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P17213

- BPI_HUMAN

UniProt

P17213 - BPI_HUMAN

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Protein

Bactericidal permeability-increasing protein

Gene

BPI

Organism
Homo sapiens (Human)
Status
Reviewed - 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 bacterium Source: UniProtKB-KW
  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: Chromosome 20

Organism-specific databases

HGNCiHGNC:1095. BPI.

Subcellular locationi

Secreted. Cytoplasmic granule membrane
Note: Membrane-associated in polymorphonuclear Leukocytes (PMN) granules.

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. extracellular vesicular exosome Source: UniProt
  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.

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 ↔ 206
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.

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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
Regioni240 – 2456Cleavage sites for elastaseSequence Analysis

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

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG262970.
GeneTreeiENSGT00730000110583.
HOVERGENiHBG002797.
InParanoidiP17213.
OMAiCSSHINS.
PhylomeDBiP17213.
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.

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. 1 PublicationCurated
Sequence conflicti375 – 3751F → L(PubMed:7517398)Curated
Sequence conflicti411 – 4111K → R in AAG42844. 1 PublicationCurated
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:
EMBL
GenBank
DDBJ
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 databases

DMDMi215274242.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS13303.1.
PIRi A33850. A30909.
RefSeqi NP_001716.2. NM_001725.2.
UniGenei Hs.529019.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BP1 X-ray 2.40 A 32-487 [» ]
1EWF X-ray 1.70 A 32-487 [» ]
ProteinModelPortali P17213.
SMRi P17213. Positions 32-487.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

TCDBi 1.C.40.1.1. the bactericidal permeability increasing protein (bpip) family.

PTM databases

PhosphoSitei P17213.

Polymorphism databases

DMDMi 215274242.

Proteomic databases

MaxQBi P17213.
PaxDbi P17213.
PRIDEi P17213.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262865 ; ENSP00000262865 ; ENSG00000101425 .
GeneIDi 671.
KEGGi hsa:671.
UCSCi uc002xib.2. human.

Organism-specific databases

CTDi 671.
GeneCardsi GC20P036888.
H-InvDB HIX0027669.
HGNCi HGNC:1095. BPI.
MIMi 109195. gene.
neXtProti NX_P17213.
PharmGKBi PA25403.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG262970.
GeneTreei ENSGT00730000110583.
HOVERGENi HBG002797.
InParanoidi P17213.
OMAi CSSHINS.
PhylomeDBi P17213.
TreeFami TF315617.

Miscellaneous databases

ChiTaRSi BPI. human.
EvolutionaryTracei P17213.
GenomeRNAii 671.
NextBioi 2748.
PROi P17213.
SOURCEi Search...

Gene expression databases

Bgeei P17213.
ExpressionAtlasi P17213. baseline and differential.
Genevestigatori P17213.

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. "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.

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: October 29, 2014
This is version 146 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