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O95998

- I18BP_HUMAN

UniProt

O95998 - I18BP_HUMAN

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Protein

Interleukin-18-binding protein

Gene

IL18BP

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

Functioni

Isoform A binds to IL-18 and inhibits its activity. Functions as an inhibitor of the early TH1 cytokine response.2 Publications

GO - Molecular functioni

  1. interleukin-18 binding Source: UniProtKB
  2. receptor antagonist activity Source: UniProtKB

GO - Biological processi

  1. cellular response to hydrogen peroxide Source: Ensembl
  2. cellular response to tumor necrosis factor Source: Ensembl
  3. extracellular negative regulation of signal transduction Source: GOC
  4. response to lipopolysaccharide Source: Ensembl
  5. T-helper 1 type immune response Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-18-binding protein
Short name:
IL-18BP
Alternative name(s):
Tadekinig-alfa
Gene namesi
Name:IL18BP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:5987. IL18BP.

Subcellular locationi

Secreted Curated

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29803.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 30303 PublicationsAdd
BLAST
Chaini31 – 194164Interleukin-18-binding proteinPRO_0000014778Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi53 – 531O-linked (GalNAc...)1 Publication
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi86 ↔ 150PROSITE-ProRule annotation
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi103 – 1031N-linked (GlcNAc...) (complex)1 Publication
Glycosylationi147 – 1471N-linked (GlcNAc...) (complex)1 Publication

Post-translational modificationi

N- and O-glycosylated. O-glycosylated with core 1-like and core 2-like glycans. O-glycan heterogeneity at Ser-53: HexHexNAc (major) and Hex2HexNAc2 (minor). N-glycan heterogeneity at Asn-103: Hex5HexNAc4 (minor), dHex1Hex5HexNAc4 (major) and Hex6HexNAc5 (minor); N-glycan at Asn-147: dHex1Hex5HexNAc4.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO95998.
PRIDEiO95998.

Expressioni

Tissue specificityi

Strongly expressed in heart, lung, placenta and spleen.2 Publications

Gene expression databases

BgeeiO95998.
CleanExiHS_IL18BP.
ExpressionAtlasiO95998. baseline and differential.
GenevestigatoriO95998.

Organism-specific databases

HPAiCAB025980.

Interactioni

Protein-protein interaction databases

BioGridi115379. 1 interaction.
IntActiO95998. 3 interactions.
STRINGi9606.ENSP00000260049.

Structurei

3D structure databases

ProteinModelPortaliO95998.
SMRiO95998. Positions 74-169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 166102Ig-like C2-typeAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Signal

Phylogenomic databases

eggNOGiNOG45302.
GeneTreeiENSGT00390000004026.
HOVERGENiHBG052064.
InParanoidiO95998.
OMAiHFSILYW.
OrthoDBiEOG7MD4RH.
PhylomeDBiO95998.
TreeFamiTF337962.

Family and domain databases

InterProiIPR007110. Ig-like_dom.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform A (identifier: O95998-2) [UniParc]FASTAAdd to Basket

Also known as: IL-18BPA

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTMRHNWTPD LSPLWVLLLC AHVVTLLVRA TPVSQTTTAA TASVRSTKDP
60 70 80 90 100
CPSQPPVFPA AKQCPALEVT WPEVEVPLNG TLSLSCVACS RFPNFSILYW
110 120 130 140 150
LGNGSFIEHL PGRLWEGSTS RERGSTGTQL CKALVLEQLT PALHSTNFSC
160 170 180 190
VLVDPEQVVQ RHVVLAQLWA GLRATLPPTQ EALPSSHSSP QQQG
Length:194
Mass (Da):21,099
Last modified:July 7, 2009 - v2
Checksum:i5E520D6E46AFA843
GO
Isoform B (identifier: O95998-3) [UniParc]FASTAAdd to Basket

Also known as: IL-18BPB

The sequence of this isoform differs from the canonical sequence as follows:
     79-115: NGTLSLSCVACSRFPNFSILYWLGNGSFIEHLPGRLW → SWAEGNLAPHPRSPALQPQQSTAAGLRLSTGPAAAQP
     116-194: Missing.

Show »
Length:115
Mass (Da):12,221
Checksum:i2D6C79F64E1937BF
GO
Isoform D (identifier: O95998-4) [UniParc]FASTAAdd to Basket

Also known as: IL-18BPD

The sequence of this isoform differs from the canonical sequence as follows:
     128-163: TQLCKALVLEQLTPALHSTNFSCVLVDPEQVVQRHV → WAEGNLAPHPRSPALQPQQSTAAGLRLSTGPAAAQP
     164-194: Missing.

Show »
Length:163
Mass (Da):17,478
Checksum:iD25DD52998594ABB
GO

Sequence cautioni

The sequence AAD17189.1 differs from that shown. Reason: Intron retention.
The sequence AAD17192.1 differs from that shown. Reason: Intron retention.
The sequence AAD17187.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAD17188.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAD17190.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAD17191.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAF31697.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti91 – 911R → H.
Corresponds to variant rs5743672 [ dbSNP | Ensembl ].
VAR_059393
Natural varianti121 – 1211R → Q.
Corresponds to variant rs5743673 [ dbSNP | Ensembl ].
VAR_024497

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei79 – 11537NGTLS…PGRLW → SWAEGNLAPHPRSPALQPQQ STAAGLRLSTGPAAAQP in isoform B. 1 PublicationVSP_002515Add
BLAST
Alternative sequencei116 – 19479Missing in isoform B. 1 PublicationVSP_002516Add
BLAST
Alternative sequencei128 – 16336TQLCK…VQRHV → WAEGNLAPHPRSPALQPQQS TAAGLRLSTGPAAAQP in isoform D. 1 PublicationVSP_037605Add
BLAST
Alternative sequencei164 – 19431Missing in isoform D. 1 PublicationVSP_037606Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF110798 Genomic DNA. Translation: AAD17187.1. Different initiation.
AF110798 Genomic DNA. Translation: AAD17188.1. Different initiation.
AF110798 Genomic DNA. Translation: AAD17189.1. Sequence problems.
AF110799 mRNA. Translation: AAD17190.1. Different initiation.
AF110800 mRNA. Translation: AAD17191.1. Different initiation.
AF110801 mRNA. Translation: AAD17192.1. Sequence problems.
AB019504 mRNA. Translation: BAA76374.1.
AF122906 mRNA. Translation: AAD41051.1.
AF215907 mRNA. Translation: AAF31697.1. Different initiation.
AK098255 mRNA. Translation: BAG53602.1.
AP002490 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74813.1.
CH471076 Genomic DNA. Translation: EAW74816.1.
BC044215 mRNA. Translation: AAH44215.1.
CCDSiCCDS44666.1. [O95998-3]
CCDS8206.2. [O95998-2]
RefSeqiNP_001034748.1. NM_001039659.1. [O95998-2]
NP_001034749.1. NM_001039660.1. [O95998-2]
NP_001138527.1. NM_001145055.1. [O95998-3]
NP_001138529.1. NM_001145057.1. [O95998-2]
NP_005690.2. NM_005699.3.
NP_766630.2. NM_173042.2. [O95998-2]
NP_766632.2. NM_173044.2. [O95998-4]
XP_005273762.1. XM_005273705.1. [O95998-2]
UniGeneiHs.591967.

Genome annotation databases

EnsembliENST00000260049; ENSP00000260049; ENSG00000137496. [O95998-2]
ENST00000337131; ENSP00000338723; ENSG00000137496. [O95998-2]
ENST00000343898; ENSP00000343309; ENSG00000137496. [O95998-4]
ENST00000393703; ENSP00000377306; ENSG00000137496. [O95998-2]
ENST00000393705; ENSP00000377308; ENSG00000137496. [O95998-2]
ENST00000393707; ENSP00000377310; ENSG00000137496. [O95998-3]
ENST00000404792; ENSP00000384212; ENSG00000137496. [O95998-2]
ENST00000534583; ENSP00000434376; ENSG00000137496. [O95998-2]
ENST00000620017; ENSP00000480621; ENSG00000137496. [O95998-4]
GeneIDi10068.
KEGGihsa:10068.
UCSCiuc001ore.1. human. [O95998-2]
uc009ysv.1. human. [O95998-3]
uc021qmv.1. human. [O95998-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF110798 Genomic DNA. Translation: AAD17187.1 . Different initiation.
AF110798 Genomic DNA. Translation: AAD17188.1 . Different initiation.
AF110798 Genomic DNA. Translation: AAD17189.1 . Sequence problems.
AF110799 mRNA. Translation: AAD17190.1 . Different initiation.
AF110800 mRNA. Translation: AAD17191.1 . Different initiation.
AF110801 mRNA. Translation: AAD17192.1 . Sequence problems.
AB019504 mRNA. Translation: BAA76374.1 .
AF122906 mRNA. Translation: AAD41051.1 .
AF215907 mRNA. Translation: AAF31697.1 . Different initiation.
AK098255 mRNA. Translation: BAG53602.1 .
AP002490 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74813.1 .
CH471076 Genomic DNA. Translation: EAW74816.1 .
BC044215 mRNA. Translation: AAH44215.1 .
CCDSi CCDS44666.1. [O95998-3 ]
CCDS8206.2. [O95998-2 ]
RefSeqi NP_001034748.1. NM_001039659.1. [O95998-2 ]
NP_001034749.1. NM_001039660.1. [O95998-2 ]
NP_001138527.1. NM_001145055.1. [O95998-3 ]
NP_001138529.1. NM_001145057.1. [O95998-2 ]
NP_005690.2. NM_005699.3.
NP_766630.2. NM_173042.2. [O95998-2 ]
NP_766632.2. NM_173044.2. [O95998-4 ]
XP_005273762.1. XM_005273705.1. [O95998-2 ]
UniGenei Hs.591967.

3D structure databases

ProteinModelPortali O95998.
SMRi O95998. Positions 74-169.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115379. 1 interaction.
IntActi O95998. 3 interactions.
STRINGi 9606.ENSP00000260049.

Proteomic databases

PaxDbi O95998.
PRIDEi O95998.

Protocols and materials databases

DNASUi 10068.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260049 ; ENSP00000260049 ; ENSG00000137496 . [O95998-2 ]
ENST00000337131 ; ENSP00000338723 ; ENSG00000137496 . [O95998-2 ]
ENST00000343898 ; ENSP00000343309 ; ENSG00000137496 . [O95998-4 ]
ENST00000393703 ; ENSP00000377306 ; ENSG00000137496 . [O95998-2 ]
ENST00000393705 ; ENSP00000377308 ; ENSG00000137496 . [O95998-2 ]
ENST00000393707 ; ENSP00000377310 ; ENSG00000137496 . [O95998-3 ]
ENST00000404792 ; ENSP00000384212 ; ENSG00000137496 . [O95998-2 ]
ENST00000534583 ; ENSP00000434376 ; ENSG00000137496 . [O95998-2 ]
ENST00000620017 ; ENSP00000480621 ; ENSG00000137496 . [O95998-4 ]
GeneIDi 10068.
KEGGi hsa:10068.
UCSCi uc001ore.1. human. [O95998-2 ]
uc009ysv.1. human. [O95998-3 ]
uc021qmv.1. human. [O95998-4 ]

Organism-specific databases

CTDi 10068.
GeneCardsi GC11P071709.
H-InvDB HIX0009903.
HGNCi HGNC:5987. IL18BP.
HPAi CAB025980.
MIMi 604113. gene.
neXtProti NX_O95998.
PharmGKBi PA29803.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG45302.
GeneTreei ENSGT00390000004026.
HOVERGENi HBG052064.
InParanoidi O95998.
OMAi HFSILYW.
OrthoDBi EOG7MD4RH.
PhylomeDBi O95998.
TreeFami TF337962.

Miscellaneous databases

GeneWikii IL18BP.
GenomeRNAii 10068.
NextBioi 38051.
PROi O95998.
SOURCEi Search...

Gene expression databases

Bgeei O95998.
CleanExi HS_IL18BP.
ExpressionAtlasi O95998. baseline and differential.
Genevestigatori O95998.

Family and domain databases

InterProi IPR007110. Ig-like_dom.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Interleukin-18 binding protein: a novel modulator of the Th1 cytokine response."
    Novick D., Kim S.-H., Fantuzzi G., Reznikov L.L., Dinarello C.A., Rubinstein M.
    Immunity 10:127-136(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B), PROTEIN SEQUENCE OF 31-70, FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 31-35; 39-45; 48-54; 57-60; 63-74; 91-95; 107-144 AND 151-169, TISSUE SPECIFICITY.
  3. "Identification of human and mouse homologs of the MC51L-53L-54L family of secreted glycoproteins encoded by the Molluscum contagiosum poxvirus."
    Xiang Y., Moss B.
    Virology 257:297-302(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
  4. "Structural requirements of six naturally occurring isoforms of the IL-18 binding protein to inhibit IL-18."
    Kim S.-H., Eisenstein M., Reznikov L., Fantuzzi G., Novick D., Rubinstein M., Dinarello C.A.
    Proc. Natl. Acad. Sci. U.S.A. 97:1190-1195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), FUNCTION, ALTERNATIVE SPLICING (ISOFORMS A AND B).
    Tissue: T-cell.
  5. "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] (ISOFORM A).
    Tissue: Uterus.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM A).
    Tissue: Leukocyte.
  9. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-45.
  10. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
    Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
    Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-53; ASN-103 AND ASN-147, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiI18BP_HUMAN
AccessioniPrimary (citable) accession number: O95998
Secondary accession number(s): B3KUZ0
, B7WPK4, O95993, O96027, Q9NZA9, Q9UBR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 7, 2009
Last modified: October 29, 2014
This is version 124 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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