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Gamma-interferon-inducible protein 16 (Ifi-16) (Interferon-inducible myeloid differentiation transcriptional activator)

 IF16_HUMAN              Reviewed;         785 AA.
Q16666; B4DJT8; H3BLV7; Q59GX0; Q5T3W7; Q5T3W8; Q5T3X0; Q5T3X1;
Q5T3X2; Q8N9E5; Q8NEQ7; Q96AJ5; Q9UH78;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
28-NOV-2006, sequence version 3.
22-NOV-2017, entry version 188.
RecName: Full=Gamma-interferon-inducible protein 16;
Short=Ifi-16;
AltName: Full=Interferon-inducible myeloid differentiation transcriptional activator;
Name=IFI16; Synonyms=IFNGIP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT HIS-103.
TISSUE=T-cell;
PubMed=1526658; DOI=10.1007/BF00218044;
Trapani J.A., Browne K.A., Dawson M.J., Ramsay R.G., Eddy R.L.,
Show T.B., White P.C., Dupont B.;
"A novel gene constitutively expressed in human lymphoid cells is
inducible with interferon-gamma in myeloid cells.";
Immunogenetics 36:369-376(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND VARIANT HIS-103.
PubMed=7959953; DOI=10.1007/BF00177824;
Trapani J.A., Dawson M.J., Apostolidis V.A., Browne K.A.;
"Genomic organization of IFI16, an interferon-inducible gene whose
expression is associated with human myeloid cell differentiation:
correlation of predicted protein domains with exon organization.";
Immunogenetics 40:415-424(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT HIS-103.
TISSUE=Bone marrow;
Jiang C., Zhang D., Peng Y., Zhang X., Han Z., Fu G., Chen Z.;
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
INDUCTION, AND VARIANTS THR-179; SER-409 AND ASN-413.
PubMed=12894224; DOI=10.1038/sj.onc.1206754;
Xin H., Curry J., Johnstone R.W., Nickoloff B.J., Choubey D.;
"Role of IFI 16, a member of the interferon-inducible p200-protein
family, in prostate epithelial cellular senescence.";
Oncogene 22:4831-4840(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS
THR-179; SER-409 AND ASN-413.
TISSUE=Hippocampus, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
SER-409 AND ASN-413.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
THR-179; SER-409 AND ASN-413.
TISSUE=Uterus;
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).
[9]
ALTERNATIVE SPLICING, SUBUNIT, PHOSPHORYLATION, AND GLYCOSYLATION.
PubMed=9718316; DOI=10.1021/bi981069a;
Johnstone R.W., Kershaw M.H., Trapani J.A.;
"Isotypic variants of the interferon-inducible transcriptional
repressor IFI 16 arise through differential mRNA splicing.";
Biochemistry 37:11924-11931(1998).
[10]
INDUCTION, SUBCELLULAR LOCATION, AND DNA-BINDING.
PubMed=7536752; DOI=10.1002/jcb.240570106;
Dawson M.J., Trapani J.A.;
"IFI 16 gene encodes a nuclear protein whose expression is induced by
interferons in human myeloid leukaemia cell lines.";
J. Cell. Biochem. 57:39-51(1995).
[11]
TISSUE-SPECIFIC INDUCTION.
PubMed=7806273; DOI=10.1007/BF00188431;
Dawson M.J., Trapani J.A., Briggs R.C., Nicholl J.K., Sutherland G.R.,
Baker E.;
"The closely linked genes encoding the myeloid nuclear differentiation
antigen (MNDA) and IFI16 exhibit contrasting haemopoietic
expression.";
Immunogenetics 41:40-43(1995).
[12]
TISSUE SPECIFIC INDUCTION.
PubMed=9766636;
Dawson M.J., Elwood N.J., Johnstone R.W., Trapani J.A.;
"The IFN-inducible nucleoprotein IFI 16 is expressed in cells of the
monocyte lineage, but is rapidly and markedly down-regulated in other
myeloid precursor populations.";
J. Leukoc. Biol. 64:546-554(1998).
[13]
FUNCTION.
PubMed=9642285; DOI=10.1074/jbc.273.27.17172;
Johnstone R.W., Kerry J.A., Trapani J.A.;
"The human interferon-inducible protein, IFI 16, is a repressor of
transcription.";
J. Biol. Chem. 273:17172-17177(1998).
[14]
FUNCTION, AND INTERACTION WITH TP53.
PubMed=11146555; DOI=10.1038/sj.onc.1204005;
Johnstone R.W., Wei W., Greenway A., Trapani J.A.;
"Functional interaction between p53 and the interferon-inducible
nucleoprotein IFI 16.";
Oncogene 19:6033-6042(2000).
[15]
FUNCTION, AND INTERACTION WITH BRCA1.
PubMed=14654789; DOI=10.1038/sj.onc.1207057;
Aglipay J.A., Lee S.W., Okada S., Fujiuchi N., Ohtsuka T., Kwak J.C.,
Wang Y., Johnstone R.W., Deng C., Qin J., Ouchi T.;
"A member of the Pyrin family, IFI16, is a novel BRCA1-associated
protein involved in the p53-mediated apoptosis pathway.";
Oncogene 22:8931-8938(2003).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-153, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-153, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-214, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[20]
SUMOYLATION AT LYS-561.
TISSUE=Cervix carcinoma;
PubMed=20388717; DOI=10.1074/jbc.M110.106955;
Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,
Eriksson J.E., Sistonen L.;
"In vivo identification of sumoylation sites by a signature tag and
cysteine-targeted affinity purification.";
J. Biol. Chem. 285:19324-19329(2010).
[21]
FUNCTION, DNA-BINDING, INTERACTION WITH TMEM173, AND INDUCTION.
PubMed=20890285; DOI=10.1038/ni.1932;
Unterholzner L., Keating S.E., Baran M., Horan K.A., Jensen S.B.,
Sharma S., Sirois C.M., Jin T., Latz E., Xiao T.S., Fitzgerald K.A.,
Paludan S.R., Bowie A.G.;
"IFI16 is an innate immune sensor for intracellular DNA.";
Nat. Immunol. 11:997-1004(2010).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-153 AND
SER-575, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
FUNCTION, AND INTERACTION WITH PYCARD AND CASP1.
PubMed=21575908; DOI=10.1016/j.chom.2011.04.008;
Kerur N., Veettil M.V., Sharma-Walia N., Bottero V., Sadagopan S.,
Otageri P., Chandran B.;
"IFI16 acts as a nuclear pathogen sensor to induce the inflammasome in
response to Kaposi Sarcoma-associated herpesvirus infection.";
Cell Host Microbe 9:363-375(2011).
[25]
FUNCTION, AND INDUCTION.
PubMed=21573174; DOI=10.1371/journal.pone.0019532;
Duan X., Ponomareva L., Veeranki S., Choubey D.;
"IFI16 induction by glucose restriction in human fibroblasts
contributes to autophagy through activation of the ATM/AMPK/p53
pathway.";
PLoS ONE 6:E19532-E19532(2011).
[26]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AIM2.
PubMed=22046441; DOI=10.1371/journal.pone.0027040;
Veeranki S., Duan X., Panchanathan R., Liu H., Choubey D.;
"IFI16 protein mediates the anti-inflammatory actions of the type-I
interferons through suppression of activation of caspase-1 by
inflammasomes.";
PLoS ONE 6:E27040-E27040(2011).
[27]
DNA-BINDING.
PubMed=22618232; DOI=10.1016/j.bbrc.2012.05.065;
Brazda V., Coufal J., Liao J.C., Arrowsmith C.H.;
"Preferential binding of IFI16 protein to cruciform structure and
superhelical DNA.";
Biochem. Biophys. Res. Commun. 422:716-720(2012).
[28]
FUNCTION, AND INTERACTION WITH SP1.
PubMed=22291595; DOI=10.1371/journal.ppat.1002498;
Gariano G.R., Dell'Oste V., Bronzini M., Gatti D., Luganini A.,
De Andrea M., Gribaudo G., Gariglio M., Landolfo S.;
"The intracellular DNA sensor IFI16 gene acts as restriction factor
for human cytomegalovirus replication.";
PLoS Pathog. 8:E1002498-E1002498(2012).
[29]
FUNCTION, SUBCELLULAR LOCATION, AND PROTEASOMAL DEGRADATION.
PubMed=23027953; DOI=10.1073/pnas.1211302109;
Orzalli M.H., DeLuca N.A., Knipe D.M.;
"Nuclear IFI16 induction of IRF-3 signaling during herpesviral
infection and degradation of IFI16 by the viral ICP0 protein.";
Proc. Natl. Acad. Sci. U.S.A. 109:E3008-E3017(2012).
[30]
SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
PHOSPHORYLATION AT SER-106; SER-153; SER-168; SER-174 AND SER-780,
ACETYLATION AT LYS-45; LYS-99; LYS-128; LYS-214; LYS-444; LYS-451;
LYS-561; LYS-598 AND LYS-614, AND MUTAGENESIS OF 96-ARG--LYS-100;
LYS-99; LYS-128; 128-LYS--LYS-131; 134-LYS--LYS-136 AND
140-LYS--LYS-143.
PubMed=22691496; DOI=10.1073/pnas.1203447109;
Li T., Diner B.A., Chen J., Cristea I.M.;
"Acetylation modulates cellular distribution and DNA sensing ability
of interferon-inducible protein IFI16.";
Proc. Natl. Acad. Sci. U.S.A. 109:10558-10563(2012).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-153, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[32]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24198334; DOI=10.1073/pnas.1316194110;
Orzalli M.H., Conwell S.E., Berrios C., DeCaprio J.A., Knipe D.M.;
"Nuclear interferon-inducible protein 16 promotes silencing of
herpesviral and transfected DNA.";
Proc. Natl. Acad. Sci. U.S.A. 110:E4492-E4501(2013).
[33]
FUNCTION, INTERACTION WITH MTA1, AND SUBCELLULAR LOCATION.
PubMed=24413532; DOI=10.1158/0008-5472.CAN-13-2020;
Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y.,
Kim Y.N., Seong J.K., Lee M.O.;
"Differential regulation of estrogen receptor alpha expression in
breast cancer cells by metastasis-associated protein 1.";
Cancer Res. 74:1484-1494(2014).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-153, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[35]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116 AND LYS-561, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[36]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-561, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[37]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-561 AND LYS-683, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116; LYS-128; LYS-561 AND
LYS-683, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[39]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 192-393, AND MUTAGENESIS OF
TYR-218; GLU-222; TYR-267 AND GLU-272.
PubMed=21397192; DOI=10.1016/j.str.2010.12.015;
Liao J.C., Lam R., Brazda V., Duan S., Ravichandran M., Ma J.,
Xiao T., Tempel W., Zuo X., Wang Y.X., Chirgadze N.Y.,
Arrowsmith C.H.;
"Interferon-inducible protein 16: insight into the interaction with
tumor suppressor p53.";
Structure 19:418-429(2011).
[40]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 571-766 IN COMPLEX WITH
DOUBLE-STRANDED DNA, AND MUTAGENESIS OF LYS-627; LYS-663; ARG-667;
SER-670; LYS-674; LYS-732; LYS-734 AND LYS-759.
PubMed=22483801; DOI=10.1016/j.immuni.2012.02.014;
Jin T., Perry A., Jiang J., Smith P., Curry J.A., Unterholzner L.,
Jiang Z., Horvath G., Rathinam V.A., Johnstone R.W., Hornung V.,
Latz E., Bowie A.G., Fitzgerald K.A., Xiao T.S.;
"Structures of the HIN domain:DNA complexes reveal ligand binding and
activation mechanisms of the AIM2 inflammasome and IFI16 receptor.";
Immunity 36:561-571(2012).
[41]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 192-393.
Northeast structural genomics consortium (NESG);
"Crystal structure of the first HIN-200 domain of interferon-inducible
protein 16.";
Submitted (FEB-2007) to the PDB data bank.
[42]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 571-766.
Northeast structural genomics consortium (NESG);
"Crystal structure analysis of the second HIN domain of IFI16.";
Submitted (NOV-2007) to the PDB data bank.
-!- FUNCTION: Binds double-stranded DNA. Binds preferentially to
supercoiled DNA and cruciform DNA structures. Seems to be involved
in transcriptional regulation. May function as a transcriptional
repressor. Could have a role in the regulation of hematopoietic
differentiation through activation of unknown target genes.
Controls cellular proliferation by modulating the functions of
cell cycle regulatory factors including p53/TP53 and the
retinoblastoma protein. May be involved in TP53-mediated
transcriptional activation by enhancing TP53 sequence-specific DNA
binding and modulating TP53 phosphorylation status. Seems to be
involved in energy-level-dependent activation of the ATM/
AMPK/TP53 pathway coupled to regulation of autophagy. May be
involved in regulation of TP53-mediated cell death also involving
BRCA1. May be involved in the senescence of prostate epithelial
cells. Involved in innate immune response by recognizing viral
dsDNA in the cytosol and probably in the nucleus. After binding to
viral DNA in the cytoplasm recruits TMEM173/STING and mediates the
induction of IFN-beta. Has anti-inflammatory activity and inhibits
the activation of the AIM2 inflammasome, probably via association
with AIM2. Proposed to bind viral DNA in the nucleus, such as of
Kaposi's sarcoma-associated herpesvirus, and to induce the
formation of nuclear caspase-1-activating inflammasome formation
via association with PYCARD. Inhibits replication of herpesviruses
such as human cytomegalovirus (HCMV) probably by interfering with
promoter recruitment of members of the Sp1 family of transcription
factors. Necessary to activate the IRF3 signaling cascade during
human herpes simplex virus 1 (HHV-1) infection and promotes the
assembly of heterochromatin on herpesviral DNA and inhibition of
viral immediate-early gene expression and replication. Involved in
the MTA1-mediated epigenetic regulation of ESR1 expression in
breast cancer. {ECO:0000269|PubMed:11146555,
ECO:0000269|PubMed:12894224, ECO:0000269|PubMed:14654789,
ECO:0000269|PubMed:20890285, ECO:0000269|PubMed:21573174,
ECO:0000269|PubMed:21575908, ECO:0000269|PubMed:22046441,
ECO:0000269|PubMed:22291595, ECO:0000269|PubMed:23027953,
ECO:0000269|PubMed:24198334, ECO:0000269|PubMed:24413532,
ECO:0000269|PubMed:9642285}.
-!- SUBUNIT: Forms homooligomers; isoform 2 can self-associate or
associate with isoform 1 or isoform 3. Interacts with TMEM173,
AIM2, PYCARD and CASP1. Interacts with BRCA1, TP53, E2F1, RB1 and
SP1. Interacts with MTA1. {ECO:0000269|PubMed:11146555,
ECO:0000269|PubMed:14654789, ECO:0000269|PubMed:20890285,
ECO:0000269|PubMed:21575908, ECO:0000269|PubMed:22046441,
ECO:0000269|PubMed:22291595, ECO:0000269|PubMed:22483801,
ECO:0000269|PubMed:24413532, ECO:0000269|PubMed:9718316}.
-!- INTERACTION:
P10275:AR; NbExp=3; IntAct=EBI-2867186, EBI-608057;
P38398:BRCA1; NbExp=9; IntAct=EBI-2867186, EBI-349905;
Q86WV6:TMEM173; NbExp=2; IntAct=EBI-2867186, EBI-2800345;
P04637:TP53; NbExp=6; IntAct=EBI-6273540, EBI-366083;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cellular
distribution is dependent on the acetylation status of the
multipartite nuclear localization signal (NLS); NLS acetylation
promotes cytoplasmic localization. Localizes in the nucleus during
human herpes simplex virus 1 (HHV-1) infection.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=IFI 16A;
IsoId=Q16666-1; Sequence=Displayed;
Name=2; Synonyms=IFI 16B;
IsoId=Q16666-2; Sequence=VSP_002676;
Note=Major isoform.;
Name=3; Synonyms=IFI 16C;
IsoId=Q16666-3; Sequence=VSP_002675;
Name=4;
IsoId=Q16666-6; Sequence=VSP_044691;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes,
fibroblasts and lymphoid cells. Present in myeloid precursors
(CD34+) and throughout monocyte development, but its expression is
down-regulated in erythroid and polymorphonuclear precursor cells.
Present in prostate, ovary and breast (at protein level).
{ECO:0000269|PubMed:12894224}.
-!- INDUCTION: Strongly induced by IFNG/IFN-gamma and, to a lesser
extent, by alpha interferon. In HL-60 cells, maximum induction by
IFNG/IFN-gamma occurs within 12 hours whereas, for IFN-alpha, only
10-fold induction was observed after 36 hours. Induced in vitro by
dimethylsulfoxide, retinoic acid and 1,25 dihydroxyvitamin D3.
Induced in monocytes by IFN-alpha and viral dsDNA. Induced by
glucose restriction. {ECO:0000269|PubMed:12894224,
ECO:0000269|PubMed:20890285, ECO:0000269|PubMed:21573174,
ECO:0000269|PubMed:7536752}.
-!- DOMAIN: The HIN-20 domains mediates dsDNA binding via
electrostatic interactions. {ECO:0000269|PubMed:22483801}.
-!- PTM: Ubiquitinated by human herpes simplex virus 1 (HHV-1) ICP0
protein; leading to degradation by the proteasome.
-!- PTM: Lysine acetylation in the multipartite nuclear localization
signal (NLS) regulates the subcellular location. In vitro can be
acetylated by p300/EP300 coupled to cytoplasmic localization.
{ECO:0000269|PubMed:22691496}.
-!- PTM: Phosphorylated on Ser and Thr. {ECO:0000269|PubMed:22691496,
ECO:0000269|PubMed:9718316}.
-!- PTM: Isoform 3 seems to show a minor degree of complex
carbohydrate addition.
-!- SIMILARITY: Belongs to the HIN-200 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF20997.1; Type=Frameshift; Positions=776; Evidence={ECO:0000305};
Sequence=AAF20997.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=BAC04462.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
Sequence=BAD92226.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAG58950.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M63838; AAA58683.1; -; mRNA.
EMBL; S75433; AAB32519.2; -; Genomic_DNA.
EMBL; S75417; AAB32519.2; JOINED; Genomic_DNA.
EMBL; S75419; AAB32519.2; JOINED; Genomic_DNA.
EMBL; S75421; AAB32519.2; JOINED; Genomic_DNA.
EMBL; S75423; AAB32519.2; JOINED; Genomic_DNA.
EMBL; S75424; AAB32519.2; JOINED; Genomic_DNA.
EMBL; S75426; AAB32519.2; JOINED; Genomic_DNA.
EMBL; S75429; AAB32519.2; JOINED; Genomic_DNA.
EMBL; S75431; AAB32519.2; JOINED; Genomic_DNA.
EMBL; AF208043; AAF20997.1; ALT_SEQ; mRNA.
EMBL; AY138863; AAM96005.1; -; mRNA.
EMBL; AK094968; BAC04462.1; ALT_SEQ; mRNA.
EMBL; AK296228; BAG58950.1; ALT_INIT; mRNA.
EMBL; AB208989; BAD92226.1; ALT_INIT; mRNA.
EMBL; AL359753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC017059; AAH17059.1; -; mRNA.
CCDS; CCDS1180.3; -. [Q16666-2]
CCDS; CCDS58039.1; -. [Q16666-6]
PIR; I54501; I54501.
RefSeq; NP_001193496.1; NM_001206567.1. [Q16666-6]
RefSeq; NP_005522.2; NM_005531.2. [Q16666-2]
UniGene; Hs.380250; -.
PDB; 2OQ0; X-ray; 2.00 A; A/B/C/D=192-393.
PDB; 3B6Y; X-ray; 2.35 A; A/B=571-766.
PDB; 3RLN; X-ray; 2.25 A; A=571-766.
PDB; 3RLO; X-ray; 1.80 A; A=571-766.
PDB; 3RNU; X-ray; 2.50 A; A/B/C/D=571-766.
PDB; 4QGU; X-ray; 2.54 A; A/B=192-393.
PDBsum; 2OQ0; -.
PDBsum; 3B6Y; -.
PDBsum; 3RLN; -.
PDBsum; 3RLO; -.
PDBsum; 3RNU; -.
PDBsum; 4QGU; -.
ProteinModelPortal; Q16666; -.
SMR; Q16666; -.
BioGrid; 109654; 394.
DIP; DIP-42868N; -.
IntAct; Q16666; 173.
MINT; MINT-1781545; -.
STRING; 9606.ENSP00000357113; -.
iPTMnet; Q16666; -.
PhosphoSitePlus; Q16666; -.
SwissPalm; Q16666; -.
BioMuta; IFI16; -.
DMDM; 118572657; -.
EPD; Q16666; -.
MaxQB; Q16666; -.
PaxDb; Q16666; -.
PeptideAtlas; Q16666; -.
PRIDE; Q16666; -.
DNASU; 3428; -.
Ensembl; ENST00000295809; ENSP00000295809; ENSG00000163565. [Q16666-1]
Ensembl; ENST00000359709; ENSP00000352740; ENSG00000163565. [Q16666-6]
Ensembl; ENST00000368131; ENSP00000357113; ENSG00000163565. [Q16666-2]
Ensembl; ENST00000368132; ENSP00000357114; ENSG00000163565. [Q16666-2]
Ensembl; ENST00000448393; ENSP00000404325; ENSG00000163565. [Q16666-3]
GeneID; 3428; -.
KEGG; hsa:3428; -.
UCSC; uc001ftg.4; human. [Q16666-1]
CTD; 3428; -.
DisGeNET; 3428; -.
EuPathDB; HostDB:ENSG00000163565.18; -.
GeneCards; IFI16; -.
H-InvDB; HIX0001194; -.
HGNC; HGNC:5395; IFI16.
HPA; CAB016293; -.
HPA; HPA002134; -.
MIM; 147586; gene.
neXtProt; NX_Q16666; -.
OpenTargets; ENSG00000163565; -.
PharmGKB; PA29642; -.
eggNOG; ENOG410J5NP; Eukaryota.
eggNOG; ENOG410Y78B; LUCA.
GeneTree; ENSGT00390000013296; -.
HOGENOM; HOG000033871; -.
HOVERGEN; HBG006122; -.
InParanoid; Q16666; -.
KO; K20914; -.
OMA; RKKNQMS; -.
OrthoDB; EOG091G02W0; -.
PhylomeDB; Q16666; -.
TreeFam; TF337385; -.
Reactome; R-HSA-1834941; STING mediated induction of host immune responses.
Reactome; R-HSA-3270619; IRF3-mediated induction of type I IFN.
SIGNOR; Q16666; -.
ChiTaRS; IFI16; human.
EvolutionaryTrace; Q16666; -.
GeneWiki; IFI16; -.
GenomeRNAi; 3428; -.
PRO; PR:Q16666; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000163565; -.
ExpressionAtlas; Q16666; baseline and differential.
Genevisible; Q16666; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:MGI.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
GO; GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0030097; P:hemopoiesis; NAS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:MGI.
GO; GO:0030224; P:monocyte differentiation; IDA:UniProtKB.
GO; GO:0030099; P:myeloid cell differentiation; NAS:UniProtKB.
GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
GO; GO:0045824; P:negative regulation of innate immune response; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0001819; P:positive regulation of cytokine production; TAS:UniProtKB.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
GO; GO:0010506; P:regulation of autophagy; IEP:UniProtKB.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR004020; DAPIN.
InterPro; IPR004021; HIN200/IF120x.
Pfam; PF02760; HIN; 2.
Pfam; PF02758; PYRIN; 1.
SMART; SM01289; PYRIN; 1.
PROSITE; PS50824; DAPIN; 1.
PROSITE; PS50834; HIN_200; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing; Apoptosis;
Autophagy; Complete proteome; Cytoplasm; DNA-binding; Immunity;
Inflammatory response; Innate immunity; Isopeptide bond; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 785 Gamma-interferon-inducible protein 16.
/FTId=PRO_0000153723.
DOMAIN 1 88 Pyrin. {ECO:0000255|PROSITE-
ProRule:PRU00061}.
DOMAIN 189 389 HIN-200 1. {ECO:0000255|PROSITE-
ProRule:PRU00106}.
DOMAIN 562 761 HIN-200 2. {ECO:0000255|PROSITE-
ProRule:PRU00106}.
REGION 192 393 Interaction with TP53 C-terminus.
REGION 571 766 Interaction with TP53 core domain.
MOTIF 96 100 Nuclear localization signal.
MOTIF 128 131 Nuclear localization signal.
MOTIF 134 136 Nuclear localization signal.
MOTIF 140 143 Nuclear localization signal.
COMPBIAS 1 150 Lys-rich.
COMPBIAS 258 261 Poly-Ile.
MOD_RES 45 45 N6-acetyllysine.
{ECO:0000269|PubMed:22691496}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000269|PubMed:9718316}.
MOD_RES 99 99 N6-acetyllysine.
{ECO:0000269|PubMed:22691496}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:22691496}.
MOD_RES 128 128 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:22691496}.
MOD_RES 153 153 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:22691496}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000269|PubMed:22691496}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000269|PubMed:22691496}.
MOD_RES 214 214 N6-acetyllysine.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:22691496}.
MOD_RES 444 444 N6-acetyllysine.
{ECO:0000269|PubMed:22691496}.
MOD_RES 451 451 N6-acetyllysine.
{ECO:0000269|PubMed:22691496}.
MOD_RES 561 561 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:22691496}.
MOD_RES 575 575 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 598 598 N6-acetyllysine.
{ECO:0000269|PubMed:22691496}.
MOD_RES 614 614 N6-acetyllysine.
{ECO:0000269|PubMed:22691496}.
MOD_RES 780 780 Phosphoserine.
{ECO:0000269|PubMed:22691496}.
CROSSLNK 116 116 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 128 128 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 561 561 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 561 561 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 683 683 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 128 183 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044691.
VAR_SEQ 444 555 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_002675.
VAR_SEQ 444 499 Missing (in isoform 2).
{ECO:0000303|PubMed:12894224,
ECO:0000303|PubMed:1526658,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.3, ECO:0000303|Ref.6}.
/FTId=VSP_002676.
VARIANT 103 103 D -> H (in dbSNP:rs1057018).
{ECO:0000269|PubMed:1526658,
ECO:0000269|PubMed:7959953,
ECO:0000269|Ref.3}.
/FTId=VAR_029486.
VARIANT 179 179 S -> T (in dbSNP:rs866484).
{ECO:0000269|PubMed:12894224,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_029487.
VARIANT 202 202 K -> E (in dbSNP:rs11585341).
/FTId=VAR_029488.
VARIANT 409 409 R -> S (in dbSNP:rs1057027).
{ECO:0000269|PubMed:12894224,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.6}.
/FTId=VAR_029489.
VARIANT 413 413 Y -> N (in dbSNP:rs1057028).
{ECO:0000269|PubMed:12894224,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.6}.
/FTId=VAR_029490.
VARIANT 723 723 T -> S (in dbSNP:rs6940).
/FTId=VAR_029491.
VARIANT 779 779 T -> S (in dbSNP:rs6940).
/FTId=VAR_057582.
MUTAGEN 96 100 Missing: Predominant cytoplasmic
localization.
{ECO:0000269|PubMed:22691496}.
MUTAGEN 99 99 K->Q: Predominant cytoplasmic, reduces
nuclear localization (mimics non-
acetylated state).
{ECO:0000269|PubMed:22691496}.
MUTAGEN 99 99 K->R: Minor effect on nuclear
localization (mimics acetylated state).
{ECO:0000269|PubMed:22691496}.
MUTAGEN 128 131 Missing: Predominant nuclear, some
cytoplasmic localization.
{ECO:0000269|PubMed:22691496}.
MUTAGEN 128 128 K->Q: Predominant cytoplasmic, reduces
nuclear localization (mimics non-
acetylated state).
{ECO:0000269|PubMed:22691496}.
MUTAGEN 128 128 K->R: Minor effect on nuclear
localization (mimics acetylated state).
{ECO:0000269|PubMed:22691496}.
MUTAGEN 134 136 Missing: Mostly nuclear, minor
cytoplasmic localization.
{ECO:0000269|PubMed:22691496}.
MUTAGEN 140 143 Missing: Mostly nuclear, minor
cytoplasmic localization.
{ECO:0000269|PubMed:22691496}.
MUTAGEN 218 218 Y->A: Abolishes TP53-mediated
transcriptional activation; when
associated with A-267.
{ECO:0000269|PubMed:21397192}.
MUTAGEN 222 222 E->A: Abolishes TP53-mediated
transcriptional activation; when
associated with A-272.
{ECO:0000269|PubMed:21397192}.
MUTAGEN 267 267 Y->A: Abolishes TP53-mediated
transcriptional activation; when
associated with A-218.
{ECO:0000269|PubMed:21397192}.
MUTAGEN 272 272 E->A: Abolishes TP53-mediated
transcriptional activation; when
associated with A-222.
{ECO:0000269|PubMed:21397192}.
MUTAGEN 627 627 K->A: Impairs DNA binding; when
associated with A-663; A-667; A-670; A-
674; A-732; A-734 and A-759.
{ECO:0000269|PubMed:22483801}.
MUTAGEN 663 663 K->A: Impairs DNA binding; when
associated with A-627; A-667; A-670; A-
674; A-732; A-734 and A-759.
{ECO:0000269|PubMed:22483801}.
MUTAGEN 667 667 R->A: Impairs DNA binding; when
associated with A-627; A-663; A-670; A-
674; A-732; A-734 and A-759.
{ECO:0000269|PubMed:22483801}.
MUTAGEN 670 670 S->A: Impairs DNA binding; when
associated with A-627; A-663; A-667; A-
674; A-732; A-734 and A-759.
{ECO:0000269|PubMed:22483801}.
MUTAGEN 674 674 K->A: Impairs DNA binding; when
associated with A-627; A-663; A-667; A-
670; A-732; A-734 and A-759.
{ECO:0000269|PubMed:22483801}.
MUTAGEN 732 732 K->A: Impairs DNA binding; when
associated with A-627; A-663; A-667; A-
670; A- 674; A-734 and A-759.
{ECO:0000269|PubMed:22483801}.
MUTAGEN 734 734 K->A: Impairs DNA binding; when
associated with A-627; A-663; A-667; A-
670; A- 674; A-732 and A-759.
{ECO:0000269|PubMed:22483801}.
MUTAGEN 759 759 K->A: Impairs DNA binding; when
associated with A-627; A-663; A-667; A-
670; A- 674; A-732 and A-734.
{ECO:0000269|PubMed:22483801}.
CONFLICT 401 401 S -> G (in Ref. 5; BAG58950).
{ECO:0000305}.
CONFLICT 544 544 P -> S (in Ref. 5; BAG58950).
{ECO:0000305}.
CONFLICT 683 683 K -> R (in Ref. 4; AAM96005).
{ECO:0000305}.
CONFLICT 723 723 T -> N (in Ref. 1; AAA58683 and 2;
AAB32519). {ECO:0000305}.
CONFLICT 737 737 C -> S (in Ref. 1; AAA58683 and 2;
AAB32519). {ECO:0000305}.
STRAND 205 212 {ECO:0000244|PDB:2OQ0}.
STRAND 216 219 {ECO:0000244|PDB:2OQ0}.
STRAND 225 234 {ECO:0000244|PDB:2OQ0}.
STRAND 239 244 {ECO:0000244|PDB:2OQ0}.
HELIX 247 253 {ECO:0000244|PDB:2OQ0}.
STRAND 254 257 {ECO:0000244|PDB:2OQ0}.
STRAND 259 267 {ECO:0000244|PDB:2OQ0}.
STRAND 270 273 {ECO:0000244|PDB:2OQ0}.
STRAND 278 281 {ECO:0000244|PDB:2OQ0}.
HELIX 284 286 {ECO:0000244|PDB:2OQ0}.
HELIX 292 298 {ECO:0000244|PDB:2OQ0}.
HELIX 304 307 {ECO:0000244|PDB:2OQ0}.
STRAND 315 327 {ECO:0000244|PDB:2OQ0}.
STRAND 329 338 {ECO:0000244|PDB:2OQ0}.
STRAND 341 348 {ECO:0000244|PDB:2OQ0}.
HELIX 349 351 {ECO:0000244|PDB:2OQ0}.
STRAND 361 372 {ECO:0000244|PDB:2OQ0}.
STRAND 375 379 {ECO:0000244|PDB:2OQ0}.
STRAND 385 388 {ECO:0000244|PDB:2OQ0}.
STRAND 578 585 {ECO:0000244|PDB:3RLO}.
STRAND 589 592 {ECO:0000244|PDB:3RLO}.
TURN 593 596 {ECO:0000244|PDB:3RLO}.
STRAND 597 605 {ECO:0000244|PDB:3RLO}.
STRAND 610 615 {ECO:0000244|PDB:3RLO}.
HELIX 618 620 {ECO:0000244|PDB:3RLO}.
TURN 621 624 {ECO:0000244|PDB:3RLO}.
STRAND 629 634 {ECO:0000244|PDB:3RLO}.
STRAND 636 638 {ECO:0000244|PDB:3RLO}.
STRAND 641 644 {ECO:0000244|PDB:3RLO}.
STRAND 648 652 {ECO:0000244|PDB:3RLO}.
STRAND 655 657 {ECO:0000244|PDB:3RLO}.
HELIX 663 670 {ECO:0000244|PDB:3RLO}.
HELIX 675 679 {ECO:0000244|PDB:3RLO}.
STRAND 685 699 {ECO:0000244|PDB:3RLO}.
STRAND 702 709 {ECO:0000244|PDB:3RLO}.
STRAND 712 718 {ECO:0000244|PDB:3RLO}.
HELIX 720 724 {ECO:0000244|PDB:3RLO}.
STRAND 732 741 {ECO:0000244|PDB:3RLO}.
TURN 744 747 {ECO:0000244|PDB:3RLO}.
STRAND 749 761 {ECO:0000244|PDB:3RLO}.
TURN 764 766 {ECO:0000244|PDB:3RLO}.
SEQUENCE 785 AA; 88256 MW; 216CD103D8F5206A CRC64;
MGKKYKNIVL LKGLEVINDY HFRMVKSLLS NDLKLNLKMR EEYDKIQIAD LMEEKFRGDA
GLGKLIKIFE DIPTLEDLAE TLKKEKLKVK GPALSRKRKK EVDATSPAPS TSSTVKTEGA
EATPGAQKRK KSTKEKAGPK GSKVSEEQTQ PPSPAGAGMS TAMGRSPSPK TSLSAPPNSS
STENPKTVAK CQVTPRRNVL QKRPVIVKVL STTKPFEYET PEMEKKIMFH ATVATQTQFF
HVKVLNTSLK EKFNGKKIII ISDYLEYDSL LEVNEESTVS EAGPNQTFEV PNKIINRAKE
TLKIDILHKQ ASGNIVYGVF MLHKKTVNQK TTIYEIQDDR GKMDVVGTGQ CHNIPCEEGD
KLQLFCFRLR KKNQMSKLIS EMHSFIQIKK KTNPRNNDPK SMKLPQEQRQ LPYPSEASTT
FPESHLRTPQ MPPTTPSSSF FTKKSEDTIS KMNDFMRMQI LKEGSHFPGP FMTSIGPAES
HPHTPQMPPS TPSSSFLTTK SEDTISKMND FMRMQILKEG SHFPGPFMTS IGPAESHPHT
PQMPPSTPSS SFLTTLKPRL KTEPEEVSIE DSAQSDLKEV MVLNATESFV YEPKEQKKMF
HATVATENEV FRVKVFNIDL KEKFTPKKII AIANYVCRNG FLEVYPFTLV ADVNADRNME
IPKGLIRSAS VTPKINQLCS QTKGSFVNGV FEVHKKNVRG EFTYYEIQDN TGKMEVVVHG
RLTTINCEEG DKLKLTCFEL APKSGNTGEL RSVIHSHIKV IKTRKNKKDI LNPDSSMETS
PDFFF


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