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Entry version 231 (13 Feb 2019)
Sequence version 6 (24 Jan 2006)
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Protein

Lactotransferrin

Gene

LTF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate.
Lactotransferrin is a major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity, which depends on the extracellular cation concentration. Antimicrobial properties include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. Can also prevent bacterial biofilm development in P.aeruginosa infection. Has weak antifungal activity against C.albicans. Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. Promotes binding of species C adenoviruses to epithelial cells, promoting adenovirus infection. Can inhibit papillomavirus infections. Stimulates the TLR4 signaling pathway leading to NF-kappa-B activation and subsequent pro-inflammatory cytokine production while also interfering with the lipopolysaccharide (LPS)-stimulated TLR4 signaling. Inhibits neutrophil granulocyte migration to sites of apoptosis, when secreted by apoptotic cells. Stimulates VEGFA-mediated endothelial cell migration and proliferation. Binds heparin, chondroitin sulfate and possibly other glycosaminoglycans (GAGs). Also binds specifically to pneumococcal surface protein A (pspA), the lipid A portion of bacterial lipopolysaccharide (LPS), lysozyme and DNA.
Lactoferricin binds to the bacterial surface and is crucial for the bactericidal functions. Has some antiviral activity against papillomavirus infection. N-terminal region shows strong antifungal activity against C.albicans. Contains two BBXB heparin-binding consensus sequences that appear to form the predominate functional GAG-binding site.
Kaliocin-1 has antimicrobial activity and is able to permeabilize different ions through liposomal membranes.
Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors.
The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites.
Isoform DeltaLf: transcription factor with antiproliferative properties and ability to induce cell cycle arrest. Binds to the DeltaLf response element found in the SKP1, BAX, DCPS, and SELENOH promoters.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei23PspA1
Binding sitei32PspA1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi79Iron or copper 1PROSITE-ProRule annotation13 Publications1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei92Curated1
Metal bindingi111Iron or copper 1PROSITE-ProRule annotation13 Publications1
Binding sitei136Carbonate or oxalate 1PROSITE-ProRule annotation14 Publications1
Binding sitei140Carbonate or oxalate 1PROSITE-ProRule annotation14 Publications1
Binding sitei142Carbonate or oxalate 1; via amide nitrogenPROSITE-ProRule annotation14 Publications1
Binding sitei143Carbonate or oxalate 1; via amide nitrogenPROSITE-ProRule annotation14 Publications1
Metal bindingi211Iron or copper 1PROSITE-ProRule annotation13 Publications1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei229Important for iron binding1
Metal bindingi272Iron or copper 1; via tele nitrogenPROSITE-ProRule annotation13 Publications1
Active sitei278NucleophileCurated1
Metal bindingi414Iron or copper 2PROSITE-ProRule annotation13 Publications1
Metal bindingi454Iron or copper 2PROSITE-ProRule annotation13 Publications1
Binding sitei480Carbonate or oxalate 2PROSITE-ProRule annotation14 Publications1
Binding sitei484Carbonate or oxalate 2PROSITE-ProRule annotation14 Publications1
Binding sitei486Carbonate or oxalate 2; via amide nitrogenPROSITE-ProRule annotation14 Publications1
Binding sitei487Carbonate or oxalate 2; via amide nitrogenPROSITE-ProRule annotation14 Publications1
Metal bindingi547Iron or copper 2PROSITE-ProRule annotation13 Publications1
Metal bindingi616Iron or copper 2; via tele nitrogenPROSITE-ProRule annotation13 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAntibiotic, Antimicrobial, DNA-binding, Heparin-binding, Hydrolase, Protease, Serine protease
Biological processImmunity, Ion transport, Iron transport, Osteogenesis, Transcription, Transcription regulation, Transport
LigandIron, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1222449 Mtb iron assimilation by chelation
R-HSA-6798695 Neutrophil degranulation
R-HSA-6799990 Metal sequestration by antimicrobial proteins
R-HSA-6803157 Antimicrobial peptides
R-HSA-977225 Amyloid fiber formation

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P02788

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S60.001

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Lactotransferrin (EC:3.4.21.-)
Short name:
Lactoferrin
Alternative name(s):
Growth-inhibiting protein 12
Talalactoferrin
Cleaved into the following 5 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:LTF
Synonyms:GIG12, LF
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000012223.12

Human Gene Nomenclature Database

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HGNCi
HGNC:6720 LTF

Online Mendelian Inheritance in Man (OMIM)

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MIMi
150210 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P02788

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi20 – 23Missing : Abolishes binding to heparin, lipid A, lysozyme and DNA. 1 Publication4
Mutagenesisi20 – 22Missing : Greatly impairs binding to heparin, lipid A, lysozyme and DNA. Impairs antibacterial activity. 1 Publication3
Mutagenesisi20 – 21Missing : Impairs binding to heparin, lipid A, lysozyme and DNA. 2
Mutagenesisi79D → S: Impairs iron binding and changes domain closure. 1 Publication1
Mutagenesisi92K → A: Almost no protease activity. 1 Publication1
Mutagenesisi140R → D, E or S: Disrupts anion binding site and destabilizes iron binding. 2 Publications1
Mutagenesisi229R → G or E: Destabilizes iron binding slightly. 2 Publications1
Mutagenesisi229R → K or L: Destabilizes iron binding significantly. 2 Publications1
Mutagenesisi270P → V: No effect. 1 Publication1
Mutagenesisi272H → A, C, G, E, F, L, M, P, Q, T or Y: Destabilizes iron binding. 1 Publication1
Mutagenesisi278S → A: No protease activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
4057

Open Targets

More...
OpenTargetsi
ENSG00000012223

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA30482

Protein family/group databases

Allergome; a platform for allergen knowledge

More...
Allergomei
1384 Hom s LF

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB06987 2-(4-(2-HYDROXY-3-(ISOPROPYLAMINO)PROPOXY)PHENYL)ETHANAMIDE
DB03485 Alpha-D-Fucose
DB03017 Lauric Acid
DB04743 Nimesulide
DB03040 Nitrilotriacetic Acid
DB08439 Parecoxib

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
LTF

Domain mapping of disease mutations (DMDM)

More...
DMDMi
85700158

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 191 PublicationAdd BLAST19
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003573220 – 710LactotransferrinAdd BLAST691
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_000042277020 – 67Lactoferricin-HAdd BLAST48
PeptideiPRO_0000035733171 – 201Kaliocin-1Add BLAST31
PeptideiPRO_0000035734338 – 343Lactoferroxin-A6
PeptideiPRO_0000035735543 – 547Lactoferroxin-B5
PeptideiPRO_0000035736680 – 686Lactoferroxin-C7

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi28 ↔ 64
Disulfide bondi38 ↔ 55
Disulfide bondi134 ↔ 217
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi156N-linked (GlcNAc...) asparagine7 Publications1
Disulfide bondi176 ↔ 192
Disulfide bondi189 ↔ 200
Disulfide bondi250 ↔ 264
Disulfide bondi367 ↔ 399
Disulfide bondi377 ↔ 390
Disulfide bondi424 ↔ 705
Disulfide bondi446 ↔ 668
Disulfide bondi478 ↔ 553
Glycosylationi497N-linked (GlcNAc...) asparagine6 Publications1
Disulfide bondi502 ↔ 696
Disulfide bondi512 ↔ 526
Disulfide bondi523 ↔ 536
Disulfide bondi594 ↔ 608
Glycosylationi642N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi646 ↔ 651
Isoform DeltaLf (identifier: P02788-2)
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki379Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki391Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Isoform DeltaLf: Ubiquitinated at Lys-379 and Lys-391.
Poly-N-acetyllactosaminic carbohydrate moiety seems to be needed for TLR4 activation.

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P02788

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P02788

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P02788

PeptideAtlas

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PeptideAtlasi
P02788

PRoteomics IDEntifications database

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PRIDEi
P02788

ProteomicsDB human proteome resource

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ProteomicsDBi
12709
51597

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
320

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P02788

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P02788

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P02788

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

High levels are found in saliva and tears, intermediate levels in serum and plasma, and low levels in urine. In kidney, detected in the distal collecting tubules in the medulla but not in the cortical region or in blood vessels. Detected in peripheral blood neutrophils (at protein level). Isoform 1 and isoform DeltaLf are expressed in breast, prostate, spleen, pancreas, kidney, small intestine, lung, skeletal muscle, uterus, thymus and fetal liver. Isoform 1 is expressed in brain, testis and peripheral blood leukocytes; isoform DeltaLf is barely detectable in these tissues. Isoform DeltaLf is expressed in placenta, liver and ovary; isoform 1 is barely detectable in these tissues. In kidney, isoform 1 is expressed at high levels in the collecting tubules of the medulla but at very low levels in the cortex.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000012223 Expressed in 159 organ(s), highest expression level in trachea

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P02788 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P02788 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB008646
CAB016201
HPA057177
HPA059976

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer. Found in a complex with LTF, CLU, EPPIN and SEMG1.20 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
110235, 45 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P02788

Database of interacting proteins

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DIPi
DIP-41354N

Protein interaction database and analysis system

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IntActi
P02788, 19 interactors

Molecular INTeraction database

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MINTi
P02788

STRING: functional protein association networks

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STRINGi
9606.ENSP00000231751

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1710
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B0LX-ray2.20A20-710[»]
1BKAX-ray2.40A20-710[»]
1CB6X-ray2.00A20-710[»]
1DSNX-ray2.05A21-352[»]
1EH3X-ray2.00A21-352[»]
1FCKX-ray2.20A21-710[»]
1H43X-ray2.20A21-352[»]
1H44X-ray2.00A21-352[»]
1H45X-ray1.95A21-352[»]
1HSEX-ray2.20A21-353[»]
1L5TX-ray3.00A/B21-351[»]
1LCFX-ray2.00A20-710[»]
1LCTX-ray2.00A21-352[»]
1LFGX-ray2.20A20-710[»]
1LFHX-ray2.80A20-710[»]
1LFIX-ray2.10A20-710[»]
1LGBX-ray3.30C110-268[»]
1N76X-ray3.40A21-710[»]
1SQYX-ray2.50A20-710[»]
1U62NMR-A39-49[»]
1VFDX-ray2.50A20-349[»]
1VFEX-ray2.30A20-352[»]
1XV4NMR-A39-49[»]
1XV7NMR-A39-49[»]
1Z6VNMR-A21-67[»]
1Z6WNMR-A21-67[»]
2BJJX-ray2.40X21-710[»]
2DP4X-ray2.90I528-535[»]
2GMCNMR-A39-49[»]
2GMDNMR-A39-49[»]
2HD4X-ray2.15B528-535[»]
2PMSX-ray2.91A/B21-362[»]

Database of protein disorder

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DisProti
DP00616

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P02788

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P02788

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P02788

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini25 – 352Transferrin-like 1PROSITE-ProRule annotationAdd BLAST328
Domaini364 – 695Transferrin-like 2PROSITE-ProRule annotationAdd BLAST332

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni20 – 29Bactericidal and antifungal activity10
Regioni20 – 24Critical for glycosaminoglycan, lipid A, lysozyme and DNA binding5
Regioni21 – 22Important for full bactericidal and antifungal activities2
Regioni39 – 49Bactericidal and antifungal activityAdd BLAST11
Regioni39 – 49Interaction with lipopolysaccharideAdd BLAST11
Regioni39 – 46Interaction with pspA8
Regioni46 – 51Involved in glycosaminoglycan binding6
Regioni57 – 58Interaction with pspA2

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the transferrin family.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IEAI Eukaryota
ENOG410XQ36 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156055

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000055

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P02788

KEGG Orthology (KO)

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KOi
K17283

Identification of Orthologs from Complete Genome Data

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OMAi
NKCAFSS

Database of Orthologous Groups

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OrthoDBi
436779at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P02788

TreeFam database of animal gene trees

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TreeFami
TF324013

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR030684 Lactotransferrin
IPR016357 Transferrin
IPR001156 Transferrin-like_dom
IPR018195 Transferrin_Fe_BS

The PANTHER Classification System

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PANTHERi
PTHR11485:SF33 PTHR11485:SF33, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00405 Transferrin, 2 hits

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF500683 Lactotransferrin, 1 hit
PIRSF002549 Transferrin, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00422 TRANSFERRIN

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00094 TR_FER, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00205 TRANSFERRIN_LIKE_1, 2 hits
PS00206 TRANSFERRIN_LIKE_2, 2 hits
PS00207 TRANSFERRIN_LIKE_3, 2 hits
PS51408 TRANSFERRIN_LIKE_4, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative promoter usage. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P02788-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MKLVFLVLLF LGALGLCLAG RRRSVQWCAV SQPEATKCFQ WQRNMRKVRG
60 70 80 90 100
PPVSCIKRDS PIQCIQAIAE NRADAVTLDG GFIYEAGLAP YKLRPVAAEV
110 120 130 140 150
YGTERQPRTH YYAVAVVKKG GSFQLNELQG LKSCHTGLRR TAGWNVPIGT
160 170 180 190 200
LRPFLNWTGP PEPIEAAVAR FFSASCVPGA DKGQFPNLCR LCAGTGENKC
210 220 230 240 250
AFSSQEPYFS YSGAFKCLRD GAGDVAFIRE STVFEDLSDE AERDEYELLC
260 270 280 290 300
PDNTRKPVDK FKDCHLARVP SHAVVARSVN GKEDAIWNLL RQAQEKFGKD
310 320 330 340 350
KSPKFQLFGS PSGQKDLLFK DSAIGFSRVP PRIDSGLYLG SGYFTAIQNL
360 370 380 390 400
RKSEEEVAAR RARVVWCAVG EQELRKCNQW SGLSEGSVTC SSASTTEDCI
410 420 430 440 450
ALVLKGEADA MSLDGGYVYT AGKCGLVPVL AENYKSQQSS DPDPNCVDRP
460 470 480 490 500
VEGYLAVAVV RRSDTSLTWN SVKGKKSCHT AVDRTAGWNI PMGLLFNQTG
510 520 530 540 550
SCKFDEYFSQ SCAPGSDPRS NLCALCIGDE QGENKCVPNS NERYYGYTGA
560 570 580 590 600
FRCLAENAGD VAFVKDVTVL QNTDGNNNEA WAKDLKLADF ALLCLDGKRK
610 620 630 640 650
PVTEARSCHL AMAPNHAVVS RMDKVERLKQ VLLHQQAKFG RNGSDCPDKF
660 670 680 690 700
CLFQSETKNL LFNDNTECLA RLHGKTTYEK YLGPQYVAGI TNLKKCSTSP
710
LLEACEFLRK
Length:710
Mass (Da):78,182
Last modified:January 24, 2006 - v6
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0489CABA6D13C098
GO
Isoform DeltaLf (identifier: P02788-2) [UniParc]FASTAAdd to basket
Also known as: Delta-lactoferrin

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.

Note: Contains a phosphoserine at position 10 (alternate). Contains a O-linked (GlcNAc) serine at position 10 (alternate). O-GlcNAcylation at Ser-10 inhibits DNA binding and negatively regulates DeltaLf transcriptional activity, whereas phosphorylation activates it. Phosphorylation at Ser-10 also promotes proteasomal degradation.1 Publication
Show »
Length:666
Mass (Da):73,161
Checksum:iC498CC5861CA1A12
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7ER44E7ER44_HUMAN
Lactotransferrin
LTF
708Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9JCF5C9JCF5_HUMAN
Lactotransferrin
LTF
182Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7EQB2E7EQB2_HUMAN
Lactotransferrin
LTF
696Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti14L → P in AAA58656 (Ref. 17) Curated1
Sequence conflicti21R → S in AAH15822 (PubMed:15489334).Curated1
Sequence conflicti21R → S in AAH15823 (PubMed:15489334).Curated1
Sequence conflicti36T → D AA sequence (PubMed:8551695).Curated1
Sequence conflicti49R → C in AAH22347 (PubMed:15489334).Curated1
Sequence conflicti130G → C in AAH15823 (PubMed:15489334).Curated1
Sequence conflicti138L → R in AAH22347 (PubMed:15489334).Curated1
Sequence conflicti140Missing AA sequence (PubMed:6510420).Curated1
Sequence conflicti169Missing AA sequence (PubMed:6510420).Curated1
Sequence conflicti409 – 410DA → NASVLMDSEGGFLAR AA sequence (PubMed:6510420).Curated2
Sequence conflicti415G → E in AAA59511 (Ref. 17) Curated1
Sequence conflicti431A → G in AAA58656 (Ref. 17) Curated1
Sequence conflicti456A → T in AAH15822 (PubMed:15489334).Curated1
Sequence conflicti456A → T in AAH15823 (PubMed:15489334).Curated1
Sequence conflicti487G → A in AAA86665 (PubMed:3477300).Curated1
Sequence conflicti531Q → E AA sequence (PubMed:6510420).Curated1
Sequence conflicti537V → E in AAH15822 (PubMed:15489334).Curated1
Sequence conflicti694K → R AA sequence (PubMed:6510420).Curated1
Sequence conflicti694K → R AA sequence (PubMed:7049727).Curated1

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 5737.8 Da from positions 20 - 67. Determined by ESI. 1 Publication

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

The sequence shown corresponds to the reference genome sequence and is likely to represent the minor allele, whereas most publications refer to the longer sequence containing variant Arg-22 ins. Insertion of the additional arginine in variant Arg-22 ins creates an N-terminal basic cluster of four arginines, all of which appear to be important for the full functionality of the protein, including bactericidal and antifungal activities as well as binding to glycosaminoglycans, pspA, LPS, lysozyme and DNA.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_06929822R → RR Associated with lower plasma lactoferrin concentrations. 14 PublicationsCorresponds to variant dbSNP:rs10662431Ensembl.1
Natural variantiVAR_01350429A → T7 PublicationsCorresponds to variant dbSNP:rs1126477Ensembl.1
Natural variantiVAR_01350547K → R Decreased antibacterial activity against Gram-positive bacteria; seems to reduce susceptibility to localized juvenile periodontitis; associated with increased plasma lactoferrin concentrations and possibly with susceptibility to coronary artery stenosis. 8 PublicationsCorresponds to variant dbSNP:rs1126478Ensembl.1
Natural variantiVAR_013506148I → T1 PublicationCorresponds to variant dbSNP:rs1126479Ensembl.1
Natural variantiVAR_013507422G → C2 PublicationsCorresponds to variant dbSNP:rs1042055Ensembl.1
Natural variantiVAR_013508579E → D6 PublicationsCorresponds to variant dbSNP:rs2073495Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0443081 – 44Missing in isoform DeltaLf. 2 PublicationsAdd BLAST44

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X53961 mRNA Translation: CAA37914.1
U07643 mRNA Translation: AAB60324.1
AF332168 mRNA Translation: AAG48753.1
AY178998 mRNA Translation: AAN75578.2
AY137470 mRNA Translation: AAN11304.1
M73700 Genomic DNA Translation: AAA59479.1
M93150 mRNA Translation: AAA36159.1
AY165046 mRNA Translation: AAN63998.1
AY493417 mRNA Translation: AAS72878.1
EU622050 Genomic DNA Translation: ACC95966.1
AK292813 mRNA Translation: BAF85502.1
AK298035 mRNA Translation: BAH12708.1
AC098613 Genomic DNA No translation available.
BC015822 mRNA Translation: AAH15822.1
BC015823 mRNA Translation: AAH15823.1
BC022347 mRNA Translation: AAH22347.1
S52659 Genomic DNA Translation: AAB24877.1
X52941 mRNA Translation: CAA37116.1
M83202 mRNA Translation: AAA59511.1
M83205 mRNA Translation: AAA58656.1
U95626 Genomic DNA Translation: AAB57795.1
M18642 mRNA Translation: AAA86665.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS33747.1 [P02788-1]
CCDS56251.1 [P02788-2]

Protein sequence database of the Protein Information Resource

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PIRi
G01394 TFHUL

NCBI Reference Sequences

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RefSeqi
NP_001186078.1, NM_001199149.1 [P02788-2]
NP_001308050.1, NM_001321121.1
NP_001308051.1, NM_001321122.1
NP_002334.2, NM_002343.5 [P02788-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.529517

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000231751; ENSP00000231751; ENSG00000012223 [P02788-1]
ENST00000426532; ENSP00000405719; ENSG00000012223 [P02788-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
4057

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:4057

UCSC genome browser

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UCSCi
uc003fzr.4 human [P02788-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Lactotransferrin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53961 mRNA Translation: CAA37914.1
U07643 mRNA Translation: AAB60324.1
AF332168 mRNA Translation: AAG48753.1
AY178998 mRNA Translation: AAN75578.2
AY137470 mRNA Translation: AAN11304.1
M73700 Genomic DNA Translation: AAA59479.1
M93150 mRNA Translation: AAA36159.1
AY165046 mRNA Translation: AAN63998.1
AY493417 mRNA Translation: AAS72878.1
EU622050 Genomic DNA Translation: ACC95966.1
AK292813 mRNA Translation: BAF85502.1
AK298035 mRNA Translation: BAH12708.1
AC098613 Genomic DNA No translation available.
BC015822 mRNA Translation: AAH15822.1
BC015823 mRNA Translation: AAH15823.1
BC022347 mRNA Translation: AAH22347.1
S52659 Genomic DNA Translation: AAB24877.1
X52941 mRNA Translation: CAA37116.1
M83202 mRNA Translation: AAA59511.1
M83205 mRNA Translation: AAA58656.1
U95626 Genomic DNA Translation: AAB57795.1
M18642 mRNA Translation: AAA86665.1
CCDSiCCDS33747.1 [P02788-1]
CCDS56251.1 [P02788-2]
PIRiG01394 TFHUL
RefSeqiNP_001186078.1, NM_001199149.1 [P02788-2]
NP_001308050.1, NM_001321121.1
NP_001308051.1, NM_001321122.1
NP_002334.2, NM_002343.5 [P02788-1]
UniGeneiHs.529517

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B0LX-ray2.20A20-710[»]
1BKAX-ray2.40A20-710[»]
1CB6X-ray2.00A20-710[»]
1DSNX-ray2.05A21-352[»]
1EH3X-ray2.00A21-352[»]
1FCKX-ray2.20A21-710[»]
1H43X-ray2.20A21-352[»]
1H44X-ray2.00A21-352[»]
1H45X-ray1.95A21-352[»]
1HSEX-ray2.20A21-353[»]
1L5TX-ray3.00A/B21-351[»]
1LCFX-ray2.00A20-710[»]
1LCTX-ray2.00A21-352[»]
1LFGX-ray2.20A20-710[»]
1LFHX-ray2.80A20-710[»]
1LFIX-ray2.10A20-710[»]
1LGBX-ray3.30C110-268[»]
1N76X-ray3.40A21-710[»]
1SQYX-ray2.50A20-710[»]
1U62NMR-A39-49[»]
1VFDX-ray2.50A20-349[»]
1VFEX-ray2.30A20-352[»]
1XV4NMR-A39-49[»]
1XV7NMR-A39-49[»]
1Z6VNMR-A