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O60494

- CUBN_HUMAN

UniProt

O60494 - CUBN_HUMAN

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Protein
Cubilin
Gene
CUBN, IFCR
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 furin Reviewed prediction
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
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; Peripheral membrane protein By similarity. Lysosome membrane; Peripheral membrane protein By similarity
Note: Colocalizes with AMN and LRP2 in the endocytotic apparatus of epithelial cells By similarity.

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. apical plasma membrane Source: UniProt
  3. brush border membrane Source: UniProtKB
  4. coated pit Source: Ensembl
  5. cytosol Source: Reactome
  6. endocytic vesicle Source: UniProt
  7. endoplasmic reticulum Source: Ensembl
  8. endosome membrane Source: Reactome
  9. extracellular vesicular exosome Source: UniProt
  10. extrinsic component of external side of plasma membrane Source: UniProtKB
  11. lysosomal lumen Source: Reactome
  12. lysosomal membrane Source: UniProtKB-SubCell
  13. membrane Source: ProtInc
  14. 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.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1297 – 12971P → L in RH-MGA1; decreases strongly the GIF binding affinity. 2 Publications
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 – 2323 Reviewed prediction
Add
BLAST
Propeptidei24 – 3512Removed in mature form
PRO_0000046072Add
BLAST
Chaini36 – 36233588Cubilin
PRO_0000046073Add
BLAST

Amino acid modifications

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

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

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.

Miscellaneous databases

EvolutionaryTraceiO60494.

Family & Domainsi

Domains and Repeats

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

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

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. 2 Publications
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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251A → R in AAC82612. 1 Publication
Sequence conflicti146 – 1461T → N in AAC82612. 1 Publication

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

« 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: September 3, 2014
This is version 131 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

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