P02787 (TRFE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serotransferrin
Short name=Transferrin

Alternative name(s):
Beta-1 metal-binding globulin
Siderophilin

Gene names

Name:	TF
ORF Names:	PRO1400

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	698 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	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.37
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 process	Ion transport Iron transport Transport
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Repeat Signal
Ligand	Iron Metal-binding
PTM	Disulfide bond Glycoprotein Methylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular iron ion homeostasis Traceable author statement. Source: Reactome platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome transferrin transport Traceable author statement. Source: Reactome transmembrane transport Traceable author statement. Source: Reactome
Cellular_component	apical plasma membrane Inferred from direct assay PubMed 11208127. Source: UniProtKB basal plasma membrane Inferred from direct assay PubMed 15880641. Source: UniProtKB coated pit 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 late endosome Inferred from direct assay PubMed 15880641. Source: UniProtKB mitochondrion Inferred from direct assay. Source: HPA perinuclear region of cytoplasm Inferred from direct assay PubMed 15880641. Source: UniProtKB recycling endosome Inferred from direct assay PubMed 15880641. Source: UniProtKB secretory granule Traceable author statement. Source: Reactome
Molecular_function	ferric iron binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.12

Chain

20 – 698

679

Serotransferrin

PRO_0000035715

Regions

Domain

25 – 347

323

Transferrin-like 1

Domain

361 – 683

323

Transferrin-like 2

Sites

Metal binding

82

1

Iron 1

Metal binding

114

1

Iron 1

Metal binding

207

1

Iron 1

Metal binding

268

1

Iron 1

Metal binding

411

1

Iron 2 By similarity

Metal binding

445

1

Iron 2 By similarity

Metal binding

536

1

Iron 2 By similarity

Metal binding

604

1

Iron 2 By similarity

Binding site

139

1

Carbonate 1

Binding site

143

1

Carbonate 1

Binding site

145

1

Carbonate 1; via amide nitrogen

Binding site

146

1

Carbonate 1; via amide nitrogen

Binding site

471

1

Carbonate 2 By similarity

Binding site

475

1

Carbonate 2 By similarity

Binding site

477

1

Carbonate 2; via amide nitrogen By similarity

Binding site

478

1

Carbonate 2; via amide nitrogen By similarity

Amino acid modifications

Modified residue

42

1

Omega-N-methylated arginine By similarity

Glycosylation

51

1

O-linked (GalNAc...)

CAR_000073

Glycosylation

432

1

N-linked (GlcNAc...) (complex) Ref.24 Ref.25 Ref.26 Ref.28 Ref.29

CAR_000074

Glycosylation

630

1

N-linked (GlcNAc...) (complex) Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29

CAR_000075

Disulfide bond

28 ↔ 67

Ref.22

Disulfide bond

38 ↔ 58

Ref.22

Disulfide bond

137 ↔ 213

Ref.22

Disulfide bond

156 ↔ 350

Ref.22

Disulfide bond

177 ↔ 193

Ref.22

Disulfide bond

180 ↔ 196

Ref.22

Disulfide bond

190 ↔ 198

Ref.22

Disulfide bond

246 ↔ 260

Ref.22

Disulfide bond

358 ↔ 615

Ref.22

Disulfide bond

364 ↔ 396

Ref.22

Disulfide bond

374 ↔ 387

Ref.22

Disulfide bond

421 ↔ 693

Ref.22

Disulfide bond

437 ↔ 656

Ref.22

Disulfide bond

469 ↔ 542

Ref.22

Disulfide bond

493 ↔ 684

Ref.22

Disulfide bond

503 ↔ 517

Ref.22

Disulfide bond

514 ↔ 525

Ref.22

Disulfide bond

582 ↔ 596

Ref.22

Disulfide bond

634 ↔ 639

Ref.22

Natural variations

Natural variant

42

1

R → L.
Corresponds to variant rs41298293 [ dbSNP | Ensembl ].

VAR_034569

Natural variant

55

1

S → R. Ref.5
Corresponds to variant rs8177318 [ dbSNP | Ensembl ].

VAR_029280

Natural variant

76

1

A → V.
Corresponds to variant rs41298977 [ dbSNP | Ensembl ].

VAR_034570

Natural variant

77

1

D → N in ATRAF. Ref.37

VAR_038810

Natural variant

142

1

G → S. Ref.33
Corresponds to variant rs1799830 [ dbSNP | Ensembl ].

VAR_011997

Natural variant

277

1

G → 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.35 Ref.36
Corresponds to variant rs1799899 [ dbSNP | Ensembl ].

VAR_011998

Natural variant

296

1

D → G in allele TF*D1. Ref.5
Corresponds to variant rs8177238 [ dbSNP | Ensembl ].

VAR_007544

Natural variant

319

1

H → R in allele TF*CHI.

VAR_007545

Natural variant

377

1

W → C.
Corresponds to variant rs1804498 [ dbSNP | Ensembl ].

VAR_011999

Natural variant

448

1

I → 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.38
Corresponds to variant rs2692696 [ dbSNP | Ensembl ].

VAR_058199

Natural variant

477

1

A → P in ATRAF. Ref.4

VAR_012997

Natural variant

562

1

G → V.
Corresponds to variant rs41296590 [ dbSNP | Ensembl ].

VAR_034571

Natural variant

589

1

P → S in allele TF*C2. Ref.5 Ref.19 Ref.35 Ref.36
Corresponds to variant rs1049296 [ dbSNP | Ensembl ].

VAR_012000

Natural variant

645

1

T → P.
Corresponds to variant rs1130537 [ dbSNP | Ensembl ].

VAR_012001

Natural variant

646

1

K → E in allele TF*BV. Ref.34

VAR_012998

Natural variant

671

1

G → E in allele TF*B2. Ref.35

VAR_012999

Experimental info

Sequence conflict

216

1

D → N in AAH59367. Ref.9

Sequence conflict

264

1

Q → E AA sequence Ref.12

Sequence conflict

329

1

D → N AA sequence Ref.12

Sequence conflict

329

1

D → N in AAA61141. Ref.14

Sequence conflict

351

1

P → Q in AAH59367. Ref.9

Sequence conflict

380 – 381

2

NS → SD AA sequence Ref.12

Sequence conflict

436

1

N → D AA sequence Ref.12

Sequence conflict

558 – 561

4

PQNT → TQNP AA sequence Ref.12

Sequence conflict

591

1

E → Q AA sequence Ref.12

Sequence conflict

672

1

E → Q AA sequence Ref.12

Sequence conflict

691

1

E → G in AAA61142. Ref.18

Secondary structure

1

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698

Helix Strand Turn

Details...

Beta strand

24 – 30

7

Helix

31 – 48

18

Beta strand

51 – 54

4

Beta strand

55 – 63

9

Helix

64 – 72

9

Beta strand

78 – 81

4

Helix

83 – 90

8

Turn

92 – 94

3

Beta strand

97 – 105

9

Beta strand

107 – 121

15

Helix

128 – 130

3

Beta strand

136 – 139

4

Turn

144 – 147

4

Helix

148 – 154

7

Helix

155 – 157

3

Beta strand

158 – 160

3

Helix

165 – 172

8

Beta strand

173 – 177

5

Turn

183 – 185

3

Helix

187 – 190

4

Beta strand

191 – 193

3

Helix

194 – 196

3

Beta strand

198 – 202

5

Helix

206 – 215

10

Beta strand

220 – 225

6

Helix

228 – 232

5

Helix

236 – 239

4

Beta strand

242 – 245

4

Turn

247 – 249

3

Beta strand

251 – 253

3

Helix

254 – 259

6

Beta strand

262 – 266

5

Beta strand

269 – 272

4

Beta strand

274 – 276

3

Helix

279 – 293

15

Turn

295 – 297

3

Beta strand

298 – 300

3

Beta strand

310 – 314

5

Beta strand

318 – 323

6

Helix

330 – 334

5

Helix

336 – 345

10

Turn

346 – 348

3

Helix

354 – 357

4

Beta strand

360 – 365

6

Helix

368 – 380

13

Turn

381 – 383

3

Beta strand

384 – 389

6

Helix

393 – 401

9

Beta strand

407 – 410

4

Helix

412 – 420

9

Beta strand

424 – 430

7

Helix

437 – 439

3

Beta strand

445 – 452

8

Beta strand

455 – 457

3

Helix

460 – 462

3

Beta strand

466 – 471

6

Turn

476 – 479

4

Helix

480 – 485

6

Helix

487 – 489

3

Helix

495 – 497

3

Beta strand

498 – 503

6

Beta strand

509 – 511

3

Helix

512 – 514

3

Helix

521 – 523

3

Beta strand

531 – 533

3

Helix

535 – 545

11

Beta strand

548 – 553

6

Helix

556 – 559

4

Turn

568 – 572

5

Helix

575 – 577

3

Beta strand

578 – 581

4

Beta strand

587 – 589

3

Helix

590 – 595

6

Beta strand

598 – 601

4

Beta strand

605 – 608

4

Helix

610 – 612

3

Helix

613 – 627

15

Beta strand

628 – 630

3

Beta strand

635 – 637

3

Beta strand

644 – 646

3

Beta strand

648 – 650

3

Beta strand

656 – 659

4

Helix

661 – 663

3

Helix

666 – 669

4

Helix

672 – 684

13

Helix

688 – 694

7

Sequences

	Sequence		Length	Mass (Da)
	P02787 [UniParc]. Last modified November 30, 2010. Version 3. Checksum: 9A73B90D8C5671E9	FASTA	698	77,064
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Plasma.
[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-432 AND ASN-630, MASS SPECTROMETRY. Tissue: Plasma.
[27]	"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, MASS SPECTROMETRY. Tissue: Saliva.
[28]	"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, MASS SPECTROMETRY. Tissue: Liver.
[29]	"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, MASS SPECTROMETRY. Tissue: Cerebrospinal fluid.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"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.
[38]	"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, MASS SPECTROMETRY.
+	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 , 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 , 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.

IPI

IPI00022463.

PIR

TFHUP. A20981.

RefSeq

NP_001054.1. NM_001063.3.

UniGene

Hs.518267.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A8E	X-ray	1.60	A	22-350	[»]
1A8F	X-ray	1.80	A	22-350	[»]
1B3E	X-ray	2.50	A	23-352	[»]
1BP5	X-ray	2.20	A/B/C/D	20-356	[»]
1BTJ	X-ray	3.20	A/B	20-356	[»]
1D3K	X-ray	1.80	A	22-350	[»]
1D4N	X-ray	2.00	A	22-350	[»]
1DTG	X-ray	2.40	A	20-353	[»]
1FQE	X-ray	1.80	A	20-350	[»]
1FQF	X-ray	2.10	A	20-350	[»]
1JQF	X-ray	1.85	A	20-353	[»]
1N7W	X-ray	2.20	A	22-350	[»]
1N7X	X-ray	2.10	A	20-350	[»]
1N84	X-ray	2.05	A	20-350	[»]
1OQG	X-ray	1.90	A	20-354	[»]
1OQH	X-ray	2.40	A	20-354	[»]
1RYO	X-ray	1.20	A	20-346	[»]
1SUV	electron microscopy	7.50	C/D	22-350	[»]
2HAU	X-ray	2.70	A/B	23-698	[»]
2HAV	X-ray	2.70	A/B	23-698	[»]
2O7U	X-ray	2.80	A/B/C/D/E/F/G/H/I	20-356	[»]
2O84	X-ray	2.60	X	20-356	[»]
3FGS	X-ray	1.80	A	20-356	[»]
3QYT	X-ray	2.80	A	20-698	[»]
3S9L	X-ray	3.22	C/D	20-698	[»]
3S9M	X-ray	3.32	C/D	20-698	[»]
3S9N	X-ray	3.25	C/D	20-698	[»]
3SKP	X-ray	1.70	A	358-698	[»]
3V83	X-ray	2.10	A/B/C/D/E/F	1-698	[»]
3V89	X-ray	3.10	B	356-698	[»]
3V8X	X-ray	2.60	B	1-698	[»]
3VE1	X-ray	2.96	B/D	20-698	[»]
4H0W	X-ray	2.40	A	20-698	[»]

ProteinModelPortal

P02787.

SMR

P02787. Positions 20-698.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2738N.

IntAct

P02787. 28 interactions.

MINT

MINT-1400694.

STRING

9606.ENSP00000264998.

Protein family/group databases

MEROPS

S60.972.

PTM databases

GlycoSuiteDB

P02787.

PhosphoSite

P02787.

2D gel databases

DOSAC-COBS-2DPAGE

P02787.

REPRODUCTION-2DPAGE

IPI00022463.
P02787.

SWISS-2DPAGE

P02787.

UCD-2DPAGE

P02787.

Proteomic databases

PaxDb

P02787.

PRIDE

P02787.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000402696; ENSP00000385834; ENSG00000091513.

GeneID

7018.

KEGG

hsa:7018.

UCSC

uc003epu.2. human.

Organism-specific databases

CTD

7018.

GeneCards

GC03P133464.

HGNC

HGNC:11740. TF.

HPA

CAB009538.
HPA001527.
HPA005692.

MIM

190000. gene.
209300. phenotype.

neXtProt

NX_P02787.

Orphanet

1195. Atransferrinemia.

PharmGKB

PA36457.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG87503.

HOGENOM

HOG000252723.

HOVERGEN

HBG000055.

InParanoid

P02787.

KO

K14736.

OMA

FYYAVAV.

OrthoDB

EOG4CRKZG.

PhylomeDB

P02787.

Enzyme and pathway databases

Pathway_Interaction_DB

ephbfwdpathway. EPHB forward signaling.
hif1_tfpathway. HIF-1-alpha transcription factor network.

Reactome

REACT_15518. Transmembrane transport of small molecules.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P02787.

Bgee

P02787.

CleanEx

HS_TF.

Genevestigator

P02787.

GermOnline

ENSG00000091513. Homo sapiens.

Family and domain databases

InterPro

IPR016357. Transferrin.
IPR001156. Transferrin_fam.
IPR018195. Transferrin_Fe_BS.
[Graphical view]

PANTHER

PTHR11485. PTHR11485. 1 hit.

Pfam

PF00405. Transferrin. 2 hits.
[Graphical view]

PIRSF

PIRSF002549. Transferrin. 1 hit.

PRINTS

PR00422. TRANSFERRIN.

SMART

SM00094. TR_FER. 2 hits.
[Graphical view]

PROSITE

PS00205. 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]

ProtoNet

Search...

Other

ChEMBL

CHEMBL4865.

ChiTaRS

TF. human.

DrugBank

DB01370. Aluminium.
DB01402. Bismuth.
DB00893. Iron Dextran.

EvolutionaryTrace

P02787.

GenomeRNAi

7018.

NextBio

27415.

PMAP-CutDB

P02787.

SOURCE

Search...

Entry information

Entry name

TRFE_HUMAN

Accession

Primary (citable) accession number: P02787
Secondary accession number(s): O43890 , Q1HBA5, Q9NQB8, Q9UHV0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 30, 2010
Last modified:	May 1, 2013
This is version 172 of the entry and version 3 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.