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P18428

- LBP_HUMAN

UniProt

P18428 - LBP_HUMAN

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Protein

Lipopolysaccharide-binding protein

Gene

LBP

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

Functioni

Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria, and acts as an affinity enhancer for CD14, facilitating its association with LPS. Promotes the release of cytokines in response to bacterial lipopolysaccharide.2 Publications

GO - Molecular functioni

  1. lipopolysaccharide binding Source: BHF-UCL
  2. lipoteichoic acid binding Source: MGI
  3. receptor binding Source: BHF-UCL

GO - Biological processi

  1. acute-phase response Source: BHF-UCL
  2. cellular defense response Source: BHF-UCL
  3. cellular response to lipopolysaccharide Source: MGI
  4. cellular response to lipoteichoic acid Source: MGI
  5. defense response to Gram-negative bacterium Source: BHF-UCL
  6. defense response to Gram-positive bacterium Source: BHF-UCL
  7. detection of molecule of bacterial origin Source: BHF-UCL
  8. innate immune response Source: BHF-UCL
  9. leukocyte chemotaxis involved in inflammatory response Source: Ensembl
  10. lipopolysaccharide-mediated signaling pathway Source: BHF-UCL
  11. lipopolysaccharide transport Source: BHF-UCL
  12. macrophage activation involved in immune response Source: BHF-UCL
  13. negative regulation of growth of symbiont in host Source: Ensembl
  14. negative regulation of tumor necrosis factor production Source: BHF-UCL
  15. opsonization Source: BHF-UCL
  16. positive regulation of chemokine production Source: Ensembl
  17. positive regulation of interleukin-6 production Source: BHF-UCL
  18. positive regulation of interleukin-8 production Source: BHF-UCL
  19. positive regulation of macrophage activation Source: BHF-UCL
  20. positive regulation of neutrophil chemotaxis Source: Ensembl
  21. positive regulation of respiratory burst involved in inflammatory response Source: BHF-UCL
  22. positive regulation of toll-like receptor 4 signaling pathway Source: BHF-UCL
  23. positive regulation of tumor necrosis factor biosynthetic process Source: Ensembl
  24. positive regulation of tumor necrosis factor production Source: BHF-UCL
  25. response to lipopolysaccharide Source: BHF-UCL
  26. toll-like receptor 4 signaling pathway Source: Reactome
  27. toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial

Keywords - Biological processi

Immunity, Innate immunity, Lipid transport, Transport

Enzyme and pathway databases

ReactomeiREACT_6822. Transfer of LPS from LBP carrier to CD14.
REACT_6894. Toll Like Receptor 4 (TLR4) Cascade.
SignaLinkiP18428.

Protein family/group databases

TCDBi1.C.40.1.2. the bactericidal permeability increasing protein (bpip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipopolysaccharide-binding protein
Short name:
LBP
Gene namesi
Name:LBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:6517. LBP.

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. cell surface Source: BHF-UCL
  2. extracellular region Source: Reactome
  3. extracellular space Source: BHF-UCL
  4. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30303.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Add
BLAST
Chaini26 – 481456Lipopolysaccharide-binding proteinPRO_0000017158Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi159 ↔ 198By similarity
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi386 – 3861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi394 – 3941N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP18428.
PaxDbiP18428.
PeptideAtlasiP18428.
PRIDEiP18428.

PTM databases

PhosphoSiteiP18428.

Expressioni

Tissue specificityi

Detected in blood serum (at protein level).1 Publication

Gene expression databases

BgeeiP18428.
CleanExiHS_LBP.
GenevestigatoriP18428.

Organism-specific databases

HPAiCAB025905.
HPA001508.

Interactioni

Subunit structurei

When bound to LPS, interacts (via C-terminus) with soluble CD14.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PRDX4Q131624EBI-3927059,EBI-2211957

Protein-protein interaction databases

BioGridi110121. 17 interactions.
DIPiDIP-90N.
IntActiP18428. 13 interactions.
STRINGi9606.ENSP00000217407.

Structurei

3D structure databases

ProteinModelPortaliP18428.
SMRiP18428. Positions 27-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG262970.
GeneTreeiENSGT00730000110583.
HOGENOMiHOG000231250.
HOVERGENiHBG002797.
InParanoidiP18428.
KOiK05399.
OMAiRNHRSPV.
OrthoDBiEOG76739B.
PhylomeDBiP18428.
TreeFamiTF315617.

Family and domain databases

InterProiIPR017943. Bactericidal_perm-incr_a/b_dom.
IPR001124. Lipid-bd_serum_glycop_C.
IPR017954. Lipid-bd_serum_glycop_CS.
IPR017942. Lipid-bd_serum_glycop_N.
[Graphical view]
PfamiPF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view]
SMARTiSM00328. BPI1. 1 hit.
SM00329. BPI2. 1 hit.
[Graphical view]
SUPFAMiSSF55394. SSF55394. 2 hits.
PROSITEiPS00400. LBP_BPI_CETP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P18428-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGALARALPS ILLALLLTST PEALGANPGL VARITDKGLQ YAAQEGLLAL
60 70 80 90 100
QSELLRITLP DFTGDLRIPH VGRGRYEFHS LNIHSCELLH SALRPVPGQG
110 120 130 140 150
LSLSISDSSI RVQGRWKVRK SFFKLQGSFD VSVKGISISV NLLLGSESSG
160 170 180 190 200
RPTVTASSCS SDIADVEVDM SGDLGWLLNL FHNQIESKFQ KVLESRICEM
210 220 230 240 250
IQKSVSSDLQ PYLQTLPVTT EIDSFADIDY SLVEAPRATA QMLEVMFKGE
260 270 280 290 300
IFHRNHRSPV TLLAAVMSLP EEHNKMVYFA ISDYVFNTAS LVYHEEGYLN
310 320 330 340 350
FSITDDMIPP DSNIRLTTKS FRPFVPRLAR LYPNMNLELQ GSVPSAPLLN
360 370 380 390 400
FSPGNLSVDP YMEIDAFVLL PSSSKEPVFR LSVATNVSAT LTFNTSKITG
410 420 430 440 450
FLKPGKVKVE LKESKVGLFN AELLEALLNY YILNTFYPKF NDKLAEGFPL
460 470 480
PLLKRVQLYD LGLQIHKDFL FLGANVQYMR V
Length:481
Mass (Da):53,384
Last modified:October 17, 2006 - v3
Checksum:i5A0E4B9E5E604C72
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61R → H(PubMed:7517398)Curated
Sequence conflicti22 – 221E → C(PubMed:7517398)Curated
Sequence conflicti82 – 821N → K in AAC39547. (PubMed:9441745)Curated
Sequence conflicti128 – 1281S → F in AAC39547. (PubMed:9441745)Curated
Sequence conflicti154 – 1574VTAS → GYCL in AAA59493. (PubMed:2402637)Curated
Sequence conflicti174 – 1741L → S in AAA59493. (PubMed:2402637)Curated
Sequence conflicti257 – 2571R → S in AAC39547. (PubMed:9441745)Curated
Sequence conflicti266 – 2705VMSLP → A in AAA59493. (PubMed:2402637)Curated
Sequence conflicti369 – 3691L → H in AAC39547. (PubMed:9441745)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91P → L.
Corresponds to variant rs2232580 [ dbSNP | Ensembl ].
VAR_028243
Natural varianti111 – 1111R → Q.
Corresponds to variant rs2232583 [ dbSNP | Ensembl ].
VAR_049737
Natural varianti125 – 1251L → I.
Corresponds to variant rs2232585 [ dbSNP | Ensembl ].
VAR_028244
Natural varianti147 – 1471E → K.
Corresponds to variant rs36015492 [ dbSNP | Ensembl ].
VAR_049738
Natural varianti157 – 1571S → C.
Corresponds to variant rs2232586 [ dbSNP | Ensembl ].
VAR_061293
Natural varianti166 – 1661V → M.
Corresponds to variant rs5744204 [ dbSNP | Ensembl ].
VAR_028245
Natural varianti242 – 2421M → I.
Corresponds to variant rs2232601 [ dbSNP | Ensembl ].
VAR_028246
Natural varianti283 – 2831D → G.
Corresponds to variant rs2232607 [ dbSNP | Ensembl ].
VAR_028247
Natural varianti294 – 2941H → R.
Corresponds to variant rs2232608 [ dbSNP | Ensembl ].
VAR_028248
Natural varianti333 – 3331P → L Abolishes lipopolysaccharide binding and causes increased proteolytic degradation of the protein. 1 Publication
Corresponds to variant rs2232613 [ dbSNP | Ensembl ].
VAR_028249
Natural varianti339 – 3391L → F.
Corresponds to variant rs5744212 [ dbSNP | Ensembl ].
VAR_028250
Natural varianti364 – 3641I → T.
Corresponds to variant rs2232615 [ dbSNP | Ensembl ].
VAR_049739
Natural varianti436 – 4361F → L.3 Publications
Corresponds to variant rs2232618 [ dbSNP | Ensembl ].
VAR_028251
Natural varianti445 – 4451A → T.
Corresponds to variant rs2232619 [ dbSNP | Ensembl ].
VAR_028252

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35533 mRNA. Translation: AAA59493.1.
X98657
, X98658, X98659, X98660, X98661, X98662, X98663, X98664, X98665, X98666, X98667, X98668 Genomic DNA. Translation: CAA67226.1.
AF013512
, AF013500, AF013501, AF013502, AF013503, AF013504, AF013505, AF013506, AF013507, AF013508, AF013509, AF013510, AF013511 Genomic DNA. Translation: AAC39547.1.
AF105067 mRNA. Translation: AAD21962.1.
AK313625 mRNA. Translation: BAG36385.1.
AL080249 Genomic DNA. Translation: CAC10462.1.
CH471077 Genomic DNA. Translation: EAW76034.1.
L42172 Genomic DNA. Translation: AAA66446.1.
CCDSiCCDS13304.1.
PIRiA35843.
A54136.
RefSeqiNP_004130.2. NM_004139.4.
UniGeneiHs.154078.

Genome annotation databases

EnsembliENST00000217407; ENSP00000217407; ENSG00000129988.
GeneIDi3929.
KEGGihsa:3929.
UCSCiuc002xic.2. human.

Polymorphism databases

DMDMi116242615.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35533 mRNA. Translation: AAA59493.1 .
X98657
, X98658 , X98659 , X98660 , X98661 , X98662 , X98663 , X98664 , X98665 , X98666 , X98667 , X98668 Genomic DNA. Translation: CAA67226.1 .
AF013512
, AF013500 , AF013501 , AF013502 , AF013503 , AF013504 , AF013505 , AF013506 , AF013507 , AF013508 , AF013509 , AF013510 , AF013511 Genomic DNA. Translation: AAC39547.1 .
AF105067 mRNA. Translation: AAD21962.1 .
AK313625 mRNA. Translation: BAG36385.1 .
AL080249 Genomic DNA. Translation: CAC10462.1 .
CH471077 Genomic DNA. Translation: EAW76034.1 .
L42172 Genomic DNA. Translation: AAA66446.1 .
CCDSi CCDS13304.1.
PIRi A35843.
A54136.
RefSeqi NP_004130.2. NM_004139.4.
UniGenei Hs.154078.

3D structure databases

ProteinModelPortali P18428.
SMRi P18428. Positions 27-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110121. 17 interactions.
DIPi DIP-90N.
IntActi P18428. 13 interactions.
STRINGi 9606.ENSP00000217407.

Protein family/group databases

TCDBi 1.C.40.1.2. the bactericidal permeability increasing protein (bpip) family.

PTM databases

PhosphoSitei P18428.

Polymorphism databases

DMDMi 116242615.

Proteomic databases

MaxQBi P18428.
PaxDbi P18428.
PeptideAtlasi P18428.
PRIDEi P18428.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000217407 ; ENSP00000217407 ; ENSG00000129988 .
GeneIDi 3929.
KEGGi hsa:3929.
UCSCi uc002xic.2. human.

Organism-specific databases

CTDi 3929.
GeneCardsi GC20P036974.
HGNCi HGNC:6517. LBP.
HPAi CAB025905.
HPA001508.
MIMi 151990. gene.
neXtProti NX_P18428.
PharmGKBi PA30303.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG262970.
GeneTreei ENSGT00730000110583.
HOGENOMi HOG000231250.
HOVERGENi HBG002797.
InParanoidi P18428.
KOi K05399.
OMAi RNHRSPV.
OrthoDBi EOG76739B.
PhylomeDBi P18428.
TreeFami TF315617.

Enzyme and pathway databases

Reactomei REACT_6822. Transfer of LPS from LBP carrier to CD14.
REACT_6894. Toll Like Receptor 4 (TLR4) Cascade.
SignaLinki P18428.

Miscellaneous databases

GeneWikii Lipopolysaccharide-binding_protein.
GenomeRNAii 3929.
NextBioi 15427.
PROi P18428.
SOURCEi Search...

Gene expression databases

Bgeei P18428.
CleanExi HS_LBP.
Genevestigatori P18428.

Family and domain databases

InterProi IPR017943. Bactericidal_perm-incr_a/b_dom.
IPR001124. Lipid-bd_serum_glycop_C.
IPR017954. Lipid-bd_serum_glycop_CS.
IPR017942. Lipid-bd_serum_glycop_N.
[Graphical view ]
Pfami PF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view ]
SMARTi SM00328. BPI1. 1 hit.
SM00329. BPI2. 1 hit.
[Graphical view ]
SUPFAMi SSF55394. SSF55394. 2 hits.
PROSITEi PS00400. LBP_BPI_CETP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-436.
  2. "Bactericidal/permeability-increasing protein and lipopolysaccharide (LPS)-binding protein. LPS binding properties and effects on LPS-mediated cell activation."
    Wilde C.G., Seilhamer J.J., McGrogan M., Ashton N., Snable J.L., Lane J.C., Leong S.R., Thornton M.B., Miller K.L., Scott R.W.
    J. Biol. Chem. 269:17411-17416(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The genomic organization of the genes for human lipopolysaccharide binding protein (LBP) and bactericidal permeability increasing protein (BPI) is highly conserved."
    Hubacek J.A., Buchler C., Aslanidis C., Schmitz G.
    Biochem. Biophys. Res. Commun. 236:427-430(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-436.
  4. "Similar organization of the lipopolysaccharide-binding protein (LBP) and phospholipid transfer protein (PLTP) genes suggests a common gene family of lipid-binding proteins."
    Kirschning C.J., Au-Young J., Lamping N., Reuter D., Pfeil D., Seilhamer J.J., Schumann R.R.
    Genomics 46:416-425(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Cloning and sequencing of human lipopolysaccharide-binding protein gene."
    Long J.Y., Liu J.Q., Xue Y.N., Wang H.X.
    Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 25:469-471(1998)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-436.
    Tissue: Liver.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  7. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "Cloning and characterization of the human LBP upstream sequence."
    Sutton C.L., Smith R.I.F., Centola M.B., Theofan G.
    Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
  10. "Structural biology of the LPS recognition."
    Jerala R.
    Int. J. Med. Microbiol. 297:353-363(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  11. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394.
    Tissue: Liver.
  12. "The crystal structure of lipopolysaccharide binding protein reveals the location of a frequent mutation that impairs innate immunity."
    Eckert J.K., Kim Y.J., Kim J.I., Guertler K., Oh D.Y., Sur S., Lundvall L., Hamann L., van der Ploeg A., Pickkers P., Giamarellos-Bourboulis E., Kubarenko A.V., Weber A.N., Kabesch M., Kumpf O., An H.J., Lee J.O., Schumann R.R.
    Immunity 39:647-660(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, 3D-STRUCTURE MODELING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, VARIANT LEU-333, CHARACTERIZATION OF VARIANT LEU-333.

Entry informationi

Entry nameiLBP_HUMAN
AccessioniPrimary (citable) accession number: P18428
Secondary accession number(s): B2R938
, O43438, Q92672, Q9H403, Q9UD66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 17, 2006
Last modified: October 29, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3