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Q08481

- PECA1_MOUSE

UniProt

Q08481 - PECA1_MOUSE

Protein

Platelet endothelial cell adhesion molecule

Gene

Pecam1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    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.By similarity1 Publication

    GO - Molecular functioni

    1. protein binding Source: MGI

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. cellular component movement Source: Ensembl
    3. negative regulation of actin filament polymerization Source: Ensembl
    4. negative regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
    5. negative regulation of Rho GTPase activity Source: Ensembl
    6. positive regulation of leukocyte migration Source: Ensembl
    7. positive regulation of tyrosine phosphorylation of Stat5 protein Source: MGI
    8. regulation of cell migration Source: MGI
    9. response to cytokine Source: Ensembl
    10. Rho protein signal transduction Source: MGI
    11. wound healing Source: MGI

    Keywords - Biological processi

    Cell adhesion

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet endothelial cell adhesion molecule
    Short name:
    PECAM-1
    Alternative name(s):
    CD_antigen: CD31
    Gene namesi
    Name:Pecam1
    Synonyms:Pecam, Pecam-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:97537. Pecam1.

    Subcellular locationi

    Cell membrane By similarity; Single-pass type I membrane protein By similarity. Cell membrane By similarity; Lipid-anchor By similarity. Cell junction
    Note: Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-SubCell
    2. cell periphery Source: MGI
    3. external side of plasma membrane Source: BHF-UCL
    4. integral component of membrane Source: UniProtKB-KW
    5. membrane Source: MGI
    6. membrane raft Source: MGI
    7. plasma membrane Source: MGI
    8. smooth muscle contractile fiber Source: MGI

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    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.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi679 – 6791Y → F: Reduces tyrosine phosphorylation by FER by about 60%. 1 Publication
    Mutagenesisi702 – 7021Y → F: Reduces tyrosine phosphorylation by FER by about 60%. 1 Publication
    Mutagenesisi717 – 7171Y → F: No significant effect on phosphorylation by FER. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17171 PublicationAdd
    BLAST
    Chaini18 – 727710Platelet endothelial cell adhesion moleculePRO_0000014896Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi47 ↔ 99PROSITE-ProRule annotation
    Glycosylationi74 – 741N-linked (GlcNAc...)1 Publication
    Glycosylationi141 – 1411N-linked (GlcNAc...)1 Publication
    Disulfide bondi142 ↔ 195PROSITE-ProRule annotation
    Disulfide bondi245 ↔ 293PROSITE-ProRule annotation
    Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi336 ↔ 375PROSITE-ProRule annotation
    Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi360 – 3601N-linked (GlcNAc...)1 Publication
    Disulfide bondi420 ↔ 465PROSITE-ProRule annotation
    Glycosylationi424 – 4241N-linked (GlcNAc...)1 Publication
    Disulfide bondi512 ↔ 561PROSITE-ProRule annotation
    Glycosylationi540 – 5401N-linked (GlcNAc...)1 Publication
    Lipidationi611 – 6111S-palmitoyl cysteineBy similarity
    Modified residuei679 – 6791Phosphotyrosine; by FER1 Publication
    Modified residuei702 – 7021Phosphotyrosine; by FER2 Publications

    Post-translational modificationi

    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.By similarity2 Publications
    Palmitoylation by ZDHHC21 is necessary for cell surface expression in endothelial cells.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiQ08481.
    PaxDbiQ08481.
    PRIDEiQ08481.

    PTM databases

    PhosphoSiteiQ08481.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 3 are expressed in lung and platelets.1 Publication

    Gene expression databases

    ArrayExpressiQ08481.
    BgeeiQ08481.
    CleanExiMM_PECAM1.
    GenevestigatoriQ08481.

    Interactioni

    Subunit structurei

    Interacts with PTPN11; Tyr-702 is critical for PTPN11 recruitment. Forms a complex with BDKRB2 and GNAQ. Interacts with BDKRB2 and GNAQ By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ08481. 5 interactions.
    MINTiMINT-4106994.
    STRINGi10090.ENSMUSP00000067111.

    Structurei

    3D structure databases

    ProteinModelPortaliQ08481.
    SMRiQ08481. Positions 193-393, 693-727.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini18 – 590573ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini610 – 727118CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei591 – 60919HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 12687Ig-like C2-type 1Add
    BLAST
    Domaini135 – 21379Ig-like C2-type 2Add
    BLAST
    Domaini225 – 30985Ig-like C2-type 3Add
    BLAST
    Domaini315 – 39177Ig-like C2-type 4Add
    BLAST
    Domaini413 – 47260Ig-like C2-type 5Add
    BLAST
    Domaini488 – 57891Ig-like C2-type 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni710 – 72718May play a role in cytoprotective signalingBy similarityAdd
    BLAST

    Domaini

    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

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG78738.
    GeneTreeiENSGT00440000034155.
    HOGENOMiHOG000049132.
    HOVERGENiHBG059434.
    KOiK06471.
    OrthoDBiEOG7Z95KP.
    TreeFamiTF338229.

    Family and domain databases

    Gene3Di2.60.40.10. 4 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    [Graphical view]
    SMARTiSM00409. IG. 2 hits.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 3 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q08481-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MLLALGLTLV LYASLQAEEN SFTINSIHME SLPSWEVMNG QQLTLECLVD    50
    ISTTSKSRSQ HRVLFYKDDA MVYNVTSREH TESYVIPQAR VFHSGKYKCT 100
    VMLNNKEKTT IEYEVKVHGV SKPKVTLDKK EVTEGGVVTV NCSLQEEKPP 150
    IFFKIEKLEV GTKFVKRRID KTSNENFVLM EFPIEAQDHV LVFRCQAGIL 200
    SGFKLQESEP IRSEYVTVQE SFSTPKFEIK PPGMIIEGDQ LHIRCIVQVT 250
    HLVQEFTEII IQKDKAIVAT SKQSSEAVYS VMAMVEYSGH YTCKVESNRI 300
    SKASSIMVNI TELFPKPKLE FSSSRLDQGE LLDLSCSVSG TPVANFTIQK 350
    EETVLSQYQN FSKIAEESDS GEYSCTAGIG KVVKRSGLVP IQVCEMLSKP 400
    SIFHDAKSEI IKGHAIGISC QSENGTAPIT YHLMKAKSDF QTLEVTSNDP 450
    ATFTDKPTRD MEYQCRADNC HSHPAVFSEI LRVRVIAPVD EVVISILSSN 500
    EVQSGSEMVL RCSVKEGTSP ITFQFYKEKE DRPFHQAVVN DTQAFWHNKQ 550
    ASKKQEGQYY CTASNRASSM RTSPRSSTLA VRVFLAPWKK GLIAVVVIGV 600
    VIATLIVAAK CYFLRKAKAK QKPVEMSRPA APLLNSNSEK ISEPSVEANS 650
    HYGYDDVSGN DAVKPINQNK DPQNMDVEYT EVEVSSLEPH QALGTRATET 700
    VYSEIRKVDP NLMENRYSRT EGSLNGT 727
    Length:727
    Mass (Da):81,263
    Last modified:October 1, 1994 - v1
    Checksum:i34C04752D199BAA5
    GO
    Isoform 2 (identifier: Q08481-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:697
    Mass (Da):77,917
    Checksum:iEF8538025C1AB55F
    GO
    Isoform 3 (identifier: Q08481-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:716
    Mass (Da):80,004
    Checksum:iE4D281B5523017B6
    GO
    Isoform 4 (identifier: Q08481-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:626
    Mass (Da):69,823
    Checksum:i0CF4D64C49CE468B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181E → T AA sequence (PubMed:1415479)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei119 – 219101Missing in isoform 4. 1 PublicationVSP_038723Add
    BLAST
    Alternative sequencei692 – 72736ALGTR…SLNGT → ENGRLP in isoform 2. 1 PublicationVSP_038724Add
    BLAST
    Alternative sequencei711 – 72717NLMEN…SLNGT → KNGRLP in isoform 3. CuratedVSP_038725Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS25558.1. [Q08481-2]
    CCDS25559.1. [Q08481-3]
    RefSeqiNP_001027550.1. NM_001032378.1. [Q08481-2]
    NP_032842.2. NM_008816.2. [Q08481-3]
    XP_006532533.1. XM_006532470.1. [Q08481-1]
    XP_006532539.1. XM_006532476.1. [Q08481-4]
    UniGeneiMm.343951.

    Genome annotation databases

    EnsembliENSMUST00000080853; ENSMUSP00000079664; ENSMUSG00000020717. [Q08481-3]
    ENSMUST00000103069; ENSMUSP00000099358; ENSMUSG00000020717. [Q08481-2]
    ENSMUST00000106796; ENSMUSP00000102408; ENSMUSG00000020717. [Q08481-1]
    ENSMUST00000183610; ENSMUSP00000138959; ENSMUSG00000020717. [Q08481-4]
    GeneIDi18613.
    KEGGimmu:18613.
    UCSCiuc007lze.1. mouse. [Q08481-1]
    uc007lzf.1. mouse. [Q08481-3]
    uc007lzg.1. mouse. [Q08481-2]
    uc007lzh.1. mouse. [Q08481-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    PECAM-1

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS25558.1. [Q08481-2 ]
    CCDS25559.1. [Q08481-3 ]
    RefSeqi NP_001027550.1. NM_001032378.1. [Q08481-2 ]
    NP_032842.2. NM_008816.2. [Q08481-3 ]
    XP_006532533.1. XM_006532470.1. [Q08481-1 ]
    XP_006532539.1. XM_006532476.1. [Q08481-4 ]
    UniGenei Mm.343951.

    3D structure databases

    ProteinModelPortali Q08481.
    SMRi Q08481. Positions 193-393, 693-727.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q08481. 5 interactions.
    MINTi MINT-4106994.
    STRINGi 10090.ENSMUSP00000067111.

    PTM databases

    PhosphoSitei Q08481.

    Proteomic databases

    MaxQBi Q08481.
    PaxDbi Q08481.
    PRIDEi Q08481.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000080853 ; ENSMUSP00000079664 ; ENSMUSG00000020717 . [Q08481-3 ]
    ENSMUST00000103069 ; ENSMUSP00000099358 ; ENSMUSG00000020717 . [Q08481-2 ]
    ENSMUST00000106796 ; ENSMUSP00000102408 ; ENSMUSG00000020717 . [Q08481-1 ]
    ENSMUST00000183610 ; ENSMUSP00000138959 ; ENSMUSG00000020717 . [Q08481-4 ]
    GeneIDi 18613.
    KEGGi mmu:18613.
    UCSCi uc007lze.1. mouse. [Q08481-1 ]
    uc007lzf.1. mouse. [Q08481-3 ]
    uc007lzg.1. mouse. [Q08481-2 ]
    uc007lzh.1. mouse. [Q08481-4 ]

    Organism-specific databases

    CTDi 5175.
    MGIi MGI:97537. Pecam1.

    Phylogenomic databases

    eggNOGi NOG78738.
    GeneTreei ENSGT00440000034155.
    HOGENOMi HOG000049132.
    HOVERGENi HBG059434.
    KOi K06471.
    OrthoDBi EOG7Z95KP.
    TreeFami TF338229.

    Miscellaneous databases

    NextBioi 294550.
    PROi Q08481.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q08481.
    Bgeei Q08481.
    CleanExi MM_PECAM1.
    Genevestigatori Q08481.

    Family and domain databases

    Gene3Di 2.60.40.10. 4 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    [Graphical view ]
    SMARTi SM00409. IG. 2 hits.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    9. 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.

    Entry informationi

    Entry nameiPECA1_MOUSE
    AccessioniPrimary (citable) accession number: Q08481
    Secondary accession number(s): B1ARB1
    , B1ARB2, Q3TES6, Q922E0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3