Details for: LTF

Gene ID: 4057

Symbol: LTF

Ensembl ID: ENSG00000012223

Description: lactotransferrin

Associated with

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: myelocyte (CL0002193)
    Fold Change: 4.39
    Marker Score: 1896
  • Cell Name: serous secreting cell (CL0000313)
    Fold Change: 3.47
    Marker Score: 1386
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: 3.17
    Marker Score: 7213
  • Cell Name: tracheobronchial serous cell (CL0019001)
    Fold Change: 2.38
    Marker Score: 868
  • Cell Name: kidney loop of Henle epithelial cell (CL1000909)
    Fold Change: 2.04
    Marker Score: 1276
  • Cell Name: mammary gland epithelial cell (CL0002327)
    Fold Change: 2
    Marker Score: 711
  • Cell Name: epithelial cell of prostate (CL0002231)
    Fold Change: 1.89
    Marker Score: 1310
  • Cell Name: duct epithelial cell (CL0000068)
    Fold Change: 1.85
    Marker Score: 864
  • Cell Name: tracheobronchial goblet cell (CL0019003)
    Fold Change: 1.75
    Marker Score: 481
  • Cell Name: colon goblet cell (CL0009039)
    Fold Change: 1.6
    Marker Score: 1166
  • Cell Name: mucous neck cell (CL0000651)
    Fold Change: 1.53
    Marker Score: 3482
  • Cell Name: luminal epithelial cell of mammary gland (CL0002326)
    Fold Change: 1.38
    Marker Score: 2440
  • Cell Name: mucus secreting cell (CL0000319)
    Fold Change: 1.26
    Marker Score: 321
  • Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
    Fold Change: 1.26
    Marker Score: 850
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: 1.25
    Marker Score: 1244
  • Cell Name: glandular cell of esophagus (CL0002657)
    Fold Change: 1.22
    Marker Score: 387
  • Cell Name: keratocyte (CL0002363)
    Fold Change: 1.2
    Marker Score: 276
  • Cell Name: peptic cell (CL0000155)
    Fold Change: 1.2
    Marker Score: 501
  • Cell Name: enterocyte of epithelium of small intestine (CL1000334)
    Fold Change: 1.15
    Marker Score: 4810
  • Cell Name: bronchial goblet cell (CL1000312)
    Fold Change: 1.1
    Marker Score: 544
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: 1.07
    Marker Score: 16711
  • Cell Name: early T lineage precursor (CL0002425)
    Fold Change: 1.04
    Marker Score: 791
  • Cell Name: cardiac endothelial cell (CL0010008)
    Fold Change: 1
    Marker Score: 1903.5
  • Cell Name: cerebral cortex GABAergic interneuron (CL0010011)
    Fold Change: 1
    Marker Score: 71822
  • Cell Name: forebrain radial glial cell (CL0013000)
    Fold Change: 1
    Marker Score: 48047
  • Cell Name: respiratory goblet cell (CL0002370)
    Fold Change: 0.99
    Marker Score: 287
  • Cell Name: absorptive cell (CL0000212)
    Fold Change: 0.98
    Marker Score: 30408
  • Cell Name: tuft cell of colon (CL0009041)
    Fold Change: 0.98
    Marker Score: 504
  • Cell Name: BEST4+ intestinal epithelial cell, human (CL4030026)
    Fold Change: 0.97
    Marker Score: 459
  • Cell Name: kidney proximal convoluted tubule epithelial cell (CL1000838)
    Fold Change: 0.96
    Marker Score: 1983
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: 0.95
    Marker Score: 2411
  • Cell Name: immature innate lymphoid cell (CL0001082)
    Fold Change: 0.94
    Marker Score: 1902
  • Cell Name: transit amplifying cell (CL0009010)
    Fold Change: 0.93
    Marker Score: 5308
  • Cell Name: small intestine goblet cell (CL1000495)
    Fold Change: 0.93
    Marker Score: 372
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: 0.91
    Marker Score: 2737
  • Cell Name: transit amplifying cell of small intestine (CL0009012)
    Fold Change: 0.91
    Marker Score: 378.5
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: 0.9
    Marker Score: 324
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 0.87
    Marker Score: 5285
  • Cell Name: retinal blood vessel endothelial cell (CL0002585)
    Fold Change: 0.86
    Marker Score: 207
  • Cell Name: transit amplifying cell of colon (CL0009011)
    Fold Change: 0.85
    Marker Score: 391
  • Cell Name: renal beta-intercalated cell (CL0002201)
    Fold Change: 0.81
    Marker Score: 258
  • Cell Name: intestinal epithelial cell (CL0002563)
    Fold Change: 0.77
    Marker Score: 1256
  • Cell Name: brush cell (CL0002204)
    Fold Change: 0.77
    Marker Score: 705
  • Cell Name: club cell (CL0000158)
    Fold Change: 0.77
    Marker Score: 901
  • Cell Name: Cajal-Retzius cell (CL0000695)
    Fold Change: 0.76
    Marker Score: 394
  • Cell Name: lung secretory cell (CL1000272)
    Fold Change: 0.74
    Marker Score: 661
  • Cell Name: neutrophil progenitor cell (CL0000834)
    Fold Change: 0.69
    Marker Score: 177
  • Cell Name: kidney connecting tubule epithelial cell (CL1000768)
    Fold Change: 0.68
    Marker Score: 969
  • Cell Name: epithelial cell of proximal tubule (CL0002306)
    Fold Change: 0.66
    Marker Score: 2332
  • Cell Name: lymphoid lineage restricted progenitor cell (CL0000838)
    Fold Change: 0.59
    Marker Score: 357
  • Cell Name: gut absorptive cell (CL0000677)
    Fold Change: 0.58
    Marker Score: 369
  • Cell Name: intestinal enteroendocrine cell (CL1001516)
    Fold Change: 0.56
    Marker Score: 444
  • Cell Name: intestinal tuft cell (CL0019032)
    Fold Change: 0.55
    Marker Score: 173
  • Cell Name: precursor B cell (CL0000817)
    Fold Change: 0.54
    Marker Score: 357
  • Cell Name: kidney loop of Henle thin ascending limb epithelial cell (CL1001107)
    Fold Change: 0.5
    Marker Score: 506
  • Cell Name: gut endothelial cell (CL0000131)
    Fold Change: 0.5
    Marker Score: 178
  • Cell Name: common myeloid progenitor (CL0000049)
    Fold Change: 0.49
    Marker Score: 131
  • Cell Name: kidney collecting duct principal cell (CL1001431)
    Fold Change: 0.49
    Marker Score: 1241
  • Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
    Fold Change: 0.49
    Marker Score: 1881
  • Cell Name: promyelocyte (CL0000836)
    Fold Change: 0.48
    Marker Score: 238
  • Cell Name: lung goblet cell (CL1000143)
    Fold Change: 0.48
    Marker Score: 137
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: 0.47
    Marker Score: 4164
  • Cell Name: vascular lymphangioblast (CL0005022)
    Fold Change: 0.45
    Marker Score: 754
  • Cell Name: kidney capillary endothelial cell (CL1000892)
    Fold Change: 0.44
    Marker Score: 139
  • Cell Name: renal intercalated cell (CL0005010)
    Fold Change: 0.44
    Marker Score: 236
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: 0.42
    Marker Score: 475
  • Cell Name: neutrophil (CL0000775)
    Fold Change: 0.42
    Marker Score: 253
  • Cell Name: secretory cell (CL0000151)
    Fold Change: 0.4
    Marker Score: 737
  • Cell Name: professional antigen presenting cell (CL0000145)
    Fold Change: 0.38
    Marker Score: 198
  • Cell Name: kidney epithelial cell (CL0002518)
    Fold Change: 0.37
    Marker Score: 391
  • Cell Name: mononuclear cell (CL0000842)
    Fold Change: 0.36
    Marker Score: 116
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 0.35
    Marker Score: 12003
  • Cell Name: CD8-positive, alpha-beta cytokine secreting effector T cell (CL0000908)
    Fold Change: 0.33
    Marker Score: 141
  • Cell Name: erythrocyte (CL0000232)
    Fold Change: 0.31
    Marker Score: 174
  • Cell Name: basal cell (CL0000646)
    Fold Change: 0.31
    Marker Score: 403
  • Cell Name: podocyte (CL0000653)
    Fold Change: 0.31
    Marker Score: 115
  • Cell Name: eukaryotic cell (CL0000255)
    Fold Change: 0.3
    Marker Score: 157
  • Cell Name: adventitial cell (CL0002503)
    Fold Change: 0.3
    Marker Score: 75
  • Cell Name: megakaryocyte-erythroid progenitor cell (CL0000050)
    Fold Change: 0.3
    Marker Score: 126
  • Cell Name: immature neutrophil (CL0000776)
    Fold Change: 0.3
    Marker Score: 100
  • Cell Name: kidney proximal straight tubule epithelial cell (CL1000839)
    Fold Change: 0.29
    Marker Score: 690
  • Cell Name: intermediate monocyte (CL0002393)
    Fold Change: 0.29
    Marker Score: 99
  • Cell Name: myoepithelial cell (CL0000185)
    Fold Change: 0.29
    Marker Score: 80
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: 0.28
    Marker Score: 601
  • Cell Name: paneth cell (CL0000510)
    Fold Change: 0.28
    Marker Score: 193
  • Cell Name: smooth muscle myoblast (CL0000514)
    Fold Change: 0.27
    Marker Score: 128
  • Cell Name: granulocyte monocyte progenitor cell (CL0000557)
    Fold Change: 0.26
    Marker Score: 168
  • Cell Name: endothelial cell (CL0000115)
    Fold Change: 0.26
    Marker Score: 237
  • Cell Name: medullary thymic epithelial cell (CL0002365)
    Fold Change: 0.25
    Marker Score: 406
  • Cell Name: hematopoietic cell (CL0000988)
    Fold Change: 0.25
    Marker Score: 163.5
  • Cell Name: kidney loop of Henle thin descending limb epithelial cell (CL1001111)
    Fold Change: 0.24
    Marker Score: 260
  • Cell Name: basal cell of epithelium of trachea (CL1000348)
    Fold Change: 0.24
    Marker Score: 1784
  • Cell Name: ionocyte (CL0005006)
    Fold Change: 0.23
    Marker Score: 69
  • Cell Name: luminal cell of prostate epithelium (CL0002340)
    Fold Change: 0.23
    Marker Score: 132
  • Cell Name: enteroendocrine cell of small intestine (CL0009006)
    Fold Change: 0.22
    Marker Score: 64
  • Cell Name: granulocyte (CL0000094)
    Fold Change: 0.22
    Marker Score: 98
  • Cell Name: enteroendocrine cell of colon (CL0009042)
    Fold Change: 0.22
    Marker Score: 73
  • Cell Name: leukocyte (CL0000738)
    Fold Change: 0.21
    Marker Score: 123
  • Cell Name: stratified epithelial cell (CL0000079)
    Fold Change: 0.21
    Marker Score: 1654.5
  • Cell Name: kidney interstitial fibroblast (CL1000692)
    Fold Change: 0.21
    Marker Score: 399

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Other Information

**Key characteristics:** * Lactoferrin is a glycoprotein with a molecular weight of approximately 120 kDa. * It is expressed in high levels in mucosal tissues, such as the gut, lungs, and skin. * It is a potent activator of the complement system, which is a complex network of proteins that is involved in inflammation and infection. * Lactoferrin is also a potent inhibitor of the metallopeptidase MMP-12, which is a protein that is involved in the degradation of proteins. **Pathways and functions:** * Lactoferrin is involved in the formation of amyloid fibers by binding to amyloid beta and promoting the aggregation of amyloid beta into amyloid plaques. * It is also involved in the regulation of inflammation by binding to complement proteins and inhibiting their activity. * Lactoferrin also has antimicrobial properties, and it can kill bacteria by binding to their cell walls and disrupting their metabolism. * It also has a role in the metabolism of proteins, and it can bind to and transport iron ions, which is essential for the activity of many enzymes. **Clinical significance:** Lactoferrin is a potential therapeutic agent for a variety of diseases, including amyloidosis, Crohn's disease, and tuberculosis. In amyloidosis, lactoferrin can help to slow the progression of the disease by preventing the formation of amyloid plaques. In Crohn's disease, lactoferrin can help to reduce inflammation and damage to the colon. In tuberculosis, lactoferrin can inhibit the growth of M. tuberculosis, the bacteria that causes tuberculosis.

Genular Protein ID: 693237699

Symbol: TRFL_HUMAN

Name: Lactotransferrin

UniProtKB Accession Codes:

P02788 A8K9U8 B2MV13 B7Z4X2 E7EQH5 O00756 Q16780 Q16785 Q16786 Q16789 Q5DSM0 Q8IU92 Q8IZH6 Q8TCD2 Q96KZ4 Q96KZ5 Q9H1Z3 Q9UCY5

Database IDs:

AGR 1 Allergome 1 AlphaFoldDB 1 Antibodypedia 1 Bgee 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 2 CDD 2 CORUM 1 CTD 1 ChEBI 16 ChEMBL 1 ChiTaRS 1 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 DisProt 1 DrugBank 9 EMBL 22 EMDB 1 EPD 1 Ensembl 2 EvolutionaryTrace 1 ExpressionAtlas 1 GO 54 Gene3D 1 GeneCards 1 GeneTree 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyConnect 2 GlyCosmos 1 GlyGen 1 HGNC 1 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 4 KEGG 1 MANE-Select 1 MEROPS 2 MIM 1 MINT 1 MassIVE 1 NCBI Taxonomy 1 OMA 1 OpenTargets 1 OrthoDB 1 PANTHER 2 PDB 44 PDBsum 34 PIR 1 PIRSF 2 PRIDE 1 PRINTS 1 PRO 1 PROSITE 4 PROSITE-ProRule 1 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 1 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 2 Pumba 1 RNAct 1 Reactome 5 RefSeq 4 SASBDB 1 SIGNOR 1 SMART 1 SMR 1 STRING 1 SUPFAM 1 SignaLink 1 TreeFam 1 UCSC 1 UniProtKB 2 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 2402455

Title: Complete nucleotide sequence of human mammary gland lactoferrin.

PubMed ID: 2402455

DOI: 10.1093/nar/18.17.5288

PubMed ID: 9122171

Title: Identification of an alternative form of human lactoferrin mRNA that is expressed differentially in normal tissues and tumor-derived cell lines.

PubMed ID: 9122171

DOI: 10.1073/pnas.94.6.2198

PubMed ID: 11702692

Title: cDNA cloning and sequence analysis of human lactoferrin.

PubMed ID: 11702692

PubMed ID: 22900286

Title: Crystal structure of human seminal diferric lactoferrin at 3.4 Angstrom resolution.

PubMed ID: 22900286

PubMed ID: 14573629

Title: One of two human lactoferrin variants exhibits increased antibacterial and transcriptional activation activities and is associated with localized juvenile periodontitis.

PubMed ID: 14573629

DOI: 10.1128/iai.71.11.6141-6147.2003

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16641997

Title: The DNA sequence, annotation and analysis of human chromosome 3.

PubMed ID: 16641997

DOI: 10.1038/nature04728

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 1480183

Title: Differential molecular mechanism of the estrogen action that regulates lactoferrin gene in human and mouse.

PubMed ID: 1480183

DOI: 10.1210/mend.6.11.1480183

PubMed ID: 2374734

Title: Nucleotide sequence of human lactoferrin cDNA.

PubMed ID: 2374734

DOI: 10.1093/nar/18.13.4013

PubMed ID: 6510420

Title: Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins.

PubMed ID: 6510420

DOI: 10.1111/j.1432-1033.1984.tb08607.x

PubMed ID: 6794640

Title: The present state of the human lactotransferrin sequence. Study and alignment of the cyanogen bromide fragments and characterization of N- and C-terminal domains.

PubMed ID: 6794640

DOI: 10.1016/0005-2795(81)90016-7

PubMed ID: 1599934

Title: Identification of the bactericidal domain of lactoferrin.

PubMed ID: 1599934

DOI: 10.1016/0167-4838(92)90346-f

PubMed ID: 8089135

Title: Delineation of the glycosaminoglycan-binding site in the human inflammatory response protein lactoferrin.

PubMed ID: 8089135

DOI: 10.1016/s0021-9258(17)31566-1

PubMed ID: 8551695

Title: Characterization of the 84-kDa protein with ABH activity in human seminal plasma.

PubMed ID: 8551695

PubMed ID: 16048952

Title: Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent.

PubMed ID: 16048952

DOI: 10.1128/aac.49.8.3387-3395.2005

PubMed ID: 25946035

Title: Human basal tear peptidome characterization by CID, HCD, and ETD followed by in silico and in vitro analyses for antimicrobial peptide identification.

PubMed ID: 25946035

DOI: 10.1021/acs.jproteome.5b00179

PubMed ID: 3477300

Title: Isolation of lactoferrin cDNA from a human myeloid library and expression of mRNA during normal and leukemic myelopoiesis.

PubMed ID: 3477300

PubMed ID: 7049727

Title: An 88 amino acid long C-terminal sequence of human lactotransferrin.

PubMed ID: 7049727

DOI: 10.1016/0014-5793(82)80229-9

PubMed ID: 6802759

Title: Bactericidal activity of human lactoferrin: differentiation from the stasis of iron deprivation.

PubMed ID: 6802759

DOI: 10.1128/iai.35.3.792-799.1982

PubMed ID: 2981589

Title: Ultrastructural localization of lactoferrin and myeloperoxidase in human neutrophils by immunogold.

PubMed ID: 2981589

PubMed ID: 3169987

Title: Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin.

PubMed ID: 3169987

DOI: 10.1128/iai.56.11.2774-2781.1988

PubMed ID: 1369293

Title: Isolation and characterization of opioid antagonist peptides derived from human lactoferrin.

PubMed ID: 1369293

DOI: 10.1271/bbb1961.54.1803

PubMed ID: 9359845

Title: N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA.

PubMed ID: 9359845

DOI: 10.1042/bj3280145

PubMed ID: 11083624

Title: Candidacidal activities of human lactoferrin peptides derived from the N terminus.

PubMed ID: 11083624

DOI: 10.1128/aac.44.12.3257-3263.2000

PubMed ID: 10792619

Title: Expression of lactoferrin in the kidney: implications for innate immunity and iron metabolism.

PubMed ID: 10792619

DOI: 10.1046/j.1523-1755.2000.00050.x

PubMed ID: 11179314

Title: Human lactoferrin and peptides derived from its N terminus are highly effective against infections with antibiotic-resistant bacteria.

PubMed ID: 11179314

DOI: 10.1128/iai.69.3.1469-1476.2001

PubMed ID: 12037568

Title: A component of innate immunity prevents bacterial biofilm development.

PubMed ID: 12037568

DOI: 10.1038/417552a

PubMed ID: 12565886

Title: An intronic alternative promoter of the human lactoferrin gene is activated by Ets.

PubMed ID: 12565886

DOI: 10.1016/s0006-291x(02)03077-2

PubMed ID: 12693969

Title: Potassium efflux induced by a new lactoferrin-derived peptide mimicking the effect of native human lactoferrin on the bacterial cytoplasmic membrane.

PubMed ID: 12693969

DOI: 10.1023/a:1022657630698

PubMed ID: 12535064

Title: Human milk lactoferrin is a serine protease that cleaves Haemophilus surface proteins at arginine-rich sites.

PubMed ID: 12535064

DOI: 10.1046/j.1365-2958.2003.03327.x

PubMed ID: 15222485

Title: Expression of delta-lactoferrin induces cell cycle arrest.

PubMed ID: 15222485

DOI: 10.1023/b:biom.0000027712.81056.13

PubMed ID: 15166119

Title: Lactoferrin is a potent regulator of bone cell activity and increases bone formation in vivo.

PubMed ID: 15166119

DOI: 10.1210/en.2003-1307

PubMed ID: 16842782

Title: Human lactoferrin upregulates expression of KDR/Flk-1 and stimulates VEGF-A-mediated endothelial cell proliferation and migration.

PubMed ID: 16842782

DOI: 10.1016/j.febslet.2006.06.091

PubMed ID: 17481742

Title: The anti-papillomavirus activity of human and bovine lactoferricin.

PubMed ID: 17481742

DOI: 10.1016/j.antiviral.2007.03.012

PubMed ID: 17567961

Title: Characterization of an eppin protein complex from human semen and spermatozoa.

PubMed ID: 17567961

DOI: 10.1095/biolreprod.107.060194

PubMed ID: 17079302

Title: Adenoviruses use lactoferrin as a bridge for CAR-independent binding to and infection of epithelial cells.

PubMed ID: 17079302

DOI: 10.1128/jvi.01995-06

PubMed ID: 18780401

Title: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.

PubMed ID: 18780401

DOI: 10.1002/pmic.200701057

PubMed ID: 19033648

Title: Apoptotic human cells inhibit migration of granulocytes via release of lactoferrin.

PubMed ID: 19033648

DOI: 10.1172/jci36226

PubMed ID: 19159218

Title: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.

PubMed ID: 19159218

DOI: 10.1021/pr8008012

PubMed ID: 20345905

Title: Human lactoferrin activates NF-kappaB through the Toll-like receptor 4 pathway while it interferes with the lipopolysaccharide-stimulated TLR4 signaling.

PubMed ID: 20345905

DOI: 10.1111/j.1742-4658.2010.07620.x

PubMed ID: 20404350

Title: O-GlcNAcylation/phosphorylation cycling at Ser10 controls both transcriptional activity and stability of delta-lactoferrin.

PubMed ID: 20404350

DOI: 10.1074/jbc.m109.080572

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22320386

Title: Delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor.

PubMed ID: 22320386

DOI: 10.1139/o11-070

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 2585506

Title: Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8-A resolution.

PubMed ID: 2585506

DOI: 10.1016/0022-2836(89)90602-5

PubMed ID: 1772635

Title: Molecular replacement solution of the structure of apolactoferrin, a protein displaying large-scale conformational change.

PubMed ID: 1772635

DOI: 10.1107/s0108768191008418

PubMed ID: 1581307

Title: Metal substitution in transferrins: the crystal structure of human copper-lactoferrin at 2.1-A resolution.

PubMed ID: 1581307

DOI: 10.1021/bi00133a020

PubMed ID: 8371268

Title: Structure of the recombinant N-terminal lobe of human lactoferrin at 2.0 A resolution.

PubMed ID: 8371268

DOI: 10.1006/jmbi.1993.1462

PubMed ID: 15299444

Title: Structure of copper- and oxalate-substituted human lactoferrin at 2.0 A resolution.

PubMed ID: 15299444

DOI: 10.1107/s0907444994000491

PubMed ID: 8069634

Title: Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety.

PubMed ID: 8069634

DOI: 10.1016/s0969-2126(00)00022-8

PubMed ID: 15299793

Title: Structure of human diferric lactoferrin refined at 2.2-A resolution.

PubMed ID: 15299793

DOI: 10.1107/s0907444994013521

PubMed ID: 8703903

Title: Anion binding by transferrins: importance of second-shell effects revealed by the crystal structure of oxalate-substituted diferric lactoferrin.

PubMed ID: 8703903

DOI: 10.1021/bi960288y

PubMed ID: 8931543

Title: Mutation of arginine 121 in lactoferrin destabilizes iron binding by disruption of anion binding: crystal structures of R121S and R121E mutants.

PubMed ID: 8931543

DOI: 10.1021/bi961729g

PubMed ID: 8594202

Title: Altered domain closure and iron binding in transferrins: the crystal structure of the Asp60Ser mutant of the amino-terminal half-molecule of human lactoferrin.

PubMed ID: 8594202

DOI: 10.1006/jmbi.1996.0091

PubMed ID: 9003186

Title: Mutagenesis of the histidine ligand in human lactoferrin: iron binding properties and crystal structure of the histidine-253-->methionine mutant.

PubMed ID: 9003186

DOI: 10.1021/bi961908y

PubMed ID: 10089508

Title: Structure of human apolactoferrin at 2.0 A resolution. Refinement and analysis of ligand-induced conformational change.

PubMed ID: 10089508

DOI: 10.1107/s0907444998004417

PubMed ID: 10089347

Title: Structure of recombinant human lactoferrin expressed in Aspergillus awamori.

PubMed ID: 10089347

DOI: 10.1107/s0907444998011226

PubMed ID: 10828980

Title: Crystal structure and iron-binding properties of the R210K mutant of the N-lobe of human lactoferrin: implications for iron release from transferrins.

PubMed ID: 10828980

DOI: 10.1021/bi0001224

PubMed ID: 11128996

Title: Metal substitution in transferrins: specific binding of cerium(IV) revealed by the crystal structure of cerium-substituted human lactoferrin.

PubMed ID: 11128996

DOI: 10.1007/s007750000157

PubMed ID: 12037297

Title: Structure of a domain-opened mutant (R121D) of the human lactoferrin N-lobe refined from a merohedrally twinned crystal form.

PubMed ID: 12037297

DOI: 10.1107/s0907444902005127

PubMed ID: 12450380

Title: 'Dilysine trigger' in transferrins probed by mutagenesis of lactoferrin: crystal structures of the R210G, R210E, and R210L mutants of human lactoferrin.

PubMed ID: 12450380

DOI: 10.1021/bi020443a

PubMed ID: 15687491

Title: Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide.

PubMed ID: 15687491

DOI: 10.1074/jbc.m500266200

PubMed ID: 16201406

Title: The protein structure of recombinant human lactoferrin produced in the milk of transgenic cows closely matches the structure of human milk-derived lactoferrin.

PubMed ID: 16201406

DOI: 10.1007/s11248-005-3233-0

PubMed ID: 17263370

Title: The acyl group as the central element of the structural organization of antimicrobial lipopeptide.

PubMed ID: 17263370

DOI: 10.1021/ja067419v

PubMed ID: 17543335

Title: Structure of a complex of human lactoferrin N-lobe with pneumococcal surface protein a provides insight into microbial defense mechanism.

PubMed ID: 17543335

DOI: 10.1016/j.jmb.2007.04.075

PubMed ID: 9873069

Title: Familial subepithelial corneal amyloidosis (gelatinous drop-like corneal dystrophy): exclusion of linkage to lactoferrin gene.

PubMed ID: 9873069

PubMed ID: 22406253

Title: Functional polymorphisms in the LTF gene and risk of coronary artery stenosis.

PubMed ID: 22406253

DOI: 10.1016/j.humimm.2012.02.014

Sequence Information:

  • Length: 710
  • Mass: 78182
  • Checksum: 0489CABA6D13C098
  • Sequence:
    • MKLVFLVLLF LGALGLCLAG RRRSVQWCAV SQPEATKCFQ WQRNMRKVRG PPVSCIKRDS 
PIQCIQAIAE NRADAVTLDG GFIYEAGLAP YKLRPVAAEV YGTERQPRTH YYAVAVVKKG 
GSFQLNELQG LKSCHTGLRR TAGWNVPIGT LRPFLNWTGP PEPIEAAVAR FFSASCVPGA 
DKGQFPNLCR LCAGTGENKC AFSSQEPYFS YSGAFKCLRD GAGDVAFIRE STVFEDLSDE 
AERDEYELLC PDNTRKPVDK FKDCHLARVP SHAVVARSVN GKEDAIWNLL RQAQEKFGKD 
KSPKFQLFGS PSGQKDLLFK DSAIGFSRVP PRIDSGLYLG SGYFTAIQNL RKSEEEVAAR 
RARVVWCAVG EQELRKCNQW SGLSEGSVTC SSASTTEDCI ALVLKGEADA MSLDGGYVYT 
AGKCGLVPVL AENYKSQQSS DPDPNCVDRP VEGYLAVAVV RRSDTSLTWN SVKGKKSCHT 
AVDRTAGWNI PMGLLFNQTG SCKFDEYFSQ SCAPGSDPRS NLCALCIGDE QGENKCVPNS 
NERYYGYTGA FRCLAENAGD VAFVKDVTVL QNTDGNNNEA WAKDLKLADF ALLCLDGKRK 
PVTEARSCHL AMAPNHAVVS RMDKVERLKQ VLLHQQAKFG RNGSDCPDKF CLFQSETKNL 
LFNDNTECLA RLHGKTTYEK YLGPQYVAGI TNLKKCSTSP LLEACEFLRK

Genular Protein ID: 1241478997

Symbol: B3KSL2_HUMAN

Name: N/A

UniProtKB Accession Codes:

B3KSL2

Database IDs:

ARBA 13 AlphaFoldDB 1 BioGRID-ORCS 1 CDD 2 CTD 1 DNASU 1 EMBL 2 GO 8 Gene3D 1 GenomeRNAi 1 InterPro 4 MEROPS 1 MaxQB 1 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PIRSF 2 PIRSR 1 PRINTS 1 PROSITE 5 PeptideAtlas 1 Pfam 1 RefSeq 1 SMART 1 SUPFAM 1

Citations:

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

Sequence Information:

  • Length: 697
  • Mass: 76753
  • Checksum: 68857D9CBA06D96E
  • Sequence:
    • MGLCLAGRRR RSVQWCAVSQ PEATKCFQWQ RNMRKVRGPP VSCIKRDSPI QCIQAIAENR 
ADAVTLDGGF IYEAGLAPYK LRPVAAEVYG TERQPRTHYY AVAVVKKGGS FQLNELQGLK 
SCHTGLRRTA GWNVPIGTLR PFLNWTGPPE PIEAAVARFF SASCVPGADK GQFPNLCRLC 
AGTGENKCAF SSQEPYFSYS GAFKCLRDGA GDVAFIREST VFEDLSDEAE RDEYELLCPD 
NTRKPVDKFK DCHLARVPSH AVVARSVNGK EDAIWNLLRQ AQEKFGKDKS PKFQLFGSPS 
GQKDLLFKDS AIGFSRVPPR IDSGLYLGSG YFTAIQNLRK SEEEVAARRA RVVWCAVGEQ 
ELRKCNQWSG LSEGSVTCSS ASTTEDCIAL VLKGEADAMS LDGGYVYTAG KCGLVPVLAE 
NYKSQQSSDP DPNCVDRPVE GYLAVAVVRR SDTSLTWNSV KGKKSCHTAV DRTAGWNIPM 
GLLFNQTGSC KFDEYFSQSC APGSDPRSNL CALCIGDEQG ENKCVPNSNE RYYGYTGAFR 
CLAENAGDVA FVKDVTVLQN TDGNNNDAWA KDLKLADFAL LCLDGKRKPV TEARSCHLAM 
APNHAVVSRM DKVERLIQVL LHQQAKFGRN GSDCPDKFCL FQSETKNLLF NDNTECLARL 
HGKTTYEKYL GPQYVAGITN LKKCSTSPLL EACEFLR

Genular Protein ID: 2274427556

Symbol: E7ER44_HUMAN

Name: N/A

UniProtKB Accession Codes:

E7ER44

Database IDs:

ARBA 13 AlphaFoldDB 1 Antibodypedia 1 Bgee 1 BioGRID-ORCS 1 CDD 2 CTD 1 ChiTaRS 1 DNASU 1 EMBL 2 EPD 1 Ensembl 2 ExpressionAtlas 1 GO 8 Gene3D 1 GeneTree 1 GenomeRNAi 1 HGNC 1 InterPro 4 MassIVE 1 MaxQB 2 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PIRNR 1 PIRSF 2 PIRSR 1 PRIDE 1 PRINTS 1 PROSITE 5 PeptideAtlas 1 Pfam 1 Proteomes 2 ProteomicsDB 1 RefSeq 1 SAM 1 SMART 1 SMR 1 SUPFAM 1 UCSC 1 VEuPathDB 1

Citations:

PubMed ID: 16641997

Title: The DNA sequence, annotation and analysis of human chromosome 3.

PubMed ID: 16641997

DOI: 10.1038/nature04728

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

Sequence Information:

  • Length: 708
  • Mass: 77970
  • Checksum: 0D4702D85E1F553E
  • Sequence:
    • MKLVFLVLLF LGALGLCLAG RRRSVQWCAV SQPEATKCFQ WQRNMRKVRG PPVSCIKRDS 
PIQCIQAIAE NRADAVTLDG GFIYEAGLAP YKLRPVAAEV YGTERQPRTH YYAVAVVKKG 
GSFQLNELQG LKSCHTGLRR TAGWNVPIGT LRPFLNWTGP PEPIEAAVAR FFSASCVPGA 
DKGQFPNLCR LCAGTGENKC AFSSQEPYFS YSGAFKCLRD GAGDVAFIRE STVFEDLSDE 
AERDEYELLC PDNTRKPVDK FKDCHLARVP SHAVVARSVN GKEDAIWNLL RQAQEKFGKD 
KSPKFQLFGS PSGQKDLLFK DSAIGFSRVP PRIDSGLYLG SGYFTAIQNL RKSEEEVAAR 
RARVVWCAVG EQELRKCNQW SGLSEGSVTC SSASTTEDCI ALKGEADAMS LDGGYVYTAG 
KCGLVPVLAE NYKSQQSSDP DPNCVDRPVE GYLAVAVVRR SDTSLTWNSV KGKKSCHTAV 
DRTAGWNIPM GLLFNQTGSC KFDEYFSQSC APGSDPRSNL CALCIGDEQG ENKCVPNSNE 
RYYGYTGAFR CLAENAGDVA FVKDVTVLQN TDGNNNEAWA KDLKLADFAL LCLDGKRKPV 
TEARSCHLAM APNHAVVSRM DKVERLKQVL LHQQAKFGRN GSDCPDKFCL FQSETKNLLF 
NDNTECLARL HGKTTYEKYL GPQYVAGITN LKKCSTSPLL EACEFLRK

Genular Protein ID: 2523239929

Symbol: Q2TUW9_HUMAN

Name: N/A

UniProtKB Accession Codes:

Q2TUW9

Database IDs:

ARBA 13 AlphaFoldDB 1 BioGRID-ORCS 1 CDD 2 CTD 1 DNASU 1 EMBL 2 GO 8 Gene3D 1 GenomeRNAi 1 InterPro 4 MEROPS 1 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PIRNR 1 PIRSF 2 PIRSR 1 PRINTS 1 PROSITE 5 Pfam 1 RefSeq 1 SAM 1 SMART 1 SMR 1 SUPFAM 1

Sequence Information:

  • Length: 709
  • Mass: 77981
  • Checksum: 5C6A0ED0C6985157
  • Sequence:
    • MKLVFLVLLF LGALGLCLAG RRRGSVQWCA VSQPEATKCF QWQRNMRRVR GPPVSCIKRD 
SPIQCIQAIA ENRADAVTLD GGFIYEAGLA PYKLRPVAAE VYGTERQPRT HYYAVAVVKK 
GGSFQLNELQ GLKSCHTGLR RTAGWNVPIG TLRPFLNWTG PPEPIEAAVA RFFSASCVPG 
ADKGQFPNLC RLCAGTGENK CAFSSQEPYF SYSGAFKCLR DGAGDVAFIR ESTVFEDLSD 
EAERDEYELL CPDNTRKPVD KFKDCHLARV PSHAVVARSV NGKEDAIWNL LRQAQEKFGK 
DKSPKFQLFG SPSGQKDLLF KDSAIGSSRV PPRIDSGLYL GSGYFTAIQN LRKSEEEVAA 
RRARVVWCAV GEQELRKCNQ WSGLSEGSVT CSSASTTEDC IALKGEADAM SLDGGYVYTA 
GKCGLVPVLA ENYKSQQSSD PDPNCVDRPV EGYLAVAVVR RSDTSLTWNS VKGKKSCHTA 
VDRTAGWNIP MGLLFNQTGS CKFDEYFSQS CAPGSDPRSN LCALCIGDEQ GENKCVPNSN 
ERYYGYTGAF RCLAENAGDV AFVKDVTVLQ NTDGNNNDAW AKDLKLADFA LLCLDGKRKP 
VTEARSCHLA MAPNHAVVSR MDKVERLKQV LLHQQAKFGR NGSDCPDKFC LFQSETKNLL 
FNDNTECLAR LHGKTTYEKY LGPQYVAGIT NLKKCSTSPL LEACEFLRK

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. For the full schema, download it here.