Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serotransferrin

Gene

TF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Metal bindingi82Iron 11
Metal bindingi114Iron 11
Binding sitei139Carbonate 11
Binding sitei143Carbonate 11
Binding sitei145Carbonate 1; via amide nitrogen1
Binding sitei146Carbonate 1; via amide nitrogen1
Metal bindingi207Iron 11
Metal bindingi268Iron 11
Metal bindingi411Iron 2PROSITE-ProRule annotation1
Metal bindingi445Iron 2PROSITE-ProRule annotation1
Binding sitei471Carbonate 2PROSITE-ProRule annotation1
Binding sitei475Carbonate 2PROSITE-ProRule annotation1
Binding sitei477Carbonate 2; via amide nitrogenPROSITE-ProRule annotation1
Binding sitei478Carbonate 2; via amide nitrogenPROSITE-ProRule annotation1
Metal bindingi536Iron 2PROSITE-ProRule annotation1
Metal bindingi604Iron 2PROSITE-ProRule annotation1

GO - Molecular functioni

  • ferric iron binding Source: InterPro
  • ferric iron transmembrane transporter activity Source: InterPro
  • ferrous iron binding Source: BHF-UCL
  • transferrin receptor binding Source: BHF-UCL

GO - Biological processi

  • cellular iron ion homeostasis Source: Reactome
  • cellular response to iron ion Source: BHF-UCL
  • ferrous iron import into cell Source: BHF-UCL
  • iron ion homeostasis Source: BHF-UCL
  • platelet degranulation Source: Reactome
  • positive regulation of receptor-mediated endocytosis Source: BHF-UCL
  • regulation of protein stability Source: BHF-UCL
  • retina homeostasis Source: UniProtKB
  • transferrin transport Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Ion transport, Iron transport, Transport

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000091513-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
R-HSA-917937. Iron uptake and transport.
R-HSA-917977. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:11740. TF.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • basal part of cell Source: UniProtKB
  • basal plasma membrane Source: UniProtKB
  • blood microparticle Source: UniProtKB
  • cell surface Source: UniProtKB
  • clathrin-coated pit Source: UniProtKB
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB
  • early endosome Source: UniProtKB
  • endocytic vesicle Source: MGI
  • endosome membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • extrinsic component of external side of plasma membrane Source: BHF-UCL
  • HFE-transferrin receptor complex Source: BHF-UCL
  • late endosome Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • recycling endosome Source: UniProtKB
  • secretory granule lumen Source: Reactome
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Atransferrinemia (ATRAF)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare autosomal recessive disorder characterized by abnormal synthesis of transferrin leading to iron overload and microcytic hypochromic anemia.
See also OMIM:209300
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03881077D → N in ATRAF. 1 PublicationCorresponds to variant rs121918681dbSNPEnsembl.1
Natural variantiVAR_012997477A → P in ATRAF. 1 PublicationCorresponds to variant rs121918679dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi7018.
MalaCardsiTF.
MIMi209300. phenotype.
OpenTargetsiENSG00000091513.
Orphaneti1195. Congenital atransferrinemia.
PharmGKBiPA36457.

Chemistry databases

ChEMBLiCHEMBL4865.
DrugBankiDB01370. Aluminium.
DB01294. Bismuth Subsalicylate.
DB05260. Gallium nitrate.
DB00893. Iron Dextran.

Polymorphism and mutation databases

BioMutaiTF.
DMDMi313104271.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000003571520 – 698SerotransferrinAdd BLAST679

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 67PROSITE-ProRule annotation1 Publication
Disulfide bondi38 ↔ 58PROSITE-ProRule annotation1 Publication
Modified residuei42Dimethylated arginineBy similarity1
GlycosylationiCAR_00007351O-linked (GalNAc...)1
Disulfide bondi137 ↔ 213PROSITE-ProRule annotation1 Publication
Disulfide bondi156 ↔ 350PROSITE-ProRule annotation1 Publication
Disulfide bondi177 ↔ 193PROSITE-ProRule annotation1 Publication
Disulfide bondi180 ↔ 196PROSITE-ProRule annotation1 Publication
Disulfide bondi190 ↔ 198PROSITE-ProRule annotation1 Publication
Disulfide bondi246 ↔ 260PROSITE-ProRule annotation1 Publication
Disulfide bondi358 ↔ 615PROSITE-ProRule annotation1 Publication
Disulfide bondi364 ↔ 396PROSITE-ProRule annotation1 Publication
Disulfide bondi374 ↔ 387PROSITE-ProRule annotation1 Publication
Modified residuei389Phosphoserine; by FAM20C1 Publication1
Disulfide bondi421 ↔ 693PROSITE-ProRule annotation1 Publication
GlycosylationiCAR_000074432N-linked (GlcNAc...) (complex)6 Publications1
Disulfide bondi437 ↔ 656PROSITE-ProRule annotation1 Publication
Disulfide bondi469 ↔ 542PROSITE-ProRule annotation1 Publication
Glycosylationi491N-linked (GlcNAc...); atypical; partial1 Publication1
Disulfide bondi493 ↔ 684PROSITE-ProRule annotation1 Publication
Disulfide bondi503 ↔ 517PROSITE-ProRule annotation1 Publication
Disulfide bondi514 ↔ 525PROSITE-ProRule annotation1 Publication
Disulfide bondi582 ↔ 596PROSITE-ProRule annotation1 Publication
GlycosylationiCAR_000075630N-linked (GlcNAc...) (complex)8 Publications1
Disulfide bondi634 ↔ 639PROSITE-ProRule annotation1 Publication
Modified residuei685Phosphoserine; by FAM20C1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

EPDiP02787.
MaxQBiP02787.
PaxDbiP02787.
PeptideAtlasiP02787.
PRIDEiP02787.
TopDownProteomicsiP02787.

2D gel databases

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

PTM databases

iPTMnetiP02787.
PhosphoSitePlusiP02787.
SwissPalmiP02787.
UniCarbKBiP02787.

Miscellaneous databases

PMAP-CutDBP02787.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

BgeeiENSG00000091513.
CleanExiHS_TF.
ExpressionAtlasiP02787. baseline and differential.
GenevisibleiP02787. HS.

Organism-specific databases

HPAiCAB009538.
HPA001527.
HPA005692.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

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

GO - Molecular functioni

  • transferrin receptor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi112876. 38 interactors.
DIPiDIP-2738N.
IntActiP02787. 33 interactors.
MINTiMINT-1400694.
STRINGi9606.ENSP00000385834.

Structurei

Secondary structure

1698
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 30Combined sources7
Helixi31 – 48Combined sources18
Beta strandi51 – 54Combined sources4
Beta strandi55 – 63Combined sources9
Helixi64 – 72Combined sources9
Beta strandi78 – 81Combined sources4
Helixi83 – 90Combined sources8
Turni92 – 94Combined sources3
Beta strandi97 – 105Combined sources9
Beta strandi107 – 121Combined sources15
Helixi128 – 130Combined sources3
Beta strandi136 – 139Combined sources4
Turni144 – 147Combined sources4
Helixi148 – 154Combined sources7
Helixi155 – 157Combined sources3
Beta strandi158 – 160Combined sources3
Helixi165 – 172Combined sources8
Beta strandi173 – 177Combined sources5
Turni183 – 185Combined sources3
Helixi187 – 190Combined sources4
Beta strandi191 – 193Combined sources3
Helixi194 – 196Combined sources3
Beta strandi198 – 202Combined sources5
Helixi206 – 215Combined sources10
Beta strandi220 – 225Combined sources6
Helixi228 – 232Combined sources5
Helixi236 – 239Combined sources4
Beta strandi242 – 245Combined sources4
Turni247 – 249Combined sources3
Beta strandi251 – 253Combined sources3
Helixi254 – 259Combined sources6
Beta strandi262 – 266Combined sources5
Beta strandi269 – 272Combined sources4
Beta strandi274 – 276Combined sources3
Helixi279 – 293Combined sources15
Turni295 – 297Combined sources3
Beta strandi298 – 300Combined sources3
Beta strandi310 – 314Combined sources5
Beta strandi318 – 323Combined sources6
Helixi330 – 334Combined sources5
Helixi336 – 345Combined sources10
Turni346 – 348Combined sources3
Helixi354 – 357Combined sources4
Beta strandi360 – 365Combined sources6
Helixi368 – 380Combined sources13
Turni381 – 383Combined sources3
Beta strandi384 – 389Combined sources6
Helixi393 – 401Combined sources9
Beta strandi407 – 410Combined sources4
Helixi412 – 420Combined sources9
Beta strandi424 – 430Combined sources7
Helixi437 – 439Combined sources3
Beta strandi445 – 452Combined sources8
Beta strandi455 – 457Combined sources3
Helixi460 – 462Combined sources3
Beta strandi466 – 471Combined sources6
Turni476 – 479Combined sources4
Helixi480 – 485Combined sources6
Helixi487 – 489Combined sources3
Helixi495 – 497Combined sources3
Beta strandi498 – 503Combined sources6
Beta strandi509 – 511Combined sources3
Helixi512 – 514Combined sources3
Helixi521 – 523Combined sources3
Beta strandi531 – 533Combined sources3
Helixi535 – 545Combined sources11
Beta strandi548 – 553Combined sources6
Helixi556 – 559Combined sources4
Turni568 – 572Combined sources5
Helixi575 – 577Combined sources3
Beta strandi578 – 581Combined sources4
Beta strandi583 – 585Combined sources3
Beta strandi587 – 589Combined sources3
Helixi590 – 595Combined sources6
Beta strandi598 – 601Combined sources4
Beta strandi605 – 608Combined sources4
Helixi610 – 612Combined sources3
Helixi613 – 627Combined sources15
Beta strandi628 – 630Combined sources3
Beta strandi635 – 637Combined sources3
Beta strandi644 – 646Combined sources3
Beta strandi648 – 650Combined sources3
Beta strandi656 – 659Combined sources4
Helixi661 – 663Combined sources3
Helixi666 – 669Combined sources4
Helixi672 – 684Combined sources13
Helixi688 – 694Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4X1BX-ray2.45A20-698[»]
4X1DX-ray2.80A/B20-698[»]
5DYHX-ray2.68A/B1-698[»]
ProteinModelPortaliP02787.
SMRiP02787.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02787.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 347Transferrin-like 1PROSITE-ProRule annotationAdd BLAST323
Domaini361 – 683Transferrin-like 2PROSITE-ProRule annotationAdd BLAST323

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IEAI. Eukaryota.
ENOG410XQ36. LUCA.
GeneTreeiENSGT00390000001619.
HOGENOMiHOG000252723.
HOVERGENiHBG000055.
InParanoidiP02787.
KOiK14736.
OMAiIGLLYCD.
OrthoDBiEOG091G0242.
PhylomeDBiP02787.
TreeFamiTF324013.

Family and domain databases

InterProiIPR030685. Serotransferrin_mammal.
IPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF500682. Serotransferrin. 1 hit.
PIRSF002549. 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

        10         20         30         40         50
MRLAVGALLV CAVLGLCLAV PDKTVRWCAV SEHEATKCQS FRDHMKSVIP
60 70 80 90 100
SDGPSVACVK KASYLDCIRA IAANEADAVT LDAGLVYDAY LAPNNLKPVV
110 120 130 140 150
AEFYGSKEDP QTFYYAVAVV KKDSGFQMNQ LRGKKSCHTG LGRSAGWNIP
160 170 180 190 200
IGLLYCDLPE PRKPLEKAVA NFFSGSCAPC ADGTDFPQLC QLCPGCGCST
210 220 230 240 250
LNQYFGYSGA FKCLKDGAGD VAFVKHSTIF ENLANKADRD QYELLCLDNT
260 270 280 290 300
RKPVDEYKDC HLAQVPSHTV VARSMGGKED LIWELLNQAQ EHFGKDKSKE
310 320 330 340 350
FQLFSSPHGK DLLFKDSAHG FLKVPPRMDA KMYLGYEYVT AIRNLREGTC
360 370 380 390 400
PEAPTDECKP VKWCALSHHE RLKCDEWSVN SVGKIECVSA ETTEDCIAKI
410 420 430 440 450
MNGEADAMSL DGGFVYIAGK CGLVPVLAEN YNKSDNCEDT PEAGYFAIAV
460 470 480 490 500
VKKSASDLTW DNLKGKKSCH TAVGRTAGWN IPMGLLYNKI NHCRFDEFFS
510 520 530 540 550
EGCAPGSKKD SSLCKLCMGS GLNLCEPNNK EGYYGYTGAF RCLVEKGDVA
560 570 580 590 600
FVKHQTVPQN TGGKNPDPWA KNLNEKDYEL LCLDGTRKPV EEYANCHLAR
610 620 630 640 650
APNHAVVTRK DKEACVHKIL RQQQHLFGSN VTDCSGNFCL FRSETKDLLF
660 670 680 690
RDDTVCLAKL HDRNTYEKYL GEEYVKAVGN LRKCSTSSLL EACTFRRP
Length:698
Mass (Da):77,064
Last modified:November 30, 2010 - v3
Checksum:i9A73B90D8C5671E9
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti216D → N in AAH59367 (PubMed:15489334).Curated1
Sequence conflicti264Q → E AA sequence (PubMed:6833213).Curated1
Sequence conflicti329D → N AA sequence (PubMed:6833213).Curated1
Sequence conflicti329D → N in AAA61141 (PubMed:3858812).Curated1
Sequence conflicti351P → Q in AAH59367 (PubMed:15489334).Curated1
Sequence conflicti380 – 381NS → SD AA sequence (PubMed:6833213).Curated2
Sequence conflicti436N → D AA sequence (PubMed:6833213).Curated1
Sequence conflicti558 – 561PQNT → TQNP AA sequence (PubMed:6833213).Curated4
Sequence conflicti591E → Q AA sequence (PubMed:6833213).Curated1
Sequence conflicti672E → Q AA sequence (PubMed:6833213).Curated1
Sequence conflicti691E → G in AAA61142 (PubMed:6322780).Curated1

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_03456942R → L.Corresponds to variant rs41298293dbSNPEnsembl.1
Natural variantiVAR_02928055S → R.1 PublicationCorresponds to variant rs8177318dbSNPEnsembl.1
Natural variantiVAR_03457076A → V.Corresponds to variant rs41298977dbSNPEnsembl.1
Natural variantiVAR_03881077D → N in ATRAF. 1 PublicationCorresponds to variant rs121918681dbSNPEnsembl.1
Natural variantiVAR_011997142G → S.1 PublicationCorresponds to variant rs1799830dbSNPEnsembl.1
Natural variantiVAR_011998277G → 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 PublicationsCorresponds to variant rs1799899dbSNPEnsembl.1
Natural variantiVAR_007544296D → G in allele TF*D1. 1 PublicationCorresponds to variant rs8177238dbSNPEnsembl.1
Natural variantiVAR_007545319H → R in allele TF*CHI. Corresponds to variant rs41295774dbSNPEnsembl.1
Natural variantiVAR_011999377W → C.Corresponds to variant rs1804498dbSNPEnsembl.1
Natural variantiVAR_058199448I → V.Combined sources12 PublicationsCorresponds to variant rs2692696dbSNPEnsembl.1
Natural variantiVAR_012997477A → P in ATRAF. 1 PublicationCorresponds to variant rs121918679dbSNPEnsembl.1
Natural variantiVAR_034571562G → V.Corresponds to variant rs41296590dbSNPEnsembl.1
Natural variantiVAR_012000589P → S in allele TF*C2. 4 PublicationsCorresponds to variant rs1049296dbSNPEnsembl.1
Natural variantiVAR_012001645T → P.Corresponds to variant rs1130537dbSNPEnsembl.1
Natural variantiVAR_012998646K → E in allele TF*BV. 1 PublicationCorresponds to variant rs121918678dbSNPEnsembl.1
Natural variantiVAR_012999671G → E in allele TF*B2. 1 PublicationCorresponds to variant rs121918677dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
XP_016862578.1. XM_017007089.1.
XP_016862579.1. XM_017007090.1.
UniGeneiHs.518267.

Genome annotation databases

EnsembliENST00000402696; ENSP00000385834; ENSG00000091513.
GeneIDi7018.
KEGGihsa:7018.
UCSCiuc003epv.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Transferrin entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
XP_016862578.1. XM_017007089.1.
XP_016862579.1. XM_017007090.1.
UniGeneiHs.518267.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4X1BX-ray2.45A20-698[»]
4X1DX-ray2.80A/B20-698[»]
5DYHX-ray2.68A/B1-698[»]
ProteinModelPortaliP02787.
SMRiP02787.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112876. 38 interactors.
DIPiDIP-2738N.
IntActiP02787. 33 interactors.
MINTiMINT-1400694.
STRINGi9606.ENSP00000385834.

Chemistry databases

ChEMBLiCHEMBL4865.
DrugBankiDB01370. Aluminium.
DB01294. Bismuth Subsalicylate.
DB05260. Gallium nitrate.
DB00893. Iron Dextran.

Protein family/group databases

MEROPSiS60.972.

PTM databases

iPTMnetiP02787.
PhosphoSitePlusiP02787.
SwissPalmiP02787.
UniCarbKBiP02787.

Polymorphism and mutation databases

BioMutaiTF.
DMDMi313104271.

2D gel databases

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

Proteomic databases

EPDiP02787.
MaxQBiP02787.
PaxDbiP02787.
PeptideAtlasiP02787.
PRIDEiP02787.
TopDownProteomicsiP02787.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000402696; ENSP00000385834; ENSG00000091513.
GeneIDi7018.
KEGGihsa:7018.
UCSCiuc003epv.2. human.

Organism-specific databases

CTDi7018.
DisGeNETi7018.
GeneCardsiTF.
HGNCiHGNC:11740. TF.
HPAiCAB009538.
HPA001527.
HPA005692.
MalaCardsiTF.
MIMi190000. gene.
209300. phenotype.
neXtProtiNX_P02787.
OpenTargetsiENSG00000091513.
Orphaneti1195. Congenital atransferrinemia.
PharmGKBiPA36457.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEAI. Eukaryota.
ENOG410XQ36. LUCA.
GeneTreeiENSGT00390000001619.
HOGENOMiHOG000252723.
HOVERGENiHBG000055.
InParanoidiP02787.
KOiK14736.
OMAiIGLLYCD.
OrthoDBiEOG091G0242.
PhylomeDBiP02787.
TreeFamiTF324013.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000091513-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
R-HSA-917937. Iron uptake and transport.
R-HSA-917977. Transferrin endocytosis and recycling.

Miscellaneous databases

ChiTaRSiTF. human.
EvolutionaryTraceiP02787.
GeneWikiiTransferrin.
GenomeRNAii7018.
PMAP-CutDBP02787.
PROiP02787.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000091513.
CleanExiHS_TF.
ExpressionAtlasiP02787. baseline and differential.
GenevisibleiP02787. HS.

Family and domain databases

InterProiIPR030685. Serotransferrin_mammal.
IPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF500682. Serotransferrin. 1 hit.
PIRSF002549. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 209 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.