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Transcription factor AP-2 gamma (AP2-gamma) (Activating enhancer-binding protein 2 gamma) (Transcription factor ERF-1)

 AP2C_HUMAN              Reviewed;         450 AA.
Q92754; B4DWK3; O00685; O00730; Q86V30; Q8IVB6; Q9P1X2;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
22-NOV-2017, entry version 166.
RecName: Full=Transcription factor AP-2 gamma;
Short=AP2-gamma;
AltName: Full=Activating enhancer-binding protein 2 gamma;
AltName: Full=Transcription factor ERF-1;
Name=TFAP2C;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Mammary tumor;
PubMed=8661133; DOI=10.1006/geno.1996.0351;
Williamson J.A., Bosher J.M., Skinner A., Sheer D., Williams T.,
Hurst H.C.;
"Chromosomal mapping of the human and mouse homologues of two new
members of the AP-2 family of transcription factors.";
Genomics 35:262-264(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF
203-211 AND 361-370.
TISSUE=Mammary tumor;
PubMed=9113991; DOI=10.1073/pnas.94.9.4342;
McPherson L.A., Baichwal V.R., Weigel R.J.;
"Identification of ERF-1 as a member of the AP2 transcription factor
family.";
Proc. Natl. Acad. Sci. U.S.A. 94:4342-4347(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Haselton M.D., Ibbitt C.J., Hurst H.C.;
"Characterisation of the human AP-2gamma and AP-2beta genes.";
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Mammary gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Ovary, and Skin;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-450.
TISSUE=Liver;
Nishizawa M., Ito S.;
"Structure of human AP-2gamma gene.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, AND INTERACTION WITH CITED2.
PubMed=11694877; DOI=10.1038/ng768;
Bamforth S.D., Braganca J., Eloranta J.J., Murdoch J.N., Marques F.I.,
Kranc K.R., Farza H., Henderson D.J., Hurst H.C., Bhattacharya S.;
"Cardiac malformations, adrenal agenesis, neural crest defects and
exencephaly in mice lacking Cited2, a new Tfap2 co-activator.";
Nat. Genet. 29:469-474(2001).
[9]
INTERACTION WITH CITED4.
PubMed=11744733; DOI=10.1074/jbc.M110850200;
Braganca J., Swingler T., Marques F.I.R., Jones T., Eloranta J.J.,
Hurst H.C., Shioda T., Bhattacharya S.;
"Human CREB-binding protein/p300-interacting transactivator with ED-
rich tail (CITED) 4, a new member of the CITED family, functions as a
co-activator for transcription factor AP-2.";
J. Biol. Chem. 277:8559-8565(2002).
[10]
INTERACTION WITH UBE2I, AND SUMOYLATION AT LYS-10.
PubMed=12072434; DOI=10.1074/jbc.M202780200;
Eloranta J.J., Hurst H.C.;
"Transcription factor AP-2 interacts with the SUMO-conjugating enzyme
UBC9 and is sumolated in vivo.";
J. Biol. Chem. 277:30798-30804(2002).
[11]
INTERACTION WITH CITED2.
PubMed=12586840; DOI=10.1074/jbc.M208144200;
Braganca J., Eloranta J.J., Bamforth S.D., Ibbitt J.C., Hurst H.C.,
Bhattacharya S.;
"Physical and functional interactions among AP-2 transcription
factors, p300/CREB-binding protein, and CITED2.";
J. Biol. Chem. 278:16021-16029(2003).
[12]
INTERACTION WITH WWOX, DOMAIN, AND MUTAGENESIS OF TYR-59 AND TYR-64.
PubMed=15548692; DOI=10.1158/0008-5472.CAN-04-2055;
Aqeilan R.I., Palamarchuk A., Weigel R.J., Herrero J.J., Pekarsky Y.,
Croce C.M.;
"Physical and functional interactions between the Wwox tumor
suppressor protein and the AP-2gamma transcription factor.";
Cancer Res. 64:8256-8261(2004).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, 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).
[14]
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).
[15]
INTERACTION WITH KCTD1.
PubMed=19115315; DOI=10.1002/jcb.22002;
Ding X., Luo C., Zhou J., Zhong Y., Hu X., Zhou F., Ren K., Gan L.,
He A., Zhu J., Gao X., Zhang J.;
"The interaction of KCTD1 with transcription factor AP-2alpha inhibits
its transactivation.";
J. Cell. Biochem. 106:285-295(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, 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).
[18]
FUNCTION, INTERACTION WITH MTA1, AND SUBCELLULAR LOCATION.
PubMed=24413532; DOI=10.1158/0008-5472.CAN-13-2020;
Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y.,
Kim Y.N., Seong J.K., Lee M.O.;
"Differential regulation of estrogen receptor alpha expression in
breast cancer cells by metastasis-associated protein 1.";
Cancer Res. 74:1484-1494(2014).
-!- FUNCTION: Sequence-specific DNA-binding protein that interacts
with inducible viral and cellular enhancer elements to regulate
transcription of selected genes. AP-2 factors bind to the
consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in
a large spectrum of important biological functions including
proper eye, face, body wall, limb and neural tube development.
They also suppress a number of genes including MCAM/MUC18, C/EBP
alpha and MYC. Involved in the MTA1-mediated epigenetic regulation
of ESR1 expression in breast cancer. {ECO:0000269|PubMed:11694877,
ECO:0000269|PubMed:24413532}.
-!- SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers
with other AP-2 family members (By similarity). Interacts with
WWOX. Interacts with CITED4. Interacts with UBE2I. Interacts with
KCTD1; this interaction represses transcription activation.
Interacts with CITED2 (via C-terminus); the interaction stimulates
TFAP2B-transcriptional activity. Interacts with MTA1.
{ECO:0000250, ECO:0000269|PubMed:11694877,
ECO:0000269|PubMed:11744733, ECO:0000269|PubMed:12072434,
ECO:0000269|PubMed:12586840, ECO:0000269|PubMed:15548692,
ECO:0000269|PubMed:19115315, ECO:0000269|PubMed:24413532}.
-!- INTERACTION:
Q99967:CITED2; NbExp=2; IntAct=EBI-937309, EBI-937732;
P63279:UBE2I; NbExp=5; IntAct=EBI-937309, EBI-80168;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24413532}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q92754-1; Sequence=Displayed;
Name=2;
IsoId=Q92754-2; Sequence=VSP_056501;
Note=No experimental confirmation available.;
-!- INDUCTION: During retinoic acid-mediated differentiation.
-!- DOMAIN: The PPxY motif mediates interaction with WWOX.
{ECO:0000269|PubMed:15548692}.
-!- PTM: Sumoylated on Lys-10; which inhibits transcriptional
activity. {ECO:0000269|PubMed:12072434}.
-!- SIMILARITY: Belongs to the AP-2 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Activating protein 2 entry;
URL="https://en.wikipedia.org/wiki/Activating_protein_2";
-----------------------------------------------------------------------
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EMBL; X95693; CAA64989.1; -; mRNA.
EMBL; U85658; AAC51305.1; -; mRNA.
EMBL; AJ315934; CAC86997.1; -; Genomic_DNA.
EMBL; AK301572; BAG63065.1; -; mRNA.
EMBL; AL121920; CAC10334.1; -; Genomic_DNA.
EMBL; BC035664; AAH35664.2; -; mRNA.
EMBL; BC051829; AAH51829.2; -; mRNA.
EMBL; AB041717; BAC11805.1; -; Genomic_DNA.
CCDS; CCDS13454.1; -. [Q92754-1]
RefSeq; NP_003213.1; NM_003222.3. [Q92754-1]
UniGene; Hs.473152; -.
ProteinModelPortal; Q92754; -.
BioGrid; 112880; 17.
CORUM; Q92754; -.
ELM; Q92754; -.
IntAct; Q92754; 78.
STRING; 9606.ENSP00000201031; -.
iPTMnet; Q92754; -.
PhosphoSitePlus; Q92754; -.
BioMuta; TFAP2C; -.
DMDM; 12643310; -.
EPD; Q92754; -.
MaxQB; Q92754; -.
PaxDb; Q92754; -.
PeptideAtlas; Q92754; -.
PRIDE; Q92754; -.
DNASU; 7022; -.
Ensembl; ENST00000201031; ENSP00000201031; ENSG00000087510. [Q92754-1]
GeneID; 7022; -.
KEGG; hsa:7022; -.
UCSC; uc002xya.4; human. [Q92754-1]
CTD; 7022; -.
DisGeNET; 7022; -.
EuPathDB; HostDB:ENSG00000087510.6; -.
GeneCards; TFAP2C; -.
HGNC; HGNC:11744; TFAP2C.
HPA; CAB016061; -.
HPA; CAB016079; -.
HPA; HPA055179; -.
HPA; HPA057076; -.
MIM; 601602; gene.
neXtProt; NX_Q92754; -.
OpenTargets; ENSG00000087510; -.
PharmGKB; PA36461; -.
eggNOG; KOG3811; Eukaryota.
eggNOG; ENOG410XR9E; LUCA.
GeneTree; ENSGT00550000074577; -.
HOGENOM; HOG000231737; -.
HOVERGEN; HBG002455; -.
InParanoid; Q92754; -.
KO; K09177; -.
OMA; YSHLGDP; -.
OrthoDB; EOG091G0PR6; -.
PhylomeDB; Q92754; -.
TreeFam; TF313718; -.
Reactome; R-HSA-3232118; SUMOylation of transcription factors.
Reactome; R-HSA-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
Reactome; R-HSA-8866906; TFAP2 (AP-2) family regulates transcription of other transcription factors.
Reactome; R-HSA-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
Reactome; R-HSA-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
SignaLink; Q92754; -.
GeneWiki; TFAP2C; -.
GenomeRNAi; 7022; -.
PRO; PR:Q92754; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000087510; -.
CleanEx; HS_TFAP2C; -.
ExpressionAtlas; Q92754; baseline and differential.
Genevisible; Q92754; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:UniProtKB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
InterPro; IPR004979; TF_AP2.
InterPro; IPR013854; TF_AP2_C.
InterPro; IPR008123; TF_AP2_gamma.
PANTHER; PTHR10812; PTHR10812; 1.
Pfam; PF03299; TF_AP-2; 1.
PRINTS; PR01751; AP2CTNSCPFCT.
PRINTS; PR01748; AP2TNSCPFCT.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome;
Direct protein sequencing; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 450 Transcription factor AP-2 gamma.
/FTId=PRO_0000184803.
REGION 293 424 H-S-H (helix-span-helix), dimerization.
MOTIF 59 64 PPxY motif.
COMPBIAS 30 119 Gln/Pro-rich (transactivation domain).
MOD_RES 252 252 Phosphoserine; by PKA. {ECO:0000250}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 10 10 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:12072434}.
VAR_SEQ 1 169 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056501.
MUTAGEN 59 59 Y->A: Loss of interaction with WWOX; when
associated with A-64.
{ECO:0000269|PubMed:15548692}.
MUTAGEN 64 64 Y->A: Loss of interaction with WWOX; when
associated with A-59.
{ECO:0000269|PubMed:15548692}.
SEQUENCE 450 AA; 49177 MW; 2D4F5FBC269A34A8 CRC64;
MLWKITDNVK YEEDCEDRHD GSSNGNPRVP HLSSAGQHLY SPAPPLSHTG VAEYQPPPYF
PPPYQQLAYS QSADPYSHLG EAYAAAINPL HQPAPTGSQQ QAWPGRQSQE GAGLPSHHGR
PAGLLPHLSG LEAGAVSARR DAYRRSDLLL PHAHALDAAG LAENLGLHDM PHQMDEVQNV
DDQHLLLHDQ TVIRKGPISM TKNPLNLPCQ KELVGAVMNP TEVFCSVPGR LSLLSSTSKY
KVTVAEVQRR LSPPECLNAS LLGGVLRRAK SKNGGRSLRE KLDKIGLNLP AGRRKAAHVT
LLTSLVEGEA VHLARDFAYV CEAEFPSKPV AEYLTRPHLG GRNEMAARKN MLLAAQQLCK
EFTELLSQDR TPHGTSRLAP VLETNIQNCL SHFSLITHGF GSQAICAAVS ALQNYIKEAL
IVIDKSYMNP GDQSPADSNK TLEKMEKHRK


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EIAAB41090 General transcription factor IIA subunit 2,Gtf2a2,Rat,Rattus norvegicus,TFIIA-gamma,Transcription initiation factor IIA gamma chain,Transcription initiation factor IIA subunit 2
EIAAB41092 General transcription factor IIA subunit 2,Gtf2a2,Mouse,Mus musculus,TFIIA-gamma,Transcription initiation factor IIA gamma chain,Transcription initiation factor IIA subunit 2
EIAAB41091 General transcription factor IIA subunit 2,GTF2A2,Homo sapiens,Human,TF2A2,TFIIA p12 subunit,TFIIA-12,TFIIA-gamma,TFIIAS,Transcription initiation factor IIA gamma chain,Transcription initiation factor
EIAAB27113 CAAT box DNA-binding protein subunit C,CBF-C,CCAAT-binding transcription factor subunit C,Nfyc,NF-YC,Nuclear transcription factor Y subunit C,Nuclear transcription factor Y subunit gamma,Rat,Rattus no
20-372-60120 transcription factor AP-2 alpha (activating enhancer binding protein 2 alpha) - Mouse monoclonal anti-human TFAP2A antibody; AP2-alpha; Activating enhancer-binding protein 2 alpha; AP-2 transcription 0.1 mg
EIAAB42103 Immunoglobulin enhancer-binding factor E12_E47,Pan,Pancreas specific transcription factor 1c,Ptf1c,Rat,Rattus norvegicus,Tcf3,TCF-3,Tcfe2a,Transcription factor 3,Transcription factor E2-alpha,Transcri
EIAAB42104 Alf2,Immunoglobulin enhancer-binding factor E12_E47,Me2,Mouse,Mus musculus,Tcf3,TCF-3,Tcfe2a,Transcription factor 3,Transcription factor A1,Transcription factor E2-alpha
EIAAB06706 C_EBP gamma,CCAAT_enhancer-binding protein gamma,Cebpg,GPE1-binding protein,GPE1-BP,Granulocyte colony-stimulating factor promoter element 1-binding protein,IG_EBP-1,Immunoglobulin enhancer-binding pr
18-003-44075 Transcription factor E2-alpha - Immunoglobulin enhancer-binding factor E12_E47; Transcription factor 3; TCF-3; Immunoglobulin transcription factor 1; Transcription factor ITF-1; Kappa-E2-binding facto 0.1 mg Protein A
EIAAB27116 CAAT box DNA-binding protein subunit C,Homo sapiens,Human,NFYC,NF-YC,Nuclear transcription factor Y subunit C,Nuclear transcription factor Y subunit gamma,Transactivator HSM-1_2


 

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