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Protein

Serotransferrin

Gene

TF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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
  • iron chaperone activity Source: BHF-UCL
  • transferrin receptor binding Source: BHF-UCL

GO - Biological processi

Keywordsi

Biological processIon transport, Iron transport, Transport
LigandIron, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-8856825 Cargo recognition for clathrin-mediated endocytosis
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-8957275 Post-translational protein phosphorylation
R-HSA-917937 Iron uptake and transport
R-HSA-917977 Transferrin endocytosis and recycling
SIGNORiP02787

Protein family/group databases

MEROPSiS60.975

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

EuPathDBiHostDB:ENSG00000091513.14
HGNCiHGNC:11740 TF
MIMi190000 gene
neXtProtiNX_P02787

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 dbSNP:rs121918681EnsemblClinVar.1
Natural variantiVAR_012997477A → P in ATRAF. 1 PublicationCorresponds to variant dbSNP:rs121918679EnsemblClinVar.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
DB09146 Iron saccharate

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...) serine1
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) asparagine6 Publications1
Disulfide bondi437 ↔ 656PROSITE-ProRule annotation1 Publication
Disulfide bondi469 ↔ 542PROSITE-ProRule annotation1 Publication
Glycosylationi491N-linked (GlcNAc...) asparagine; 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) asparagine8 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
ProteomicsDBi12708
51596
TopDownProteomicsiP02787

2D gel databases

DOSAC-COBS-2DPAGEiP02787
REPRODUCTION-2DPAGEiIPI00022463
P02787
SWISS-2DPAGEiP02787
UCD-2DPAGEiP02787

PTM databases

CarbonylDBiP02787
GlyConnecti558
iPTMnetiP02787
PhosphoSitePlusiP02787
SwissPalmiP02787
UniCarbKBiP02787

Miscellaneous databases

PMAP-CutDBiP02787

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

BgeeiENSG00000091513 Expressed in 193 organ(s), highest expression level in inferior vagus X ganglion
CleanExiHS_TF
ExpressionAtlasiP02787 baseline and differential
GenevisibleiP02787 HS

Organism-specific databases

HPAiCAB009538
HPA001527
HPA005692

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi112876, 44 interactors
DIPiDIP-2738N
IntActiP02787, 54 interactors
MINTiP02787
STRINGi9606.ENSP00000385834

Structurei

Secondary structure

1698
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

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

Family and domain databases

InterProiView protein in InterPro
IPR030685 Serotransferrin_mammal
IPR016357 Transferrin
IPR001156 Transferrin-like_dom
IPR018195 Transferrin_Fe_BS
PfamiView protein in Pfam
PF00405 Transferrin, 2 hits
PIRSFiPIRSF500682 Serotransferrin, 1 hit
PIRSF002549 Transferrin, 1 hit
PRINTSiPR00422 TRANSFERRIN
SMARTiView protein in SMART
SM00094 TR_FER, 2 hits
PROSITEiView protein in 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

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 6 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8WCI6F8WCI6_HUMAN
Serotransferrin
TF
120Annotation score:
F8WEK9F8WEK9_HUMAN
Serotransferrin
TF
115Annotation score:
F8WC57F8WC57_HUMAN
Serotransferrin
TF
102Annotation score:
C9JVG0C9JVG0_HUMAN
Serotransferrin
TF
134Annotation score:
H7C5E8H7C5E8_HUMAN
Serotransferrin
TF
143Annotation score:
C9JB55C9JB55_HUMAN
Serotransferrin
TF
75Annotation score:

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 dbSNP:rs41298293Ensembl.1
Natural variantiVAR_02928055S → R1 PublicationCorresponds to variant dbSNP:rs8177318Ensembl.1
Natural variantiVAR_03457076A → V. Corresponds to variant dbSNP:rs41298977Ensembl.1
Natural variantiVAR_03881077D → N in ATRAF. 1 PublicationCorresponds to variant dbSNP:rs121918681EnsemblClinVar.1
Natural variantiVAR_011997142G → S1 PublicationCorresponds to variant dbSNP:rs1799830Ensembl.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 dbSNP:rs1799899EnsemblClinVar.1
Natural variantiVAR_007544296D → G in allele TF*D1. 1 PublicationCorresponds to variant dbSNP:rs8177238EnsemblClinVar.1
Natural variantiVAR_007545319H → R in allele TF*CHI. Corresponds to variant dbSNP:rs41295774EnsemblClinVar.1
Natural variantiVAR_011999377W → C. Corresponds to variant dbSNP:rs1804498Ensembl.1
Natural variantiVAR_058199448I → VCombined sources12 PublicationsCorresponds to variant dbSNP:rs2692696Ensembl.1
Natural variantiVAR_012997477A → P in ATRAF. 1 PublicationCorresponds to variant dbSNP:rs121918679EnsemblClinVar.1
Natural variantiVAR_034571562G → V. Corresponds to variant dbSNP:rs41296590Ensembl.1
Natural variantiVAR_012000589P → S in allele TF*C2. 4 PublicationsCorresponds to variant dbSNP:rs1049296EnsemblClinVar.1
Natural variantiVAR_012001645T → P. Corresponds to variant dbSNP:rs1130537Ensembl.1
Natural variantiVAR_012998646K → E in allele TF*BV. 1 PublicationCorresponds to variant dbSNP:rs121918678EnsemblClinVar.1
Natural variantiVAR_012999671G → E in allele TF*B2. 1 PublicationCorresponds to variant dbSNP:rs121918677EnsemblClinVar.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

Similar proteinsi

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[»]
5H52X-ray3.00A20-698[»]
5WTDX-ray2.50A20-698[»]
5X5PX-ray2.70A20-698[»]
5Y6KX-ray2.86A20-698[»]
6D03electron microscopy3.68C/D1-698[»]
6D04electron microscopy3.74C/D1-698[»]
6D05electron microscopy3.80C/D1-698[»]
ProteinModelPortaliP02787
SMRiP02787
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112876, 44 interactors
DIPiDIP-2738N
IntActiP02787, 54 interactors
MINTiP02787
STRINGi9606.ENSP00000385834

Chemistry databases

ChEMBLiCHEMBL4865
DrugBankiDB01370 Aluminium
DB01294 Bismuth Subsalicylate
DB05260 Gallium nitrate
DB00893 Iron Dextran
DB09146 Iron saccharate

Protein family/group databases

MEROPSiS60.975

PTM databases

CarbonylDBiP02787
GlyConnecti558
iPTMnetiP02787
PhosphoSitePlusiP02787
SwissPalmiP02787
UniCarbKBiP02787

Polymorphism and mutation databases

BioMutaiTF
DMDMi313104271

2D gel databases

DOSAC-COBS-2DPAGEiP02787
REPRODUCTION-2DPAGEiIPI00022463
P02787
SWISS-2DPAGEiP02787
UCD-2DPAGEiP02787

Proteomic databases

EPDiP02787
MaxQBiP02787
PaxDbiP02787
PeptideAtlasiP02787
PRIDEiP02787
ProteomicsDBi12708
51596
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
EuPathDBiHostDB:ENSG00000091513.14
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
OMAiREGTCPE
OrthoDBiEOG091G0242
PhylomeDBiP02787
TreeFamiTF324013

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-8856825 Cargo recognition for clathrin-mediated endocytosis
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-8957275 Post-translational protein phosphorylation
R-HSA-917937 Iron uptake and transport
R-HSA-917977 Transferrin endocytosis and recycling
SIGNORiP02787

Miscellaneous databases

ChiTaRSiTF human
EvolutionaryTraceiP02787
GeneWikiiTransferrin
GenomeRNAii7018
PMAP-CutDBiP02787
PROiPR:P02787
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000091513 Expressed in 193 organ(s), highest expression level in inferior vagus X ganglion
CleanExiHS_TF
ExpressionAtlasiP02787 baseline and differential
GenevisibleiP02787 HS

Family and domain databases

InterProiView protein in InterPro
IPR030685 Serotransferrin_mammal
IPR016357 Transferrin
IPR001156 Transferrin-like_dom
IPR018195 Transferrin_Fe_BS
PfamiView protein in Pfam
PF00405 Transferrin, 2 hits
PIRSFiPIRSF500682 Serotransferrin, 1 hit
PIRSF002549 Transferrin, 1 hit
PRINTSiPR00422 TRANSFERRIN
SMARTiView protein in SMART
SM00094 TR_FER, 2 hits
PROSITEiView protein in 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
ProtoNetiSearch...

Entry informationi

Entry nameiTRFE_HUMAN
AccessioniPrimary (citable) accession number: P02787
Secondary accession number(s): O43890
, Q1HBA5, Q9NQB8, Q9UHV0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 30, 2010
Last modified: November 7, 2018
This is version 229 of the entry and version 3 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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