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TNFAIP3-interacting protein 2 (A20-binding inhibitor of NF-kappa-B activation 2) (ABIN-2) (Fetal liver LKB1-interacting protein)

 TNIP2_HUMAN             Reviewed;         429 AA.
Q8NFZ5; B1AKS4; B3KTY8; D3DVQ9; Q7L5L2; Q9BQR6; Q9H682;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
12-SEP-2018, entry version 125.
RecName: Full=TNFAIP3-interacting protein 2;
AltName: Full=A20-binding inhibitor of NF-kappa-B activation 2;
Short=ABIN-2;
AltName: Full=Fetal liver LKB1-interacting protein;
Name=TNIP2 {ECO:0000312|EMBL:EAW82514.1};
Synonyms=ABIN2, FLIP1 {ECO:0000312|EMBL:AAM21315.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:CAC34835.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11390377; DOI=10.1074/jbc.M100048200;
Van Huffel S.C., Delaei F., Heyninck K., De Valck D., Beyaert R.;
"Identification of a novel A20-binding inhibitor of nuclear factor-
kappaB activation termed ABIN-2.";
J. Biol. Chem. 276:30216-30223(2001).
[2] {ECO:0000305, ECO:0000312|EMBL:AAM21315.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH STK11/LKB1.
PubMed=12595760; DOI=10.1007/BF02256059;
Liu W.-K., Chien C.-Y., Chou C.-K., Su J.-Y.;
"An LKB1-interacting protein negatively regulates TNFalpha-induced NF-
kappaB activation.";
J. Biomed. Sci. 10:242-252(2003).
[3] {ECO:0000305, ECO:0000312|EMBL:BAB15382.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
VAL-396.
TISSUE=Kidney epithelium {ECO:0000312|EMBL:BAB15382.1};
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4] {ECO:0000305, ECO:0000312|EMBL:EAW82514.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6] {ECO:0000305, ECO:0000312|EMBL:AAH02740.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
VAL-396.
TISSUE=Uterus {ECO:0000312|EMBL:AAH02740.2};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH TNFAIP3.
PubMed=11389905; DOI=10.1016/S0014-5793(01)02504-2;
Klinkenberg M., Van Huffel S., Heyninck K., Beyaert R.;
"Functional redundancy of the zinc fingers of A20 for inhibition of
NF-kappaB activation and protein-protein interactions.";
FEBS Lett. 498:93-97(2001).
[8]
FUNCTION.
PubMed=12933576; DOI=10.1182/blood-2003-05-1602;
Tadros A., Hughes D.P., Dunmore B.J., Brindle N.P.;
"ABIN-2 protects endothelial cells from death and has a role in the
antiapoptotic effect of angiopoietin-1.";
Blood 102:4407-4409(2003).
[9]
INTERACTION WITH TEK.
PubMed=12609966; DOI=10.1161/01.RES.0000063422.38690.DC;
Hughes D.P., Marron M.B., Brindle N.P.;
"The antiinflammatory endothelial tyrosine kinase Tie2 interacts with
a novel nuclear factor-kappaB inhibitor ABIN-2.";
Circ. Res. 92:630-636(2003).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SMARCD1.
PubMed=12753905; DOI=10.1016/S0014-5793(03)00401-0;
Chien C.Y., Liu W.K., Chou C.K., Su J.Y.;
"The A20-binding protein ABIN-2 exerts unexpected function in
mediating transcriptional coactivation.";
FEBS Lett. 543:55-60(2003).
[11] {ECO:0000305}
FUNCTION, AND INTERACTION WITH IKBKG.
PubMed=14653779; DOI=10.1042/BJ20031736;
Liu W.-K., Yen P.-F., Chien C.-Y., Fann M.-J., Su J.-Y., Chou C.-K.;
"The inhibitor ABIN-2 disrupts the interaction of receptor-interacting
protein with the kinase subunit IKKgamma to block activation of the
transcription factor NF-kappaB and potentiate apoptosis.";
Biochem. J. 378:867-876(2004).
[12] {ECO:0000305}
FUNCTION, AND INTERACTION WITH NFKB1; MAP3K8 AND TNFAIP3.
PubMed=15169888; DOI=10.1128/MCB.24.12.5235-5248.2004;
Lang V., Symons A., Watton S.J., Janzen J., Soneji Y., Beinke S.,
Howell S., Ley S.C.;
"ABIN-2 forms a ternary complex with TPL-2 and NF-kappa B1 p105 and is
essential for TPL-2 protein stability.";
Mol. Cell. Biol. 24:5235-5248(2004).
[13]
UBIQUITIN-BINDING, AND MUTAGENESIS OF 309-ASP-PHE-310 AND
313-GLU-ARG-314.
PubMed=18212736; DOI=10.1038/sj.onc.1211042;
Wagner S., Carpentier I., Rogov V., Kreike M., Ikeda F., Lohr F.,
Wu C.J., Ashwell J.D., Dotsch V., Dikic I., Beyaert R.;
"Ubiquitin binding mediates the NF-kappaB inhibitory potential of ABIN
proteins.";
Oncogene 27:3739-3745(2008).
[14]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHUK AND IKBKB,
UBIQUITINATION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-62 AND
SER-146.
PubMed=21784860; DOI=10.1074/jbc.M111.236448;
Leotoing L., Chereau F., Baron S., Hube F., Valencia H.J.,
Bordereaux D., Demmers J.A., Strouboulis J., Baud V.;
"A20-binding inhibitor of nuclear factor-kappaB (NF-kappaB)-2 (ABIN-2)
is an activator of inhibitor of NF-kappaB (IkappaB) kinase alpha
(IKKalpha)-mediated NF-kappaB transcriptional activity.";
J. Biol. Chem. 286:32277-32288(2011).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
VARIANTS HIS-249 AND LYS-255, INTERACTION WITH TNFAIP3, AND
CHARACTERIZATION OF VARIANT LYS-255.
PubMed=21266526; DOI=10.1158/1078-0432.CCR-10-1859;
Dong G., Chanudet E., Zeng N., Appert A., Chen Y.W., Au W.Y.,
Hamoudi R.A., Watkins A.J., Ye H., Liu H., Gao Z., Chuang S.S.,
Srivastava G., Du M.Q.;
"A20, ABIN-1/2, and CARD11 mutations and their prognostic value in
gastrointestinal diffuse large B-cell lymphoma.";
Clin. Cancer Res. 17:1440-1451(2011).
-!- FUNCTION: Inhibits NF-kappa-B activation by blocking the
interaction of RIPK1 with its downstream effector NEMO/IKBKG.
Forms a ternary complex with NFKB1 and MAP3K8 but appears to
function upstream of MAP3K8 in the TLR4 signaling pathway that
regulates MAP3K8 activation. Involved in activation of the MEK/ERK
signaling pathway during innate immune response; this function
seems to be stimulus- and cell type specific. Required for
stability of MAP3K8. Involved in regulation of apoptosis in
endothelial cells; promotes TEK agonist-stimulated endothelial
survival. May act as transcriptional coactivator when translocated
to the nucleus. Enhances CHUK-mediated NF-kappa-B activation
involving NF-kappa-B p50-p65 and p50-c-Rel complexes.
{ECO:0000269|PubMed:12595760, ECO:0000269|PubMed:12753905,
ECO:0000269|PubMed:12933576, ECO:0000269|PubMed:14653779,
ECO:0000269|PubMed:15169888, ECO:0000269|PubMed:21784860}.
-!- SUBUNIT: Interacts with STK11/LKB1, TNFAIP3, IKBKG, NFKB1, MAP3K8,
TEK, RIPK1, CHUK, IKBKB and SMARCD1. Interacts with polyubiquitin.
{ECO:0000269|PubMed:11389905, ECO:0000269|PubMed:12595760,
ECO:0000269|PubMed:12609966, ECO:0000269|PubMed:12753905,
ECO:0000269|PubMed:14653779, ECO:0000269|PubMed:15169888,
ECO:0000269|PubMed:21266526, ECO:0000269|PubMed:21784860}.
-!- INTERACTION:
Q9Y6K9:IKBKG; NbExp=6; IntAct=EBI-359372, EBI-81279;
P41279:MAP3K8; NbExp=10; IntAct=EBI-359372, EBI-354900;
P19838:NFKB1; NbExp=5; IntAct=EBI-359372, EBI-300010;
P19838-1:NFKB1; NbExp=8; IntAct=EBI-359372, EBI-1452239;
Q15831:STK11; NbExp=5; IntAct=EBI-359372, EBI-306838;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12595760}.
Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:11390377, ECO:0000269|PubMed:12595760,
ECO:0000269|PubMed:15489334};
IsoId=Q8NFZ5-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:14702039};
IsoId=Q8NFZ5-2; Sequence=VSP_052701;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues
examined. {ECO:0000269|PubMed:12595760}.
-!- PTM: In vitro phosphorylated by CHUK.
{ECO:0000269|PubMed:21784860}.
-!- PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination
probably leading to constitutive proteasomal degradation which can
be impaired by IKK-A/CHUK or IKBKB probably involving
deubiquitination. {ECO:0000269|PubMed:21784860}.
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EMBL; AJ304866; CAC34835.1; -; mRNA.
EMBL; AF372839; AAM21315.1; -; mRNA.
EMBL; AK026176; BAB15382.1; -; mRNA.
EMBL; AK096296; BAG53250.1; -; mRNA.
EMBL; CH471131; EAW82514.1; -; Genomic_DNA.
EMBL; AL121750; CAM28233.1; -; Genomic_DNA.
EMBL; AL110117; CAM28233.1; JOINED; Genomic_DNA.
EMBL; CH471131; EAW82516.1; -; Genomic_DNA.
EMBL; BC002740; AAH02740.2; -; mRNA.
CCDS; CCDS3362.1; -. [Q8NFZ5-1]
CCDS; CCDS54714.1; -. [Q8NFZ5-2]
RefSeq; NP_001154999.1; NM_001161527.1. [Q8NFZ5-2]
RefSeq; NP_001278945.1; NM_001292016.1.
RefSeq; NP_077285.3; NM_024309.3. [Q8NFZ5-1]
UniGene; Hs.368551; -.
PDB; 5H07; X-ray; 2.59 A; C/D=257-344.
PDBsum; 5H07; -.
ProteinModelPortal; Q8NFZ5; -.
SMR; Q8NFZ5; -.
BioGrid; 122573; 35.
CORUM; Q8NFZ5; -.
DIP; DIP-27617N; -.
IntAct; Q8NFZ5; 20.
MINT; Q8NFZ5; -.
STRING; 9606.ENSP00000321203; -.
iPTMnet; Q8NFZ5; -.
PhosphoSitePlus; Q8NFZ5; -.
BioMuta; TNIP2; -.
DMDM; 74715616; -.
EPD; Q8NFZ5; -.
MaxQB; Q8NFZ5; -.
PaxDb; Q8NFZ5; -.
PeptideAtlas; Q8NFZ5; -.
PRIDE; Q8NFZ5; -.
ProteomicsDB; 73398; -.
ProteomicsDB; 73399; -. [Q8NFZ5-2]
Ensembl; ENST00000315423; ENSP00000321203; ENSG00000168884. [Q8NFZ5-1]
Ensembl; ENST00000510267; ENSP00000427613; ENSG00000168884. [Q8NFZ5-2]
GeneID; 79155; -.
KEGG; hsa:79155; -.
UCSC; uc003gff.3; human. [Q8NFZ5-1]
CTD; 79155; -.
DisGeNET; 79155; -.
EuPathDB; HostDB:ENSG00000168884.14; -.
GeneCards; TNIP2; -.
H-InvDB; HIX0164015; -.
HGNC; HGNC:19118; TNIP2.
HPA; CAB020818; -.
HPA; HPA049886; -.
HPA; HPA063197; -.
MIM; 610669; gene.
neXtProt; NX_Q8NFZ5; -.
OpenTargets; ENSG00000168884; -.
PharmGKB; PA134957006; -.
eggNOG; ENOG410IEB1; Eukaryota.
eggNOG; ENOG410XRZP; LUCA.
GeneTree; ENSGT00390000009019; -.
HOGENOM; HOG000049046; -.
HOVERGEN; HBG055553; -.
InParanoid; Q8NFZ5; -.
OMA; FKSERAD; -.
OrthoDB; EOG091G0JC8; -.
PhylomeDB; Q8NFZ5; -.
TreeFam; TF332167; -.
Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
SignaLink; Q8NFZ5; -.
SIGNOR; Q8NFZ5; -.
GeneWiki; TNIP2; -.
GenomeRNAi; 79155; -.
PRO; PR:Q8NFZ5; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000168884; Expressed in 222 organ(s), highest expression level in left coronary artery.
CleanEx; HS_TNIP2; -.
ExpressionAtlas; Q8NFZ5; baseline and differential.
Genevisible; Q8NFZ5; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0023035; P:CD40 signaling pathway; ISS:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISS:UniProtKB.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:UniProtKB.
GO; GO:0050871; P:positive regulation of B cell activation; ISS:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0043032; P:positive regulation of macrophage activation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0051403; P:stress-activated MAPK cascade; TAS:Reactome.
GO; GO:0034134; P:toll-like receptor 2 signaling pathway; ISS:UniProtKB.
GO; GO:0034138; P:toll-like receptor 3 signaling pathway; ISS:UniProtKB.
GO; GO:0034162; P:toll-like receptor 9 signaling pathway; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR032419; CC2-LZ_dom.
InterPro; IPR022008; EABR.
InterPro; IPR034735; NEMO_ZF.
Pfam; PF16516; CC2-LZ; 1.
Pfam; PF12180; EABR; 1.
PROSITE; PS51801; ZF_CCHC_NOA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Coiled coil;
Complete proteome; Cytoplasm; Inflammatory response; Metal-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 429 TNFAIP3-interacting protein 2.
/FTId=PRO_0000322583.
ZN_FING 397 429 CCHC NOA-type. {ECO:0000255|PROSITE-
ProRule:PRU01142}.
REGION 289 347 Ubiquitin-binding domain (UBD).
COILED 29 117 {ECO:0000255}.
COILED 196 226 {ECO:0000255}.
COILED 255 340 {ECO:0000255}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 107 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_052701.
VARIANT 249 249 Q -> H (found in patients with
gastrointestinal diffuse large cell
lymphoma; impairs inhibitory activity on
CARD11-induced NF-kappa-B activation;
dbSNP:rs116129895).
{ECO:0000269|PubMed:21266526}.
/FTId=VAR_067969.
VARIANT 255 255 E -> K (found in patients with
gastrointestinal diffuse large cell
lymphoma; somatic mutation; impairs
inhibitory activity on CARD11-induced NF-
kappa-B activation and impairs
interaction with TNFAIP3;
dbSNP:rs116412781).
{ECO:0000269|PubMed:21266526}.
/FTId=VAR_067970.
VARIANT 396 396 A -> V (in dbSNP:rs2269495).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_039463.
MUTAGEN 62 62 S->A: Reduces phosphorylation.
{ECO:0000269|PubMed:21784860}.
MUTAGEN 146 146 S->A: Reduces phosphorylation; reduces
CHUK-mediated NF-kappa-B activation.
{ECO:0000269|PubMed:21784860}.
MUTAGEN 309 310 DF->NA: Abolishes ubiquitin binding.
{ECO:0000269|PubMed:18212736}.
MUTAGEN 313 314 ER->AA: Abolishes ubiquitin binding; loss
of inhibitory activity on NF-kappa-B
activation.
{ECO:0000269|PubMed:18212736}.
CONFLICT 153 153 Q -> H (in Ref. 1; CAC34835).
{ECO:0000305}.
HELIX 263 273 {ECO:0000244|PDB:5H07}.
HELIX 276 336 {ECO:0000244|PDB:5H07}.
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


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