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MLX-interacting protein (Class E basic helix-loop-helix protein 36) (bHLHe36) (Transcriptional activator MondoA)

 MLXIP_HUMAN             Reviewed;         919 AA.
Q9HAP2; A7MBN0; O94945; Q7LC47; Q8IXP1; Q8TAH9; Q8WVQ0; Q8WYA5;
21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
21-AUG-2007, sequence version 2.
25-OCT-2017, entry version 122.
RecName: Full=MLX-interacting protein;
AltName: Full=Class E basic helix-loop-helix protein 36;
Short=bHLHe36;
AltName: Full=Transcriptional activator MondoA;
Name=MLXIP {ECO:0000312|HGNC:HGNC:17055};
Synonyms=BHLHE36, KIAA0867, MIR {ECO:0000312|EMBL:AAL55689.1}, MONDOA;
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:AAG34121.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=11073985; DOI=10.1128/MCB.20.23.8845-8854.2000;
Billin A.N., Eilers A.L., Coulter K.L., Logan J.S., Ayer D.E.;
"MondoA, a novel basic helix-loop-helix-leucine zipper transcriptional
activator that constitutes a positive branch of a max-like network.";
Mol. Cell. Biol. 20:8845-8854(2000).
[2] {ECO:0000305, ECO:0000312|EMBL:AAL55689.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), AND VARIANT GLY-396.
Merla G., Cairo S., Reymond A.;
"Mir, a new bHLHZip protein interacting with Mlx.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=10048485; DOI=10.1093/dnares/5.6.355;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:355-364(1998).
[4] {ECO:0000305, ECO:0000312|EMBL:AAH28309.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 176-919 (ISOFORM 3), AND VARIANT
GLY-396.
TISSUE=Pancreas {ECO:0000312|EMBL:AAH17656.1}, and
Placenta {ECO:0000312|EMBL:AAH28309.1};
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).
[5] {ECO:0000305}
FUNCTION, DNA-BINDING, INTERACTION WITH MLX, AND SUBCELLULAR LOCATION.
PubMed=12446771; DOI=10.1128/MCB.22.24.8514-8526.2002;
Eilers A.L., Sundwall E., Lin M., Sullivan A.A., Ayer D.E.;
"A novel heterodimerization domain, CRM1, and 14-3-3 control
subcellular localization of the MondoA-Mlx heterocomplex.";
Mol. Cell. Biol. 22:8514-8526(2002).
[6] {ECO:0000305}
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16782875; DOI=10.1128/MCB.00657-05;
Sans C.L., Satterwhite D.J., Stoltzman C.A., Breen K.T., Ayer D.E.;
"MondoA-Mlx heterodimers are candidate sensors of cellular energy
status: mitochondrial localization and direct regulation of
glycolysis.";
Mol. Cell. Biol. 26:4863-4871(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-33, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-669, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
-!- FUNCTION: Binds DNA as a heterodimer with MLX and activates
transcription. Binds to the canonical E box sequence 5'-CACGTG-3'.
Plays a role in transcriptional activation of glycolytic target
genes. Involved in glucose-responsive gene regulation.
{ECO:0000250|UniProtKB:Q2VPU4, ECO:0000269|PubMed:12446771,
ECO:0000269|PubMed:16782875}.
-!- SUBUNIT: Efficient DNA binding requires dimerization with another
bHLH protein. Binds DNA as a homodimer or a heterodimer with MLX.
{ECO:0000250|UniProtKB:Q2VPU4, ECO:0000269|PubMed:12446771}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12446771,
ECO:0000269|PubMed:16782875}. Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00981, ECO:0000269|PubMed:12446771,
ECO:0000269|PubMed:16782875}. Mitochondrion outer membrane
{ECO:0000269|PubMed:12446771, ECO:0000269|PubMed:16782875}.
Note=Predominantly cytoplasmic but shuttles between cytoplasm and
nucleus when associated with MLX. Also associates with the outer
mitochondrial membrane and may shuttle between the outer
mitochondrial membrane and the nucleus.
{ECO:0000250|UniProtKB:Q2VPU4, ECO:0000269|PubMed:12446771,
ECO:0000269|PubMed:16782875}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1 {ECO:0000269|PubMed:11073985};
IsoId=Q9HAP2-1; Sequence=Displayed;
Name=2 {ECO:0000269|Ref.2};
IsoId=Q9HAP2-2; Sequence=VSP_052499;
Name=3 {ECO:0000269|PubMed:15489334};
IsoId=Q9HAP2-3; Sequence=VSP_052501, VSP_052502;
Note=No experimental confirmation available. {ECO:0000305};
Name=4 {ECO:0000269|Ref.2};
IsoId=Q9HAP2-4; Sequence=VSP_052499, VSP_052503, VSP_052504;
Name=5 {ECO:0000269|PubMed:15489334};
IsoId=Q9HAP2-5; Sequence=VSP_052499, VSP_052500, VSP_052501,
VSP_052502;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Widely expressed in adult tissues. Most
abundant in skeletal muscle. {ECO:0000269|PubMed:11073985}.
-!- SEQUENCE CAUTION:
Sequence=BAA74890.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF312918; AAG34121.1; -; mRNA.
EMBL; AF245480; AAL55689.1; -; mRNA.
EMBL; AF245481; AAL55690.1; -; mRNA.
EMBL; AB020674; BAA74890.2; ALT_INIT; mRNA.
EMBL; BC017656; AAH17656.1; -; mRNA.
EMBL; BC028309; AAH28309.1; -; mRNA.
EMBL; BC039704; AAH39704.1; -; mRNA.
EMBL; BC151841; AAI51842.1; -; mRNA.
CCDS; CCDS73540.1; -. [Q9HAP2-1]
RefSeq; NP_055753.3; NM_014938.5. [Q9HAP2-1]
UniGene; Hs.437153; -.
UniGene; Hs.721711; -.
UniGene; Hs.731847; -.
ProteinModelPortal; Q9HAP2; -.
SMR; Q9HAP2; -.
BioGrid; 116544; 5.
IntAct; Q9HAP2; 6.
MINT; MINT-7032145; -.
STRING; 9606.ENSP00000312834; -.
iPTMnet; Q9HAP2; -.
PhosphoSitePlus; Q9HAP2; -.
BioMuta; MLXIP; -.
DMDM; 156632588; -.
EPD; Q9HAP2; -.
MaxQB; Q9HAP2; -.
PaxDb; Q9HAP2; -.
PeptideAtlas; Q9HAP2; -.
PRIDE; Q9HAP2; -.
DNASU; 22877; -.
Ensembl; ENST00000319080; ENSP00000312834; ENSG00000175727. [Q9HAP2-1]
Ensembl; ENST00000377037; ENSP00000366236; ENSG00000175727. [Q9HAP2-5]
Ensembl; ENST00000538698; ENSP00000440769; ENSG00000175727. [Q9HAP2-2]
Ensembl; ENST00000625732; ENSP00000486569; ENSG00000281178. [Q9HAP2-2]
Ensembl; ENST00000628109; ENSP00000486016; ENSG00000281178. [Q9HAP2-5]
Ensembl; ENST00000629738; ENSP00000487003; ENSG00000281178. [Q9HAP2-1]
GeneID; 22877; -.
KEGG; hsa:22877; -.
UCSC; uc001ubq.4; human. [Q9HAP2-1]
CTD; 22877; -.
DisGeNET; 22877; -.
EuPathDB; HostDB:ENSG00000175727.13; -.
GeneCards; MLXIP; -.
H-InvDB; HIX0019678; -.
HGNC; HGNC:17055; MLXIP.
HPA; HPA023084; -.
MIM; 608090; gene.
neXtProt; NX_Q9HAP2; -.
OpenTargets; ENSG00000175727; -.
PharmGKB; PA128394590; -.
eggNOG; KOG3582; Eukaryota.
eggNOG; ENOG410XTA5; LUCA.
GeneTree; ENSGT00530000063219; -.
HOVERGEN; HBG062003; -.
InParanoid; Q9HAP2; -.
KO; K09113; -.
OMA; AQPTLHQ; -.
OrthoDB; EOG091G02A1; -.
PhylomeDB; Q9HAP2; -.
TreeFam; TF324749; -.
ChiTaRS; MLXIP; human.
GenomeRNAi; 22877; -.
PRO; PR:Q9HAP2; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000175727; -.
CleanEx; HS_MLXIP; -.
ExpressionAtlas; Q9HAP2; baseline and differential.
Genevisible; Q9HAP2; HS.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0000989; F:transcription factor activity, transcription factor binding; IEA:InterPro.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:1900402; P:regulation of carbohydrate metabolic process by regulation of transcription from RNA polymerase II promoter; IMP:GO_Central.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR032648; MLXIP.
PANTHER; PTHR15741:SF23; PTHR15741:SF23; 1.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Complete proteome;
Cytoplasm; DNA-binding; Membrane; Mitochondrion;
Mitochondrion outer membrane; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 919 MLX-interacting protein.
/FTId=PRO_0000298763.
DOMAIN 719 769 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 73 327 Required for cytoplasmic localization.
{ECO:0000269|PubMed:12446771}.
REGION 322 445 Transactivation domain.
{ECO:0000269|PubMed:12446771}.
REGION 769 790 Leucine-zipper.
REGION 832 881 Mediates heterotypic interactions between
MLXIP and MLX and is required for
cytoplasmic localization.
{ECO:0000269|PubMed:12446771}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 33 33 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000250|UniProtKB:Q2VPU4}.
MOD_RES 669 669 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 393 Missing (in isoform 2, isoform 4 and
isoform 5). {ECO:0000303|PubMed:10048485,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_052499.
VAR_SEQ 426 443 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_052500.
VAR_SEQ 578 628 AAFSGQPQAVIMTSGPLKREGMLASTVSQSNVVIAPAAIAR
APGVPEFHSS -> GEPGGETQCGAPPDPEGCFPIPKAFKL
VTTTTTLVCTCMRTHIHLNETKVS (in isoform 3
and isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_052501.
VAR_SEQ 629 919 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_052502.
VAR_SEQ 770 772 QQE -> LLS (in isoform 4).
{ECO:0000303|Ref.2}.
/FTId=VSP_052503.
VAR_SEQ 773 919 Missing (in isoform 4).
{ECO:0000303|Ref.2}.
/FTId=VSP_052504.
VARIANT 396 396 E -> G (in dbSNP:rs7978353).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2}.
/FTId=VAR_059344.
VARIANT 539 539 V -> L (in dbSNP:rs34702867).
/FTId=VAR_059345.
SEQUENCE 919 AA; 101185 MW; 47375FCC4333E0C2 CRC64;
MAADVFMCSP RRPRSRGRQV LLKPQVSEDD DDSDTDEPSP PPASGAATPA RAHASAAPPP
PRAGPGREEP PRRQQIIHSG HFMVSSPHRE HPPKKGYDFD TVNKQTCQTY SFGKTSSCHL
SIDASLTKLF ECMTLAYSGK LVSPKWKNFK GLKLQWRDKI RLNNAIWRAW YMQYLEKRKN
PVCHFVTPLD GSVDVDEHRR PEAITTEGKY WKSRIEIVIR EYHKWRTYFK KRLQQHKDED
LSSLVQDDDM LYWHKHGDGW KTPVPMEEDP LLDTDMLMSE FSDTLFSTLS SHQPVAWPNP
REIAHLGNAD MIQPGLIPLQ PNLDFMDTFE PFQDLFSSSR SIFGSMLPAS ASAPVPDPNN
PPAQESILPT TALPTVSLPD SLIAPPTAPS LAHMDEQGCE HTSRTEDPFI QPTDFGPSEP
PLSVPQPFLP VFTMPLLSPS PAPPPISPVL PLVPPPATAL NPPAPPTFHQ PQKFAGVNKA
PSVITHTASA TLTHDAPATT FSQSQGLVIT THHPAPSAAP CGLALSPVTR PPQPRLTFVH
PKPVSLTGGR PKQPHKIVPA PKPEPVSLVL KNARIAPAAF SGQPQAVIMT SGPLKREGML
ASTVSQSNVV IAPAAIARAP GVPEFHSSIL VTDLGHGTSS PPAPVSRLFP STAQDPLGKG
EQVPLHGGSP QVTVTGPSRD CPNSGQASPC ASEQSPSPQS PQNNCSGKSD PKNVAALKNR
QMKHISAEQK RRFNIKMCFD MLNSLISNNS KLTSHAITLQ KTVEYITKLQ QERGQMQEEA
RRLREEIEEL NATIISCQQL LPATGVPVTR RQFDHMKDMF DEYVKTRTLQ NWKFWIFSII
IKPLFESFKG MVSTSSLEEL HRTALSWLDQ HCSLPILRPM VLSTLRQLST STSILTDPAQ
LPEQASKAVT RIGKRLGES


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