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Q96KG7

- MEG10_HUMAN

UniProt

Q96KG7 - MEG10_HUMAN

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Protein

Multiple epidermal growth factor-like domains protein 10

Gene

MEGF10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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.4 Publications

GO - Biological processi

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

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
Synonyms:KIAA1780
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:29634. MEGF10.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein. Basolateral cell membrane; Single-pass type I membrane protein. Cell projectionphagocytic cup
Note: Enriched at the sites of contact with apoptotic thymocyte cells (By similarity). 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 857832ExtracellularSequence AnalysisAdd
BLAST
Transmembranei858 – 87821HelicalSequence AnalysisAdd
BLAST
Topological domaini879 – 1140262CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. phagocytic cup Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Involvement in diseasei

Myopathy, early-onset, areflexia, respiratory distress, and dysphagia (EMARDD) [MIM:614399]: An autosomal recessive congenital myopathy characterized by onset at birth, or early in infancy, of respiratory distress caused by diaphragmatic weakness. Additional features are dysphagia resulting in poor feeding, failure to thrive, poor head control, facial weakness, cleft palate, contractures and scoliosis. Affected individuals become ventilator-dependent, and most require feeding by gastrostomy. The disorder results in severe muscle weakness and most patients never achieve walking. Death from respiratory failure in childhood occurs in about half of patients. Muscle biopsies from affected individuals show myopathic changes, replacement of myofibers with fatty tissue, small and incompletely fused muscle fibers, and variation in fiber size. Short regions of sarcomeric disorganization with few or no mitochondria (minicores) have been observed in some cases.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti71 – 711R → W in a patient with EMARDD; unknown pathological significance. 1 Publication
VAR_067469
Natural varianti326 – 3261C → R in EMARDD. 1 Publication
VAR_067470
Natural varianti774 – 7741C → R in EMARDD. 2 Publications
VAR_067471

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi927 – 9271N → A: Does not interact with GULP1; when associated with A-930. 1 Publication
Mutagenesisi930 – 9301Y → A: Does not interact with GULP1; when associated with A-927. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614399. phenotype.
Orphaneti98920. Spinal muscular atrophy with respiratory distress type 1.
PharmGKBiPA144596410.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 11401115Multiple epidermal growth factor-like domains protein 10PRO_0000309732Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 95Sequence Analysis
Disulfide bondi60 ↔ 69Sequence Analysis
Disulfide bondi94 ↔ 105Sequence Analysis
Disulfide bondi109 ↔ 118By similarity
Disulfide bondi113 ↔ 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.1 Publication
Ubiquitinated; mono- and polyubiquitinated forms are detected.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ96KG7.
PRIDEiQ96KG7.

PTM databases

PhosphoSiteiQ96KG7.

Expressioni

Gene expression databases

BgeeiQ96KG7.
CleanExiHS_MEGF10.
GenevestigatoriQ96KG7.

Organism-specific databases

HPAiHPA026876.

Interactioni

Subunit structurei

Homopolymer (Probable). Interacts with GULP1 and ABCA1. Interacts with AP2M1. Does not interact with MEGF11.3 PublicationsCurated

Protein-protein interaction databases

BioGridi124099. 5 interactions.
IntActiQ96KG7. 24 interactions.
STRINGi9606.ENSP00000274473.

Structurei

3D structure databases

ProteinModelPortaliQ96KG7.
SMRiQ96KG7. Positions 124-833.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 10778EMIPROSITE-ProRule annotationAdd
BLAST
Domaini106 – 13631EGF-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 patternAdd
BLAST
Regioni945 – 1140196Necessary for formation of large intracellular vacuolesAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1119 – 113921Ser-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.
InParanoidiQ96KG7.
OMAiFGCNLTC.
OrthoDBiEOG72C50D.
PhylomeDBiQ96KG7.
TreeFamiTF332598.

Family and domain databases

InterProiIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR011489. EMI_domain.
[Graphical view]
PfamiPF12661. hEGF. 3 hits.
PF00053. Laminin_EGF. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 11 hits.
SM00180. EGF_Lam. 6 hits.
[Graphical view]
PROSITEiPS00022. EGF_1. 17 hits.
PS01186. EGF_2. 17 hits.
PS50026. EGF_3. 15 hits.
PS51041. EMI. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96KG7-1) [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

        10         20         30         40         50
MVISLNSCLS FICLLLCHWI GTASPLNLED PNVCSHWESY SVTVQESYPH
60 70 80 90 100
PFDQIYYTSC TDILNWFKCT RHRVSYRTAY RHGEKTMYRR KSQCCPGFYE
110 120 130 140 150
SGEMCVPHCA DKCVHGRCIA PNTCQCEPGW GGTNCSSACD GDHWGPHCTS
160 170 180 190 200
RCQCKNGALC NPITGACHCA AGFRGWRCED RCEQGTYGND CHQRCQCQNG
210 220 230 240 250
ATCDHVTGEC RCPPGYTGAF CEDLCPPGKH GPQCEQRCPC QNGGVCHHVT
260 270 280 290 300
GECSCPSGWM GTVCGQPCPE GRFGKNCSQE CQCHNGGTCD AATGQCHCSP
310 320 330 340 350
GYTGERCQDE CPVGTYGVLC AETCQCVNGG KCYHVSGACL CEAGFAGERC
360 370 380 390 400
EARLCPEGLY GIKCDKRCPC HLENTHSCHP MSGECACKPG WSGLYCNETC
410 420 430 440 450
SPGFYGEACQ QICSCQNGAD CDSVTGKCTC APGFKGIDCS TPCPLGTYGI
460 470 480 490 500
NCSSRCGCKN DAVCSPVDGS CTCKAGWHGV DCSIRCPSGT WGFGCNLTCQ
510 520 530 540 550
CLNGGACNTL DGTCTCAPGW RGEKCELPCQ DGTYGLNCAE RCDCSHADGC
560 570 580 590 600
HPTTGHCRCL PGWSGVHCDS VCAEGRWGPN CSLPCYCKNG ASCSPDDGIC
610 620 630 640 650
ECAPGFRGTT CQRICSPGFY GHRCSQTCPQ CVHSSGPCHH ITGLCDCLPG
660 670 680 690 700
FTGALCNEVC PSGRFGKNCA GICTCTNNGT CNPIDRSCQC YPGWIGSDCS
710 720 730 740 750
QPCPPAHWGP NCIHTCNCHN GAFCSAYDGE CKCTPGWTGL YCTQRCPLGF
760 770 780 790 800
YGKDCALICQ CQNGADCDHI SGQCTCRTGF MGRHCEQKCP SGTYGYGCRQ
810 820 830 840 850
ICDCLNNSTC DHITGTCYCS PGWKGARCDQ AGVIIVGNLN SLSRTSTALP
860 870 880 890 900
ADSYQIGAIA GIIILVLVVL FLLALFIIYR HKQKGKESSM PAVTYTPAMR
910 920 930 940 950
VVNADYTISG TLPHSNGGNA NSHYFTNPSY HTLTQCATSP HVNNRDRMTV
960 970 980 990 1000
TKSKNNQLFV NLKNVNPGKR GPVGDCTGTL PADWKHGGYL NELGAFGLDR
1010 1020 1030 1040 1050
SYMGKSLKDL GKNSEYNSSN CSLSSSENPY ATIKDPPVLI PKSSECGYVE
1060 1070 1080 1090 1100
MKSPARRDSP YAEINNSTSA NRNVYEVEPT VSVVQGVFSN NGRLSQDPYD
1110 1120 1130 1140
LPKNSHIPCH YDLLPVRDSS SSPKQEDSGG SSSNSSSSSE
Length:1,140
Mass (Da):122,205
Last modified:December 1, 2001 - v1
Checksum:i45B2FA239423895A
GO
Isoform 2 (identifier: Q96KG7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     566-567: VH → LF
     568-1140: Missing.

Note: No experimental confirmation available.

Show »
Length:567
Mass (Da):60,797
Checksum:iCF2FB8CDEB7CF627
GO

Sequence cautioni

The sequence BAB47409.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti543 – 5431D → G in CAH18275. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti71 – 711R → W in a patient with EMARDD; unknown pathological significance. 1 Publication
VAR_067469
Natural varianti206 – 2061V → I.
Corresponds to variant rs3812054 [ dbSNP | Ensembl ].
VAR_036988
Natural varianti326 – 3261C → R in EMARDD. 1 Publication
VAR_067470
Natural varianti774 – 7741C → R in EMARDD. 2 Publications
VAR_067471
Natural varianti897 – 8971P → L.
Corresponds to variant rs13183625 [ dbSNP | Ensembl ].
VAR_046377
Natural varianti1072 – 10721R → K.
Corresponds to variant rs17164935 [ dbSNP | Ensembl ].
VAR_036989

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei566 – 5672VH → LF in isoform 2. 1 PublicationVSP_029244
Alternative sequencei568 – 1140573Missing in isoform 2. 1 PublicationVSP_029245Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB058676 mRNA. Translation: BAB47409.2. Different initiation.
CR749437 mRNA. Translation: CAH18275.1.
CH471062 Genomic DNA. Translation: EAW62406.1.
BC020198 mRNA. Translation: AAH20198.1.
BC152478 mRNA. Translation: AAI52479.1.
CCDSiCCDS4142.1. [Q96KG7-1]
RefSeqiNP_001243474.1. NM_001256545.1. [Q96KG7-1]
NP_115822.1. NM_032446.2. [Q96KG7-1]
UniGeneiHs.438709.

Genome annotation databases

EnsembliENST00000274473; ENSP00000274473; ENSG00000145794. [Q96KG7-1]
ENST00000418761; ENSP00000416284; ENSG00000145794. [Q96KG7-2]
ENST00000503335; ENSP00000423354; ENSG00000145794. [Q96KG7-1]
ENST00000508365; ENSP00000423195; ENSG00000145794. [Q96KG7-2]
GeneIDi84466.
KEGGihsa:84466.
UCSCiuc003kuh.4. human. [Q96KG7-1]
uc010jdc.1. human. [Q96KG7-2]

Polymorphism databases

DMDMi74716908.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB058676 mRNA. Translation: BAB47409.2 . Different initiation.
CR749437 mRNA. Translation: CAH18275.1 .
CH471062 Genomic DNA. Translation: EAW62406.1 .
BC020198 mRNA. Translation: AAH20198.1 .
BC152478 mRNA. Translation: AAI52479.1 .
CCDSi CCDS4142.1. [Q96KG7-1 ]
RefSeqi NP_001243474.1. NM_001256545.1. [Q96KG7-1 ]
NP_115822.1. NM_032446.2. [Q96KG7-1 ]
UniGenei Hs.438709.

3D structure databases

ProteinModelPortali Q96KG7.
SMRi Q96KG7. Positions 124-833.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124099. 5 interactions.
IntActi Q96KG7. 24 interactions.
STRINGi 9606.ENSP00000274473.

PTM databases

PhosphoSitei Q96KG7.

Polymorphism databases

DMDMi 74716908.

Proteomic databases

PaxDbi Q96KG7.
PRIDEi Q96KG7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000274473 ; ENSP00000274473 ; ENSG00000145794 . [Q96KG7-1 ]
ENST00000418761 ; ENSP00000416284 ; ENSG00000145794 . [Q96KG7-2 ]
ENST00000503335 ; ENSP00000423354 ; ENSG00000145794 . [Q96KG7-1 ]
ENST00000508365 ; ENSP00000423195 ; ENSG00000145794 . [Q96KG7-2 ]
GeneIDi 84466.
KEGGi hsa:84466.
UCSCi uc003kuh.4. human. [Q96KG7-1 ]
uc010jdc.1. human. [Q96KG7-2 ]

Organism-specific databases

CTDi 84466.
GeneCardsi GC05P126654.
HGNCi HGNC:29634. MEGF10.
HPAi HPA026876.
MIMi 612453. gene.
614399. phenotype.
neXtProti NX_Q96KG7.
Orphaneti 98920. Spinal muscular atrophy with respiratory distress type 1.
PharmGKBi PA144596410.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00730000110380.
HOGENOMi HOG000294130.
HOVERGENi HBG108333.
InParanoidi Q96KG7.
OMAi FGCNLTC.
OrthoDBi EOG72C50D.
PhylomeDBi Q96KG7.
TreeFami TF332598.

Miscellaneous databases

GeneWikii MEGF10.
GenomeRNAii 84466.
NextBioi 74274.
PROi Q96KG7.
SOURCEi Search...

Gene expression databases

Bgeei Q96KG7.
CleanExi HS_MEGF10.
Genevestigatori Q96KG7.

Family and domain databases

InterProi IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR011489. EMI_domain.
[Graphical view ]
Pfami PF12661. hEGF. 3 hits.
PF00053. Laminin_EGF. 4 hits.
[Graphical view ]
SMARTi SM00181. EGF. 11 hits.
SM00180. EGF_Lam. 6 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

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
    DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Retina.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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).
    Tissue: Muscle.
  5. "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: INTERACTION WITH GULP1 AND ABCA1, MUTAGENESIS OF ASN-927 AND TYR-930, SUBCELLULAR LOCATION.
  6. "The mammalian Ced-1 ortholog MEGF10/KIAA1780 displays a novel adhesion pattern."
    Suzuki E., Nakayama M.
    Exp. Cell Res. 313:2451-2464(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "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: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH AP2M1 AND GULP1, PHOSPHORYLATION, UBIQUITINATION.
  8. "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.
  9. Cited for: FUNCTION IN MYOGENESIS, VARIANT EMARDD ARG-774.
  10. Cited for: VARIANTS EMARDD ARG-326 AND ARG-774, VARIANT TRP-71.

Entry informationi

Entry nameiMEG10_HUMAN
AccessioniPrimary (citable) accession number: Q96KG7
Secondary accession number(s): Q68DE5, Q8WUL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: December 1, 2001
Last modified: November 26, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3