ID TNIP2_HUMAN Reviewed; 429 AA. AC Q8NFZ5; B1AKS4; B3KTY8; D3DVQ9; Q7L5L2; Q9BQR6; Q9H682; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 157. DE RecName: Full=TNFAIP3-interacting protein 2; DE AltName: Full=A20-binding inhibitor of NF-kappa-B activation 2; DE Short=ABIN-2; DE AltName: Full=Fetal liver LKB1-interacting protein; GN Name=TNIP2 {ECO:0000312|EMBL:EAW82514.1}; GN Synonyms=ABIN2, FLIP1 {ECO:0000312|EMBL:AAM21315.1}; 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] {ECO:0000305, ECO:0000312|EMBL:CAC34835.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=11390377; DOI=10.1074/jbc.m100048200; RA Van Huffel S.C., Delaei F., Heyninck K., De Valck D., Beyaert R.; RT "Identification of a novel A20-binding inhibitor of nuclear factor-kappaB RT activation termed ABIN-2."; RL J. Biol. Chem. 276:30216-30223(2001). RN [2] {ECO:0000305, ECO:0000312|EMBL:AAM21315.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND INTERACTION WITH STK11/LKB1. RX PubMed=12595760; DOI=10.1007/bf02256059; RA Liu W.-K., Chien C.-Y., Chou C.-K., Su J.-Y.; RT "An LKB1-interacting protein negatively regulates TNFalpha-induced NF- RT kappaB activation."; RL J. Biomed. Sci. 10:242-252(2003). RN [3] {ECO:0000305, ECO:0000312|EMBL:BAB15382.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP VAL-396. RC TISSUE=Kidney epithelium {ECO:0000312|EMBL:BAB15382.1}; 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] {ECO:0000305, ECO:0000312|EMBL:EAW82514.1} 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [6] {ECO:0000305, ECO:0000312|EMBL:AAH02740.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-396. RC TISSUE=Uterus {ECO:0000312|EMBL:AAH02740.2}; 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 [7] RP INTERACTION WITH TNFAIP3. RX PubMed=11389905; DOI=10.1016/s0014-5793(01)02504-2; RA Klinkenberg M., Van Huffel S., Heyninck K., Beyaert R.; RT "Functional redundancy of the zinc fingers of A20 for inhibition of NF- RT kappaB activation and protein-protein interactions."; RL FEBS Lett. 498:93-97(2001). RN [8] RP FUNCTION. RX PubMed=12933576; DOI=10.1182/blood-2003-05-1602; RA Tadros A., Hughes D.P., Dunmore B.J., Brindle N.P.; RT "ABIN-2 protects endothelial cells from death and has a role in the RT antiapoptotic effect of angiopoietin-1."; RL Blood 102:4407-4409(2003). RN [9] RP INTERACTION WITH TEK. RX PubMed=12609966; DOI=10.1161/01.res.0000063422.38690.dc; RA Hughes D.P., Marron M.B., Brindle N.P.; RT "The antiinflammatory endothelial tyrosine kinase Tie2 interacts with a RT novel nuclear factor-kappaB inhibitor ABIN-2."; RL Circ. Res. 92:630-636(2003). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SMARCD1. RX PubMed=12753905; DOI=10.1016/s0014-5793(03)00401-0; RA Chien C.Y., Liu W.K., Chou C.K., Su J.Y.; RT "The A20-binding protein ABIN-2 exerts unexpected function in mediating RT transcriptional coactivation."; RL FEBS Lett. 543:55-60(2003). RN [11] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH IKBKG. RX PubMed=14653779; DOI=10.1042/bj20031736; RA Liu W.-K., Yen P.-F., Chien C.-Y., Fann M.-J., Su J.-Y., Chou C.-K.; RT "The inhibitor ABIN-2 disrupts the interaction of receptor-interacting RT protein with the kinase subunit IKKgamma to block activation of the RT transcription factor NF-kappaB and potentiate apoptosis."; RL Biochem. J. 378:867-876(2004). RN [12] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH NFKB1; MAP3K8 AND TNFAIP3. RX PubMed=15169888; DOI=10.1128/mcb.24.12.5235-5248.2004; RA Lang V., Symons A., Watton S.J., Janzen J., Soneji Y., Beinke S., RA Howell S., Ley S.C.; RT "ABIN-2 forms a ternary complex with TPL-2 and NF-kappa B1 p105 and is RT essential for TPL-2 protein stability."; RL Mol. Cell. Biol. 24:5235-5248(2004). RN [13] RP UBIQUITIN-BINDING, AND MUTAGENESIS OF 309-ASP-PHE-310 AND 313-GLU-ARG-314. RX PubMed=18212736; DOI=10.1038/sj.onc.1211042; RA Wagner S., Carpentier I., Rogov V., Kreike M., Ikeda F., Lohr F., Wu C.J., RA Ashwell J.D., Dotsch V., Dikic I., Beyaert R.; RT "Ubiquitin binding mediates the NF-kappaB inhibitory potential of ABIN RT proteins."; RL Oncogene 27:3739-3745(2008). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHUK AND IKBKB, RP UBIQUITINATION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-62 AND SER-146. RX PubMed=21784860; DOI=10.1074/jbc.m111.236448; RA Leotoing L., Chereau F., Baron S., Hube F., Valencia H.J., Bordereaux D., RA Demmers J.A., Strouboulis J., Baud V.; RT "A20-binding inhibitor of nuclear factor-kappaB (NF-kappaB)-2 (ABIN-2) is RT an activator of inhibitor of NF-kappaB (IkappaB) kinase alpha (IKKalpha)- RT mediated NF-kappaB transcriptional activity."; RL J. Biol. Chem. 286:32277-32288(2011). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS RP 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 [17] RP FUNCTION, AND DEUBIQUITINATION BY USP35. RX PubMed=26348204; DOI=10.18632/oncotarget.4451; RA Liu C., Wang L., Chen W., Zhao S., Yin C., Lin Y., Jiang A., Zhang P.; RT "USP35 activated by miR let-7a inhibits cell proliferation and NF-kappaB RT activation through stabilization of ABIN-2."; RL Oncotarget 6:27891-27906(2015). RN [18] RP INTERACTION WITH SFTSV VIRUS NSS (MICROBIAL INFECTION). RX PubMed=30617349; DOI=10.1038/s41564-018-0329-x; RA Choi Y., Park S.J., Sun Y., Yoo J.S., Pudupakam R.S., Foo S.S., Shin W.J., RA Chen S.B., Tsichlis P.N., Lee W.J., Lee J.S., Li W., Brennan B., Choi Y.K., RA Jung J.U.; RT "Severe fever with thrombocytopenia syndrome phlebovirus non-structural RT protein activates TPL2 signalling pathway for viral immunopathogenesis."; RL Nat. Microbiol. 4:429-437(2019). RN [19] RP VARIANTS HIS-249 AND LYS-255, INTERACTION WITH TNFAIP3, AND RP CHARACTERIZATION OF VARIANT LYS-255. RX PubMed=21266526; DOI=10.1158/1078-0432.ccr-10-1859; RA Dong G., Chanudet E., Zeng N., Appert A., Chen Y.W., Au W.Y., Hamoudi R.A., RA Watkins A.J., Ye H., Liu H., Gao Z., Chuang S.S., Srivastava G., Du M.Q.; RT "A20, ABIN-1/2, and CARD11 mutations and their prognostic value in RT gastrointestinal diffuse large B-cell lymphoma."; RL Clin. Cancer Res. 17:1440-1451(2011). CC -!- FUNCTION: Inhibits NF-kappa-B activation by blocking the interaction of CC RIPK1 with its downstream effector NEMO/IKBKG. Forms a ternary complex CC with NFKB1 and MAP3K8 but appears to function upstream of MAP3K8 in the CC TLR4 signaling pathway that regulates MAP3K8 activation. Involved in CC activation of the MEK/ERK signaling pathway during innate immune CC response; this function seems to be stimulus- and cell type specific. CC Required for stability of MAP3K8. Involved in regulation of apoptosis CC in endothelial cells; promotes TEK agonist-stimulated endothelial CC survival. May act as transcriptional coactivator when translocated to CC the nucleus. Enhances CHUK-mediated NF-kappa-B activation involving NF- CC kappa-B p50-p65 and p50-c-Rel complexes. {ECO:0000269|PubMed:11389905, CC ECO:0000269|PubMed:12595760, ECO:0000269|PubMed:12753905, CC ECO:0000269|PubMed:12933576, ECO:0000269|PubMed:14653779, CC ECO:0000269|PubMed:15169888, ECO:0000269|PubMed:21784860}. CC -!- SUBUNIT: Interacts with STK11/LKB1, TNFAIP3, IKBKG, NFKB1, MAP3K8, TEK, CC RIPK1, CHUK, IKBKB and SMARCD1. Interacts with polyubiquitin. CC {ECO:0000269|PubMed:11389905, ECO:0000269|PubMed:12595760, CC ECO:0000269|PubMed:12609966, ECO:0000269|PubMed:12753905, CC ECO:0000269|PubMed:14653779, ECO:0000269|PubMed:15169888, CC ECO:0000269|PubMed:21266526, ECO:0000269|PubMed:21784860}. CC -!- SUBUNIT: (Microbial infection) Interacts with severe fever with CC thrombocytopenia syndrome virus (SFTSV) NSs; this interaction promotes CC TPL2 complex formation and signaling activity leading to IL-10 CC production. {ECO:0000269|PubMed:30617349}. CC -!- INTERACTION: CC Q8NFZ5; Q9Y6K9: IKBKG; NbExp=8; IntAct=EBI-359372, EBI-81279; CC Q8NFZ5; P41279: MAP3K8; NbExp=10; IntAct=EBI-359372, EBI-354900; CC Q8NFZ5; P19838: NFKB1; NbExp=7; IntAct=EBI-359372, EBI-300010; CC Q8NFZ5; P19838-1: NFKB1; NbExp=8; IntAct=EBI-359372, EBI-1452239; CC Q8NFZ5; Q04864: REL; NbExp=2; IntAct=EBI-359372, EBI-307352; CC Q8NFZ5; Q15831: STK11; NbExp=5; IntAct=EBI-359372, EBI-306838; CC Q8NFZ5; P21580: TNFAIP3; NbExp=4; IntAct=EBI-359372, EBI-527670; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12595760}. Nucleus CC {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1 {ECO:0000269|PubMed:11390377, ECO:0000269|PubMed:12595760, CC ECO:0000269|PubMed:15489334}; CC IsoId=Q8NFZ5-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:14702039}; CC IsoId=Q8NFZ5-2; Sequence=VSP_052701; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined. CC {ECO:0000269|PubMed:12595760}. CC -!- PTM: In vitro phosphorylated by CHUK. {ECO:0000269|PubMed:21784860}. CC -!- PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination CC probably leading to constitutive proteasomal degradation which can be CC impaired by IKK-A/CHUK or IKBKB probably involving deubiquitination CC (PubMed:21784860). Deubiquitinated by USP35; leading to stabilization CC and inhibition of TNFalpha-induced NF-kappa-B activation CC (PubMed:26348204). {ECO:0000269|PubMed:21784860, CC ECO:0000269|PubMed:26348204}. 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; AJ304866; CAC34835.1; -; mRNA. DR EMBL; AF372839; AAM21315.1; -; mRNA. DR EMBL; AK026176; BAB15382.1; -; mRNA. DR EMBL; AK096296; BAG53250.1; -; mRNA. DR EMBL; CH471131; EAW82514.1; -; Genomic_DNA. DR EMBL; AL121750; CAM28233.1; -; Genomic_DNA. DR EMBL; AL110117; CAM28233.1; JOINED; Genomic_DNA. DR EMBL; CH471131; EAW82516.1; -; Genomic_DNA. DR EMBL; BC002740; AAH02740.2; -; mRNA. DR CCDS; CCDS3362.1; -. [Q8NFZ5-1] DR CCDS; CCDS54714.1; -. [Q8NFZ5-2] DR RefSeq; NP_001154999.1; NM_001161527.1. [Q8NFZ5-2] DR RefSeq; NP_001278945.1; NM_001292016.1. DR RefSeq; NP_077285.3; NM_024309.3. [Q8NFZ5-1] DR PDB; 5H07; X-ray; 2.59 A; C/D=257-344. DR PDBsum; 5H07; -. DR AlphaFoldDB; Q8NFZ5; -. DR SMR; Q8NFZ5; -. DR BioGRID; 122573; 953. DR CORUM; Q8NFZ5; -. DR DIP; DIP-27617N; -. DR IntAct; Q8NFZ5; 94. DR MINT; Q8NFZ5; -. DR STRING; 9606.ENSP00000321203; -. DR GlyGen; Q8NFZ5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8NFZ5; -. DR PhosphoSitePlus; Q8NFZ5; -. DR BioMuta; TNIP2; -. DR DMDM; 74715616; -. DR EPD; Q8NFZ5; -. DR jPOST; Q8NFZ5; -. DR MassIVE; Q8NFZ5; -. DR MaxQB; Q8NFZ5; -. DR PaxDb; 9606-ENSP00000321203; -. DR PeptideAtlas; Q8NFZ5; -. DR ProteomicsDB; 73398; -. [Q8NFZ5-1] DR ProteomicsDB; 73399; -. [Q8NFZ5-2] DR Pumba; Q8NFZ5; -. DR Antibodypedia; 22391; 261 antibodies from 27 providers. DR DNASU; 79155; -. DR Ensembl; ENST00000315423.12; ENSP00000321203.7; ENSG00000168884.15. [Q8NFZ5-1] DR Ensembl; ENST00000510267.5; ENSP00000427613.1; ENSG00000168884.15. [Q8NFZ5-2] DR GeneID; 79155; -. DR KEGG; hsa:79155; -. DR MANE-Select; ENST00000315423.12; ENSP00000321203.7; NM_024309.4; NP_077285.3. DR UCSC; uc003gff.3; human. [Q8NFZ5-1] DR AGR; HGNC:19118; -. DR CTD; 79155; -. DR DisGeNET; 79155; -. DR GeneCards; TNIP2; -. DR HGNC; HGNC:19118; TNIP2. DR HPA; ENSG00000168884; Low tissue specificity. DR MIM; 610669; gene. DR neXtProt; NX_Q8NFZ5; -. DR OpenTargets; ENSG00000168884; -. DR PharmGKB; PA134957006; -. DR VEuPathDB; HostDB:ENSG00000168884; -. DR eggNOG; ENOG502QUCD; Eukaryota. DR GeneTree; ENSGT00510000046908; -. DR HOGENOM; CLU_039735_1_0_1; -. DR InParanoid; Q8NFZ5; -. DR OMA; CMRFFND; -. DR OrthoDB; 5353272at2759; -. DR PhylomeDB; Q8NFZ5; -. DR TreeFam; TF332167; -. DR PathwayCommons; Q8NFZ5; -. DR Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation. DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases. DR SignaLink; Q8NFZ5; -. DR SIGNOR; Q8NFZ5; -. DR BioGRID-ORCS; 79155; 20 hits in 1167 CRISPR screens. DR ChiTaRS; TNIP2; human. DR GeneWiki; TNIP2; -. DR GenomeRNAi; 79155; -. DR Pharos; Q8NFZ5; Tbio. DR PRO; PR:Q8NFZ5; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q8NFZ5; Protein. DR Bgee; ENSG00000168884; Expressed in tendon of biceps brachii and 201 other cell types or tissues. DR ExpressionAtlas; Q8NFZ5; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0023035; P:CD40 signaling pathway; ISS:UniProtKB. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISS:UniProtKB. DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:UniProtKB. DR GO; GO:0050871; P:positive regulation of B cell activation; ISS:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IDA:UniProtKB. DR GO; GO:0043032; P:positive regulation of macrophage activation; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; ISS:UniProtKB. DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; ISS:UniProtKB. DR GO; GO:0034162; P:toll-like receptor 9 signaling pathway; ISS:UniProtKB. DR Gene3D; 1.20.5.990; Nemo cc2-lz domain - 1d5 darpin complex; 1. DR InterPro; IPR022008; EABR. DR InterPro; IPR034735; NEMO_ZF. DR PANTHER; PTHR31882:SF12; TNFAIP3-INTERACTING PROTEIN 2; 1. DR PANTHER; PTHR31882; TNFAIP3-INTERACTING PROTEIN COILED COIL FAMILY MEMBER; 1. DR Pfam; PF12180; EABR; 1. DR PROSITE; PS51801; ZF_CCHC_NOA; 1. DR Genevisible; Q8NFZ5; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Coiled coil; Cytoplasm; KW Host-virus interaction; Inflammatory response; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..429 FT /note="TNFAIP3-interacting protein 2" FT /id="PRO_0000322583" FT ZN_FING 397..429 FT /note="CCHC NOA-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142" FT REGION 177..199 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 289..347 FT /note="Ubiquitin-binding domain (UBD)" FT REGION 372..400 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 29..117 FT /evidence="ECO:0000255" FT COILED 196..226 FT /evidence="ECO:0000255" FT COILED 255..340 FT /evidence="ECO:0000255" FT COMPBIAS 177..192 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 405 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142" FT BINDING 408 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142" FT BINDING 423 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142" FT BINDING 427 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..107 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_052701" FT VARIANT 249 FT /note="Q -> H (found in patients with gastrointestinal FT diffuse large cell lymphoma; impairs inhibitory activity on FT CARD11-induced NF-kappa-B activation; dbSNP:rs116129895)" FT /evidence="ECO:0000269|PubMed:21266526" FT /id="VAR_067969" FT VARIANT 255 FT /note="E -> K (found in patients with gastrointestinal FT diffuse large cell lymphoma; somatic mutation; impairs FT inhibitory activity on CARD11-induced NF-kappa-B activation FT and impairs interaction with TNFAIP3; dbSNP:rs116412781)" FT /evidence="ECO:0000269|PubMed:21266526" FT /id="VAR_067970" FT VARIANT 396 FT /note="A -> V (in dbSNP:rs2269495)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_039463" FT MUTAGEN 62 FT /note="S->A: Reduces phosphorylation." FT /evidence="ECO:0000269|PubMed:21784860" FT MUTAGEN 146 FT /note="S->A: Reduces phosphorylation; reduces CHUK-mediated FT NF-kappa-B activation." FT /evidence="ECO:0000269|PubMed:21784860" FT MUTAGEN 309..310 FT /note="DF->NA: Abolishes ubiquitin binding." FT /evidence="ECO:0000269|PubMed:18212736" FT MUTAGEN 313..314 FT /note="ER->AA: Abolishes ubiquitin binding; loss of FT inhibitory activity on NF-kappa-B activation." FT /evidence="ECO:0000269|PubMed:18212736" FT CONFLICT 153 FT /note="Q -> H (in Ref. 1; CAC34835)" FT /evidence="ECO:0000305" FT HELIX 263..273 FT /evidence="ECO:0007829|PDB:5H07" FT HELIX 276..336 FT /evidence="ECO:0007829|PDB:5H07" SQ SEQUENCE 429 AA; 48700 MW; 0F6B049C2B3483DC CRC64; MSRDPGSGGW EEAPRAAAAL CTLYHEAGQR LRRLQDQLAA RDALIARLRA RLAALEGDAA PSLVDALLEQ VARFREQLRR QEGGAAEAQM RQEIERLTER LEEKEREMQQ LLSQPQHERE KEVVLLRRSM AEGERARAAS DVLCRSLANE THQLRRTLTA TAHMCQHLAK CLDERQHAQR NVGERSPDQS EHTDGHTSVQ SVIEKLQEEN RLLKQKVTHV EDLNAKWQRY NASRDEYVRG LHAQLRGLQI PHEPELMRKE ISRLNRQLEE KINDCAEVKQ ELAASRTARD AALERVQMLE QQILAYKDDF MSERADRERA QSRIQELEEK VASLLHQVSW RQDSREPDAG RIHAGSKTAK YLAADALELM VPGGWRPGTG SQQPEPPAEG GHPGAAQRGQ GDLQCPHCLQ CFSDEQGEEL LRHVAECCQ //