 with transmigrating lymphocytes following antigenic stimulation." Bogen S.A., Baldwin H.S., Watkins S.C., Albelda S.M., Abbas A.K. Am. J. Pathol. 141:843-854(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-26. Tissue: Heart.
[7]	"Fer and Fps/Fes participate in a Lyn-dependent pathway from FcepsilonRI to platelet-endothelial cell adhesion molecule 1 to limit mast cell activation." Udell C.M., Samayawardhena L.A., Kawakami Y., Kawakami T., Craig A.W. J. Biol. Chem. 281:20949-20957(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-679 AND TYR-702 BY FES AND FER, MUTAGENESIS OF TYR-679; TYR-702 AND TYR-717.
[8]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-702, MASS SPECTROMETRY. Tissue: Mast cell.
[9]	"PECAM-1 is a critical mediator of atherosclerosis." Stevens H.Y., Melchior B., Bell K.S., Yun S., Yeh J.C., Frangos J.A. Dis. Model. Mech. 1:175-181(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[10]	"An alternatively spliced isoform of PECAM-1 is expressed at high levels in human and murine tissues, and suggests a novel role for the C-terminus of PECAM-1 in cytoprotective signaling." Bergom C., Paddock C., Gao C., Holyst T., Newman D.K., Newman P.J. J. Cell Sci. 121:1235-1242(2008) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), TISSUE SPECIFICITY.
[11]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74; ASN-141; ASN-360; ASN-424 AND ASN-540, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - Glycan Binding

PECAM-1

Cross-references

Sequence databases
EMBL GenBank DDBJ	L06039 mRNA. Translation: AAA16230.1. AK169431 mRNA. Translation: BAE41172.1. AL603664 Genomic DNA. Translation: CAM18558.1. AL603664 Genomic DNA. Translation: CAM18559.1. AL603664 Genomic DNA. Translation: CAM18560.1. CH466558 Genomic DNA. Translation: EDL34303.1. CH466558 Genomic DNA. Translation: EDL34304.1. CH466558 Genomic DNA. Translation: EDL34305.1. BC008519 mRNA. Translation: AAH08519.1. BC085502 mRNA. Translation: AAH85502.1.
IPI	IPI00554934. IPI00648680. IPI00649034. IPI00955102.
RefSeq	NP_001027550.1. NM_001032378.1. NP_032842.2. NM_008816.2.
UniGene	Mm.343951.
3D structure databases
ProteinModelPortal	Q08481.
SMR	Q08481. Positions 193-393, 693-727.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q08481. 4 interactions.
STRING	10090.ENSMUSP00000067111.
PTM databases
PhosphoSite	Q08481.
Proteomic databases
PaxDb	Q08481.
PRIDE	Q08481.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000080853; ENSMUSP00000079664; ENSMUSG00000020717. ENSMUST00000103069; ENSMUSP00000099358; ENSMUSG00000020717. ENSMUST00000106796; ENSMUSP00000102408; ENSMUSG00000020717.
GeneID	18613.
KEGG	mmu:18613.
UCSC	uc007lze.1. mouse. uc007lzf.1. mouse. uc007lzg.1. mouse. uc007lzh.1. mouse.
Organism-specific databases
CTD	5175.
MGI	MGI:97537. Pecam1.
Phylogenomic databases
eggNOG	NOG78738.
GeneTree	ENSGT00440000034155.
HOGENOM	HOG000049132.
HOVERGEN	HBG059434.
KO	K06471.
Gene expression databases
ArrayExpress	Q08481.
Bgee	Q08481.
CleanEx	MM_PECAM1.
Genevestigator	Q08481.
GermOnline	ENSMUSG00000020717. Mus musculus.
Family and domain databases
Gene3D	2.60.40.10. 4 hits.
InterPro	IPR007110. Ig-like_dom. IPR013783. Ig-like_fold. IPR003599. Ig_sub. [Graphical view]
SMART	SM00409. IG. 2 hits. [Graphical view]
PROSITE	PS50835. IG_LIKE. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	294550.
SOURCE	Search...

Entry information

Entry name

PECA1_MOUSE

Accession

Primary (citable) accession number: Q08481
Secondary accession number(s): B1ARB1 , B1ARB2, Q3TES6, Q922E0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program