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P18428 (LBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipopolysaccharide-binding protein

Short name=LBP
Gene names
Name:LBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.12

Subunit structure

When bound to LPS, interacts (via C-terminus) with soluble CD14. Ref.10

Subcellular location

Secreted Ref.12.

Tissue specificity

Detected in blood serum (at protein level). Ref.12

Sequence similarities

Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.

Ontologies

Keywords
   Biological processImmunity
Innate immunity
Lipid transport
Transport
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionAntibiotic
Antimicrobial
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from expression pattern PubMed 12932360. Source: BHF-UCL

cellular defense response

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

cellular response to lipopolysaccharide

Inferred from direct assay PubMed 12594207. Source: MGI

cellular response to lipoteichoic acid

Inferred from direct assay PubMed 12594207. Source: MGI

defense response to Gram-negative bacterium

Inferred from direct assay PubMed 11528597. Source: BHF-UCL

defense response to Gram-positive bacterium

Inferred from direct assay PubMed 12932360. Source: BHF-UCL

detection of molecule of bacterial origin

Inferred from direct assay PubMed 11528597. Source: BHF-UCL

innate immune response

Inferred from sequence or structural similarity PubMed 2477488. Source: BHF-UCL

leukocyte chemotaxis involved in inflammatory response

Inferred from electronic annotation. Source: Ensembl

lipopolysaccharide transport

Inferred from direct assay PubMed 8985160. Source: BHF-UCL

lipopolysaccharide-mediated signaling pathway

Inferred from direct assay PubMed 11739189PubMed 8409400. Source: BHF-UCL

macrophage activation involved in immune response

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

negative regulation of growth of symbiont in host

Inferred from electronic annotation. Source: Ensembl

negative regulation of tumor necrosis factor production

Inferred from direct assay PubMed 11739189. Source: BHF-UCL

opsonization

Inferred from sequence or structural similarity PubMed 2477488. Source: BHF-UCL

positive regulation of chemokine production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-6 production

Inferred from direct assay PubMed 8409400. Source: BHF-UCL

positive regulation of interleukin-8 production

Inferred from direct assay PubMed 8409400. Source: BHF-UCL

positive regulation of macrophage activation

Inferred from direct assay PubMed 8409400. Source: BHF-UCL

positive regulation of neutrophil chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of respiratory burst involved in inflammatory response

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of toll-like receptor 4 signaling pathway

Inferred from direct assay PubMed 11528597. Source: BHF-UCL

positive regulation of tumor necrosis factor biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of tumor necrosis factor production

Inferred from direct assay PubMed 8409400. Source: BHF-UCL

response to lipopolysaccharide

Inferred from direct assay PubMed 11739189PubMed 8409400. Source: BHF-UCL

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcell surface

Inferred from direct assay PubMed 11528597. Source: BHF-UCL

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 11528597Ref.1. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

   Molecular_functionlipopolysaccharide binding

Inferred from sequence or structural similarity PubMed 2477488. Source: BHF-UCL

lipoteichoic acid binding

Inferred from direct assay PubMed 12594207. Source: MGI

protein binding

Inferred from physical interaction PubMed 21988832. Source: IntAct

receptor binding

Inferred from sequence or structural similarity PubMed 2477488. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRDX4Q131624EBI-3927059,EBI-2211957

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525
Chain26 – 481456Lipopolysaccharide-binding protein
PRO_0000017158

Amino acid modifications

Glycosylation3001N-linked (GlcNAc...) Potential
Glycosylation3551N-linked (GlcNAc...) Potential
Glycosylation3861N-linked (GlcNAc...) Potential
Glycosylation3941N-linked (GlcNAc...) Ref.11
Disulfide bond159 ↔ 198 By similarity

Natural variations

Natural variant91P → L.
Corresponds to variant rs2232580 [ dbSNP | Ensembl ].
VAR_028243
Natural variant1111R → Q.
Corresponds to variant rs2232583 [ dbSNP | Ensembl ].
VAR_049737
Natural variant1251L → I.
Corresponds to variant rs2232585 [ dbSNP | Ensembl ].
VAR_028244
Natural variant1471E → K.
Corresponds to variant rs36015492 [ dbSNP | Ensembl ].
VAR_049738
Natural variant1571S → C.
Corresponds to variant rs2232586 [ dbSNP | Ensembl ].
VAR_061293
Natural variant1661V → M.
Corresponds to variant rs5744204 [ dbSNP | Ensembl ].
VAR_028245
Natural variant2421M → I.
Corresponds to variant rs2232601 [ dbSNP | Ensembl ].
VAR_028246
Natural variant2831D → G.
Corresponds to variant rs2232607 [ dbSNP | Ensembl ].
VAR_028247
Natural variant2941H → R.
Corresponds to variant rs2232608 [ dbSNP | Ensembl ].
VAR_028248
Natural variant3331P → L Abolishes lipopolysaccharide binding and causes increased proteolytic degradation of the protein. Ref.12
Corresponds to variant rs2232613 [ dbSNP | Ensembl ].
VAR_028249
Natural variant3391L → F.
Corresponds to variant rs5744212 [ dbSNP | Ensembl ].
VAR_028250
Natural variant3641I → T.
Corresponds to variant rs2232615 [ dbSNP | Ensembl ].
VAR_049739
Natural variant4361F → L. Ref.1 Ref.3 Ref.5
Corresponds to variant rs2232618 [ dbSNP | Ensembl ].
VAR_028251
Natural variant4451A → T.
Corresponds to variant rs2232619 [ dbSNP | Ensembl ].
VAR_028252

Experimental info

Sequence conflict61R → H Ref.2
Sequence conflict221E → C Ref.2
Sequence conflict821N → K in AAC39547. Ref.4
Sequence conflict1281S → F in AAC39547. Ref.4
Sequence conflict154 – 1574VTAS → GYCL in AAA59493. Ref.1
Sequence conflict1741L → S in AAA59493. Ref.1
Sequence conflict2571R → S in AAC39547. Ref.4
Sequence conflict266 – 2705VMSLP → A in AAA59493. Ref.1
Sequence conflict3691L → H in AAC39547. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P18428 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 5A0E4B9E5E604C72

FASTA48153,384
        10         20         30         40         50         60 
MGALARALPS ILLALLLTST PEALGANPGL VARITDKGLQ YAAQEGLLAL QSELLRITLP 

        70         80         90        100        110        120 
DFTGDLRIPH VGRGRYEFHS LNIHSCELLH SALRPVPGQG LSLSISDSSI RVQGRWKVRK 

       130        140        150        160        170        180 
SFFKLQGSFD VSVKGISISV NLLLGSESSG RPTVTASSCS SDIADVEVDM SGDLGWLLNL 

       190        200        210        220        230        240 
FHNQIESKFQ KVLESRICEM IQKSVSSDLQ PYLQTLPVTT EIDSFADIDY SLVEAPRATA 

       250        260        270        280        290        300 
QMLEVMFKGE IFHRNHRSPV TLLAAVMSLP EEHNKMVYFA ISDYVFNTAS LVYHEEGYLN 

       310        320        330        340        350        360 
FSITDDMIPP DSNIRLTTKS FRPFVPRLAR LYPNMNLELQ GSVPSAPLLN FSPGNLSVDP 

       370        380        390        400        410        420 
YMEIDAFVLL PSSSKEPVFR LSVATNVSAT LTFNTSKITG FLKPGKVKVE LKESKVGLFN 

       430        440        450        460        470        480 
AELLEALLNY YILNTFYPKF NDKLAEGFPL PLLKRVQLYD LGLQIHKDFL FLGANVQYMR 


V 

« Hide

References

« Hide 'large scale' references
[1]"Structure and function of lipopolysaccharide binding protein."
Schumann R.R., Leong S.R., Flaggs G.W., Gray P.W., Wright S.D., Mathison J.C., Tobias P.S., Ulevitch R.J.
Science 249:1429-1431(1990) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M35533 mRNA. Translation: AAA59493.1.
X98657 expand/collapse EMBL AC list , X98658, X98659, X98660, X98661, X98662, X98663, X98664, X98665, X98666, X98667, X98668 Genomic DNA. Translation: CAA67226.1.
AF013512 expand/collapse EMBL AC list , 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.
CCDSCCDS13304.1.
PIRA35843.
A54136.
RefSeqNP_004130.2. NM_004139.4.
UniGeneHs.154078.

3D structure databases

ProteinModelPortalP18428.
SMRP18428. Positions 27-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110121. 17 interactions.
DIPDIP-90N.
IntActP18428. 13 interactions.
STRING9606.ENSP00000217407.

Protein family/group databases

TCDB1.C.40.1.2. the bactericidal permeability increasing protein (bpip) family.

PTM databases

PhosphoSiteP18428.

Polymorphism databases

DMDM116242615.

Proteomic databases

MaxQBP18428.
PaxDbP18428.
PeptideAtlasP18428.
PRIDEP18428.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217407; ENSP00000217407; ENSG00000129988.
GeneID3929.
KEGGhsa:3929.
UCSCuc002xic.2. human.

Organism-specific databases

CTD3929.
GeneCardsGC20P036974.
HGNCHGNC:6517. LBP.
HPACAB025905.
HPA001508.
MIM151990. gene.
neXtProtNX_P18428.
PharmGKBPA30303.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262970.
HOGENOMHOG000231250.
HOVERGENHBG002797.
InParanoidP18428.
KOK05399.
OMARNHRSPV.
OrthoDBEOG76739B.
PhylomeDBP18428.
TreeFamTF315617.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP18428.

Gene expression databases

BgeeP18428.
CleanExHS_LBP.
GenevestigatorP18428.

Family and domain databases

InterProIPR017943. 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]
PfamPF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view]
SMARTSM00328. BPI1. 1 hit.
SM00329. BPI2. 1 hit.
[Graphical view]
SUPFAMSSF55394. SSF55394. 2 hits.
PROSITEPS00400. LBP_BPI_CETP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiLipopolysaccharide-binding_protein.
GenomeRNAi3929.
NextBio15427.
PROP18428.
SOURCESearch...

Entry information

Entry nameLBP_HUMAN
AccessionPrimary (citable) accession number: P18428
Secondary accession number(s): B2R938 expand/collapse secondary AC list , O43438, Q92672, Q9H403, Q9UD66
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM