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Transcription factor AP-4 (Activating enhancer-binding protein 4) (Class C basic helix-loop-helix protein 41) (bHLHc41)

 TFAP4_HUMAN             Reviewed;         338 AA.
Q01664; O60409;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
18-JUL-2018, entry version 176.
RecName: Full=Transcription factor AP-4;
AltName: Full=Activating enhancer-binding protein 4;
AltName: Full=Class C basic helix-loop-helix protein 41;
Short=bHLHc41;
Name=TFAP4; Synonyms=BHLHC41;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7933101;
Ou S.H., Garcia-Martinez L.F., Paulssen E.J., Gaynor R.B.;
"Role of flanking E box motifs in human immunodeficiency virus type 1
TATA element function.";
J. Virol. 68:7188-7199(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-218.
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 18-338, AND PARTIAL PROTEIN SEQUENCE.
PubMed=2123466; DOI=10.1101/gad.4.10.1741;
Hu Y.-F., Luescher B., Admon A., Mermod N., Tjian R.;
"Transcription factor AP-4 contains multiple dimerization domains that
regulate dimer specificity.";
Genes Dev. 4:1741-1752(1990).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, 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).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-139, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-124 AND
SER-139, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-139, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[11]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-147; LYS-187; LYS-189 AND
LYS-285, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Transcription factor that activates both viral and
cellular genes by binding to the symmetrical DNA sequence 5'-
CAGCTG-3'.
-!- SUBUNIT: Efficient DNA binding requires dimerization with another
bHLH protein. Homodimer.
-!- INTERACTION:
Q96B26:EXOSC8; NbExp=5; IntAct=EBI-2514218, EBI-371922;
P55040:GEM; NbExp=2; IntAct=EBI-2514218, EBI-744104;
Q08379:GOLGA2; NbExp=5; IntAct=EBI-2514218, EBI-618309;
Q13077:TRAF1; NbExp=3; IntAct=EBI-2514218, EBI-359224;
-!- SUBCELLULAR LOCATION: Nucleus.
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EMBL; S73885; AAB32235.1; -; mRNA.
EMBL; AC004653; AAC17116.1; -; Genomic_DNA.
EMBL; BC010576; AAH10576.1; -; mRNA.
EMBL; X57435; CAA40683.1; -; mRNA.
CCDS; CCDS10510.1; -.
PIR; I56893; I56893.
RefSeq; NP_003214.1; NM_003223.2.
UniGene; Hs.513305; -.
ProteinModelPortal; Q01664; -.
SMR; Q01664; -.
BioGrid; 112881; 115.
DIP; DIP-53627N; -.
IntAct; Q01664; 25.
MINT; Q01664; -.
STRING; 9606.ENSP00000204517; -.
iPTMnet; Q01664; -.
PhosphoSitePlus; Q01664; -.
BioMuta; TFAP4; -.
DMDM; 1729833; -.
EPD; Q01664; -.
MaxQB; Q01664; -.
PaxDb; Q01664; -.
PeptideAtlas; Q01664; -.
PRIDE; Q01664; -.
ProteomicsDB; 57980; -.
DNASU; 7023; -.
Ensembl; ENST00000204517; ENSP00000204517; ENSG00000090447.
GeneID; 7023; -.
KEGG; hsa:7023; -.
UCSC; uc010uxg.3; human.
CTD; 7023; -.
DisGeNET; 7023; -.
EuPathDB; HostDB:ENSG00000090447.11; -.
GeneCards; TFAP4; -.
HGNC; HGNC:11745; TFAP4.
HPA; HPA001912; -.
MIM; 600743; gene.
neXtProt; NX_Q01664; -.
OpenTargets; ENSG00000090447; -.
PharmGKB; PA36462; -.
eggNOG; KOG0561; Eukaryota.
eggNOG; ENOG4111JPE; LUCA.
GeneTree; ENSGT00390000015189; -.
HOGENOM; HOG000294087; -.
HOVERGEN; HBG061473; -.
InParanoid; Q01664; -.
KO; K09108; -.
OMA; HHVNVVT; -.
OrthoDB; EOG091G194I; -.
PhylomeDB; Q01664; -.
TreeFam; TF316489; -.
SIGNOR; Q01664; -.
GeneWiki; TFAP4; -.
GenomeRNAi; 7023; -.
PRO; PR:Q01664; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000090447; -.
CleanEx; HS_TFAP4; -.
ExpressionAtlas; Q01664; baseline and differential.
Genevisible; Q01664; HS.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0017053; C:transcriptional repressor complex; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:UniProtKB.
GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:UniProtKB.
GO; GO:0071157; P:negative regulation of cell cycle arrest; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IDA:UniProtKB.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
Activator; Complete proteome; Direct protein sequencing; DNA-binding;
Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 338 Transcription factor AP-4.
/FTId=PRO_0000127458.
DOMAIN 48 99 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 100 120 Leucine-zipper 1.
REGION 151 179 Leucine-zipper 2.
COMPBIAS 193 222 Gln-rich.
COMPBIAS 225 244 Pro-rich.
MOD_RES 123 123 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 147 147 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 187 187 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 189 189 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 285 285 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 218 218 Q -> H (in dbSNP:rs251732).
{ECO:0000269|PubMed:15616553}.
/FTId=VAR_059346.
SEQUENCE 338 AA; 38726 MW; 540C008658596B83 CRC64;
MEYFMVPTQK VPSLQHFRKT EKEVIGGLCS LANIPLTPET QRDQERRIRR EIANSNERRR
MQSINAGFQS LKTLIPHTDG EKLSKAAILQ QTAEYIFSLE QEKTRLLQQN TQLKRFIQEL
SGSSPKRRRA EDKDEGIGSP DIWEDEKAED LRREMIELRQ QLDKERSVRM MLEEQVRSLE
AHMYPEKLKV IAQQVQLQQQ QEQVRLLHQE KLEREQQQLR TQLLPPPAPT HHPTVIVPAP
PPPPSHHINV VTMGPSSVIN SVSTSRQNLD TIVQAIQHIE GTQEKQELEE EQRRAVIVKP
VRSCPEAPTS DTASDSEASD SDAMDQSREE PSGDGELP


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