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TNIP3_HUMAN
ID   TNIP3_HUMAN             Reviewed;         325 AA.
AC   Q96KP6; A1A574; A8K2Z4; B4DVF5; B4E023; Q96PQ3; Q9H780;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=TNFAIP3-interacting protein 3;
DE   AltName: Full=A20-binding inhibitor of NF-kappa-B activation 3;
DE            Short=ABIN-3;
DE   AltName: Full=Listeria-induced gene protein;
GN   Name=TNIP3 {ECO:0000312|HGNC:HGNC:19315}; Synonyms=ABIN3, LIND;
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:AAL02151.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RC   TISSUE=Macrophage {ECO:0000269|PubMed:11345586}, and Monocyte;
RX   PubMed=11345586; DOI=10.1007/s002510100306;
RA   Staege H., Brauchlin A., Schoedon G., Schaffner A.;
RT   "Two novel genes FIND and LIND differentially expressed in deactivated and
RT   Listeria-infected human macrophages.";
RL   Immunogenetics 53:105-113(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH TNFAIP3,
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=17088249; DOI=10.1074/jbc.m607481200;
RA   Wullaert A., Verstrepen L., Van Huffel S., Adib-Conquy M., Cornelis S.,
RA   Kreike M., Haegman M., El Bakkouri K., Sanders M., Verhelst K.,
RA   Carpentier I., Cavaillon J.-M., Heyninck K., Beyaert R.;
RT   "LIND/ABIN-3 is a novel lipopolysaccharide-inducible inhibitor of NF-kappaB
RT   activation.";
RL   J. Biol. Chem. 282:81-90(2007).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:BAB15018.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Smooth muscle {ECO:0000312|EMBL:BAB15018.1}, Spleen, Thymus, and
RC   Umbilical cord blood;
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=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   [5] {ECO:0000312|EMBL:CAC85929.1}
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   UBIQUITIN-BINDING, AND MUTAGENESIS OF 214-GLU-ARG-215.
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).
CC   -!- FUNCTION: Binds to zinc finger protein TNFAIP3 and inhibits NF-kappa-B
CC       activation induced by tumor necrosis factor, Toll-like receptor 4
CC       (TLR4), interleukin-1 and 12-O-tetradecanoylphorbol-13-acetate.
CC       Overexpression inhibits NF-kappa-B-dependent gene expression in
CC       response to lipopolysaccharide at a level downstream of TRAF6 and
CC       upstream of IKBKB. NF-kappa-B inhibition is independent of TNFAIP3
CC       binding. {ECO:0000269|PubMed:17088249}.
CC   -!- SUBUNIT: Interacts with TNFAIP3. Interacts with polyubiquitin.
CC       {ECO:0000269|PubMed:17088249}.
CC   -!- INTERACTION:
CC       Q96KP6; Q86V38: ATN1; NbExp=3; IntAct=EBI-2509913, EBI-11954292;
CC       Q96KP6; P48745: CCN3; NbExp=3; IntAct=EBI-2509913, EBI-3904822;
CC       Q96KP6; P02489: CRYAA; NbExp=3; IntAct=EBI-2509913, EBI-6875961;
CC       Q96KP6; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2509913, EBI-3867333;
CC       Q96KP6; Q15038: DAZAP2; NbExp=9; IntAct=EBI-2509913, EBI-724310;
CC       Q96KP6; G5E9A7: DMWD; NbExp=3; IntAct=EBI-2509913, EBI-10976677;
CC       Q96KP6; Q3B820: FAM161A; NbExp=3; IntAct=EBI-2509913, EBI-719941;
CC       Q96KP6; P42858: HTT; NbExp=9; IntAct=EBI-2509913, EBI-466029;
CC       Q96KP6; Q92876: KLK6; NbExp=3; IntAct=EBI-2509913, EBI-2432309;
CC       Q96KP6; O00505: KPNA3; NbExp=3; IntAct=EBI-2509913, EBI-358297;
CC       Q96KP6; Q6A162: KRT40; NbExp=4; IntAct=EBI-2509913, EBI-10171697;
CC       Q96KP6; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2509913, EBI-10171774;
CC       Q96KP6; Q99732: LITAF; NbExp=3; IntAct=EBI-2509913, EBI-725647;
CC       Q96KP6; P02545: LMNA; NbExp=3; IntAct=EBI-2509913, EBI-351935;
CC       Q96KP6; Q9BRK4: LZTS2; NbExp=6; IntAct=EBI-2509913, EBI-741037;
CC       Q96KP6; P43356: MAGEA2B; NbExp=3; IntAct=EBI-2509913, EBI-5650739;
CC       Q96KP6; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2509913, EBI-11522433;
CC       Q96KP6; P35240: NF2; NbExp=3; IntAct=EBI-2509913, EBI-1014472;
CC       Q96KP6; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-2509913, EBI-945833;
CC       Q96KP6; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-2509913, EBI-22310682;
CC       Q96KP6; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2509913, EBI-741158;
CC       Q96KP6; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-2509913, EBI-14066006;
CC       Q96KP6; Q9NRY6: PLSCR3; NbExp=3; IntAct=EBI-2509913, EBI-750734;
CC       Q96KP6; D3DTS7: PMP22; NbExp=3; IntAct=EBI-2509913, EBI-25882629;
CC       Q96KP6; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2509913, EBI-5235340;
CC       Q96KP6; Q86VP1: TAX1BP1; NbExp=7; IntAct=EBI-2509913, EBI-529518;
CC       Q96KP6; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-2509913, EBI-11955057;
CC       Q96KP6; P21580: TNFAIP3; NbExp=3; IntAct=EBI-2509913, EBI-527670;
CC       Q96KP6; Q15025: TNIP1; NbExp=6; IntAct=EBI-2509913, EBI-357849;
CC       Q96KP6; Q9BZR9: TRIM8; NbExp=3; IntAct=EBI-2509913, EBI-2340370;
CC       Q96KP6; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-2509913, EBI-742740;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q96KP6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96KP6-2; Sequence=VSP_045101, VSP_045103;
CC       Name=3;
CC         IsoId=Q96KP6-3; Sequence=VSP_045102, VSP_045103;
CC   -!- TISSUE SPECIFICITY: Highly expressed in lung, lymph node, thymus and
CC       fetal liver. Expressed at lower levels in bone marrow, brain, kidney,
CC       spleen, leukocytes and tonsils. Could be detected in heart, salivary
CC       gland, adrenal gland, pancreas, ovary and fetal brain. High levels
CC       detected in liver, colon, small intestine, muscle, stomach, testis,
CC       placenta, thyroid, uterus, prostate, skin and PBL.
CC       {ECO:0000269|PubMed:11345586, ECO:0000269|PubMed:17088249}.
CC   -!- INDUCTION: By Listeria infection. Expression is slightly down-regulated
CC       by dexamethasone and slightly up-regulated by IL-10. Strongly induced
CC       mRNA and protein expression by lipopolysaccharide.
CC       {ECO:0000269|PubMed:11345586, ECO:0000269|PubMed:17088249}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15018.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB15018.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAC85929.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF277289; AAL02151.1; -; mRNA.
DR   EMBL; AJ320534; CAC85929.1; ALT_FRAME; mRNA.
DR   EMBL; AK024815; BAB15018.1; ALT_SEQ; mRNA.
DR   EMBL; AK290409; BAF83098.1; -; mRNA.
DR   EMBL; AK301058; BAG62667.1; -; mRNA.
DR   EMBL; AK303192; BAG64285.1; -; mRNA.
DR   EMBL; AC105254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC108027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471056; EAX05264.1; -; Genomic_DNA.
DR   EMBL; BC128408; AAI28409.1; -; mRNA.
DR   CCDS; CCDS3718.1; -. [Q96KP6-1]
DR   CCDS; CCDS58925.1; -. [Q96KP6-2]
DR   CCDS; CCDS58926.1; -. [Q96KP6-3]
DR   RefSeq; NP_001122315.2; NM_001128843.2. [Q96KP6-2]
DR   RefSeq; NP_001231693.1; NM_001244764.1. [Q96KP6-3]
DR   RefSeq; NP_079149.3; NM_024873.5. [Q96KP6-1]
DR   AlphaFoldDB; Q96KP6; -.
DR   SMR; Q96KP6; -.
DR   BioGRID; 123006; 35.
DR   IntAct; Q96KP6; 50.
DR   STRING; 9606.ENSP00000426613; -.
DR   iPTMnet; Q96KP6; -.
DR   PhosphoSitePlus; Q96KP6; -.
DR   BioMuta; TNIP3; -.
DR   DMDM; 269849474; -.
DR   EPD; Q96KP6; -.
DR   jPOST; Q96KP6; -.
DR   MassIVE; Q96KP6; -.
DR   PaxDb; Q96KP6; -.
DR   PeptideAtlas; Q96KP6; -.
DR   PRIDE; Q96KP6; -.
DR   ProteomicsDB; 5265; -.
DR   ProteomicsDB; 5641; -.
DR   ProteomicsDB; 77100; -. [Q96KP6-1]
DR   Antibodypedia; 26709; 129 antibodies from 29 providers.
DR   DNASU; 79931; -.
DR   Ensembl; ENST00000057513.8; ENSP00000057513.3; ENSG00000050730.16. [Q96KP6-1]
DR   Ensembl; ENST00000507879.5; ENSP00000427106.1; ENSG00000050730.16. [Q96KP6-2]
DR   Ensembl; ENST00000509841.1; ENSP00000426613.1; ENSG00000050730.16. [Q96KP6-3]
DR   GeneID; 79931; -.
DR   KEGG; hsa:79931; -.
DR   MANE-Select; ENST00000057513.8; ENSP00000057513.3; NM_024873.6; NP_079149.3.
DR   UCSC; uc010ing.4; human. [Q96KP6-1]
DR   CTD; 79931; -.
DR   DisGeNET; 79931; -.
DR   GeneCards; TNIP3; -.
DR   HGNC; HGNC:19315; TNIP3.
DR   HPA; ENSG00000050730; Tissue enhanced (lymphoid tissue, urinary bladder).
DR   MIM; 608019; gene.
DR   neXtProt; NX_Q96KP6; -.
DR   OpenTargets; ENSG00000050730; -.
DR   PharmGKB; PA134934429; -.
DR   VEuPathDB; HostDB:ENSG00000050730; -.
DR   eggNOG; ENOG502RYDP; Eukaryota.
DR   GeneTree; ENSGT00510000046908; -.
DR   HOGENOM; CLU_052353_0_0_1; -.
DR   InParanoid; Q96KP6; -.
DR   OMA; HFPTCNC; -.
DR   OrthoDB; 701614at2759; -.
DR   PhylomeDB; Q96KP6; -.
DR   TreeFam; TF351138; -.
DR   PathwayCommons; Q96KP6; -.
DR   Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR   SignaLink; Q96KP6; -.
DR   BioGRID-ORCS; 79931; 11 hits in 1066 CRISPR screens.
DR   GenomeRNAi; 79931; -.
DR   Pharos; Q96KP6; Tbio.
DR   PRO; PR:Q96KP6; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q96KP6; protein.
DR   Bgee; ENSG00000050730; Expressed in colonic epithelium and 102 other tissues.
DR   ExpressionAtlas; Q96KP6; baseline and differential.
DR   Genevisible; Q96KP6; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IDA:UniProtKB.
DR   InterPro; IPR032419; CC2-LZ_dom.
DR   InterPro; IPR033574; TNIP3.
DR   PANTHER; PTHR31882:SF2; PTHR31882:SF2; 1.
DR   Pfam; PF16516; CC2-LZ; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Inflammatory response;
KW   Reference proteome.
FT   CHAIN           1..325
FT                   /note="TNFAIP3-interacting protein 3"
FT                   /id="PRO_0000072607"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..248
FT                   /note="Ubiquitin-binding domain (UBD)"
FT   COILED          27..265
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1
FT                   /note="M -> MNKNEKHDDKLVMFTNQSEDSERCESMELDKKIQDLIERNASPHPKR
FT                   FTPEAMPTHRNLCSLKTPGKTASM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045101"
FT   VAR_SEQ         1
FT                   /note="M -> MIPCGWLMNKNEKHDDKLVMFTNQSEDSERCESMELDKKIQDLIERN
FT                   ASPHPKRFTPEAMPTHRNLCSLKTPGKTASM (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045102"
FT   VAR_SEQ         296..325
FT                   /note="PDYQWYALDQLPPDVQHKANGLSSVKKVHP -> VYPQ (in isoform 2
FT                   and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045103"
FT   VARIANT         99
FT                   /note="K -> E (in dbSNP:rs10000692)"
FT                   /id="VAR_057006"
FT   MUTAGEN         214..215
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        109
FT                   /note="Q -> H (in Ref. 6; AAI28409)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        298
FT                   /note="Y -> C (in Ref. 1; AAL02151)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   325 AA;  38943 MW;  C03EDCCA38B59D29 CRC64;
     MAHFVQGTSR MIAAESSTEH KECAEPSTRK NLMNSLEQKI RCLEKQRKEL LEVNQQWDQQ
     FRSMKELYER KVAELKTKLD AAERFLSTRE KDPHQRQRKD DRQREDDRQR DLTRDRLQRE
     EKEKERLNEE LHELKEENKL LKGKNTLANK EKEHYECEIK RLNKALQDAL NIKCSFSEDC
     LRKSRVEFCH EEMRTEMEVL KQQVQIYEED FKKERSDRER LNQEKEELQQ INETSQSQLN
     RLNSQIKACQ MEKEKLEKQL KQMYCPPCNC GLVFHLQDPW VPTGPGAVQK QREHPPDYQW
     YALDQLPPDV QHKANGLSSV KKVHP
 
 
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