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Q6DIB5

- MEG10_MOUSE

UniProt

Q6DIB5 - MEG10_MOUSE

Protein

Multiple epidermal growth factor-like domains protein 10

Gene

Megf10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (16 Aug 2004)
      Previous versions | rss
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    Functioni

    Membrane receptor involved in phagocytosis by macrophages of apoptotic cells. Cooperates with ABCA1 within the process of engulfment. Promotes the formation of large intracellular vacuoles and may be responsible for the uptake of amyloid-beta peptides. May also function in the mosaic spacing of specific neuron subtypes in the retina through homotypic retinal neuron repulsion. Mosaics provide a mechanism to distribute each cell type evenly across the retina, ensuring that all parts of the visual field have access to a full set of processing elements. May play role in cell adhesion and motility. Is also an essential factor in the regulation of myogenesis. Controls the balance between skeletal muscle satellite cells proliferation and differentiation problably through regulation of the notch signaling pathway.3 Publications

    GO - Biological processi

    1. homotypic cell-cell adhesion Source: UniProtKB
    2. muscle cell development Source: UniProtKB
    3. recognition of apoptotic cell Source: MGI
    4. regulation of muscle cell differentiation Source: UniProtKB
    5. regulation of skeletal muscle tissue development Source: Ensembl
    6. skeletal muscle satellite cell activation Source: UniProtKB
    7. skeletal muscle satellite cell differentiation Source: UniProtKB
    8. skeletal muscle satellite cell proliferation Source: UniProtKB

    Keywords - Biological processi

    Cell adhesion, Myogenesis, Phagocytosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Multiple epidermal growth factor-like domains protein 10
    Short name:
    Multiple EGF-like domains protein 10
    Gene namesi
    Name:Megf10
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:2685177. Megf10.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Basolateral cell membrane By similarity; Single-pass type I membrane protein By similarity. Cell projectionphagocytic cup By similarity
    Note: Forms an irregular, mosaic-like adhesion pattern in region of the cell surface that becomes firmely fixed to the substrate. Expressed at the cell surface in clusters around cell corpses during engulfment. During the engulfment of apoptotic thymocytes, recruited at the bottom of the forming phagocytic cup. Colocalizes with ABCA1 in absence of any phagocytic challenge. Does not localize within lamellipodia. Does not localize with MEGF11 By similarity. Enriched at the sites of contact with apoptotic thymocyte cells.By similarity

    GO - Cellular componenti

    1. basolateral plasma membrane Source: UniProtKB-SubCell
    2. cell projection Source: UniProtKB-KW
    3. integral component of membrane Source: UniProtKB-KW
    4. phagocytic cup Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 11471122Multiple epidermal growth factor-like domains protein 10PRO_0000309733Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi34 ↔ 95Sequence Analysis
    Disulfide bondi60 ↔ 69Sequence Analysis
    Disulfide bondi94 ↔ 105Sequence Analysis
    Disulfide bondi109 ↔ 124By similarity
    Disulfide bondi126 ↔ 135By similarity
    Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi148 ↔ 160By similarity
    Disulfide bondi154 ↔ 167By similarity
    Disulfide bondi169 ↔ 178By similarity
    Disulfide bondi191 ↔ 203By similarity
    Disulfide bondi197 ↔ 210By similarity
    Disulfide bondi212 ↔ 221By similarity
    Disulfide bondi234 ↔ 246By similarity
    Disulfide bondi240 ↔ 253By similarity
    Disulfide bondi255 ↔ 264By similarity
    Disulfide bondi281 ↔ 289By similarity
    Disulfide bondi283 ↔ 296By similarity
    Disulfide bondi298 ↔ 307By similarity
    Disulfide bondi320 ↔ 332By similarity
    Disulfide bondi326 ↔ 339By similarity
    Disulfide bondi341 ↔ 350By similarity
    Disulfide bondi409 ↔ 421By similarity
    Disulfide bondi415 ↔ 428By similarity
    Disulfide bondi430 ↔ 439By similarity
    Disulfide bondi456 ↔ 464By similarity
    Disulfide bondi458 ↔ 471By similarity
    Disulfide bondi473 ↔ 482By similarity
    Disulfide bondi495 ↔ 507By similarity
    Glycosylationi496 – 4961N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi501 ↔ 514By similarity
    Disulfide bondi516 ↔ 525By similarity
    Disulfide bondi542 ↔ 550By similarity
    Disulfide bondi544 ↔ 557By similarity
    Disulfide bondi559 ↔ 568By similarity
    Disulfide bondi581 ↔ 593By similarity
    Disulfide bondi587 ↔ 600By similarity
    Disulfide bondi602 ↔ 611By similarity
    Disulfide bondi669 ↔ 681By similarity
    Disulfide bondi675 ↔ 688By similarity
    Disulfide bondi690 ↔ 699By similarity
    Disulfide bondi716 ↔ 724By similarity
    Disulfide bondi718 ↔ 731By similarity
    Disulfide bondi733 ↔ 742By similarity
    Disulfide bondi755 ↔ 767By similarity
    Disulfide bondi761 ↔ 774By similarity
    Disulfide bondi776 ↔ 785By similarity
    Disulfide bondi802 ↔ 810By similarity
    Disulfide bondi804 ↔ 817By similarity
    Disulfide bondi819 ↔ 828By similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues.By similarity
    Ubiquitinated; mono- and polyubiquitinated forms are detected.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ6DIB5.
    PRIDEiQ6DIB5.

    PTM databases

    PhosphoSiteiQ6DIB5.

    Expressioni

    Tissue specificityi

    Expressed in cerebellum (at protein level). Expressed in kidney, stellate cells of the cerebellum and macrophage cell lines.3 Publications

    Developmental stagei

    Expressed in embryo at 15 dpc (at protein level). Expressed in embryo at 8, 10, 11, 13, 14 and 15 dpc.1 Publication

    Gene expression databases

    BgeeiQ6DIB5.
    CleanExiMM_MEGF10.
    GenevestigatoriQ6DIB5.

    Interactioni

    Subunit structurei

    Homopolymer Probable. Interacts with GULP1 and ABCA1. Interacts with AP2M1. Does not interact with MEGF11 By similarity.By similarityCurated

    Structurei

    3D structure databases

    ProteinModelPortaliQ6DIB5.
    SMRiQ6DIB5. Positions 93-833.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 857832ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini879 – 1147269CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei858 – 87821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 10778EMIPROSITE-ProRule annotationAdd
    BLAST
    Domaini101 – 13636EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini144 – 17936EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini187 – 22236EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini230 – 26536EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini278 – 30831EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini316 – 35136EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini405 – 44036EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini453 – 48331EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini491 – 52636EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini539 – 56931EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini577 – 61236EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini665 – 70036EGF-like 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini713 – 74331EGF-like 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini751 – 78636EGF-like 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini799 – 82931EGF-like 15PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 857857Necessary for interaction with AP2M1, self-assembly and formation of the irregular, mosaic-like adhesion patternBy similarityAdd
    BLAST
    Regioni945 – 1147203Necessary for formation of large intracellular vacuolesBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1119 – 114628Ser-richAdd
    BLAST

    Domaini

    The EMI and EGF-like domains work in concert to promote self-assembly.

    Sequence similaritiesi

    Belongs to the MEGF family.Curated
    Contains 15 EGF-like domains.PROSITE-ProRule annotation
    Contains 1 EMI domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG12793.
    GeneTreeiENSGT00730000110380.
    HOGENOMiHOG000294130.
    HOVERGENiHBG108333.
    InParanoidiQ6DIB5.
    OMAiFGCNLTC.
    OrthoDBiEOG72C50D.
    PhylomeDBiQ6DIB5.
    TreeFamiTF332598.

    Family and domain databases

    InterProiIPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR002049. EGF_laminin.
    IPR011489. EMI_domain.
    [Graphical view]
    PfamiPF12661. hEGF. 4 hits.
    PF00053. Laminin_EGF. 5 hits.
    [Graphical view]
    SMARTiSM00181. EGF. 12 hits.
    SM00180. EGF_Lam. 5 hits.
    [Graphical view]
    PROSITEiPS00022. EGF_1. 17 hits.
    PS01186. EGF_2. 17 hits.
    PS50026. EGF_3. 15 hits.
    PS51041. EMI. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q6DIB5-1 [UniParc]FASTAAdd to Basket

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    MAISSSSCLG LICSLLCHWV GTASSLNLED PNVCSHWESY SVTVQESYPH     50
    PFDQIYYTSC TDILNWFKCT RHRISYRTAY RHGEKTMYRR KSQCCPGFYE 100
    SRDMCVPHCA DKCVHGRCIA PNTCQCEPGW GGTNCSSACD GDHWGPHCSS 150
    RCQCKNRALC NPITGACHCA AGYRGWRCED RCEQGTYGND CHQRCQCQNG 200
    ATCDHITGEC RCSPGYTGAF CEDLCPPGKH GPHCEQRCPC QNGGVCHHVT 250
    GECSCPSGWM GTVCGQPCPE GRFGKNCSQE CQCHNGGTCD AATGQCHCSP 300
    GYTGERCQDE CPVGSYGVRC AEACRCVNGG KCYHVSGTCL CEAGFSGELC 350
    EARLCPEGLY GIKCDKRCPC HLDNTHSCHP MSGECGCKPG WSGLYCNETC 400
    SPGFYGEACQ QICSCQNGAD CDSVTGRCAC APGFKGTDCS TPCPLGRYGI 450
    NCSSRCGCKN DAVCSPVDGS CICKAGWHGV DCSIRCPSGT WGFGCNLTCQ 500
    CLNGGACNTL DGTCTCAPGW RGAKCEFPCQ DGTYGLNCAE RCDCSHADGC 550
    HPTTGHCRCL PGWSGVHCDS VCAEGRWGPN CSLPCYCKNG ASCSPDDGIC 600
    ECAPGFRGTT CQRICSPGFY GHRCSQTCPQ CVHSSGPCHH ITGLCDCLPG 650
    FTGALCNEVC PSGRFGKNCA GVCTCTNNGT CNPIDRSCQC YPGWIGSDCS 700
    QPCPPAHWGP NCIHTCNCHN GAFCSAYDGE CKCTPGWTGL YCTQRCPLGF 750
    YGKDCALICQ CQNGADCDHI SGQCTCRTGF MGRHCEQKCP AGTYGYGCRQ 800
    ICDCLNNSTC DHITGTCYCS PGWKGARCDQ AGVIIVGNLN SLSRTSTALP 850
    ADSYQIGAIA GIVVLVLVVL FLLALFIIYR HKQKRKESSM PAVTYTPAMR 900
    VINADYTIAE TLPHSNGGNA NSHYFTNPSY HTLSQCATSP HVNNRDRMTI 950
    AKSKNNQLFV NLKNVNPGKR GTLVDCTGTL PADWKQGGYL NELGAFGLDR 1000
    SYMGKSLKDL GKNSEYNSST CSLSSSENPY ATIKDPPALL PKSSECGYVE 1050
    MKSPARRDSP YAEINNSTPA NRNVYEVEPT VSVVQGVFSN SGHVTQDPYD 1100
    LPKNSHIPCH YDLLPVRDSS SSPKREDGGG SNSTSSNSTS SSSSSSE 1147
    Length:1,147
    Mass (Da):122,972
    Last modified:August 16, 2004 - v1
    Checksum:iFBC50896096181CC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti323 – 3231A → T in BAE38699. (PubMed:16141072)Curated
    Sequence conflicti1092 – 10921G → S in BAE38699. (PubMed:16141072)Curated
    Sequence conflicti1137 – 11371N → S in BAE38699. (PubMed:16141072)Curated
    Sequence conflicti1140 – 11401S → T in BAE38699. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK147238 mRNA. Translation: BAE27788.1.
    AK148084 mRNA. Translation: BAE28336.1.
    AK166316 mRNA. Translation: BAE38699.1.
    BC075647 mRNA. Translation: AAH75647.1.
    CCDSiCCDS29264.1.
    RefSeqiNP_001001979.1. NM_001001979.2.
    UniGeneiMm.297863.

    Genome annotation databases

    EnsembliENSMUST00000075770; ENSMUSP00000075174; ENSMUSG00000024593.
    GeneIDi70417.
    KEGGimmu:70417.
    UCSCiuc008eyz.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK147238 mRNA. Translation: BAE27788.1 .
    AK148084 mRNA. Translation: BAE28336.1 .
    AK166316 mRNA. Translation: BAE38699.1 .
    BC075647 mRNA. Translation: AAH75647.1 .
    CCDSi CCDS29264.1.
    RefSeqi NP_001001979.1. NM_001001979.2.
    UniGenei Mm.297863.

    3D structure databases

    ProteinModelPortali Q6DIB5.
    SMRi Q6DIB5. Positions 93-833.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q6DIB5.

    Proteomic databases

    PaxDbi Q6DIB5.
    PRIDEi Q6DIB5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000075770 ; ENSMUSP00000075174 ; ENSMUSG00000024593 .
    GeneIDi 70417.
    KEGGi mmu:70417.
    UCSCi uc008eyz.2. mouse.

    Organism-specific databases

    CTDi 84466.
    MGIi MGI:2685177. Megf10.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00730000110380.
    HOGENOMi HOG000294130.
    HOVERGENi HBG108333.
    InParanoidi Q6DIB5.
    OMAi FGCNLTC.
    OrthoDBi EOG72C50D.
    PhylomeDBi Q6DIB5.
    TreeFami TF332598.

    Miscellaneous databases

    ChiTaRSi MEGF10. mouse.
    NextBioi 331567.
    PROi Q6DIB5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q6DIB5.
    CleanExi MM_MEGF10.
    Genevestigatori Q6DIB5.

    Family and domain databases

    InterProi IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR002049. EGF_laminin.
    IPR011489. EMI_domain.
    [Graphical view ]
    Pfami PF12661. hEGF. 4 hits.
    PF00053. Laminin_EGF. 5 hits.
    [Graphical view ]
    SMARTi SM00181. EGF. 12 hits.
    SM00180. EGF_Lam. 5 hits.
    [Graphical view ]
    PROSITEi PS00022. EGF_1. 17 hits.
    PS01186. EGF_2. 17 hits.
    PS50026. EGF_3. 15 hits.
    PS51041. EMI. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Strain: C57BL/6J.
      Tissue: Mammary gland.
    2. "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].
      Strain: C57BL/6.
      Tissue: Brain.
    3. "Cooperation between engulfment receptors: the case of ABCA1 and MEGF10."
      Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V., Zhou Z., Chimini G.
      PLoS ONE 1:E120-E120(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    4. "MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin assembly protein complex 2 medium chain and induces large vacuole formation."
      Suzuki E., Nakayama M.
      Exp. Cell Res. 313:3729-3742(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    5. "Megf10 regulates the progression of the satellite cell myogenic program."
      Holterman C.E., Le Grand F., Kuang S., Seale P., Rudnicki M.A.
      J. Cell Biol. 179:911-922(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MYOGENESIS, TISSUE SPECIFICITY.
    6. "MEGF10 functions as a receptor for the uptake of amyloid-beta."
      Singh T.D., Park S.Y., Bae J.S., Yun Y., Bae Y.C., Park R.W., Kim I.S.
      FEBS Lett. 584:3936-3942(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ENDOCYTOSIS.
    7. "MEGF10 and MEGF11 mediate homotypic interactions required for mosaic spacing of retinal neurons."
      Kay J.N., Chu M.W., Sanes J.R.
      Nature 483:465-469(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NEURONAL MOSAIC SPACING.

    Entry informationi

    Entry nameiMEG10_MOUSE
    AccessioniPrimary (citable) accession number: Q6DIB5
    Secondary accession number(s): Q3TLU3, Q3UG73
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 102 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, 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