TNIP1_HUMAN
ID TNIP1_HUMAN Reviewed; 636 AA.
AC Q15025; A4F1W8; A4F1W9; A4F1X2; A4F1X4; A4F1X5; A4F1X6; A4F1X7; A4F1X9;
AC B7Z699; E7EPY1; E7ET96; O76008; Q05KP3; Q05KP4; Q6N077; Q96EL9; Q99833;
AC Q9H1J3;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=TNFAIP3-interacting protein 1;
DE AltName: Full=A20-binding inhibitor of NF-kappa-B activation 1;
DE Short=ABIN-1;
DE AltName: Full=HIV-1 Nef-interacting protein;
DE AltName: Full=Nef-associated factor 1;
DE Short=Naf1;
DE AltName: Full=Nip40-1;
DE AltName: Full=Virion-associated nuclear shuttling protein;
DE Short=VAN;
DE Short=hVAN;
GN Name=TNIP1; Synonyms=KIAA0113, NAF1;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Peripheral blood;
RX PubMed=9923610; DOI=10.1016/s0014-5793(98)01631-7;
RA Fukushi M., Dixon J., Kimura T., Tsurutani N., Dixon M.J., Yamamoto N.;
RT "Identification and cloning of a novel cellular protein Naf1, Nef-
RT associated factor 1, that increases cell surface CD4 expression.";
RL FEBS Lett. 442:83-88(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Leukocyte;
RX PubMed=11090181; DOI=10.1128/jvi.74.24.11811-11824.2000;
RA Gupta K., Ott D., Hope T.J., Siliciano R.F., Boeke J.D.;
RT "A human nuclear shuttling protein that interacts with human
RT immunodeficiency virus type 1 matrix is packaged into virions.";
RL J. Virol. 74:11811-11824(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8),
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=17016622;
RA Shiote Y., Ouchida M., Jitsumori Y., Ogama Y., Matsuo Y., Ishimaru F.,
RA Tanimoto M., Shimizu K.;
RT "Multiple splicing variants of Naf1/ABIN-1 transcripts and their
RT alterations in hematopoietic tumors.";
RL Int. J. Mol. Med. 18:917-923(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Colon endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 136-636 (ISOFORM 2).
RC TISSUE=Craniofacial;
RX PubMed=8681136; DOI=10.1101/gr.6.1.26;
RA Loftus S.K., Dixon J., Koprivnikar K., Dixon M.J., Wasmuth J.J.;
RT "Transcriptional map of the Treacher Collins candidate gene region.";
RL Genome Res. 6:26-34(1996).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 94-412.
RA Fukushi M., Kimura T., Yamamoto N.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP FUNCTION, AND INTERACTION WITH MAPK1.
RX PubMed=12220502; DOI=10.1016/s0006-291x(02)02086-7;
RA Zhang S., Fukushi M., Hashimoto S., Gao C., Huang L., Fukuyo Y.,
RA Nakajima T., Amagasa T., Enomoto S., Koike K., Miura O., Yamamoto N.,
RA Tsuchida N.;
RT "A new ERK2 binding protein, Naf1, attenuates the EGF/ERK2 nuclear
RT signaling.";
RL Biochem. Biophys. Res. Commun. 297:17-23(2002).
RN [14]
RP FUNCTION, AND INTERACTION WITH IKBKG AND TNFAIP3.
RX PubMed=16684768; DOI=10.1074/jbc.m601502200;
RA Mauro C., Pacifico F., Lavorgna A., Mellone S., Iannetti A., Acquaviva R.,
RA Formisano S., Vito P., Leonardi A.;
RT "ABIN-1 binds to NEMO/IKKgamma and co-operates with A20 in inhibiting NF-
RT kappaB.";
RL J. Biol. Chem. 281:18482-18488(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, 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 [16]
RP FUNCTION, INTERACTION WITH SELPLG AND PIK3CD, PHOSPHORYLATION AT TYR-552,
RP AND MUTAGENESIS OF TYR-552.
RX PubMed=17632516; DOI=10.1038/ni1491;
RA Wang H.B., Wang J.T., Zhang L., Geng Z.H., Xu W.L., Xu T., Huo Y., Zhu X.,
RA Plow E.F., Chen M., Geng J.G.;
RT "P-selectin primes leukocyte integrin activation during inflammation.";
RL Nat. Immunol. 8:882-892(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, AND IDENTIFICATION BY
RP 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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-438, AND IDENTIFICATION BY
RP 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 FUNCTION, INTERACTION WITH SHIGELLA FLEXNERI IPAH9.8, AND MUTAGENESIS OF
RP 476-GLU-ARG-477.
RX PubMed=20010814; DOI=10.1038/ncb2006;
RA Ashida H., Kim M., Schmidt-Supprian M., Ma A., Ogawa M., Sasakawa C.;
RT "A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen
RT the host NF-kappaB-mediated inflammatory response.";
RL Nat. Cell Biol. 12:66-73(2010).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-442, 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 [22]
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 [23]
RP UBIQUITIN-BINDING, AND MUTAGENESIS OF ASP-472.
RX PubMed=21606507; DOI=10.1084/jem.20102177;
RA Nanda S.K., Venigalla R.K., Ordureau A., Patterson-Kane J.C., Powell D.W.,
RA Toth R., Arthur J.S., Cohen P.;
RT "Polyubiquitin binding to ABIN1 is required to prevent autoimmunity.";
RL J. Exp. Med. 208:1215-1228(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-627, AND
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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-284, 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 [26]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-599, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [27]
RP VARIANTS TRP-263; MET-286; THR-374 AND LYS-476.
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 and TNF-induced NF-kappa-B-
CC dependent gene expression by regulating A20/TNFAIP3-mediated
CC deubiquitination of IKBKG; proposed to link A20/TNFAIP3 to
CC ubiquitinated IKBKG. Involved in regulation of EGF-induced ERK1/ERK2
CC signaling pathway; blocks MAPK3/MAPK1 nuclear translocation and MAPK1-
CC dependent transcription. Increases cell surface CD4(T4) antigen
CC expression. Involved in the anti-inflammatory response of macrophages
CC and positively regulates TLR-induced activation of CEBPB. Involved in
CC the prevention of autoimmunity; this function implicates binding to
CC polyubiquitin. Involved in leukocyte integrin activation during
CC inflammation; this function is mediated by association with SELPLG and
CC dependent on phosphorylation by SRC-family kinases. Interacts with HIV-
CC 1 matrix protein and is packaged into virions and overexpression can
CC inhibit viral replication. May regulate matrix nuclear localization,
CC both nuclear import of PIC (Preintegration complex) and export of GAG
CC polyprotein and viral genomic RNA during virion production. In case of
CC infection, promotes association of IKBKG with Shigella flexneri E3
CC ubiquitin-protein ligase ipah9.8 p which in turn promotes
CC polyubiquitination of IKBKG leading to its proteasome-dependent
CC degradation and thus is perturbing NF-kappa-B activation during
CC bacterial infection. {ECO:0000269|PubMed:12220502,
CC ECO:0000269|PubMed:16684768, ECO:0000269|PubMed:17016622,
CC ECO:0000269|PubMed:17632516, ECO:0000269|PubMed:20010814}.
CC -!- SUBUNIT: Interacts with TNFAIP3 and IKBKG (polyubiquitinated);
CC facilitates TNFAIP3-mediated de-ubiquitination of NEMO/IKBKG. Interacts
CC with polyubiquitin. Interacts with MAPK1, SELPLG and PIK3CD. Interacts
CC with IRAK1 (polyubiquitinated). Interacts with MYD88; the interaction
CC is indicative for participation in an activated TLR-signaling complex.
CC Interacts with HIV-1 matrix protein. Interacts with Shigella flexneri
CC ipah9.8; the interaction promotes polyubiquitination of IKBKG.
CC {ECO:0000269|PubMed:12220502, ECO:0000269|PubMed:16684768,
CC ECO:0000269|PubMed:17632516, ECO:0000269|PubMed:20010814}.
CC -!- INTERACTION:
CC Q15025; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-357849, EBI-541426;
CC Q15025; Q13895: BYSL; NbExp=8; IntAct=EBI-357849, EBI-358049;
CC Q15025; Q9H7E9: C8orf33; NbExp=3; IntAct=EBI-357849, EBI-715389;
CC Q15025; Q8NEF3: CCDC112; NbExp=3; IntAct=EBI-357849, EBI-745040;
CC Q15025; P51959: CCNG1; NbExp=8; IntAct=EBI-357849, EBI-3905829;
CC Q15025; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-357849, EBI-396137;
CC Q15025; Q16543: CDC37; NbExp=3; IntAct=EBI-357849, EBI-295634;
CC Q15025; Q9H305: CDIP1; NbExp=4; IntAct=EBI-357849, EBI-2876678;
CC Q15025; Q96M91: CFAP53; NbExp=3; IntAct=EBI-357849, EBI-742422;
CC Q15025; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-357849, EBI-3867333;
CC Q15025; Q15038: DAZAP2; NbExp=3; IntAct=EBI-357849, EBI-724310;
CC Q15025; Q7L190: DPPA4; NbExp=3; IntAct=EBI-357849, EBI-710457;
CC Q15025; Q08426: EHHADH; NbExp=4; IntAct=EBI-357849, EBI-2339219;
CC Q15025; Q14241: ELOA; NbExp=3; IntAct=EBI-357849, EBI-742350;
CC Q15025; Q3B820: FAM161A; NbExp=6; IntAct=EBI-357849, EBI-719941;
CC Q15025; Q92567: FAM168A; NbExp=3; IntAct=EBI-357849, EBI-7957930;
CC Q15025; Q9H0R8: GABARAPL1; NbExp=7; IntAct=EBI-357849, EBI-746969;
CC Q15025; P60520: GABARAPL2; NbExp=6; IntAct=EBI-357849, EBI-720116;
CC Q15025; Q14161: GIT2; NbExp=3; IntAct=EBI-357849, EBI-1046878;
CC Q15025; Q00403: GTF2B; NbExp=7; IntAct=EBI-357849, EBI-389564;
CC Q15025; Q8N4P3: HDDC3; NbExp=3; IntAct=EBI-357849, EBI-750003;
CC Q15025; Q9Y6K9: IKBKG; NbExp=6; IntAct=EBI-357849, EBI-81279;
CC Q15025; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-357849, EBI-2125614;
CC Q15025; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-357849, EBI-14069005;
CC Q15025; Q7Z4W3: KRTAP19-3; NbExp=3; IntAct=EBI-357849, EBI-12020132;
CC Q15025; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-357849, EBI-1048945;
CC Q15025; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-357849, EBI-10241353;
CC Q15025; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-357849, EBI-12111050;
CC Q15025; Q3LI66: KRTAP6-2; NbExp=6; IntAct=EBI-357849, EBI-11962084;
CC Q15025; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-357849, EBI-10261141;
CC Q15025; Q96PV6: LENG8; NbExp=3; IntAct=EBI-357849, EBI-739546;
CC Q15025; Q99732: LITAF; NbExp=3; IntAct=EBI-357849, EBI-725647;
CC Q15025; Q96M61: MAGEB18; NbExp=5; IntAct=EBI-357849, EBI-741835;
CC Q15025; Q9H213: MAGEH1; NbExp=3; IntAct=EBI-357849, EBI-473834;
CC Q15025; Q9H492: MAP1LC3A; NbExp=7; IntAct=EBI-357849, EBI-720768;
CC Q15025; Q9GZQ8: MAP1LC3B; NbExp=4; IntAct=EBI-357849, EBI-373144;
CC Q15025; Q9BXW4: MAP1LC3C; NbExp=3; IntAct=EBI-357849, EBI-2603996;
CC Q15025; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-357849, EBI-348259;
CC Q15025; Q7L9L4: MOB1B; NbExp=3; IntAct=EBI-357849, EBI-2558745;
CC Q15025; Q70IA8: MOB3C; NbExp=3; IntAct=EBI-357849, EBI-9679267;
CC Q15025; Q9UBU8: MORF4L1; NbExp=4; IntAct=EBI-357849, EBI-399246;
CC Q15025; Q15014: MORF4L2; NbExp=4; IntAct=EBI-357849, EBI-399257;
CC Q15025; O14777: NDC80; NbExp=9; IntAct=EBI-357849, EBI-715849;
CC Q15025; P19838: NFKB1; NbExp=5; IntAct=EBI-357849, EBI-300010;
CC Q15025; Q9BYG3: NIFK; NbExp=3; IntAct=EBI-357849, EBI-2561019;
CC Q15025; Q9Y5B8: NME7; NbExp=8; IntAct=EBI-357849, EBI-744782;
CC Q15025; Q96CV9: OPTN; NbExp=19; IntAct=EBI-357849, EBI-748974;
CC Q15025; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-357849, EBI-14066006;
CC Q15025; Q13526: PIN1; NbExp=7; IntAct=EBI-357849, EBI-714158;
CC Q15025; Q96T60: PNKP; NbExp=6; IntAct=EBI-357849, EBI-1045072;
CC Q15025; Q15311: RALBP1; NbExp=4; IntAct=EBI-357849, EBI-749285;
CC Q15025; O76064: RNF8; NbExp=3; IntAct=EBI-357849, EBI-373337;
CC Q15025; A0MZ66-4: SHTN1; NbExp=3; IntAct=EBI-357849, EBI-12097232;
CC Q15025; Q8TAD8: SNIP1; NbExp=4; IntAct=EBI-357849, EBI-749336;
CC Q15025; Q9UM82: SPATA2; NbExp=3; IntAct=EBI-357849, EBI-744066;
CC Q15025; Q5T7P8-2: SYT6; NbExp=3; IntAct=EBI-357849, EBI-10246152;
CC Q15025; Q86VP1: TAX1BP1; NbExp=8; IntAct=EBI-357849, EBI-529518;
CC Q15025; Q15560: TCEA2; NbExp=8; IntAct=EBI-357849, EBI-710310;
CC Q15025; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-357849, EBI-11955057;
CC Q15025; Q96MN5: TCEANC2; NbExp=4; IntAct=EBI-357849, EBI-5462748;
CC Q15025; P21580: TNFAIP3; NbExp=11; IntAct=EBI-357849, EBI-527670;
CC Q15025; Q15025: TNIP1; NbExp=7; IntAct=EBI-357849, EBI-357849;
CC Q15025; Q96KP6: TNIP3; NbExp=6; IntAct=EBI-357849, EBI-2509913;
CC Q15025; Q99816: TSG101; NbExp=3; IntAct=EBI-357849, EBI-346882;
CC Q15025; Q5SRH9-6: TTC39A; NbExp=3; IntAct=EBI-357849, EBI-12259184;
CC Q15025; Q9UNY4-2: TTF2; NbExp=3; IntAct=EBI-357849, EBI-11980463;
CC Q15025; P40222: TXLNA; NbExp=6; IntAct=EBI-357849, EBI-359793;
CC Q15025; Q9H267: VPS33B; NbExp=9; IntAct=EBI-357849, EBI-749072;
CC Q15025; Q15007: WTAP; NbExp=3; IntAct=EBI-357849, EBI-751647;
CC Q15025; P24278: ZBTB25; NbExp=6; IntAct=EBI-357849, EBI-739899;
CC Q15025; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-357849, EBI-2682299;
CC Q15025; O43257: ZNHIT1; NbExp=3; IntAct=EBI-357849, EBI-347522;
CC Q15025; Q8VSC3: ipaH9.8; Xeno; NbExp=4; IntAct=EBI-357849, EBI-6125799;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the
CC nucleus and cytoplasm in a CRM1-dependent manner.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Alpha, FL;
CC IsoId=Q15025-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q15025-2; Sequence=VSP_003913;
CC Name=3;
CC IsoId=Q15025-3; Sequence=VSP_045296;
CC Name=4; Synonyms=Alpha2;
CC IsoId=Q15025-4; Sequence=VSP_055208;
CC Name=5; Synonyms=Alpha4;
CC IsoId=Q15025-5; Sequence=VSP_055209, VSP_055214;
CC Name=6; Synonyms=Beta2;
CC IsoId=Q15025-6; Sequence=VSP_055208, VSP_003913;
CC Name=7; Synonyms=Alpha3, Beta3;
CC IsoId=Q15025-7; Sequence=VSP_055211, VSP_055212;
CC Name=8; Synonyms=Beta4;
CC IsoId=Q15025-8; Sequence=VSP_055210, VSP_055213;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in peripheral blood
CC lymphocytes, spleen and skeletal muscle, and is weakly expressed in the
CC brain. In peripheral blood mononucleocytes, isoform 4 is mainly
CC expressed and isoform 1 and isoform 7 are almost not expressed.
CC Expression of isoform 1 and isoform 7 increases in leukemic cells.
CC {ECO:0000269|PubMed:17016622}.
CC -!- PTM: Phosphorylation at Tyr-552 by SRC-family kinases recruits
CC phosphoinositide-3-kinase (PI3K) PIK3CD:p85 heterodimer which results
CC in integrin activation and leukocyte adhesion to activated endothelium
CC during inflammation. {ECO:0000269|PubMed:17632516}.
CC -!- MISCELLANEOUS: [Isoform 5]: Less effective in the NF-kappa-B inhibitory
CC effect. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB41438.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ011895; CAA09855.1; -; mRNA.
DR EMBL; AJ011896; CAA09856.1; -; mRNA.
DR EMBL; AY012155; AAG42154.1; -; mRNA.
DR EMBL; AB177543; BAF34946.1; -; mRNA.
DR EMBL; AB177544; BAF34947.1; -; mRNA.
DR EMBL; AB252970; BAF48787.1; -; mRNA.
DR EMBL; AB252971; BAF48788.1; -; mRNA.
DR EMBL; AB252972; BAF48789.1; -; mRNA.
DR EMBL; AB252973; BAF48790.1; -; mRNA.
DR EMBL; AB252974; BAF48791.1; -; mRNA.
DR EMBL; AB252975; BAF48792.1; -; mRNA.
DR EMBL; AB252976; BAF48793.1; -; mRNA.
DR EMBL; AB252977; BAF48794.1; -; mRNA.
DR EMBL; AB252978; BAF48795.1; -; mRNA.
DR EMBL; AB252979; BAF48796.1; -; mRNA.
DR EMBL; AB252980; BAF48797.1; -; mRNA.
DR EMBL; AB252981; BAF48798.1; -; mRNA.
DR EMBL; D30755; BAA06416.2; -; mRNA.
DR EMBL; AK299975; BAH13185.1; -; mRNA.
DR EMBL; BX640647; CAE45793.1; -; mRNA.
DR EMBL; AC008641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61688.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61689.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61690.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61691.1; -; Genomic_DNA.
DR EMBL; BC012133; AAH12133.1; -; mRNA.
DR EMBL; BC014008; AAH14008.1; -; mRNA.
DR EMBL; U39403; AAC99999.1; -; mRNA.
DR EMBL; U83844; AAB41438.1; ALT_FRAME; mRNA.
DR CCDS; CCDS34280.1; -. [Q15025-1]
DR CCDS; CCDS58982.1; -. [Q15025-3]
DR CCDS; CCDS58983.1; -. [Q15025-5]
DR CCDS; CCDS58984.1; -. [Q15025-4]
DR CCDS; CCDS58985.1; -. [Q15025-2]
DR RefSeq; NP_001239314.1; NM_001252385.1.
DR RefSeq; NP_001239315.1; NM_001252386.1. [Q15025-3]
DR RefSeq; NP_001239319.1; NM_001252390.1. [Q15025-1]
DR RefSeq; NP_001239320.1; NM_001252391.1. [Q15025-1]
DR RefSeq; NP_001239321.1; NM_001252392.1. [Q15025-2]
DR RefSeq; NP_001239322.1; NM_001252393.1. [Q15025-2]
DR RefSeq; NP_001245383.1; NM_001258454.1. [Q15025-1]
DR RefSeq; NP_001245384.1; NM_001258455.1. [Q15025-4]
DR RefSeq; NP_001245385.1; NM_001258456.1. [Q15025-5]
DR RefSeq; NP_006049.3; NM_006058.4. [Q15025-1]
DR RefSeq; XP_006714814.1; XM_006714751.1.
DR RefSeq; XP_006714815.1; XM_006714752.2. [Q15025-6]
DR PDB; 7EAL; X-ray; 2.50 A; B/C/E/F=405-513.
DR PDB; 7EAO; X-ray; 2.90 A; B/C=415-513.
DR PDB; 7EB9; X-ray; 3.20 A; B/C=415-513.
DR PDBsum; 7EAL; -.
DR PDBsum; 7EAO; -.
DR PDBsum; 7EB9; -.
DR AlphaFoldDB; Q15025; -.
DR SMR; Q15025; -.
DR BioGRID; 115602; 210.
DR CORUM; Q15025; -.
DR DIP; DIP-27577N; -.
DR IntAct; Q15025; 165.
DR MINT; Q15025; -.
DR STRING; 9606.ENSP00000317891; -.
DR iPTMnet; Q15025; -.
DR PhosphoSitePlus; Q15025; -.
DR BioMuta; TNIP1; -.
DR DMDM; 20138952; -.
DR EPD; Q15025; -.
DR jPOST; Q15025; -.
DR MassIVE; Q15025; -.
DR MaxQB; Q15025; -.
DR PaxDb; Q15025; -.
DR PeptideAtlas; Q15025; -.
DR PRIDE; Q15025; -.
DR ProteomicsDB; 17465; -.
DR ProteomicsDB; 18155; -.
DR ProteomicsDB; 60376; -. [Q15025-1]
DR ProteomicsDB; 60377; -. [Q15025-2]
DR Antibodypedia; 28121; 307 antibodies from 28 providers.
DR DNASU; 10318; -.
DR Ensembl; ENST00000315050.11; ENSP00000317891.7; ENSG00000145901.16. [Q15025-1]
DR Ensembl; ENST00000518977.5; ENSP00000430971.1; ENSG00000145901.16. [Q15025-2]
DR Ensembl; ENST00000520931.5; ENSP00000429891.1; ENSG00000145901.16. [Q15025-3]
DR Ensembl; ENST00000521591.6; ENSP00000430760.1; ENSG00000145901.16. [Q15025-1]
DR Ensembl; ENST00000522226.5; ENSP00000428187.1; ENSG00000145901.16. [Q15025-1]
DR Ensembl; ENST00000523200.5; ENSP00000431105.1; ENSG00000145901.16. [Q15025-4]
DR Ensembl; ENST00000523338.5; ENSP00000428243.1; ENSG00000145901.16. [Q15025-2]
DR Ensembl; ENST00000524280.5; ENSP00000429912.1; ENSG00000145901.16. [Q15025-5]
DR Ensembl; ENST00000610535.5; ENSP00000483944.1; ENSG00000145901.16. [Q15025-4]
DR Ensembl; ENST00000610874.4; ENSP00000484665.1; ENSG00000145901.16. [Q15025-5]
DR GeneID; 10318; -.
DR KEGG; hsa:10318; -.
DR MANE-Select; ENST00000521591.6; ENSP00000430760.1; NM_006058.5; NP_006049.3.
DR UCSC; uc003ltg.5; human. [Q15025-1]
DR CTD; 10318; -.
DR DisGeNET; 10318; -.
DR GeneCards; TNIP1; -.
DR HGNC; HGNC:16903; TNIP1.
DR HPA; ENSG00000145901; Low tissue specificity.
DR MalaCards; TNIP1; -.
DR MIM; 607714; gene.
DR neXtProt; NX_Q15025; -.
DR OpenTargets; ENSG00000145901; -.
DR Orphanet; 536; Systemic lupus erythematosus.
DR PharmGKB; PA128394573; -.
DR VEuPathDB; HostDB:ENSG00000145901; -.
DR eggNOG; ENOG502QPYT; Eukaryota.
DR GeneTree; ENSGT00510000046908; -.
DR HOGENOM; CLU_033970_0_0_1; -.
DR InParanoid; Q15025; -.
DR OMA; HPMYHGY; -.
DR OrthoDB; 701614at2759; -.
DR PhylomeDB; Q15025; -.
DR TreeFam; TF351138; -.
DR PathwayCommons; Q15025; -.
DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR SignaLink; Q15025; -.
DR BioGRID-ORCS; 10318; 17 hits in 1078 CRISPR screens.
DR ChiTaRS; TNIP1; human.
DR GeneWiki; TNIP1; -.
DR GenomeRNAi; 10318; -.
DR Pharos; Q15025; Tbio.
DR PRO; PR:Q15025; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q15025; protein.
DR Bgee; ENSG00000145901; Expressed in lower esophagus mucosa and 207 other tissues.
DR ExpressionAtlas; Q15025; baseline and differential.
DR Genevisible; Q15025; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IDA:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; TAS:ProtInc.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; TAS:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:1903003; P:positive regulation of protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR InterPro; IPR033372; TNIP1.
DR PANTHER; PTHR31882:SF3; PTHR31882:SF3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW Inflammatory response; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..636
FT /note="TNFAIP3-interacting protein 1"
FT /id="PRO_0000096691"
FT REGION 61..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..412
FT /note="Interaction with Nef"
FT REGION 252..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..367
FT /note="Interaction with Shigella flexneri ipah9.8"
FT REGION 431..588
FT /note="Required for inhibitory activity of TNF-induced NF-
FT kappa-B activation"
FT /evidence="ECO:0000250"
FT REGION 452..510
FT /note="Ubiquitin-binding domain (UBD)"
FT REGION 603..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 20..73
FT /evidence="ECO:0000255"
FT COILED 196..258
FT /evidence="ECO:0000255"
FT COILED 294..535
FT /evidence="ECO:0000255"
FT MOTIF 524..530
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 114..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 438
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 552
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17632516"
FT MOD_RES 571
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUU8"
FT MOD_RES 599
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 599
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17016622, ECO:0000303|PubMed:17974005"
FT /id="VSP_045296"
FT VAR_SEQ 530..593
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:17016622"
FT /id="VSP_055208"
FT VAR_SEQ 530..556
FT /note="ASGERYHVEPHPEHLCGAYPYAYPPMP -> SLQKMTVRGLSETRLCHLAPP
FT SSCRAS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17016622"
FT /id="VSP_055209"
FT VAR_SEQ 530..552
FT /note="ASGERYHVEPHPEHLCGAYPYAY -> SQLISDCQETRSHLHGVARASAG
FT (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:17016622"
FT /id="VSP_055210"
FT VAR_SEQ 530..545
FT /note="ASGERYHVEPHPEHLC -> GTHRGCPRRLPERKVK (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:17016622"
FT /id="VSP_055211"
FT VAR_SEQ 546..636
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:17016622"
FT /id="VSP_055212"
FT VAR_SEQ 553..636
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:17016622"
FT /id="VSP_055213"
FT VAR_SEQ 557..636
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17016622"
FT /id="VSP_055214"
FT VAR_SEQ 627..636
FT /note="SPKNDREGPQ -> PADLRLPRN (in isoform 2 and isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:17016622,
FT ECO:0000303|PubMed:8681136, ECO:0000303|PubMed:9923610"
FT /id="VSP_003913"
FT VARIANT 103
FT /note="P -> S (in dbSNP:rs2303018)"
FT /id="VAR_051453"
FT VARIANT 146
FT /note="A -> V (in dbSNP:rs2233289)"
FT /id="VAR_051454"
FT VARIANT 151
FT /note="P -> A (in dbSNP:rs2233290)"
FT /id="VAR_051455"
FT VARIANT 233
FT /note="R -> Q (in dbSNP:rs2233292)"
FT /id="VAR_051456"
FT VARIANT 260
FT /note="A -> V (in dbSNP:rs2233295)"
FT /id="VAR_051457"
FT VARIANT 263
FT /note="R -> W (in patients with gastrointestinal diffuse
FT large cell lymphoma; dbSNP:rs117663772)"
FT /evidence="ECO:0000269|PubMed:21266526"
FT /id="VAR_067965"
FT VARIANT 286
FT /note="T -> M (in patients with gastrointestinal diffuse
FT large cell lymphoma; somatic mutation; dbSNP:rs185683917)"
FT /evidence="ECO:0000269|PubMed:21266526"
FT /id="VAR_067966"
FT VARIANT 374
FT /note="I -> T (in patients with gastrointestinal diffuse
FT large cell lymphoma; dbSNP:rs748495842)"
FT /evidence="ECO:0000269|PubMed:21266526"
FT /id="VAR_067967"
FT VARIANT 476
FT /note="E -> K (in patients with gastrointestinal diffuse
FT large cell lymphoma; somatic mutation; loss of inhibitory
FT activity on CARD11- and TNF-induced NF-kappa-B activation)"
FT /evidence="ECO:0000269|PubMed:21266526"
FT /id="VAR_067968"
FT MUTAGEN 472
FT /note="D->N: Abolishes binding to polyubiquitin ('K-63'-
FT linked and linear)."
FT /evidence="ECO:0000269|PubMed:21606507"
FT MUTAGEN 552
FT /note="Y->F: Abolishes interaction with PI3K p85 regulatory
FT subunit and abolishes interaction between SELPLG and PI3K
FT p85 regulatory subunit."
FT /evidence="ECO:0000269|PubMed:17632516"
FT CONFLICT 148
FT /note="G -> D (in Ref. 10; AAH12133)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="G -> S (in Ref. 6; BAH13185)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="A -> P (in Ref. 2; AAG42154 and 3; BAF34946)"
FT /evidence="ECO:0000305"
FT HELIX 448..451
FT /evidence="ECO:0007829|PDB:7EB9"
FT HELIX 455..510
FT /evidence="ECO:0007829|PDB:7EAL"
SQ SEQUENCE 636 AA; 71864 MW; D81B96BEAD50D871 CRC64;
MEGRGPYRIY DPGGSVPSGE ASAAFERLVK ENSRLKEKMQ GIKMLGELLE ESQMEATRLR
QKAEELVKDN ELLPPPSPSL GSFDPLAELT GKDSNVTASP TAPACPSDKP APVQKPPSSG
TSSEFEVVTP EEQNSPESSS HANAMALGPL PREDGNLMLH LQRLETTLSV CAEEPDHGQL
FTHLGRMALE FNRLASKVHK NEQRTSILQT LCEQLRKENE ALKAKLDKGL EQRDQAAERL
REENLELKKL LMSNGNKEGA SGRPGSPKME GTGKKAVAGQ QQASVTAGKV PEVVALGAAE
KKVKMLEQQR SELLEVNKQW DQHFRSMKQQ YEQKITELRQ KLADLQKQVT DLEAEREQKQ
RDFDRKLLLA KSKIEMEETD KEQLTAEAKE LRQKVKYLQD QLSPLTRQRE YQEKEIQRLN
KALEEALSIQ TPPSSPPTAF GSPEGAGALL RKQELVTQNE LLKQQVKIFE EDFQRERSDR
ERMNEEKEEL KKQVEKLQAQ VTLSNAQLKA FKDEEKAREA LRQQKRKAKA SGERYHVEPH
PEHLCGAYPY AYPPMPAMVP HHGFEDWSQI RYPPPPMAME HPPPLPNSRL FHLPEYTWRL
PCGGVRNPNQ SSQVMDPPTA RPTEPESPKN DREGPQ
