HUMAN:TFR1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	TFRC
Protein Name(s)	Transferrin receptor protein 1 TR TfR TfR1 Trfr T9 p90 Transferrin receptor protein 1, serum form sTfR
External Links
UniProt	P02786
EMBL	X01060 M11507 AF187320 AB209254 DQ496099 CH471191 CH471191 BC001188
CCDS	CCDS3312.1
PIR	A93343
RefSeq	NP_001121620.1 NP_003225.2
UniGene	Hs.529618
PDB	1CX8 1DE4 1SUV 2NSU 3KAS 3S9L 3S9M 3S9N
PDBsum	1CX8 1DE4 1SUV 2NSU 3KAS 3S9L 3S9M 3S9N
ProteinModelPortal	P02786
SMR	P02786
BioGrid	112895
DIP	DIP-2736N
IntAct	P02786
MINT	MINT-4999032
STRING	9606.ENSP00000353224
DrugBank	DB05260
MEROPS	M28.972
PhosphoSite	P02786
UniCarbKB	P02786
DMDM	108935939
MaxQB	P02786
PaxDb	P02786
PeptideAtlas	P02786
PRIDE	P02786
DNASU	7037
Ensembl	ENST00000360110 ENST00000392396
GeneID	7037
KEGG	hsa:7037
UCSC	uc003fvz.4
CTD	7037
GeneCards	GC03M195754
HGNC	HGNC:11763
HPA	CAB000153 HPA028598
MIM	190010
neXtProt	NX_P02786
PharmGKB	PA36478
eggNOG	COG2234
GeneTree	ENSGT00550000074421
HOVERGEN	HBG023177
InParanoid	P02786
KO	K06503
OMA	DNSHVEM
PhylomeDB	P02786
TreeFam	TF312981
Reactome	REACT_19400 REACT_25283
ChiTaRS	TFRC
EvolutionaryTrace	P02786
GeneWiki	TFRC
GenomeRNAi	7037
NextBio	27493
PRO	PR:P02786
Proteomes	UP000005640
Bgee	P02786
CleanEx	HS_TFRC
ExpressionAtlas	P02786
Genevestigator	P02786
GO	GO:0072562 GO:0009986 GO:0005905 GO:0016023 GO:0005768 GO:0009897 GO:0005576 GO:0005615 GO:0070062 GO:0005887 GO:0043231 GO:0042470 GO:0016020 GO:0048471 GO:0005886 GO:0055037 GO:0031982 GO:0003725 GO:0042802 GO:0044822 GO:0004998 GO:0006879 GO:0097286 GO:0030316 GO:0045780 GO:0033572 GO:0055085 GO:0016032
Gene3D	1.20.930.40
InterPro	IPR007484 IPR003137 IPR029513 IPR007365
PANTHER	PTHR10404:SF26
Pfam	PF02225 PF04389 PF04253
SUPFAM	SSF47672

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0048471	perinuclear region of cytoplasm	PMID:20202662^[1]	ECO:0000314			C		Fig. 2C	complete CACAO 2403
involved_in	GO:0042102	positive regulation of T cell proliferation	PMID:26642240^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030890	positive regulation of B cell proliferation	PMID:26642240^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045830	positive regulation of isotype switching	PMID:26642240^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031623	receptor internalization	PMID:26642240^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004998	transferrin receptor activity	PMID:26642240^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0033572	transferrin transport	PMID:26642240^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:16380373^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0010008	endosome membrane	PMID:16380373^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1990712	HFE-transferrin receptor complex	PMID:9465039^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0033572	transferrin transport	PMID:18353247^[5]	ECO:0000305	curator inference used in manual assertion	GO:0005515	P		Seeded From UniProt	complete
enables	GO:0004998	transferrin receptor activity	PMID:18353247^[5]	ECO:0000305	curator inference used in manual assertion	GO:0005515	F		Seeded From UniProt	complete
part_of	GO:1990712	HFE-transferrin receptor complex	PMID:9990067^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	occurs_in:(UBERON:0002114)	Seeded From UniProt	complete
part_of	GO:0016323	basolateral plasma membrane	PMID:9990067^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:1000338)	Seeded From UniProt	complete
part_of	GO:0005887	integral component of plasma membrane	PMID:18353247^[5]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P61769,UniProtKB:Q30201	C		Seeded From UniProt	complete
part_of	GO:0009897	external side of plasma membrane	PMID:18353247^[5]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P61769,UniProtKB:Q30201	C		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:9546397^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02786	F		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:20202662^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0055037	recycling endosome	PMID:24561039^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	exists_during:(GO:0000087)	Seeded From UniProt	complete
part_of	GO:1903561	extracellular vesicle	PMID:24769233^[9]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001359)	Seeded From UniProt	complete
involved_in	GO:0006826	iron ion transport	PMID:7556058^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0072562	blood microparticle	PMID:22516433^[11]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[12]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
NOT\|involved_in	GO:0042127	regulation of cell population proliferation	PMID:7556058^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:7556058^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:22664934^[13]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001827)	Seeded From UniProt	complete
NOT\|involved_in	GO:0001558	regulation of cell growth	PMID:7556058^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:1990712	HFE-transferrin receptor complex	PMID:9546397^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[14]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:1871153^[15]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006879	cellular iron ion homeostasis	PMID:1871153^[15]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005905	clathrin-coated pit	PMID:12857860^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:1871153^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004998	transferrin receptor activity	PMID:1871153^[15]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0055037	recycling endosome	PMID:22456507^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0035690	cellular response to drug	PMID:16254249^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0031410	cytoplasmic vesicle	PMID:15229288^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005768	endosome	PMID:14612438^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003725	double-stranded RNA binding	PMID:21266579^[21]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:29302006^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02786	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23384347^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02786	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20208545^[24]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02786	F		Seeded From UniProt	complete
involved_in	GO:0046718	viral entry into host cell	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0001618	P		Seeded From UniProt	complete
involved_in	GO:1990830	cellular response to leukemia inhibitory factor	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62351 ensembl:ENSMUSP00000023486	P		Seeded From UniProt	complete
part_of	GO:1990712	HFE-transferrin receptor complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62351 ensembl:ENSMUSP00000023486	C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62351 ensembl:ENSMUSP00000023486	C		Seeded From UniProt	complete
part_of	GO:0055037	recycling endosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62351 ensembl:ENSMUSP00000023486	C		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62351 ensembl:ENSMUSP00000023486	C		Seeded From UniProt	complete
involved_in	GO:0045780	positive regulation of bone resorption	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62351 ensembl:ENSMUSP00000023486	P		Seeded From UniProt	complete
involved_in	GO:0030316	osteoclast differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62351 ensembl:ENSMUSP00000023486	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62351 ensembl:ENSMUSP00000023486	C		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62351 ensembl:ENSMUSP00000023486	C		Seeded From UniProt	complete
part_of	GO:0009897	external side of plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62351 ensembl:ENSMUSP00000023486	C		Seeded From UniProt	complete
involved_in	GO:0006879	cellular iron ion homeostasis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62351 ensembl:ENSMUSP00000023486	P		Seeded From UniProt	complete
part_of	GO:0005905	clathrin-coated pit	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62351 ensembl:ENSMUSP00000023486	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62351 ensembl:ENSMUSP00000023486	C		Seeded From UniProt	complete
part_of	GO:0005769	early endosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62351 ensembl:ENSMUSP00000023486	C		Seeded From UniProt	complete
part_of	GO:0005768	endosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62351 ensembl:ENSMUSP00000023486	C		Seeded From UniProt	complete
enables	GO:0004998	transferrin receptor activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR029513	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR029513	C		Seeded From UniProt	complete
involved_in	GO:0006879	cellular iron ion homeostasis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR029513	P		Seeded From UniProt	complete
involved_in	GO:0006898	receptor-mediated endocytosis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR029513	P		Seeded From UniProt	complete
enables	GO:0033570	transferrin transmembrane transporter activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR037324	F		Seeded From UniProt	complete
involved_in	GO:0033572	transferrin transport	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR029513 InterPro:IPR037324	P		Seeded From UniProt	complete
involved_in	GO:0006879	cellular iron ion homeostasis	PMID:10192390^[25]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005887	integral component of plasma membrane	PMID:6090955^[26]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005768	endosome	PMID:8394993^[27]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004998	transferrin receptor activity	PMID:10192390^[25]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0061024	membrane organization	Reactome:R-HSA-199991	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0033572	transferrin transport	Reactome:R-HSA-917977	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030665	clathrin-coated vesicle membrane	Reactome:R-HSA-8871194 Reactome:R-HSA-8871193 Reactome:R-HSA-8869438 Reactome:R-HSA-8868661 Reactome:R-HSA-8868660 Reactome:R-HSA-8868659 Reactome:R-HSA-8868658	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0010008	endosome membrane	Reactome:R-HSA-917835 Reactome:R-HSA-917814 Reactome:R-HSA-917807	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-HSA-917987 Reactome:R-HSA-917839 Reactome:R-HSA-917814 Reactome:R-HSA-917807 Reactome:R-HSA-8868661 Reactome:R-HSA-8868651 Reactome:R-HSA-8868648 Reactome:R-HSA-8868236 Reactome:R-HSA-8868230 Reactome:R-HSA-8868072 Reactome:R-HSA-8868071 Reactome:R-HSA-8867756 Reactome:R-HSA-8867754 Reactome:R-HSA-8866277 Reactome:R-HSA-5691154	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
involved_in	GO:0006897	endocytosis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0254	P		Seeded From UniProt	complete
enables	GO:0001618	virus receptor activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1183	F		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
part_of	GO:0042470	melanosome	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0161	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Bhattacharyya, S et al. (2010) Ebola virus uses clathrin-mediated endocytosis as an entry pathway. Virology 401 18-28 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Jabara, HH et al. (2016) A missense mutation in TFRC, encoding transferrin receptor 1, causes combined immunodeficiency. Nat. Genet. 48 74-8 PubMed GONUTS page
↑ ^3.0 ^3.1 Sirokmány, G et al. (2006) Sec14 homology domain targets p50RhoGAP to endosomes and provides a link between Rab and Rho GTPases. J. Biol. Chem. 281 6096-105 PubMed GONUTS page
↑ Feder, JN et al. (1998) The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding. Proc. Natl. Acad. Sci. U.S.A. 95 1472-7 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 Waheed, A et al. (2008) HFE association with transferrin receptor 2 increases cellular uptake of transferrin-bound iron. Arch. Biochem. Biophys. 474 193-7 PubMed GONUTS page
↑ ^6.0 ^6.1 Waheed, A et al. (1999) Association of HFE protein with transferrin receptor in crypt enterocytes of human duodenum. Proc. Natl. Acad. Sci. U.S.A. 96 1579-84 PubMed GONUTS page
↑ ^7.0 ^7.1 Lebrón, JA et al. (1998) Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor. Cell 93 111-23 PubMed GONUTS page
↑ Hehnly, H & Doxsey, S (2014) Rab11 endosomes contribute to mitotic spindle organization and orientation. Dev. Cell 28 497-507 PubMed GONUTS page
↑ Chiasserini, D et al. (2014) Proteomic analysis of cerebrospinal fluid extracellular vesicles: a comprehensive dataset. J Proteomics 106 191-204 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 Kennard, ML et al. (1995) A novel iron uptake mechanism mediated by GPI-anchored human p97. EMBO J. 14 4178-86 PubMed GONUTS page
↑ Bastos-Amador, P et al. (2012) Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. J Proteomics 75 3574-84 PubMed GONUTS page
↑ Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ Böhm, D et al. (2012) Comparison of tear protein levels in breast cancer patients and healthy controls using a de novo proteomic approach. Oncol. Rep. 28 429-38 PubMed GONUTS page
↑ Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 Baynes, RD et al. (1991) Characterization of transferrin receptor released by K562 erythroleukemia cells. Proc. Soc. Exp. Biol. Med. 197 416-23 PubMed GONUTS page
↑ Aschenbrenner, L et al. (2003) Myo6 facilitates the translocation of endocytic vesicles from cell peripheries. Mol. Biol. Cell 14 2728-43 PubMed GONUTS page
↑ Orsi, A et al. (2012) Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy. Mol. Biol. Cell 23 1860-73 PubMed GONUTS page
↑ Taylor, DR et al. (2005) Assigning functions to distinct regions of the N-terminus of the prion protein that are involved in its copper-stimulated, clathrin-dependent endocytosis. J. Cell. Sci. 118 5141-53 PubMed GONUTS page
↑ Coumailleau, F et al. (2004) Over-expression of Rififylin, a new RING finger and FYVE-like domain-containing protein, inhibits recycling from the endocytic recycling compartment. Mol. Biol. Cell 15 4444-56 PubMed GONUTS page
↑ Kim, BE et al. (2004) Zn2+-stimulated endocytosis of the mZIP4 zinc transporter regulates its location at the plasma membrane. J. Biol. Chem. 279 4523-30 PubMed GONUTS page
↑ Watanabe, A et al. (2011) Raftlin is involved in the nucleocapture complex to induce poly(I:C)-mediated TLR3 activation. J. Biol. Chem. 286 10702-11 PubMed GONUTS page
↑ Gruszczyk, J et al. (2018) Transferrin receptor 1 is a reticulocyte-specific receptor for . Science 359 48-55 PubMed GONUTS page
↑ Zahn, C et al. (2013) The transferrin receptor-1 membrane stub undergoes intramembrane proteolysis by signal peptide peptidase-like 2b. FEBS J. 280 1653-63 PubMed GONUTS page
↑ Abraham, J et al. (2010) Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses. Nat. Struct. Mol. Biol. 17 438-44 PubMed GONUTS page
↑ ^25.0 ^25.1 Levy, JE et al. (1999) Transferrin receptor is necessary for development of erythrocytes and the nervous system. Nat. Genet. 21 396-9 PubMed GONUTS page
↑ Schneider, C et al. () Primary structure of human transferrin receptor deduced from the mRNA sequence. Nature 311 675-8 PubMed GONUTS page
↑ Liao, JF & Perkins, JP (1993) Differential effects of antimycin A on endocytosis and exocytosis of transferrin also are observed for internalization and externalization of beta-adrenergic receptors. Mol. Pharmacol. 44 364-70 PubMed GONUTS page

[PMID:20202662-1] 1.0 ^1.1 Bhattacharyya, S et al. (2010) Ebola virus uses clathrin-mediated endocytosis as an entry pathway. Virology 401 18-28 PubMed GONUTS page

[PMID:26642240-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Jabara, HH et al. (2016) A missense mutation in TFRC, encoding transferrin receptor 1, causes combined immunodeficiency. Nat. Genet. 48 74-8 PubMed GONUTS page

[PMID:16380373-3] 3.0 ^3.1 Sirokmány, G et al. (2006) Sec14 homology domain targets p50RhoGAP to endosomes and provides a link between Rab and Rho GTPases. J. Biol. Chem. 281 6096-105 PubMed GONUTS page

[PMID:9465039-4] Feder, JN et al. (1998) The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding. Proc. Natl. Acad. Sci. U.S.A. 95 1472-7 PubMed GONUTS page

[PMID:18353247-5] 5.0 ^5.1 ^5.2 ^5.3 Waheed, A et al. (2008) HFE association with transferrin receptor 2 increases cellular uptake of transferrin-bound iron. Arch. Biochem. Biophys. 474 193-7 PubMed GONUTS page

[PMID:9990067-6] 6.0 ^6.1 Waheed, A et al. (1999) Association of HFE protein with transferrin receptor in crypt enterocytes of human duodenum. Proc. Natl. Acad. Sci. U.S.A. 96 1579-84 PubMed GONUTS page

[PMID:9546397-7] 7.0 ^7.1 Lebrón, JA et al. (1998) Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor. Cell 93 111-23 PubMed GONUTS page

[PMID:24561039-8] Hehnly, H & Doxsey, S (2014) Rab11 endosomes contribute to mitotic spindle organization and orientation. Dev. Cell 28 497-507 PubMed GONUTS page

[PMID:24769233-9] Chiasserini, D et al. (2014) Proteomic analysis of cerebrospinal fluid extracellular vesicles: a comprehensive dataset. J Proteomics 106 191-204 PubMed GONUTS page

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