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UniProtKB - P02786 (TFR1_HUMAN)

Entry version 231 (13 Feb 2019)
Sequence version 2 (30 May 2006)
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Protein

Transferrin receptor protein 1

Gene

TFRC

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

Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. Positively regulates T and B cell proliferation through iron uptake (PubMed:26642240).By similarity2 Publications
(Microbial infection) Acts as a receptor for new-world arenaviruses: Guanarito, Junin and Machupo virus.2 Publications

Miscellaneous

Serum transferrin receptor (sTfR) is used as a means of detecting erythropoietin (EPO) misuse by athletes and as a diagnostic test for anemia resulting from a number of conditions including rheumatoid arthritis, pregnancy, irritable bowel syndrome and in HIV patients.
Canine and feline parvoviruses bind human and feline transferrin receptors and use these receptors to enter and infect cells.

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 functionHost cell receptor for virus entry, Receptor
Biological processEndocytosis, Host-virus interaction

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-432722 Golgi Associated Vesicle Biogenesis
R-HSA-8856825 Cargo recognition for clathrin-mediated endocytosis
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-917977 Transferrin endocytosis and recycling

SIGNOR Signaling Network Open Resource

More...SIGNORi		P02786

Protein family/group databases

MEROPS protease database

More...MEROPSi		M28.972

Transport Classification Database

More...TCDBi		9.B.229.1.1 the transferrin receptor, cd71, (tfr) family

<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:
Transferrin receptor protein 1
Short name:
TR
Short name:
TfR
Short name:
TfR1
Short name:
Trfr
Alternative name(s):
T9
p90
CD_antigen: CD71
Cleaved into the following chain:
Transferrin receptor protein 1, serum form
Short name:
sTfR
<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:TFRC
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000072274.12

Human Gene Nomenclature Database

More...HGNCi		HGNC:11763 TFRC

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		190010 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P02786

<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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 67CytoplasmicSequence analysisAdd BLAST67
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei68 – 88Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini89 – 760ExtracellularSequence analysisAdd BLAST672

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

<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

Immunodeficiency 46 (IMD46)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive primary immunodeficiency disorder characterized by early-onset chronic diarrhea, recurrent infections, hypo- or agammaglobulinemia, normal lymphocyte counts, intermittent neutropenia, and intermittent thrombocytopenia.
See also OMIM:616740
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_07636520Y → H in IMD46; increases protein expression; increases cell surface expression on T and B cells; increases soluble form level; impairs receptor internalization; impairs transferrin transport; impairs T and B cell proliferation as well as B cell class-switching; interacts with STEAP3; doesn't affect receptor internalization in erythroid precursor cells. 1 PublicationCorresponds to variant dbSNP:rs863225436EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi9 – 12FSNL → YTRF: Only 80% as active as wild-type receptor. 4
Mutagenesisi20 – 34YTRFS…DGDNS → PPGYSLARQVDYTRF: No influence on endocytic uptake of the receptor. Add BLAST15
Mutagenesisi20 – 23YTRF → PPGY: Only 16% as active as wild-type receptor. 1 Publication4
Mutagenesisi20Y → C: Only 35% as active as wild-type receptor. 3 Publications1
Mutagenesisi20Y → G: Only 20% as active as wild-type receptor. 3 Publications1
Mutagenesisi21T → F: Only 88% as active as wild-type receptor. 1 Publication1
Mutagenesisi21T → TA: Only 14% as active as wild-type receptor. 1 Publication1
Mutagenesisi21T → TAA: Only 19% as active as wild-type receptor. 1 Publication1
Mutagenesisi23F → Y: Only 48% as active as wild-type receptor. 1 Publication1
Mutagenesisi31 – 34GDNS → YTRF: 2-fold increase of the endocytic uptake of the receptor. 4
Mutagenesisi47 – 50NADN → YTRF: 1.27-fold increase of the endocytic uptake of the receptor. 4
Mutagenesisi619L → A: 20-fold reduced affinity for transferrin receptor. No binding to HFE. 1
Mutagenesisi622V → A: No significant effect on binding to transferrin nor HFE. 1
Mutagenesisi623R → A: No significant effect on binding to transferrin nor HFE. 1
Mutagenesisi629R → A: >5-fold reduced affinity for transferrin. >10-fold reduced affinity for HFE. 1
Mutagenesisi640Q → A: No effect on binding to transferrin. >10-fold reduced affinity for HFE. 1
Mutagenesisi641W → A: No significant effect on binding to transferrin nor HFE. 1
Mutagenesisi643Y → A: 20-fold reduced affinity for transferrin. No binding to HFE. 1
Mutagenesisi644S → A: No significant effect on binding to transferrin nor HFE. 1
Mutagenesisi646R → A or H: No binding to transferrin. 1 Publication1
Mutagenesisi646R → K: 5% binding to transferrin. 1 Publication1
Mutagenesisi647G → A: Large effect on affinity for transferrin. 4-fold reduced affinity for HFE. 1 Publication1
Mutagenesisi648D → A: 16% binding to transferrin. 1 Publication1
Mutagenesisi648D → E: 57% binding to transferrin. 1 Publication1
Mutagenesisi650F → Q: >5-fold reduced affinity for transferrin. >10-fold reduced affinity for HFE. 1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		7037

MalaCards human disease database

More...MalaCardsi		TFRC
MIMi616740 phenotype

Open Targets

More...OpenTargetsi		ENSG00000072274

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

More...Orphaneti		476113 Combined immunodeficiency due to TFRC deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA36478

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3712860

Drug and drug target database

More...DrugBanki		DB09412 Gallium citrate Ga-67
DB05260 Gallium nitrate

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		TFRC

Domain mapping of disease mutations (DMDM)

More...DMDMi		108935939

<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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001741321 – 760Transferrin receptor protein 1Add BLAST760
ChainiPRO_0000292265101 – 760Transferrin receptor protein 1, serum formAdd BLAST660

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei10PhosphoserineCombined sources1
Modified residuei19PhosphoserineBy similarity1
Modified residuei20PhosphotyrosineCombined sources1
Modified residuei21PhosphothreonineCombined sources1
Modified residuei24Phosphoserine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi62S-palmitoyl cysteine1 Publication1
Lipidationi67S-palmitoyl cysteine1 Publication1
<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 bondi89Interchain
Disulfide bondi98Interchain
<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>GlycosylationiCAR_000072104O-linked (GalNAc...) threonine2 Publications1
Glycosylationi251N-linked (GlcNAc...) asparagineCombined sources4 Publications1
Glycosylationi317N-linked (GlcNAc...) asparagineCombined sources1 Publication1
GlycosylationiCAR_000173727N-linked (GlcNAc...) asparagineCombined sources3 Publications1

<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

N- and O-glycosylated, phosphorylated and palmitoylated. The serum form is only glycosylated.6 Publications
Proteolytically cleaved on Arg-100 to produce the soluble serum form (sTfR).
Palmitoylated on both Cys-62 and Cys-67. Cys-62 seems to be the major site of palmitoylation.1 Publication

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>Sitei100 – 101Cleavage; by trypsin; to produce soluble form2

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P02786

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P02786

MaxQB - The MaxQuant DataBase

More...MaxQBi		P02786

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

More...PaxDbi		P02786

PeptideAtlas

More...PeptideAtlasi		P02786

PRoteomics IDEntifications database

More...PRIDEi		P02786

ProteomicsDB human proteome resource

More...ProteomicsDBi		51595

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		607

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P02786

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

More...PhosphoSitePlusi		P02786

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P02786

UniCarbKB; an annotated and curated database of glycan structures

More...UniCarbKBi		P02786

<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Regulated by cellular iron levels through binding of the iron regulatory proteins, IRP1 and IRP2, to iron-responsive elements in the 3'-UTR. Up-regulated upon mitogenic stimulation.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000072274 Expressed in 243 organ(s), highest expression level in liver

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P02786 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P02786 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB000153
HPA028598

<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

Homodimer; disulfide-linked. Binds one transferrin or HFE molecule per subunit. Binds the HLA class II histocompatibility antigen, DR1. Interacts with SH3BP3. Interacts with STEAP3; facilitates TFRC endocytosis in erythroid precursor cells (PubMed:26642240).2 Publications
(Microbial infection) Interacts with Guanarito, Junin and Machupo arenavirus glycoprotein complex (PubMed:17287727, PubMed:18268337).2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		112895, 98 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P02786

Database of interacting proteins

More...DIPi		DIP-2736N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P02786

Protein interaction database and analysis system

More...IntActi		P02786, 101 interactors

Molecular INTeraction database

More...MINTi		P02786

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000353224

<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

1760
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1CX8X-ray3.20A/B/C/D/E/F/G/H122-760[»]
1DE4X-ray2.80C/F/I121-760[»]
1SUVelectron microscopy7.50A/B122-760[»]
2NSUelectron microscopy27.00A/B122-760[»]
3KASX-ray2.40A121-760[»]
3S9LX-ray3.22A/B120-760[»]
3S9MX-ray3.32A/B120-760[»]
3S9NX-ray3.25A/B120-760[»]
6D03electron microscopy3.68A/B121-760[»]
6D04electron microscopy3.74A/B121-760[»]
6D05electron microscopy3.80A/B121-760[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P02786

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

More...SMRi		P02786

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P02786

<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>Domaini223 – 313PAAdd BLAST91

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>Regioni1 – 67Mediates interaction with SH3BP41 PublicationAdd BLAST67
Regioni569 – 760Ligand-bindingAdd BLAST192

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi20 – 23Endocytosis signal4
Motifi58 – 61Stop-transfer sequence4
Motifi646 – 648Cell attachment site; required for binding to transferrin3

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase M28 family. M28B subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2195 Eukaryota
COG2234 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153978

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG023177

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P02786

KEGG Orthology (KO)

More...KOi		K06503

Identification of Orthologs from Complete Genome Data

More...OMAi		IMKVEYH

Database of Orthologous Groups

More...OrthoDBi		156519at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P02786

TreeFam database of animal gene trees

More...TreeFami		TF312981

Family and domain databases

Conserved Domains Database

More...CDDi		cd02128 PA_TfR, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.930.40, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003137 PA_domain
IPR007484 Peptidase_M28
IPR039373 Peptidase_M28B
IPR029513 TfR
IPR007365 TFR-like_dimer_dom
IPR036757 TFR-like_dimer_dom_sf
IPR037324 TfR1/2_PA

The PANTHER Classification System

More...PANTHERi		PTHR10404 PTHR10404, 1 hit
PTHR10404:SF26 PTHR10404:SF26, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02225 PA, 1 hit
PF04389 Peptidase_M28, 1 hit
PF04253 TFR_dimer, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47672 SSF47672, 1 hit

<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>.<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 3 potential isoforms that are computationally mapped.Show allAlign All

P02786-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMDQARSAFS NLFGGEPLSY TRFSLARQVD GDNSHVEMKL AVDEEENADN 
        60         70         80         90        100
NTKANVTKPK RCSGSICYGT IAVIVFFLIG FMIGYLGYCK GVEPKTECER 
       110        120        130        140        150
LAGTESPVRE EPGEDFPAAR RLYWDDLKRK LSEKLDSTDF TGTIKLLNEN 
       160        170        180        190        200
SYVPREAGSQ KDENLALYVE NQFREFKLSK VWRDQHFVKI QVKDSAQNSV 
       210        220        230        240        250
IIVDKNGRLV YLVENPGGYV AYSKAATVTG KLVHANFGTK KDFEDLYTPV 
       260        270        280        290        300
NGSIVIVRAG KITFAEKVAN AESLNAIGVL IYMDQTKFPI VNAELSFFGH 
       310        320        330        340        350
AHLGTGDPYT PGFPSFNHTQ FPPSRSSGLP NIPVQTISRA AAEKLFGNME 
       360        370        380        390        400
GDCPSDWKTD STCRMVTSES KNVKLTVSNV LKEIKILNIF GVIKGFVEPD 
       410        420        430        440        450
HYVVVGAQRD AWGPGAAKSG VGTALLLKLA QMFSDMVLKD GFQPSRSIIF 
       460        470        480        490        500
ASWSAGDFGS VGATEWLEGY LSSLHLKAFT YINLDKAVLG TSNFKVSASP 
       510        520        530        540        550
LLYTLIEKTM QNVKHPVTGQ FLYQDSNWAS KVEKLTLDNA AFPFLAYSGI 
       560        570        580        590        600
PAVSFCFCED TDYPYLGTTM DTYKELIERI PELNKVARAA AEVAGQFVIK 
       610        620        630        640        650
LTHDVELNLD YERYNSQLLS FVRDLNQYRA DIKEMGLSLQ WLYSARGDFF 
       660        670        680        690        700
RATSRLTTDF GNAEKTDRFV MKKLNDRVMR VEYHFLSPYV SPKESPFRHV 
       710        720        730        740        750
FWGSGSHTLP ALLENLKLRK QNNGAFNETL FRNQLALATW TIQGAANALS 
       760
GDVWDIDNEF
Length:760
Mass (Da):84,871
Last modified:May 30, 2006 - v2
<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:iC886F14000D90154
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 are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8WBE5F8WBE5_HUMAN
Transferrin receptor protein 1
TFRC
81Annotation 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>
G3V0E5G3V0E5_HUMAN
Transferrin receptor (P90, CD71), i...
TFRC hCG_22086
679Annotation 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>
H7C3V5H7C3V5_HUMAN
Transferrin receptor protein 1
TFRC
118Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAD92491 differs from that shown. Reason: Erroneous initiation.Curated

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 conflicti104T → K AA sequence (PubMed:1871153).Curated1
Sequence conflicti109R → V AA sequence (PubMed:1871153).Curated1
Sequence conflicti123Y → T AA sequence (PubMed:1871153).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07636520Y → H in IMD46; increases protein expression; increases cell surface expression on T and B cells; increases soluble form level; impairs receptor internalization; impairs transferrin transport; impairs T and B cell proliferation as well as B cell class-switching; interacts with STEAP3; doesn't affect receptor internalization in erythroid precursor cells. 1 PublicationCorresponds to variant dbSNP:rs863225436EnsemblClinVar.1
Natural variantiVAR_012737142G → S Rare polymorphism. 3 PublicationsCorresponds to variant dbSNP:rs3817672Ensembl.1
Natural variantiVAR_051806212L → V. Corresponds to variant dbSNP:rs41301381Ensembl.1
Natural variantiVAR_051807420G → S. Corresponds to variant dbSNP:rs41295879Ensembl.1
Natural variantiVAR_051808677R → H. Corresponds to variant dbSNP:rs41298067Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X01060 mRNA Translation: CAA25527.1
M11507 mRNA Translation: AAA61153.1
AF187320 Genomic DNA Translation: AAF04564.1
AB209254 mRNA Translation: BAD92491.1 Different initiation.
DQ496099 Genomic DNA Translation: ABF47088.1
CH471191 Genomic DNA Translation: EAW53670.1
CH471191 Genomic DNA Translation: EAW53673.1
BC001188 mRNA Translation: AAH01188.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS3312.1

Protein sequence database of the Protein Information Resource

More...PIRi		A93343 JXHU

NCBI Reference Sequences

More...RefSeqi		NP_001121620.1, NM_001128148.2
NP_001300894.1, NM_001313965.1
NP_001300895.1, NM_001313966.1
NP_003225.2, NM_003234.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.529618

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000360110; ENSP00000353224; ENSG00000072274
ENST00000392396; ENSP00000376197; ENSG00000072274

Database of genes from NCBI RefSeq genomes

More...GeneIDi		7037

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:7037

UCSC genome browser

More...UCSCi		uc003fvz.5 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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01060 mRNA Translation: CAA25527.1
M11507 mRNA Translation: AAA61153.1
AF187320 Genomic DNA Translation: AAF04564.1
AB209254 mRNA Translation: BAD92491.1 Different initiation.
DQ496099 Genomic DNA Translation: ABF47088.1
CH471191 Genomic DNA Translation: EAW53670.1
CH471191 Genomic DNA Translation: EAW53673.1
BC001188 mRNA Translation: AAH01188.1
CCDSiCCDS3312.1
PIRiA93343 JXHU
RefSeqiNP_001121620.1, NM_001128148.2
NP_001300894.1, NM_001313965.1
NP_001300895.1, NM_001313966.1
NP_003225.2, NM_003234.3
UniGeneiHs.529618

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CX8X-ray3.20A/B/C/D/E/F/G/H122-760[»]
1DE4X-ray2.80C/F/I121-760[»]
1SUVelectron microscopy7.50A/B122-760[»]
2NSUelectron microscopy27.00A/B122-760[»]
3KASX-ray2.40A121-760[»]
3S9LX-ray3.22A/B120-760[»]
3S9MX-ray3.32A/B120-760[»]
3S9NX-ray3.25A/B120-760[»]
6D03electron microscopy3.68A/B121-760[»]
6D04electron microscopy3.74A/B121-760[»]
6D05electron microscopy3.80A/B121-760[»]
ProteinModelPortaliP02786
SMRiP02786
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112895, 98 interactors
CORUMiP02786
DIPiDIP-2736N
ELMiP02786
IntActiP02786, 101 interactors
MINTiP02786
STRINGi9606.ENSP00000353224

Chemistry databases

ChEMBLiCHEMBL3712860
DrugBankiDB09412 Gallium citrate Ga-67
DB05260 Gallium nitrate

Protein family/group databases

MEROPSiM28.972
TCDBi9.B.229.1.1 the transferrin receptor, cd71, (tfr) family

PTM databases

GlyConnecti607
iPTMnetiP02786
PhosphoSitePlusiP02786
SwissPalmiP02786
UniCarbKBiP02786

Polymorphism and mutation databases

BioMutaiTFRC
DMDMi108935939

Proteomic databases

EPDiP02786
jPOSTiP02786
MaxQBiP02786
PaxDbiP02786
PeptideAtlasiP02786
PRIDEiP02786
ProteomicsDBi51595

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		7037
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360110; ENSP00000353224; ENSG00000072274
ENST00000392396; ENSP00000376197; ENSG00000072274
GeneIDi7037
KEGGihsa:7037
UCSCiuc003fvz.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7037
DisGeNETi7037
EuPathDBiHostDB:ENSG00000072274.12

GeneCards: human genes, protein and diseases

More...GeneCardsi		TFRC
HGNCiHGNC:11763 TFRC
HPAiCAB000153
HPA028598
MalaCardsiTFRC
MIMi190010 gene
616740 phenotype
neXtProtiNX_P02786
OpenTargetsiENSG00000072274
Orphaneti476113 Combined immunodeficiency due to TFRC deficiency
PharmGKBiPA36478

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2195 Eukaryota
COG2234 LUCA
GeneTreeiENSGT00940000153978
HOVERGENiHBG023177
InParanoidiP02786
KOiK06503
OMAiIMKVEYH
OrthoDBi156519at2759
PhylomeDBiP02786
TreeFamiTF312981

Enzyme and pathway databases

ReactomeiR-HSA-432722 Golgi Associated Vesicle Biogenesis
R-HSA-8856825 Cargo recognition for clathrin-mediated endocytosis
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-917977 Transferrin endocytosis and recycling
SIGNORiP02786

Miscellaneous databases

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

More...ChiTaRSi		TFRC human
EvolutionaryTraceiP02786

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		TFRC

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

More...GenomeRNAii		7037

Protein Ontology

More...PROi		PR:P02786

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000072274 Expressed in 243 organ(s), highest expression level in liver
ExpressionAtlasiP02786 baseline and differential
GenevisibleiP02786 HS

Family and domain databases

CDDicd02128 PA_TfR, 1 hit
Gene3Di1.20.930.40, 1 hit
InterProiView protein in InterPro
IPR003137 PA_domain
IPR007484 Peptidase_M28
IPR039373 Peptidase_M28B
IPR029513 TfR
IPR007365 TFR-like_dimer_dom
IPR036757 TFR-like_dimer_dom_sf
IPR037324 TfR1/2_PA
PANTHERiPTHR10404 PTHR10404, 1 hit
PTHR10404:SF26 PTHR10404:SF26, 1 hit
PfamiView protein in Pfam
PF02225 PA, 1 hit
PF04389 Peptidase_M28, 1 hit
PF04253 TFR_dimer, 1 hit
SUPFAMiSSF47672 SSF47672, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<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 nameiTFR1_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: P02786
Secondary accession number(s): D3DXB0
, Q1HE24, Q59G55, Q9UCN0, Q9UCU5, Q9UDF9, Q9UK21
<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: July 21, 1986
Last sequence update: May 30, 2006
Last modified: February 13, 2019
This is version 231 of the entry and version 2 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 cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  8. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
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