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MyoD family inhibitor domain-containing protein (I-mfa domain-containing protein) (hIC)

 MDFIC_HUMAN             Reviewed;         246 AA.
Q9P1T7; Q9P1T6;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
01-SEP-2009, sequence version 2.
18-JUL-2018, entry version 118.
RecName: Full=MyoD family inhibitor domain-containing protein;
AltName: Full=I-mfa domain-containing protein;
Short=hIC;
Name=MDFIC {ECO:0000312|HGNC:HGNC:28870};
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:AAF36998.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=T-cell {ECO:0000269|PubMed:10671520};
PubMed=10671520; DOI=10.1074/jbc.275.7.4848;
Thebault S., Gachon F., Lemasson I., Devaux C., Mesnard J.-M.;
"Molecular cloning of a novel human I-mfa domain-containing protein
that differently regulates human T-cell leukemia virus type I and HIV-
1 expression.";
J. Biol. Chem. 275:4848-4857(2000).
[2] {ECO:0000305, ECO:0000312|EMBL:AAP33842.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
HIV-1 TAT (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
TISSUE=Leukocyte {ECO:0000269|PubMed:16260749};
PubMed=16260749; DOI=10.1073/pnas.0503519102;
Gautier V.W., Sheehy N., Duffy M., Hashimoto K., Hall W.W.;
"Direct interaction of the human I-mfa domain-containing protein, HIC,
with HIV-1 Tat results in cytoplasmic sequestration and control of Tat
activity.";
Proc. Natl. Acad. Sci. U.S.A. 102:16362-16367(2005).
[3] {ECO:0000305}
SUBCELLULAR LOCATION, DOMAIN, AND NUCLEOLAR LOCALIZATION SIGNAL.
PubMed=11139147; DOI=10.1078/0171-9335-00111;
Thebault S., Basbous J., Gay B., Devaux C., Mesnard J.-M.;
"Sequence requirement for the nucleolar localization of human I-mfa
domain-containing protein (HIC p40).";
Eur. J. Cell Biol. 79:834-838(2000).
[4] {ECO:0000305}
FUNCTION, AND INTERACTION WITH AXIN1 AND LEF1.
PubMed=12192039; DOI=10.1128/MCB.22.18.6393-6405.2002;
Kusano S., Raab-Traub N.;
"I-mfa domain proteins interact with Axin and affect its regulation of
the Wnt and c-Jun N-terminal kinase signaling pathways.";
Mol. Cell. Biol. 22:6393-6405(2002).
[5] {ECO:0000305}
FUNCTION, INTERACTION WITH CCNT1 AND HIV-1 TAT (MICROBIAL INFECTION),
AND SUBCELLULAR LOCATION.
PubMed=12944466; DOI=10.1128/MCB.23.18.6373-6384.2003;
Young T.M., Wang Q., Pe'ery T., Mathews M.B.;
"The human I-mfa domain-containing protein, HIC, interacts with cyclin
T1 and modulates P-TEFb-dependent transcription.";
Mol. Cell. Biol. 23:6373-6384(2003).
[6]
FUNCTION, AND INTERACTION WITH HIV-1 TAT AND HIV-1 REV (MICROBIAL
INFECTION).
DOI=10.1186/1742-4690-3-S1-S106;
Gu L., Gautier V., Sheehy N., Tsuji T., Hayakawa H., Hall W.;
"The human I-mfa domain containing protein, HIC, interacts with HIV-1
Tat and Rev and sequesters them in the cytoplasm.";
Retrovirology 3:S106-S106(2006).
[7]
INTERACTION WITH CCNT2.
PubMed=17289077; DOI=10.1016/j.jmb.2007.01.020;
Wang Q., Young T.M., Mathews M.B., Pe'ery T.;
"Developmental regulators containing the I-mfa domain interact with T
cyclins and Tat and modulate transcription.";
J. Mol. Biol. 367:630-646(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, 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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-140 AND
SER-143, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
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: Acts as a transcriptional activator or repressor.
Inhibits the transcriptional activation of Zic family proteins
ZIC1, ZIC2 and ZIC3. Retains nuclear Zic proteins ZIC1, ZIC2 and
ZIC3 in the cytoplasm. Modulates the expression from both cellular
and viral promoters. Down-regulates Tat-dependent transcription of
the human immunodeficiency virus type 1 (HIV-1) LTR by interacting
with HIV-1 Tat and Rev and impairing their nuclear import,
probably by rendering the NLS domains inaccessible to importin-
beta. Also stimulates activation of human T-cell leukemia virus
type I (HTLV-I) LTR. Binds to the axin complex, resulting in an
increase in the level of free beta-catenin. Affects axin
regulation of the WNT and JNK signaling pathways.
{ECO:0000269|PubMed:10671520, ECO:0000269|PubMed:12192039,
ECO:0000269|PubMed:12944466, ECO:0000269|PubMed:16260749,
ECO:0000269|Ref.6}.
-!- SUBUNIT: Interacts with HAND1; leading to sequester HAND1 into the
nucleolus and prevent its activity. Interacts with ZIC2 (By
similarity). The C-terminus interacts with AXIN1, the histidine-
rich region of CCNT1/cyclin-T and weakly with LEF1
(PubMed:12192039). Interacts with CCNT2 (PubMed:17289077).
{ECO:0000250|UniProtKB:Q8BX65, ECO:0000269|PubMed:12192039,
ECO:0000269|PubMed:17289077}.
-!- SUBUNIT: (Microbial infection) Interacts (via C-terminus) with
HIV-1 Tat and Rev. {ECO:0000269|PubMed:12944466,
ECO:0000269|PubMed:16260749, ECO:0000269|Ref.6}.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleolus. Note=Also
shows a granular distribution in the cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:10671520, ECO:0000269|PubMed:11139147,
ECO:0000269|PubMed:12944466, ECO:0000269|PubMed:16260749}.
Note=Weak expression in the nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=2 {ECO:0000269|PubMed:10671520, ECO:0000269|PubMed:16260749};
Synonyms=p32 {ECO:0000269|PubMed:10671520};
IsoId=Q9P1T7-2; Sequence=Displayed;
Note=Major isoform.;
Name=1 {ECO:0000269|PubMed:10671520}; Synonyms=p40
{ECO:0000269|PubMed:10671520};
IsoId=Q9P1T7-1; Sequence=VSP_037970;
Note=Minor isoform. Initiates from a GTG codon. Contains a
Nucleolar localization signal at positions 45-63.;
-!- TISSUE SPECIFICITY: Expressed in lymphoid organs (spleen, thymus,
peripheral blood leukocytes) as well as prostate, uterus and small
intestine. {ECO:0000269|PubMed:10671520}.
-!- DOMAIN: The C2H2-type 3, 4 and 5 zinc finger domains are necessary
for transcription activation (By similarity). The cysteine-rich C-
terminus is involved in its granular distribution in the
cytoplasm. {ECO:0000250, ECO:0000269|PubMed:11139147}.
-!- SIMILARITY: Belongs to the MDFI family. {ECO:0000255}.
-----------------------------------------------------------------------
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EMBL; AF054589; AAF36998.1; -; mRNA.
EMBL; AF054589; AAF36999.1; -; mRNA.
EMBL; AY196485; AAP33842.1; -; mRNA.
CCDS; CCDS34737.1; -. [Q9P1T7-1]
CCDS; CCDS55155.1; -. [Q9P1T7-2]
RefSeq; NP_001159817.1; NM_001166345.1. [Q9P1T7-2]
RefSeq; NP_951038.1; NM_199072.4. [Q9P1T7-1]
UniGene; Hs.741413; -.
ProteinModelPortal; Q9P1T7; -.
SMR; Q9P1T7; -.
BioGrid; 119002; 7.
IntAct; Q9P1T7; 10.
STRING; 9606.ENSP00000257724; -.
iPTMnet; Q9P1T7; -.
PhosphoSitePlus; Q9P1T7; -.
SwissPalm; Q9P1T7; -.
BioMuta; MDFIC; -.
DMDM; 257051035; -.
EPD; Q9P1T7; -.
PaxDb; Q9P1T7; -.
PeptideAtlas; Q9P1T7; -.
PRIDE; Q9P1T7; -.
ProteomicsDB; 83663; -.
ProteomicsDB; 83664; -. [Q9P1T7-1]
TopDownProteomics; Q9P1T7-1; -. [Q9P1T7-1]
Ensembl; ENST00000393486; ENSP00000377126; ENSG00000135272. [Q9P1T7-2]
Ensembl; ENST00000614186; ENSP00000484656; ENSG00000135272. [Q9P1T7-1]
GeneID; 29969; -.
KEGG; hsa:29969; -.
UCSC; uc064hfm.1; human. [Q9P1T7-2]
CTD; 29969; -.
DisGeNET; 29969; -.
EuPathDB; HostDB:ENSG00000135272.9; -.
GeneCards; MDFIC; -.
HGNC; HGNC:28870; MDFIC.
HPA; HPA030716; -.
MIM; 614511; gene.
neXtProt; NX_Q9P1T7; -.
OpenTargets; ENSG00000135272; -.
PharmGKB; PA142671474; -.
eggNOG; ENOG410IKRS; Eukaryota.
eggNOG; ENOG4111J6Q; LUCA.
GeneTree; ENSGT00390000010600; -.
HOGENOM; HOG000001577; -.
HOVERGEN; HBG068212; -.
InParanoid; Q9P1T7; -.
PhylomeDB; Q9P1T7; -.
GenomeRNAi; 29969; -.
PRO; PR:Q9P1T7; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000135272; -.
CleanEx; HS_MDFIC; -.
ExpressionAtlas; Q9P1T7; baseline and differential.
Genevisible; Q9P1T7; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
GO; GO:0030957; F:Tat protein binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0007257; P:activation of JUN kinase activity; IDA:UniProtKB.
GO; GO:0042308; P:negative regulation of protein import into nucleus; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0050434; P:positive regulation of viral transcription; IDA:UniProtKB.
GO; GO:0030111; P:regulation of Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR026134; MDFI/MDFIC.
PANTHER; PTHR15304; PTHR15304; 1.
Pfam; PF15316; MDFI; 1.
1: Evidence at protein level;
Activator; Alternative initiation; Complete proteome; Cytoplasm;
Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome;
Repressor; Transcription; Transcription regulation.
CHAIN 1 246 MyoD family inhibitor domain-containing
protein.
/FTId=PRO_0000280222.
DOMAIN 74 246 MDFI.
COMPBIAS 166 243 Cys-rich.
MOD_RES 128 128 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 1 M -> MRGVRAATAAAVAATAASGLSRREAGGRAGAAAAVV
RPPGRKCGRCRRLANFPGRKRRRRRRKGLGATTGGCGEAVS
SLHPAPHSPSSVRPAGRRARRQRRGAGSAERPM (in
isoform 1).
{ECO:0000303|PubMed:10671520}.
/FTId=VSP_037970.
SEQUENCE 246 AA; 25788 MW; B8DAAE9ADF5772A0 CRC64;
MSGAGEALAP GPVGPQRVAE AGGGQLGSTA QGKCDKDNTE KDITQATNSH FTHGEMQDQS
IWGNPSDGEL IRTQPQRLPQ LQTSAQVPSG EEIGKIKNGH TGLSNGNGIH HGAKHGSADN
RKLSAPVSQK MHRKIQSSLS VNSDISKKSK VNAVFSQKTG SSPEDCCVHC ILACLFCEFL
TLCNIVLGQA SCGICTSEAC CCCCGDEMGD DCNCPCDMDC GIMDACCESS DCLEICMECC
GICFPS


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