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AMP deaminase (AtAMPD) (EC 3.5.4.6) (Protein EMBRYONIC FACTOR 1)

 AMPD_ARATH              Reviewed;         839 AA.
O80452; B9DFX9; Q56XX1; Q93ZR9;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 2.
25-OCT-2017, entry version 124.
RecName: Full=AMP deaminase {ECO:0000303|PubMed:15918887};
Short=AtAMPD {ECO:0000303|PubMed:15918887};
EC=3.5.4.6 {ECO:0000305};
AltName: Full=Protein EMBRYONIC FACTOR 1 {ECO:0000303|PubMed:15918887};
Name=AMPD {ECO:0000303|PubMed:15918887};
Synonyms=FAC1 {ECO:0000303|PubMed:15918887};
OrderedLocusNames=At2g38280 {ECO:0000312|Araport:AT2G38280};
ORFNames=F16M14.21 {ECO:0000312|EMBL:AAC27176.2};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF ASP-598, FUNCTION,
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=cv. Landsberg erecta;
PubMed=15918887; DOI=10.1111/j.1365-313X.2005.02411.x;
Xu J., Zhang H.-Y., Xie C.-H., Xue H.-W., Dijkhuis P., Liu C.-M.;
"EMBRYONIC FACTOR 1 encodes an AMP deaminase and is essential for the
zygote to embryo transition in Arabidopsis.";
Plant J. 42:743-756(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-357.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-140 AND
SER-203, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Root;
PubMed=18433157; DOI=10.1021/pr8000173;
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,
Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
Hirt H.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by
mass spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[8]
INTERACTION WITH AHK4.
PubMed=18642946; DOI=10.1021/pr0703831;
Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T.,
Heyl A.;
"Toward an interaction map of the two-component signaling pathway of
Arabidopsis thaliana.";
J. Proteome Res. 7:3649-3660(2008).
[9]
CRYSTALLIZATION, AND X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 140-839
IN COMPLEX WITH COFORMYCIN 5'-PHOSPHATE AND ZINC IONS.
PubMed=16511144; DOI=10.1107/S1744309105019792;
Han B.W., Bingman C.A., Mahnke D.K., Sabina R.L., Phillips G.N. Jr.;
"Crystallization and preliminary X-ray crystallographic analysis of
adenosine 5'-monophosphate deaminase (AMPD) from Arabidopsis thaliana
in complex with coformycin 5'-phosphate.";
Acta Crystallogr. F 61:740-742(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[11]
INTERACTION WITH EER5.
PubMed=19843313; DOI=10.1111/j.1365-313X.2009.04048.x;
Lu Q., Tang X., Tian G., Wang F., Liu K., Nguyen V., Kohalmi S.E.,
Keller W.A., Tsang E.W., Harada J.J., Rothstein S.J., Cui Y.;
"Arabidopsis homolog of the yeast TREX-2 mRNA export complex:
components and anchoring nucleoporin.";
Plant J. 61:259-270(2010).
[12]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 140-839 IN COMPLEX WITH
COFORMYCIN 5'-PHOSPHATE; PHOSPHATE AND ZINC IONS, CATALYTIC ACTIVITY,
SUBUNIT, COFACTOR, SUBCELLULAR LOCATION, ENZYME REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16543243; DOI=10.1074/jbc.M513009200;
Han B.W., Bingman C.A., Mahnke D.K., Bannen R.M., Bednarek S.Y.,
Sabina R.L., Phillips G.N. Jr.;
"Membrane association, mechanism of action, and structure of
Arabidopsis embryonic factor 1 (FAC1).";
J. Biol. Chem. 281:14939-14947(2006).
-!- FUNCTION: AMP deaminase plays a critical role in energy
metabolism. Essential for the transition from zygote to embryo.
{ECO:0000269|PubMed:15918887}.
-!- CATALYTIC ACTIVITY: AMP + H(2)O = IMP + NH(3).
{ECO:0000269|PubMed:16543243}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:16543243};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:16543243};
-!- ENZYME REGULATION: Activated by ATP. Activated by sulfate ions (in
vitro). Inhibited by phosphate ions.
{ECO:0000269|PubMed:16543243}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=6.7 mM for AMP (in the absence of ATP)
{ECO:0000269|PubMed:16543243};
KM=0.26 mM for AMP (in the presence of 1 mM ATP)
{ECO:0000269|PubMed:16543243};
Vmax=17 umol/min/mg enzyme (in the absence of ATP)
{ECO:0000269|PubMed:16543243};
Vmax=375 umol/min/mg enzyme (in the presence of 1 mM ATP)
{ECO:0000269|PubMed:16543243};
-!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway;
IMP from AMP: step 1/1.
-!- SUBUNIT: Homodimer. Interacts with AHK4. Interacts with EER5
(PubMed:19843313). {ECO:0000269|PubMed:16511144,
ECO:0000269|PubMed:16543243, ECO:0000269|PubMed:18642946,
ECO:0000269|PubMed:19843313}.
-!- INTERACTION:
Q9C5U0:AHK4; NbExp=2; IntAct=EBI-1807679, EBI-1100775;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16543243};
Single-pass membrane protein {ECO:0000269|PubMed:16543243}.
Microsome membrane {ECO:0000269|PubMed:16543243}. Note=Might be
associated with the inner mitochondrial membrane. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves,
flowers, pollen grains, pollen tubes and siliques, and at a lower
level in stems. {ECO:0000269|PubMed:15918887}.
-!- DEVELOPMENTAL STAGE: Expressed in both male and female
gametophytes, at the zygote stage, in the endosperm, and during
early embryo development. Observed in cotyledonary embryos and in
the basal part of the embryo, but not in the suspensor or in
mature embryos. Also expressed during somatic embryogenesis.
{ECO:0000269|PubMed:15918887}.
-!- SIMILARITY: Belongs to the metallo-dependent hydrolases
superfamily. Adenosine and AMP deaminases family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD94943.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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EMBL; AC003028; AAC27176.2; -; Genomic_DNA.
EMBL; CP002685; AEC09516.1; -; Genomic_DNA.
EMBL; CP002685; AEC09517.1; -; Genomic_DNA.
EMBL; AY056301; AAL07150.1; -; mRNA.
EMBL; AY133852; AAM91786.1; -; mRNA.
EMBL; AK316943; BAH19646.1; -; mRNA.
EMBL; AK221552; BAD94943.1; ALT_SEQ; mRNA.
PIR; T01259; T01259.
RefSeq; NP_565886.1; NM_129384.3.
RefSeq; NP_850294.1; NM_179963.3.
UniGene; At.12466; -.
PDB; 2A3L; X-ray; 3.34 A; A=139-839.
PDBsum; 2A3L; -.
ProteinModelPortal; O80452; -.
SMR; O80452; -.
BioGrid; 3750; 5.
IntAct; O80452; 2.
STRING; 3702.AT2G38280.1; -.
BindingDB; O80452; -.
ChEMBL; CHEMBL2366458; -.
iPTMnet; O80452; -.
PaxDb; O80452; -.
EnsemblPlants; AT2G38280.1; AT2G38280.1; AT2G38280.
EnsemblPlants; AT2G38280.2; AT2G38280.2; AT2G38280.
GeneID; 818408; -.
Gramene; AT2G38280.1; AT2G38280.1; AT2G38280.
Gramene; AT2G38280.2; AT2G38280.2; AT2G38280.
KEGG; ath:AT2G38280; -.
Araport; AT2G38280; -.
TAIR; locus:2042902; AT2G38280.
eggNOG; KOG1096; Eukaryota.
eggNOG; COG1816; LUCA.
HOGENOM; HOG000092200; -.
InParanoid; O80452; -.
KO; K01490; -.
OMA; NMTWMIQ; -.
OrthoDB; EOG093602O5; -.
PhylomeDB; O80452; -.
BioCyc; ARA:AT2G38280-MONOMER; -.
BRENDA; 3.5.4.6; 399.
Reactome; R-ATH-6798695; Neutrophil degranulation.
Reactome; R-ATH-74217; Purine salvage.
SABIO-RK; O80452; -.
UniPathway; UPA00591; UER00663.
EvolutionaryTrace; O80452; -.
PRO; PR:O80452; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; O80452; baseline and differential.
Genevisible; O80452; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:TAIR.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0003876; F:AMP deaminase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
GO; GO:0009737; P:response to abscisic acid; IDA:TAIR.
CDD; cd01319; AMPD; 1.
InterPro; IPR006650; A/AMP_deam_AS.
InterPro; IPR001365; A/AMP_deaminase_dom.
InterPro; IPR006329; AMPD.
InterPro; IPR032466; Metal_Hydrolase.
PANTHER; PTHR11359; PTHR11359; 1.
Pfam; PF00962; A_deaminase; 1.
SUPFAM; SSF51556; SSF51556; 1.
TIGRFAMs; TIGR01429; AMP_deaminase; 1.
PROSITE; PS00485; A_DEAMINASE; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; ATP-binding; Complete proteome;
Endoplasmic reticulum; Hydrolase; Membrane; Metal-binding; Microsome;
Nucleotide metabolism; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Zinc.
CHAIN 1 839 AMP deaminase.
/FTId=PRO_0000238455.
TRANSMEM 8 28 Helical. {ECO:0000255}.
NP_BIND 289 296 ATP. {ECO:0000255}.
REGION 462 467 Substrate binding.
REGION 737 740 Substrate binding.
COMPBIAS 86 92 Poly-Gly.
COMPBIAS 158 161 Poly-Asp.
ACT_SITE 681 681 Proton acceptor. {ECO:0000305}.
METAL 391 391 Zinc; catalytic.
METAL 393 393 Zinc; catalytic.
METAL 659 659 Zinc; catalytic.
METAL 736 736 Zinc; catalytic.
BINDING 393 393 Substrate.
BINDING 662 662 Substrate.
MOD_RES 134 134 Phosphoserine.
{ECO:0000244|PubMed:18433157}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000244|PubMed:18433157}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:18433157}.
MUTAGEN 598 598 D->N: In fac1-1; zygote-lethal phenotype.
{ECO:0000269|PubMed:15918887}.
CONFLICT 324 324 D -> G (in Ref. 5; BAH19646).
{ECO:0000305}.
TURN 215 217 {ECO:0000244|PDB:2A3L}.
TURN 244 247 {ECO:0000244|PDB:2A3L}.
HELIX 248 259 {ECO:0000244|PDB:2A3L}.
HELIX 325 338 {ECO:0000244|PDB:2A3L}.
HELIX 342 373 {ECO:0000244|PDB:2A3L}.
HELIX 374 376 {ECO:0000244|PDB:2A3L}.
TURN 382 384 {ECO:0000244|PDB:2A3L}.
STRAND 387 393 {ECO:0000244|PDB:2A3L}.
TURN 394 396 {ECO:0000244|PDB:2A3L}.
HELIX 400 412 {ECO:0000244|PDB:2A3L}.
STRAND 420 422 {ECO:0000244|PDB:2A3L}.
STRAND 425 427 {ECO:0000244|PDB:2A3L}.
HELIX 429 436 {ECO:0000244|PDB:2A3L}.
STRAND 461 463 {ECO:0000244|PDB:2A3L}.
HELIX 464 467 {ECO:0000244|PDB:2A3L}.
HELIX 474 479 {ECO:0000244|PDB:2A3L}.
STRAND 482 484 {ECO:0000244|PDB:2A3L}.
TURN 485 490 {ECO:0000244|PDB:2A3L}.
HELIX 491 502 {ECO:0000244|PDB:2A3L}.
STRAND 505 515 {ECO:0000244|PDB:2A3L}.
STRAND 518 521 {ECO:0000244|PDB:2A3L}.
HELIX 523 532 {ECO:0000244|PDB:2A3L}.
TURN 533 535 {ECO:0000244|PDB:2A3L}.
STRAND 539 548 {ECO:0000244|PDB:2A3L}.
HELIX 551 554 {ECO:0000244|PDB:2A3L}.
STRAND 557 559 {ECO:0000244|PDB:2A3L}.
HELIX 564 570 {ECO:0000244|PDB:2A3L}.
HELIX 573 579 {ECO:0000244|PDB:2A3L}.
HELIX 581 583 {ECO:0000244|PDB:2A3L}.
TURN 585 587 {ECO:0000244|PDB:2A3L}.
HELIX 588 591 {ECO:0000244|PDB:2A3L}.
STRAND 594 601 {ECO:0000244|PDB:2A3L}.
TURN 617 619 {ECO:0000244|PDB:2A3L}.
STRAND 622 624 {ECO:0000244|PDB:2A3L}.
HELIX 628 646 {ECO:0000244|PDB:2A3L}.
TURN 647 650 {ECO:0000244|PDB:2A3L}.
STRAND 661 664 {ECO:0000244|PDB:2A3L}.
HELIX 667 675 {ECO:0000244|PDB:2A3L}.
HELIX 683 687 {ECO:0000244|PDB:2A3L}.
HELIX 689 698 {ECO:0000244|PDB:2A3L}.
STRAND 702 704 {ECO:0000244|PDB:2A3L}.
HELIX 706 709 {ECO:0000244|PDB:2A3L}.
TURN 710 713 {ECO:0000244|PDB:2A3L}.
HELIX 721 726 {ECO:0000244|PDB:2A3L}.
STRAND 731 733 {ECO:0000244|PDB:2A3L}.
HELIX 738 741 {ECO:0000244|PDB:2A3L}.
STRAND 744 746 {ECO:0000244|PDB:2A3L}.
HELIX 747 759 {ECO:0000244|PDB:2A3L}.
HELIX 763 776 {ECO:0000244|PDB:2A3L}.
HELIX 781 787 {ECO:0000244|PDB:2A3L}.
TURN 790 793 {ECO:0000244|PDB:2A3L}.
STRAND 794 796 {ECO:0000244|PDB:2A3L}.
HELIX 797 799 {ECO:0000244|PDB:2A3L}.
HELIX 802 805 {ECO:0000244|PDB:2A3L}.
HELIX 809 826 {ECO:0000244|PDB:2A3L}.
TURN 827 829 {ECO:0000244|PDB:2A3L}.
SEQUENCE 839 AA; 95130 MW; 188F1F4A589A17DA CRC64;
MEPNIYQLAL AALFGASFVA VSGFFMHFKA LNLVLERGKE RKENPDGDEP QNPTLVRRRS
QVRRKVNDQY GRSPASLPDA TPFTDGGGGG GGDTGRSNGH VYVDEIPPGL PRLHTPSEGR
ASVHGASSIR KTGSFVRPIS PKSPVASASA FESVEESDDD DNLTNSEGLD ASYLQANGDN
EMPADANEEQ ISMAASSMIR SHSVSGDLHG VQPDPIAADI LRKEPEQETF VRLNVPLEVP
TSDEVEAYKC LQECLELRKR YVFQETVAPW EKEVISDPST PKPNTEPFAH YPQGKSDHCF
EMQDGVVHVF ANKDAKEDLF PVADATAFFT DLHHVLKVIA AGNIRTLCHR RLVLLEQKFN
LHLMLNADKE FLAQKSAPHR DFYNVRKVDT HVHHSACMNQ KHLLRFIKSK LRKEPDEVVI
FRDGTYLTLR EVFESLDLTG YDLNVDLLDV HADKSTFHRF DKFNLKYNPC GQSRLREIFL
KQDNLIQGRF LGEITKQVFS DLEASKYQMA EYRISIYGRK MSEWDQLASW IVNNDLYSEN
VVWLIQLPRL YNIYKDMGIV TSFQNILDNI FIPLFEATVD PDSHPQLHVF LKQVVGFDLV
DDESKPERRP TKHMPTPAQW TNAFNPAFSY YVYYCYANLY VLNKLRESKG MTTITLRPHS
GEAGDIDHLA ATFLTCHSIA HGINLRKSPV LQYLYYLAQI GLAMSPLSNN SLFLDYHRNP
FPVFFLRGLN VSLSTDDPLQ IHLTKEPLVE EYSIAASVWK LSACDLCEIA RNSVYQSGFS
HALKSHWIGK DYYKRGPDGN DIHKTNVPHI RVEFRDTIWK EEMQQVYLGK AVISDEVVP


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EIAAB34200 ADAR3,ADARB2,Double-stranded RNA-specific editase B2,dsRNA adenosine deaminase B2,Homo sapiens,Human,RED2,RNA-dependent adenosine deaminase 3,RNA-editing deaminase 2,RNA-editing enzyme 2
EIAAB12870 AHCTF1,ELYS,Embryonic large molecule derived from yolk sac,Homo sapiens,Human,MSTP108,Protein ELYS,Protein MEL-28,Putative AT-hook-containing transcription factor 1,TMBS62
EIAAB10033 Cwc15,Ed1,Embryonic development factor 1,mED1,Mouse,Mus musculus,Protein CWC15 homolog
EIAAB28856 Factor located in oocytes permitting embryonic development,Floped,mOEP19,Mouse,Mus musculus,Oep19,Oocyte- and embryo-specific protein 19,Oocyte-expressed protein homolog,Ooep,Sddr,STAT3 downstream gen
28-637 TEF (thyrotroph embryonic factor) is a member of the PAR bZip (proline and acidic amino acid-rich basic leucine zipper) transcription factor family. It accumulates with robust circadian rhythms in tis 0.1 mg
28-837 TEF (thyrotroph embryonic factor) is a member of the PAR bZip (proline and acidic amino acid-rich basic leucine zipper) transcription factor family. It accumulates with robust circadian rhythms in tis 0.05 mg
EIAAB34264 ATP6AP2,ATP6IP2,ATP6M8-9,ATPase H(+)-transporting lysosomal accessory protein 2,ATPase H(+)-transporting lysosomal-interacting protein 2,CAPER,ELDF10,Embryonic liver differentiation factor 10,ER-local
EIAAB10659 dCMP deaminase,DCTD,Deoxycytidylate deaminase,Homo sapiens,Human
EIAAB10657 dCMP deaminase,Dctd,Deoxycytidylate deaminase,Rat,Rattus norvegicus
EIAAB10658 dCMP deaminase,Dctd,Deoxycytidylate deaminase,Mouse,Mus musculus
ARP37237_T100 Thyrotroph embryonic factor (TEF) 0.1 mg
ARP37237_T100 Thyrotroph embryonic factor (TEF) 100 µg
ARP38279_P050 Thyrotroph embryonic factor (TEF) 50 µg


 

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