P02786 (TFR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Transferrin receptor protein 1, serum form
   Short name=sTfR

Gene names

Name:

TFRC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	760 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.13
Subunit structure	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. Ref.25 Ref.29
Subcellular location	Cell membrane; Single-pass type II membrane protein. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.28 Transferrin receptor protein 1, serum form: Secreted Ref.28.
Induction	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.
Post-translational modification	N- and O-glycosylated, phosphorylated and palmitoylated. The serum form is only glycosylated. 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. Ref.14
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.
Sequence similarities	Belongs to the peptidase M28 family. M28B subfamily. Contains 1 PA (protease associated) domain.
Sequence caution	The sequence BAD92491.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Endocytosis Host-virus interaction
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular iron ion homeostasis Non-traceable author statement Ref.10. Source: UniProtKB osteoclast differentiation Inferred from electronic annotation. Source: Compara positive regulation of bone resorption Inferred from electronic annotation. Source: Compara proteolysis Inferred from electronic annotation. Source: InterPro transferrin transport Traceable author statement. Source: Reactome transmembrane transport Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	coated pit Inferred from direct assay PubMed 12857860. Source: UniProtKB cytoplasmic membrane-bounded vesicle Inferred from direct assay PubMed 15229288. Source: MGI endosome Inferred from direct assay PubMed 14612438. Source: MGI external side of plasma membrane Inferred from electronic annotation. Source: Compara extracellular region Inferred from direct assay Ref.10. Source: UniProtKB extracellular vesicular exosome Inferred from electronic annotation. Source: Compara integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	peptidase activity Inferred from electronic annotation. Source: InterPro transferrin receptor activity Non-traceable author statement Ref.10. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 760

760

Transferrin receptor protein 1

PRO_0000174132

Chain

101 – 760

660

Transferrin receptor protein 1, serum form

PRO_0000292265

Regions

Topological domain

1 – 67

67

Cytoplasmic Potential

Transmembrane

68 – 88

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

89 – 760

672

Extracellular Potential

Domain

223 – 313

91

PA

Region

1 – 67

67

Mediates interaction with SH3BP4

Region

569 – 760

192

Ligand-binding

Motif

20 – 23

4

Endocytosis signal

Motif

58 – 61

4

Stop-transfer sequence

Motif

646 – 648

3

Cell attachment site; required for binding to transferrin

Sites

Site

100 – 101

2

Cleavage; by trypsin; to produce soluble form

Amino acid modifications

Modified residue

20

1

Phosphotyrosine Ref.34

Modified residue

21

1

Phosphothreonine Ref.30

Modified residue

24

1

Phosphoserine

Lipidation

62

1

S-palmitoyl cysteine Ref.14

Lipidation

67

1

S-palmitoyl cysteine

Glycosylation

104

1

O-linked (GalNAc...) Ref.18 Ref.19

CAR_000072

Glycosylation

251

1

N-linked (GlcNAc...) Ref.26 Ref.31 Ref.32

Glycosylation

317

1

N-linked (GlcNAc...)

Glycosylation

727

1

N-linked (GlcNAc...) Ref.31

CAR_000173

Disulfide bond

89

Interchain

Disulfide bond

98

Interchain

Natural variations

Natural variant

142

1

G → S Rare polymorphism. Ref.1 Ref.2 Ref.38
Corresponds to variant rs3817672 [ dbSNP | Ensembl ].

VAR_012737

Natural variant

212

1

L → V.
Corresponds to variant rs41301381 [ dbSNP | Ensembl ].

VAR_051806

Natural variant

420

1

G → S.
Corresponds to variant rs41295879 [ dbSNP | Ensembl ].

VAR_051807

Natural variant

677

1

R → H.
Corresponds to variant rs41298067 [ dbSNP | Ensembl ].

VAR_051808

Experimental info

Mutagenesis

9 – 12

4

FSNL → YTRF: Only 80% as active as wild-type receptor. Ref.15

Mutagenesis

20 – 34

15

YTRFS…DGDNS → PPGYSLARQVDYTRF: No influence on endocytic uptake of the receptor. Ref.15 Ref.16 Ref.17 Ref.20

Mutagenesis

20 – 23

4

YTRF → PPGY: Only 16% as active as wild-type receptor. Ref.15 Ref.16 Ref.17 Ref.20

Mutagenesis

20

1

Y → C: Only 35% as active as wild-type receptor. Ref.15 Ref.16 Ref.17 Ref.20

Mutagenesis

20

1

Y → G: Only 20% as active as wild-type receptor. Ref.15 Ref.16 Ref.17 Ref.20

Mutagenesis

21

1

T → F: Only 88% as active as wild-type receptor. Ref.15 Ref.20

Mutagenesis

21

1

T → TA: Only 14% as active as wild-type receptor. Ref.15 Ref.20

Mutagenesis

21

1

T → TAA: Only 19% as active as wild-type receptor. Ref.15 Ref.20

Mutagenesis

23

1

F → Y: Only 48% as active as wild-type receptor. Ref.15 Ref.20

Mutagenesis

31 – 34

4

GDNS → YTRF: 2-fold increase of the endocytic uptake of the receptor. Ref.15

Mutagenesis

47 – 50

4

NADN → YTRF: 1.27-fold increase of the endocytic uptake of the receptor. Ref.15

Mutagenesis

619

1

L → A: 20-fold reduced affinity for transferrin receptor. No binding to HFE. Ref.15

Mutagenesis

622

1

V → A: No significant effect on binding to transferrin nor HFE. Ref.15

Mutagenesis

623

1

R → A: No significant effect on binding to transferrin nor HFE. Ref.15

Mutagenesis

629

1

R → A: >5-fold reduced affinity for transferrin. >10-fold reduced affinity for HFE. Ref.15

Mutagenesis

640

1

Q → A: No effect on binding to transferrin. >10-fold reduced affinity for HFE. Ref.15

Mutagenesis

641

1

W → A: No significant effect on binding to transferrin nor HFE. Ref.15

Mutagenesis

643

1

Y → A: 20-fold reduced affinity for transferrin. No binding to HFE. Ref.15

Mutagenesis

644

1

S → A: No significant effect on binding to transferrin nor HFE. Ref.15

Mutagenesis

646

1

R → A or H: No binding to transferrin. Ref.15 Ref.23

Mutagenesis

646

1

R → K: 5% binding to transferrin. Ref.15 Ref.23

Mutagenesis

647

1

G → A: Large effect on affinity for transferrin. 4-fold reduced affinity for HFE. Ref.15 Ref.23

Mutagenesis

648

1

D → A: 16% binding to transferrin. Ref.15 Ref.23

Mutagenesis

648

1

D → E: 57% binding to transferrin. Ref.15 Ref.23

Mutagenesis

650

1

F → Q: >5-fold reduced affinity for transferrin. >10-fold reduced affinity for HFE. Ref.15

Sequence conflict

104

1

T → K AA sequence Ref.10

Sequence conflict

109

1

R → V AA sequence Ref.10

Sequence conflict

123

1

Y → T AA sequence Ref.10

Secondary structure

1

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760

Helix Strand Turn

Details...

Helix

124 – 136

13

Helix

140 – 146

7

Turn

150 – 152

3

Helix

160 – 176

17

Beta strand

179 – 192

14

Beta strand

199 – 204

6

Turn

205 – 208

4

Beta strand

209 – 214

6

Beta strand

220 – 222

3

Beta strand

226 – 230

5

Beta strand

232 – 234

3

Turn

236 – 238

3

Helix

240 – 244

5

Beta strand

245 – 248

4

Beta strand

253 – 259

7

Helix

264 – 272

9

Turn

273 – 275

3

Beta strand

277 – 282

6

Turn

285 – 287

3

Beta strand

303 – 306

4

Beta strand

308 – 310

3

Beta strand

311 – 313

3

Helix

317 – 319

3

Beta strand

334 – 336

3

Helix

339 – 346

8

Beta strand

349 – 352

4

Helix

355 – 357

3

Beta strand

364 – 367

4

Beta strand

371 – 377

7

Beta strand

380 – 393

14

Beta strand

396 – 408

13

Beta strand

411 – 413

3

Turn

416 – 419

4

Helix

420 – 438

19

Beta strand

445 – 455

11

Helix

456 – 458

3

Helix

461 – 469

9

Turn

470 – 473

4

Helix

474 – 476

3

Beta strand

478 – 483

6

Beta strand

491 – 498

8

Helix

500 – 502

3

Helix

503 – 510

8

Turn

516 – 518

3

Beta strand

520 – 522

3

Helix

528 – 531

4

Helix

541 – 546

6

Beta strand

552 – 558

7

Turn

564 – 567

4

Helix

573 – 579

7

Helix

583 – 603

21

Beta strand

604 – 606

3

Helix

613 – 625

13

Helix

626 – 628

3

Turn

629 – 636

8

Helix

640 – 662

23

Helix

668 – 680

13

Helix

682 – 685

4

Beta strand

688 – 690

3

Turn

692 – 694

3

Turn

700 – 702

3

Beta strand

705 – 708

4

Helix

709 – 717

9

Turn

718 – 722

5

Helix

728 – 749

22

Helix

753 – 755

3

Sequences

	Sequence		Length	Mass (Da)
	P02786 [UniParc]. Last modified May 30, 2006. Version 2. Checksum: C886F14000D90154	FASTA	760	84,871
	10 20 30 40 50 60 MMDQARSAFS NLFGGEPLSY TRFSLARQVD GDNSHVEMKL AVDEEENADN NTKANVTKPK 70 80 90 100 110 120 RCSGSICYGT IAVIVFFLIG FMIGYLGYCK GVEPKTECER LAGTESPVRE EPGEDFPAAR 130 140 150 160 170 180 RLYWDDLKRK LSEKLDSTDF TGTIKLLNEN SYVPREAGSQ KDENLALYVE NQFREFKLSK 190 200 210 220 230 240 VWRDQHFVKI QVKDSAQNSV IIVDKNGRLV YLVENPGGYV AYSKAATVTG KLVHANFGTK 250 260 270 280 290 300 KDFEDLYTPV NGSIVIVRAG KITFAEKVAN AESLNAIGVL IYMDQTKFPI VNAELSFFGH 310 320 330 340 350 360 AHLGTGDPYT PGFPSFNHTQ FPPSRSSGLP NIPVQTISRA AAEKLFGNME GDCPSDWKTD 370 380 390 400 410 420 STCRMVTSES KNVKLTVSNV LKEIKILNIF GVIKGFVEPD HYVVVGAQRD AWGPGAAKSG 430 440 450 460 470 480 VGTALLLKLA QMFSDMVLKD GFQPSRSIIF ASWSAGDFGS VGATEWLEGY LSSLHLKAFT 490 500 510 520 530 540 YINLDKAVLG TSNFKVSASP LLYTLIEKTM QNVKHPVTGQ FLYQDSNWAS KVEKLTLDNA 550 560 570 580 590 600 AFPFLAYSGI PAVSFCFCED TDYPYLGTTM DTYKELIERI PELNKVARAA AEVAGQFVIK 610 620 630 640 650 660 LTHDVELNLD YERYNSQLLS FVRDLNQYRA DIKEMGLSLQ WLYSARGDFF RATSRLTTDF 670 680 690 700 710 720 GNAEKTDRFV MKKLNDRVMR VEYHFLSPYV SPKESPFRHV FWGSGSHTLP ALLENLKLRK 730 740 750 760 QNNGAFNETL FRNQLALATW TIQGAANALS GDVWDIDNEF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY. 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]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. 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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[35]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00022462.

PIR

JXHU. A93343.

RefSeq

NP_001121620.1. NM_001128148.1.
NP_003225.2. NM_003234.2.

UniGene

Hs.529618.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P02786.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2736N.

IntAct

P02786. 11 interactions.

MINT

MINT-4999032.

STRING

9606.ENSP00000353224.

Protein family/group databases

MEROPS

M28.972.

PTM databases

GlycoSuiteDB

P02786.

PhosphoSite

P02786.

Polymorphism databases

DMDM

108935939.

Proteomic databases

PaxDb

P02786.

PeptideAtlas

P02786.

PRIDE

P02786.

Protocols and materials databases

DNASU

7037.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000360110; ENSP00000353224; ENSG00000072274.
ENST00000392396; ENSP00000376197; ENSG00000072274.

GeneID

7037.

KEGG

hsa:7037.

UCSC

uc003fvz.4. human.

Organism-specific databases

CTD

7037.

GeneCards

GC03M195754.

HGNC

HGNC:11763. TFRC.

HPA

CAB000153.
HPA028598.

MIM

190010. gene.

neXtProt

NX_P02786.

PharmGKB

PA36478.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2234.

HOVERGEN

HBG023177.

InParanoid

P02786.

KO

K06503.

OMA

YVAYSKA.

OrthoDB

EOG41C6VQ.

PhylomeDB

P02786.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3bpathway. FOXA2 and FOXA3 transcription factor networks.
hif1_tfpathway. HIF-1-alpha transcription factor network.

Reactome

REACT_11123. Membrane Trafficking.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpress

P02786.

Bgee

P02786.

CleanEx

HS_TFRC.

Genevestigator

P02786.

GermOnline

ENSG00000072274. Homo sapiens.

Family and domain databases

Gene3D

1.20.930.40. 1 hit.

InterPro

IPR007484. Peptidase_M28.
IPR003137. Protease-assoc_domain.
IPR007365. TFR-like_dimer_dom.
[Graphical view]

Pfam

PF02225. PA. 1 hit.
PF04389. Peptidase_M28. 1 hit.
PF04253. TFR_dimer. 1 hit.
[Graphical view]

SUPFAM

SSF47672. Transferrin_rcpt-like_dimerise. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

TFRC. human.

EvolutionaryTrace

P02786.

GenomeRNAi

7037.

NextBio

27493.

SOURCE

Search...

Entry information

Entry name

TFR1_HUMAN

Accession

Primary (citable) accession number: P02786
Secondary accession number(s): D3DXB0 , Q1HE24, Q59G55, Q9UCN0, Q9UCU5, Q9UDF9, Q9UK21

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	May 30, 2006
Last modified:	May 1, 2013
This is version 169 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.