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P01563

- IFNA2_HUMAN

UniProt

P01563 - IFNA2_HUMAN

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Protein
Interferon alpha-2
Gene
IFNA2, IFNA2A, IFNA2B, IFNA2C
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Produced by macrophages, IFN-alpha have antiviral activities.

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. type I interferon receptor binding Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. apoptotic process Source: ProtInc
  2. blood coagulation Source: Reactome
  3. cell surface receptor signaling pathway Source: ProtInc
  4. cell-cell signaling Source: ProtInc
  5. cytokine-mediated signaling pathway Source: Reactome
  6. defense response to virus Source: UniProtKB-KW
  7. inflammatory response Source: ProtInc
  8. innate immune response Source: Reactome
  9. negative regulation of T cell differentiation Source: UniProtKB
  10. negative regulation of T-helper 2 cell cytokine production Source: UniProtKB
  11. negative regulation of gene expression Source: UniProtKB
  12. negative regulation of interleukin-13 secretion Source: UniProtKB
  13. negative regulation of interleukin-5 secretion Source: UniProtKB
  14. negative regulation of transcription, DNA-templated Source: UniProtKB
  15. negative regulation of viral entry into host cell Source: BHF-UCL
  16. positive regulation of tyrosine phosphorylation of Stat3 protein Source: BHF-UCL
  17. regulation of type I interferon-mediated signaling pathway Source: Reactome
  18. type I interferon signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Antiviral defense

Enzyme and pathway databases

ReactomeiREACT_24938. TRAF6 mediated IRF7 activation.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_25162. Interferon alpha/beta signaling.
REACT_25216. Regulation of IFNA signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon alpha-2
Short name:
IFN-alpha-2
Alternative name(s):
Interferon alpha-A
Short name:
LeIF A
Gene namesi
Name:IFNA2
Synonyms:IFNA2A, IFNA2B, IFNA2C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:5423. IFNA2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Pharmaceutical usei

Available under the names Roferon-A (Roche) or Intron-A (Schering-Plough). Used as an anticancer drug for its antiproliferative activity.

Organism-specific databases

PharmGKBiPA29662.

Protein family/group databases

Allergomei9876. Hom s IFN alpha.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23232 Publications
Add
BLAST
Chaini24 – 188165Interferon alpha-2
PRO_0000016360Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 1213 Publications
Disulfide bondi52 ↔ 1613 Publications
Glycosylationi129 – 1291O-linked (GalNAc...)1 Publication
CAR_000049

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP01563.
PRIDEiP01563.

PTM databases

PhosphoSiteiP01563.
UniCarbKBiP01563.

Expressioni

Gene expression databases

CleanExiHS_IFNA2.
GenevestigatoriP01563.

Organism-specific databases

HPAiHPA047557.

Interactioni

Subunit structurei

Interacts with IFNAR2.2 Publications

Protein-protein interaction databases

BioGridi109663. 1 interaction.
DIPiDIP-3784N.
DIP-481N.
IntActiP01563. 1 interaction.
STRINGi9606.ENSP00000369554.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 283
Helixi32 – 4413
Helixi50 – 556
Helixi63 – 653
Beta strandi67 – 693
Beta strandi71 – 755
Helixi76 – 8914
Helixi93 – 986
Helixi101 – 12020
Beta strandi126 – 1294
Helixi138 – 15518
Turni156 – 1583
Helixi160 – 17718
Turni179 – 1824

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ITFNMR-A24-188[»]
1RH2X-ray2.90A/B/C/D/E/F24-188[»]
2HIEmodel-A24-188[»]
2HYMNMR-B24-188[»]
2KZ1NMR-A24-188[»]
2LAGNMR-A24-188[»]
2LMSNMR-A24-188[»]
3S9DX-ray2.00A/C24-188[»]
3SE3X-ray4.00B24-188[»]
ProteinModelPortaliP01563.
SMRiP01563. Positions 24-188.

Miscellaneous databases

EvolutionaryTraceiP01563.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG246451.
HOGENOMiHOG000230500.
HOVERGENiHBG052086.
InParanoidiP01563.
KOiK05414.
OrthoDBiEOG7M98HV.
PhylomeDBiP01563.
TreeFamiTF336177.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR000471. Interferon_alpha/beta/delta.
[Graphical view]
PANTHERiPTHR11691. PTHR11691. 1 hit.
PfamiPF00143. Interferon. 1 hit.
[Graphical view]
PRINTSiPR00266. INTERFERONAB.
SMARTiSM00076. IFabd. 1 hit.
[Graphical view]
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00252. INTERFERON_A_B_D. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01563-1 [UniParc]FASTAAdd to Basket

« Hide

MALTFALLVA LLVLSCKSSC SVGCDLPQTH SLGSRRTLML LAQMRKISLF    50
SCLKDRHDFG FPQEEFGNQF QKAETIPVLH EMIQQIFNLF STKDSSAAWD 100
ETLLDKFYTE LYQQLNDLEA CVIQGVGVTE TPLMKEDSIL AVRKYFQRIT 150
LYLKEKKYSP CAWEVVRAEI MRSFSLSTNL QESLRSKE 188
Length:188
Mass (Da):21,550
Last modified:July 21, 1986 - v1
Checksum:i101DD21D394CBF97
GO

Polymorphismi

Three forms exist; alpha-2a (shown here), alpha-2b and alpha-2c.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61A → D.
Corresponds to variant rs35971916 [ dbSNP | Ensembl ].
VAR_055972
Natural varianti46 – 461K → R in alpha-2B and alpha-2C. 1 Publication
Corresponds to variant rs1061959 [ dbSNP | Ensembl ].
VAR_004012
Natural varianti57 – 571H → R in alpha-2C.
VAR_013001
Natural varianti177 – 1771S → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_036329

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851Q → L in AEX60803. 1 Publication
Sequence conflicti93 – 931K → M in AEX60802. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J00207 Genomic DNA. Translation: AAB59402.1.
V00544 mRNA. Translation: CAA23805.1.
V00548 mRNA. Translation: CAA23809.1.
V00549 mRNA. Translation: CAA23810.1.
Y11834 Genomic DNA. Translation: CAA72532.1.
JN591568 mRNA. Translation: AEX60802.1.
JN591569 mRNA. Translation: AEX60803.1.
JN591570 mRNA. Translation: AEX60804.1.
JN848522 mRNA. Translation: AET86951.1.
CR541921 mRNA. Translation: CAG46719.1.
CH471071 Genomic DNA. Translation: EAW58611.1.
BC074936 mRNA. Translation: AAH74936.1.
BC074937 mRNA. Translation: AAH74937.1.
BC104163 mRNA. Translation: AAI04164.1.
BC104164 mRNA. Translation: AAI04165.1.
M54886 mRNA. Translation: AAA59181.1.
M29883 Genomic DNA. Translation: AAA52715.1.
CCDSiCCDS6506.1.
PIRiA93234. IVHUA2.
I78570.
RefSeqiNP_000596.2. NM_000605.3.
UniGeneiHs.211575.

Genome annotation databases

EnsembliENST00000380206; ENSP00000369554; ENSG00000188379.
GeneIDi3440.
KEGGihsa:3440.

Polymorphism databases

DMDMi124449.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J00207 Genomic DNA. Translation: AAB59402.1 .
V00544 mRNA. Translation: CAA23805.1 .
V00548 mRNA. Translation: CAA23809.1 .
V00549 mRNA. Translation: CAA23810.1 .
Y11834 Genomic DNA. Translation: CAA72532.1 .
JN591568 mRNA. Translation: AEX60802.1 .
JN591569 mRNA. Translation: AEX60803.1 .
JN591570 mRNA. Translation: AEX60804.1 .
JN848522 mRNA. Translation: AET86951.1 .
CR541921 mRNA. Translation: CAG46719.1 .
CH471071 Genomic DNA. Translation: EAW58611.1 .
BC074936 mRNA. Translation: AAH74936.1 .
BC074937 mRNA. Translation: AAH74937.1 .
BC104163 mRNA. Translation: AAI04164.1 .
BC104164 mRNA. Translation: AAI04165.1 .
M54886 mRNA. Translation: AAA59181.1 .
M29883 Genomic DNA. Translation: AAA52715.1 .
CCDSi CCDS6506.1.
PIRi A93234. IVHUA2.
I78570.
RefSeqi NP_000596.2. NM_000605.3.
UniGenei Hs.211575.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ITF NMR - A 24-188 [» ]
1RH2 X-ray 2.90 A/B/C/D/E/F 24-188 [» ]
2HIE model - A 24-188 [» ]
2HYM NMR - B 24-188 [» ]
2KZ1 NMR - A 24-188 [» ]
2LAG NMR - A 24-188 [» ]
2LMS NMR - A 24-188 [» ]
3S9D X-ray 2.00 A/C 24-188 [» ]
3SE3 X-ray 4.00 B 24-188 [» ]
ProteinModelPortali P01563.
SMRi P01563. Positions 24-188.
ModBasei Search...

Protein-protein interaction databases

BioGridi 109663. 1 interaction.
DIPi DIP-3784N.
DIP-481N.
IntActi P01563. 1 interaction.
STRINGi 9606.ENSP00000369554.

Chemistry

DrugBanki DB00034. Interferon Alfa-2a, Recombinant.
DB00105. Interferon Alfa-2b, Recombinant.
DB00011. Interferon alfa-n1.
DB00008. Peginterferon alfa-2a.
DB00022. Peginterferon alfa-2b.

Protein family/group databases

Allergomei 9876. Hom s IFN alpha.

PTM databases

PhosphoSitei P01563.
UniCarbKBi P01563.

Polymorphism databases

DMDMi 124449.

Proteomic databases

PaxDbi P01563.
PRIDEi P01563.

Protocols and materials databases

DNASUi 3440.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380206 ; ENSP00000369554 ; ENSG00000188379 .
GeneIDi 3440.
KEGGi hsa:3440.

Organism-specific databases

CTDi 3440.
GeneCardsi GC09M021374.
H-InvDB HIX0034810.
HGNCi HGNC:5423. IFNA2.
HPAi HPA047557.
MIMi 147562. gene.
neXtProti NX_P01563.
PharmGKBi PA29662.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG246451.
HOGENOMi HOG000230500.
HOVERGENi HBG052086.
InParanoidi P01563.
KOi K05414.
OrthoDBi EOG7M98HV.
PhylomeDBi P01563.
TreeFami TF336177.

Enzyme and pathway databases

Reactomei REACT_24938. TRAF6 mediated IRF7 activation.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_25162. Interferon alpha/beta signaling.
REACT_25216. Regulation of IFNA signaling.

Miscellaneous databases

EvolutionaryTracei P01563.
GeneWikii IFNA2.
GenomeRNAii 3440.
NextBioi 13556.
PROi P01563.
SOURCEi Search...

Gene expression databases

CleanExi HS_IFNA2.
Genevestigatori P01563.

Family and domain databases

Gene3Di 1.20.1250.10. 1 hit.
InterProi IPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR000471. Interferon_alpha/beta/delta.
[Graphical view ]
PANTHERi PTHR11691. PTHR11691. 1 hit.
Pfami PF00143. Interferon. 1 hit.
[Graphical view ]
PRINTSi PR00266. INTERFERONAB.
SMARTi SM00076. IFabd. 1 hit.
[Graphical view ]
SUPFAMi SSF47266. SSF47266. 1 hit.
PROSITEi PS00252. INTERFERON_A_B_D. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "The structure of eight distinct cloned human leukocyte interferon cDNAs."
    Goeddel D.V., Leung D.W., Dull T.J., Gross M., Lawn R.M., McCandliss R., Seeburg P.H., Ullrich A., Yelverton E., Gray P.W.
    Nature 290:20-26(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  4. "Cloning of human leukocyte interferon cDNA and a strategy for its production in E. coli."
    Oliver G., Balbas P., Valle F., Soberon X., Bolivar F.
    Rev. Latinoam. Microbiol. 27:141-150(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Bone marrow tumor.
  5. "A defective retroviral vector encoding human interferon alpha 2 can transduce human leukemic cell lines."
    Austruy E., Bagnis C., Carbuccia N., Maroc C., Birg F., Dubreuil P., Mannoni P., Chabannon C.
    Cancer Gene Ther. 5:247-256(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  6. "Heterologous expression, immunochemical and computational analysis of recombinant human interferon alpha 2b."
    Gull I., Samra Z.Q., Aslam M.S., Athar M.A.
    Springerplus 2:264-264(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-46.
  7. Hanif K., Noor S., Naveed Y., Bashir B., Hussain T., Kanwal N.
    Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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].
  11. "At least three human type alpha interferons: structure of alpha 2."
    Streuli M., Nagata S., Weissmann C.
    Science 209:1343-1347(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 7-188.
  12. "Formation of genes coding for hybrid proteins by recombination between related, cloned genes in E. coli."
    Weber H., Weissmann C.
    Nucleic Acids Res. 11:5661-5669(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-188.
  13. "A family of structural genes for human lymphoblastoid (leukocyte-type) interferon."
    Allen G., Fantes K.H.
    Nature 287:408-411(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-112 AND 136-188.
  14. "Identification of nine interferon-alpha subtypes produced by Sendai virus-induced human peripheral blood leucocytes."
    Nyman T.A., Toeloe H., Parkkinen J., Kalkkinen N.
    Biochem. J. 329:295-302(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-58.
  15. "Assignment of the disulphide bonds of leukocyte interferon."
    Wetzel R.
    Nature 289:606-607(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  16. "Natural human interferon-alpha 2 is O-glycosylated."
    Adolf G.R., Kalsner I., Ahorn H., Maurer-Fogy I., Cantell K.
    Biochem. J. 276:511-518(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-129, ALLELES ALPHA-2B AND ALPHA-2C.
  17. Cited for: POLYMORPHISM.
  18. Cited for: 3D-STRUCTURE MODELING.
  19. "Zinc mediated dimer of human interferon-alpha 2b revealed by X-ray crystallography."
    Radhakrishnan R., Walter L.J., Hruza A., Reichert P., Trotta P.P., Nagabhushan T.L., Walter M.R.
    Structure 4:1453-1463(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
  20. "The three-dimensional high resolution structure of human interferon alpha-2a determined by heteronuclear NMR spectroscopy in solution."
    Klaus W., Gsell B., Labhardt A.M., Wipf B., Senn H.
    J. Mol. Biol. 274:661-675(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  21. "Determination of the human type I interferon receptor binding site on human interferon-alpha2 by cross saturation and an NMR-based model of the complex."
    Quadt-Akabayov S.R., Chill J.H., Levy R., Kessler N., Anglister J.
    Protein Sci. 15:2656-2668(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 24-188 IN COMPLEX WITH IFNAR2, SUBUNIT, DISULFIDE BONDS.
  22. "Intermolecular interactions in a 44 kDa interferon-receptor complex detected by asymmetric reverse-protonation and two-dimensional NOESY."
    Nudelman I., Akabayov S.R., Schnur E., Biron Z., Levy R., Xu Y., Yang D., Anglister J.
    Biochemistry 49:5117-5133(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 24-188 IN COMPLEX WITH IFNAR2, SUBUNIT, DISULFIDE BONDS.
  23. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-177.

Entry informationi

Entry nameiIFNA2_HUMAN
AccessioniPrimary (citable) accession number: P01563
Secondary accession number(s): H2DF54
, H2DF55, P01564, Q14606, Q6DJX8, Q96KI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 3, 2014
This is version 149 of the entry and version 1 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, Pharmaceutical, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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

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