ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P05000


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name IFNW1_HUMAN
Primary accession number P05000
Secondary accession numbers Q13168 Q5U802 Q5VWD0 Q7M4P5
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on July 1, 1993 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 90)
Name and origin of the protein
Protein name Interferon omega-1 [Precursor]
Synonym Interferon alpha-II-1
Gene name
Name: IFNW1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2985969 [NCBI, ExPASy, EBI, Israel, Japan]
Capon D.J., Shepard H.M., Goeddel D.V.;
"Two distinct families of human and bovine interferon-alpha genes are coordinately expressed and encode functional polypeptides.";
Mol. Cell. Biol. 5:768-779(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Leukocyte;
DOI=10.1016/0167-4781(91)90004-6; PubMed=1647209 [NCBI, ExPASy, EBI, Israel, Japan]
Adolf G.R., Fruehbeis B., Hauptmann R., Kalsner I., Maurer-Fogy I., Ostermann E., Patzelt E., Schwendenwein R., Sommergruber W., Zoephel A.;
"Human interferon omega 1: isolation of the gene, expression in Chinese hamster ovary cells and characterization of the recombinant protein.";
Biochim. Biophys. Acta 1089:167-174(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02465; PubMed=15164053 [NCBI, ExPASy, EBI, Israel, Japan]
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 22-195.
DOI=10.1093/nar/13.13.4739; PubMed=3895159 [NCBI, ExPASy, EBI, Israel, Japan]
Hauptmann R., Swetly P.;
"A novel class of human type I interferons.";
Nucleic Acids Res. 13:4739-4749(1985).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-195.
PubMed=8142025 [NCBI, ExPASy, EBI, Israel, Japan]
Li M.F., Zeng Q., Zhou Y., Guo H.Y., Hou Y.D.;
"Cloning, sequencing and expression in E. coli of interferon-omega 1 gene.";
Sci. China, Ser. B, Chem. Life Sci. Earth Sci. 36:1361-1366(1993).
[8]
PROTEIN SEQUENCE OF 22-55.
PubMed=7765487 [NCBI, ExPASy, EBI, Israel, Japan]
Shirono H., Koga J., Uemura H., Matsuo A.;
"Identification of glycosylated subtypes of interferon-alpha produced by human leukocytes.";
Biosci. Biotechnol. Biochem. 58:1714-1715(1994).
[9]
PROTEIN SEQUENCE OF 22-36.
DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[10]
PROTEIN SEQUENCE OF 22-33, AND GLYCOSYLATION AT ASN-101.
PubMed=1693148 [NCBI, ExPASy, EBI, Israel, Japan]
Adolf G.R., Maurer-Fogy I., Kalsner I., Cantell K.;
"Purification and characterization of natural human interferon omega 1. Two alternative cleavage sites for the signal peptidase.";
J. Biol. Chem. 265:9290-9295(1990).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 24-195.
TISSUE=Liver;
Yang R.Y., Yang Z.F., Zhu Y.T., Feng L.L., Liu N., Zhao F., Zhang F.X., Fu L.C.;
"Human IFN-omega 1 gene isolated from embryonic hepar.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M11003; AAA52724.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X58822; CAA41626.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390882; CAH70158.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471071; EAW58624.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069095; AAH69095.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC117290; AAI17291.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC117292; AAI17293.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X02669; CAA26501.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
A12140; CAA01011.1; -; Unassigned_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U25670; AAA70091.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY780805; AAV49320.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A93070; IVHUII.
PC2204; PC2204.
PC2205; PC2205.
RefSeq NP_002168.1; -.
UniGene Hs.73010
3D structure databases
HSSP P01563; 1ITF. [HSSP ENTRY / PDB]
ModBase P05000.
PTM databases
GlycoSuiteDB P05000; -.
Organism-specific databases
H-InvDB HIX0034819; -.
HGNC HGNC:5448; IFNW1.
GenAtlas IFNW1.
MIM 147553; gene. [NCBI / EBI]
PharmGKB PA29683; -.
GeneCards P05000.
Gene expression databases
ArrayExpress P05000; -.
CleanEx HS_IFNW1; -.
GermOnline ENSG00000177047; Homo sapiens.
Ontologies
GO
GO:0005126; Molecular function: hematopoietin/interferon-class (D200-domain) cytokine receptor binding (traceable author statement from ProtInc).
GO:0007050; Biological process: cell cycle arrest (traceable author statement from ProtInc).
GO:0009615; Biological process: response to virus (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR012351; 4_helix_cytokine_core.
IPR000471; Interferon_abd.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1250.10; 4_helix_cytokine_core; 1.
PANTHER PTHR11691; Interferon_abd; 1.
Pfam PF00143; Interferon; 1.
Pfam graphical view of domain structure.
PRINTS PR00266; INTERFERONAB.
ProDom PD000550; Interferon_abd; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00076; IFabd; 1.
SMART graphical view of domain structure.
PROSITE PS00252; INTERFERON_A_B_D; 1.
BLOCKS P05000.
Genome annotation databases
Ensembl ENSG00000177047; Homo sapiens. [Contig view]
GeneID 3467; -.
KEGG hsa:3467; -.
Phylogenomic databases
HOGENOM P05000; -.
HOVERGEN P05000; -.
Other
LinkHub P05000; -.
SOURCE IFNW1; Homo sapiens.
ProtoNet P05000.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Antiviral defense; Cytokine; Direct protein sequencing; Glycoprotein; Polymorphism; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    21  21     Or 23 in some molecules. 
CHAIN   22   195  174     Interferon omega-1. PRO_0000016408
CARBOHYD   101   101        N-linked (GlcNAc...) [GlycoSuiteDB]. CAR_000050
DISULFID   24   122        By similarity. 
DISULFID   52   162        By similarity. 
VARIANT   95    95  1     R -> S (in dbSNP:rs2230055 [NCBI]). VAR_020028 
CONFLICT   22    23        LG -> EF (in Ref. 7; AAA70091). 
CONFLICT   42    42        H -> M (in Ref. 8; AA sequence). 
CONFLICT   79    79        V -> A (in Ref. 7; AAA70091). 
CONFLICT   111   111        G -> E (in Ref. 1; AAA52724). 
CONFLICT   167   167        V -> D (in Ref. 7; AAA70091). 
Sequence information
Length: 195 AA [This is the length of the unprocessed precursor] Molecular weight: 22319 Da [This is the MW of the unprocessed precursor] CRC64: 1E4306F3487987FA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MALLFPLLAA LVMTSYSPVG SLGCDLPQNH GLLSRNTLVL LHQMRRISPF LCLKDRRDFR 

        70         80         90        100        110        120 
FPQEMVKGSQ LQKAHVMSVL HEMLQQIFSL FHTERSSAAW NMTLLDQLHT GLHQQLQHLE 

       130        140        150        160        170        180 
TCLLQVVGEG ESAGAISSPA LTLRRYFQGI RVYLKEKKYS DCAWEVVRME IMKSLFLSTN 

       190 
MQERLRSKDR DLGSS 

P05000 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!