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IL27B_HUMAN
ID   IL27B_HUMAN             Reviewed;         229 AA.
AC   Q14213; A0N0N2; O75269;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   03-AUG-2022, entry version 178.
DE   RecName: Full=Interleukin-27 subunit beta;
DE            Short=IL-27 subunit beta;
DE            Short=IL-27B;
DE   AltName: Full=Epstein-Barr virus-induced gene 3 protein;
DE            Short=EBV-induced gene 3 protein;
DE   Flags: Precursor;
GN   Name=EBI3; Synonyms=IL27B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, GLYCOSYLATION, AND INTERACTION WITH
RP   SQSTM1.
RC   TISSUE=B-cell;
RX   PubMed=8551575; DOI=10.1128/jvi.70.2.1143-1153.1996;
RA   Devergne O., Hummel M., Koeppen H., Le Beau M.M., Nathanson E.C., Kieff E.,
RA   Birkenbach M.;
RT   "A novel interleukin-12 p40-related protein induced by latent Epstein-Barr
RT   virus infection in B lymphocytes.";
RL   J. Virol. 70:1143-1153(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-201.
RA   Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
RA   Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
RA   Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
RA   Nickerson D.A.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-201.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=9342359; DOI=10.1073/pnas.94.22.12041;
RA   Devergne O., Birkenbach M., Kieff E.;
RT   "Epstein-Barr virus-induced gene 3 and the p35 subunit of interleukin 12
RT   form a novel heterodimeric hematopoietin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:12041-12046(1997).
RN   [7]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=12121660; DOI=10.1016/s1074-7613(02)00324-2;
RA   Pflanz S., Timans J.C., Cheung J., Rosales R., Kanzler H., Gilbert J.,
RA   Hibbert L., Churakova T., Travis M., Vaisberg E., Blumenschein W.M.,
RA   Mattson J.D., Wagner J.L., To W., Zurawski S., McClanahan T.K.,
RA   Gorman D.M., Bazan J.F., de Waal Malefyt R., Rennick D., Kastelein R.A.;
RT   "IL-27, a heterodimeric cytokine composed of EBI3 and p28 protein, induces
RT   proliferation of naive CD4(+) T cells.";
RL   Immunity 16:779-790(2002).
RN   [8]
RP   REVIEW ON IL-27.
RX   PubMed=17294231; DOI=10.1007/s00109-007-0164-7;
RA   Batten M., Ghilardi N.;
RT   "The biology and therapeutic potential of interleukin 27.";
RL   J. Mol. Med. 85:661-672(2007).
CC   -!- FUNCTION: Associates with IL27 to form the IL-27 interleukin, a
CC       heterodimeric cytokine which functions in innate immunity. IL-27 has
CC       pro- and anti-inflammatory properties, that can regulate T-helper cell
CC       development, suppress T-cell proliferation, stimulate cytotoxic T-cell
CC       activity, induce isotype switching in B-cells, and that has diverse
CC       effects on innate immune cells. Among its target cells are CD4 T-helper
CC       cells which can differentiate in type 1 effector cells (TH1), type 2
CC       effector cells (TH2) and IL17 producing helper T-cells (TH17). It
CC       drives rapid clonal expansion of naive but not memory CD4 T-cells. It
CC       also strongly synergizes with IL-12 to trigger interferon-gamma/IFN-
CC       gamma production of naive CD4 T-cells, binds to the cytokine receptor
CC       WSX-1/TCCR. Another important role of IL-27 is its antitumor activity
CC       as well as its antiangiogenic activity with activation of production of
CC       antiangiogenic chemokines. {ECO:0000269|PubMed:12121660}.
CC   -!- SUBUNIT: Heterodimer with IL27/IL27A; not disulfide-linked
CC       (PubMed:12121660). This heterodimer is known as interleukin IL-27
CC       (PubMed:12121660). Heterodimer with IL12A; not disulfide-linked
CC       (PubMed:9342359). This heterodimer is known as interleukin IL-35
CC       (PubMed:9342359). Interacts with SQSTM1 (PubMed:8551575).
CC       {ECO:0000269|PubMed:12121660, ECO:0000269|PubMed:8551575,
CC       ECO:0000269|PubMed:9342359}.
CC   -!- INTERACTION:
CC       Q14213; Q8NEV9: IL27; NbExp=2; IntAct=EBI-742959, EBI-15887997;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9342359}.
CC   -!- INDUCTION: By Epstein-Barr virus (EBV). {ECO:0000269|PubMed:8551575}.
CC   -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 3
CC       subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-27 entry;
CC       URL="https://en.wikipedia.org/wiki/Interleukin_27";
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DR   EMBL; L08187; AAA93193.1; -; mRNA.
DR   EMBL; EF064740; ABK41923.1; -; Genomic_DNA.
DR   EMBL; AC005578; AAC33488.1; -; Genomic_DNA.
DR   EMBL; CH471139; EAW69245.1; -; Genomic_DNA.
DR   EMBL; BC015364; AAH15364.1; -; mRNA.
DR   EMBL; BC046112; AAH46112.1; -; mRNA.
DR   CCDS; CCDS12123.1; -.
DR   RefSeq; NP_005746.2; NM_005755.2.
DR   RefSeq; XP_011525921.1; XM_011527619.2.
DR   AlphaFoldDB; Q14213; -.
DR   SMR; Q14213; -.
DR   BioGRID; 115450; 36.
DR   DIP; DIP-57556N; -.
DR   IntAct; Q14213; 8.
DR   MINT; Q14213; -.
DR   STRING; 9606.ENSP00000221847; -.
DR   GlyGen; Q14213; 2 sites.
DR   BioMuta; EBI3; -.
DR   DMDM; 47605806; -.
DR   MassIVE; Q14213; -.
DR   MaxQB; Q14213; -.
DR   PaxDb; Q14213; -.
DR   PeptideAtlas; Q14213; -.
DR   PRIDE; Q14213; -.
DR   ProteomicsDB; 59933; -.
DR   Antibodypedia; 23527; 1092 antibodies from 39 providers.
DR   DNASU; 10148; -.
DR   Ensembl; ENST00000221847.6; ENSP00000221847.4; ENSG00000105246.6.
DR   GeneID; 10148; -.
DR   KEGG; hsa:10148; -.
DR   MANE-Select; ENST00000221847.6; ENSP00000221847.4; NM_005755.3; NP_005746.2.
DR   UCSC; uc002lzu.4; human.
DR   CTD; 10148; -.
DR   DisGeNET; 10148; -.
DR   GeneCards; EBI3; -.
DR   HGNC; HGNC:3129; EBI3.
DR   HPA; ENSG00000105246; Tissue enriched (placenta).
DR   MIM; 605816; gene.
DR   neXtProt; NX_Q14213; -.
DR   OpenTargets; ENSG00000105246; -.
DR   PharmGKB; PA27584; -.
DR   VEuPathDB; HostDB:ENSG00000105246; -.
DR   eggNOG; ENOG502RXJ4; Eukaryota.
DR   GeneTree; ENSGT00940000160050; -.
DR   HOGENOM; CLU_047259_2_0_1; -.
DR   InParanoid; Q14213; -.
DR   OMA; TSCTIAD; -.
DR   OrthoDB; 857138at2759; -.
DR   PhylomeDB; Q14213; -.
DR   TreeFam; TF331210; -.
DR   PathwayCommons; Q14213; -.
DR   Reactome; R-HSA-8984722; Interleukin-35 Signalling.
DR   Reactome; R-HSA-9020956; Interleukin-27 signaling.
DR   SignaLink; Q14213; -.
DR   BioGRID-ORCS; 10148; 25 hits in 1068 CRISPR screens.
DR   ChiTaRS; EBI3; human.
DR   GeneWiki; EBI3; -.
DR   GenomeRNAi; 10148; -.
DR   Pharos; Q14213; Tbio.
DR   PRO; PR:Q14213; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q14213; protein.
DR   Bgee; ENSG00000105246; Expressed in placenta and 101 other tissues.
DR   Genevisible; Q14213; HS.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR   GO; GO:0004896; F:cytokine receptor activity; IPI:UniProtKB.
DR   GO; GO:0045523; F:interleukin-27 receptor binding; IEA:Ensembl.
DR   GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
DR   GO; GO:0033210; P:leptin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; TAS:UniProtKB.
DR   GO; GO:0032729; P:positive regulation of interferon-gamma production; TAS:UniProtKB.
DR   GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR   GO; GO:0042088; P:T-helper 1 type immune response; TAS:UniProtKB.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR003530; Hematopoietin_rcpt_L_F3_CS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF00041; fn3; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS01354; HEMATOPO_REC_L_F3; 1.
PE   1: Evidence at protein level;
KW   Cytokine; Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..229
FT                   /note="Interleukin-27 subunit beta"
FT                   /id="PRO_0000010937"
FT   DOMAIN          24..130
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          131..227
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         174
FT                   /note="A -> V (in dbSNP:rs1803524)"
FT                   /id="VAR_049171"
FT   VARIANT         201
FT                   /note="V -> I (in dbSNP:rs4740)"
FT                   /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.4"
FT                   /id="VAR_024342"
FT   CONFLICT        144..145
FT                   /note="QL -> HV (in Ref. 1; AAA93193)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   229 AA;  25396 MW;  CFBAD72D91859EF0 CRC64;
     MTPQLLLALV LWASCPPCSG RKGPPAALTL PRVQCRASRY PIAVDCSWTL PPAPNSTSPV
     SFIATYRLGM AARGHSWPCL QQTPTSTSCT ITDVQLFSMA PYVLNVTAVH PWGSSSSFVP
     FITEHIIKPD PPEGVRLSPL AERQLQVQWE PPGSWPFPEI FSLKYWIRYK RQGAARFHRV
     GPIEATSFIL RAVRPRARYY VQVAAQDLTD YGELSDWSLP ATATMSLGK
 
 
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