IL24_HUMAN
ID IL24_HUMAN Reviewed; 206 AA.
AC Q13007; Q2YHE5; Q53XZ7; Q5YLN8; Q96DB0; Q96KG4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Interleukin-24;
DE Short=IL-24;
DE AltName: Full=Melanoma differentiation-associated gene 7 protein;
DE Short=MDA-7;
DE AltName: Full=Suppression of tumorigenicity 16 protein;
DE Flags: Precursor;
GN Name=IL24; Synonyms=MDA7, ST16;
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] (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=8545104;
RA Jiang H., Lin J.J., Su Z.-Z., Goldstein N.I., Fisher P.B.;
RT "Subtraction hybridization identifies a novel melanoma differentiation
RT associated gene, mda-7, modulated during human melanoma differentiation,
RT growth and progression.";
RL Oncogene 11:2477-2486(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Peat J., Kube D., Eskdale J., Jueliger S., Gallagher G.;
RT "The human MDA-7 gene.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-124.
RC TISSUE=Fibroblast;
RX PubMed=11704829; DOI=10.1038/sj.onc.1204897;
RA Huang E.Y., Madireddi M.T., Gopalkrishnan R.V., Leszczyniecka M., Su Z.-Z.,
RA Lebedeva I.V., Kang D., Jiang H., Lin J.J., Alexandre D., Chen Y.,
RA Vozhilla N., Mei M.X., Christiansen K.A., Sivo F., Goldstein N.I.,
RA Mhashilkar A.B., Chada S., Huberman E., Pestka S., Fisher P.B.;
RT "Genomic structure, chromosomal localization and expression profile of a
RT novel melanoma differentiation associated (mda-7) gene with cancer specific
RT growth suppressing and apoptosis inducing properties.";
RL Oncogene 20:7051-7063(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=15304100; DOI=10.1111/j.0022-202x.2004.23321.x;
RA Allen M., Pratscher B., Roka F., Krepler C., Wacheck V., Schofer C.,
RA Pehamberger H., Muller M., Lucas T.;
RT "Loss of novel mda-7 splice variant (mda-7s) expression is associated with
RT metastatic melanoma.";
RL J. Invest. Dermatol. 123:583-588(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-124; ARG-125 AND
RP LEU-131.
RG SeattleSNPs variation discovery resource;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
RX PubMed=16313301; DOI=10.1111/j.1744-313x.2005.00540.x;
RA Allen M., Pratscher B., Krepler C., Frei K., Schofer C., Pehamberger H.,
RA Muller M., Lucas T.;
RT "Alternative splicing of IL-24 in melanocytes by deletion of exons 3 and
RT 5.";
RL Int. J. Immunogenet. 32:375-378(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [10]
RP PROTEIN SEQUENCE OF 52-66.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [11]
RP CHARACTERIZATION.
RX PubMed=9826712; DOI=10.1073/pnas.95.24.14400;
RA Su Z.-Z., Madireddi M.T., Lin J.J., Young C.S.H., Kitada S., Reed J.C.,
RA Goldstein N.I., Fisher P.B.;
RT "The cancer growth suppressor gene mda-7 selectively induces apoptosis in
RT human breast cancer cells and inhibits tumor growth in nude mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:14400-14405(1998).
RN [12]
RP UBIQUITINATION AT LYS-122.
RX PubMed=23078624; DOI=10.1089/jir.2012.0055;
RA Tian H., Li L., Zhang B., Di J., Chen F., Li H., Liu J., Pei D., Zheng J.;
RT "Critical role of lysine 123 in the ubiquitin-mediated degradation of MDA-
RT 7/IL-24.";
RL J. Interferon Cytokine Res. 32:575-582(2012).
CC -!- FUNCTION: Has antiproliferative properties on melanoma cells and may
CC contribute to terminal cell differentiation.
CC -!- INTERACTION:
CC Q13007; Q13315: ATM; NbExp=2; IntAct=EBI-3915542, EBI-495465;
CC Q13007; O96017: CHEK2; NbExp=3; IntAct=EBI-3915542, EBI-1180783;
CC Q13007; P09874: PARP1; NbExp=2; IntAct=EBI-3915542, EBI-355676;
CC Q13007; Q06609: RAD51; NbExp=2; IntAct=EBI-3915542, EBI-297202;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q13007-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13007-2; Sequence=VSP_042673;
CC Name=3;
CC IsoId=Q13007-3; Sequence=VSP_042673, VSP_042674;
CC Name=4; Synonyms=mda-7s;
CC IsoId=Q13007-4; Sequence=VSP_043915;
CC -!- TISSUE SPECIFICITY: Up-regulated in melanoma cells induced to
CC terminally differentiate.
CC -!- PTM: Ubiquitination at Lys-122 promotes proteasomal degradation.
CC {ECO:0000269|PubMed:23078624}.
CC -!- SIMILARITY: Belongs to the IL-10 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-24 entry;
CC URL="https://en.wikipedia.org/wiki/Interleukin_24";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il24/";
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DR EMBL; U16261; AAA91780.1; -; mRNA.
DR EMBL; AF276916; AAG41401.1; -; Genomic_DNA.
DR EMBL; AF235005; AAK52589.1; -; Genomic_DNA.
DR EMBL; AY237723; AAO67513.1; -; mRNA.
DR EMBL; AY062931; AAL34146.1; -; Genomic_DNA.
DR EMBL; AY641441; AAV52801.1; -; mRNA.
DR EMBL; BT007156; AAP35820.1; -; mRNA.
DR EMBL; AC098935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009681; AAH09681.1; -; mRNA.
DR CCDS; CCDS1471.1; -. [Q13007-1]
DR CCDS; CCDS53465.1; -. [Q13007-2]
DR CCDS; CCDS53466.1; -. [Q13007-3]
DR CCDS; CCDS73021.1; -. [Q13007-4]
DR RefSeq; NP_001172085.1; NM_001185156.1. [Q13007-2]
DR RefSeq; NP_001172086.1; NM_001185157.1. [Q13007-3]
DR RefSeq; NP_001172087.1; NM_001185158.1. [Q13007-4]
DR RefSeq; NP_006841.1; NM_006850.3. [Q13007-1]
DR PDB; 6DF3; X-ray; 2.15 A; C=52-206.
DR PDB; 6GG1; X-ray; 1.30 A; A=54-206.
DR PDBsum; 6DF3; -.
DR PDBsum; 6GG1; -.
DR AlphaFoldDB; Q13007; -.
DR SMR; Q13007; -.
DR BioGRID; 116199; 31.
DR IntAct; Q13007; 25.
DR MINT; Q13007; -.
DR STRING; 9606.ENSP00000375795; -.
DR GlyGen; Q13007; 3 sites.
DR iPTMnet; Q13007; -.
DR PhosphoSitePlus; Q13007; -.
DR BioMuta; IL24; -.
DR DMDM; 2497340; -.
DR MassIVE; Q13007; -.
DR PaxDb; Q13007; -.
DR PeptideAtlas; Q13007; -.
DR PRIDE; Q13007; -.
DR ProteomicsDB; 59095; -. [Q13007-1]
DR ProteomicsDB; 59096; -. [Q13007-2]
DR ProteomicsDB; 59097; -. [Q13007-3]
DR Antibodypedia; 1466; 489 antibodies from 30 providers.
DR DNASU; 11009; -.
DR Ensembl; ENST00000294984.7; ENSP00000294984.2; ENSG00000162892.16. [Q13007-1]
DR Ensembl; ENST00000367093.3; ENSP00000356060.3; ENSG00000162892.16. [Q13007-3]
DR Ensembl; ENST00000391929.7; ENSP00000375795.3; ENSG00000162892.16. [Q13007-2]
DR Ensembl; ENST00000611909.4; ENSP00000484900.1; ENSG00000162892.16. [Q13007-4]
DR GeneID; 11009; -.
DR KEGG; hsa:11009; -.
DR MANE-Select; ENST00000294984.7; ENSP00000294984.2; NM_006850.3; NP_006841.1.
DR UCSC; uc001hes.3; human. [Q13007-1]
DR CTD; 11009; -.
DR DisGeNET; 11009; -.
DR GeneCards; IL24; -.
DR HGNC; HGNC:11346; IL24.
DR HPA; ENSG00000162892; Group enriched (intestine, lymphoid tissue, urinary bladder).
DR MIM; 604136; gene.
DR neXtProt; NX_Q13007; -.
DR OpenTargets; ENSG00000162892; -.
DR PharmGKB; PA29825; -.
DR VEuPathDB; HostDB:ENSG00000162892; -.
DR eggNOG; ENOG502SUXZ; Eukaryota.
DR GeneTree; ENSGT00950000183124; -.
DR HOGENOM; CLU_098690_0_0_1; -.
DR InParanoid; Q13007; -.
DR OMA; WMGKFYR; -.
DR OrthoDB; 1434107at2759; -.
DR PhylomeDB; Q13007; -.
DR TreeFam; TF333253; -.
DR PathwayCommons; Q13007; -.
DR Reactome; R-HSA-8854691; Interleukin-20 family signaling.
DR SignaLink; Q13007; -.
DR BioGRID-ORCS; 11009; 11 hits in 1068 CRISPR screens.
DR GeneWiki; Interleukin_24; -.
DR GenomeRNAi; 11009; -.
DR Pharos; Q13007; Tbio.
DR PRO; PR:Q13007; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13007; protein.
DR Bgee; ENSG00000162892; Expressed in buccal mucosa cell and 89 other tissues.
DR ExpressionAtlas; Q13007; baseline and differential.
DR Genevisible; Q13007; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:0042501; P:serine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR020423; IL-10_CS.
DR InterPro; IPR020444; IL-24.
DR PRINTS; PR01937; INTRLEUKIN24.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00520; INTERLEUKIN_10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytokine;
KW Direct protein sequencing; Glycoprotein; Isopeptide bond;
KW Reference proteome; Secreted; Signal; Ubl conjugation.
FT SIGNAL 1..51
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 52..206
FT /note="Interleukin-24"
FT /id="PRO_0000015386"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23078624"
FT VAR_SEQ 14
FT /note="A -> AS (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16313301, ECO:0000303|Ref.7"
FT /id="VSP_042673"
FT VAR_SEQ 15..206
FT /note="RPFCPPLLATASQMQMVVLPCLGFTLLLWSQVSGAQGQEFHFGPCQVKGVVP
FT QKLWEAFWAVKDTMQAQDNITSARLLQQEVLQNVSDAESCYLVHTLLEFYLKTVFKNYH
FT NRTVEVRTLKSFSTLANNFVLIVSQLQPSQENEMFSIRDSAHRRFLLFRRAFKQLDVEA
FT ALTKALGEVDILLTWMQKFYKL -> SKLRITSRVPGCCSRRFCRTSRKKMRCFPSETV
FT HTGGFCYSGEHSNSWT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15304100"
FT /id="VSP_043915"
FT VAR_SEQ 101..153
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16313301"
FT /id="VSP_042674"
FT VARIANT 124
FT /note="Y -> H (in dbSNP:rs1150258)"
FT /evidence="ECO:0000269|PubMed:11704829, ECO:0000269|Ref.5"
FT /id="VAR_011974"
FT VARIANT 125
FT /note="H -> R (in dbSNP:rs3093431)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_013097"
FT VARIANT 131
FT /note="V -> L (in dbSNP:rs3093446)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_013098"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6GG1"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:6GG1"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:6GG1"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:6GG1"
FT HELIX 102..118
FT /evidence="ECO:0007829|PDB:6GG1"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:6GG1"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:6GG1"
FT HELIX 131..156
FT /evidence="ECO:0007829|PDB:6GG1"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:6DF3"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:6GG1"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:6GG1"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:6GG1"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:6GG1"
SQ SEQUENCE 206 AA; 23825 MW; CB8135083EAB8DDD CRC64;
MNFQQRLQSL WTLARPFCPP LLATASQMQM VVLPCLGFTL LLWSQVSGAQ GQEFHFGPCQ
VKGVVPQKLW EAFWAVKDTM QAQDNITSAR LLQQEVLQNV SDAESCYLVH TLLEFYLKTV
FKNYHNRTVE VRTLKSFSTL ANNFVLIVSQ LQPSQENEMF SIRDSAHRRF LLFRRAFKQL
DVEAALTKAL GEVDILLTWM QKFYKL
