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O60494

- CUBN_HUMAN

UniProt

O60494 - CUBN_HUMAN

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Protein

Cubilin

Gene

CUBN

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

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 homodimerization activity Source: UniProtKB
  4. receptor activity Source: ProtInc
  5. 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
Complete GO annotation...

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. membrane Source: ProtInc
  13. plasma membrane Source: Reactome
Complete GO annotation...

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...)1 Publication
Disulfide bondi985 ↔ 10051 Publication
Disulfide bondi1048 ↔ 10741 Publication
Glycosylationi1092 – 10921N-linked (GlcNAc...)1 Publication
Disulfide bondi1165 ↔ 11911 Publication
Glycosylationi1168 – 11681N-linked (GlcNAc...)1 Publication
Glycosylationi1217 – 12171N-linked (GlcNAc...)1 Publication
Disulfide bondi1218 ↔ 12401 Publication
Disulfide bondi1278 ↔ 13061 Publication
Glycosylationi1285 – 12851N-linked (GlcNAc...)1 Publication
Glycosylationi1307 – 13071N-linked (GlcNAc...)1 Publication
Glycosylationi1319 – 13191N-linked (GlcNAc...)1 Publication
Glycosylationi1332 – 13321N-linked (GlcNAc...)1 Publication
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

BgeeiO60494.
CleanExiHS_CUBN.
ExpressionAtlasiO60494. baseline and differential.
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 – 9425Combined sources
Beta strandi959 – 9635Combined sources
Beta strandi966 – 9727Combined sources
Beta strandi987 – 9937Combined sources
Beta strandi997 – 10048Combined sources
Beta strandi1016 – 102510Combined sources
Beta strandi1038 – 10469Combined sources
Beta strandi1048 – 10525Combined sources
Turni1062 – 10654Combined sources
Beta strandi1073 – 10786Combined sources
Beta strandi1087 – 10948Combined sources
Beta strandi1104 – 111411Combined sources
Beta strandi1119 – 11235Combined sources
Beta strandi1125 – 11273Combined sources
Beta strandi1135 – 11373Combined sources
Beta strandi1139 – 11446Combined sources
Beta strandi1153 – 11597Combined sources
Beta strandi1171 – 11777Combined sources
Turni1179 – 11824Combined sources
Beta strandi1190 – 11956Combined sources
Beta strandi1203 – 12097Combined sources
Beta strandi1220 – 123011Combined sources
Beta strandi1233 – 12397Combined sources
Beta strandi1251 – 12533Combined sources
Beta strandi1255 – 12606Combined sources
Beta strandi1271 – 12766Combined sources
Beta strandi1279 – 12835Combined sources
Beta strandi1287 – 12926Combined sources
Turni1294 – 12974Combined sources
Beta strandi1305 – 13117Combined sources
Beta strandi1319 – 13268Combined sources
Turni1331 – 13344Combined sources
Beta strandi1335 – 13428Combined sources
Beta strandi1345 – 13506Combined sources
Beta strandi1362 – 137110Combined sources
Beta strandi1381 – 13866Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119018.
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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        10         20         30         40         50
MMNMSLPFLW SLLTLLIFAE VNGEAGELEL QRQKRSINLQ QPRMATERGN
60 70 80 90 100
LVFLTGSAQN IEFRTGSLGK IKLNDEDLSE CLHQIQKNKE DIIELKGSAI
110 120 130 140 150
GLPQNISSQI YQLNSKLVDL ERKFQGLQQT VDKKVCSSNP CQNGGTCLNL
160 170 180 190 200
HDSFFCICPP QWKGPLCSAD VNECEIYSGT PLSCQNGGTC VNTMGSYSCH
210 220 230 240 250
CPPETYGPQC ASKYDDCEGG SVARCVHGIC EDLMREQAGE PKYSCVCDAG
260 270 280 290 300
WMFSPNSPAC TLDRDECSFQ PGPCSTLVQC FNTQGSFYCG ACPTGWQGNG
310 320 330 340 350
YICEDINECE INNGGCSVAP PVECVNTPGS SHCQACPPGY QGDGRVCTLT
360 370 380 390 400
DICSVSNGGC HPDASCSSTL GSLPLCTCLP GYTGNGYGPN GCVQLSNICL
410 420 430 440 450
SHPCLNGQCI DTVSGYFCKC DSGWTGVNCT ENINECLSNP CLNGGTCVDG
460 470 480 490 500
VDSFSCECTR LWTGALCQVP QQVCGESLSG INGSFSYRSP DVGYVHDVNC
510 520 530 540 550
FWVIKTEMGK VLRITFTFFR LESMDNCPHE FLQVYDGDSS SAFQLGRFCG
560 570 580 590 600
SSLPHELLSS DNALYFHLYS EHLRNGRGFT VRWETQQPEC GGILTGPYGS
610 620 630 640 650
IKSPGYPGNY PPGRDCVWIV VTSPDLLVTF TFGTLSLEHH DDCNKDYLEI
660 670 680 690 700
RDGPLYQDPL LGKFCTTFSV PPLQTTGPFA RIHFHSDSQI SDQGFHITYL
710 720 730 740 750
TSPSDLRCGG NYTDPEGELF LPELSGPFTH TRQCVYMMKQ PQGEQIQINF
760 770 780 790 800
THVELQCQSD SSQNYIEVRD GETLLGKVCG NGTISHIKSI TNSVWIRFKI
810 820 830 840 850
DASVEKASFR AVYQVACGDE LTGEGVIRSP FFPNVYPGER TCRWTIHQPQ
860 870 880 890 900
SQVILLNFTV FEIGSSAHCE TDYVEIGSSS ILGSPENKKY CGTDIPSFIT
910 920 930 940 950
SVYNFLYVTF VKSSSTENHG FMAKFSAEDL ACGEILTEST GTIQSPGHPN
960 970 980 990 1000
VYPHGINCTW HILVQPNHLI HLMFETFHLE FHYNCTNDYL EVYDTDSETS
1010 1020 1030 1040 1050
LGRYCGKSIP PSLTSSGNSL MLVFVTDSDL AYEGFLINYE AISAATACLQ
1060 1070 1080 1090 1100
DYTDDLGTFT SPNFPNNYPN NWECIYRITV RTGQLIAVHF TNFSLEEAIG
1110 1120 1130 1140 1150
NYYTDFLEIR DGGYEKSPLL GIFYGSNLPP TIISHSNKLW LKFKSDQIDT
1160 1170 1180 1190 1200
RSGFSAYWDG SSTGCGGNLT TSSGTFISPN YPMPYYHSSE CYWWLKSSHG
1210 1220 1230 1240 1250
SAFELEFKDF HLEHHPNCTL DYLAVYDGPS SNSHLLTQLC GDEKPPLIRS
1260 1270 1280 1290 1300
SGDSMFIKLR TDEGQQGRGF KAEYRQTCEN VVIVNQTYGI LESIGYPNPY
1310 1320 1330 1340 1350
SENQHCNWTI RATTGNTVNY TFLAFDLEHH INCSTDYLEL YDGPRQMGRY
1360 1370 1380 1390 1400
CGVDLPPPGS TTSSKLQVLL LTDGVGRREK GFQMQWFVYG CGGELSGATG
1410 1420 1430 1440 1450
SFSSPGFPNR YPPNKECIWY IRTDPGSSIQ LTIHDFDVEY HSRCNFDVLE
1460 1470 1480 1490 1500
IYGGPDFHSP RIAQLCTQRS PENPMQVSST GNELAIRFKT DLSINGRGFN
1510 1520 1530 1540 1550
ASWQAVTGGC GGIFQAPSGE IHSPNYPSPY RSNTDCSWVI RVDRNHRVLL
1560 1570 1580 1590 1600
NFTDFDLEPQ DSCIMAYDGL SSTMSRLART CGREQLANPI VSSGNSLFLR
1610 1620 1630 1640 1650
FQSGPSRQNR GFRAQFRQAC GGHILTSSFD TVSSPRFPAN YPNNQNCSWI
1660 1670 1680 1690 1700
IQAQPPLNHI TLSFTHFELE RSTTCARDFV EILDGGHEDA PLRGRYCGTD
1710 1720 1730 1740 1750
MPHPITSFSS ALTLRFVSDS SISAGGFHTT VTASVSACGG TFYMAEGIFN
1760 1770 1780 1790 1800
SPGYPDIYPP NVECVWNIVS SPGNRLQLSF ISFQLEDSQD CSRDFVEIRE
1810 1820 1830 1840 1850
GNATGHLVGR YCGNSFPLNY SSIVGHTLWV RFISDGSGSG TGFQATFMKI
1860 1870 1880 1890 1900
FGNDNIVGTH GKVASPFWPE NYPHNSNYQW TVNVNASHVV HGRILEMDIE
1910 1920 1930 1940 1950
EIQNCYYDKL RIYDGPSIHA RLIGAYCGTQ TESFSSTGNS LTFHFYSDSS
1960 1970 1980 1990 2000
ISGKGFLLEW FAVDAPDGVL PTIAPGACGG FLRTGDAPVF LFSPGWPDSY
2010 2020 2030 2040 2050
SNRVDCTWLI QAPDSTVELN ILSLDIESHR TCAYDSLVIR DGDNNLAQQL
2060 2070 2080 2090 2100
AVLCGREIPG PIRSTGEYMF IRFTSDSSVT RAGFNASFHK SCGGYLHADR
2110 2120 2130 2140 2150
GIITSPKYPE TYPSNLNCSW HVLVQSGLTI AVHFEQPFQI PNGDSSCNQG
2160 2170 2180 2190 2200
DYLVLRNGPD ICSPPLGPPG GNGHFCGSHA SSTLFTSDNQ MFVQFISDHS
2210 2220 2230 2240 2250
NEGQGFKIKY EAKSLACGGN VYIHDADSAG YVTSPNHPHN YPPHADCIWI
2260 2270 2280 2290 2300
LAAPPETRIQ LQFEDRFDIE VTPNCTSNYL ELRDGVDSDA PILSKFCGTS
2310 2320 2330 2340 2350
LPSSQWSSGE VMYLRFRSDN SPTHVGFKAK YSIAQCGGRV PGQSGVVESI
2360 2370 2380 2390 2400
GHPTLPYRDN LFCEWHLQGL SGHYLTISFE DFNLQNSSGC EKDFVEIWDN
2410 2420 2430 2440 2450
HTSGNILGRY CGNTIPDSID TSSNTAVVRF VTDGSVTASG FRLRFESSME
2460 2470 2480 2490 2500
ECGGDLQGSI GTFTSPNYPN PNPHGRICEW RITAPEGRRI TLMFNNLRLA
2510 2520 2530 2540 2550
THPSCNNEHV IVFNGIRSNS PQLEKLCSSV NVSNEIKSSG NTMKVIFFTD
2560 2570 2580 2590 2600
GSRPYGGFTA SYTSSEDAVC GGSLPNTPEG NFTSPGYDGV RNYSRNLNCE
2610 2620 2630 2640 2650
WTLSNPNQGN SSISIHFEDF YLESHQDCQF DVLEFRVGDA DGPLMWRLCG
2660 2670 2680 2690 2700
PSKPTLPLVI PYSQVWIHFV TNERVEHIGF HAKYSFTDCG GIQIGDSGVI
2710 2720 2730 2740 2750
TSPNYPNAYD SLTHCSSLLE APQGHTITLT FSDFDIEPHT TCAWDSVTVR
2760 2770 2780 2790 2800
NGGSPESPII GQYCGNSNPR TIQSGSNQLV VTFNSDHSLQ GGGFYATWNT
2810 2820 2830 2840 2850
QTLGCGGIFH SDNGTIRSPH WPQNFPENSR CSWTAITHKS KHLEISFDNN
2860 2870 2880 2890 2900
FLIPSGDGQC QNSFVKVWAG TEEVDKALLA TGCGNVAPGP VITPSNTFTA
2910 2920 2930 2940 2950
VFQSQEAPAQ GFSASFVSRC GSNFTGPSGY IISPNYPKQY DNNMNCTYVI
2960 2970 2980 2990 3000
EANPLSVVLL TFVSFHLEAR SAVTGSCVND GVHIIRGYSV MSTPFATVCG
3010 3020 3030 3040 3050
DEMPAPLTIA GPVLLNFYSN EQITDFGFKF SYRIISCGGV FNFSSGIITS
3060 3070 3080 3090 3100
PAYSYADYPN DMHCLYTITV SDDKVIELKF SDFDVVPSTS CSHDYLAIYD
3110 3120 3130 3140 3150
GANTSDPLLG KFCGSKRPPN VKSSNNSMLL VFKTDSFQTA KGWKMSFRQT
3160 3170 3180 3190 3200
LGPQQGCGGY LTGSNNTFAS PDSDSNGMYD KNLNCVWIII APVNKVIHLT
3210 3220 3230 3240 3250
FNTFALEAAS TRQRCLYDYV KLYDGDSENA NLAGTFCGST VPAPFISSGN
3260 3270 3280 3290 3300
FLTVQFISDL TLEREGFNAT YTIMDMPCGG TYNATWTPQN ISSPNSSDPD
3310 3320 3330 3340 3350
VPFSICTWVI DSPPHQQVKI TVWALQLTSQ DCTQNYLQLQ DSPQGHGNSR
3360 3370 3380 3390 3400
FQFCGRNASA VPVFYSSMST AMVIFKSGVV NRNSRMSFTY QIADCNRDYH
3410 3420 3430 3440 3450
KAFGNLRSPG WPDNYDNDKD CTVTLTAPQN HTISLFFHSL GIENSVECRN
3460 3470 3480 3490 3500
DFLEVRNGSN SNSPLLGKYC GTLLPNPVFS QNNELYLRFK SDSVTSDRGY
3510 3520 3530 3540 3550
EIIWTSSPSG CGGTLYGDRG SFTSPGYPGT YPNNTYCEWV LVAPAGRLVT
3560 3570 3580 3590 3600
INFYFISIDD PGDCVQNYLT LYDGPNASSP SSGPYCGGDT SIAPFVASSN
3610 3620
QVFIKFHADY ARRPSAFRLT WDS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00760000119018.
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

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

Gene expression databases

Bgeei O60494.
CleanExi HS_CUBN.
ExpressionAtlasi O60494. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 134 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