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Interferon regulatory factor 1 (IRF-1)

 IRF1_HUMAN              Reviewed;         325 AA.
P10914; Q96GG7;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
16-APR-2002, sequence version 2.
12-SEP-2018, entry version 174.
RecName: Full=Interferon regulatory factor 1;
Short=IRF-1;
Name=IRF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2726461; DOI=10.1093/nar/17.8.3292;
Maruyama M., Fujita T., Taniguchi T.;
"Sequence of a cDNA coding for human IRF-1.";
Nucleic Acids Res. 17:3292-3292(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3409321; DOI=10.1016/S0092-8674(88)91307-4;
Miyamoto M., Fujita T., Kimura Y., Maruyama M., Harada H., Sudo Y.,
Miyata T., Taniguchi T.;
"Regulated expression of a gene encoding a nuclear factor, IRF-1, that
specifically binds to IFN-beta gene regulatory elements.";
Cell 54:903-913(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=1382447; DOI=10.1089/dna.1992.11.605;
Cha Y., Sims S.H., Romine M.F., Kaufmann M., Deisseroth A.B.;
"Human interferon regulatory factor 1: intron-exon organization.";
DNA Cell Biol. 11:605-611(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
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]
INVOLVEMENT IN LEUKEMIAS.
PubMed=8438156; DOI=10.1126/science.8438156;
Willman C.L., Sever C.E., Pallavicini M.G., Harada H., Tanaka N.,
Slovak M.L., Yamamoto H., Harada K., Meeker T.C., List A.F.,
Taniguchi T.;
"Deletion of IRF-1, mapping to chromosome 5q31.1, in human leukemia
and preleukemic myelodysplasia.";
Science 259:968-971(1993).
[7]
PHOSPHORYLATION.
PubMed=10094406; DOI=10.1023/A:1006850009017;
Lin R., Hiscott J.;
"A role for casein kinase II phosphorylation in the regulation of IRF-
1 transcriptional activity.";
Mol. Cell. Biochem. 191:169-180(1999).
[8]
REVIEW ON FUNCTION.
PubMed=11244049; DOI=10.1146/annurev.immunol.19.1.623;
Taniguchi T., Ogasawara K., Takaoka A., Tanaka N.;
"IRF family of transcription factors as regulators of host defense.";
Annu. Rev. Immunol. 19:623-655(2001).
[9]
REVIEW ON FUNCTION.
PubMed=11846971; DOI=10.1089/107999002753452610;
Kroeger A., Koester M., Schroeder K., Hauser H., Mueller P.P.;
"Activities of IRF-1.";
J. Interferon Cytokine Res. 22:5-14(2002).
[10]
REVIEW ON FUNCTION.
PubMed=11846974; DOI=10.1089/107999002753452647;
Romeo G., Fiorucci G., Chiantore M.V., Percario Z.A., Vannucchi S.,
Affabris E.;
"IRF-1 as a negative regulator of cell proliferation.";
J. Interferon Cytokine Res. 22:39-47(2002).
[11]
FUNCTION.
PubMed=15226432; DOI=10.1128/MCB.24.14.6298-6310.2004;
Oshima S., Nakamura T., Namiki S., Okada E., Tsuchiya K., Okamoto R.,
Yamazaki M., Yokota T., Aida M., Yamaguchi Y., Kanai T., Handa H.,
Watanabe M.;
"Interferon regulatory factor 1 (IRF-1) and IRF-2 distinctively up-
regulate gene expression and production of interleukin-7 in human
intestinal epithelial cells.";
Mol. Cell. Biol. 24:6298-6310(2004).
[12]
FUNCTION, AND INTERACTION WITH EP300.
PubMed=15509808; DOI=10.1128/MCB.24.22.10083-10098.2004;
Dornan D., Eckert M., Wallace M., Shimizu H., Ramsay E., Hupp T.R.,
Ball K.L.;
"Interferon regulatory factor 1 binding to p300 stimulates DNA-
dependent acetylation of p53.";
Mol. Cell. Biol. 24:10083-10098(2004).
[13]
REVIEW ON FUNCTION.
PubMed=16932750; DOI=10.1038/nri1900;
Honda K., Taniguchi T.;
"IRFs: master regulators of signalling by Toll-like receptors and
cytosolic pattern-recognition receptors.";
Nat. Rev. Immunol. 6:644-658(2006).
[14]
FUNCTION.
PubMed=17516545; DOI=10.1002/jcp.21128;
Su Z.Z., Sarkar D., Emdad L., Barral P.M., Fisher P.B.;
"Central role of interferon regulatory factor-1 (IRF-1) in controlling
retinoic acid inducible gene-I (RIG-I) expression.";
J. Cell. Physiol. 213:502-510(2007).
[15]
FUNCTION.
PubMed=18084608; DOI=10.1593/neo.07640;
Maratheftis C.I., Giannouli S., Spachidou M.P., Panayotou G.,
Voulgarelis M.;
"RNA interference of interferon regulatory factor-1 gene expression in
THP-1 cell line leads to Toll-like receptor-4
overexpression/activation as well as up-modulation of annexin-II.";
Neoplasia 9:1012-1020(2007).
[16]
SUMOYLATION AT LYS-275 AND LYS-299, UBIQUITINATION AT LYS-275 AND
LYS-299, FUNCTION, AND MUTAGENESIS OF LYS-275 AND LYS-299.
PubMed=17942705; DOI=10.1073/pnas.0609852104;
Park J., Kim K., Lee E.-J., Seo Y.-J., Lim S.-N., Park K., Rho S.B.,
Lee S.-H., Lee J.-H.;
"Elevated level of SUMOylated IRF-1 in tumor cells interferes with
IRF-1-mediated apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 104:17028-17033(2007).
[17]
FUNCTION.
PubMed=18497060; DOI=10.1007/978-0-387-69080-3_35;
Bowie M.L., Ibarra C., Seewalt V.L.;
"IRF-1 promotes apoptosis in p53-damaged basal-type human mammary
epithelial cells: a model for early basal-type mammary
carcinogenesis.";
Adv. Exp. Med. Biol. 617:367-374(2008).
[18]
FUNCTION.
PubMed=18641303; DOI=10.4049/jimmunol.181.3.1673;
Fragale A., Gabriele L., Stellacci E., Borghi P., Perrotti E.,
Ilari R., Lanciotti A., Remoli A.L., Venditti M., Belardelli F.,
Battistini A.;
"IFN regulatory factor-1 negatively regulates CD4+ CD25+ regulatory T
cell differentiation by repressing Foxp3 expression.";
J. Immunol. 181:1673-1682(2008).
[19]
FUNCTION.
PubMed=19404407; DOI=10.1371/journal.pone.0005397;
Huang Y., Walstrom A., Zhang L., Zhao Y., Cui M., Ye L., Zheng J.C.;
"Type I interferons and interferon regulatory factors regulate TNF-
related apoptosis-inducing ligand (TRAIL) in HIV-1-infected
macrophages.";
PLoS ONE 4:E5397-E5397(2009).
[20]
REVIEW ON FUNCTION.
PubMed=20049431; DOI=10.1007/s00262-009-0804-6;
Savitsky D., Tamura T., Yanai H., Taniguchi T.;
"Regulation of immunity and oncogenesis by the IRF transcription
factor family.";
Cancer Immunol. Immunother. 59:489-510(2010).
[21]
FUNCTION.
PubMed=19851330; DOI=10.1038/cdd.2009.156;
Gao J., Senthil M., Ren B., Yan J., Xing Q., Yu J., Zhang L.,
Yim J.H.;
"IRF-1 transcriptionally upregulates PUMA, which mediates the
mitochondrial apoptotic pathway in IRF-1-induced apoptosis in cancer
cells.";
Cell Death Differ. 17:699-709(2010).
[22]
FUNCTION.
PubMed=21389130; DOI=10.1128/JVI.02114-10;
Muto V., Stellacci E., Lamberti A.G., Perrotti E., Carrabba A.,
Matera G., Sgarbanti M., Battistini A., Liberto M.C., Foca A.;
"Human papillomavirus type 16 E5 protein induces expression of beta
interferon through interferon regulatory factor 1 in human
keratinocytes.";
J. Virol. 85:5070-5080(2011).
[23]
FUNCTION.
PubMed=22200613; DOI=10.1016/j.canlet.2011.12.027;
Armstrong M.J., Stang M.T., Liu Y., Gao J., Ren B., Zuckerbraun B.S.,
Mahidhara R.S., Xing Q., Pizzoferrato E., Yim J.H.;
"Interferon regulatory factor 1 (IRF-1) induces p21(WAF1/CIP1)
dependent cell cycle arrest and p21(WAF1/CIP1) independent modulation
of survivin in cancer cells.";
Cancer Lett. 319:56-65(2012).
[24]
FUNCTION, ACETYLATION AT LYS-78, AND MUTAGENESIS OF LYS-78.
PubMed=22367195; DOI=10.1074/jbc.M111.313429;
Qi H., Zhu H., Lou M., Fan Y., Liu H., Shen J., Li Z., Lv X., Shan J.,
Zhu L., Chin Y.E., Shao J.;
"Interferon regulatory factor 1 transactivates the expression of human
DNA polymerase eta in response to the carcinogen N-methyl-N'-nitro-N-
nitrosoguanidine.";
J. Biol. Chem. 287:12622-12633(2012).
[25]
VARIANT GASC LEU-8, AND CHARACTERIZATION OF VARIANT GASC LEU-8.
PubMed=9679752;
DOI=10.1002/(SICI)1097-0215(19980812)77:4<522::AID-IJC8>3.0.CO;2-W;
Nozawa H., Oda E., Ueda S., Tamura G., Maesawa C., Muto T.,
Taniguchi T., Tanaka N.;
"Functionally inactivating point mutation in the tumor-suppressor IRF-
1 gene identified in human gastric cancer.";
Int. J. Cancer 77:522-527(1998).
[26]
VARIANT GASC ARG-11.
PubMed=10395927; DOI=10.1016/S0167-4781(99)00078-0;
Eason D.D., Shepherd A.T., Blanck G.;
"Interferon regulatory factor 1 tryptophan 11 to arginine point
mutation abolishes DNA binding.";
Biochim. Biophys. Acta 1446:140-144(1999).
-!- FUNCTION: Transcriptional regulator which displays a remarkable
functional diversity in the regulation of cellular responses.
These include the regulation of IFN and IFN-inducible genes, host
response to viral and bacterial infections, regulation of many
genes expressed during hematopoiesis, inflammation, immune
responses and cell proliferation and differentiation, regulation
of the cell cycle and induction of growth arrest and programmed
cell death following DNA damage. Stimulates both innate and
acquired immune responses through the activation of specific
target genes and can act as a transcriptional activator and
repressor regulating target genes by binding to an interferon-
stimulated response element (ISRE) in their promoters. Its target
genes for transcriptional activation activity include: genes
involved in anti-viral response, such as IFN-alpha/beta,
DDX58/RIG-I, TNFSF10/TRAIL, OAS1/2, PIAS1/GBP, EIF2AK2/PKR and
RSAD2/viperin; antibacterial response, such as NOS2/INOS; anti-
proliferative response, such as p53/TP53, LOX and CDKN1A;
apoptosis, such as BBC3/PUMA, CASP1, CASP7 and CASP8; immune
response, such as IL7, IL12A/B and IL15, PTGS2/COX2 and CYBB; DNA
damage responses and DNA repair, such as POLQ/POLH; MHC class I
expression, such as TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B and
B2M and MHC class II expression, such as CIITA. Represses genes
involved in anti-proliferative response, such as BIRC5/survivin,
CCNB1, CCNE1, CDK1, CDK2 and CDK4 and in immune response, such as
FOXP3, IL4, ANXA2 and TLR4. Stimulates p53/TP53-dependent
transcription through enhanced recruitment of EP300 leading to
increased acetylation of p53/TP53. Plays an important role in
immune response directly affecting NK maturation and activity,
macrophage production of IL12, Th1 development and maturation of
CD8+ T-cells. Also implicated in the differentiation and
maturation of dendritic cells and in the suppression of regulatory
T (Treg) cells development. Acts as a tumor suppressor and plays a
role not only in antagonism of tumor cell growth but also in
stimulating an immune response against tumor cells.
{ECO:0000269|PubMed:15226432, ECO:0000269|PubMed:15509808,
ECO:0000269|PubMed:17516545, ECO:0000269|PubMed:17942705,
ECO:0000269|PubMed:18084608, ECO:0000269|PubMed:18497060,
ECO:0000269|PubMed:18641303, ECO:0000269|PubMed:19404407,
ECO:0000269|PubMed:19851330, ECO:0000269|PubMed:21389130,
ECO:0000269|PubMed:22200613, ECO:0000269|PubMed:22367195}.
-!- ACTIVITY REGULATION: Activated by MYD88. {ECO:0000250}.
-!- SUBUNIT: Monomer. Homodimer. Interacts with MYD88 and PIAS3 (By
similarity). Interacts with EP300. {ECO:0000250,
ECO:0000269|PubMed:15509808}.
-!- INTERACTION:
P03129:E7 (xeno); NbExp=3; IntAct=EBI-1055781, EBI-866453;
P63165:SUMO1; NbExp=2; IntAct=EBI-1055781, EBI-80140;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=MYD88-associated
IRF1 migrates into the nucleus more efficiently than non-MYD88-
associated IRF1.
-!- INDUCTION: By viruses and interferon (IFN).
-!- PTM: Phosphorylated by CK2 and this positively regulates its
activity. {ECO:0000269|PubMed:10094406}.
-!- PTM: Sumoylation represses the transcriptional activity and
displays enhanced resistance to protein degradation. Inactivates
the tumor suppressor activity. Elevated levels in tumor cells.
Major site is Lys-275. Sumoylation is enhanced by PIAS3 (By
similarity). Desumoylated by SENP1 in tumor cells and appears to
compete with ubiquitination on C-terminal sites. {ECO:0000250,
ECO:0000269|PubMed:17942705}.
-!- PTM: Ubiquitinated. Appears to compete with sumoylation on C-
terminal sites. {ECO:0000269|PubMed:17942705}.
-!- DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease
which starts in the stomach, can spread to the esophagus or the
small intestine, and can extend through the stomach wall to nearby
lymph nodes and organs. It also can metastasize to other parts of
the body. The term gastric cancer or gastric carcinoma refers to
adenocarcinoma of the stomach that accounts for most of all
gastric malignant tumors. Two main histologic types are
recognized, diffuse type and intestinal type carcinomas. Diffuse
tumors are poorly differentiated infiltrating lesions, resulting
in thickening of the stomach. In contrast, intestinal tumors are
usually exophytic, often ulcerating, and associated with
intestinal metaplasia of the stomach, most often observed in
sporadic disease. {ECO:0000269|PubMed:10395927,
ECO:0000269|PubMed:9679752}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- MISCELLANEOUS: Deletion or rearrangement of IRF1 are found in
preleukemic myelodysplastic syndrome (MDS) and acute myelogenous
leukemia (AML).
-!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
ProRule:PRU00840}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/IRF1ID40990ch5q23.html";
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EMBL; X14454; CAA32624.1; -; mRNA.
EMBL; L05072; AAA36043.1; -; Genomic_DNA.
EMBL; BT019756; AAV38561.1; -; mRNA.
EMBL; BC009483; AAH09483.1; -; mRNA.
CCDS; CCDS4155.1; -.
PIR; B31595; B31595.
PIR; I52998; I52998.
RefSeq; NP_002189.1; NM_002198.2.
UniGene; Hs.436061; -.
ProteinModelPortal; P10914; -.
BioGrid; 109867; 34.
DIP; DIP-40988N; -.
IntAct; P10914; 5.
MINT; P10914; -.
STRING; 9606.ENSP00000245414; -.
iPTMnet; P10914; -.
PhosphoSitePlus; P10914; -.
BioMuta; IRF1; -.
DMDM; 20178295; -.
EPD; P10914; -.
PaxDb; P10914; -.
PeptideAtlas; P10914; -.
PRIDE; P10914; -.
ProteomicsDB; 52676; -.
DNASU; 3659; -.
Ensembl; ENST00000245414; ENSP00000245414; ENSG00000125347.
Ensembl; ENST00000405885; ENSP00000384406; ENSG00000125347.
GeneID; 3659; -.
KEGG; hsa:3659; -.
CTD; 3659; -.
DisGeNET; 3659; -.
EuPathDB; HostDB:ENSG00000125347.13; -.
GeneCards; IRF1; -.
H-InvDB; HIX0200727; -.
HGNC; HGNC:6116; IRF1.
HPA; CAB011662; -.
HPA; HPA063131; -.
MalaCards; IRF1; -.
MIM; 147575; gene.
MIM; 613659; phenotype.
neXtProt; NX_P10914; -.
OpenTargets; ENSG00000125347; -.
PharmGKB; PA29915; -.
eggNOG; ENOG410IER3; Eukaryota.
eggNOG; ENOG4111HM7; LUCA.
GeneTree; ENSGT00760000119093; -.
HOGENOM; HOG000037937; -.
HOVERGEN; HBG003455; -.
InParanoid; P10914; -.
KO; K09444; -.
OMA; CKEEPEV; -.
OrthoDB; EOG091G0CB8; -.
PhylomeDB; P10914; -.
TreeFam; TF328512; -.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; P10914; -.
SIGNOR; P10914; -.
ChiTaRS; IRF1; human.
GeneWiki; IRF1; -.
GenomeRNAi; 3659; -.
PRO; PR:P10914; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000125347; Expressed in 206 organ(s), highest expression level in blood.
CleanEx; HS_IRF1; -.
ExpressionAtlas; P10914; baseline and differential.
Genevisible; P10914; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; TAS:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IMP:NTNU_SB.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0043374; P:CD8-positive, alpha-beta T cell differentiation; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; IDA:UniProtKB.
GO; GO:0035458; P:cellular response to interferon-beta; IDA:BHF-UCL.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:UniProtKB.
GO; GO:0045590; P:negative regulation of regulatory T cell differentiation; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:UniProtKB.
GO; GO:0045084; P:positive regulation of interleukin-12 biosynthetic process; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032481; P:positive regulation of type I interferon production; ISS:UniProtKB.
GO; GO:0002819; P:regulation of adaptive immune response; TAS:UniProtKB.
GO; GO:2000564; P:regulation of CD8-positive, alpha-beta T cell proliferation; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; TAS:UniProtKB.
GO; GO:0045088; P:regulation of innate immune response; TAS:UniProtKB.
GO; GO:0034124; P:regulation of MyD88-dependent toll-like receptor signaling pathway; ISS:UniProtKB.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
CDD; cd00103; IRF; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR019817; Interferon_reg_fac_CS.
InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom.
InterPro; IPR031215; IRF1.
InterPro; IPR017431; IRF1/IRF2.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR11949; PTHR11949; 1.
PANTHER; PTHR11949:SF3; PTHR11949:SF3; 1.
Pfam; PF00605; IRF; 1.
PIRSF; PIRSF038196; IFN_RF1/2; 1.
PRINTS; PR00267; INTFRNREGFCT.
SMART; SM00348; IRF; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS00601; IRF_1; 1.
PROSITE; PS51507; IRF_2; 1.
1: Evidence at protein level;
Acetylation; Activator; Antiviral defense; Complete proteome;
Cytoplasm; Disease mutation; DNA-binding; Immunity; Innate immunity;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
Repressor; Transcription; Transcription regulation; Tumor suppressor;
Ubl conjugation.
CHAIN 1 325 Interferon regulatory factor 1.
/FTId=PRO_0000154545.
DNA_BIND 5 113 IRF tryptophan pentad repeat.
{ECO:0000255|PROSITE-ProRule:PRU00840}.
MOD_RES 78 78 N6-acetyllysine.
{ECO:0000269|PubMed:22367195}.
CROSSLNK 275 275 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
CROSSLNK 299 299 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
VARIANT 8 8 M -> L (in GASC; somatic mutation;
produces a protein with markedly reduced
transcriptional activity but unaltered
DNA-binding activity; dbSNP:rs121912469).
{ECO:0000269|PubMed:9679752}.
/FTId=VAR_065134.
VARIANT 11 11 W -> R (in GASC; the mutation abolishes
DNA binding and transactivating
activities; dbSNP:rs121912470).
{ECO:0000269|PubMed:10395927}.
/FTId=VAR_065135.
MUTAGEN 78 78 K->R: Loss of acetylation. Partial loss
of DNA-binding and transcriptional
activity. {ECO:0000269|PubMed:22367195}.
MUTAGEN 275 275 K->R: Some loss of sumoylation. Partial
inhibition of acetylation and activity.
Abolishes sumoylation, diminished
ubiquitination, higher resistance to
degradation, and increased apoptotic
activity; when associated with R-299.
{ECO:0000269|PubMed:17942705}.
MUTAGEN 299 299 K->R: Large loss of sumoylation.
Abolishes sumoylation, diminished
ubiquitination, higher resistance to
degradation, and increased apoptotic
activity; when associated with R-275.
{ECO:0000269|PubMed:17942705}.
CONFLICT 5 5 R -> W (in Ref. 1; no nucleotide entry
and 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 34 35 FQ -> LE (in Ref. 1; no nucleotide entry
and 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 220 220 T -> I (in Ref. 1; no nucleotide entry
and 2; no nucleotide entry).
{ECO:0000305}.
SEQUENCE 325 AA; 36502 MW; 2E06245A212D1541 CRC64;
MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKH AAKHGWDINK DACLFRSWAI
HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPPLTKNQR
KERKSKSSRD AKSKAKRKSC GDSSPDTFSD GLSSSTLPDD HSSYTVPGYM QDLEVEQALT
PALSPCAVSS TLPDWHIPVE VVPDSTSDLY NFQVSPMPST SEATTDEDEE GKLPEDIMKL
LEQSEWQPTN VDGKGYLLNE PGVQPTSVYG DFSCKEEPEI DSPGGDIGLS LQRVFTDLKN
MDATWLDSLL TPVRLPSIQA IPCAP


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