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P02787

- TRFE_HUMAN

UniProt

P02787 - TRFE_HUMAN

Protein

Serotransferrin

Gene

TF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 188 (01 Oct 2014)
      Sequence version 3 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi82 – 821Iron 1
    Metal bindingi114 – 1141Iron 1
    Binding sitei139 – 1391Carbonate 1
    Binding sitei143 – 1431Carbonate 1
    Binding sitei145 – 1451Carbonate 1; via amide nitrogen
    Binding sitei146 – 1461Carbonate 1; via amide nitrogen
    Metal bindingi207 – 2071Iron 1
    Metal bindingi268 – 2681Iron 1
    Metal bindingi411 – 4111Iron 2PROSITE-ProRule annotation
    Metal bindingi445 – 4451Iron 2PROSITE-ProRule annotation
    Binding sitei471 – 4711Carbonate 2PROSITE-ProRule annotation
    Binding sitei475 – 4751Carbonate 2PROSITE-ProRule annotation
    Binding sitei477 – 4771Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei478 – 4781Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
    Metal bindingi536 – 5361Iron 2PROSITE-ProRule annotation
    Metal bindingi604 – 6041Iron 2PROSITE-ProRule annotation

    GO - Molecular functioni

    1. ferric iron binding Source: InterPro
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cellular iron ion homeostasis Source: Reactome
    3. platelet activation Source: Reactome
    4. platelet degranulation Source: Reactome
    5. retina homeostasis Source: UniProt
    6. transferrin transport Source: Reactome
    7. transmembrane transport Source: Reactome

    Keywords - Biological processi

    Ion transport, Iron transport, Transport

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_25060. Iron uptake and transport.
    REACT_25283. Transferrin endocytosis and recycling.

    Protein family/group databases

    MEROPSiS60.972.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serotransferrin
    Short name:
    Transferrin
    Alternative name(s):
    Beta-1 metal-binding globulin
    Siderophilin
    Gene namesi
    Name:TF
    ORF Names:PRO1400
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:11740. TF.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB
    2. basal part of cell Source: UniProtKB
    3. basal plasma membrane Source: UniProtKB
    4. blood microparticle Source: UniProt
    5. cell surface Source: UniProt
    6. coated pit Source: UniProtKB
    7. cytoplasmic membrane-bounded vesicle Source: UniProtKB
    8. early endosome Source: UniProtKB
    9. endocytic vesicle Source: MGI
    10. endosome membrane Source: Reactome
    11. extracellular region Source: UniProtKB
    12. extracellular space Source: UniProt
    13. extracellular vesicular exosome Source: UniProt
    14. late endosome Source: UniProtKB
    15. perinuclear region of cytoplasm Source: UniProtKB
    16. recycling endosome Source: UniProtKB
    17. secretory granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Atransferrinemia (ATRAF) [MIM:209300]: A rare autosomal recessive disorder characterized by abnormal synthesis of transferrin leading to iron overload and microcytic hypochromic anemia.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti77 – 771D → N in ATRAF. 1 Publication
    VAR_038810
    Natural varianti477 – 4771A → P in ATRAF. 1 Publication
    VAR_012997

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi209300. phenotype.
    Orphaneti1195. Congenital atransferrinemia.
    PharmGKBiPA36457.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 698679SerotransferrinPRO_0000035715Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 671 PublicationPROSITE-ProRule annotation
    Disulfide bondi38 ↔ 581 PublicationPROSITE-ProRule annotation
    Modified residuei42 – 421Omega-N-methylated arginineBy similarity
    Glycosylationi51 – 511O-linked (GalNAc...)CAR_000073
    Disulfide bondi137 ↔ 2131 PublicationPROSITE-ProRule annotation
    Disulfide bondi156 ↔ 3501 PublicationPROSITE-ProRule annotation
    Disulfide bondi177 ↔ 1931 PublicationPROSITE-ProRule annotation
    Disulfide bondi180 ↔ 1961 PublicationPROSITE-ProRule annotation
    Disulfide bondi190 ↔ 1981 PublicationPROSITE-ProRule annotation
    Disulfide bondi246 ↔ 2601 PublicationPROSITE-ProRule annotation
    Disulfide bondi358 ↔ 6151 PublicationPROSITE-ProRule annotation
    Disulfide bondi364 ↔ 3961 PublicationPROSITE-ProRule annotation
    Disulfide bondi374 ↔ 3871 PublicationPROSITE-ProRule annotation
    Disulfide bondi421 ↔ 6931 PublicationPROSITE-ProRule annotation
    Glycosylationi432 – 4321N-linked (GlcNAc...) (complex)6 PublicationsCAR_000074
    Disulfide bondi437 ↔ 6561 PublicationPROSITE-ProRule annotation
    Disulfide bondi469 ↔ 5421 PublicationPROSITE-ProRule annotation
    Glycosylationi491 – 4911N-linked (GlcNAc...); partial; atypical1 Publication
    Disulfide bondi493 ↔ 6841 PublicationPROSITE-ProRule annotation
    Disulfide bondi503 ↔ 5171 PublicationPROSITE-ProRule annotation
    Disulfide bondi514 ↔ 5251 PublicationPROSITE-ProRule annotation
    Disulfide bondi582 ↔ 5961 PublicationPROSITE-ProRule annotation
    Glycosylationi630 – 6301N-linked (GlcNAc...) (complex)8 PublicationsCAR_000075
    Disulfide bondi634 ↔ 6391 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Methylation

    Proteomic databases

    MaxQBiP02787.
    PaxDbiP02787.
    PRIDEiP02787.

    2D gel databases

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

    PTM databases

    PhosphoSiteiP02787.
    UniCarbKBiP02787.

    Miscellaneous databases

    PMAP-CutDBP02787.

    Expressioni

    Tissue specificityi

    Expressed by the liver and secreted in plasma.

    Gene expression databases

    ArrayExpressiP02787.
    BgeeiP02787.
    CleanExiHS_TF.
    GenevestigatoriP02787.

    Organism-specific databases

    HPAiCAB009538.
    HPA001527.
    HPA005692.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GASTP013505EBI-714319,EBI-3436637

    Protein-protein interaction databases

    BioGridi112876. 23 interactions.
    DIPiDIP-2738N.
    IntActiP02787. 33 interactions.
    MINTiMINT-1400694.
    STRINGi9606.ENSP00000264998.

    Structurei

    Secondary structure

    1
    698
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 307
    Helixi31 – 4818
    Beta strandi51 – 544
    Beta strandi55 – 639
    Helixi64 – 729
    Beta strandi78 – 814
    Helixi83 – 908
    Turni92 – 943
    Beta strandi97 – 1059
    Beta strandi107 – 12115
    Helixi128 – 1303
    Beta strandi136 – 1394
    Turni144 – 1474
    Helixi148 – 1547
    Helixi155 – 1573
    Beta strandi158 – 1603
    Helixi165 – 1728
    Beta strandi173 – 1775
    Turni183 – 1853
    Helixi187 – 1904
    Beta strandi191 – 1933
    Helixi194 – 1963
    Beta strandi198 – 2025
    Helixi206 – 21510
    Beta strandi220 – 2256
    Helixi228 – 2325
    Helixi236 – 2394
    Beta strandi242 – 2454
    Turni247 – 2493
    Beta strandi251 – 2533
    Helixi254 – 2596
    Beta strandi262 – 2665
    Beta strandi269 – 2724
    Beta strandi274 – 2763
    Helixi279 – 29315
    Turni295 – 2973
    Beta strandi298 – 3003
    Beta strandi310 – 3145
    Beta strandi318 – 3236
    Helixi330 – 3345
    Helixi336 – 34510
    Turni346 – 3483
    Helixi354 – 3574
    Beta strandi360 – 3656
    Helixi368 – 38013
    Turni381 – 3833
    Beta strandi384 – 3896
    Helixi393 – 4019
    Beta strandi407 – 4104
    Helixi412 – 4209
    Beta strandi424 – 4307
    Helixi437 – 4393
    Beta strandi445 – 4528
    Beta strandi455 – 4573
    Helixi460 – 4623
    Beta strandi466 – 4716
    Turni476 – 4794
    Helixi480 – 4856
    Helixi487 – 4893
    Helixi495 – 4973
    Beta strandi498 – 5036
    Beta strandi509 – 5113
    Helixi512 – 5143
    Helixi521 – 5233
    Beta strandi531 – 5333
    Helixi535 – 54511
    Beta strandi548 – 5536
    Helixi556 – 5594
    Turni568 – 5725
    Helixi575 – 5773
    Beta strandi578 – 5814
    Beta strandi587 – 5893
    Helixi590 – 5956
    Beta strandi598 – 6014
    Beta strandi605 – 6084
    Helixi610 – 6123
    Helixi613 – 62715
    Beta strandi628 – 6303
    Beta strandi635 – 6373
    Beta strandi644 – 6463
    Beta strandi648 – 6503
    Beta strandi656 – 6594
    Helixi661 – 6633
    Helixi666 – 6694
    Helixi672 – 68413
    Helixi688 – 6947

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP02787.
    SMRiP02787. Positions 20-698.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02787.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 347323Transferrin-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini361 – 683323Transferrin-like 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the transferrin family.PROSITE-ProRule annotation
    Contains 2 transferrin-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG87503.
    HOGENOMiHOG000252723.
    HOVERGENiHBG000055.
    InParanoidiP02787.
    KOiK14736.
    OMAiFYYAVAV.
    OrthoDBiEOG7D59N7.
    PhylomeDBiP02787.
    TreeFamiTF324013.

    Family and domain databases

    InterProiIPR016357. Transferrin.
    IPR001156. Transferrin-like_dom.
    IPR018195. Transferrin_Fe_BS.
    [Graphical view]
    PfamiPF00405. Transferrin. 2 hits.
    [Graphical view]
    PIRSFiPIRSF002549. Transferrin. 1 hit.
    PRINTSiPR00422. TRANSFERRIN.
    SMARTiSM00094. TR_FER. 2 hits.
    [Graphical view]
    PROSITEiPS00205. 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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P02787-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLAVGALLV CAVLGLCLAV PDKTVRWCAV SEHEATKCQS FRDHMKSVIP    50
    SDGPSVACVK KASYLDCIRA IAANEADAVT LDAGLVYDAY LAPNNLKPVV 100
    AEFYGSKEDP QTFYYAVAVV KKDSGFQMNQ LRGKKSCHTG LGRSAGWNIP 150
    IGLLYCDLPE PRKPLEKAVA NFFSGSCAPC ADGTDFPQLC QLCPGCGCST 200
    LNQYFGYSGA FKCLKDGAGD VAFVKHSTIF ENLANKADRD QYELLCLDNT 250
    RKPVDEYKDC HLAQVPSHTV VARSMGGKED LIWELLNQAQ EHFGKDKSKE 300
    FQLFSSPHGK DLLFKDSAHG FLKVPPRMDA KMYLGYEYVT AIRNLREGTC 350
    PEAPTDECKP VKWCALSHHE RLKCDEWSVN SVGKIECVSA ETTEDCIAKI 400
    MNGEADAMSL DGGFVYIAGK CGLVPVLAEN YNKSDNCEDT PEAGYFAIAV 450
    VKKSASDLTW DNLKGKKSCH TAVGRTAGWN IPMGLLYNKI NHCRFDEFFS 500
    EGCAPGSKKD SSLCKLCMGS GLNLCEPNNK EGYYGYTGAF RCLVEKGDVA 550
    FVKHQTVPQN TGGKNPDPWA KNLNEKDYEL LCLDGTRKPV EEYANCHLAR 600
    APNHAVVTRK DKEACVHKIL RQQQHLFGSN VTDCSGNFCL FRSETKDLLF 650
    RDDTVCLAKL HDRNTYEKYL GEEYVKAVGN LRKCSTSSLL EACTFRRP 698
    Length:698
    Mass (Da):77,064
    Last modified:November 30, 2010 - v3
    Checksum:i9A73B90D8C5671E9
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti216 – 2161D → N in AAH59367. (PubMed:15489334)Curated
    Sequence conflicti264 – 2641Q → E AA sequence (PubMed:6833213)Curated
    Sequence conflicti329 – 3291D → N AA sequence (PubMed:6833213)Curated
    Sequence conflicti329 – 3291D → N in AAA61141. (PubMed:3858812)Curated
    Sequence conflicti351 – 3511P → Q in AAH59367. (PubMed:15489334)Curated
    Sequence conflicti380 – 3812NS → SD AA sequence (PubMed:6833213)Curated
    Sequence conflicti436 – 4361N → D AA sequence (PubMed:6833213)Curated
    Sequence conflicti558 – 5614PQNT → TQNP AA sequence (PubMed:6833213)Curated
    Sequence conflicti591 – 5911E → Q AA sequence (PubMed:6833213)Curated
    Sequence conflicti672 – 6721E → Q AA sequence (PubMed:6833213)Curated
    Sequence conflicti691 – 6911E → G in AAA61142. (PubMed:6322780)Curated

    Polymorphismi

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti42 – 421R → L.
    Corresponds to variant rs41298293 [ dbSNP | Ensembl ].
    VAR_034569
    Natural varianti55 – 551S → R.1 Publication
    Corresponds to variant rs8177318 [ dbSNP | Ensembl ].
    VAR_029280
    Natural varianti76 – 761A → V.
    Corresponds to variant rs41298977 [ dbSNP | Ensembl ].
    VAR_034570
    Natural varianti77 – 771D → N in ATRAF. 1 Publication
    VAR_038810
    Natural varianti142 – 1421G → S.1 Publication
    Corresponds to variant rs1799830 [ dbSNP | Ensembl ].
    VAR_011997
    Natural varianti277 – 2771G → S in allele TF*C3; associated with a reduction in total iron binding capacity; risk factor for iron deficiency anemia in menstruating white women. 3 Publications
    Corresponds to variant rs1799899 [ dbSNP | Ensembl ].
    VAR_011998
    Natural varianti296 – 2961D → G in allele TF*D1. 1 Publication
    Corresponds to variant rs8177238 [ dbSNP | Ensembl ].
    VAR_007544
    Natural varianti319 – 3191H → R in allele TF*CHI.
    Corresponds to variant rs41295774 [ dbSNP | Ensembl ].
    VAR_007545
    Natural varianti377 – 3771W → C.
    Corresponds to variant rs1804498 [ dbSNP | Ensembl ].
    VAR_011999
    Natural varianti448 – 4481I → V.13 Publications
    Corresponds to variant rs2692696 [ dbSNP | Ensembl ].
    VAR_058199
    Natural varianti477 – 4771A → P in ATRAF. 1 Publication
    VAR_012997
    Natural varianti562 – 5621G → V.
    Corresponds to variant rs41296590 [ dbSNP | Ensembl ].
    VAR_034571
    Natural varianti589 – 5891P → S in allele TF*C2. 4 Publications
    Corresponds to variant rs1049296 [ dbSNP | Ensembl ].
    VAR_012000
    Natural varianti645 – 6451T → P.
    Corresponds to variant rs1130537 [ dbSNP | Ensembl ].
    VAR_012001
    Natural varianti646 – 6461K → E in allele TF*BV. 1 Publication
    VAR_012998
    Natural varianti671 – 6711G → E in allele TF*B2. 1 Publication
    Corresponds to variant rs121918677 [ dbSNP | Ensembl ].
    VAR_012999

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS3080.1.
    PIRiA20981. TFHUP.
    RefSeqiNP_001054.1. NM_001063.3.
    UniGeneiHs.518267.

    Genome annotation databases

    EnsembliENST00000402696; ENSP00000385834; ENSG00000091513.
    GeneIDi7018.
    KEGGihsa:7018.
    UCSCiuc003epu.2. human.

    Polymorphism databases

    DMDMi313104271.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Transferrin entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS3080.1.
    PIRi A20981. TFHUP.
    RefSeqi NP_001054.1. NM_001063.3.
    UniGenei Hs.518267.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P02787.
    SMRi P02787. Positions 20-698.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112876. 23 interactions.
    DIPi DIP-2738N.
    IntActi P02787. 33 interactions.
    MINTi MINT-1400694.
    STRINGi 9606.ENSP00000264998.

    Chemistry

    ChEMBLi CHEMBL4865.
    DrugBanki DB01370. Aluminium.
    DB01402. Bismuth.
    DB00893. Iron Dextran.

    Protein family/group databases

    MEROPSi S60.972.

    PTM databases

    PhosphoSitei P02787.
    UniCarbKBi P02787.

    Polymorphism databases

    DMDMi 313104271.

    2D gel databases

    DOSAC-COBS-2DPAGE P02787.
    REPRODUCTION-2DPAGE IPI00022463.
    P02787.
    SWISS-2DPAGE P02787.
    UCD-2DPAGE P02787.

    Proteomic databases

    MaxQBi P02787.
    PaxDbi P02787.
    PRIDEi P02787.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000402696 ; ENSP00000385834 ; ENSG00000091513 .
    GeneIDi 7018.
    KEGGi hsa:7018.
    UCSCi uc003epu.2. human.

    Organism-specific databases

    CTDi 7018.
    GeneCardsi GC03P133464.
    HGNCi HGNC:11740. TF.
    HPAi CAB009538.
    HPA001527.
    HPA005692.
    MIMi 190000. gene.
    209300. phenotype.
    neXtProti NX_P02787.
    Orphaneti 1195. Congenital atransferrinemia.
    PharmGKBi PA36457.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG87503.
    HOGENOMi HOG000252723.
    HOVERGENi HBG000055.
    InParanoidi P02787.
    KOi K14736.
    OMAi FYYAVAV.
    OrthoDBi EOG7D59N7.
    PhylomeDBi P02787.
    TreeFami TF324013.

    Enzyme and pathway databases

    Reactomei REACT_25060. Iron uptake and transport.
    REACT_25283. Transferrin endocytosis and recycling.

    Miscellaneous databases

    ChiTaRSi TF. human.
    EvolutionaryTracei P02787.
    GeneWikii Transferrin.
    GenomeRNAii 7018.
    NextBioi 27415.
    PMAP-CutDB P02787.
    PROi P02787.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02787.
    Bgeei P02787.
    CleanExi HS_TF.
    Genevestigatori P02787.

    Family and domain databases

    InterProi IPR016357. Transferrin.
    IPR001156. Transferrin-like_dom.
    IPR018195. Transferrin_Fe_BS.
    [Graphical view ]
    Pfami PF00405. Transferrin. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF002549. Transferrin. 1 hit.
    PRINTSi PR00422. TRANSFERRIN.
    SMARTi SM00094. TR_FER. 2 hits.
    [Graphical view ]
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    1. 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. 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. 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. 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. 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTRFE_HUMAN
    AccessioniPrimary (citable) accession number: P02787
    Secondary accession number(s): O43890
    , Q1HBA5, Q9NQB8, Q9UHV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 188 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3