Full text data of NMI
NMI
[Confidence: low (only semi-automatic identification from reviews)]
N-myc-interactor; Nmi (N-myc and STAT interactor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
N-myc-interactor; Nmi (N-myc and STAT interactor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q13287
ID NMI_HUMAN Reviewed; 307 AA.
AC Q13287; B5BU69; Q53TI8; Q9BVE5;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=N-myc-interactor;
DE Short=Nmi;
DE AltName: Full=N-myc and STAT interactor;
GN Name=NMI;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cervix carcinoma;
RX PubMed=8668343;
RA Bao J., Zervos A.S.;
RT "Isolation and characterization of Nmi, a novel partner of Myc
RT proteins.";
RL Oncogene 12:2171-2176(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [3]
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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH STATS.
RX PubMed=9989503; DOI=10.1016/S0092-8674(00)80965-4;
RA Zhu M.-H., John S., Berg M., Leonard W.J.;
RT "Functional association of Nmi with Stat5 and Stat1 in IL-2- and
RT IFNgamma-mediated signaling.";
RL Cell 96:121-130(1999).
RN [7]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May be involved in augmenting coactivator protein
CC recruitment to a group of sequence-specific transcription factors.
CC Augments cytokine-mediated STAT transcription. Enhances CBP/p300
CC coactivator protein recruitment to STAT1 and STAT5.
CC -!- SUBUNIT: Interacts with MYCN and MYC, as well as with other
CC transcription factors with a Zip, HLH or a HLH-Zip motif.
CC Interacts with all STAT proteins except STAT2.
CC -!- INTERACTION:
CC Q9HCU9:BRMS1; NbExp=2; IntAct=EBI-372942, EBI-714781;
CC Q9XRX5:HHLA3; NbExp=2; IntAct=EBI-372942, EBI-750554;
CC P04198:MYCN; NbExp=3; IntAct=EBI-372942, EBI-878369;
CC P56693:SOX10; NbExp=2; IntAct=EBI-372942, EBI-1167533;
CC O55170:Sox10 (xeno); NbExp=4; IntAct=EBI-372942, EBI-1185693;
CC P51692:STAT5B; NbExp=7; IntAct=EBI-372942, EBI-1186119;
CC Q13748:TUBA3D; NbExp=2; IntAct=EBI-372942, EBI-355068;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in all adult and fetal tissues
CC except brain and skin. More abundant in fetal tissues especially
CC liver.
CC -!- INDUCTION: By IL2/interleukin-2 and IFNG/IFN-gamma.
CC -!- SIMILARITY: Belongs to the NMI family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U32849; AAC12949.1; -; mRNA.
DR EMBL; AB451305; BAG70119.1; -; mRNA.
DR EMBL; AB451436; BAG70250.1; -; mRNA.
DR EMBL; AC009311; AAY15066.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11513.1; -; Genomic_DNA.
DR EMBL; BC001268; AAH01268.1; -; mRNA.
DR RefSeq; NP_004679.2; NM_004688.2.
DR RefSeq; XP_005246998.1; XM_005246941.1.
DR UniGene; Hs.54483; -.
DR ProteinModelPortal; Q13287; -.
DR IntAct; Q13287; 35.
DR STRING; 9606.ENSP00000243346; -.
DR PhosphoSite; Q13287; -.
DR DMDM; 116242679; -.
DR PaxDb; Q13287; -.
DR PeptideAtlas; Q13287; -.
DR PRIDE; Q13287; -.
DR DNASU; 9111; -.
DR Ensembl; ENST00000243346; ENSP00000243346; ENSG00000123609.
DR GeneID; 9111; -.
DR KEGG; hsa:9111; -.
DR UCSC; uc002txi.2; human.
DR CTD; 9111; -.
DR GeneCards; GC02M152126; -.
DR H-InvDB; HIX0002501; -.
DR HGNC; HGNC:7854; NMI.
DR HPA; HPA008588; -.
DR MIM; 603525; gene.
DR neXtProt; NX_Q13287; -.
DR PharmGKB; PA31659; -.
DR eggNOG; NOG39231; -.
DR HOGENOM; HOG000072676; -.
DR HOVERGEN; HBG019086; -.
DR InParanoid; Q13287; -.
DR OMA; EDQMRDK; -.
DR OrthoDB; EOG7SR4N0; -.
DR PhylomeDB; Q13287; -.
DR ChiTaRS; NMI; human.
DR GeneWiki; N-myc-interactor; -.
DR GenomeRNAi; 9111; -.
DR NextBio; 34149; -.
DR PRO; PR:Q13287; -.
DR ArrayExpress; Q13287; -.
DR Bgee; Q13287; -.
DR CleanEx; HS_NMI; -.
DR Genevestigator; Q13287; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0003712; F:transcription cofactor activity; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0007259; P:JAK-STAT cascade; TAS:UniProtKB.
DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR InterPro; IPR009909; Nmi/IFP35_dom.
DR InterPro; IPR009938; Nmi/IFP35_N.
DR Pfam; PF07334; IFP_35_N; 1.
DR Pfam; PF07292; NID; 2.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Polymorphism; Reference proteome.
FT CHAIN 1 307 N-myc-interactor.
FT /FTId=PRO_0000159702.
FT VARIANT 16 16 S -> L (in dbSNP:rs1048135).
FT /FTId=VAR_028190.
FT CONFLICT 184 184 S -> F (in Ref. 1; AAC12949).
SQ SEQUENCE 307 AA; 35057 MW; EC228BD0C9E643F1 CRC64;
MEADKDDTQQ ILKEHSPDEF IKDEQNKGLI DEITKKNIQL KKEIQKLETE LQEATKEFQI
KEDIPETKMK FLSVETPEND SQLSNISCSF QVSSKVPYEI QKGQALITFE KEEVAQNVVS
MSKHHVQIKD VNLEVTAKPV PLNSGVRFQV YVEVSKMKIN VTEIPDTLRE DQMRDKLELS
FSKSRNGGGE VDRVDYDRQS GSAVITFVEI GVADKILKKK EYPLYINQTC HRVTVSPYTE
IHLKKYQIFS GTSKRTVLLT GMEGIQMDEE IVEDLINIHF QRAKNGGGEV DVVKCSLGQP
HIAYFEE
//
ID NMI_HUMAN Reviewed; 307 AA.
AC Q13287; B5BU69; Q53TI8; Q9BVE5;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=N-myc-interactor;
DE Short=Nmi;
DE AltName: Full=N-myc and STAT interactor;
GN Name=NMI;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cervix carcinoma;
RX PubMed=8668343;
RA Bao J., Zervos A.S.;
RT "Isolation and characterization of Nmi, a novel partner of Myc
RT proteins.";
RL Oncogene 12:2171-2176(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [3]
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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH STATS.
RX PubMed=9989503; DOI=10.1016/S0092-8674(00)80965-4;
RA Zhu M.-H., John S., Berg M., Leonard W.J.;
RT "Functional association of Nmi with Stat5 and Stat1 in IL-2- and
RT IFNgamma-mediated signaling.";
RL Cell 96:121-130(1999).
RN [7]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May be involved in augmenting coactivator protein
CC recruitment to a group of sequence-specific transcription factors.
CC Augments cytokine-mediated STAT transcription. Enhances CBP/p300
CC coactivator protein recruitment to STAT1 and STAT5.
CC -!- SUBUNIT: Interacts with MYCN and MYC, as well as with other
CC transcription factors with a Zip, HLH or a HLH-Zip motif.
CC Interacts with all STAT proteins except STAT2.
CC -!- INTERACTION:
CC Q9HCU9:BRMS1; NbExp=2; IntAct=EBI-372942, EBI-714781;
CC Q9XRX5:HHLA3; NbExp=2; IntAct=EBI-372942, EBI-750554;
CC P04198:MYCN; NbExp=3; IntAct=EBI-372942, EBI-878369;
CC P56693:SOX10; NbExp=2; IntAct=EBI-372942, EBI-1167533;
CC O55170:Sox10 (xeno); NbExp=4; IntAct=EBI-372942, EBI-1185693;
CC P51692:STAT5B; NbExp=7; IntAct=EBI-372942, EBI-1186119;
CC Q13748:TUBA3D; NbExp=2; IntAct=EBI-372942, EBI-355068;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in all adult and fetal tissues
CC except brain and skin. More abundant in fetal tissues especially
CC liver.
CC -!- INDUCTION: By IL2/interleukin-2 and IFNG/IFN-gamma.
CC -!- SIMILARITY: Belongs to the NMI family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U32849; AAC12949.1; -; mRNA.
DR EMBL; AB451305; BAG70119.1; -; mRNA.
DR EMBL; AB451436; BAG70250.1; -; mRNA.
DR EMBL; AC009311; AAY15066.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11513.1; -; Genomic_DNA.
DR EMBL; BC001268; AAH01268.1; -; mRNA.
DR RefSeq; NP_004679.2; NM_004688.2.
DR RefSeq; XP_005246998.1; XM_005246941.1.
DR UniGene; Hs.54483; -.
DR ProteinModelPortal; Q13287; -.
DR IntAct; Q13287; 35.
DR STRING; 9606.ENSP00000243346; -.
DR PhosphoSite; Q13287; -.
DR DMDM; 116242679; -.
DR PaxDb; Q13287; -.
DR PeptideAtlas; Q13287; -.
DR PRIDE; Q13287; -.
DR DNASU; 9111; -.
DR Ensembl; ENST00000243346; ENSP00000243346; ENSG00000123609.
DR GeneID; 9111; -.
DR KEGG; hsa:9111; -.
DR UCSC; uc002txi.2; human.
DR CTD; 9111; -.
DR GeneCards; GC02M152126; -.
DR H-InvDB; HIX0002501; -.
DR HGNC; HGNC:7854; NMI.
DR HPA; HPA008588; -.
DR MIM; 603525; gene.
DR neXtProt; NX_Q13287; -.
DR PharmGKB; PA31659; -.
DR eggNOG; NOG39231; -.
DR HOGENOM; HOG000072676; -.
DR HOVERGEN; HBG019086; -.
DR InParanoid; Q13287; -.
DR OMA; EDQMRDK; -.
DR OrthoDB; EOG7SR4N0; -.
DR PhylomeDB; Q13287; -.
DR ChiTaRS; NMI; human.
DR GeneWiki; N-myc-interactor; -.
DR GenomeRNAi; 9111; -.
DR NextBio; 34149; -.
DR PRO; PR:Q13287; -.
DR ArrayExpress; Q13287; -.
DR Bgee; Q13287; -.
DR CleanEx; HS_NMI; -.
DR Genevestigator; Q13287; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0003712; F:transcription cofactor activity; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0007259; P:JAK-STAT cascade; TAS:UniProtKB.
DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR InterPro; IPR009909; Nmi/IFP35_dom.
DR InterPro; IPR009938; Nmi/IFP35_N.
DR Pfam; PF07334; IFP_35_N; 1.
DR Pfam; PF07292; NID; 2.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Polymorphism; Reference proteome.
FT CHAIN 1 307 N-myc-interactor.
FT /FTId=PRO_0000159702.
FT VARIANT 16 16 S -> L (in dbSNP:rs1048135).
FT /FTId=VAR_028190.
FT CONFLICT 184 184 S -> F (in Ref. 1; AAC12949).
SQ SEQUENCE 307 AA; 35057 MW; EC228BD0C9E643F1 CRC64;
MEADKDDTQQ ILKEHSPDEF IKDEQNKGLI DEITKKNIQL KKEIQKLETE LQEATKEFQI
KEDIPETKMK FLSVETPEND SQLSNISCSF QVSSKVPYEI QKGQALITFE KEEVAQNVVS
MSKHHVQIKD VNLEVTAKPV PLNSGVRFQV YVEVSKMKIN VTEIPDTLRE DQMRDKLELS
FSKSRNGGGE VDRVDYDRQS GSAVITFVEI GVADKILKKK EYPLYINQTC HRVTVSPYTE
IHLKKYQIFS GTSKRTVLLT GMEGIQMDEE IVEDLINIHF QRAKNGGGEV DVVKCSLGQP
HIAYFEE
//
MIM
603525
*RECORD*
*FIELD* NO
603525
*FIELD* TI
*603525 NMYC INTERACTOR; NMI
;;NMYC AND STAT INTERACTOR
*FIELD* TX
Using a yeast genetic screen, Bao and Zervos (1996) identified a human
read moregene, NMYC interactor (NMI), that encodes a protein that binds to NMYC
(164840). The NMI protein also interacts with MYC (190080) and other
transcription factors containing a Zip, HLH, or HLH-Zip motif. The
deduced NMI protein contains 307 amino acids. The carboxyl terminus of
NMI is 25% identical to an interferon-induced leucine zipper protein,
IFP35 (600735), whereas its amino terminus is 22% identical to the
coiled-coil heptad repeats of the C. elegans protein CEF59.
Coprecipitation studies of NMI with NMYC and MYC confirmed their
interaction in mammalian cells. By Northern blot analysis, NMI mRNA was
expressed at low levels in all human fetal and adult tissues tested
except brain. Among several cancer cell lines, high expression of NMI
was found in myeloid leukemias, which also express high levels of MYC.
Using the coiled-coil region of STAT5B as the bait in a yeast 2-hybrid
screen, Zhu et al. (1999) identified the association of NMI with STAT5B.
They showed that NMI interacts with all STATs except STAT2 (600556).
They evaluated 2 cytokine systems, IL2 (147680) and IFN-gamma (IFNG;
147570), and demonstrated that NMI augments STAT-mediated transcription
in response to these cytokines. NMI enhances the association of CBP
(600140)/p300 (602700) coactivator proteins with STAT1 (600555) and
STAT5, and together with CBP/p300, can augment IL2- and IFNG-dependent
transcription.
By fluorescence in situ hybridization, Bao and Zervos (1996) localized
the human NMI gene to 22q13.3.
*FIELD* RF
1. Bao, J.; Zervos, A. S.: Isolation and characterization of Nmi,
a novel partner of Myc proteins. Oncogene 12: 2171-2176, 1996.
2. Zhu, M.; John, S.; Berg, M.; Leonard, W. J.: Functional association
of Nmi with Stat5 and Stat1 in IL-2- and IFN-gamma-mediated signaling. Cell 96:
121-130, 1999.
*FIELD* CD
Stylianos E. Antonarakis: 2/12/1999
*FIELD* ED
psherman: 02/18/1999
psherman: 2/15/1999
psherman: 2/12/1999
*RECORD*
*FIELD* NO
603525
*FIELD* TI
*603525 NMYC INTERACTOR; NMI
;;NMYC AND STAT INTERACTOR
*FIELD* TX
Using a yeast genetic screen, Bao and Zervos (1996) identified a human
read moregene, NMYC interactor (NMI), that encodes a protein that binds to NMYC
(164840). The NMI protein also interacts with MYC (190080) and other
transcription factors containing a Zip, HLH, or HLH-Zip motif. The
deduced NMI protein contains 307 amino acids. The carboxyl terminus of
NMI is 25% identical to an interferon-induced leucine zipper protein,
IFP35 (600735), whereas its amino terminus is 22% identical to the
coiled-coil heptad repeats of the C. elegans protein CEF59.
Coprecipitation studies of NMI with NMYC and MYC confirmed their
interaction in mammalian cells. By Northern blot analysis, NMI mRNA was
expressed at low levels in all human fetal and adult tissues tested
except brain. Among several cancer cell lines, high expression of NMI
was found in myeloid leukemias, which also express high levels of MYC.
Using the coiled-coil region of STAT5B as the bait in a yeast 2-hybrid
screen, Zhu et al. (1999) identified the association of NMI with STAT5B.
They showed that NMI interacts with all STATs except STAT2 (600556).
They evaluated 2 cytokine systems, IL2 (147680) and IFN-gamma (IFNG;
147570), and demonstrated that NMI augments STAT-mediated transcription
in response to these cytokines. NMI enhances the association of CBP
(600140)/p300 (602700) coactivator proteins with STAT1 (600555) and
STAT5, and together with CBP/p300, can augment IL2- and IFNG-dependent
transcription.
By fluorescence in situ hybridization, Bao and Zervos (1996) localized
the human NMI gene to 22q13.3.
*FIELD* RF
1. Bao, J.; Zervos, A. S.: Isolation and characterization of Nmi,
a novel partner of Myc proteins. Oncogene 12: 2171-2176, 1996.
2. Zhu, M.; John, S.; Berg, M.; Leonard, W. J.: Functional association
of Nmi with Stat5 and Stat1 in IL-2- and IFN-gamma-mediated signaling. Cell 96:
121-130, 1999.
*FIELD* CD
Stylianos E. Antonarakis: 2/12/1999
*FIELD* ED
psherman: 02/18/1999
psherman: 2/15/1999
psherman: 2/12/1999