ID AZI2_HUMAN Reviewed; 392 AA. AC Q9H6S1; A8K3M2; C9JB40; H7BXU6; Q86W99; Q9BQF1; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 10-JUN-2026, entry version 158. DE RecName: Full=5-azacytidine-induced protein 2; DE AltName: Full=NF-kappa-B-activating kinase-associated protein 1 {ECO:0000303|PubMed:14560022}; DE Short=Nak-associated protein 1 {ECO:0000303|PubMed:14560022}; DE Short=Nap1 {ECO:0000303|PubMed:14560022}; DE AltName: Full=TILP {ECO:0000303|Ref.2}; GN Name=AZI2; Synonyms=NAP1 {ECO:0000303|PubMed:14560022}, TBKBP2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH TBK1 AND RP IKBKE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=14560022; DOI=10.1128/mcb.23.21.7780-7793.2003; RA Fujita F., Taniguchi Y., Kato T., Narita Y., Furuya A., Ogawa T., RA Sakurai H., Joh T., Itoh M., Delhase M., Karin M., Nakanishi M.; RT "Identification of NAP1, a regulatory subunit of IkappaB kinase-related RT kinases that potentiates NF-kappaB signaling."; RL Mol. Cell. Biol. 23:7780-7793(2003). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1 AND RP 2). RA Inohara N., Koseki T., Nunez G.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Embryo, and Hepatoma; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP FUNCTION, AND INTERACTION WITH TICAM1. RX PubMed=15611223; DOI=10.4049/jimmunol.174.1.27; RA Sasai M., Oshiumi H., Matsumoto M., Inoue N., Fujita F., Nakanishi M., RA Seya T.; RT "NF-kappaB-activating kinase-associated protein 1 participates in RT TLR3/Toll-IL-1 homology domain-containing adapter molecule-1-mediated IFN RT regulatory factor 3 activation."; RL J. Immunol. 174:27-30(2005). RN [7] RP INTERACTION WITH IKBKE. 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [10] RP FUNCTION, AND INTERACTION WITH TBK1. RX PubMed=21931631; DOI=10.1371/journal.pone.0023971; RA Goncalves A., Burckstummer T., Dixit E., Scheicher R., Gorna M.W., RA Karayel E., Sugar C., Stukalov A., Berg T., Kralovics R., Planyavsky M., RA Bennett K.L., Colinge J., Superti-Furga G.; RT "Functional dissection of the TBK1 molecular network."; RL PLoS ONE 6:E23971-E23971(2011). RN [11] RP INTERACTION WITH VACCINIA VIRUS PROTEIN C6. RX PubMed=21931555; DOI=10.1371/journal.ppat.1002247; RA Unterholzner L., Sumner R.P., Baran M., Ren H., Mansur D.S., Bourke N.M., RA Randow F., Smith G.L., Bowie A.G.; RT "Vaccinia virus protein C6 is a virulence factor that binds TBK-1 adaptor RT proteins and inhibits activation of IRF3 and IRF7."; RL PLoS Pathog. 7:E1002247-E1002247(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; 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 [13] 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 [14] RP INTERACTION WITH TBK1. RX PubMed=29251827; DOI=10.1002/pmic.201700403; RA Shang J., Xia T., Han Q.Q., Zhao X., Hu M.M., Shu H.B., Guo L.; RT "Quantitative Proteomics Identified TTC4 as a TBK1 Interactor and a RT Positive Regulator of SeV-Induced Innate Immunity."; RL Proteomics 18:0-0(2018). RN [15] {ECO:0007744|PDB:5Z7G, ECO:0007744|PDB:5Z7L} RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 33-75, AND INTERACTION WITH RP TAXBP1 AND CALCOCO2. RX PubMed=30459273; DOI=10.1073/pnas.1811421115; RA Fu T., Liu J., Wang Y., Xie X., Hu S., Pan L.; RT "Mechanistic insights into the interactions of NAP1 with the SKICH domains RT of NDP52 and TAX1BP1."; RL Proc. Natl. Acad. Sci. U.S.A. 115:E11651-E11660(2018). CC -!- FUNCTION: Adapter protein which binds TBK1 and IKBKE playing a role in CC antiviral innate immunity (PubMed:14560022, PubMed:21931631). Activates CC serine/threonine-protein kinase TBK1 and facilitates its CC oligomerization (PubMed:14560022, PubMed:21931631). Enhances the CC phosphorylation of NF-kappa-B p65 subunit RELA by TBK1 CC (PubMed:14560022, PubMed:21931631). Promotes TBK1-induced as well as CC TNF or PMA-induced activation of NF-kappa-B (PubMed:14560022, CC PubMed:21931631). Participates in IFNB promoter activation via TICAM1 CC (PubMed:15611223). {ECO:0000269|PubMed:14560022, CC ECO:0000269|PubMed:15611223, ECO:0000269|PubMed:21931631}. CC -!- SUBUNIT: Homodimer (By similarity). Interacts with IKBKE CC (PubMed:14560022, PubMed:17568778). Interacts with TBK1 CC (PubMed:14560022, PubMed:21931631, PubMed:29251827). Interacts with CC TICAM1 (PubMed:15611223). Interacts with TAX1BP1 (PubMed:30459273). CC Interacts with CALCOCO2 (PubMed:30459273). CC {ECO:0000250|UniProtKB:Q9QYP6, ECO:0000269|PubMed:14560022, CC ECO:0000269|PubMed:15611223, ECO:0000269|PubMed:17568778, CC ECO:0000269|PubMed:21931631, ECO:0000269|PubMed:29251827, CC ECO:0000269|PubMed:30459273}. CC -!- SUBUNIT: (Microbial infection) Interacts with vaccinia virus protein C6 CC (PubMed:21931555). {ECO:0000269|PubMed:21931555}. CC -!- INTERACTION: CC Q9H6S1; Q9UHD2: TBK1; NbExp=7; IntAct=EBI-359973, EBI-356402; CC Q9H6S1; P17362: OPG029; Xeno; NbExp=2; IntAct=EBI-359973, EBI-9519257; CC Q9H6S1; Q9E7P0; Xeno; NbExp=2; IntAct=EBI-359973, EBI-11361108; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14560022}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=Long; CC IsoId=Q9H6S1-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=Q9H6S1-3; Sequence=VSP_023817, VSP_023818; CC Name=3; CC IsoId=Q9H6S1-4; Sequence=VSP_047087, VSP_047090; CC Name=4; CC IsoId=Q9H6S1-5; Sequence=VSP_047088, VSP_047089; CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:14560022). Abundant CC expression seen in the pancreas and testis (PubMed:14560022). CC {ECO:0000269|PubMed:14560022}. CC -!- PTM: Ubiquitinated via 'Lys-48'-linked polyubiquitination by TRIM38, CC leading to its degradation. {ECO:0000250|UniProtKB:Q9QYP6}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY151386; AAO05967.1; -; mRNA. DR EMBL; AF044917; AAF22368.1; -; Genomic_DNA. DR EMBL; AF044918; AAF22369.1; -; Genomic_DNA. DR EMBL; AK025592; BAB15182.1; -; mRNA. DR EMBL; AK290637; BAF83326.1; -; mRNA. DR EMBL; AC092503; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC098616; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW64395.1; -; Genomic_DNA. DR CCDS; CCDS2647.1; -. [Q9H6S1-1] DR CCDS; CCDS46782.1; -. [Q9H6S1-4] DR CCDS; CCDS46783.1; -. [Q9H6S1-5] DR RefSeq; NP_001127904.1; NM_001134432.2. [Q9H6S1-4] DR RefSeq; NP_001127905.1; NM_001134433.2. [Q9H6S1-5] DR RefSeq; NP_071906.1; NM_022461.5. [Q9H6S1-1] DR RefSeq; XP_005265449.1; XM_005265392.4. [Q9H6S1-1] DR RefSeq; XP_047304674.1; XM_047448718.1. [Q9H6S1-1] DR RefSeq; XP_054203514.1; XM_054347539.1. [Q9H6S1-1] DR PDB; 5EP6; X-ray; 1.45 A; A/C=215-255. DR PDB; 5Z7G; X-ray; 2.30 A; C/D=33-75. DR PDB; 5Z7L; X-ray; 2.02 A; C/D=33-75. DR PDB; 7EA2; X-ray; 2.14 A; A/B=6-16. DR PDB; 7EA7; X-ray; 2.69 A; C=6-16. DR PDBsum; 5EP6; -. DR PDBsum; 5Z7G; -. DR PDBsum; 5Z7L; -. DR PDBsum; 7EA2; -. DR PDBsum; 7EA7; -. DR AlphaFoldDB; Q9H6S1; -. DR SMR; Q9H6S1; -. DR BioGRID; 122142; 43. DR ComplexPortal; CPX-6038; TBK1-IKKepsilon-NAP1 complex. DR CORUM; Q9H6S1; -. DR DIP; DIP-27605N; -. DR FunCoup; Q9H6S1; 803. DR IntAct; Q9H6S1; 25. DR MINT; Q9H6S1; -. DR NDEx; IQUERY-CP-AZI2; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000419371; -. DR ChEMBL; CHEMBL4523456; -. DR iPTMnet; Q9H6S1; -. DR MetOSite; Q9H6S1; -. DR PhosphoSitePlus; Q9H6S1; -. DR BioMuta; AZI2; -. DR DMDM; 74718550; -. DR jPOST; Q9H6S1; -. DR MassIVE; Q9H6S1; -. DR PaxDb; 9606-ENSP00000419371; -. DR PeptideAtlas; Q9H6S1; -. DR ProteomicsDB; 43401; -. DR ProteomicsDB; 81026; -. [Q9H6S1-1] DR ProteomicsDB; 81027; -. [Q9H6S1-3] DR ProteomicsDB; 9412; -. DR Pumba; Q9H6S1; -. DR Antibodypedia; 27537; 135 antibodies from 25 providers. DR DNASU; 64343; -. DR Ensembl; ENST00000334100.10; ENSP00000335609.6; ENSG00000163512.15. [Q9H6S1-5] DR Ensembl; ENST00000420543.6; ENSP00000391696.2; ENSG00000163512.15. [Q9H6S1-4] DR Ensembl; ENST00000457172.5; ENSP00000389577.1; ENSG00000163512.15. [Q9H6S1-4] DR Ensembl; ENST00000479665.6; ENSP00000419371.1; ENSG00000163512.15. [Q9H6S1-1] DR Ensembl; ENST00000889265.1; ENSP00000559324.1; ENSG00000163512.15. [Q9H6S1-1] DR Ensembl; ENST00000889266.1; ENSP00000559325.1; ENSG00000163512.15. [Q9H6S1-1] DR Ensembl; ENST00000889267.1; ENSP00000559326.1; ENSG00000163512.15. [Q9H6S1-1] DR Ensembl; ENST00000889268.1; ENSP00000559327.1; ENSG00000163512.15. [Q9H6S1-1] DR Ensembl; ENST00000889269.1; ENSP00000559328.1; ENSG00000163512.15. [Q9H6S1-1] DR Ensembl; ENST00000958176.1; ENSP00000628235.1; ENSG00000163512.15. [Q9H6S1-1] DR Ensembl; ENST00000958177.1; ENSP00000628236.1; ENSG00000163512.15. [Q9H6S1-1] DR Ensembl; ENST00000958179.1; ENSP00000628238.1; ENSG00000163512.15. [Q9H6S1-1] DR GeneID; 64343; -. DR KEGG; hsa:64343; -. DR MANE-Select; ENST00000479665.6; ENSP00000419371.1; NM_022461.5; NP_071906.1. DR UCSC; uc003ceb.5; human. [Q9H6S1-1] DR AGR; HGNC:24002; -. DR ClinPGx; PA134950985; -. DR CTD; 64343; -. DR DisGeNET; 64343; -. DR GeneCards; AZI2; -. DR HGNC; HGNC:24002; AZI2. DR HPA; ENSG00000163512; Low tissue specificity. DR MIM; 609916; gene. DR OpenTargets; ENSG00000163512; -. DR VEuPathDB; HostDB:ENSG00000163512; -. DR eggNOG; ENOG502QV07; Eukaryota. DR GeneTree; ENSGT00940000153704; -. DR InParanoid; Q9H6S1; -. DR OMA; PWPSQSC; -. DR OrthoDB; 8744179at2759; -. DR PAN-GO; Q9H6S1; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q9H6S1; -. DR PathwayCommons; Q9H6S1; -. DR SignaLink; Q9H6S1; -. DR Agora; ENSG00000163512; -. DR BioGRID-ORCS; 64343; 50 hits in 1152 CRISPR screens. DR CD-CODE; E8F4C1F2; Sint speckle. DR ChiTaRS; AZI2; human. DR GeneWiki; AZI2; -. DR GenomeRNAi; 64343; -. DR Pharos; Q9H6S1; Tbio. DR PRO; PR:Q9H6S1; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9H6S1; protein. DR Bgee; ENSG00000163512; Expressed in stromal cell of endometrium and 196 other cell types or tissues. DR ExpressionAtlas; Q9H6S1; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0051607; P:defense response to virus; NAS:ComplexPortal. DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl. DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; NAS:ComplexPortal. DR InterPro; IPR024581; TBD. DR InterPro; IPR051891; TBK1-IKBKE_adapters. DR PANTHER; PTHR14432:SF6; 5-AZACYTIDINE-INDUCED PROTEIN 2; 1. DR PANTHER; PTHR14432; PROSAPIP2 PROTEIN/5-AZACYTIDINE INDUCED GENE 2; 1. DR Pfam; PF12845; TBD; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; KW Host-virus interaction; Phosphoprotein; Proteomics identification; KW Reference proteome; Ubl conjugation. FT CHAIN 1..392 FT /note="5-azacytidine-induced protein 2" FT /id="PRO_0000280602" FT REGION 1..197 FT /note="Homodimerization" FT /evidence="ECO:0000250|UniProtKB:Q9QYP6" FT REGION 216..257 FT /note="Interaction with TBK1 and IKBKE" FT /evidence="ECO:0000269|PubMed:14560022" FT COILED 40..76 FT /evidence="ECO:0000255" FT COILED 102..196 FT /evidence="ECO:0000255" FT MOD_RES 318 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q4KMA0" FT MOD_RES 353 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163" FT VAR_SEQ 216..243 FT /note="SDNMQHAYWELKREMSNLHLVTQVQAEL -> RQSICSTAWSAVAQSWDSMN FT FEDCSLFA (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_047087" FT VAR_SEQ 216..232 FT /note="SDNMQHAYWELKREMSN -> RVSVAQPGVQWRNHGIA (in isoform FT 4)" FT /evidence="ECO:0000305" FT /id="VSP_047088" FT VAR_SEQ 216..228 FT /note="SDNMQHAYWELKR -> TQPGVQWRNHGIA (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_023817" FT VAR_SEQ 229..392 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_023818" FT VAR_SEQ 233..392 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_047089" FT VAR_SEQ 244..392 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_047090" FT STRAND 8..16 FT /evidence="ECO:0007829|PDB:7EA2" FT HELIX 34..72 FT /evidence="ECO:0007829|PDB:5Z7L" FT HELIX 216..246 FT /evidence="ECO:0007829|PDB:5EP6" FT STRAND 247..249 FT /evidence="ECO:0007829|PDB:5EP6" SQ SEQUENCE 392 AA; 44935 MW; EFDBDDA60C5CD624 CRC64; MDALVEDDIC ILNHEKAHKR DTVTPVSIYS GDESVASHFA LVTAYEDIKK RLKDSEKENS LLKKRIRFLE EKLIARFEEE TSSVGREQVN KAYHAYREVC IDRDNLKSKL DKMNKDNSES LKVLNEQLQS KEVELLQLRT EVETQQVMRN LNPPSSNWEV EKLSCDLKIH GLEQELELMR KECSDLKIEL QKAKQTDPYQ EDNLKSRDLQ KLSISSDNMQ HAYWELKREM SNLHLVTQVQ AELLRKLKTS TAIKKACAPV GCSEDLGRDS TKLHLMNFTA TYTRHPPLLP NGKALCHTTS SPLPGDVKVL SEKAILQSWT DNERSIPNDG TCFQEHSSYG RNSLEDNSWV FPSPPKSSET AFGETKTKTL PLPNLPPLHY LDQHNQNCLY KN //