AZI2_MOUSE
ID AZI2_MOUSE Reviewed; 405 AA.
AC Q9QYP6; Q3TIN1; Q3V3R2; Q9CUI5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=5-azacytidine-induced protein 2 {ECO:0000303|PubMed:10580148};
DE AltName: Full=NF-kappa-B-activating kinase-associated protein 1 {ECO:0000303|PubMed:17568778};
DE Short=Nak-associated protein 1 {ECO:0000303|PubMed:17568778};
DE Short=Nap1 {ECO:0000303|PubMed:17568778};
GN Name=Azi2;
GN Synonyms=Az2 {ECO:0000303|PubMed:10580148},
GN Nap1 {ECO:0000303|PubMed:17568778}, Tbkp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10580148; DOI=10.1016/s0378-1119(99)00450-3;
RA Miyagawa J., Muguruma M., Aoto H., Suetake I., Nakamura M., Tajima S.;
RT "Isolation of the novel cDNA of a gene of which expression is induced by a
RT demethylating stimulus.";
RL Gene 240:289-295(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and DBA/2J;
RC TISSUE=Bone marrow, Cerebellum, Liver, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP FUNCTION, INTERACTION WITH IKBKE AND TBK1, SUBUNIT, AND MUTAGENESIS OF
RP TYR-236; TRP-237; GLU-238; GLN-253 AND LEU-257.
RX PubMed=17568778; DOI=10.1038/sj.emboj.7601743;
RA Ryzhakov G., Randow F.;
RT "SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-
RT binding domain with NAP1 and TANK.";
RL EMBO J. 26:3180-3190(2007).
RN [5]
RP PROTEIN SEQUENCE OF 241-258, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP FUNCTION, AND UBIQUITINATION.
RX PubMed=22539786; DOI=10.4049/jimmunol.1103506;
RA Zhao W., Wang L., Zhang M., Wang P., Yuan C., Qi J., Meng H., Gao C.;
RT "Tripartite motif-containing protein 38 negatively regulates TLR3/4- and
RT RIG-I-mediated IFN-beta production and antiviral response by targeting
RT NAP1.";
RL J. Immunol. 188:5311-5318(2012).
CC -!- FUNCTION: Adapter protein which binds TBK1 and IKBKE playing a role in
CC antiviral innate immunity. Activates serine/threonine-protein kinase
CC TBK1 and facilitates its oligomerization. Enhances the phosphorylation
CC of NF-kappa-B p65 subunit RELA by TBK1. Promotes TBK1-induced as well
CC as TNF-alpha or PMA-induced activation of NF-kappa-B. Participates in
CC IFNB promoter activation via TICAM1. {ECO:0000269|PubMed:17568778,
CC ECO:0000269|PubMed:22539786}.
CC -!- SUBUNIT: Homodimer (PubMed:17568778). Interacts with IKBKE and TBK1
CC (PubMed:17568778). Interacts with TICAM1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H6S1, ECO:0000269|PubMed:17568778}.
CC -!- INTERACTION:
CC Q9QYP6; O96018: APBA3; Xeno; NbExp=2; IntAct=EBI-6115874, EBI-6115839;
CC Q9QYP6; Q86YT6: MIB1; Xeno; NbExp=2; IntAct=EBI-6115874, EBI-2129148;
CC Q9QYP6; Q9NVV4: MTPAP; Xeno; NbExp=2; IntAct=EBI-6115874, EBI-2556166;
CC Q9QYP6; O75113: N4BP1; Xeno; NbExp=2; IntAct=EBI-6115874, EBI-5278391;
CC Q9QYP6; Q96EP0: RNF31; Xeno; NbExp=2; IntAct=EBI-6115874, EBI-948111;
CC Q9QYP6; Q13114: TRAF3; Xeno; NbExp=2; IntAct=EBI-6115874, EBI-357631;
CC Q9QYP6; P40222: TXLNA; Xeno; NbExp=2; IntAct=EBI-6115874, EBI-359793;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10580148}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9QYP6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QYP6-2; Sequence=VSP_023823, VSP_023824;
CC Name=3;
CC IsoId=Q9QYP6-3; Sequence=VSP_023822;
CC -!- TISSUE SPECIFICITY: Testis, ovary, heart, lung, kidney and brain.
CC Expressed mainly in the spermatocytes or spermatids in the testis.
CC {ECO:0000269|PubMed:10580148}.
CC -!- INDUCTION: By 5-azacytidine. {ECO:0000269|PubMed:10580148}.
CC -!- PTM: Ubiquitinated via 'Lys-48'-linked polyubiquitination by TRIM38,
CC leading to its degradation. {ECO:0000269|PubMed:22539786}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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DR EMBL; AB007141; BAA88213.1; -; mRNA.
DR EMBL; AK004992; BAB23727.1; -; mRNA.
DR EMBL; AK015942; BAB30044.1; -; mRNA.
DR EMBL; AK030076; BAC26770.1; -; mRNA.
DR EMBL; AK036102; BAE43294.1; -; mRNA.
DR EMBL; AK153477; BAE32027.1; -; mRNA.
DR EMBL; AK165549; BAE38249.1; -; mRNA.
DR EMBL; AK167783; BAE39815.1; -; mRNA.
DR EMBL; BC006851; AAH06851.1; -; mRNA.
DR CCDS; CCDS40799.1; -. [Q9QYP6-1]
DR CCDS; CCDS52959.1; -. [Q9QYP6-2]
DR RefSeq; NP_001041611.1; NM_001048146.2. [Q9QYP6-2]
DR RefSeq; NP_001273436.1; NM_001286507.1.
DR RefSeq; NP_001273437.1; NM_001286508.1. [Q9QYP6-1]
DR RefSeq; NP_038755.1; NM_013727.4. [Q9QYP6-1]
DR AlphaFoldDB; Q9QYP6; -.
DR SMR; Q9QYP6; -.
DR BioGRID; 205136; 4.
DR IntAct; Q9QYP6; 11.
DR STRING; 10090.ENSMUSP00000044350; -.
DR iPTMnet; Q9QYP6; -.
DR PhosphoSitePlus; Q9QYP6; -.
DR EPD; Q9QYP6; -.
DR MaxQB; Q9QYP6; -.
DR PaxDb; Q9QYP6; -.
DR PeptideAtlas; Q9QYP6; -.
DR PRIDE; Q9QYP6; -.
DR ProteomicsDB; 273640; -. [Q9QYP6-1]
DR ProteomicsDB; 273641; -. [Q9QYP6-2]
DR ProteomicsDB; 273642; -. [Q9QYP6-3]
DR Antibodypedia; 27537; 135 antibodies from 23 providers.
DR DNASU; 27215; -.
DR Ensembl; ENSMUST00000044454; ENSMUSP00000044350; ENSMUSG00000039285. [Q9QYP6-1]
DR Ensembl; ENSMUST00000133580; ENSMUSP00000118765; ENSMUSG00000039285. [Q9QYP6-1]
DR Ensembl; ENSMUST00000134433; ENSMUSP00000114980; ENSMUSG00000039285. [Q9QYP6-2]
DR Ensembl; ENSMUST00000154583; ENSMUSP00000122063; ENSMUSG00000039285. [Q9QYP6-3]
DR GeneID; 27215; -.
DR KEGG; mmu:27215; -.
DR UCSC; uc009rzi.2; mouse. [Q9QYP6-2]
DR UCSC; uc009rzj.2; mouse. [Q9QYP6-1]
DR CTD; 64343; -.
DR MGI; MGI:1351332; Azi2.
DR VEuPathDB; HostDB:ENSMUSG00000039285; -.
DR eggNOG; ENOG502QV07; Eukaryota.
DR GeneTree; ENSGT00940000153704; -.
DR HOGENOM; CLU_059745_0_0_1; -.
DR InParanoid; Q9QYP6; -.
DR OMA; PWPSQSC; -.
DR OrthoDB; 1268120at2759; -.
DR PhylomeDB; Q9QYP6; -.
DR TreeFam; TF331289; -.
DR BioGRID-ORCS; 27215; 10 hits in 72 CRISPR screens.
DR ChiTaRS; Azi2; mouse.
DR PRO; PR:Q9QYP6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9QYP6; protein.
DR Bgee; ENSMUSG00000039285; Expressed in retinal neural layer and 258 other tissues.
DR ExpressionAtlas; Q9QYP6; baseline and differential.
DR Genevisible; Q9QYP6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0097028; P:dendritic cell differentiation; IMP:MGI.
DR GO; GO:0044565; P:dendritic cell proliferation; IGI:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:MGI.
DR GO; GO:0042110; P:T cell activation; IDA:MGI.
DR InterPro; IPR024581; TBD.
DR Pfam; PF12845; TBD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..405
FT /note="5-azacytidine-induced protein 2"
FT /id="PRO_0000280604"
FT REGION 1..198
FT /note="Homodimerization"
FT /evidence="ECO:0000269|PubMed:17568778"
FT REGION 229..270
FT /note="Interaction with TBK1 and IKBKE"
FT /evidence="ECO:0000269|PubMed:17568778"
FT REGION 357..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 40..197
FT /evidence="ECO:0000255"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMA0"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6S1"
FT VAR_SEQ 115..405
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023822"
FT VAR_SEQ 269..283
FT /note="ACTPVGCVEDLGRDS -> GKSLLAANADSSQTA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023823"
FT VAR_SEQ 284..405
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023824"
FT MUTAGEN 236
FT /note="Y->A: Abolishes interaction with TBK1 but not with
FT IKBKE."
FT /evidence="ECO:0000269|PubMed:17568778"
FT MUTAGEN 237
FT /note="W->A: No effect on interaction with TBK1 and IKBKE."
FT /evidence="ECO:0000269|PubMed:17568778"
FT MUTAGEN 238
FT /note="E->A: No effect on interaction with TBK1 and IKBKE."
FT /evidence="ECO:0000269|PubMed:17568778"
FT MUTAGEN 253
FT /note="Q->A: Abolishes interaction with TBK1 and IKBKE."
FT /evidence="ECO:0000269|PubMed:17568778"
FT MUTAGEN 257
FT /note="L->A: Abolishes interaction with TBK1 and IKBKE."
FT /evidence="ECO:0000269|PubMed:17568778"
SQ SEQUENCE 405 AA; 46091 MW; 5EBD91369CBCB89F CRC64;
MDTLVEDDIC ILNHEKAHRR EAVTPLSAYP GDESVASHFA LVTAYEDIKK RLKDSEKENS
FLKKRIRALE ERLVGARADE ETSSVGREQV NKAYHAYREV CIDRDNLKNQ LEKINKDNSE
SLKMLNEQLQ SKEVELLQLR TEVETQQVMR NLNPPSSSWE VEKLSCDLKI HGLEQELGLL
RKECSDLRTE LQKARQTGPP QEDILQGRDV IRPSLSREEH VPHQGLHHSD NMQHAYWELK
REMSNLHLVT QVQAELLRKL KTSAAVKKAC TPVGCVEDLG RDSTKLHLTN FTATYKRHPS
LSPNGKAPCY APSSPLPGDR KVFSDKAVLQ SWTDNERLVP NDGADFPEHS SYGRNSLEDN
SWVFPSPPKS SETAFGENKS KILPLSNLPP LHYLDQQNQN CLYKS
