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P02786

- TFR1_HUMAN

UniProt

P02786 - TFR1_HUMAN

Protein

Transferrin receptor protein 1

Gene

TFRC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 184 (01 Oct 2014)
      Sequence version 2 (30 May 2006)
      Previous versions | rss
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    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.By similarity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei100 – 1012Cleavage; by trypsin; to produce soluble form

    GO - Molecular functioni

    1. double-stranded RNA binding Source: MGI
    2. identical protein binding Source: IntAct
    3. peptidase activity Source: InterPro
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. transferrin receptor activity Source: UniProtKB

    GO - Biological processi

    1. cellular iron ion homeostasis Source: UniProtKB
    2. iron ion import Source: UniProt
    3. osteoclast differentiation Source: Ensembl
    4. positive regulation of bone resorption Source: Ensembl
    5. receptor-mediated endocytosis Source: GOC
    6. transferrin transport Source: Reactome
    7. transmembrane transport Source: Reactome
    8. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Endocytosis, Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.
    REACT_25283. Transferrin endocytosis and recycling.

    Protein family/group databases

    MEROPSiM28.972.

    Names & Taxonomyi

    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:
    Gene namesi
    Name:TFRC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:11763. TFRC.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type II membrane protein 1 Publication. Melanosome 1 Publication
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cell surface Source: UniProt
    3. coated pit Source: UniProtKB
    4. cytoplasmic membrane-bounded vesicle Source: MGI
    5. endosome Source: MGI
    6. external side of plasma membrane Source: Ensembl
    7. extracellular region Source: UniProtKB
    8. extracellular space Source: UniProt
    9. extracellular vesicular exosome Source: UniProt
    10. integral component of plasma membrane Source: ProtInc
    11. intracellular membrane-bounded organelle Source: HPA
    12. melanosome Source: UniProtKB-SubCell
    13. membrane Source: UniProtKB
    14. perinuclear region of cytoplasm Source: Ensembl
    15. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 124FSNL → YTRF: Only 80% as active as wild-type receptor.
    Mutagenesisi20 – 3415YTRFS…DGDNS → PPGYSLARQVDYTRF: No influence on endocytic uptake of the receptor. 3 PublicationsAdd
    BLAST
    Mutagenesisi20 – 234YTRF → PPGY: Only 16% as active as wild-type receptor. 3 Publications
    Mutagenesisi20 – 201Y → C: Only 35% as active as wild-type receptor. 3 Publications
    Mutagenesisi20 – 201Y → G: Only 20% as active as wild-type receptor. 3 Publications
    Mutagenesisi21 – 211T → F: Only 88% as active as wild-type receptor. 1 Publication
    Mutagenesisi21 – 211T → TA: Only 14% as active as wild-type receptor. 1 Publication
    Mutagenesisi21 – 211T → TAA: Only 19% as active as wild-type receptor. 1 Publication
    Mutagenesisi23 – 231F → Y: Only 48% as active as wild-type receptor. 1 Publication
    Mutagenesisi31 – 344GDNS → YTRF: 2-fold increase of the endocytic uptake of the receptor.
    Mutagenesisi47 – 504NADN → YTRF: 1.27-fold increase of the endocytic uptake of the receptor.
    Mutagenesisi619 – 6191L → A: 20-fold reduced affinity for transferrin receptor. No binding to HFE.
    Mutagenesisi622 – 6221V → A: No significant effect on binding to transferrin nor HFE.
    Mutagenesisi623 – 6231R → A: No significant effect on binding to transferrin nor HFE.
    Mutagenesisi629 – 6291R → A: >5-fold reduced affinity for transferrin. >10-fold reduced affinity for HFE.
    Mutagenesisi640 – 6401Q → A: No effect on binding to transferrin. >10-fold reduced affinity for HFE.
    Mutagenesisi641 – 6411W → A: No significant effect on binding to transferrin nor HFE.
    Mutagenesisi643 – 6431Y → A: 20-fold reduced affinity for transferrin. No binding to HFE.
    Mutagenesisi644 – 6441S → A: No significant effect on binding to transferrin nor HFE.
    Mutagenesisi646 – 6461R → A or H: No binding to transferrin. 1 Publication
    Mutagenesisi646 – 6461R → K: 5% binding to transferrin. 1 Publication
    Mutagenesisi647 – 6471G → A: Large effect on affinity for transferrin. 4-fold reduced affinity for HFE. 1 Publication
    Mutagenesisi648 – 6481D → A: 16% binding to transferrin. 1 Publication
    Mutagenesisi648 – 6481D → E: 57% binding to transferrin. 1 Publication
    Mutagenesisi650 – 6501F → Q: >5-fold reduced affinity for transferrin. >10-fold reduced affinity for HFE.

    Organism-specific databases

    PharmGKBiPA36478.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 760760Transferrin receptor protein 1PRO_0000174132Add
    BLAST
    Chaini101 – 760660Transferrin receptor protein 1, serum formPRO_0000292265Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201Phosphotyrosine1 Publication
    Modified residuei21 – 211Phosphothreonine1 Publication
    Modified residuei24 – 241Phosphoserine
    Lipidationi62 – 621S-palmitoyl cysteine1 Publication
    Lipidationi67 – 671S-palmitoyl cysteine
    Disulfide bondi89 – 89Interchain
    Disulfide bondi98 – 98Interchain
    Glycosylationi104 – 1041O-linked (GalNAc...)2 PublicationsCAR_000072
    Glycosylationi251 – 2511N-linked (GlcNAc...)3 Publications
    Glycosylationi317 – 3171N-linked (GlcNAc...)
    Glycosylationi727 – 7271N-linked (GlcNAc...)1 PublicationCAR_000173

    Post-translational modificationi

    N- and O-glycosylated, phosphorylated and palmitoylated. The serum form is only glycosylated.8 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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP02786.
    PaxDbiP02786.
    PeptideAtlasiP02786.
    PRIDEiP02786.

    PTM databases

    PhosphoSiteiP02786.
    UniCarbKBiP02786.

    Expressioni

    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

    ArrayExpressiP02786.
    BgeeiP02786.
    CleanExiHS_TFRC.
    GenevestigatoriP02786.

    Organism-specific databases

    HPAiCAB000153.
    HPA028598.

    Interactioni

    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 Machupo arenavirus GPC.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-355727,EBI-355727
    ALBP027682EBI-355727,EBI-714423
    SH3BP4Q9P0V36EBI-355727,EBI-1049513

    Protein-protein interaction databases

    BioGridi112895. 45 interactions.
    DIPiDIP-2736N.
    IntActiP02786. 23 interactions.
    MINTiMINT-4999032.
    STRINGi9606.ENSP00000353224.

    Structurei

    Secondary structure

    1
    760
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi124 – 13613
    Helixi140 – 1467
    Turni150 – 1523
    Helixi160 – 17617
    Beta strandi179 – 19214
    Beta strandi199 – 2046
    Turni205 – 2084
    Beta strandi209 – 2146
    Beta strandi220 – 2223
    Beta strandi226 – 2305
    Beta strandi232 – 2343
    Turni236 – 2383
    Helixi240 – 2445
    Beta strandi245 – 2484
    Beta strandi253 – 2597
    Helixi264 – 2729
    Turni273 – 2753
    Beta strandi277 – 2826
    Turni285 – 2873
    Beta strandi303 – 3064
    Beta strandi308 – 3103
    Beta strandi311 – 3133
    Helixi317 – 3193
    Beta strandi334 – 3363
    Helixi339 – 3468
    Beta strandi349 – 3524
    Helixi355 – 3573
    Beta strandi364 – 3674
    Beta strandi371 – 3777
    Beta strandi380 – 39314
    Beta strandi396 – 40813
    Beta strandi411 – 4133
    Turni416 – 4194
    Helixi420 – 43819
    Beta strandi445 – 45511
    Helixi456 – 4583
    Helixi461 – 4699
    Turni470 – 4734
    Helixi474 – 4763
    Beta strandi478 – 4836
    Beta strandi491 – 4988
    Helixi500 – 5023
    Helixi503 – 5108
    Turni516 – 5183
    Beta strandi520 – 5223
    Helixi528 – 5314
    Helixi541 – 5466
    Beta strandi552 – 5587
    Turni564 – 5674
    Helixi573 – 5797
    Helixi583 – 60321
    Beta strandi604 – 6063
    Helixi613 – 62513
    Helixi626 – 6283
    Turni629 – 6368
    Helixi640 – 66223
    Helixi668 – 68013
    Helixi682 – 6854
    Beta strandi688 – 6903
    Turni692 – 6943
    Turni700 – 7023
    Beta strandi705 – 7084
    Helixi709 – 7179
    Turni718 – 7225
    Helixi728 – 74922
    Helixi753 – 7553

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP02786.
    SMRiP02786. Positions 122-756.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02786.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6767CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini89 – 760672ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei68 – 8821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini223 – 31391PAAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 6767Mediates interaction with SH3BP4Add
    BLAST
    Regioni569 – 760192Ligand-bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi20 – 234Endocytosis signal
    Motifi58 – 614Stop-transfer sequence
    Motifi646 – 6483Cell attachment site; required for binding to transferrin

    Sequence similaritiesi

    Belongs to the peptidase M28 family. M28B subfamily.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2234.
    HOVERGENiHBG023177.
    InParanoidiP02786.
    KOiK06503.
    OMAiDNSHVEM.
    PhylomeDBiP02786.
    TreeFamiTF312981.

    Family and domain databases

    Gene3Di1.20.930.40. 1 hit.
    InterProiIPR007484. Peptidase_M28.
    IPR003137. Protease-assoc_domain.
    IPR029513. TfR.
    IPR007365. TFR-like_dimer_dom.
    [Graphical view]
    PANTHERiPTHR10404:SF26. PTHR10404:SF26. 1 hit.
    PfamiPF02225. PA. 1 hit.
    PF04389. Peptidase_M28. 1 hit.
    PF04253. TFR_dimer. 1 hit.
    [Graphical view]
    SUPFAMiSSF47672. SSF47672. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P02786-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMDQARSAFS NLFGGEPLSY TRFSLARQVD GDNSHVEMKL AVDEEENADN    50
    NTKANVTKPK RCSGSICYGT IAVIVFFLIG FMIGYLGYCK GVEPKTECER 100
    LAGTESPVRE EPGEDFPAAR RLYWDDLKRK LSEKLDSTDF TGTIKLLNEN 150
    SYVPREAGSQ KDENLALYVE NQFREFKLSK VWRDQHFVKI QVKDSAQNSV 200
    IIVDKNGRLV YLVENPGGYV AYSKAATVTG KLVHANFGTK KDFEDLYTPV 250
    NGSIVIVRAG KITFAEKVAN AESLNAIGVL IYMDQTKFPI VNAELSFFGH 300
    AHLGTGDPYT PGFPSFNHTQ FPPSRSSGLP NIPVQTISRA AAEKLFGNME 350
    GDCPSDWKTD STCRMVTSES KNVKLTVSNV LKEIKILNIF GVIKGFVEPD 400
    HYVVVGAQRD AWGPGAAKSG VGTALLLKLA QMFSDMVLKD GFQPSRSIIF 450
    ASWSAGDFGS VGATEWLEGY LSSLHLKAFT YINLDKAVLG TSNFKVSASP 500
    LLYTLIEKTM QNVKHPVTGQ FLYQDSNWAS KVEKLTLDNA AFPFLAYSGI 550
    PAVSFCFCED TDYPYLGTTM DTYKELIERI PELNKVARAA AEVAGQFVIK 600
    LTHDVELNLD YERYNSQLLS FVRDLNQYRA DIKEMGLSLQ WLYSARGDFF 650
    RATSRLTTDF GNAEKTDRFV MKKLNDRVMR VEYHFLSPYV SPKESPFRHV 700
    FWGSGSHTLP ALLENLKLRK QNNGAFNETL FRNQLALATW TIQGAANALS 750
    GDVWDIDNEF 760
    Length:760
    Mass (Da):84,871
    Last modified:May 30, 2006 - v2
    Checksum:iC886F14000D90154
    GO

    Sequence cautioni

    The sequence BAD92491.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti104 – 1041T → K AA sequence (PubMed:1871153)Curated
    Sequence conflicti109 – 1091R → V AA sequence (PubMed:1871153)Curated
    Sequence conflicti123 – 1231Y → T AA sequence (PubMed:1871153)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti142 – 1421G → S Rare polymorphism. 3 Publications
    Corresponds to variant rs3817672 [ dbSNP | Ensembl ].
    VAR_012737
    Natural varianti212 – 2121L → V.
    Corresponds to variant rs41301381 [ dbSNP | Ensembl ].
    VAR_051806
    Natural varianti420 – 4201G → S.
    Corresponds to variant rs41295879 [ dbSNP | Ensembl ].
    VAR_051807
    Natural varianti677 – 6771R → H.
    Corresponds to variant rs41298067 [ dbSNP | Ensembl ].
    VAR_051808

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_001128148.1.
    NP_003225.2. NM_003234.2.
    UniGeneiHs.529618.

    Genome annotation databases

    EnsembliENST00000360110; ENSP00000353224; ENSG00000072274.
    ENST00000392396; ENSP00000376197; ENSG00000072274.
    GeneIDi7037.
    KEGGihsa:7037.
    UCSCiuc003fvz.4. human.

    Polymorphism databases

    DMDMi108935939.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS3312.1.
    PIRi A93343. JXHU.
    RefSeqi NP_001121620.1. NM_001128148.1.
    NP_003225.2. NM_003234.2.
    UniGenei Hs.529618.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CX8 X-ray 3.20 A/B/C/D/E/F/G/H 122-760 [» ]
    1DE4 X-ray 2.80 C/F/I 121-760 [» ]
    1SUV electron microscopy 7.50 A/B 122-760 [» ]
    2NSU electron microscopy 27.00 A/B 122-760 [» ]
    3KAS X-ray 2.40 A 121-760 [» ]
    3S9L X-ray 3.22 A/B 120-760 [» ]
    3S9M X-ray 3.32 A/B 120-760 [» ]
    3S9N X-ray 3.25 A/B 120-760 [» ]
    ProteinModelPortali P02786.
    SMRi P02786. Positions 122-756.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112895. 45 interactions.
    DIPi DIP-2736N.
    IntActi P02786. 23 interactions.
    MINTi MINT-4999032.
    STRINGi 9606.ENSP00000353224.

    Protein family/group databases

    MEROPSi M28.972.

    PTM databases

    PhosphoSitei P02786.
    UniCarbKBi P02786.

    Polymorphism databases

    DMDMi 108935939.

    Proteomic databases

    MaxQBi P02786.
    PaxDbi P02786.
    PeptideAtlasi P02786.
    PRIDEi P02786.

    Protocols and materials databases

    DNASUi 7037.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360110 ; ENSP00000353224 ; ENSG00000072274 .
    ENST00000392396 ; ENSP00000376197 ; ENSG00000072274 .
    GeneIDi 7037.
    KEGGi hsa:7037.
    UCSCi uc003fvz.4. human.

    Organism-specific databases

    CTDi 7037.
    GeneCardsi GC03M195754.
    HGNCi HGNC:11763. TFRC.
    HPAi CAB000153.
    HPA028598.
    MIMi 190010. gene.
    neXtProti NX_P02786.
    PharmGKBi PA36478.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2234.
    HOVERGENi HBG023177.
    InParanoidi P02786.
    KOi K06503.
    OMAi DNSHVEM.
    PhylomeDBi P02786.
    TreeFami TF312981.

    Enzyme and pathway databases

    Reactomei REACT_19400. Golgi Associated Vesicle Biogenesis.
    REACT_25283. Transferrin endocytosis and recycling.

    Miscellaneous databases

    ChiTaRSi TFRC. human.
    EvolutionaryTracei P02786.
    GeneWikii TFRC.
    GenomeRNAii 7037.
    NextBioi 27493.
    PROi P02786.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02786.
    Bgeei P02786.
    CleanExi HS_TFRC.
    Genevestigatori P02786.

    Family and domain databases

    Gene3Di 1.20.930.40. 1 hit.
    InterProi IPR007484. Peptidase_M28.
    IPR003137. Protease-assoc_domain.
    IPR029513. TfR.
    IPR007365. TFR-like_dimer_dom.
    [Graphical view ]
    PANTHERi PTHR10404:SF26. PTHR10404:SF26. 1 hit.
    Pfami PF02225. PA. 1 hit.
    PF04389. Peptidase_M28. 1 hit.
    PF04253. TFR_dimer. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47672. SSF47672. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of human transferrin receptor deduced from the mRNA sequence."
      Schneider C., Owen M.J., Banville D., Williams J.G.
      Nature 311:675-678(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-142.
    2. "The human transferrin receptor gene: genomic organization, and the complete primary structure of the receptor deduced from a cDNA sequence."
      McClelland A., Kuhn L.C., Ruddle F.H.
      Cell 39:267-274(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-142.
    3. "Exon/intron structure of the human transferrin receptor gene."
      Evans P., Kemp J.
      Gene 199:123-131(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    4. "Molecular and evolutionary studies of the transferrin receptor."
      Wheeler D.L.
      Thesis (1999), University of Iowa, United States
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    6. NIEHS SNPs program
      Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Eye.
    9. "Serum transferrin receptor is a truncated form of tissue receptor."
      Shih Y.J., Baynes R.D., Hudson B.G., Flowers C.H., Skikne B.S., Cook J.D.
      J. Biol. Chem. 265:19077-19081(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 101-119 (STFR).
    10. "Characterization of transferrin receptor released by K562 erythroleukemia cells."
      Baynes R.D., Shih Y.J., Hudson B.G., Cook J.D.
      Proc. Soc. Exp. Biol. Med. 197:416-423(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 101-123 (STFR), CHARACTERIZATION.
      Tissue: Erythroleukemia.
    11. "Identification of a novel form of the alpha 3 integrin subunit: covalent association with transferrin receptor."
      Coppolino M., Migliorini M., Argraves W.S., Dedhar S.
      Biochem. J. 306:129-134(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 288-302; 694-708 AND 721-730.
      Tissue: Prostatic carcinoma.
    12. "Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size."
      Chicz R.M., Urban R.G., Lane W.S., Gorga J.C., Stern L.J., Vignali D.A.A., Strominger J.L.
      Nature 358:764-768(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 680-696.
    13. "Endocytosis of the transferrin receptor requires the cytoplasmic domain but not its phosphorylation site."
      Rothenberger S., Iacopetta B.J., Kuhn L.C.
      Cell 49:423-431(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Identification of the intermolecular disulfide bonds of the human transferrin receptor and its lipid-attachment site."
      Jing S., Trowbridge I.S.
      EMBO J. 6:327-331(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-62.
    15. "Intermolecular disulfide bonds are not required for the expression of the dimeric state and functional activity of the transferrin receptor."
      Alvarez E., Girones N., Davis R.J.
      EMBO J. 8:2231-2240(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYSTEINE RESIDUES INVOLVED IN INTERMOLECULAR BONDS.
    16. "A point mutation in the cytoplasmic domain of the transferrin receptor inhibits endocytosis."
      Alvarez E., Girones N., Davis R.J.
      Biochem. J. 267:31-35(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-20.
    17. "Role of the human transferrin receptor cytoplasmic domain in endocytosis: localization of a specific signal sequence for internalization."
      Jing S., Spencer T., Miller K., Hopkins C., Trowbridge I.S.
      J. Cell Biol. 110:283-294(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERNALIZATION SEQUENCE, MUTAGENESIS OF TYR-20.
    18. "Presence of O-linked oligosaccharide on a threonine residue in the human transferrin receptor."
      Do S.-I., Cummings R.D.
      Glycobiology 2:345-353(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-104.
    19. "Identification of the O-linked glycosylation site of the human transferrin receptor."
      Hayes G.R., Enns C.A., Lucas J.J.
      Glycobiology 2:355-359(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-104.
    20. "YTRF is the conserved internalization signal of the transferrin receptor, and a second YTRF signal at position 31-34 enhances endocytosis."
      Collawn J.F., Lai A., Domingo D.L., Fitch M., Hatton S., Trowbridge I.S.
      J. Biol. Chem. 268:21686-21692(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 20-TYR--PHE-23; TYR-20; THR-21 AND PHE-23.
    21. "The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide."
      Hayes G.R., Williams A., Costello C.E., Enns C.A., Lucas J.J.
      Glycobiology 5:227-232(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF CARBOHYDRATES ON ASN-727.
    22. "Functional analysis of human/chicken transferrin receptor chimeras indicates that the carboxy-terminal region is important for ligand binding."
      Buchegger F., Trowbridge I.S., Liu L.F., White S., Collawn J.F.
      Eur. J. Biochem. 235:9-17(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF LIGAND-BINDING DOMAIN.
    23. "A conserved RGD (Arg-Gly-Asp) motif in the transferrin receptor is required for binding to transferrin."
      Dubljevic V., Sali A., Goding J.W.
      Biochem. J. 341:11-14(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-646; GLY-647 AND ASP-648.
    24. "Mutational analysis of the transferrin receptor reveals overlapping HFE and transferrin binding sites."
      West A.P. Jr., Giannetti A.M., Herr A.B., Bennett M.J., Nangiana J.S., Pierce J.R., Weiner L.P., Snow P.M., Bjorkman P.J.
      J. Mol. Biol. 313:385-397(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    25. "TTP specifically regulates the internalization of the transferrin receptor."
      Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P., Tacchetti C., Di Fiore P.P.
      Cell 123:875-888(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SH3BP4.
    26. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-251.
      Tissue: Plasma.
    27. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    29. "Transferrin receptor 1 is a cellular receptor for New World haemorrhagic fever arenaviruses."
      Radoshitzky S.R., Abraham J., Spiropoulou C.F., Kuhn J.H., Nguyen D., Li W., Nagel J., Schmidt P.J., Nunberg J.H., Andrews N.C., Farzan M., Choe H.
      Nature 446:92-96(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MACHUPO ARENAVIRUS PROTEIN GPC.
    30. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    31. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-251 AND ASN-727.
      Tissue: Liver.
    32. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-251.
      Tissue: Leukemic T-cell.
    33. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    34. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "Structural model of phospholipid-reconstituted human transferrin receptor derived by electron microscopy."
      Fuchs H., Luecken W., Tauber R., Engel A.
      Structure 6:1235-1243(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ELECTRON MICROSCOPY.
    37. "Crystal structure of the ectodomain of human transferrin receptor."
      Lawrence C.M., Ray S., Babyonyshev M., Galluser R., Borhani D.W., Harrison S.C.
      Science 286:779-782(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 121-760.
    38. "Identification of 96 single nucleotide polymorphisms in eight genes involved in iron metabolism: efficiency of bioinformatic extraction compared with a systematic sequencing approach."
      Douabin-Gicquel V., Soriano N., Ferran H., Wojcik F., Palierne E., Tamim S., Jovelin T., McKie A.T., Le Gall J.-Y., David V., Mosser J.
      Hum. Genet. 109:393-401(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SER-142.

    Entry informationi

    Entry nameiTFR1_HUMAN
    AccessioniPrimary (citable) accession number: P02786
    Secondary accession number(s): D3DXB0
    , Q1HE24, Q59G55, Q9UCN0, Q9UCU5, Q9UDF9, Q9UK21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 184 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    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.

    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. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. Peptidase families
      Classification of peptidase families and list of entries
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3