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Entry version 181 (16 Oct 2019)
Sequence version 5 (02 Nov 2010)
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Protein

Cubilin

Gene

CUBN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Endocytic receptor which plays a role in lipoprotein, vitamin and iron metabolism by facilitating their uptake (PubMed:9572993, PubMed:10371504, PubMed:11717447, PubMed:11606717, PubMed:14576052). Acts together with LRP2 to mediate endocytosis of high-density lipoproteins, GC, hemoglobin, ALB, TF and SCGB1A1. Acts together with AMN to mediate endocytosis of the CBLIF-cobalamin complex (PubMed:9572993, PubMed:14576052). Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the CBLIF-cobalamin complex. Ligand binding requires calcium (PubMed:9572993). Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. 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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi980Calcium 1Combined sources1 Publication1
Metal bindingi988Calcium 1Combined sources1 Publication1
Metal bindingi1027Calcium 1Combined sources1 Publication1
Metal bindingi1029Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1030Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1096Calcium 2Combined sources1 Publication1
Metal bindingi1105Calcium 2Combined sources1 Publication1
Metal bindingi1146Calcium 2Combined sources1 Publication1
Metal bindingi1148Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1149Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1213Calcium 3Combined sources1 Publication1
Metal bindingi1221Calcium 3Combined sources1 Publication1
Metal bindingi1262Calcium 3Combined sources1 Publication1
Metal bindingi1264Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1265Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1328Calcium 4Combined sources1 Publication1
Metal bindingi1336Calcium 4Combined sources1 Publication1
Metal bindingi1373Calcium 4Combined sources1 Publication1
Metal bindingi1375Calcium 4; via carbonyl oxygenCombined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionReceptor
Biological processCholesterol metabolism, Endocytosis, Lipid metabolism, Protein transport, Steroid metabolism, Sterol metabolism, Transport
LigandCalcium, Cobalamin, Cobalt, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-196741 Cobalamin (Cbl, vitamin B12) transport and metabolism
R-HSA-196791 Vitamin D (calciferol) metabolism
R-HSA-3359462 Defective AMN causes hereditary megaloblastic anemia 1
R-HSA-3359463 Defective CUBN causes hereditary megaloblastic anemia 1
R-HSA-8964011 HDL clearance

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cubilin1 Publication
Alternative name(s):
460 kDa receptor
Intestinal intrinsic factor receptor
Intrinsic factor-cobalamin receptor
Intrinsic factor-vitamin B12 receptor1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CUBN
Synonyms:IFCR
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:2548 CUBN

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
602997 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O60494

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Coated pit, Endosome, Lysosome, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Recessive hereditary megaloblastic anemia 1 (RH-MGA1)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionDue 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0252881297P → L in RH-MGA1; decreases strongly the CBLIF binding affinity. 2 PublicationsCorresponds to variant dbSNP:rs121434430EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
8029

MalaCards human disease database

More...
MalaCardsi
CUBN
MIMi261100 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000107611

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
35858 Imerslund-Graesbeck syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA27044

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
O60494

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB00115 Cyanocobalamin
DB00200 Hydroxocobalamin

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CUBN

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 23Sequence analysisAdd BLAST23
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000004607224 – 35Removed in mature form1 PublicationAdd BLAST12
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000004607336 – 3623CubilinAdd BLAST3588

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi105N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>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
Glycosylationi428N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi436 ↔ 447By similarity
Disulfide bondi441 ↔ 456By similarity
Disulfide bondi458 ↔ 467By similarity
Disulfide bondi474 ↔ 500By similarity
Glycosylationi482N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi527 ↔ 549By similarity
Disulfide bondi590 ↔ 616By similarity
Disulfide bondi643 ↔ 665By similarity
Disulfide bondi708 ↔ 734By similarity
Glycosylationi711N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi749N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi781N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi857N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi869 ↔ 891By similarity
Disulfide bondi932 ↔ 958Combined sources1 Publication
Glycosylationi957N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi984N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi985 ↔ 1005Combined sources1 Publication
Disulfide bondi1048 ↔ 1074Combined sources1 Publication
Glycosylationi1092N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi1165 ↔ 1191Combined sources1 Publication
Glycosylationi1168N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi1217N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi1218 ↔ 1240Combined sources1 Publication
Disulfide bondi1278 ↔ 1306Combined sources1 Publication
Glycosylationi1285N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi1307N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi1319N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi1332N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi1333 ↔ 1351Combined sources1 Publication
Disulfide bondi1391 ↔ 1417By similarity
Disulfide bondi1444 ↔ 1466By similarity
Glycosylationi1500N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1510 ↔ 1536By similarity
Glycosylationi1551N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1563 ↔ 1581By similarity
Disulfide bondi1620 ↔ 1647By similarity
Glycosylationi1646N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1675 ↔ 1697By similarity
Disulfide bondi1738 ↔ 1764By similarity
Disulfide bondi1791 ↔ 1812By similarity
Glycosylationi1802N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1819N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1885N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1905 ↔ 1927By similarity
Disulfide bondi1978 ↔ 2006By similarity
Disulfide bondi2032 ↔ 2054By similarity
Glycosylationi2085N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2092 ↔ 2118By similarity
Glycosylationi2117N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2217 ↔ 2247By similarity
Glycosylationi2274N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2275 ↔ 2297By similarity
Disulfide bondi2336 ↔ 2363By similarity
Glycosylationi2386N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2390 ↔ 2411By similarity
Glycosylationi2400N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2452 ↔ 2478By similarity
Disulfide bondi2505 ↔ 2527By similarity
Glycosylationi2531N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2570 ↔ 2599By similarity
Glycosylationi2581N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2592N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2610N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2628 ↔ 2649By similarity
Disulfide bondi2689 ↔ 2715By similarity
Disulfide bondi2742 ↔ 2764By similarity
Disulfide bondi2805 ↔ 2831By similarity
Glycosylationi2813N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2860 ↔ 2883By similarity
Disulfide bondi2920 ↔ 2946By similarity
Glycosylationi2923N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2945N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2977 ↔ 2999By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei3008PhosphothreonineBy similarity1
Disulfide bondi3037 ↔ 3064By similarity
Glycosylationi3042N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3091 ↔ 3113By similarity
Glycosylationi3103N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3125N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3157 ↔ 3185By similarity
Glycosylationi3165N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3215 ↔ 3237By similarity
Glycosylationi3268N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3278 ↔ 3306By similarity
Glycosylationi3283N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3290N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3295N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3332 ↔ 3354By similarity
Glycosylationi3357N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3395 ↔ 3421By similarity
Glycosylationi3430N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3448 ↔ 3470By similarity
Glycosylationi3457N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3511 ↔ 3537By similarity
Glycosylationi3533N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3564 ↔ 3586By similarity
Glycosylationi3576N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The precursor is cleaved by a trans-Golgi proteinase furin, removing a propeptide.1 Publication
N-glycosylated.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei35 – 36Cleavage; by furinSequence analysis2

Keywords - PTMi

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

Proteomic databases

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
O60494

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O60494

PeptideAtlas

More...
PeptideAtlasi
O60494

PRoteomics IDEntifications database

More...
PRIDEi
O60494

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
49432

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
2033

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O60494

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O60494

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in kidney cortex (at protein level) (PubMed:9572993). Expressed in kidney proximal tubule cells, placenta, visceral yolk-sac cells and in absorptive intestinal cells. Expressed in the epithelium of intestine and kidney.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000107611 Expressed in 121 organ(s), highest expression level in cortex of kidney

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O60494 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O60494 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA004133
HPA043854

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with AMN (PubMed:14576052, PubMed:29402915, PubMed:20237569, PubMed:30523278).

Component of the cubam complex composed of one CUBN trimer and one AMN chain (PubMed:30523278). The cubam complex can dimerize (By similarity).

Interacts with LRP2 in a dual-receptor complex in a calcium-dependent manner.

Found in a complex with PID1/PCLI1, LRP1 and CUBNI.

Interacts with LRP1 and PID1/PCLI1.

By similarity8 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
113724, 10 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O60494

Database of interacting proteins

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DIPi
DIP-58583N

Protein interaction database and analysis system

More...
IntActi
O60494, 3 interactors

Molecular INTeraction database

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MINTi
O60494

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000367064

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

13623
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O60494

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O60494

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini132 – 168EGF-like 1PROSITE-ProRule annotationAdd BLAST37
Domaini170 – 211EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini263 – 304EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini305 – 348EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST44
Domaini349 – 385EGF-like 5PROSITE-ProRule annotationAdd BLAST37
Domaini395 – 430EGF-like 6PROSITE-ProRule annotationAdd BLAST36
Domaini432 – 468EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini474 – 586CUB 1PROSITE-ProRule annotationAdd BLAST113
Domaini590 – 702CUB 2PROSITE-ProRule annotationAdd BLAST113
Domaini708 – 816CUB 3PROSITE-ProRule annotationAdd BLAST109
Domaini816 – 928CUB 4PROSITE-ProRule annotationAdd BLAST113
Domaini932 – 1042CUB 5PROSITE-ProRule annotationAdd BLAST111
Domaini1048 – 1161CUB 6PROSITE-ProRule annotationAdd BLAST114
Domaini1165 – 1277CUB 7PROSITE-ProRule annotationAdd BLAST113
Domaini1278 – 1389CUB 8PROSITE-ProRule annotationAdd BLAST112
Domaini1391 – 1506CUB 9PROSITE-ProRule annotationAdd BLAST116
Domaini1510 – 1619CUB 10PROSITE-ProRule annotationAdd BLAST110
Domaini1620 – 1734CUB 11PROSITE-ProRule annotationAdd BLAST115
Domaini1738 – 1850CUB 12PROSITE-ProRule annotationAdd BLAST113
Domaini1852 – 1963CUB 13PROSITE-ProRule annotationAdd BLAST112
Domaini1978 – 2091CUB 14PROSITE-ProRule annotationAdd BLAST114
Domaini2092 – 2213CUB 15PROSITE-ProRule annotationAdd BLAST122
Domaini2217 – 2334CUB 16PROSITE-ProRule annotationAdd BLAST118
Domaini2336 – 2448CUB 17PROSITE-ProRule annotationAdd BLAST113
Domaini2452 – 2565CUB 18PROSITE-ProRule annotationAdd BLAST114
Domaini2570 – 2687CUB 19PROSITE-ProRule annotationAdd BLAST118
Domaini2689 – 2801CUB 20PROSITE-ProRule annotationAdd BLAST113
Domaini2805 – 2919CUB 21PROSITE-ProRule annotationAdd BLAST115
Domaini2920 – 3035CUB 22PROSITE-ProRule annotationAdd BLAST116
Domaini3037 – 3150CUB 23PROSITE-ProRule annotationAdd BLAST114
Domaini3157 – 3274CUB 24PROSITE-ProRule annotationAdd BLAST118
Domaini3278 – 3393CUB 25PROSITE-ProRule annotationAdd BLAST116
Domaini3395 – 3507CUB 26PROSITE-ProRule annotationAdd BLAST113
Domaini3511 – 3623CUB 27PROSITE-ProRule annotationAdd BLAST113

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni42 – 49Interaction with AMN1 Publication8

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The CUB domains 5 to 8 mediate binding to CBLIF and ALB. CUB domains 1 and 2 mediate interaction with LRP2.By similarity
The cubam complex is composed of a 400 Angstrom long stem and a globular crown region. The stem region is probably formed by AMN and the CUBN N-terminal region, including the EGF-like domains. The crown is probably formed by the CUBN CUB domains.By similarity

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3714 Eukaryota
ENOG410ZPX7 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155299

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000049236

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O60494

KEGG Orthology (KO)

More...
KOi
K14616

Identification of Orthologs from Complete Genome Data

More...
OMAi
FHLEYHP

Database of Orthologous Groups

More...
OrthoDBi
4105at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O60494

TreeFam database of animal gene trees

More...
TreeFami
TF316224

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00041 CUB, 27 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.290, 27 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000859 CUB_dom
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR024731 EGF_dom
IPR009030 Growth_fac_rcpt_cys_sf
IPR035914 Sperma_CUB_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00431 CUB, 27 hits
PF00008 EGF, 3 hits
PF12947 EGF_3, 1 hit
PF07645 EGF_CA, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00042 CUB, 27 hits
SM00181 EGF, 8 hits
SM00179 EGF_CA, 7 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49854 SSF49854, 27 hits
SSF57184 SSF57184, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

O60494-1 [UniParc]FASTAAdd to basket
« Hide
        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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8D602663C6D4751F
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7C480H7C480_HUMAN
Cubilin
CUBN
105Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti25A → R in AAC82612 (PubMed:9572993).Curated1
Sequence conflicti146T → N in AAC82612 (PubMed:9572993).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04744366G → R. Corresponds to variant dbSNP:rs12259370EnsemblClinVar.1
Natural variantiVAR_025284124F → I1 PublicationCorresponds to variant dbSNP:rs1801220Ensembl.1
Natural variantiVAR_025285253F → S2 PublicationsCorresponds to variant dbSNP:rs1801222EnsemblClinVar.1
Natural variantiVAR_061154335A → T. Corresponds to variant dbSNP:rs57335729EnsemblClinVar.1
Natural variantiVAR_025286389P → T1 PublicationCorresponds to variant dbSNP:rs1801224EnsemblClinVar.1
Natural variantiVAR_047444504I → M. Corresponds to variant dbSNP:rs2228053Ensembl.1
Natural variantiVAR_047445730H → Y. Corresponds to variant dbSNP:rs7905349EnsemblClinVar.1
Natural variantiVAR_035829786H → Q in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1228797857Ensembl.1
Natural variantiVAR_047446969L → V. Corresponds to variant dbSNP:rs11254354Ensembl.1
Natural variantiVAR_0252871032Y → H1 PublicationCorresponds to variant dbSNP:rs1801227Ensembl.1
Natural variantiVAR_0252881297P → L in RH-MGA1; decreases strongly the CBLIF binding affinity. 2 PublicationsCorresponds to variant dbSNP:rs121434430EnsemblClinVar.1
Natural variantiVAR_0252891545N → Y2 Publications1
Natural variantiVAR_0252901559P → S1 PublicationCorresponds to variant dbSNP:rs1801231EnsemblClinVar.1
Natural variantiVAR_0252911769V → I2 PublicationsCorresponds to variant dbSNP:rs74116778EnsemblClinVar.1
Natural variantiVAR_0474471775R → W. Corresponds to variant dbSNP:rs1276708Ensembl.1
Natural variantiVAR_0474481840G → S. Corresponds to variant dbSNP:rs2271462EnsemblClinVar.1
Natural variantiVAR_0474491935S → G. Corresponds to variant dbSNP:rs41289305EnsemblClinVar.1
Natural variantiVAR_0474501971P → T. Corresponds to variant dbSNP:rs2356590EnsemblClinVar.1
Natural variantiVAR_0252922153L → F Higher frequency in West Africans than in individuals of European ancestry; occurs with variants V-2984 and G-3002 only in individuals of European ancestry. 2 PublicationsCorresponds to variant dbSNP:rs62619939EnsemblClinVar.1
Natural variantiVAR_0252932162C → Y1 PublicationCorresponds to variant dbSNP:rs1276712EnsemblClinVar.1
Natural variantiVAR_0358302252A → V in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs529856485Ensembl.1
Natural variantiVAR_0474512263F → C. Corresponds to variant dbSNP:rs2271460EnsemblClinVar.1
Natural variantiVAR_0474522444R → Q. Corresponds to variant dbSNP:rs11254274Ensembl.1
Natural variantiVAR_0252942575P → R1 PublicationCorresponds to variant dbSNP:rs3740168EnsemblClinVar.1
Natural variantiVAR_0252952691G → R1 PublicationCorresponds to variant dbSNP:rs1801237Ensembl.1
Natural variantiVAR_0252962717S → W1 PublicationCorresponds to variant dbSNP:rs2796835EnsemblClinVar.1
Natural variantiVAR_0252972879L → I1 PublicationCorresponds to variant dbSNP:rs1801238EnsemblClinVar.1
Natural variantiVAR_0358312914A → V in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs45551835EnsemblClinVar.1
Natural variantiVAR_0474532968E → Q. Corresponds to variant dbSNP:rs45569534EnsemblClinVar.1
Natural variantiVAR_0252982984I → V Not found in West Africans; occurs with variants F-2153 and G-3002 only in individuals of European ancestry; associated with albuminuria in individuals of European ancestry and African Americans, both with and without diabetes; associated with 42% increased risk of developing persistent microalbuminuria in individuals with type I diabetes. 3 PublicationsCorresponds to variant dbSNP:rs1801239EnsemblClinVar.1
Natural variantiVAR_0252993002E → G Higher frequency in West Africans than in individuals of European ancestry; occurs with variants F-2153 and V-2984 only in individuals of European ancestry. 2 PublicationsCorresponds to variant dbSNP:rs1801240EnsemblClinVar.1
Natural variantiVAR_0358323189I → V in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs111265129EnsemblClinVar.1
Natural variantiVAR_0647043258S → G Found in a renal cell carcinoma case; somatic mutation. 1 Publication1
Natural variantiVAR_0253003422T → I1 PublicationCorresponds to variant dbSNP:rs1801230EnsemblClinVar.1
Natural variantiVAR_0557143432T → S. Corresponds to variant dbSNP:rs7898873EnsemblClinVar.1
Natural variantiVAR_0253013552N → K1 PublicationCorresponds to variant dbSNP:rs1801232EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF034611 mRNA Translation: AAC82612.1
EF444970 Genomic DNA Translation: ACA05973.1
EF444970 Genomic DNA Translation: ACA05974.1
AC067747 Genomic DNA No translation available.
AL365215 Genomic DNA No translation available.
AL596445 Genomic DNA No translation available.
AL731551 Genomic DNA No translation available.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS7113.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T09456

NCBI Reference Sequences

More...
RefSeqi
NP_001072.2, NM_001081.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000377833; ENSP00000367064; ENSG00000107611

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
8029

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:8029

UCSC genome browser

More...
UCSCi
uc001ioo.4 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
AC067747 Genomic DNA No translation available.
AL365215 Genomic DNA No translation available.
AL596445 Genomic DNA No translation available.
AL731551 Genomic DNA No translation available.
CCDSiCCDS7113.1
PIRiT09456
RefSeqiNP_001072.2, NM_001081.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KQ4X-ray3.30B/D/F932-1388[»]
6GJEX-ray2.30B/C/D26-135[»]
SMRiO60494
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi113724, 10 interactors
CORUMiO60494
DIPiDIP-58583N
IntActiO60494, 3 interactors
MINTiO60494
STRINGi9606.ENSP00000367064

Chemistry databases

DrugBankiDB00115 Cyanocobalamin
DB00200 Hydroxocobalamin

PTM databases

GlyConnecti2033
iPTMnetiO60494
PhosphoSitePlusiO60494

Polymorphism and mutation databases

BioMutaiCUBN

Proteomic databases

MassIVEiO60494
PaxDbiO60494
PeptideAtlasiO60494
PRIDEiO60494
ProteomicsDBi49432

Genome annotation databases

EnsembliENST00000377833; ENSP00000367064; ENSG00000107611
GeneIDi8029
KEGGihsa:8029
UCSCiuc001ioo.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8029
DisGeNETi8029

GeneCards: human genes, protein and diseases

More...
GeneCardsi
CUBN
HGNCiHGNC:2548 CUBN
HPAiHPA004133
HPA043854
MalaCardsiCUBN
MIMi261100 phenotype
602997 gene
neXtProtiNX_O60494
OpenTargetsiENSG00000107611
Orphaneti35858 Imerslund-Graesbeck syndrome
PharmGKBiPA27044

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG3714 Eukaryota
ENOG410ZPX7 LUCA
GeneTreeiENSGT00940000155299
HOGENOMiHOG000049236
InParanoidiO60494
KOiK14616
OMAiFHLEYHP
OrthoDBi4105at2759
PhylomeDBiO60494
TreeFamiTF316224

Enzyme and pathway databases

ReactomeiR-HSA-196741 Cobalamin (Cbl, vitamin B12) transport and metabolism
R-HSA-196791 Vitamin D (calciferol) metabolism
R-HSA-3359462 Defective AMN causes hereditary megaloblastic anemia 1
R-HSA-3359463 Defective CUBN causes hereditary megaloblastic anemia 1
R-HSA-8964011 HDL clearance

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
CUBN human
EvolutionaryTraceiO60494

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Cubilin

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
8029
PharosiO60494

Protein Ontology

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PROi
PR:O60494

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000107611 Expressed in 121 organ(s), highest expression level in cortex of kidney
ExpressionAtlasiO60494 baseline and differential
GenevisibleiO60494 HS

Family and domain databases

CDDicd00041 CUB, 27 hits
Gene3Di2.60.120.290, 27 hits
InterProiView protein in InterPro
IPR000859 CUB_dom
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR024731 EGF_dom
IPR009030 Growth_fac_rcpt_cys_sf
IPR035914 Sperma_CUB_dom_sf
PfamiView protein in Pfam
PF00431 CUB, 27 hits
PF00008 EGF, 3 hits
PF12947 EGF_3, 1 hit
PF07645 EGF_CA, 3 hits
SMARTiView protein in SMART
SM00042 CUB, 27 hits
SM00181 EGF, 8 hits
SM00179 EGF_CA, 7 hits
SUPFAMiSSF49854 SSF49854, 27 hits
SSF57184 SSF57184, 1 hit
PROSITEiView protein in PROSITE
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCUBN_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O60494
Secondary accession number(s): B0YIZ4, Q5VTA6, Q96RU9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: November 2, 2010
Last modified: October 16, 2019
This is version 181 of the entry and version 5 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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