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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-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. 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

GO - Molecular functioni

  • double-stranded RNA binding Source: MGI
  • glycoprotein binding Source: BHF-UCL
  • poly(A) RNA binding Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL
  • transferrin receptor activity Source: UniProtKB
  • transferrin transmembrane transporter activity Source: UniProtKB
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  • cellular iron ion homeostasis Source: UniProtKB
  • cellular response to drug Source: MGI
  • iron ion import Source: UniProtKB
  • osteoclast differentiation Source: Ensembl
  • positive regulation of B cell proliferation Source: UniProtKB
  • positive regulation of bone resorption Source: Ensembl
  • positive regulation of isotype switching Source: UniProtKB
  • positive regulation of T cell proliferation Source: UniProtKB
  • receptor internalization Source: UniProtKB
  • transferrin transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Receptor

Keywords - Biological processi

Endocytosis, Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:ENSG00000072274-MONOMER.
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.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:11763. TFRC.

Subcellular locationi

Transferrin receptor protein 1, serum form :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 67CytoplasmicSequence analysisAdd BLAST67
Transmembranei68 – 88Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini89 – 760ExtracellularSequence analysisAdd BLAST672

GO - Cellular componenti

  • basolateral plasma membrane Source: BHF-UCL
  • blood microparticle Source: UniProtKB
  • cell surface Source: UniProtKB
  • clathrin-coated pit Source: UniProtKB
  • cytoplasmic, membrane-bounded vesicle Source: MGI
  • endosome Source: MGI
  • external side of plasma membrane Source: BHF-UCL
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • extracellular vesicle Source: UniProtKB
  • HFE-transferrin receptor complex Source: BHF-UCL
  • integral component of plasma membrane Source: BHF-UCL
  • intracellular membrane-bounded organelle Source: HPA
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • perinuclear region of cytoplasm Source: CACAO
  • plasma membrane Source: Reactome
  • recycling endosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

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
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 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi7037.
MIMi616740. phenotype.
OpenTargetsiENSG00000072274.
PharmGKBiPA36478.

Chemistry databases

DrugBankiDB05260. Gallium nitrate.

Polymorphism and mutation databases

BioMutaiTFRC.
DMDMi108935939.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001741321 – 760Transferrin receptor protein 1Add BLAST760
ChainiPRO_0000292265101 – 760Transferrin receptor protein 1, serum formAdd BLAST660

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei10PhosphoserineCombined sources1
Modified residuei19PhosphoserineBy similarity1
Modified residuei20PhosphotyrosineCombined sources1
Modified residuei21PhosphothreonineCombined sources1
Modified residuei24Phosphoserine1 Publication1
Lipidationi62S-palmitoyl cysteine1 Publication1
Lipidationi67S-palmitoyl cysteine1
Disulfide bondi89Interchain
Disulfide bondi98Interchain
GlycosylationiCAR_000072104O-linked (GalNAc...)2 Publications1
Glycosylationi251N-linked (GlcNAc...)Combined sources4 Publications1
Glycosylationi317N-linked (GlcNAc...)Combined sources1 Publication1
GlycosylationiCAR_000173727N-linked (GlcNAc...)Combined sources2 Publications1

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDiP02786.
MaxQBiP02786.
PaxDbiP02786.
PeptideAtlasiP02786.
PRIDEiP02786.

PTM databases

iPTMnetiP02786.
PhosphoSitePlusiP02786.
SwissPalmiP02786.
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

BgeeiENSG00000072274.
CleanExiHS_TFRC.
ExpressionAtlasiP02786. baseline and differential.
GenevisibleiP02786. HS.

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 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

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-355727,EBI-355727
ALBP027682EBI-355727,EBI-714423
HFEQ302013EBI-355727,EBI-1028850
SGTAO437653EBI-355727,EBI-347996
SH3BP4Q9P0V36EBI-355727,EBI-1049513

GO - Molecular functioni

  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi112895. 82 interactors.
DIPiDIP-2736N.
IntActiP02786. 58 interactors.
MINTiMINT-4999032.
STRINGi9606.ENSP00000353224.

Structurei

Secondary structure

1760
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi124 – 136Combined sources13
Helixi140 – 146Combined sources7
Turni150 – 152Combined sources3
Helixi160 – 176Combined sources17
Beta strandi179 – 192Combined sources14
Beta strandi199 – 204Combined sources6
Turni205 – 208Combined sources4
Beta strandi209 – 214Combined sources6
Beta strandi220 – 222Combined sources3
Beta strandi226 – 230Combined sources5
Beta strandi232 – 234Combined sources3
Turni236 – 238Combined sources3
Helixi240 – 244Combined sources5
Beta strandi245 – 248Combined sources4
Beta strandi253 – 259Combined sources7
Helixi264 – 272Combined sources9
Turni273 – 275Combined sources3
Beta strandi277 – 282Combined sources6
Turni285 – 287Combined sources3
Beta strandi303 – 306Combined sources4
Beta strandi308 – 310Combined sources3
Beta strandi311 – 313Combined sources3
Helixi317 – 319Combined sources3
Beta strandi334 – 336Combined sources3
Helixi339 – 346Combined sources8
Beta strandi349 – 352Combined sources4
Helixi355 – 357Combined sources3
Beta strandi364 – 367Combined sources4
Beta strandi371 – 377Combined sources7
Beta strandi380 – 393Combined sources14
Beta strandi396 – 408Combined sources13
Beta strandi411 – 413Combined sources3
Turni416 – 419Combined sources4
Helixi420 – 438Combined sources19
Beta strandi445 – 455Combined sources11
Helixi456 – 458Combined sources3
Helixi461 – 469Combined sources9
Turni470 – 473Combined sources4
Helixi474 – 476Combined sources3
Beta strandi478 – 483Combined sources6
Beta strandi491 – 498Combined sources8
Helixi500 – 502Combined sources3
Helixi503 – 510Combined sources8
Turni516 – 518Combined sources3
Beta strandi520 – 522Combined sources3
Helixi528 – 531Combined sources4
Helixi541 – 546Combined sources6
Beta strandi552 – 558Combined sources7
Turni564 – 567Combined sources4
Helixi573 – 579Combined sources7
Helixi583 – 603Combined sources21
Beta strandi604 – 606Combined sources3
Helixi613 – 625Combined sources13
Helixi626 – 628Combined sources3
Turni629 – 636Combined sources8
Helixi640 – 662Combined sources23
Helixi668 – 680Combined sources13
Helixi682 – 685Combined sources4
Beta strandi688 – 690Combined sources3
Turni692 – 694Combined sources3
Turni700 – 702Combined sources3
Beta strandi705 – 708Combined sources4
Helixi709 – 717Combined sources9
Turni718 – 722Combined sources5
Helixi728 – 749Combined sources22
Helixi753 – 755Combined sources3

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[»]
ProteinModelPortaliP02786.
SMRiP02786.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02786.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini223 – 313PAAdd BLAST91

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 67Mediates interaction with SH3BP41 PublicationAdd BLAST67
Regioni569 – 760Ligand-bindingAdd BLAST192

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi20 – 23Endocytosis signal4
Motifi58 – 61Stop-transfer sequence4
Motifi646 – 648Cell attachment site; required for binding to transferrin3

Sequence similaritiesi

Belongs to the peptidase M28 family. M28B subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2195. Eukaryota.
COG2234. LUCA.
GeneTreeiENSGT00550000074421.
HOVERGENiHBG023177.
InParanoidiP02786.
KOiK06503.
OMAiDNSHVEM.
OrthoDBiEOG091G02ZM.
PhylomeDBiP02786.
TreeFamiTF312981.

Family and domain databases

Gene3Di1.20.930.40. 1 hit.
InterProiIPR003137. PA_domain.
IPR007484. Peptidase_M28.
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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 Publication1
Natural variantiVAR_012737142G → S Rare polymorphism. 3 PublicationsCorresponds to variant rs3817672dbSNPEnsembl.1
Natural variantiVAR_051806212L → V.Corresponds to variant rs41301381dbSNPEnsembl.1
Natural variantiVAR_051807420G → S.Corresponds to variant rs41295879dbSNPEnsembl.1
Natural variantiVAR_051808677R → H.Corresponds to variant rs41298067dbSNPEnsembl.1

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.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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[»]
ProteinModelPortaliP02786.
SMRiP02786.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112895. 82 interactors.
DIPiDIP-2736N.
IntActiP02786. 58 interactors.
MINTiMINT-4999032.
STRINGi9606.ENSP00000353224.

Chemistry databases

DrugBankiDB05260. Gallium nitrate.

Protein family/group databases

MEROPSiM28.972.

PTM databases

iPTMnetiP02786.
PhosphoSitePlusiP02786.
SwissPalmiP02786.
UniCarbKBiP02786.

Polymorphism and mutation databases

BioMutaiTFRC.
DMDMi108935939.

Proteomic databases

EPDiP02786.
MaxQBiP02786.
PaxDbiP02786.
PeptideAtlasiP02786.
PRIDEiP02786.

Protocols and materials databases

DNASUi7037.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7037.
DisGeNETi7037.
GeneCardsiTFRC.
HGNCiHGNC:11763. TFRC.
HPAiCAB000153.
HPA028598.
MIMi190010. gene.
616740. phenotype.
neXtProtiNX_P02786.
OpenTargetsiENSG00000072274.
PharmGKBiPA36478.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2195. Eukaryota.
COG2234. LUCA.
GeneTreeiENSGT00550000074421.
HOVERGENiHBG023177.
InParanoidiP02786.
KOiK06503.
OMAiDNSHVEM.
OrthoDBiEOG091G02ZM.
PhylomeDBiP02786.
TreeFamiTF312981.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000072274-MONOMER.
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

ChiTaRSiTFRC. human.
EvolutionaryTraceiP02786.
GeneWikiiTFRC.
GenomeRNAii7037.
PROiP02786.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000072274.
CleanExiHS_TFRC.
ExpressionAtlasiP02786. baseline and differential.
GenevisibleiP02786. HS.

Family and domain databases

Gene3Di1.20.930.40. 1 hit.
InterProiIPR003137. PA_domain.
IPR007484. Peptidase_M28.
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.
ProtoNetiSearch...

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: November 30, 2016
This is version 208 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.