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P48551

- INAR2_HUMAN

UniProt

P48551 - INAR2_HUMAN

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Protein

Interferon alpha/beta receptor 2

Gene
IFNAR2, IFNABR, IFNARB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Associates with IFNAR1 to form the type I interferon receptor. Receptor for interferons alpha and beta. Involved in IFN-mediated STAT1, STAT2 and STAT3 activation. Isoform 1 and isoform 2 are directly involved in signal transduction due to their association with the TYR kinase, JAK1. Isoform 3 is a potent inhibitor of type I IFN receptor activity.5 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. protein kinase binding Source: UniProtKB
  3. type I interferon binding Source: UniProtKB
  4. type I interferon receptor activity Source: UniProtKB

GO - Biological processi

  1. cell proliferation Source: Ensembl
  2. cell surface receptor signaling pathway Source: ProtInc
  3. cytokine-mediated signaling pathway Source: Reactome
  4. JAK-STAT cascade Source: ProtInc
  5. regulation of transcription from RNA polymerase II promoter Source: Ensembl
  6. regulation of type I interferon-mediated signaling pathway Source: Reactome
  7. response to interferon-alpha Source: UniProtKB
  8. response to virus Source: ProtInc
  9. type I interferon signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

ReactomeiREACT_25162. Interferon alpha/beta signaling.
REACT_25216. Regulation of IFNA signaling.
SignaLinkiP48551.

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon alpha/beta receptor 2
Short name:
IFN-R-2
Short name:
IFN-alpha binding protein
Short name:
IFN-alpha/beta receptor 2
Alternative name(s):
Interferon alpha binding protein
Type I interferon receptor 2
Gene namesi
Name:IFNAR2
Synonyms:IFNABR, IFNARB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:5433. IFNAR2.

Subcellular locationi

Isoform 1 : Membrane; Single-pass type I membrane protein 2 Publications
Isoform 2 : Membrane; Single-pass type I membrane protein 2 Publications
Isoform 3 : Secreted 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 243217Extracellular Reviewed predictionAdd
BLAST
Transmembranei244 – 26421Helical; Reviewed predictionAdd
BLAST
Topological domaini265 – 515251Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. extracellular region Source: ProtInc
  2. extracellular space Source: UniProtKB
  3. integral component of plasma membrane Source: UniProtKB
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi269 – 2691Y → F: Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-306; F-316; F-318; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-306; F-316; F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-306; F-316; F-318 and F-337. 2 Publications
Mutagenesisi306 – 3061Y → F: Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-316; F-318; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-316; F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-316; F-318 and F-337. 2 Publications
Mutagenesisi316 – 3161Y → F: Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-318; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-318 and F-337. 2 Publications
Mutagenesisi318 – 3181Y → F: Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-411 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316 and F-337. 2 Publications
Mutagenesisi337 – 3371Y → F: Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316 and F-318. 2 Publications
Mutagenesisi411 – 4111Y → F: Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-318; F-337 and F-512. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-318 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-512. 2 Publications
Mutagenesisi512 – 5121Y → F: Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-318; F-337 and F-411. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-318 and F-411. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-411. 2 Publications

Organism-specific databases

MIMi610424. phenotype.
PharmGKBiPA29671.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Add
BLAST
Chaini27 – 515489Interferon alpha/beta receptor 2PRO_0000011006Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 1224 Publications
Glycosylationi58 – 581N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi85 ↔ 934 Publications
Glycosylationi87 – 871N-linked (GlcNAc...)1 Publication
Glycosylationi116 – 1161N-linked (GlcNAc...) Reviewed prediction
Glycosylationi188 – 1881N-linked (GlcNAc...) Reviewed prediction
Glycosylationi192 – 1921N-linked (GlcNAc...)1 Publication
Disulfide bondi207 ↔ 2274 Publications
Modified residuei337 – 3371Phosphotyrosine2 Publications
Modified residuei467 – 4671Phosphoserine By similarity
Modified residuei512 – 5121Phosphotyrosine2 Publications

Post-translational modificationi

Phosphorylated on tyrosine residues upon interferon binding. Phosphorylation at Tyr-337 or Tyr-512 are sufficient to mediate interferon dependent activation of STAT1, STAT2 and STAT3 leading to antiproliferative effects on many different cell types.3 Publications
Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP48551.
PaxDbiP48551.
PRIDEiP48551.

PTM databases

PhosphoSiteiP48551.

Miscellaneous databases

PMAP-CutDBQ6FHD7.

Expressioni

Tissue specificityi

Isoform 3 is detected in the urine (at protein level). Expressed in blood cells. Expressed in lymphoblastoid and fibrosarcoma cell lines.3 Publications

Gene expression databases

ArrayExpressiP48551.
BgeeiP48551.
CleanExiHS_IFNAR2.
GenevestigatoriP48551.

Organism-specific databases

HPAiCAB025889.

Interactioni

Subunit structurei

Heterodimer with IFNAR1; in presence of interferon alpha and/or beta ligands forms the type I interferon receptor. Isoform 1 interacts with the transcriptional factors STAT1 and STAT2. Interacts with JAK1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CREBBPQ927934EBI-958408,EBI-81215
GNB2L1P632444EBI-958408,EBI-296739
IRF9Q009786EBI-958408,EBI-626526
JAK1P234583EBI-958408,EBI-1383438
STAT2P526302EBI-958408,EBI-1546963
USP18Q9UMW84EBI-958408,EBI-356206

Protein-protein interaction databases

BioGridi109677. 10 interactions.
DIPiDIP-945N.
IntActiP48551. 13 interactions.
MINTiMINT-196715.
STRINGi9606.ENSP00000343957.

Structurei

Secondary structure

1
515
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 467
Beta strandi49 – 557
Beta strandi59 – 613
Beta strandi65 – 7511
Helixi83 – 853
Beta strandi86 – 894
Beta strandi91 – 944
Turni96 – 983
Beta strandi102 – 1043
Beta strandi106 – 1138
Beta strandi119 – 1268
Helixi128 – 1314
Beta strandi138 – 1436
Beta strandi148 – 1536
Helixi159 – 1613
Beta strandi167 – 1748
Beta strandi177 – 1815
Turni186 – 1883
Beta strandi191 – 1977
Beta strandi205 – 2139
Beta strandi226 – 2294

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N6UNMR-A28-237[»]
1N6VNMR-A28-237[»]
2HYMNMR-A28-237[»]
2KZ1NMR-B28-237[»]
2LAGNMR-B28-237[»]
3S8WX-ray2.60A/B/C131-232[»]
3S9DX-ray2.00B/D37-232[»]
3SE3X-ray4.00C34-232[»]
3SE4X-ray3.50C34-232[»]
ProteinModelPortaliP48551.
SMRiP48551. Positions 28-237.

Miscellaneous databases

EvolutionaryTraceiP48551.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG41946.
HOGENOMiHOG000013219.
HOVERGENiHBG053907.
InParanoidiP48551.
KOiK05131.
OMAiIYIRLER.
PhylomeDBiP48551.
TreeFamiTF335897.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015373. Interferon_alpha/beta_rcpt_bsu.
[Graphical view]
PfamiPF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.

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 1 (identifier: P48551-1) [UniParc]FASTAAdd to Basket

Also known as: Long form beta, IFNaR2-2, IFNaR2-1b

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

MLLSQNAFIF RSLNLVLMVY ISLVFGISYD SPDYTDESCT FKISLRNFRS    50
ILSWELKNHS IVPTHYTLLY TIMSKPEDLK VVKNCANTTR SFCDLTDEWR 100
STHEAYVTVL EGFSGNTTLF SCSHNFWLAI DMSFEPPEFE IVGFTNHINV 150
MVKFPSIVEE ELQFDLSLVI EEQSEGIVKK HKPEIKGNMS GNFTYIIDKL 200
IPNTNYCVSV YLEHSDEQAV IKSPLKCTLL PPGQESESAE SAKIGGIITV 250
FLIALVLTST IVTLKWIGYI CLRNSLPKVL NFHNFLAWPF PNLPPLEAMD 300
MVEVIYINRK KKVWDYNYDD ESDSDTEAAP RTSGGGYTMH GLTVRPLGQA 350
SATSTESQLI DPESEEEPDL PEVDVELPTM PKDSPQQLEL LSGPCERRKS 400
PLQDPFPEED YSSTEGSGGR ITFNVDLNSV FLRVLDDEDS DDLEAPLMLS 450
SHLEEMVDPE DPDNVQSNHL LASGEGTQPT FPSPSSEGLW SEDAPSDQSD 500
TSESDVDLGD GYIMR 515
Length:515
Mass (Da):57,759
Last modified:February 1, 1996 - v1
Checksum:i4D7730D93AA739F4
GO
Isoform 2 (identifier: P48551-2) [UniParc]FASTAAdd to Basket

Also known as: Short form beta, IFNaR2-1, IFNaR2-1a

The sequence of this isoform differs from the canonical sequence as follows:
     281-331: NFHNFLAWPF...SDSDTEAAPR → RQGLAKGWNA...YKRASLCPSD
     332-515: Missing.

Show »
Length:331
Mass (Da):37,393
Checksum:i6F6A2FD6E7A7449B
GO
Isoform 3 (identifier: P48551-3) [UniParc]FASTAAdd to Basket

Also known as: IFNaR2-3, IFNaR2-2a, P40

The sequence of this isoform differs from the canonical sequence as follows:
     238-239: SA → FS
     240-515: Missing.

Note: Soluble receptor.

Show »
Length:239
Mass (Da):27,384
Checksum:i705E887E728A4FB6
GO

Polymorphismi

Genetic variations in IFNAR2 influence susceptibility to hepatitis B virus (HBV) infection [MIMi:610424].

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81F → S Associated with susceptibility to HVB infection; lower cell surface levels; lower induction of MHC class 1 expression by INF-alpha. 2 Publications
Corresponds to variant rs2229207 [ dbSNP | Ensembl ].
VAR_020521
Natural varianti10 – 101F → V.5 Publications
Corresponds to variant rs1051393 [ dbSNP | Ensembl ].
VAR_020522
Natural varianti196 – 1961I → V.1 Publication
Corresponds to variant rs17860223 [ dbSNP | Ensembl ].
VAR_020523

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei238 – 2392SA → FS in isoform 3. VSP_001736
Alternative sequencei240 – 515276Missing in isoform 3. VSP_001737Add
BLAST
Alternative sequencei281 – 33151NFHNF…EAAPR → RQGLAKGWNAVAIHRCSHNA LQSETPELKQSSCLSFPSSW DYKRASLCPSD in isoform 2. VSP_001738Add
BLAST
Alternative sequencei332 – 515184Missing in isoform 2. VSP_001739Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti151 – 1511M → V in AAC50202. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X77722 mRNA. Translation: CAA54785.1.
L42243
, L42238, L42239, L42240, L42323, L42241, L42242 Genomic DNA. Translation: AAB46417.1.
L42243
, L42238, L42239, L42240, L42323, L42241 Genomic DNA. Translation: AAB46418.1.
L42243
, L42238, L42239, L42240, L42323, L42241, L42242 Genomic DNA. Translation: AAB46419.1.
L41942 mRNA. Translation: AAB46413.1.
L41943 mRNA. Translation: AAB46414.1.
L41944 mRNA. Translation: AAB46415.1.
U29584 mRNA. Translation: AAC50202.1.
X89814 mRNA. Translation: CAA61940.1.
X89772 mRNA. Translation: CAA61914.1.
AY740397 Genomic DNA. Translation: AAU21038.1.
AK293059 mRNA. Translation: BAF85748.1.
CR541817 mRNA. Translation: CAG46616.1.
AP000292 Genomic DNA. No translation available.
AP000293 Genomic DNA. No translation available.
AP000294 Genomic DNA. No translation available.
AP000295 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09842.1.
CH471079 Genomic DNA. Translation: EAX09843.1.
CH471079 Genomic DNA. Translation: EAX09844.1.
CH471079 Genomic DNA. Translation: EAX09846.1.
CCDSiCCDS13621.1. [P48551-1]
CCDS13622.1. [P48551-2]
PIRiI39073.
S59501.
RefSeqiNP_000865.2. NM_000874.4. [P48551-2]
NP_001276054.1. NM_001289125.1. [P48551-1]
NP_001276055.1. NM_001289126.1. [P48551-3]
NP_001276057.1. NM_001289128.1. [P48551-3]
NP_997467.1. NM_207584.2. [P48551-2]
NP_997468.1. NM_207585.2. [P48551-1]
UniGeneiHs.708195.

Genome annotation databases

EnsembliENST00000342101; ENSP00000343289; ENSG00000159110. [P48551-3]
ENST00000342136; ENSP00000343957; ENSG00000159110. [P48551-1]
ENST00000382241; ENSP00000371676; ENSG00000159110. [P48551-1]
ENST00000382264; ENSP00000371699; ENSG00000159110. [P48551-2]
ENST00000404220; ENSP00000384309; ENSG00000159110. [P48551-2]
GeneIDi3455.
KEGGihsa:3455.
UCSCiuc002yrb.3. human. [P48551-2]
uc002yrd.3. human. [P48551-1]
uc002yrf.3. human. [P48551-3]

Polymorphism databases

DMDMi1352466.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X77722 mRNA. Translation: CAA54785.1 .
L42243
, L42238 , L42239 , L42240 , L42323 , L42241 , L42242 Genomic DNA. Translation: AAB46417.1 .
L42243
, L42238 , L42239 , L42240 , L42323 , L42241 Genomic DNA. Translation: AAB46418.1 .
L42243
, L42238 , L42239 , L42240 , L42323 , L42241 , L42242 Genomic DNA. Translation: AAB46419.1 .
L41942 mRNA. Translation: AAB46413.1 .
L41943 mRNA. Translation: AAB46414.1 .
L41944 mRNA. Translation: AAB46415.1 .
U29584 mRNA. Translation: AAC50202.1 .
X89814 mRNA. Translation: CAA61940.1 .
X89772 mRNA. Translation: CAA61914.1 .
AY740397 Genomic DNA. Translation: AAU21038.1 .
AK293059 mRNA. Translation: BAF85748.1 .
CR541817 mRNA. Translation: CAG46616.1 .
AP000292 Genomic DNA. No translation available.
AP000293 Genomic DNA. No translation available.
AP000294 Genomic DNA. No translation available.
AP000295 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09842.1 .
CH471079 Genomic DNA. Translation: EAX09843.1 .
CH471079 Genomic DNA. Translation: EAX09844.1 .
CH471079 Genomic DNA. Translation: EAX09846.1 .
CCDSi CCDS13621.1. [P48551-1 ]
CCDS13622.1. [P48551-2 ]
PIRi I39073.
S59501.
RefSeqi NP_000865.2. NM_000874.4. [P48551-2 ]
NP_001276054.1. NM_001289125.1. [P48551-1 ]
NP_001276055.1. NM_001289126.1. [P48551-3 ]
NP_001276057.1. NM_001289128.1. [P48551-3 ]
NP_997467.1. NM_207584.2. [P48551-2 ]
NP_997468.1. NM_207585.2. [P48551-1 ]
UniGenei Hs.708195.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1N6U NMR - A 28-237 [» ]
1N6V NMR - A 28-237 [» ]
2HYM NMR - A 28-237 [» ]
2KZ1 NMR - B 28-237 [» ]
2LAG NMR - B 28-237 [» ]
3S8W X-ray 2.60 A/B/C 131-232 [» ]
3S9D X-ray 2.00 B/D 37-232 [» ]
3SE3 X-ray 4.00 C 34-232 [» ]
3SE4 X-ray 3.50 C 34-232 [» ]
ProteinModelPortali P48551.
SMRi P48551. Positions 28-237.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109677. 10 interactions.
DIPi DIP-945N.
IntActi P48551. 13 interactions.
MINTi MINT-196715.
STRINGi 9606.ENSP00000343957.

Chemistry

ChEMBLi CHEMBL2364170.
DrugBanki DB00034. Interferon Alfa-2a, Recombinant.
DB00105. Interferon Alfa-2b, Recombinant.
DB00011. Interferon alfa-n1.
DB00018. Interferon alfa-n3.
DB00069. Interferon alfacon-1.
DB00068. Interferon beta-1b.
DB00008. Peginterferon alfa-2a.
DB00022. Peginterferon alfa-2b.

PTM databases

PhosphoSitei P48551.

Polymorphism databases

DMDMi 1352466.

Proteomic databases

MaxQBi P48551.
PaxDbi P48551.
PRIDEi P48551.

Protocols and materials databases

DNASUi 3455.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000342101 ; ENSP00000343289 ; ENSG00000159110 . [P48551-3 ]
ENST00000342136 ; ENSP00000343957 ; ENSG00000159110 . [P48551-1 ]
ENST00000382241 ; ENSP00000371676 ; ENSG00000159110 . [P48551-1 ]
ENST00000382264 ; ENSP00000371699 ; ENSG00000159110 . [P48551-2 ]
ENST00000404220 ; ENSP00000384309 ; ENSG00000159110 . [P48551-2 ]
GeneIDi 3455.
KEGGi hsa:3455.
UCSCi uc002yrb.3. human. [P48551-2 ]
uc002yrd.3. human. [P48551-1 ]
uc002yrf.3. human. [P48551-3 ]

Organism-specific databases

CTDi 3455.
GeneCardsi GC21P034602.
HGNCi HGNC:5433. IFNAR2.
HPAi CAB025889.
MIMi 602376. gene.
610424. phenotype.
neXtProti NX_P48551.
PharmGKBi PA29671.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG41946.
HOGENOMi HOG000013219.
HOVERGENi HBG053907.
InParanoidi P48551.
KOi K05131.
OMAi IYIRLER.
PhylomeDBi P48551.
TreeFami TF335897.

Enzyme and pathway databases

Reactomei REACT_25162. Interferon alpha/beta signaling.
REACT_25216. Regulation of IFNA signaling.
SignaLinki P48551.

Miscellaneous databases

ChiTaRSi IFNAR2. human.
EvolutionaryTracei P48551.
GeneWikii IFNAR2.
GenomeRNAii 3455.
NextBioi 13610.
PMAP-CutDB Q6FHD7.
PROi P48551.
SOURCEi Search...

Gene expression databases

ArrayExpressi P48551.
Bgeei P48551.
CleanExi HS_IFNAR2.
Genevestigatori P48551.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
InterProi IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015373. Interferon_alpha/beta_rcpt_bsu.
[Graphical view ]
Pfami PF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The human interferon alpha/beta receptor: characterization and molecular cloning."
    Novick D., Cohen B., Rubinstein M.
    Cell 77:391-400(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-87 AND ASN-192, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT VAL-10.
    Tissue: Monocyte.
  2. "Mutant U5A cells are complemented by an interferon-alpha beta receptor subunit generated by alternative processing of a new member of a cytokine receptor gene cluster."
    Lutfalla G., Holland S.J., Cinato E., Monneron D., Reboul J., Rogers N.C., Smith J.M., Stark G.R., Gardiner K., Mogensen K.E., Kerr I.M., Uze G.
    EMBO J. 14:5100-5108(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY.
    Tissue: Lymphoblastoma.
  3. "Cloning and expression of a long form of the beta subunit of the interferon alpha beta receptor that is required for signaling."
    Domanski P., Witte M., Kellum M., Rubinstein M., Hackett R., Pitha P., Colamonici O.R.
    J. Biol. Chem. 270:21606-21611(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    Tissue: Myeloma.
  4. "Soluble and membrane-anchored forms of the human IFN-alpha/beta receptor."
    Novick D., Cohen B., Tal N., Rubinstein M.
    J. Leukoc. Biol. 57:712-718(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH JAK1, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION, VARIANT VAL-10.
    Tissue: Blood.
  5. Cohen B., Kim S.H., Novick D., Rubinstein M.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-10.
    Tissue: Blood.
  6. SeattleSNPs variation discovery resource
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-8; VAL-10 AND VAL-196.
  7. "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 1).
    Tissue: Uterus.
  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] (ISOFORM 2).
  9. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor and for signaling."
    Li X., Leung S., Kerr I.M., Stark G.R.
    Mol. Cell. Biol. 17:2048-2056(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STAT1 AND STAT2.
  12. "Formation of a uniquely stable type I interferon receptor complex by interferon beta is dependent upon particular interactions between interferon beta and its receptor and independent of tyrosine phosphorylation."
    Russell-Harde D., Wagner T.C., Perez H.D., Croze E.
    Biochem. Biophys. Res. Commun. 255:539-544(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IFNAR1.
  13. "Interferon signaling is dependent on specific tyrosines located within the intracellular domain of IFNAR2c. Expression of IFNAR2c tyrosine mutants in U5A cells."
    Wagner T.C., Velichko S., Vogel D., Rani M.R., Leung S., Ransohoff R.M., Stark G.R., Perez H.D., Croze E.
    J. Biol. Chem. 277:1493-1499(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT TYR-337 AND TYR-512, MUTAGENESIS OF TYR-269; TYR-306; TYR-316; TYR-318; TYR-337; TYR-411 AND TYR-512.
  14. "STAT3 activation by type I interferons is dependent on specific tyrosines located in the cytoplasmic domain of interferon receptor chain 2c. Activation of multiple STATS proceeds through the redundant usage of two tyrosine residues."
    Velichko S., Wagner T.C., Turkson J., Jove R., Croze E.
    J. Biol. Chem. 277:35635-35641(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT TYR-337 AND TYR-512, MUTAGENESIS OF TYR-269; TYR-306; TYR-316; TYR-318; TYR-337; TYR-411 AND TYR-512.
  15. "The human type I interferon receptor: NMR structure reveals the molecular basis of ligand binding."
    Chill J.H., Quadt S.R., Levy R., Schreiber G., Anglister J.
    Structure 11:791-802(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 28-237, DISULFIDE BONDS.
  16. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO HBV INFECTION, VARIANTS SER-8 AND VAL-10, CHARACTERIZATION OF VARIANT SER-8.
  17. "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 28-239 IN COMPLEX WITH IFNA2, DISULFIDE BONDS.
  18. "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 28-239 IN COMPLEX WITH IFNA2, DISULFIDE BONDS.
  19. "Structural linkage between ligand discrimination and receptor activation by type I interferons."
    Thomas C., Moraga I., Levin D., Krutzik P.O., Podoplelova Y., Trejo A., Lee C., Yarden G., Vleck S.E., Glenn J.S., Nolan G.P., Piehler J., Schreiber G., Garcia K.C.
    Cell 146:621-632(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 28-436 IN COMPLEX WITH IFNAR1 AND IFNW1, DISULFIDE BONDS.

Entry informationi

Entry nameiINAR2_HUMAN
AccessioniPrimary (citable) accession number: P48551
Secondary accession number(s): A8KAJ4
, D3DSE8, D3DSE9, Q15467, Q6FHD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 3, 2014
This is version 151 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, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: 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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