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Protein

Bactericidal permeability-increasing protein

Gene

BPI

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

Functioni

The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa.2 Publications

GO - Molecular functioni

  1. lipopolysaccharide binding Source: BHF-UCL

GO - Biological processi

  1. defense response to Gram-negative bacterium Source: InterPro
  2. immune response Source: Ensembl
  3. negative regulation of interleukin-6 production Source: BHF-UCL
  4. negative regulation of interleukin-8 production Source: BHF-UCL
  5. negative regulation of macrophage activation Source: BHF-UCL
  6. negative regulation of tumor necrosis factor production Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial

Protein family/group databases

TCDBi1.C.40.1.1. the bactericidal permeability increasing protein (bpip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Bactericidal permeability-increasing protein
Short name:
BPI
Alternative name(s):
CAP 57
Gene namesi
Name:BPI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:1095. BPI.

Subcellular locationi

  1. Secreted
  2. Cytoplasmic granule membrane

  3. Note: Membrane-associated in polymorphonuclear Leukocytes (PMN) granules.

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. extracellular vesicular exosome Source: UniProtKB
  3. integral component of plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi49 – 491S → C: No impairment of secretion and increased propensity for dimer formation. 1 Publication
Mutagenesisi163 – 1631C → A: No impairment of secretion and/or biological activity. Loss of dimer formation. 1 Publication
Mutagenesisi166 – 1661C → S: Poorly secreted. Loss of LPS-binding and biological activity. 1 Publication
Mutagenesisi206 – 2061C → A: Not secreted. 1 Publication

Organism-specific databases

PharmGKBiPA25403.

Polymorphism and mutation databases

BioMutaiBPI.
DMDMi215274242.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 31314 PublicationsAdd
BLAST
Chaini32 – 487456Bactericidal permeability-increasing proteinPRO_0000017154Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi166 ↔ 2061 Publication
Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP17213.
PaxDbiP17213.
PRIDEiP17213.

PTM databases

PhosphoSiteiP17213.

Expressioni

Tissue specificityi

Restricted to cells of the myeloid series.

Gene expression databases

BgeeiP17213.
ExpressionAtlasiP17213. baseline and differential.
GenevestigatoriP17213.

Organism-specific databases

HPAiHPA061284.

Interactioni

Subunit structurei

Monomer. Homodimer; disulfide-linked.1 Publication

Structurei

Secondary structure

1
487
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 417Combined sources
Helixi42 – 6019Combined sources
Beta strandi68 – 714Combined sources
Beta strandi75 – 795Combined sources
Beta strandi81 – 9313Combined sources
Beta strandi97 – 1026Combined sources
Turni103 – 1053Combined sources
Beta strandi106 – 12621Combined sources
Beta strandi129 – 15325Combined sources
Turni154 – 1574Combined sources
Beta strandi158 – 16912Combined sources
Beta strandi172 – 1765Combined sources
Helixi180 – 1823Combined sources
Helixi183 – 19210Combined sources
Helixi194 – 21522Combined sources
Helixi217 – 2215Combined sources
Beta strandi226 – 2294Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi235 – 2373Combined sources
Beta strandi240 – 2423Combined sources
Beta strandi248 – 2558Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi282 – 2909Combined sources
Helixi291 – 30313Combined sources
Beta strandi307 – 3126Combined sources
Helixi313 – 3153Combined sources
Helixi326 – 3305Combined sources
Beta strandi333 – 3353Combined sources
Helixi336 – 3394Combined sources
Beta strandi344 – 3507Combined sources
Beta strandi356 – 3605Combined sources
Beta strandi363 – 3675Combined sources
Beta strandi369 – 3779Combined sources
Beta strandi383 – 39210Combined sources
Beta strandi395 – 4017Combined sources
Beta strandi403 – 41210Combined sources
Beta strandi416 – 4249Combined sources
Helixi429 – 4324Combined sources
Helixi433 – 44311Combined sources
Helixi445 – 45410Combined sources
Beta strandi464 – 47411Combined sources
Beta strandi477 – 48610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BP1X-ray2.40A32-487[»]
1EWFX-ray1.70A32-487[»]
ProteinModelPortaliP17213.
SMRiP17213. Positions 32-487.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17213.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 193184N-terminal barrel1 PublicationAdd
BLAST
Regioni194 – 359166Central sheet1 PublicationAdd
BLAST
Regioni240 – 2456Cleavage sites for elastaseSequence Analysis
Regioni260 – 430171C-terminal barrel1 PublicationAdd
BLAST

Domaini

The N-terminal region may be exposed to the interior of the granule, whereas the C-terminal portion may be embedded in the membrane. During phagocytosis and degranulation, proteases may be released and activated and cleave BPI at the junction of the N- and C-terminal portions of the molecule, providing controlled release of the N-terminal antibacterial fragment when bacteria are ingested.1 Publication
The N- and C-terminal barrels adopt an identical fold despite having only 13% of conserved residues.1 Publication

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG262970.
GeneTreeiENSGT00730000110583.
HOVERGENiHBG002797.
InParanoidiP17213.
OMAiPHQNFLL.
PhylomeDBiP17213.
TreeFamiTF315617.

Family and domain databases

InterProiIPR017943. Bactericidal_perm-incr_a/b_dom.
IPR030181. BPI.
IPR030675. BPI/LBP.
IPR001124. Lipid-bd_serum_glycop_C.
IPR017954. Lipid-bd_serum_glycop_CS.
IPR017942. Lipid-bd_serum_glycop_N.
[Graphical view]
PANTHERiPTHR10504:SF66. PTHR10504:SF66. 1 hit.
PfamiPF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002417. Lipid_binding_protein. 1 hit.
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.

P17213-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRENMARGPC NAPRWASLMV LVAIGTAVTA AVNPGVVVRI SQKGLDYASQ
60 70 80 90 100
QGTAALQKEL KRIKIPDYSD SFKIKHLGKG HYSFYSMDIR EFQLPSSQIS
110 120 130 140 150
MVPNVGLKFS ISNANIKISG KWKAQKRFLK MSGNFDLSIE GMSISADLKL
160 170 180 190 200
GSNPTSGKPT ITCSSCSSHI NSVHVHISKS KVGWLIQLFH KKIESALRNK
210 220 230 240 250
MNSQVCEKVT NSVSSELQPY FQTLPVMTKI DSVAGINYGL VAPPATTAET
260 270 280 290 300
LDVQMKGEFY SENHHNPPPF APPVMEFPAA HDRMVYLGLS DYFFNTAGLV
310 320 330 340 350
YQEAGVLKMT LRDDMIPKES KFRLTTKFFG TFLPEVAKKF PNMKIQIHVS
360 370 380 390 400
ASTPPHLSVQ PTGLTFYPAV DVQAFAVLPN SSLASLFLIG MHTTGSMEVS
410 420 430 440 450
AESNRLVGEL KLDRLLLELK HSNIGPFPVE LLQDIMNYIV PILVLPRVNE
460 470 480
KLQKGFPLPT PARVQLYNVV LQPHQNFLLF GADVVYK
Length:487
Mass (Da):53,900
Last modified:November 25, 2008 - v4
Checksum:i30BC73B1B465B62D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51M → L in AAH40955 (PubMed:15489334).Curated
Sequence conflicti53 – 531T → R AA sequence (PubMed:1937776).Curated
Sequence conflicti355 – 3551P → S in AAG42844 (Ref. 7) Curated
Sequence conflicti375 – 3751F → L (PubMed:7517398).Curated
Sequence conflicti411 – 4111K → R in AAG42844 (Ref. 7) Curated
Sequence conflicti433 – 4331Q → L in BAG37729 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121A → T.
Corresponds to variant rs5743497 [ dbSNP | Ensembl ].
VAR_049728
Natural varianti12 – 121A → V.
Corresponds to variant rs5743498 [ dbSNP | Ensembl ].
VAR_049729
Natural varianti16 – 161A → V.2 Publications
Corresponds to variant rs1341023 [ dbSNP | Ensembl ].
VAR_018401
Natural varianti90 – 901R → C.
Corresponds to variant rs5743500 [ dbSNP | Ensembl ].
VAR_049730
Natural varianti140 – 1401E → Q.
Corresponds to variant rs5743506 [ dbSNP | Ensembl ].
VAR_049732
Natural varianti196 – 1961A → V.
Corresponds to variant rs5743509 [ dbSNP | Ensembl ].
VAR_018402
Natural varianti216 – 2161E → K.3 Publications
Corresponds to variant rs4358188 [ dbSNP | Ensembl ].
VAR_018403
Natural varianti280 – 2801A → V.
Corresponds to variant rs5741804 [ dbSNP | Ensembl ].
VAR_049733
Natural varianti377 – 3771V → I.
Corresponds to variant rs5743524 [ dbSNP | Ensembl ].
VAR_049734
Natural varianti404 – 4041N → D.2 Publications
Corresponds to variant rs5741809 [ dbSNP | Ensembl ].
VAR_049735
Natural varianti451 – 4511K → E.
Corresponds to variant rs5743542 [ dbSNP | Ensembl ].
VAR_049736

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04739 mRNA. Translation: AAA51841.1.
DQ414688 mRNA. Translation: ABD66755.1.
AK315328 mRNA. Translation: BAG37729.1.
AL359555 Genomic DNA. No translation available.
AL391095 Genomic DNA. No translation available.
AL499625 Genomic DNA. No translation available.
AL583962 Genomic DNA. No translation available.
BC040955 mRNA. Translation: AAH40955.1.
AF322588 mRNA. Translation: AAG42844.1.
CCDSiCCDS13303.1.
PIRiA33850. A30909.
RefSeqiNP_001716.2. NM_001725.2.
UniGeneiHs.529019.

Genome annotation databases

EnsembliENST00000262865; ENSP00000262865; ENSG00000101425.
GeneIDi671.
KEGGihsa:671.
UCSCiuc002xib.2. human.

Polymorphism and mutation databases

BioMutaiBPI.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04739 mRNA. Translation: AAA51841.1.
DQ414688 mRNA. Translation: ABD66755.1.
AK315328 mRNA. Translation: BAG37729.1.
AL359555 Genomic DNA. No translation available.
AL391095 Genomic DNA. No translation available.
AL499625 Genomic DNA. No translation available.
AL583962 Genomic DNA. No translation available.
BC040955 mRNA. Translation: AAH40955.1.
AF322588 mRNA. Translation: AAG42844.1.
CCDSiCCDS13303.1.
PIRiA33850. A30909.
RefSeqiNP_001716.2. NM_001725.2.
UniGeneiHs.529019.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BP1X-ray2.40A32-487[»]
1EWFX-ray1.70A32-487[»]
ProteinModelPortaliP17213.
SMRiP17213. Positions 32-487.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi1.C.40.1.1. the bactericidal permeability increasing protein (bpip) family.

PTM databases

PhosphoSiteiP17213.

Polymorphism and mutation databases

BioMutaiBPI.
DMDMi215274242.

Proteomic databases

MaxQBiP17213.
PaxDbiP17213.
PRIDEiP17213.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262865; ENSP00000262865; ENSG00000101425.
GeneIDi671.
KEGGihsa:671.
UCSCiuc002xib.2. human.

Organism-specific databases

CTDi671.
GeneCardsiGC20P036888.
H-InvDBHIX0027669.
HGNCiHGNC:1095. BPI.
HPAiHPA061284.
MIMi109195. gene.
neXtProtiNX_P17213.
PharmGKBiPA25403.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG262970.
GeneTreeiENSGT00730000110583.
HOVERGENiHBG002797.
InParanoidiP17213.
OMAiPHQNFLL.
PhylomeDBiP17213.
TreeFamiTF315617.

Miscellaneous databases

ChiTaRSiBPI. human.
EvolutionaryTraceiP17213.
GenomeRNAii671.
NextBioi2748.
PROiP17213.
SOURCEiSearch...

Gene expression databases

BgeeiP17213.
ExpressionAtlasiP17213. baseline and differential.
GenevestigatoriP17213.

Family and domain databases

InterProiIPR017943. Bactericidal_perm-incr_a/b_dom.
IPR030181. BPI.
IPR030675. BPI/LBP.
IPR001124. Lipid-bd_serum_glycop_C.
IPR017954. Lipid-bd_serum_glycop_CS.
IPR017942. Lipid-bd_serum_glycop_N.
[Graphical view]
PANTHERiPTHR10504:SF66. PTHR10504:SF66. 1 hit.
PfamiPF01273. LBP_BPI_CETP. 1 hit.
PF02886. LBP_BPI_CETP_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002417. Lipid_binding_protein. 1 hit.
SMARTiSM00328. BPI1. 1 hit.
SM00329. BPI2. 1 hit.
[Graphical view]
SUPFAMiSSF55394. SSF55394. 2 hits.
PROSITEiPS00400. LBP_BPI_CETP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the cDNA of a human neutrophil bactericidal protein. Structural and functional correlations."
    Gray P.W., Flaggs G., Leong S.R., Gumina R.J., Weiss J., Ooi C.E., Elsbach P.
    J. Biol. Chem. 264:9505-9509(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-68, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, VARIANTS VAL-16 AND LYS-216.
  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. "cDNA cloning and sequence analysis of human bactericidal/permeability protein."
    Ma H., Cao X., Sun Y., Lei W.
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-16.
  4. "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], VARIANT ASP-404.
    Tissue: Fetal heart.
  5. "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].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LYS-216.
    Tissue: Leukocyte.
  7. "Cloning of cDNA of human bactericidal/permeability-increasing protein."
    Xu J., Wang H.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-487, VARIANTS LYS-216 AND ASP-404.
  8. "Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa."
    Wasiluk K.R., Skubitz K.M., Gray B.H.
    Infect. Immun. 59:4193-4200(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 32-53, FUNCTION.
    Tissue: Leukocyte.
  9. Cited for: PROTEIN SEQUENCE OF 32-51.
  10. "A 25-kDa NH2-terminal fragment carries all the antibacterial activities of the human neutrophil 60-kDa bactericidal/permeability-increasing protein."
    Ooi C.E., Weiss J., Elsbach P., Frangione B., Mannion B.
    J. Biol. Chem. 262:14891-14894(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 32-48.
  11. "Expression and characterization of cysteine-modified variants of an amino-terminal fragment of bactericidal/permeability-increasing protein."
    Horwitz A.H., Leigh S.D., Abrahamson S., Gazzano-Santoro H., Liu P.-S., Williams R.E., Carroll S.F., Theofan G.
    Protein Expr. Purif. 8:28-40(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-49; CYS-163; CYS-166 AND CYS-206.
  12. "Crystal structure of human BPI and two bound phospholipids at 2.4-A resolution."
    Beamer L.J., Carroll S.F., Eisenberg D.
    Science 276:1861-1864(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 32-487.
  13. "The 1.7 A crystal structure of BPI: a study of how two dissimilar amino acid sequences can adopt the same fold."
    Kleiger G., Beamer L.J., Grothe R., Mallick P., Eisenberg D.
    J. Mol. Biol. 299:1019-1034(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 32-487, DISULFIDE BOND.

Entry informationi

Entry nameiBPI_HUMAN
AccessioniPrimary (citable) accession number: P17213
Secondary accession number(s): B2RCY2
, Q1ZZU8, Q5JRW0, Q8IW58, Q9BYZ9, Q9H1L2, Q9H1M8, Q9H203, Q9UCT4, Q9UD65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 25, 2008
Last modified: April 29, 2015
This is version 151 of the entry and version 4 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

3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.