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O60494

- CUBN_HUMAN

UniProt

O60494 - CUBN_HUMAN

Protein

Cubilin

Gene

CUBN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 5 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    Cotransporter which plays a role in lipoprotein, vitamin and iron metabolism, by facilitating their uptake. Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the GIF-cobalamin complex. The binding of all ligands requires calcium. Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. Interaction with LRP2 mediates its trafficking throughout vesicles and facilitates the uptake of specific ligands like GC, hemoglobin, ALB, TF and SCGB1A1. Interaction with AMN controls its trafficking to the plasma membrane and facilitates endocytosis of ligands. May play an important role in the development of the peri-implantation embryo through internalization of APOA1 and cholesterol. Binds to LGALS3 at the maternal-fetal interface.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei35 – 362Cleavage; by furinSequence Analysis
    Metal bindingi980 – 9801Calcium 1
    Metal bindingi988 – 9881Calcium 1
    Metal bindingi1027 – 10271Calcium 1
    Metal bindingi1029 – 10291Calcium 1
    Metal bindingi1030 – 10301Calcium 1; via carbonyl oxygen
    Metal bindingi1096 – 10961Calcium 2
    Metal bindingi1105 – 11051Calcium 2
    Metal bindingi1146 – 11461Calcium 2
    Metal bindingi1148 – 11481Calcium 2; via carbonyl oxygen
    Metal bindingi1149 – 11491Calcium 2; via carbonyl oxygen
    Metal bindingi1213 – 12131Calcium 3
    Metal bindingi1221 – 12211Calcium 3
    Metal bindingi1262 – 12621Calcium 3
    Metal bindingi1264 – 12641Calcium 3; via carbonyl oxygen
    Metal bindingi1265 – 12651Calcium 3; via carbonyl oxygen
    Metal bindingi1328 – 13281Calcium 4
    Metal bindingi1336 – 13361Calcium 4
    Metal bindingi1373 – 13731Calcium 4
    Metal bindingi1375 – 13751Calcium 4; via carbonyl oxygen

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. cobalamin binding Source: UniProtKB-KW
    3. protein binding Source: UniProt
    4. protein homodimerization activity Source: UniProtKB
    5. receptor activity Source: ProtInc
    6. transporter activity Source: ProtInc

    GO - Biological processi

    1. cholesterol metabolic process Source: UniProtKB-KW
    2. cobalamin metabolic process Source: Reactome
    3. cobalamin transport Source: ProtInc
    4. lipoprotein metabolic process Source: Reactome
    5. lipoprotein transport Source: Ensembl
    6. receptor-mediated endocytosis Source: UniProtKB
    7. small molecule metabolic process Source: Reactome
    8. steroid metabolic process Source: Reactome
    9. tissue homeostasis Source: UniProtKB
    10. vitamin D metabolic process Source: Reactome
    11. vitamin metabolic process Source: Reactome
    12. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Cholesterol metabolism, Endocytosis, Lipid metabolism, Protein transport, Steroid metabolism, Sterol metabolism, Transport

    Keywords - Ligandi

    Calcium, Cobalamin, Cobalt, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_13523. Vitamin D (calciferol) metabolism.
    REACT_13621. HDL-mediated lipid transport.
    REACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.
    REACT_169132. Defective CUBN causes hereditary megaloblastic anemia 1.
    REACT_169280. Defective AMN causes hereditary megaloblastic anemia 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cubilin
    Alternative name(s):
    460 kDa receptor
    Intestinal intrinsic factor receptor
    Intrinsic factor-cobalamin receptor
    Intrinsic factor-vitamin B12 receptor
    Gene namesi
    Name:CUBN
    Synonyms:IFCR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:2548. CUBN.

    Subcellular locationi

    Endosome membrane By similarity; Peripheral membrane protein By similarity. Lysosome membrane By similarity; Peripheral membrane protein By similarity
    Note: Colocalizes with AMN and LRP2 in the endocytotic apparatus of epithelial cells.By similarity

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProt
    2. brush border membrane Source: UniProtKB
    3. coated pit Source: Ensembl
    4. cytosol Source: Reactome
    5. endocytic vesicle Source: UniProt
    6. endoplasmic reticulum Source: Ensembl
    7. endosome membrane Source: Reactome
    8. extracellular vesicular exosome Source: UniProtKB
    9. extrinsic component of external side of plasma membrane Source: UniProtKB
    10. Golgi apparatus Source: Ensembl
    11. lysosomal lumen Source: Reactome
    12. lysosomal membrane Source: UniProtKB-SubCell
    13. membrane Source: ProtInc
    14. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Endosome, Lysosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Recessive hereditary megaloblastic anemia 1 (RH-MGA1) [MIM:261100]: Due to selective malabsorption of vitamin B12. Defects in vitamin B12 absorption lead to impaired function of thymidine synthase. As a consequence DNA synthesis is interrupted. Rapidly dividing cells involved in erythropoiesis are particularly affected.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1297 – 12971P → L in RH-MGA1; decreases strongly the GIF binding affinity. 1 Publication
    Corresponds to variant rs28939699 [ dbSNP | Ensembl ].
    VAR_025288

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi261100. phenotype.
    Orphaneti35858. Grasbeck-Imerslund disease.
    PharmGKBiPA27044.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Propeptidei24 – 3512Removed in mature form1 PublicationPRO_0000046072Add
    BLAST
    Chaini36 – 36233588CubilinPRO_0000046073Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi3 – 31N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi136 ↔ 147By similarity
    Disulfide bondi141 ↔ 156By similarity
    Disulfide bondi158 ↔ 167By similarity
    Disulfide bondi174 ↔ 190By similarity
    Disulfide bondi184 ↔ 199By similarity
    Disulfide bondi201 ↔ 210By similarity
    Disulfide bondi267 ↔ 280By similarity
    Disulfide bondi274 ↔ 289By similarity
    Disulfide bondi292 ↔ 303By similarity
    Disulfide bondi353 ↔ 366By similarity
    Disulfide bondi360 ↔ 376By similarity
    Disulfide bondi399 ↔ 409By similarity
    Disulfide bondi404 ↔ 418By similarity
    Disulfide bondi420 ↔ 429By similarity
    Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi436 ↔ 447By similarity
    Disulfide bondi441 ↔ 456By similarity
    Disulfide bondi458 ↔ 467By similarity
    Disulfide bondi474 ↔ 500By similarity
    Glycosylationi482 – 4821N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi527 ↔ 549By similarity
    Disulfide bondi590 ↔ 616By similarity
    Disulfide bondi643 ↔ 665By similarity
    Disulfide bondi708 ↔ 734By similarity
    Glycosylationi711 – 7111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi749 – 7491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi781 – 7811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi857 – 8571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi869 ↔ 891By similarity
    Disulfide bondi932 ↔ 9581 Publication
    Glycosylationi957 – 9571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi984 – 9841N-linked (GlcNAc...)2 Publications
    Disulfide bondi985 ↔ 10051 Publication
    Disulfide bondi1048 ↔ 10741 Publication
    Glycosylationi1092 – 10921N-linked (GlcNAc...)2 Publications
    Disulfide bondi1165 ↔ 11911 Publication
    Glycosylationi1168 – 11681N-linked (GlcNAc...)2 Publications
    Glycosylationi1217 – 12171N-linked (GlcNAc...)2 Publications
    Disulfide bondi1218 ↔ 12401 Publication
    Disulfide bondi1278 ↔ 13061 Publication
    Glycosylationi1285 – 12851N-linked (GlcNAc...)2 Publications
    Glycosylationi1307 – 13071N-linked (GlcNAc...)2 Publications
    Glycosylationi1319 – 13191N-linked (GlcNAc...)2 Publications
    Glycosylationi1332 – 13321N-linked (GlcNAc...)2 Publications
    Disulfide bondi1333 ↔ 13511 Publication
    Disulfide bondi1391 ↔ 1417By similarity
    Disulfide bondi1444 ↔ 1466By similarity
    Glycosylationi1500 – 15001N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1510 ↔ 1536By similarity
    Glycosylationi1551 – 15511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1563 ↔ 1581By similarity
    Disulfide bondi1620 ↔ 1647By similarity
    Glycosylationi1646 – 16461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1675 ↔ 1697By similarity
    Disulfide bondi1738 ↔ 1764By similarity
    Disulfide bondi1791 ↔ 1812By similarity
    Glycosylationi1802 – 18021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1819 – 18191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1885 – 18851N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1905 ↔ 1927By similarity
    Disulfide bondi1978 ↔ 2006By similarity
    Disulfide bondi2032 ↔ 2054By similarity
    Glycosylationi2085 – 20851N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2092 ↔ 2118By similarity
    Glycosylationi2117 – 21171N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2217 ↔ 2247By similarity
    Glycosylationi2274 – 22741N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2275 ↔ 2297By similarity
    Disulfide bondi2336 ↔ 2363By similarity
    Glycosylationi2386 – 23861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2390 ↔ 2411By similarity
    Glycosylationi2400 – 24001N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2452 ↔ 2478By similarity
    Disulfide bondi2505 ↔ 2527By similarity
    Glycosylationi2531 – 25311N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2570 ↔ 2599By similarity
    Glycosylationi2581 – 25811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2592 – 25921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2610 – 26101N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2628 ↔ 2649By similarity
    Disulfide bondi2689 ↔ 2715By similarity
    Disulfide bondi2742 ↔ 2764By similarity
    Disulfide bondi2805 ↔ 2831By similarity
    Glycosylationi2813 – 28131N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2860 ↔ 2883By similarity
    Disulfide bondi2920 ↔ 2946By similarity
    Glycosylationi2923 – 29231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2945 – 29451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2977 ↔ 2999By similarity
    Modified residuei3008 – 30081PhosphothreonineBy similarity
    Disulfide bondi3037 ↔ 3064By similarity
    Glycosylationi3042 – 30421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3091 ↔ 3113By similarity
    Glycosylationi3103 – 31031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3125 – 31251N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3157 ↔ 3185By similarity
    Glycosylationi3165 – 31651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3215 ↔ 3237By similarity
    Glycosylationi3268 – 32681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3278 ↔ 3306By similarity
    Glycosylationi3283 – 32831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3290 – 32901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3295 – 32951N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3332 ↔ 3354By similarity
    Glycosylationi3357 – 33571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3395 ↔ 3421By similarity
    Glycosylationi3430 – 34301N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3448 ↔ 3470By similarity
    Glycosylationi3457 – 34571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3511 ↔ 3537By similarity
    Glycosylationi3533 – 35331N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3564 ↔ 3586By similarity
    Glycosylationi3576 – 35761N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The precursor is cleaved by a trans-Golgi proteinase furin. The result is a propeptide cleaved off.1 Publication
    N-glycosylated.2 Publications

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiO60494.
    PRIDEiO60494.

    PTM databases

    PhosphoSiteiO60494.

    Expressioni

    Tissue specificityi

    Expressed in kidney proximal tubule cells, placenta, visceral yolk-sac cells and in absorptive intestinal cells. Expressed in the epithelium of intestine and kidney.

    Gene expression databases

    ArrayExpressiO60494.
    BgeeiO60494.
    CleanExiHS_CUBN.
    GenevestigatoriO60494.

    Interactioni

    Subunit structurei

    Interacts with LRP2 in a dual-receptor complex in a calcium-dependent manner. Component of the cubam complex composed of CUBN and AMN. The cubam complex can oligomerize and form cubam trimers. Found in a complex with PID1/PCLI1, LRP1 and CUBNI. Interacts with LRP1 and PID1/PCLI1.6 Publications

    Protein-protein interaction databases

    BioGridi113724. 10 interactions.
    DIPiDIP-58583N.
    IntActiO60494. 1 interaction.
    STRINGi9606.ENSP00000367064.

    Structurei

    Secondary structure

    1
    3623
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi938 – 9425
    Beta strandi959 – 9635
    Beta strandi966 – 9727
    Beta strandi987 – 9937
    Beta strandi997 – 10048
    Beta strandi1016 – 102510
    Beta strandi1038 – 10469
    Beta strandi1048 – 10525
    Turni1062 – 10654
    Beta strandi1073 – 10786
    Beta strandi1087 – 10948
    Beta strandi1104 – 111411
    Beta strandi1119 – 11235
    Beta strandi1125 – 11273
    Beta strandi1135 – 11373
    Beta strandi1139 – 11446
    Beta strandi1153 – 11597
    Beta strandi1171 – 11777
    Turni1179 – 11824
    Beta strandi1190 – 11956
    Beta strandi1203 – 12097
    Beta strandi1220 – 123011
    Beta strandi1233 – 12397
    Beta strandi1251 – 12533
    Beta strandi1255 – 12606
    Beta strandi1271 – 12766
    Beta strandi1279 – 12835
    Beta strandi1287 – 12926
    Turni1294 – 12974
    Beta strandi1305 – 13117
    Beta strandi1319 – 13268
    Turni1331 – 13344
    Beta strandi1335 – 13428
    Beta strandi1345 – 13506
    Beta strandi1362 – 137110
    Beta strandi1381 – 13866

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KQ4X-ray3.30B/D/F932-1388[»]
    ProteinModelPortaliO60494.
    SMRiO60494. Positions 932-1388.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60494.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini132 – 16837EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini170 – 21142EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini263 – 30442EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini305 – 34844EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini349 – 38537EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini395 – 43036EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini432 – 46837EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini474 – 586113CUB 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini590 – 702113CUB 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini708 – 816109CUB 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini816 – 928113CUB 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini932 – 1042111CUB 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1048 – 1161114CUB 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1165 – 1277113CUB 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1278 – 1389112CUB 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1391 – 1506116CUB 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1510 – 1619110CUB 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1620 – 1734115CUB 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1738 – 1850113CUB 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1852 – 1963112CUB 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1978 – 2091114CUB 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini2092 – 2213122CUB 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini2217 – 2334118CUB 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini2336 – 2448113CUB 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini2452 – 2565114CUB 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini2570 – 2687118CUB 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini2689 – 2801113CUB 20PROSITE-ProRule annotationAdd
    BLAST
    Domaini2805 – 2919115CUB 21PROSITE-ProRule annotationAdd
    BLAST
    Domaini2920 – 3035116CUB 22PROSITE-ProRule annotationAdd
    BLAST
    Domaini3037 – 3150114CUB 23PROSITE-ProRule annotationAdd
    BLAST
    Domaini3157 – 3274118CUB 24PROSITE-ProRule annotationAdd
    BLAST
    Domaini3278 – 3393116CUB 25PROSITE-ProRule annotationAdd
    BLAST
    Domaini3395 – 3507113CUB 26PROSITE-ProRule annotationAdd
    BLAST
    Domaini3511 – 3623113CUB 27PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The CUB domains 5 to 8 mediate binding to GIF and ALB. CUB domains 1 and 2 mediate interaction with LRP2.

    Sequence similaritiesi

    Contains 27 CUB domains.PROSITE-ProRule annotation
    Contains 7 EGF-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG287752.
    HOGENOMiHOG000049236.
    HOVERGENiHBG080357.
    InParanoidiO60494.
    KOiK14616.
    OMAiSIQLTIH.
    OrthoDBiEOG741Z18.
    PhylomeDBiO60494.
    TreeFamiTF316224.

    Family and domain databases

    Gene3Di2.60.120.290. 27 hits.
    InterProiIPR000859. CUB_dom.
    IPR028876. Cubilin.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR024731. EGF_dom_MSP1-like.
    IPR009030. Growth_fac_rcpt_N_dom.
    [Graphical view]
    PANTHERiPTHR10127:SF561. PTHR10127:SF561. 1 hit.
    PfamiPF00431. CUB. 27 hits.
    PF00008. EGF. 3 hits.
    PF12947. EGF_3. 1 hit.
    PF07645. EGF_CA. 3 hits.
    [Graphical view]
    SMARTiSM00042. CUB. 27 hits.
    SM00181. EGF. 5 hits.
    SM00179. EGF_CA. 3 hits.
    [Graphical view]
    SUPFAMiSSF49854. SSF49854. 27 hits.
    SSF57184. SSF57184. 1 hit.
    PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
    PS01180. CUB. 27 hits.
    PS00022. EGF_1. 4 hits.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 6 hits.
    PS01187. EGF_CA. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O60494-1 [UniParc]FASTAAdd to Basket

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    MMNMSLPFLW SLLTLLIFAE VNGEAGELEL QRQKRSINLQ QPRMATERGN     50
    LVFLTGSAQN IEFRTGSLGK IKLNDEDLSE CLHQIQKNKE DIIELKGSAI 100
    GLPQNISSQI YQLNSKLVDL ERKFQGLQQT VDKKVCSSNP CQNGGTCLNL 150
    HDSFFCICPP QWKGPLCSAD VNECEIYSGT PLSCQNGGTC VNTMGSYSCH 200
    CPPETYGPQC ASKYDDCEGG SVARCVHGIC EDLMREQAGE PKYSCVCDAG 250
    WMFSPNSPAC TLDRDECSFQ PGPCSTLVQC FNTQGSFYCG ACPTGWQGNG 300
    YICEDINECE INNGGCSVAP PVECVNTPGS SHCQACPPGY QGDGRVCTLT 350
    DICSVSNGGC HPDASCSSTL GSLPLCTCLP GYTGNGYGPN GCVQLSNICL 400
    SHPCLNGQCI DTVSGYFCKC DSGWTGVNCT ENINECLSNP CLNGGTCVDG 450
    VDSFSCECTR LWTGALCQVP QQVCGESLSG INGSFSYRSP DVGYVHDVNC 500
    FWVIKTEMGK VLRITFTFFR LESMDNCPHE FLQVYDGDSS SAFQLGRFCG 550
    SSLPHELLSS DNALYFHLYS EHLRNGRGFT VRWETQQPEC GGILTGPYGS 600
    IKSPGYPGNY PPGRDCVWIV VTSPDLLVTF TFGTLSLEHH DDCNKDYLEI 650
    RDGPLYQDPL LGKFCTTFSV PPLQTTGPFA RIHFHSDSQI SDQGFHITYL 700
    TSPSDLRCGG NYTDPEGELF LPELSGPFTH TRQCVYMMKQ PQGEQIQINF 750
    THVELQCQSD SSQNYIEVRD GETLLGKVCG NGTISHIKSI TNSVWIRFKI 800
    DASVEKASFR AVYQVACGDE LTGEGVIRSP FFPNVYPGER TCRWTIHQPQ 850
    SQVILLNFTV FEIGSSAHCE TDYVEIGSSS ILGSPENKKY CGTDIPSFIT 900
    SVYNFLYVTF VKSSSTENHG FMAKFSAEDL ACGEILTEST GTIQSPGHPN 950
    VYPHGINCTW HILVQPNHLI HLMFETFHLE FHYNCTNDYL EVYDTDSETS 1000
    LGRYCGKSIP PSLTSSGNSL MLVFVTDSDL AYEGFLINYE AISAATACLQ 1050
    DYTDDLGTFT SPNFPNNYPN NWECIYRITV RTGQLIAVHF TNFSLEEAIG 1100
    NYYTDFLEIR DGGYEKSPLL GIFYGSNLPP TIISHSNKLW LKFKSDQIDT 1150
    RSGFSAYWDG SSTGCGGNLT TSSGTFISPN YPMPYYHSSE CYWWLKSSHG 1200
    SAFELEFKDF HLEHHPNCTL DYLAVYDGPS SNSHLLTQLC GDEKPPLIRS 1250
    SGDSMFIKLR TDEGQQGRGF KAEYRQTCEN VVIVNQTYGI LESIGYPNPY 1300
    SENQHCNWTI RATTGNTVNY TFLAFDLEHH INCSTDYLEL YDGPRQMGRY 1350
    CGVDLPPPGS TTSSKLQVLL LTDGVGRREK GFQMQWFVYG CGGELSGATG 1400
    SFSSPGFPNR YPPNKECIWY IRTDPGSSIQ LTIHDFDVEY HSRCNFDVLE 1450
    IYGGPDFHSP RIAQLCTQRS PENPMQVSST GNELAIRFKT DLSINGRGFN 1500
    ASWQAVTGGC GGIFQAPSGE IHSPNYPSPY RSNTDCSWVI RVDRNHRVLL 1550
    NFTDFDLEPQ DSCIMAYDGL SSTMSRLART CGREQLANPI VSSGNSLFLR 1600
    FQSGPSRQNR GFRAQFRQAC GGHILTSSFD TVSSPRFPAN YPNNQNCSWI 1650
    IQAQPPLNHI TLSFTHFELE RSTTCARDFV EILDGGHEDA PLRGRYCGTD 1700
    MPHPITSFSS ALTLRFVSDS SISAGGFHTT VTASVSACGG TFYMAEGIFN 1750
    SPGYPDIYPP NVECVWNIVS SPGNRLQLSF ISFQLEDSQD CSRDFVEIRE 1800
    GNATGHLVGR YCGNSFPLNY SSIVGHTLWV RFISDGSGSG TGFQATFMKI 1850
    FGNDNIVGTH GKVASPFWPE NYPHNSNYQW TVNVNASHVV HGRILEMDIE 1900
    EIQNCYYDKL RIYDGPSIHA RLIGAYCGTQ TESFSSTGNS LTFHFYSDSS 1950
    ISGKGFLLEW FAVDAPDGVL PTIAPGACGG FLRTGDAPVF LFSPGWPDSY 2000
    SNRVDCTWLI QAPDSTVELN ILSLDIESHR TCAYDSLVIR DGDNNLAQQL 2050
    AVLCGREIPG PIRSTGEYMF IRFTSDSSVT RAGFNASFHK SCGGYLHADR 2100
    GIITSPKYPE TYPSNLNCSW HVLVQSGLTI AVHFEQPFQI PNGDSSCNQG 2150
    DYLVLRNGPD ICSPPLGPPG GNGHFCGSHA SSTLFTSDNQ MFVQFISDHS 2200
    NEGQGFKIKY EAKSLACGGN VYIHDADSAG YVTSPNHPHN YPPHADCIWI 2250
    LAAPPETRIQ LQFEDRFDIE VTPNCTSNYL ELRDGVDSDA PILSKFCGTS 2300
    LPSSQWSSGE VMYLRFRSDN SPTHVGFKAK YSIAQCGGRV PGQSGVVESI 2350
    GHPTLPYRDN LFCEWHLQGL SGHYLTISFE DFNLQNSSGC EKDFVEIWDN 2400
    HTSGNILGRY CGNTIPDSID TSSNTAVVRF VTDGSVTASG FRLRFESSME 2450
    ECGGDLQGSI GTFTSPNYPN PNPHGRICEW RITAPEGRRI TLMFNNLRLA 2500
    THPSCNNEHV IVFNGIRSNS PQLEKLCSSV NVSNEIKSSG NTMKVIFFTD 2550
    GSRPYGGFTA SYTSSEDAVC GGSLPNTPEG NFTSPGYDGV RNYSRNLNCE 2600
    WTLSNPNQGN SSISIHFEDF YLESHQDCQF DVLEFRVGDA DGPLMWRLCG 2650
    PSKPTLPLVI PYSQVWIHFV TNERVEHIGF HAKYSFTDCG GIQIGDSGVI 2700
    TSPNYPNAYD SLTHCSSLLE APQGHTITLT FSDFDIEPHT TCAWDSVTVR 2750
    NGGSPESPII GQYCGNSNPR TIQSGSNQLV VTFNSDHSLQ GGGFYATWNT 2800
    QTLGCGGIFH SDNGTIRSPH WPQNFPENSR CSWTAITHKS KHLEISFDNN 2850
    FLIPSGDGQC QNSFVKVWAG TEEVDKALLA TGCGNVAPGP VITPSNTFTA 2900
    VFQSQEAPAQ GFSASFVSRC GSNFTGPSGY IISPNYPKQY DNNMNCTYVI 2950
    EANPLSVVLL TFVSFHLEAR SAVTGSCVND GVHIIRGYSV MSTPFATVCG 3000
    DEMPAPLTIA GPVLLNFYSN EQITDFGFKF SYRIISCGGV FNFSSGIITS 3050
    PAYSYADYPN DMHCLYTITV SDDKVIELKF SDFDVVPSTS CSHDYLAIYD 3100
    GANTSDPLLG KFCGSKRPPN VKSSNNSMLL VFKTDSFQTA KGWKMSFRQT 3150
    LGPQQGCGGY LTGSNNTFAS PDSDSNGMYD KNLNCVWIII APVNKVIHLT 3200
    FNTFALEAAS TRQRCLYDYV KLYDGDSENA NLAGTFCGST VPAPFISSGN 3250
    FLTVQFISDL TLEREGFNAT YTIMDMPCGG TYNATWTPQN ISSPNSSDPD 3300
    VPFSICTWVI DSPPHQQVKI TVWALQLTSQ DCTQNYLQLQ DSPQGHGNSR 3350
    FQFCGRNASA VPVFYSSMST AMVIFKSGVV NRNSRMSFTY QIADCNRDYH 3400
    KAFGNLRSPG WPDNYDNDKD CTVTLTAPQN HTISLFFHSL GIENSVECRN 3450
    DFLEVRNGSN SNSPLLGKYC GTLLPNPVFS QNNELYLRFK SDSVTSDRGY 3500
    EIIWTSSPSG CGGTLYGDRG SFTSPGYPGT YPNNTYCEWV LVAPAGRLVT 3550
    INFYFISIDD PGDCVQNYLT LYDGPNASSP SSGPYCGGDT SIAPFVASSN 3600
    QVFIKFHADY ARRPSAFRLT WDS 3623
    Length:3,623
    Mass (Da):398,736
    Last modified:November 2, 2010 - v5
    Checksum:i8D602663C6D4751F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251A → R in AAC82612. (PubMed:9572993)Curated
    Sequence conflicti146 – 1461T → N in AAC82612. (PubMed:9572993)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti66 – 661G → R.
    Corresponds to variant rs12259370 [ dbSNP | Ensembl ].
    VAR_047443
    Natural varianti124 – 1241F → I.1 Publication
    Corresponds to variant rs1801220 [ dbSNP | Ensembl ].
    VAR_025284
    Natural varianti253 – 2531F → S.2 Publications
    Corresponds to variant rs1801222 [ dbSNP | Ensembl ].
    VAR_025285
    Natural varianti335 – 3351A → T.
    Corresponds to variant rs57335729 [ dbSNP | Ensembl ].
    VAR_061154
    Natural varianti389 – 3891P → T.1 Publication
    Corresponds to variant rs1801224 [ dbSNP | Ensembl ].
    VAR_025286
    Natural varianti504 – 5041I → M.
    Corresponds to variant rs2228053 [ dbSNP | Ensembl ].
    VAR_047444
    Natural varianti730 – 7301H → Y.
    Corresponds to variant rs7905349 [ dbSNP | Ensembl ].
    VAR_047445
    Natural varianti786 – 7861H → Q in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035829
    Natural varianti969 – 9691L → V.
    Corresponds to variant rs11254354 [ dbSNP | Ensembl ].
    VAR_047446
    Natural varianti1032 – 10321Y → H.1 Publication
    Corresponds to variant rs1801227 [ dbSNP | Ensembl ].
    VAR_025287
    Natural varianti1297 – 12971P → L in RH-MGA1; decreases strongly the GIF binding affinity. 1 Publication
    Corresponds to variant rs28939699 [ dbSNP | Ensembl ].
    VAR_025288
    Natural varianti1545 – 15451N → Y.2 Publications
    VAR_025289
    Natural varianti1559 – 15591P → S.1 Publication
    Corresponds to variant rs1801231 [ dbSNP | Ensembl ].
    VAR_025290
    Natural varianti1769 – 17691V → I.2 Publications
    Corresponds to variant rs74116778 [ dbSNP | Ensembl ].
    VAR_025291
    Natural varianti1775 – 17751R → W.
    Corresponds to variant rs1276708 [ dbSNP | Ensembl ].
    VAR_047447
    Natural varianti1840 – 18401G → S.
    Corresponds to variant rs2271462 [ dbSNP | Ensembl ].
    VAR_047448
    Natural varianti1935 – 19351S → G.
    Corresponds to variant rs41289305 [ dbSNP | Ensembl ].
    VAR_047449
    Natural varianti1971 – 19711P → T.
    Corresponds to variant rs2356590 [ dbSNP | Ensembl ].
    VAR_047450
    Natural varianti2153 – 21531L → F.1 Publication
    Corresponds to variant rs62619939 [ dbSNP | Ensembl ].
    VAR_025292
    Natural varianti2162 – 21621C → Y.1 Publication
    Corresponds to variant rs1276712 [ dbSNP | Ensembl ].
    VAR_025293
    Natural varianti2252 – 22521A → V in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035830
    Natural varianti2263 – 22631F → C.
    Corresponds to variant rs2271460 [ dbSNP | Ensembl ].
    VAR_047451
    Natural varianti2444 – 24441R → Q.
    Corresponds to variant rs11254274 [ dbSNP | Ensembl ].
    VAR_047452
    Natural varianti2575 – 25751P → R.1 Publication
    Corresponds to variant rs3740168 [ dbSNP | Ensembl ].
    VAR_025294
    Natural varianti2691 – 26911G → R.1 Publication
    Corresponds to variant rs1801237 [ dbSNP | Ensembl ].
    VAR_025295
    Natural varianti2717 – 27171S → W.1 Publication
    Corresponds to variant rs2796835 [ dbSNP | Ensembl ].
    VAR_025296
    Natural varianti2879 – 28791L → I.1 Publication
    Corresponds to variant rs45474496 [ dbSNP | Ensembl ].
    VAR_025297
    Natural varianti2914 – 29141A → V in a breast cancer sample; somatic mutation. 1 Publication
    Corresponds to variant rs45551835 [ dbSNP | Ensembl ].
    VAR_035831
    Natural varianti2968 – 29681E → Q.
    Corresponds to variant rs45569534 [ dbSNP | Ensembl ].
    VAR_047453
    Natural varianti2984 – 29841I → V.1 Publication
    Corresponds to variant rs1801239 [ dbSNP | Ensembl ].
    VAR_025298
    Natural varianti3002 – 30021E → G.1 Publication
    Corresponds to variant rs1801240 [ dbSNP | Ensembl ].
    VAR_025299
    Natural varianti3189 – 31891I → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035832
    Natural varianti3258 – 32581S → G Found in a renal cell carcinoma case; somatic mutation. 1 Publication
    VAR_064704
    Natural varianti3422 – 34221T → I.1 Publication
    Corresponds to variant rs1801230 [ dbSNP | Ensembl ].
    VAR_025300
    Natural varianti3432 – 34321T → S.
    Corresponds to variant rs7898873 [ dbSNP | Ensembl ].
    VAR_055714
    Natural varianti3552 – 35521N → K.1 Publication
    Corresponds to variant rs1801232 [ dbSNP | Ensembl ].
    VAR_025301

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF034611 mRNA. Translation: AAC82612.1.
    EF444970 Genomic DNA. Translation: ACA05973.1.
    EF444970 Genomic DNA. Translation: ACA05974.1.
    AL596445
    , AL365215, AC067747, AL731551 Genomic DNA. Translation: CAH72450.1.
    AL365215
    , AL596445, AC067747, AL731551 Genomic DNA. Translation: CAH73630.1.
    AL731551
    , AL365215, AL596445, AC067747 Genomic DNA. Translation: CAI40246.1.
    CCDSiCCDS7113.1.
    PIRiT09456.
    RefSeqiNP_001072.2. NM_001081.3.
    UniGeneiHs.166206.

    Genome annotation databases

    EnsembliENST00000377833; ENSP00000367064; ENSG00000107611.
    GeneIDi8029.
    KEGGihsa:8029.
    UCSCiuc001ioo.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF034611 mRNA. Translation: AAC82612.1 .
    EF444970 Genomic DNA. Translation: ACA05973.1 .
    EF444970 Genomic DNA. Translation: ACA05974.1 .
    AL596445
    , AL365215 , AC067747 , AL731551 Genomic DNA. Translation: CAH72450.1 .
    AL365215
    , AL596445 , AC067747 , AL731551 Genomic DNA. Translation: CAH73630.1 .
    AL731551
    , AL365215 , AL596445 , AC067747 Genomic DNA. Translation: CAI40246.1 .
    CCDSi CCDS7113.1.
    PIRi T09456.
    RefSeqi NP_001072.2. NM_001081.3.
    UniGenei Hs.166206.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3KQ4 X-ray 3.30 B/D/F 932-1388 [» ]
    ProteinModelPortali O60494.
    SMRi O60494. Positions 932-1388.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113724. 10 interactions.
    DIPi DIP-58583N.
    IntActi O60494. 1 interaction.
    STRINGi 9606.ENSP00000367064.

    Chemistry

    DrugBanki DB00115. Cyanocobalamin.
    DB00200. Hydroxocobalamin.

    PTM databases

    PhosphoSitei O60494.

    Proteomic databases

    PaxDbi O60494.
    PRIDEi O60494.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377833 ; ENSP00000367064 ; ENSG00000107611 .
    GeneIDi 8029.
    KEGGi hsa:8029.
    UCSCi uc001ioo.3. human.

    Organism-specific databases

    CTDi 8029.
    GeneCardsi GC10M016906.
    H-InvDB HIX0035313.
    HIX0035577.
    HGNCi HGNC:2548. CUBN.
    MIMi 261100. phenotype.
    602997. gene.
    neXtProti NX_O60494.
    Orphaneti 35858. Grasbeck-Imerslund disease.
    PharmGKBi PA27044.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG287752.
    HOGENOMi HOG000049236.
    HOVERGENi HBG080357.
    InParanoidi O60494.
    KOi K14616.
    OMAi SIQLTIH.
    OrthoDBi EOG741Z18.
    PhylomeDBi O60494.
    TreeFami TF316224.

    Enzyme and pathway databases

    Reactomei REACT_13523. Vitamin D (calciferol) metabolism.
    REACT_13621. HDL-mediated lipid transport.
    REACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.
    REACT_169132. Defective CUBN causes hereditary megaloblastic anemia 1.
    REACT_169280. Defective AMN causes hereditary megaloblastic anemia 1.

    Miscellaneous databases

    EvolutionaryTracei O60494.
    GeneWikii Cubilin.
    GenomeRNAii 8029.
    NextBioi 30607.
    PROi O60494.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60494.
    Bgeei O60494.
    CleanExi HS_CUBN.
    Genevestigatori O60494.

    Family and domain databases

    Gene3Di 2.60.120.290. 27 hits.
    InterProi IPR000859. CUB_dom.
    IPR028876. Cubilin.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR024731. EGF_dom_MSP1-like.
    IPR009030. Growth_fac_rcpt_N_dom.
    [Graphical view ]
    PANTHERi PTHR10127:SF561. PTHR10127:SF561. 1 hit.
    Pfami PF00431. CUB. 27 hits.
    PF00008. EGF. 3 hits.
    PF12947. EGF_3. 1 hit.
    PF07645. EGF_CA. 3 hits.
    [Graphical view ]
    SMARTi SM00042. CUB. 27 hits.
    SM00181. EGF. 5 hits.
    SM00179. EGF_CA. 3 hits.
    [Graphical view ]
    SUPFAMi SSF49854. SSF49854. 27 hits.
    SSF57184. SSF57184. 1 hit.
    PROSITEi PS00010. ASX_HYDROXYL. 4 hits.
    PS01180. CUB. 27 hits.
    PS00022. EGF_1. 4 hits.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 6 hits.
    PS01187. EGF_CA. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human intrinsic factor-vitamin B12 receptor, cubilin: molecular characterization and chromosomal mapping of the gene to 10p within the autosomal recessive megaloblastic anemia (MGA1) region."
      Kozyraki R., Kristiansen M., Silahtaroglu A., Hansen C., Jacobsen C., Tommerup N., Verroust P.J., Moestrup S.K.
      Blood 91:3593-3600(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-41, FUNCTION, BINDING TO THE GIF-COBALAMIN COMPLEX, PROTEOLYTIC PROCESSING, VARIANTS SER-253; TYR-1545; ILE-1769; TYR-2162 AND TRP-2717.
    2. NHLBI resequencing and genotyping service (RS&G)
      Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The intrinsic factor-vitamin B12 receptor, cubilin, is a high-affinity apolipoprotein A-I receptor facilitating endocytosis of high-density lipoprotein."
      Kozyraki R., Fyfe J., Kristiansen M., Gerdes C., Jacobsen C., Cui S., Christensen E.I., Aminoff M., de la Chapelle A., Krahe R., Verroust P.J., Moestrup S.K.
      Nat. Med. 5:656-661(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APOA1, FUNCTION.
    5. Cited for: INTERACTION WITH GC, FUNCTION.
    6. "Megalin-dependent cubilin-mediated endocytosis is a major pathway for the apical uptake of transferrin in polarized epithelia."
      Kozyraki R., Fyfe J., Verroust P.J., Jacobsen C., Dautry-Varsat A., Gburek J., Willnow T.E., Christensen E.I., Moestrup S.K.
      Proc. Natl. Acad. Sci. U.S.A. 98:12491-12496(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TF, FUNCTION.
    7. "The functional cobalamin (vitamin B12)-intrinsic factor receptor is a novel complex of cubilin and amnionless."
      Fyfe J.C., Madsen M., Hoejrup P., Christensen E.I., Tanner S.M., de la Chapelle A., He Q., Moestrup S.K.
      Blood 103:1573-1579(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AMN, GLYCOSYLATION, FUNCTION.
    8. "Identification of the ligands of protein interaction domains through a functional approach."
      Caratu G., Allegra D., Bimonte M., Schiattarella G.G., D'Ambrosio C., Scaloni A., Napolitano M., Russo T., Zambrano N.
      Mol. Cell. Proteomics 6:333-345(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH LRP1 AND PID1, INTERACTION WITH LRP1 AND PID1.
    9. "Structural basis for receptor recognition of vitamin-B(12)-intrinsic factor complexes."
      Andersen C.B., Madsen M., Storm T., Moestrup S.K., Andersen G.R.
      Nature 464:445-448(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 932-1388 IN COMPLEX WITH GIF AND CALCIUM IONS, INTERACTION WITH GIF, IDENTIFICATION IN CUBAM COMPLEX, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-984; ASN-1092; ASN-1168; ASN-1217; ASN-1285; ASN-1307; ASN-1319 AND ASN-1332.
    10. "Mutations in CUBN, encoding the intrinsic factor-vitamin B12 receptor, cubilin, cause hereditary megaloblastic anaemia 1."
      Aminoff M., Carter J.E., Chadwick R.B., Johnson C., Graesbeck R., Abdelaal M.A., Broch H., Jenner L.B., Verroust P.J., Moestrup S.K., de la Chapelle A., Krahe R.
      Nat. Genet. 21:309-313(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RH-MGA1 LEU-1297, VARIANTS ILE-124; SER-253; THR-389; HIS-1032; TYR-1545; SER-1559; ILE-1769; PHE-2153; ARG-2575; ARG-2691; ILE-2879; VAL-2984; GLY-3002; ILE-3422 AND LYS-3552.
    11. "Cubilin P1297L mutation associated with hereditary megaloblastic anemia 1 causes impaired recognition of intrinsic factor-vitamin B(12) by cubilin."
      Kristiansen M., Aminoff M., Jacobsen C., de La Chapelle A., Krahe R., Verroust P.J., Moestrup S.K.
      Blood 96:405-409(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT RH-MGA1 LEU-1297.
    12. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-786; VAL-2252; VAL-2914 AND VAL-3189.
    13. Cited for: VARIANT GLY-3258.

    Entry informationi

    Entry nameiCUBN_HUMAN
    AccessioniPrimary (citable) accession number: O60494
    Secondary accession number(s): B0YIZ4, Q5VTA6, Q96RU9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 7, 2006
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 132 of the entry and version 5 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3