IF16_HUMAN
ID IF16_HUMAN Reviewed; 785 AA.
AC Q16666; B4DJT8; H3BLV7; Q59GX0; Q5T3W7; Q5T3W8; Q5T3X0; Q5T3X1; Q5T3X2;
AC Q8N9E5; Q8NEQ7; Q96AJ5; Q9UH78;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 3.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Gamma-interferon-inducible protein 16;
DE Short=Ifi-16;
DE AltName: Full=Interferon-inducible myeloid differentiation transcriptional activator;
GN Name=IFI16; Synonyms=IFNGIP1;
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 2), AND VARIANT HIS-103.
RC TISSUE=T-cell;
RX PubMed=1526658; DOI=10.1007/bf00218044;
RA Trapani J.A., Browne K.A., Dawson M.J., Ramsay R.G., Eddy R.L., Show T.B.,
RA White P.C., Dupont B.;
RT "A novel gene constitutively expressed in human lymphoid cells is inducible
RT with interferon-gamma in myeloid cells.";
RL Immunogenetics 36:369-376(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND VARIANT HIS-103.
RX PubMed=7959953; DOI=10.1007/bf00177824;
RA Trapani J.A., Dawson M.J., Apostolidis V.A., Browne K.A.;
RT "Genomic organization of IFI16, an interferon-inducible gene whose
RT expression is associated with human myeloid cell differentiation:
RT correlation of predicted protein domains with exon organization.";
RL Immunogenetics 40:415-424(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT HIS-103.
RC TISSUE=Bone marrow;
RA Jiang C., Zhang D., Peng Y., Zhang X., Han Z., Fu G., Chen Z.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
RP INDUCTION, AND VARIANTS THR-179; SER-409 AND ASN-413.
RX PubMed=12894224; DOI=10.1038/sj.onc.1206754;
RA Xin H., Curry J., Johnstone R.W., Nickoloff B.J., Choubey D.;
RT "Role of IFI 16, a member of the interferon-inducible p200-protein family,
RT in prostate epithelial cellular senescence.";
RL Oncogene 22:4831-4840(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS THR-179;
RP SER-409 AND ASN-413.
RC TISSUE=Hippocampus, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS SER-409
RP AND ASN-413.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS THR-179;
RP SER-409 AND ASN-413.
RC TISSUE=Uterus;
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 [9]
RP ALTERNATIVE SPLICING, SUBUNIT, PHOSPHORYLATION, AND GLYCOSYLATION.
RX PubMed=9718316; DOI=10.1021/bi981069a;
RA Johnstone R.W., Kershaw M.H., Trapani J.A.;
RT "Isotypic variants of the interferon-inducible transcriptional repressor
RT IFI 16 arise through differential mRNA splicing.";
RL Biochemistry 37:11924-11931(1998).
RN [10]
RP INDUCTION, SUBCELLULAR LOCATION, AND DNA-BINDING.
RX PubMed=7536752; DOI=10.1002/jcb.240570106;
RA Dawson M.J., Trapani J.A.;
RT "IFI 16 gene encodes a nuclear protein whose expression is induced by
RT interferons in human myeloid leukaemia cell lines.";
RL J. Cell. Biochem. 57:39-51(1995).
RN [11]
RP TISSUE-SPECIFIC INDUCTION.
RX PubMed=7806273; DOI=10.1007/bf00188431;
RA Dawson M.J., Trapani J.A., Briggs R.C., Nicholl J.K., Sutherland G.R.,
RA Baker E.;
RT "The closely linked genes encoding the myeloid nuclear differentiation
RT antigen (MNDA) and IFI16 exhibit contrasting haemopoietic expression.";
RL Immunogenetics 41:40-43(1995).
RN [12]
RP TISSUE SPECIFIC INDUCTION.
RX PubMed=9766636; DOI=10.1002/jlb.64.4.546;
RA Dawson M.J., Elwood N.J., Johnstone R.W., Trapani J.A.;
RT "The IFN-inducible nucleoprotein IFI 16 is expressed in cells of the
RT monocyte lineage, but is rapidly and markedly down-regulated in other
RT myeloid precursor populations.";
RL J. Leukoc. Biol. 64:546-554(1998).
RN [13]
RP FUNCTION.
RX PubMed=9642285; DOI=10.1074/jbc.273.27.17172;
RA Johnstone R.W., Kerry J.A., Trapani J.A.;
RT "The human interferon-inducible protein, IFI 16, is a repressor of
RT transcription.";
RL J. Biol. Chem. 273:17172-17177(1998).
RN [14]
RP FUNCTION, AND INTERACTION WITH TP53.
RX PubMed=11146555; DOI=10.1038/sj.onc.1204005;
RA Johnstone R.W., Wei W., Greenway A., Trapani J.A.;
RT "Functional interaction between p53 and the interferon-inducible
RT nucleoprotein IFI 16.";
RL Oncogene 19:6033-6042(2000).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [16]
RP FUNCTION, AND INTERACTION WITH BRCA1.
RX PubMed=14654789; DOI=10.1038/sj.onc.1207057;
RA Aglipay J.A., Lee S.W., Okada S., Fujiuchi N., Ohtsuka T., Kwak J.C.,
RA Wang Y., Johnstone R.W., Deng C., Qin J., Ouchi T.;
RT "A member of the Pyrin family, IFI16, is a novel BRCA1-associated protein
RT involved in the p53-mediated apoptosis pathway.";
RL Oncogene 22:8931-8938(2003).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-153, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-153, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-214, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP SUMOYLATION AT LYS-561.
RC TISSUE=Cervix carcinoma;
RX PubMed=20388717; DOI=10.1074/jbc.m110.106955;
RA Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,
RA Eriksson J.E., Sistonen L.;
RT "In vivo identification of sumoylation sites by a signature tag and
RT cysteine-targeted affinity purification.";
RL J. Biol. Chem. 285:19324-19329(2010).
RN [22]
RP FUNCTION, DNA-BINDING, INTERACTION WITH TMEM173, AND INDUCTION.
RX PubMed=20890285; DOI=10.1038/ni.1932;
RA Unterholzner L., Keating S.E., Baran M., Horan K.A., Jensen S.B.,
RA Sharma S., Sirois C.M., Jin T., Latz E., Xiao T.S., Fitzgerald K.A.,
RA Paludan S.R., Bowie A.G.;
RT "IFI16 is an innate immune sensor for intracellular DNA.";
RL Nat. Immunol. 11:997-1004(2010).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-153 AND SER-575, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [25]
RP FUNCTION, AND INTERACTION WITH PYCARD AND CASP1.
RX PubMed=21575908; DOI=10.1016/j.chom.2011.04.008;
RA Kerur N., Veettil M.V., Sharma-Walia N., Bottero V., Sadagopan S.,
RA Otageri P., Chandran B.;
RT "IFI16 acts as a nuclear pathogen sensor to induce the inflammasome in
RT response to Kaposi Sarcoma-associated herpesvirus infection.";
RL Cell Host Microbe 9:363-375(2011).
RN [26]
RP FUNCTION, AND INDUCTION.
RX PubMed=21573174; DOI=10.1371/journal.pone.0019532;
RA Duan X., Ponomareva L., Veeranki S., Choubey D.;
RT "IFI16 induction by glucose restriction in human fibroblasts contributes to
RT autophagy through activation of the ATM/AMPK/p53 pathway.";
RL PLoS ONE 6:E19532-E19532(2011).
RN [27]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AIM2.
RX PubMed=22046441; DOI=10.1371/journal.pone.0027040;
RA Veeranki S., Duan X., Panchanathan R., Liu H., Choubey D.;
RT "IFI16 protein mediates the anti-inflammatory actions of the type-I
RT interferons through suppression of activation of caspase-1 by
RT inflammasomes.";
RL PLoS ONE 6:E27040-E27040(2011).
RN [28]
RP DNA-BINDING.
RX PubMed=22618232; DOI=10.1016/j.bbrc.2012.05.065;
RA Brazda V., Coufal J., Liao J.C., Arrowsmith C.H.;
RT "Preferential binding of IFI16 protein to cruciform structure and
RT superhelical DNA.";
RL Biochem. Biophys. Res. Commun. 422:716-720(2012).
RN [29]
RP FUNCTION, AND INTERACTION WITH SP1.
RX PubMed=22291595; DOI=10.1371/journal.ppat.1002498;
RA Gariano G.R., Dell'Oste V., Bronzini M., Gatti D., Luganini A.,
RA De Andrea M., Gribaudo G., Gariglio M., Landolfo S.;
RT "The intracellular DNA sensor IFI16 gene acts as restriction factor for
RT human cytomegalovirus replication.";
RL PLoS Pathog. 8:E1002498-E1002498(2012).
RN [30]
RP FUNCTION, SUBCELLULAR LOCATION, AND PROTEASOMAL DEGRADATION.
RX PubMed=23027953; DOI=10.1073/pnas.1211302109;
RA Orzalli M.H., DeLuca N.A., Knipe D.M.;
RT "Nuclear IFI16 induction of IRF-3 signaling during herpesviral infection
RT and degradation of IFI16 by the viral ICP0 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E3008-E3017(2012).
RN [31]
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION
RP AT SER-95; SER-106; SER-153; SER-168; SER-174 AND SER-780, ACETYLATION AT
RP LYS-45; LYS-99; LYS-128; LYS-214; LYS-444; LYS-451; LYS-561; LYS-598 AND
RP LYS-614, AND MUTAGENESIS OF 96-ARG--LYS-100; LYS-99; LYS-128;
RP 128-LYS--LYS-131; 134-LYS--LYS-136 AND 140-LYS--LYS-143.
RX PubMed=22691496; DOI=10.1073/pnas.1203447109;
RA Li T., Diner B.A., Chen J., Cristea I.M.;
RT "Acetylation modulates cellular distribution and DNA sensing ability of
RT interferon-inducible protein IFI16.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:10558-10563(2012).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-153, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [33]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24198334; DOI=10.1073/pnas.1316194110;
RA Orzalli M.H., Conwell S.E., Berrios C., DeCaprio J.A., Knipe D.M.;
RT "Nuclear interferon-inducible protein 16 promotes silencing of herpesviral
RT and transfected DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E4492-E4501(2013).
RN [34]
RP FUNCTION, INTERACTION WITH MTA1, AND SUBCELLULAR LOCATION.
RX PubMed=24413532; DOI=10.1158/0008-5472.can-13-2020;
RA Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y.,
RA Kim Y.N., Seong J.K., Lee M.O.;
RT "Differential regulation of estrogen receptor alpha expression in breast
RT cancer cells by metastasis-associated protein 1.";
RL Cancer Res. 74:1484-1494(2014).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-153, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [36]
RP INTERACTION WITH PYDC5.
RX PubMed=24531343; DOI=10.1038/ni.2829;
RA Khare S., Ratsimandresy R.A., de Almeida L., Cuda C.M., Rellick S.L.,
RA Misharin A.V., Wallin M.C., Gangopadhyay A., Forte E., Gottwein E.,
RA Perlman H., Reed J.C., Greaves D.R., Dorfleutner A., Stehlik C.;
RT "The PYRIN domain-only protein POP3 inhibits ALR inflammasomes and
RT regulates responses to infection with DNA viruses.";
RL Nat. Immunol. 15:343-353(2014).
RN [37]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116 AND LYS-561, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-561, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [39]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-561 AND LYS-683, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [40]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116; LYS-128; LYS-561 AND
RP LYS-683, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 192-393, AND MUTAGENESIS OF
RP TYR-218; GLU-222; TYR-267 AND GLU-272.
RX PubMed=21397192; DOI=10.1016/j.str.2010.12.015;
RA Liao J.C., Lam R., Brazda V., Duan S., Ravichandran M., Ma J., Xiao T.,
RA Tempel W., Zuo X., Wang Y.X., Chirgadze N.Y., Arrowsmith C.H.;
RT "Interferon-inducible protein 16: insight into the interaction with tumor
RT suppressor p53.";
RL Structure 19:418-429(2011).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 571-766 IN COMPLEX WITH
RP DOUBLE-STRANDED DNA, AND MUTAGENESIS OF LYS-627; LYS-663; ARG-667; SER-670;
RP LYS-674; LYS-732; LYS-734 AND LYS-759.
RX PubMed=22483801; DOI=10.1016/j.immuni.2012.02.014;
RA Jin T., Perry A., Jiang J., Smith P., Curry J.A., Unterholzner L.,
RA Jiang Z., Horvath G., Rathinam V.A., Johnstone R.W., Hornung V., Latz E.,
RA Bowie A.G., Fitzgerald K.A., Xiao T.S.;
RT "Structures of the HIN domain:DNA complexes reveal ligand binding and
RT activation mechanisms of the AIM2 inflammasome and IFI16 receptor.";
RL Immunity 36:561-571(2012).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 192-393.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of the first HIN-200 domain of interferon-inducible
RT protein 16.";
RL Submitted (FEB-2007) to the PDB data bank.
RN [44]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 571-766.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure analysis of the second HIN domain of IFI16.";
RL Submitted (NOV-2007) to the PDB data bank.
CC -!- FUNCTION: Binds double-stranded DNA. Binds preferentially to
CC supercoiled DNA and cruciform DNA structures. Seems to be involved in
CC transcriptional regulation. May function as a transcriptional
CC repressor. Could have a role in the regulation of hematopoietic
CC differentiation through activation of unknown target genes. Controls
CC cellular proliferation by modulating the functions of cell cycle
CC regulatory factors including p53/TP53 and the retinoblastoma protein.
CC May be involved in TP53-mediated transcriptional activation by
CC enhancing TP53 sequence-specific DNA binding and modulating TP53
CC phosphorylation status. Seems to be involved in energy-level-dependent
CC activation of the ATM/ AMPK/TP53 pathway coupled to regulation of
CC autophagy. May be involved in regulation of TP53-mediated cell death
CC also involving BRCA1. May be involved in the senescence of prostate
CC epithelial cells. Involved in innate immune response by recognizing
CC viral dsDNA in the cytosol and probably in the nucleus. After binding
CC to viral DNA in the cytoplasm recruits TMEM173/STING and mediates the
CC induction of IFN-beta. Has anti-inflammatory activity and inhibits the
CC activation of the AIM2 inflammasome, probably via association with
CC AIM2. Proposed to bind viral DNA in the nucleus, such as of Kaposi's
CC sarcoma-associated herpesvirus, and to induce the formation of nuclear
CC caspase-1-activating inflammasome formation via association with
CC PYCARD. Inhibits replication of herpesviruses such as human
CC cytomegalovirus (HCMV) probably by interfering with promoter
CC recruitment of members of the Sp1 family of transcription factors.
CC Necessary to activate the IRF3 signaling cascade during human herpes
CC simplex virus 1 (HHV-1) infection and promotes the assembly of
CC heterochromatin on herpesviral DNA and inhibition of viral immediate-
CC early gene expression and replication. Involved in the MTA1-mediated
CC epigenetic regulation of ESR1 expression in breast cancer.
CC {ECO:0000269|PubMed:11146555, ECO:0000269|PubMed:12894224,
CC ECO:0000269|PubMed:14654789, ECO:0000269|PubMed:20890285,
CC ECO:0000269|PubMed:21573174, ECO:0000269|PubMed:21575908,
CC ECO:0000269|PubMed:22046441, ECO:0000269|PubMed:22291595,
CC ECO:0000269|PubMed:23027953, ECO:0000269|PubMed:24198334,
CC ECO:0000269|PubMed:24413532, ECO:0000269|PubMed:9642285}.
CC -!- SUBUNIT: Forms homooligomers; isoform 2 can self-associate or associate
CC with isoform 1 or isoform 3. Interacts with TMEM173, AIM2, PYCARD and
CC CASP1. Interacts with BRCA1, TP53, E2F1, RB1 and SP1. Interacts with
CC MTA1. Interacts with PYDC5 (PubMed:24531343).
CC {ECO:0000269|PubMed:11146555, ECO:0000269|PubMed:14654789,
CC ECO:0000269|PubMed:20890285, ECO:0000269|PubMed:21575908,
CC ECO:0000269|PubMed:22046441, ECO:0000269|PubMed:22291595,
CC ECO:0000269|PubMed:22483801, ECO:0000269|PubMed:24413532,
CC ECO:0000269|PubMed:24531343, ECO:0000269|PubMed:9718316}.
CC -!- INTERACTION:
CC Q16666; P10275: AR; NbExp=3; IntAct=EBI-2867186, EBI-608057;
CC Q16666; P38398: BRCA1; NbExp=9; IntAct=EBI-2867186, EBI-349905;
CC Q16666; Q96C10: DHX58; NbExp=2; IntAct=EBI-2867186, EBI-744193;
CC Q16666; Q86WV6: STING1; NbExp=2; IntAct=EBI-2867186, EBI-2800345;
CC Q16666-2; Q16666-2: IFI16; NbExp=3; IntAct=EBI-6273540, EBI-6273540;
CC Q16666-2; P04637: TP53; NbExp=6; IntAct=EBI-6273540, EBI-366083;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cellular distribution is
CC dependent on the acetylation status of the multipartite nuclear
CC localization signal (NLS); NLS acetylation promotes cytoplasmic
CC localization. Localizes in the nucleus during human herpes simplex
CC virus 1 (HHV-1) infection.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=IFI 16A;
CC IsoId=Q16666-1; Sequence=Displayed;
CC Name=2; Synonyms=IFI 16B;
CC IsoId=Q16666-2; Sequence=VSP_002676;
CC Name=3; Synonyms=IFI 16C;
CC IsoId=Q16666-3; Sequence=VSP_002675;
CC Name=4;
CC IsoId=Q16666-6; Sequence=VSP_044691;
CC -!- TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes,
CC fibroblasts and lymphoid cells. Present in myeloid precursors (CD34+)
CC and throughout monocyte development, but its expression is down-
CC regulated in erythroid and polymorphonuclear precursor cells. Present
CC in prostate, ovary and breast (at protein level).
CC {ECO:0000269|PubMed:12894224}.
CC -!- INDUCTION: Strongly induced by IFNG/IFN-gamma and, to a lesser extent,
CC by alpha interferon. In HL-60 cells, maximum induction by IFNG/IFN-
CC gamma occurs within 12 hours whereas, for IFN-alpha, only 10-fold
CC induction was observed after 36 hours. Induced in vitro by
CC dimethylsulfoxide, retinoic acid and 1,25 dihydroxyvitamin D3. Induced
CC in monocytes by IFN-alpha and viral dsDNA. Induced by glucose
CC restriction. {ECO:0000269|PubMed:12894224, ECO:0000269|PubMed:20890285,
CC ECO:0000269|PubMed:21573174, ECO:0000269|PubMed:7536752}.
CC -!- DOMAIN: The HIN-20 domains mediates dsDNA binding via electrostatic
CC interactions. {ECO:0000269|PubMed:22483801}.
CC -!- PTM: Ubiquitinated by human herpes simplex virus 1 (HHV-1) ICP0
CC protein; leading to degradation by the proteasome.
CC -!- PTM: Lysine acetylation in the multipartite nuclear localization signal
CC (NLS) regulates the subcellular location. In vitro can be acetylated by
CC p300/EP300 coupled to cytoplasmic localization.
CC {ECO:0000269|PubMed:22691496}.
CC -!- PTM: Phosphorylated on Ser and Thr. {ECO:0000269|PubMed:22691496,
CC ECO:0000269|PubMed:9718316}.
CC -!- PTM: Isoform 3 seems to show a minor degree of complex carbohydrate
CC addition.
CC -!- MISCELLANEOUS: [Isoform 2]: Major isoform. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the HIN-200 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF20997.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF20997.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAC04462.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAD92226.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG58950.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M63838; AAA58683.1; -; mRNA.
DR EMBL; S75433; AAB32519.2; -; Genomic_DNA.
DR EMBL; S75417; AAB32519.2; JOINED; Genomic_DNA.
DR EMBL; S75419; AAB32519.2; JOINED; Genomic_DNA.
DR EMBL; S75421; AAB32519.2; JOINED; Genomic_DNA.
DR EMBL; S75423; AAB32519.2; JOINED; Genomic_DNA.
DR EMBL; S75424; AAB32519.2; JOINED; Genomic_DNA.
DR EMBL; S75426; AAB32519.2; JOINED; Genomic_DNA.
DR EMBL; S75429; AAB32519.2; JOINED; Genomic_DNA.
DR EMBL; S75431; AAB32519.2; JOINED; Genomic_DNA.
DR EMBL; AF208043; AAF20997.1; ALT_SEQ; mRNA.
DR EMBL; AY138863; AAM96005.1; -; mRNA.
DR EMBL; AK094968; BAC04462.1; ALT_SEQ; mRNA.
DR EMBL; AK296228; BAG58950.1; ALT_INIT; mRNA.
DR EMBL; AB208989; BAD92226.1; ALT_INIT; mRNA.
DR EMBL; AL359753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017059; AAH17059.1; -; mRNA.
DR CCDS; CCDS1180.3; -. [Q16666-2]
DR CCDS; CCDS58039.1; -. [Q16666-6]
DR PIR; I54501; I54501.
DR RefSeq; NP_001193496.1; NM_001206567.1. [Q16666-6]
DR RefSeq; NP_005522.2; NM_005531.2. [Q16666-2]
DR PDB; 2OQ0; X-ray; 2.00 A; A/B/C/D=192-393.
DR PDB; 3B6Y; X-ray; 2.35 A; A/B=571-766.
DR PDB; 3RLN; X-ray; 2.25 A; A=571-766.
DR PDB; 3RLO; X-ray; 1.80 A; A=571-766.
DR PDB; 3RNU; X-ray; 2.50 A; A/B/C/D=571-766.
DR PDB; 4QGU; X-ray; 2.54 A; A/B=192-393.
DR PDBsum; 2OQ0; -.
DR PDBsum; 3B6Y; -.
DR PDBsum; 3RLN; -.
DR PDBsum; 3RLO; -.
DR PDBsum; 3RNU; -.
DR PDBsum; 4QGU; -.
DR AlphaFoldDB; Q16666; -.
DR SMR; Q16666; -.
DR BioGRID; 109654; 740.
DR DIP; DIP-42868N; -.
DR IntAct; Q16666; 179.
DR MINT; Q16666; -.
DR STRING; 9606.ENSP00000357113; -.
DR CarbonylDB; Q16666; -.
DR GlyConnect; 1263; 1 N-Linked glycan (1 site).
DR GlyGen; Q16666; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q16666; -.
DR MetOSite; Q16666; -.
DR PhosphoSitePlus; Q16666; -.
DR SwissPalm; Q16666; -.
DR BioMuta; IFI16; -.
DR DMDM; 118572657; -.
DR EPD; Q16666; -.
DR jPOST; Q16666; -.
DR MassIVE; Q16666; -.
DR MaxQB; Q16666; -.
DR PaxDb; Q16666; -.
DR PeptideAtlas; Q16666; -.
DR PRIDE; Q16666; -.
DR ProteomicsDB; 40733; -.
DR ProteomicsDB; 61023; -. [Q16666-1]
DR ProteomicsDB; 61024; -. [Q16666-2]
DR ProteomicsDB; 61025; -. [Q16666-3]
DR Antibodypedia; 988; 344 antibodies from 33 providers.
DR DNASU; 3428; -.
DR Ensembl; ENST00000295809.12; ENSP00000295809.7; ENSG00000163565.20. [Q16666-1]
DR Ensembl; ENST00000359709.7; ENSP00000352740.3; ENSG00000163565.20. [Q16666-6]
DR Ensembl; ENST00000368131.8; ENSP00000357113.4; ENSG00000163565.20. [Q16666-2]
DR Ensembl; ENST00000368132.7; ENSP00000357114.3; ENSG00000163565.20. [Q16666-2]
DR Ensembl; ENST00000448393.6; ENSP00000404325.2; ENSG00000163565.20. [Q16666-3]
DR GeneID; 3428; -.
DR KEGG; hsa:3428; -.
DR MANE-Select; ENST00000295809.12; ENSP00000295809.7; NM_001376587.1; NP_001363516.1.
DR UCSC; uc001ftg.4; human. [Q16666-1]
DR CTD; 3428; -.
DR DisGeNET; 3428; -.
DR GeneCards; IFI16; -.
DR HGNC; HGNC:5395; IFI16.
DR HPA; ENSG00000163565; Low tissue specificity.
DR MIM; 147586; gene.
DR neXtProt; NX_Q16666; -.
DR OpenTargets; ENSG00000163565; -.
DR PharmGKB; PA29642; -.
DR VEuPathDB; HostDB:ENSG00000163565; -.
DR eggNOG; ENOG502QTQS; Eukaryota.
DR GeneTree; ENSGT00390000013296; -.
DR HOGENOM; CLU_022874_0_0_1; -.
DR InParanoid; Q16666; -.
DR OMA; NCEERDK; -.
DR PhylomeDB; Q16666; -.
DR TreeFam; TF337385; -.
DR PathwayCommons; Q16666; -.
DR Reactome; R-HSA-1834941; STING mediated induction of host immune responses.
DR Reactome; R-HSA-3270619; IRF3-mediated induction of type I IFN.
DR SignaLink; Q16666; -.
DR SIGNOR; Q16666; -.
DR BioGRID-ORCS; 3428; 16 hits in 1088 CRISPR screens.
DR ChiTaRS; IFI16; human.
DR EvolutionaryTrace; Q16666; -.
DR GeneWiki; IFI16; -.
DR GenomeRNAi; 3428; -.
DR Pharos; Q16666; Tbio.
DR PRO; PR:Q16666; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q16666; protein.
DR Bgee; ENSG00000163565; Expressed in germinal epithelium of ovary and 216 other tissues.
DR ExpressionAtlas; Q16666; baseline and differential.
DR Genevisible; Q16666; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
DR GO; GO:0035458; P:cellular response to interferon-beta; IBA:GO_Central.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:MGI.
DR GO; GO:0030224; P:monocyte differentiation; IDA:UniProtKB.
DR GO; GO:0030099; P:myeloid cell differentiation; NAS:UniProtKB.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:0045824; P:negative regulation of innate immune response; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; TAS:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IEP:UniProtKB.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.40.50.140; -; 4.
DR IDEAL; IID00478; -.
DR InterPro; IPR004020; DAPIN.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR040205; HIN-200.
DR InterPro; IPR004021; HIN200/IF120x.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR12200; PTHR12200; 2.
DR Pfam; PF02760; HIN; 2.
DR Pfam; PF02758; PYRIN; 1.
DR SMART; SM01289; PYRIN; 1.
DR PROSITE; PS50824; DAPIN; 1.
DR PROSITE; PS50834; HIN_200; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Apoptosis;
KW Autophagy; Cytoplasm; DNA-binding; Immunity; Inflammatory response;
KW Innate immunity; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..785
FT /note="Gamma-interferon-inducible protein 16"
FT /id="PRO_0000153723"
FT DOMAIN 1..88
FT /note="Pyrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00061"
FT DOMAIN 189..389
FT /note="HIN-200 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00106"
FT DOMAIN 562..761
FT /note="HIN-200 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00106"
FT REGION 91..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..393
FT /note="Interaction with TP53 C-terminus"
FT REGION 390..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..766
FT /note="Interaction with TP53 core domain"
FT MOTIF 96..100
FT /note="Nuclear localization signal"
FT MOTIF 128..131
FT /note="Nuclear localization signal"
FT MOTIF 134..136
FT /note="Nuclear localization signal"
FT MOTIF 140..143
FT /note="Nuclear localization signal"
FT COMPBIAS 105..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22691496"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22691496"
FT MOD_RES 99
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22691496"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22691496,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 128
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22691496"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22691496,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22691496"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22691496"
FT MOD_RES 214
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22691496,
FT ECO:0007744|PubMed:19608861"
FT MOD_RES 444
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22691496"
FT MOD_RES 451
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22691496"
FT MOD_RES 561
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22691496"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 598
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22691496"
FT MOD_RES 614
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22691496"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22691496"
FT CROSSLNK 116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 561
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 561
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 683
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 128..183
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044691"
FT VAR_SEQ 444..555
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_002675"
FT VAR_SEQ 444..499
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12894224,
FT ECO:0000303|PubMed:1526658, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.3, ECO:0000303|Ref.6"
FT /id="VSP_002676"
FT VARIANT 103
FT /note="D -> H (in dbSNP:rs1057018)"
FT /evidence="ECO:0000269|PubMed:1526658,
FT ECO:0000269|PubMed:7959953, ECO:0000269|Ref.3"
FT /id="VAR_029486"
FT VARIANT 179
FT /note="S -> T (in dbSNP:rs866484)"
FT /evidence="ECO:0000269|PubMed:12894224,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_029487"
FT VARIANT 202
FT /note="K -> E (in dbSNP:rs11585341)"
FT /id="VAR_029488"
FT VARIANT 409
FT /note="R -> S (in dbSNP:rs1057027)"
FT /evidence="ECO:0000269|PubMed:12894224,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.6"
FT /id="VAR_029489"
FT VARIANT 413
FT /note="Y -> N (in dbSNP:rs1057028)"
FT /evidence="ECO:0000269|PubMed:12894224,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.6"
FT /id="VAR_029490"
FT VARIANT 723
FT /note="T -> S (in dbSNP:rs6940)"
FT /id="VAR_029491"
FT VARIANT 779
FT /note="T -> S (in dbSNP:rs6940)"
FT /id="VAR_057582"
FT MUTAGEN 96..100
FT /note="Missing: Predominant cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:22691496"
FT MUTAGEN 99
FT /note="K->Q: Predominant cytoplasmic, reduces nuclear
FT localization (mimics non-acetylated state)."
FT /evidence="ECO:0000269|PubMed:22691496"
FT MUTAGEN 99
FT /note="K->R: Minor effect on nuclear localization (mimics
FT acetylated state)."
FT /evidence="ECO:0000269|PubMed:22691496"
FT MUTAGEN 128..131
FT /note="Missing: Predominant nuclear, some cytoplasmic
FT localization."
FT /evidence="ECO:0000269|PubMed:22691496"
FT MUTAGEN 128
FT /note="K->Q: Predominant cytoplasmic, reduces nuclear
FT localization (mimics non-acetylated state)."
FT /evidence="ECO:0000269|PubMed:22691496"
FT MUTAGEN 128
FT /note="K->R: Minor effect on nuclear localization (mimics
FT acetylated state)."
FT /evidence="ECO:0000269|PubMed:22691496"
FT MUTAGEN 134..136
FT /note="Missing: Mostly nuclear, minor cytoplasmic
FT localization."
FT /evidence="ECO:0000269|PubMed:22691496"
FT MUTAGEN 140..143
FT /note="Missing: Mostly nuclear, minor cytoplasmic
FT localization."
FT /evidence="ECO:0000269|PubMed:22691496"
FT MUTAGEN 218
FT /note="Y->A: Abolishes TP53-mediated transcriptional
FT activation; when associated with A-267."
FT /evidence="ECO:0000269|PubMed:21397192"
FT MUTAGEN 222
FT /note="E->A: Abolishes TP53-mediated transcriptional
FT activation; when associated with A-272."
FT /evidence="ECO:0000269|PubMed:21397192"
FT MUTAGEN 267
FT /note="Y->A: Abolishes TP53-mediated transcriptional
FT activation; when associated with A-218."
FT /evidence="ECO:0000269|PubMed:21397192"
FT MUTAGEN 272
FT /note="E->A: Abolishes TP53-mediated transcriptional
FT activation; when associated with A-222."
FT /evidence="ECO:0000269|PubMed:21397192"
FT MUTAGEN 627
FT /note="K->A: Impairs DNA binding; when associated with A-
FT 663; A-667; A-670; A-674; A-732; A-734 and A-759."
FT /evidence="ECO:0000269|PubMed:22483801"
FT MUTAGEN 663
FT /note="K->A: Impairs DNA binding; when associated with A-
FT 627; A-667; A-670; A-674; A-732; A-734 and A-759."
FT /evidence="ECO:0000269|PubMed:22483801"
FT MUTAGEN 667
FT /note="R->A: Impairs DNA binding; when associated with A-
FT 627; A-663; A-670; A-674; A-732; A-734 and A-759."
FT /evidence="ECO:0000269|PubMed:22483801"
FT MUTAGEN 670
FT /note="S->A: Impairs DNA binding; when associated with A-
FT 627; A-663; A-667; A-674; A-732; A-734 and A-759."
FT /evidence="ECO:0000269|PubMed:22483801"
FT MUTAGEN 674
FT /note="K->A: Impairs DNA binding; when associated with A-
FT 627; A-663; A-667; A-670; A-732; A-734 and A-759."
FT /evidence="ECO:0000269|PubMed:22483801"
FT MUTAGEN 732
FT /note="K->A: Impairs DNA binding; when associated with A-
FT 627; A-663; A-667; A-670; A- 674; A-734 and A-759."
FT /evidence="ECO:0000269|PubMed:22483801"
FT MUTAGEN 734
FT /note="K->A: Impairs DNA binding; when associated with A-
FT 627; A-663; A-667; A-670; A- 674; A-732 and A-759."
FT /evidence="ECO:0000269|PubMed:22483801"
FT MUTAGEN 759
FT /note="K->A: Impairs DNA binding; when associated with A-
FT 627; A-663; A-667; A-670; A- 674; A-732 and A-734."
FT /evidence="ECO:0000269|PubMed:22483801"
FT CONFLICT 401
FT /note="S -> G (in Ref. 5; BAG58950)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="P -> S (in Ref. 5; BAG58950)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="K -> R (in Ref. 4; AAM96005)"
FT /evidence="ECO:0000305"
FT CONFLICT 723
FT /note="T -> N (in Ref. 1; AAA58683 and 2; AAB32519)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="C -> S (in Ref. 1; AAA58683 and 2; AAB32519)"
FT /evidence="ECO:0000305"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:2OQ0"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:2OQ0"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:2OQ0"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:2OQ0"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:2OQ0"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:2OQ0"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:2OQ0"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:2OQ0"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:2OQ0"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:2OQ0"
FT HELIX 292..298
FT /evidence="ECO:0007829|PDB:2OQ0"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:2OQ0"
FT STRAND 315..327
FT /evidence="ECO:0007829|PDB:2OQ0"
FT STRAND 329..338
FT /evidence="ECO:0007829|PDB:2OQ0"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:2OQ0"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:2OQ0"
FT STRAND 361..372
FT /evidence="ECO:0007829|PDB:2OQ0"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:2OQ0"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:2OQ0"
FT STRAND 578..585
FT /evidence="ECO:0007829|PDB:3RLO"
FT STRAND 589..592
FT /evidence="ECO:0007829|PDB:3RLO"
FT TURN 593..596
FT /evidence="ECO:0007829|PDB:3RLO"
FT STRAND 597..605
FT /evidence="ECO:0007829|PDB:3RLO"
FT STRAND 610..615
FT /evidence="ECO:0007829|PDB:3RLO"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:3RLO"
FT TURN 621..624
FT /evidence="ECO:0007829|PDB:3RLO"
FT STRAND 629..634
FT /evidence="ECO:0007829|PDB:3RLO"
FT STRAND 636..638
FT /evidence="ECO:0007829|PDB:3RLO"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:3RLO"
FT STRAND 648..652
FT /evidence="ECO:0007829|PDB:3RLO"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:3RLO"
FT HELIX 663..670
FT /evidence="ECO:0007829|PDB:3RLO"
FT HELIX 675..679
FT /evidence="ECO:0007829|PDB:3RLO"
FT STRAND 685..699
FT /evidence="ECO:0007829|PDB:3RLO"
FT STRAND 702..709
FT /evidence="ECO:0007829|PDB:3RLO"
FT STRAND 712..718
FT /evidence="ECO:0007829|PDB:3RLO"
FT HELIX 720..724
FT /evidence="ECO:0007829|PDB:3RLO"
FT STRAND 732..741
FT /evidence="ECO:0007829|PDB:3RLO"
FT TURN 744..747
FT /evidence="ECO:0007829|PDB:3RLO"
FT STRAND 749..761
FT /evidence="ECO:0007829|PDB:3RLO"
FT TURN 764..766
FT /evidence="ECO:0007829|PDB:3RLO"
SQ 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
