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P02786

- TFR1_HUMAN

UniProt

P02786 - TFR1_HUMAN

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Protein

Transferrin receptor protein 1

Gene

TFRC

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

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. poly(A) RNA binding Source: UniProtKB
  4. 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. transferrin transport Source: Reactome
  6. transmembrane transport Source: Reactome
  7. viral process Source: UniProtKB-KW
Complete GO annotation...

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. membrane Source: UniProtKB
  13. perinuclear region of cytoplasm Source: Ensembl
  14. plasma membrane Source: Reactome
  15. recycling endosome Source: MGI
  16. vesicle Source: UniProtKB
Complete GO annotation...

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. Add
BLAST
Mutagenesisi20 – 234YTRF → PPGY: Only 16% as active as wild-type receptor. 1 Publication
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

BgeeiP02786.
CleanExiHS_TFRC.
ExpressionAtlasiP02786. baseline and differential.
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. 48 interactions.
DIPiDIP-2736N.
IntActiP02786. 27 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.
GeneTreeiENSGT00550000074421.
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

        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
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. 48 interactions.
DIPi DIP-2736N.
IntActi P02786. 27 interactions.
MINTi MINT-4999032.
STRINGi 9606.ENSP00000353224.

Chemistry

DrugBanki DB05260. Gallium nitrate.

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.
GeneTreei ENSGT00550000074421.
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

Bgeei P02786.
CleanExi HS_TFRC.
ExpressionAtlasi P02786. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 185 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