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Transcription factor cep-1 (C.elegans p53-like protein 1)

 CEP1_CAEEL              Reviewed;         644 AA.
Q20646; Q564Z1; Q95V13;
05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 2.
31-JAN-2018, entry version 123.
RecName: Full=Transcription factor cep-1 {ECO:0000312|EMBL:AAL28139.1};
AltName: Full=C.elegans p53-like protein 1;
Name=cep-1 {ECO:0000312|WormBase:F52B5.5a};
ORFNames=F52B5.5 {ECO:0000312|WormBase:F52B5.5a};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1] {ECO:0000305, ECO:0000312|EMBL:AAL28139.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND DISRUPTION
PHENOTYPE.
PubMed=11696333; DOI=10.1016/S0960-9822(01)00534-6;
Schumacher B., Hofmann K., Boulton S.J., Gartner A.;
"The C. elegans homolog of the p53 tumor suppressor is required for
DNA damage-induced apoptosis.";
Curr. Biol. 11:1722-1727(2001).
[2] {ECO:0000305, ECO:0000312|EMBL:CAA99857.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, AND DISRUPTION PHENOTYPE.
PubMed=11557844; DOI=10.1126/science.1065486;
Derry W.B., Putzke A.P., Rothman J.H.;
"Caenorhabditis elegans p53: role in apoptosis, meiosis, and stress
resistance.";
Science 294:591-595(2001).
[4] {ECO:0000305}
FUNCTION.
PubMed=12445383; DOI=10.1016/S0960-9822(02)01262-9;
Hofmann E.R., Milstein S., Boulton S.J., Ye M., Hofmann J.J.,
Stergiou L., Gartner A., Vidal M., Hengartner M.O.;
"Caenorhabditis elegans HUS-1 is a DNA damage checkpoint protein
required for genome stability and EGL-1-mediated apoptosis.";
Curr. Biol. 12:1908-1918(2002).
[5] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15273685; DOI=10.1038/ng1396;
Deng X., Hofmann E.R., Villanueva A., Hobert O., Capodieci P.,
Veach D.R., Yin X., Campodonico L., Glekas A., Cordon-Cardo C.,
Clarkson B., Bornmann W.G., Fuks Z., Hengartner M.O., Kolesnick R.;
"Caenorhabditis elegans ABL-1 antagonizes p53-mediated germline
apoptosis after ionizing irradiation.";
Nat. Genet. 36:906-912(2004).
[6] {ECO:0000305}
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=15707894; DOI=10.1016/j.cell.2004.12.009;
Schumacher B., Hanazawa M., Lee M.-H., Nayak S., Volkmann K.,
Hofmann E.R., Hengartner M.O., Schedl T., Gartner A.;
"Translational repression of C. elegans p53 by GLD-1 regulates DNA
damage-induced apoptosis.";
Cell 120:357-368(2005).
[7] {ECO:0000305}
FUNCTION.
PubMed=15605074; DOI=10.1038/sj.cdd.4401539;
Schumacher B., Schertel C., Wittenburg N., Tuck S., Mitani S.,
Gartner A., Conradt B., Shaham S.;
"C. elegans ced-13 can promote apoptosis and is induced in response to
DNA damage.";
Cell Death Differ. 12:153-161(2005).
[8] {ECO:0000305}
FUNCTION.
PubMed=16319925; DOI=10.1038/sj.emboj.7600896;
Garcia-Muse T., Boulton S.J.;
"Distinct modes of ATR activation after replication stress and DNA
double-strand breaks in Caenorhabditis elegans.";
EMBO J. 24:4345-4355(2005).
[9] {ECO:0000305}
FUNCTION, INDUCTION, AND PHOSPHORYLATION.
PubMed=17276923; DOI=10.1016/j.cub.2006.12.038;
Quevedo C., Kaplan D.R., Derry W.B.;
"AKT-1 regulates DNA-damage-induced germline apoptosis in C.
elegans.";
Curr. Biol. 17:286-292(2007).
[10] {ECO:0000305}
FUNCTION.
PubMed=17186023; DOI=10.1038/sj.cdd.4402075;
Derry W.B., Bierings R., van Iersel M., Satkunendran T., Reinke V.,
Rothman J.H.;
"Regulation of developmental rate and germ cell proliferation in
Caenorhabditis elegans by the p53 gene network.";
Cell Death Differ. 14:662-670(2007).
[11] {ECO:0000305}
FUNCTION.
PubMed=17347667; DOI=10.1038/sj.cdd.4402115;
Stergiou L., Doukoumetzidis K., Sendoel A., Hengartner M.O.;
"The nucleotide excision repair pathway is required for UV-C-induced
apoptosis in Caenorhabditis elegans.";
Cell Death Differ. 14:1129-1138(2007).
[12] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17895432; DOI=10.1093/gerona/62.9.951;
Arum O., Johnson T.E.;
"Reduced expression of the Caenorhabditis elegans p53 ortholog cep-1
results in increased longevity.";
J. Gerontol. 62:951-959(2007).
[13] {ECO:0000305}
FUNCTION.
PubMed=18627611; DOI=10.1186/1471-2164-9-334;
Greiss S., Schumacher B., Grandien K., Rothblatt J., Gartner A.;
"Transcriptional profiling in C. elegans suggests DNA damage dependent
apoptosis as an ancient function of the p53 family.";
BMC Genomics 9:334-334(2008).
[14] {ECO:0000305}
FUNCTION.
PubMed=18836529; DOI=10.1371/journal.pone.0003354;
Masse I., Molin L., Mouchiroud L., Vanhems P., Palladino F.,
Billaud M., Solari F.;
"A novel role for the SMG-1 kinase in lifespan and oxidative stress
resistance in Caenorhabditis elegans.";
PLoS ONE 3:E3354-E3354(2008).
[15] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19015549; DOI=10.1534/genetics.107.080515;
Luo J., Shah S., Riabowol K., Mains P.E.;
"The Caenorhabditis elegans ing-3 gene regulates ionizing radiation-
induced germ-cell apoptosis in a p53-associated pathway.";
Genetics 181:473-482(2009).
[16]
FUNCTION, INTERACTION WITH PRMT-5 AND CBP-1, AND DISRUPTION PHENOTYPE.
PubMed=19521535; DOI=10.1371/journal.pgen.1000514;
Yang M., Sun J., Sun X., Shen Q., Gao Z., Yang C.;
"Caenorhabditis elegans protein arginine methyltransferase PRMT-5
negatively regulates DNA damage-induced apoptosis.";
PLoS Genet. 5:E1000514-E1000514(2009).
[17] {ECO:0000305}
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=21901106; DOI=10.1371/journal.pgen.1002238;
Rutkowski R., Dickinson R., Stewart G., Craig A., Schimpl M.,
Keyse S.M., Gartner A.;
"Regulation of Caenorhabditis elegans p53/CEP-1-dependent germ cell
apoptosis by Ras/MAPK signaling.";
PLoS Genet. 7:E1002238-E1002238(2011).
[18]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=26598553; DOI=10.1242/jcs.174201;
Min H., Shim Y.H., Kawasaki I.;
"Loss of PGL-1 and PGL-3, members of a family of constitutive germ-
granule components, promotes germline apoptosis in C. elegans.";
J. Cell Sci. 129:341-353(2016).
[19]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), FUNCTION, AND DNA-BINDING.
PubMed=15242600; DOI=10.1016/j.str.2004.05.007;
Huyen Y., Jeffrey P.D., Derry W.B., Rothman J.H., Pavletich N.P.,
Stavridi E.S., Halazonetis T.D.;
"Structural differences in the DNA binding domains of human p53 and
its C. elegans ortholog Cep-1.";
Structure 12:1237-1243(2004).
[20]
STRUCTURE BY NMR OF 514-644, DIMERIZATION, MUTAGENESIS OF LYS-544;
ARG-551 AND GLU-552, AND ZINC-BINDING SITES.
PubMed=17581633; DOI=10.1038/sj.emboj.7601764;
Ou H.D., Loehr F., Vogel V., Maentele W., Doetsch V.;
"Structural evolution of C-terminal domains in the p53 family.";
EMBO J. 26:3463-3473(2007).
-!- FUNCTION: Transcriptional activator that binds the same DNA
consensus sequence as p53 (PubMed:11696333, PubMed:15242600). Has
a role in normal development to ensure proper meiotic chromosome
segregation (PubMed:11557844, PubMed:12445383). Promotes apoptosis
under conditions of cellular and genotoxic stress in response to
DNA damage, hypoxia, or starvation (PubMed:11696333,
PubMed:11557844, PubMed:12445383, PubMed:15273685,
PubMed:17186023, PubMed:18836529, PubMed:21901106). However, not
required for DNA repair in response to UV-C or to regulate cell-
cycle progression (PubMed:17347667). Regulates germline apoptosis
in response to DNA damage (PubMed:11696333, PubMed:15273685,
PubMed:15707894, PubMed:16319925, PubMed:17276923,
PubMed:17186023, PubMed:19015549, PubMed:26598553). Required for
induction of ced-13 in response to DNA damage (PubMed:15605074).
Regulates germline proliferation by activating phg-1
(PubMed:17186023). Regulates DNA damage-induced apoptosis by
inducing transcription of the programmed cell death activator egl-
1 (PubMed:12445383, PubMed:19521535). Negatively regulates
lifespan (PubMed:17895432, PubMed:18836529).
{ECO:0000269|PubMed:11557844, ECO:0000269|PubMed:11696333,
ECO:0000269|PubMed:12445383, ECO:0000269|PubMed:15242600,
ECO:0000269|PubMed:15273685, ECO:0000269|PubMed:15605074,
ECO:0000269|PubMed:15707894, ECO:0000269|PubMed:16319925,
ECO:0000269|PubMed:17186023, ECO:0000269|PubMed:17276923,
ECO:0000269|PubMed:17347667, ECO:0000269|PubMed:17895432,
ECO:0000269|PubMed:18627611, ECO:0000269|PubMed:18836529,
ECO:0000269|PubMed:19015549, ECO:0000269|PubMed:19521535,
ECO:0000269|PubMed:21901106, ECO:0000269|PubMed:26598553}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:17581633};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:17581633};
-!- SUBUNIT: Homodimer (PubMed:15707894). Interacts (via C-terminus
domain) with prmt-5; not methylated by prmt-5 (PubMed:19521535).
Interacts with cbp-1 (via HAT domain); cep-1 transcriptional
activity may be inhibited by interaction with methylated cbp-1
(PubMed:19521535). Component of a complex that contains prmt-5 and
cbp-1 (PubMed:19521535). {ECO:0000269|PubMed:15707894,
ECO:0000269|PubMed:19521535, ECO:0000303|PubMed:19521535}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11557844}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=a {ECO:0000269|PubMed:11696333};
IsoId=Q20646-1; Sequence=Displayed;
Name=b {ECO:0000269|PubMed:9851916};
IsoId=Q20646-2; Sequence=VSP_053085;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in pharyngeal muscle and neurons.
{ECO:0000269|PubMed:11557844}.
-!- DEVELOPMENTAL STAGE: Expressed in embryos and larvae
(PubMed:11557844, PubMed:15707894). Expressed in the distal zone
of mitotic germline and in late pachytene, diplotene and
diakinesis stages of meiotic germline (PubMed:11557844,
PubMed:15707894, PubMed:21901106). {ECO:0000269|PubMed:11557844,
ECO:0000269|PubMed:15707894, ECO:0000269|PubMed:21901106}.
-!- INDUCTION: By DNA damage. {ECO:0000269|PubMed:17276923}.
-!- PTM: Phosphorylated in response to IR-induced DNA damage which is
thought to be mediated by akt-1. {ECO:0000269|PubMed:17276923}.
-!- DISRUPTION PHENOTYPE: Reduced numbers of germ cell corpses,
hypersensitive to the lethal effects of hypoxia, increase in
production of males (Him phenotype), decreased lifespan and in
extreme cases embryonic lethality (PubMed:11557844,
PubMed:11696333, PubMed:15273685, PubMed:17895432,
PubMed:19015549, PubMed:26598553). In cep-1 and prmt-5 double
mutants, germline cell death and up-regulation of egl-1 mRNA
induced by gamma irradiation is prevented (PubMed:19521535).
{ECO:0000269|PubMed:11557844, ECO:0000269|PubMed:11696333,
ECO:0000269|PubMed:15273685, ECO:0000269|PubMed:17895432,
ECO:0000269|PubMed:19015549, ECO:0000269|PubMed:19521535,
ECO:0000269|PubMed:26598553}.
-!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}.
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EMBL; AF440800; AAL28139.1; -; mRNA.
EMBL; Z75541; CAA99857.2; -; Genomic_DNA.
EMBL; Z75541; CAI79201.1; -; Genomic_DNA.
PIR; T22495; T22495.
RefSeq; NP_001021478.1; NM_001026307.5. [Q20646-1]
RefSeq; NP_001021479.1; NM_001026308.4. [Q20646-2]
UniGene; Cel.18659; -.
PDB; 1T4W; X-ray; 2.10 A; A=223-418.
PDB; 2RP5; NMR; -; A/B=514-644.
PDBsum; 1T4W; -.
PDBsum; 2RP5; -.
ProteinModelPortal; Q20646; -.
SMR; Q20646; -.
BioGrid; 38050; 2.
IntAct; Q20646; 1.
MINT; MINT-3386616; -.
STRING; 6239.F52B5.5a.1; -.
EPD; Q20646; -.
PaxDb; Q20646; -.
PeptideAtlas; Q20646; -.
EnsemblMetazoa; F52B5.5a.1; F52B5.5a.1; WBGene00000467. [Q20646-1]
EnsemblMetazoa; F52B5.5a.2; F52B5.5a.2; WBGene00000467. [Q20646-1]
GeneID; 172616; -.
KEGG; cel:CELE_F52B5.5; -.
UCSC; F52B5.5a.1; c. elegans.
CTD; 172616; -.
WormBase; F52B5.5a; CE29805; WBGene00000467; cep-1. [Q20646-1]
WormBase; F52B5.5b; CE38369; WBGene00000467; cep-1. [Q20646-2]
eggNOG; ENOG410K8NG; Eukaryota.
eggNOG; ENOG4110K6I; LUCA.
HOGENOM; HOG000111546; -.
InParanoid; Q20646; -.
OMA; VAYPRRD; -.
OrthoDB; EOG091G0O0N; -.
EvolutionaryTrace; Q20646; -.
PRO; PR:Q20646; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00000467; -.
GO; GO:0005730; C:nucleolus; IDA:WormBase.
GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:WormBase.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:UniProtKB.
GO; GO:0045132; P:meiotic chromosome segregation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:WormBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IMP:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
GO; GO:0042594; P:response to starvation; IMP:WormBase.
GO; GO:0042770; P:signal transduction in response to DNA damage; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd08367; P53; 1.
Gene3D; 2.60.40.720; -; 1.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
InterPro; IPR011615; p53_DNA-bd.
InterPro; IPR015367; Trans_fact_CEP1_DNA-bd.
Pfam; PF09287; CEP1-DNA_bind; 1.
SUPFAM; SSF49417; SSF49417; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Apoptosis;
Complete proteome; DNA-binding; Metal-binding; Nucleus;
Reference proteome; Transcription; Transcription regulation;
Tumor suppressor; Zinc.
CHAIN 1 644 Transcription factor cep-1.
/FTId=PRO_0000371248.
DNA_BIND 223 418 {ECO:0000255}.
REGION 528 555 Required for tertiary structure stability
of the protein.
{ECO:0000269|PubMed:17581633}.
METAL 307 307 Zinc. {ECO:0000269|PubMed:17581633}.
METAL 310 310 Zinc. {ECO:0000269|PubMed:17581633}.
METAL 361 361 Zinc. {ECO:0000269|PubMed:17581633}.
METAL 365 365 Zinc. {ECO:0000269|PubMed:17581633}.
VAR_SEQ 1 447 Missing (in isoform b).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_053085.
MUTAGEN 544 544 K->L: Disrupts homodimer formation.
{ECO:0000269|PubMed:17581633}.
MUTAGEN 551 551 R->L: Disrupts homodimer formation.
{ECO:0000269|PubMed:17581633}.
MUTAGEN 552 552 E->L: Disrupts homodimer formation.
{ECO:0000269|PubMed:17581633}.
STRAND 225 230 {ECO:0000244|PDB:1T4W}.
HELIX 232 235 {ECO:0000244|PDB:1T4W}.
STRAND 239 245 {ECO:0000244|PDB:1T4W}.
STRAND 251 255 {ECO:0000244|PDB:1T4W}.
STRAND 261 268 {ECO:0000244|PDB:1T4W}.
TURN 271 275 {ECO:0000244|PDB:1T4W}.
STRAND 279 287 {ECO:0000244|PDB:1T4W}.
STRAND 289 291 {ECO:0000244|PDB:1T4W}.
HELIX 293 296 {ECO:0000244|PDB:1T4W}.
HELIX 308 312 {ECO:0000244|PDB:1T4W}.
STRAND 316 318 {ECO:0000244|PDB:1T4W}.
STRAND 322 327 {ECO:0000244|PDB:1T4W}.
STRAND 329 335 {ECO:0000244|PDB:1T4W}.
STRAND 339 345 {ECO:0000244|PDB:1T4W}.
STRAND 352 361 {ECO:0000244|PDB:1T4W}.
HELIX 363 365 {ECO:0000244|PDB:1T4W}.
HELIX 368 371 {ECO:0000244|PDB:1T4W}.
STRAND 373 382 {ECO:0000244|PDB:1T4W}.
STRAND 388 399 {ECO:0000244|PDB:1T4W}.
HELIX 403 416 {ECO:0000244|PDB:1T4W}.
STRAND 532 538 {ECO:0000244|PDB:2RP5}.
HELIX 539 554 {ECO:0000244|PDB:2RP5}.
STRAND 559 561 {ECO:0000244|PDB:2RP5}.
HELIX 563 566 {ECO:0000244|PDB:2RP5}.
TURN 571 573 {ECO:0000244|PDB:2RP5}.
HELIX 576 581 {ECO:0000244|PDB:2RP5}.
TURN 585 587 {ECO:0000244|PDB:2RP5}.
HELIX 588 594 {ECO:0000244|PDB:2RP5}.
HELIX 601 608 {ECO:0000244|PDB:2RP5}.
HELIX 612 616 {ECO:0000244|PDB:2RP5}.
HELIX 620 622 {ECO:0000244|PDB:2RP5}.
HELIX 623 641 {ECO:0000244|PDB:2RP5}.
SEQUENCE 644 AA; 74569 MW; AED566E5461212B0 CRC64;
MEPDDSQLSD ILKDARIPDS QDIGVNLTQN LSFDTVQKMI DGVFTPIFSQ GTEDSLEKDI
LKTPGISTIY NGILGNGEET KKRTPKISDA FEPDLNTSGD VFDSDKSEDG LMNDESYLSN
TTLSQVVLDS QKYEYLRVRT EEEQQLVIEK RARERFIRKS MKIAEETALS YENDGSRELS
ETMTQKVTQM DFTETNVPFD GNDESSNLAV RVQSDMNLNE DCEKWMEIDV LKQKVAKSSD
MAFAISSEHE KYLWTKMGCL VPIQVKWKLD KRHFNSNLSL RIRFVKYDKK ENVEYAIRNP
RSDVMKCRSH TEREQHFPFD SFFYIRNSEH EFSYSAEKGS TFTLIMYPGA VQANFDIIFM
CQEKCLDLDD RRKTMCLAVF LDDENGNEIL HAYIKQVRIV AYPRRDWKNF CEREDAKQKD
FRFPELPAYK KASLESINIK QEVNLENMFN VTNTTAQMEP STSYSSPSNS NNRKRFLNEC
DSPNNDYTMM HRTPPVTGYA SRLHGCVPPI ETEHENCQSP SMKRSRCTNY SFRTLTLSTA
EYTKVVEFLA REAKVPRYTW VPTQVVSHIL PTEGLERFLT AIKAGHDSVL FNANGIYTMG
DMIREFEKHN DIFERIGIDS SKLSKYYEAF LSFYRIQEAM KLPK


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18-003-42165 Early growth response protein 1 - EGR-1; Krox-24 protein; Transcription factor Zif268; Nerve growth factor-induced protein A; NGFI-A; Transcription factor ETR103; Zinc finger protein 225; AT225 Polycl 0.05 mg Aff Pur
EIAAB31754 Emb,Mouse,Mus musculus,Octamer-binding transcription factor EMB,POU domain, class 6, transcription factor 1,Pou6f1,Transcription regulatory protein MCP-1
EIAAB41684 Mouse,Mus musculus,Protein S-II-T1,Tcea2,Testis-specific S-II,Transcription elongation factor A protein 2,Transcription elongation factor S-II protein 2,Transcription elongation factor TFIIS.l
EIAAB41685 Homo sapiens,Human,TCEA2,Testis-specific S-II,Transcription elongation factor A protein 2,Transcription elongation factor S-II protein 2,Transcription elongation factor TFIIS.l
EIAAB41688 Homo sapiens,Human,TCEA3,TFIISH,Transcription elongation factor A protein 3,Transcription elongation factor S-II protein 3,Transcription elongation factor TFIIS.h
U0416h CLIA AT225,Early growth response protein 1,EGR1,EGR-1,Homo sapiens,Human,KROX24,Nerve growth factor-induced protein A,NGFI-A,Transcription factor ETR103,Transcription factor Zif268,Zinc finger protein 96T
EIAAB12289 E4F,E4F transcription factor 1,E4F1,Homo sapiens,Human,p120E4F,p50E4F,Putative E3 ubiquitin-protein ligase E4F1,Transcription factor E4F,Transcription factor E4F1
EIAAB42084 Homo sapiens,Human,Mitochondrial transcription factor 1,MtTF1,mtTFA,TCF6,TCF-6,TCF6L2,TFAM,Transcription factor 6,Transcription factor 6-like 2,Transcription factor A, mitochondrial
EIAAB41690 Mouse,Mus musculus,Tcea3,Tfiish,Transcription elongation factor A protein 3,Transcription elongation factor S-II protein 3,Transcription elongation factor TFIIS.h
EIAAB41683 Mouse,Mus musculus,Tcea1,Tceat,Transcription elongation factor A protein 1,Transcription elongation factor S-II protein 1,Transcription elongation factor TFIIS.o
EIAAB31740 Homo sapiens,Human,Oct-11,Octamer-binding protein 11,Octamer-binding transcription factor 11,OTF11,OTF-11,PLA1,POU domain, class 2, transcription factor 3,POU2F3,Transcription factor PLA-1,Transcripti
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


 

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