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P02787 (TRFE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 183. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serotransferrin

Short name=Transferrin
Alternative name(s):
Beta-1 metal-binding globulin
Siderophilin
Gene names
Name:TF
ORF Names:PRO1400
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length698 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.

Subunit structure

Monomer.

Subcellular location

Secreted.

Tissue specificity

Expressed by the liver and secreted in plasma.

Polymorphism

Different polymorphic variants of transferrin are known. The sequence shown is the predominant electrophoretic variant (C1 or TF*C1).

Involvement in disease

Atransferrinemia (ATRAF) [MIM:209300]: A rare autosomal recessive disorder characterized by abnormal synthesis of transferrin leading to iron overload and microcytic hypochromic anemia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.39

Sequence similarities

Belongs to the transferrin family.

Contains 2 transferrin-like domains.

Sequence caution

The sequence AAF22007.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processIon transport
Iron transport
Transport
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainRepeat
Signal
   LigandIron
Metal-binding
   PTMDisulfide bond
Glycoprotein
Methylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

cellular iron ion homeostasis

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

retina homeostasis

Inferred from expression pattern PubMed 23580065. Source: UniProt

transferrin transport

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 11208127. Source: UniProtKB

basal part of cell

Inferred from direct assay PubMed 15880641. Source: UniProtKB

basal plasma membrane

Inferred from direct assay PubMed 15880641. Source: UniProtKB

blood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cell surface

Inferred from direct assay PubMed 16195351. Source: UniProt

coated pit

Inferred from direct assay PubMed 12857860. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from direct assay PubMed 12857860. Source: UniProtKB

early endosome

Inferred from direct assay PubMed 15880641. Source: UniProtKB

endocytic vesicle

Inferred from direct assay PubMed 15229288PubMed 15292400. Source: MGI

endosome membrane

Traceable author statement. Source: Reactome

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 22664934PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

late endosome

Inferred from direct assay PubMed 15880641. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 15880641. Source: UniProtKB

recycling endosome

Inferred from direct assay PubMed 15880641. Source: UniProtKB

secretory granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionferric iron binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GASTP013505EBI-714319,EBI-3436637

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.12
Chain20 – 698679Serotransferrin
PRO_0000035715

Regions

Domain25 – 347323Transferrin-like 1
Domain361 – 683323Transferrin-like 2

Sites

Metal binding821Iron 1
Metal binding1141Iron 1
Metal binding2071Iron 1
Metal binding2681Iron 1
Metal binding4111Iron 2 By similarity
Metal binding4451Iron 2 By similarity
Metal binding5361Iron 2 By similarity
Metal binding6041Iron 2 By similarity
Binding site1391Carbonate 1
Binding site1431Carbonate 1
Binding site1451Carbonate 1; via amide nitrogen
Binding site1461Carbonate 1; via amide nitrogen
Binding site4711Carbonate 2 By similarity
Binding site4751Carbonate 2 By similarity
Binding site4771Carbonate 2; via amide nitrogen By similarity
Binding site4781Carbonate 2; via amide nitrogen By similarity

Amino acid modifications

Modified residue421Omega-N-methylated arginine By similarity
Glycosylation511O-linked (GalNAc...)
CAR_000073
Glycosylation4321N-linked (GlcNAc...) (complex) Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.31
CAR_000074
Glycosylation4911N-linked (GlcNAc...); partial; atypical Ref.26
Glycosylation6301N-linked (GlcNAc...) (complex) Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31
CAR_000075
Disulfide bond28 ↔ 67 Ref.22
Disulfide bond38 ↔ 58 Ref.22
Disulfide bond137 ↔ 213 Ref.22
Disulfide bond156 ↔ 350 Ref.22
Disulfide bond177 ↔ 193 Ref.22
Disulfide bond180 ↔ 196 Ref.22
Disulfide bond190 ↔ 198 Ref.22
Disulfide bond246 ↔ 260 Ref.22
Disulfide bond358 ↔ 615 Ref.22
Disulfide bond364 ↔ 396 Ref.22
Disulfide bond374 ↔ 387 Ref.22
Disulfide bond421 ↔ 693 Ref.22
Disulfide bond437 ↔ 656 Ref.22
Disulfide bond469 ↔ 542 Ref.22
Disulfide bond493 ↔ 684 Ref.22
Disulfide bond503 ↔ 517 Ref.22
Disulfide bond514 ↔ 525 Ref.22
Disulfide bond582 ↔ 596 Ref.22
Disulfide bond634 ↔ 639 Ref.22

Natural variations

Natural variant421R → L.
Corresponds to variant rs41298293 [ dbSNP | Ensembl ].
VAR_034569
Natural variant551S → R. Ref.5
Corresponds to variant rs8177318 [ dbSNP | Ensembl ].
VAR_029280
Natural variant761A → V.
Corresponds to variant rs41298977 [ dbSNP | Ensembl ].
VAR_034570
Natural variant771D → N in ATRAF. Ref.39
VAR_038810
Natural variant1421G → S. Ref.35
Corresponds to variant rs1799830 [ dbSNP | Ensembl ].
VAR_011997
Natural variant2771G → S in allele TF*C3; associated with a reduction in total iron binding capacity; risk factor for iron deficiency anemia in menstruating white women. Ref.5 Ref.37 Ref.38
Corresponds to variant rs1799899 [ dbSNP | Ensembl ].
VAR_011998
Natural variant2961D → G in allele TF*D1. Ref.5
Corresponds to variant rs8177238 [ dbSNP | Ensembl ].
VAR_007544
Natural variant3191H → R in allele TF*CHI.
Corresponds to variant rs41295774 [ dbSNP | Ensembl ].
VAR_007545
Natural variant3771W → C.
Corresponds to variant rs1804498 [ dbSNP | Ensembl ].
VAR_011999
Natural variant4481I → V. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8 Ref.9 Ref.12 Ref.14 Ref.15 Ref.16 Ref.18 Ref.40
Corresponds to variant rs2692696 [ dbSNP | Ensembl ].
VAR_058199
Natural variant4771A → P in ATRAF. Ref.4
VAR_012997
Natural variant5621G → V.
Corresponds to variant rs41296590 [ dbSNP | Ensembl ].
VAR_034571
Natural variant5891P → S in allele TF*C2. Ref.5 Ref.19 Ref.37 Ref.38
Corresponds to variant rs1049296 [ dbSNP | Ensembl ].
VAR_012000
Natural variant6451T → P.
Corresponds to variant rs1130537 [ dbSNP | Ensembl ].
VAR_012001
Natural variant6461K → E in allele TF*BV. Ref.36
VAR_012998
Natural variant6711G → E in allele TF*B2. Ref.37
Corresponds to variant rs121918677 [ dbSNP | Ensembl ].
VAR_012999

Experimental info

Sequence conflict2161D → N in AAH59367. Ref.9
Sequence conflict2641Q → E AA sequence Ref.12
Sequence conflict3291D → N AA sequence Ref.12
Sequence conflict3291D → N in AAA61141. Ref.14
Sequence conflict3511P → Q in AAH59367. Ref.9
Sequence conflict380 – 3812NS → SD AA sequence Ref.12
Sequence conflict4361N → D AA sequence Ref.12
Sequence conflict558 – 5614PQNT → TQNP AA sequence Ref.12
Sequence conflict5911E → Q AA sequence Ref.12
Sequence conflict6721E → Q AA sequence Ref.12
Sequence conflict6911E → G in AAA61142. Ref.18

Secondary structure

........................................................................................................................................................ 698
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02787 [UniParc].

Last modified November 30, 2010. Version 3.
Checksum: 9A73B90D8C5671E9

FASTA69877,064
        10         20         30         40         50         60 
MRLAVGALLV CAVLGLCLAV PDKTVRWCAV SEHEATKCQS FRDHMKSVIP SDGPSVACVK 

        70         80         90        100        110        120 
KASYLDCIRA IAANEADAVT LDAGLVYDAY LAPNNLKPVV AEFYGSKEDP QTFYYAVAVV 

       130        140        150        160        170        180 
KKDSGFQMNQ LRGKKSCHTG LGRSAGWNIP IGLLYCDLPE PRKPLEKAVA NFFSGSCAPC 

       190        200        210        220        230        240 
ADGTDFPQLC QLCPGCGCST LNQYFGYSGA FKCLKDGAGD VAFVKHSTIF ENLANKADRD 

       250        260        270        280        290        300 
QYELLCLDNT RKPVDEYKDC HLAQVPSHTV VARSMGGKED LIWELLNQAQ EHFGKDKSKE 

       310        320        330        340        350        360 
FQLFSSPHGK DLLFKDSAHG FLKVPPRMDA KMYLGYEYVT AIRNLREGTC PEAPTDECKP 

       370        380        390        400        410        420 
VKWCALSHHE RLKCDEWSVN SVGKIECVSA ETTEDCIAKI MNGEADAMSL DGGFVYIAGK 

       430        440        450        460        470        480 
CGLVPVLAEN YNKSDNCEDT PEAGYFAIAV VKKSASDLTW DNLKGKKSCH TAVGRTAGWN 

       490        500        510        520        530        540 
IPMGLLYNKI NHCRFDEFFS EGCAPGSKKD SSLCKLCMGS GLNLCEPNNK EGYYGYTGAF 

       550        560        570        580        590        600 
RCLVEKGDVA FVKHQTVPQN TGGKNPDPWA KNLNEKDYEL LCLDGTRKPV EEYANCHLAR 

       610        620        630        640        650        660 
APNHAVVTRK DKEACVHKIL RQQQHLFGSN VTDCSGNFCL FRSETKDLLF RDDTVCLAKL 

       670        680        690 
HDRNTYEKYL GEEYVKAVGN LRKCSTSSLL EACTFRRP 

« Hide

References

« Hide 'large scale' references
[1]"Human transferrin: cDNA characterization and chromosomal localization."
Yang F., Lum J.B., McGill J.R., Moore C.M., Naylor S.L., van Bragt P.H., Baldwin W.D., Bowman B.H.
Proc. Natl. Acad. Sci. U.S.A. 81:2752-2756(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS TF*B2; TF*CHI; TF*D1 AND VAL-448.
[2]"Complete structure of the human transferrin gene. Comparison with analogous chicken gene and human pseudogene."
Schaeffer E., Lucero M.A., Jeltsch J.-M., Py M.-C., Levin M.J., Chambon P., Cohen G.N., Zakin M.M.
Gene 56:109-116(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"A cloned gene for human transferrin."
Hershberger C.L., Larson J.L., Arnold B., Rosteck P.R. Jr., Williams P., Dehoff B., Dunn P., O'Neal K.L., Riemen M.W., Tice P.A.
Ann. N. Y. Acad. Sci. 646:140-154(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-448.
Tissue: Liver.
[4]"Molecular characterization of a case of atransferrinemia."
Beutler E., Gelbart T., Lee P.L., Trevino R., Fernandez M.A., Fairbanks V.F.
Blood 96:4071-4074(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-448 AND ATRAF PRO-477.
[5]SeattleSNPs variation discovery resource
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-55; SER-277; GLY-296; VAL-448 AND SER-589.
[6]NHLBI resequencing and genotyping service (RS&G)
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-448.
[7]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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. expand/collapse author list , 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], VARIANT VAL-448.
[9]"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], VARIANT VAL-448.
Tissue: Brain.
[10]"The human transferrin gene: 5' region contains conserved sequences which match the control elements regulated by heavy metals, glucocorticoids and acute phase reaction."
Adrian G.S., Korinek B.W., Bowman B.H., Yang F.
Gene 49:167-175(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72 AND 291-300.
[11]"The 5' region of the human transferrin gene: structure and potential regulatory sites."
Lucero M.A., Schaeffer E., Cohen G.N., Zakin M.M.
Nucleic Acids Res. 14:8692-8692(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
[12]"The primary structure of human serum transferrin. The structures of seven cyanogen bromide fragments and the assembly of the complete structure."
McGillivray R.T.A., Mendez E., Shewale J.G., Sinha S.K., Lineback-Zins J., Brew K.
J. Biol. Chem. 258:3543-3553(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-698, VARIANT VAL-448.
[13]"Alternative splicing prevents transferrin secretion during differentiation of a human oligodendrocyte cell line."
de Arriba Zerpa G.A., Saleh M.-C., Fernandez P.M., Guillou F., Espinosa de los Monteros A., de Vellis J., Zakin M.M., Baron B.
J. Neurosci. Res. 61:388-395(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 45-72.
[14]"Organization of the human transferrin gene: direct evidence that it originated by gene duplication."
Park I., Schaeffer E., Sidoli A., Baralle F.E., Cohen G.N., Zakin M.M.
Proc. Natl. Acad. Sci. U.S.A. 82:3149-3153(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-698, VARIANT VAL-448.
[15]"Functional prediction of the coding sequences of 33 new genes deduced by analysis of cDNA clones from human fetal liver."
Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Bi J., Zhang Y., Liu M., He F.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 99-698, VARIANT VAL-448.
Tissue: Fetal liver.
[16]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 108-121; 259-273; 332-343; 374-384; 434-452; 454-464; 495-508; 531-541; 577-600 AND 684-696, IDENTIFICATION BY MASS SPECTROMETRY, VARIANT VAL-448.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[17]"The major protein expression profile and two-dimensional protein database of human heart."
Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K.
Electrophoresis 16:1160-1169(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 263-266; 454-458; 531-538 AND 589-595.
Tissue: Heart.
[18]"Molecular cloning and sequence analysis of cDNA for human transferrin."
Uzan G., Frain M., Park I., Besmond C., Maessen G., Trepat J.S., Zakin M.M., Kahn A.
Biochem. Biophys. Res. Commun. 119:273-281(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 422-698, VARIANT VAL-448.
[19]"Human transferrin (Tf): a single mutation at codon 570 determines Tf C1 or Tf C2 variant."
Namekata K., Oyama F., Imagawa M., Ihara Y.
Hum. Genet. 100:457-458(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 564-624, VARIANTS TF*C2 AND SER-589.
Tissue: Brain.
[20]Tsuchida S., Ikemoto S., Kajii E.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 564-624.
[21]"Changes in brain gene expression shared by scrapie and Alzheimer disease."
Duguid J.R., Bohmont C.W., Liu N.G., Tourtellotte W.W.
Proc. Natl. Acad. Sci. U.S.A. 86:7260-7264(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 636-696.
[22]"The complete amino acid sequence of human serum transferrin."
McGillivray R.T.A., Mendez E., Sinha S.K., Sutton M.R., Lineback-Zins J., Brew K.
Proc. Natl. Acad. Sci. U.S.A. 79:2504-2508(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[23]"Expression and initial characterization of five site-directed mutants of the N-terminal half-molecule of human transferrin."
Woodworth R.C., Mason A.B., Funk W.D., McGillivray R.T.A.
Biochemistry 30:10824-10829(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[24]"A proteomic analysis of human bile."
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.
Mol. Cell. Proteomics 3:715-728(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630.
Tissue: Bile.
[25]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630.
Tissue: Plasma.
[26]"Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry."
Satomi Y., Shimonishi Y., Hase T., Takao T.
Rapid Commun. Mass Spectrom. 18:2983-2988(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-432; ASN-491 AND ASN-630.
[27]"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-432 AND ASN-630.
Tissue: Plasma.
[28]"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-630.
Tissue: Saliva.
[29]"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-432 AND ASN-630.
Tissue: Liver.
[30]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-630.
[31]"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630, STRUCTURE OF CARBOHYDRATES.
Tissue: Cerebrospinal fluid.
[32]"Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release."
Macgillivray R.T.A., Moore S.A., Chen J., Anderson B.F., Baker H., Luo Y., Bewley M.C., Smith C.A., Murphy M.E.P., Wang Y., Mason A.B., Woodworth R.C., Brayer G.D., Baker E.N.
Biochemistry 37:7919-7928(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 22-350.
[33]"Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin."
Jeffrey P.D., Bewley M.C., Macgillivray R.T.A., Mason A.B., Woodworth R.C., Baker E.N.
Biochemistry 37:13978-13986(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-350.
[34]"X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32."
Bewley M.C., Tam B.M., Grewal J., He S., Shewry S., Murphy M.E.P., Mason A.B., Woodworth R.C., Baker E.N., Macgillivray R.T.A.
Biochemistry 38:2535-2541(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-352.
[35]"Exon/intron structure of the human transferrin receptor gene."
Evans P., Kemp J.
Gene 199:123-131(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-142.
[36]"Identification of a mutation (A1879G) of transferrin from cDNA prepared from peripheral blood cells."
Pang H., Koda Y., Soejima M., Kimura H.
Ann. Hum. Genet. 62:271-274(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLU-646.
[37]"Human transferrin G277S mutation: a risk factor for iron deficiency anaemia."
Lee P.L., Halloran C., Trevino R., Felitti V., Beutler E.
Br. J. Haematol. 115:329-333(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-277; SER-589 AND GLU-671, CHARACTERIZATION OF VARIANT SER-277.
[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: VARIANTS SER-277 AND SER-589.
[39]"Molecular characterization of a third case of human atransferrinemia."
Knisely A.S., Gelbart T., Beutler E.
Blood 104:2607-2607(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ATRAF ASN-77.
[40]"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: VARIANT [LARGE SCALE ANALYSIS] VAL-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Wikipedia

Transferrin entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12530 mRNA. Translation: AAA61140.1.
M17611, M17610 Genomic DNA. Translation: AAA61147.1.
M17614, M17612, M17613 Genomic DNA. Translation: AAA61148.1.
S95936 mRNA. Translation: AAB22049.1.
AF288144 expand/collapse EMBL AC list , AF294270, AF294271, AF288139, AF288140, AF288141, AF288142, AF288143 Genomic DNA. Translation: AAK77664.1.
AY308797 Genomic DNA. Translation: AAP45055.1.
DQ525716 Genomic DNA. Translation: ABF47110.1.
AC080128 mRNA. No translation available.
AC083905 mRNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79167.1.
BC059367 mRNA. Translation: AAH59367.1.
M21569, M15673 Genomic DNA. Translation: AAA61143.2.
M21570 Genomic DNA. Translation: AAA61145.1.
X04600 Genomic DNA. Translation: CAA28265.1.
AJ252279 mRNA. Translation: CAB96907.1.
M11372 expand/collapse EMBL AC list , M11361, M11362, M11363, M11364, M11365, M11366, M11367, M11368, M11369, M11370, M11371 Genomic DNA. Translation: AAA61141.1.
AF118063 mRNA. Translation: AAF22007.1. Different initiation.
M12525 mRNA. Translation: AAA61142.1.
U88581 mRNA. Translation: AAB97880.1.
AF058327 Genomic DNA. Translation: AAC63506.1.
M26641 mRNA. Translation: AAA61233.1.
PIRTFHUP. A20981.
RefSeqNP_001054.1. NM_001063.3.
UniGeneHs.518267.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8EX-ray1.60A22-350[»]
1A8FX-ray1.80A22-350[»]
1B3EX-ray2.50A23-352[»]
1BP5X-ray2.20A/B/C/D20-356[»]
1BTJX-ray3.20A/B20-356[»]
1D3KX-ray1.80A22-350[»]
1D4NX-ray2.00A22-350[»]
1DTGX-ray2.40A20-353[»]
1FQEX-ray1.80A20-350[»]
1FQFX-ray2.10A20-350[»]
1JQFX-ray1.85A20-353[»]
1N7WX-ray2.20A22-350[»]
1N7XX-ray2.10A20-350[»]
1N84X-ray2.05A20-350[»]
1OQGX-ray1.90A20-354[»]
1OQHX-ray2.40A20-354[»]
1RYOX-ray1.20A20-346[»]
1SUVelectron microscopy7.50C/D22-350[»]
2HAUX-ray2.70A/B23-698[»]
2HAVX-ray2.70A/B23-698[»]
2O7UX-ray2.80A/B/C/D/E/F/G/H/I20-356[»]
2O84X-ray2.60X20-356[»]
3FGSX-ray1.80A20-356[»]
3QYTX-ray2.80A20-698[»]
3S9LX-ray3.22C/D20-698[»]
3S9MX-ray3.32C/D20-698[»]
3S9NX-ray3.25C/D20-698[»]
3SKPX-ray1.70A358-698[»]
3V83X-ray2.10A/B/C/D/E/F1-698[»]
3V89X-ray3.10B356-698[»]
3V8XX-ray2.60B1-698[»]
3VE1X-ray2.96B/D20-698[»]
4H0WX-ray2.40A20-698[»]
ProteinModelPortalP02787.
SMRP02787. Positions 20-698.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112876. 22 interactions.
DIPDIP-2738N.
IntActP02787. 33 interactions.
MINTMINT-1400694.
STRING9606.ENSP00000264998.

Chemistry

ChEMBLCHEMBL4865.
DrugBankDB01370. Aluminium.
DB01402. Bismuth.
DB00893. Iron Dextran.

Protein family/group databases

MEROPSS60.972.

PTM databases

PhosphoSiteP02787.
UniCarbKBP02787.

Polymorphism databases

DMDM313104271.

2D gel databases

DOSAC-COBS-2DPAGEP02787.
REPRODUCTION-2DPAGEIPI00022463.
P02787.
SWISS-2DPAGEP02787.
UCD-2DPAGEP02787.

Proteomic databases

PaxDbP02787.
PRIDEP02787.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000402696; ENSP00000385834; ENSG00000091513.
GeneID7018.
KEGGhsa:7018.
UCSCuc003epu.2. human.

Organism-specific databases

CTD7018.
GeneCardsGC03P133464.
HGNCHGNC:11740. TF.
HPACAB009538.
HPA001527.
HPA005692.
MIM190000. gene.
209300. phenotype.
neXtProtNX_P02787.
Orphanet1195. Congenital atransferrinemia.
PharmGKBPA36457.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG87503.
HOGENOMHOG000252723.
HOVERGENHBG000055.
InParanoidP02787.
KOK14736.
OMAFYYAVAV.
OrthoDBEOG7D59N7.
PhylomeDBP02787.
TreeFamTF324013.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP02787.
BgeeP02787.
CleanExHS_TF.
GenevestigatorP02787.

Family and domain databases

InterProIPR016357. Transferrin.
IPR001156. Transferrin_fam.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFPIRSF002549. Transferrin. 1 hit.
PRINTSPR00422. TRANSFERRIN.
SMARTSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEPS00205. TRANSFERRIN_LIKE_1. 1 hit.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTF. human.
EvolutionaryTraceP02787.
GeneWikiTransferrin.
GenomeRNAi7018.
NextBio27415.
PMAP-CutDBP02787.
PROP02787.
SOURCESearch...

Entry information

Entry nameTRFE_HUMAN
AccessionPrimary (citable) accession number: P02787
Secondary accession number(s): O43890 expand/collapse secondary AC list , Q1HBA5, Q9NQB8, Q9UHV0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 183 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM