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Protein AATF (Apoptosis-antagonizing transcription factor) (Rb-binding protein Che-1)

 AATF_HUMAN              Reviewed;         560 AA.
Q9NY61; A6NCJ6; B3KQ26; Q9P0A4; Q9UNX5;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 141.
RecName: Full=Protein AATF;
AltName: Full=Apoptosis-antagonizing transcription factor;
AltName: Full=Rb-binding protein Che-1;
Name=AATF; Synonyms=CHE1, DED; ORFNames=HSPC277;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=11027528; DOI=10.1006/bbrc.2000.3480;
Lindfors K., Halttunen T., Huotari P., Nupponen N., Vihinen M.,
Visakorpi T., Maki M., Kainulainen H.;
"Identification of novel transcription factor-like gene from human
intestinal cells.";
Biochem. Biophys. Res. Commun. 276:660-666(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH POLR2J AND RB1, AND
TISSUE SPECIFICITY.
TISSUE=Skeletal muscle;
PubMed=10783144;
Fanciulli M., Bruno T., Di Padova M., De Angelis R., Iezzi S.,
Iacobini C., Floridi A., Passananti C.;
"Identification of a novel partner of RNA polymerase II subunit 11,
Che-1, which interacts with and affects the growth suppression
function of Rb.";
FASEB J. 14:904-912(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=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 [LARGE SCALE MRNA] OF 361-560.
TISSUE=Umbilical cord blood;
Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
"Human partial CDS from CD34+ stem cells.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, PHOSPHORYLATION AT THE G1/S TRANSITION, AND INTERACTION WITH
RB1; RBL1 AND RBL2.
PubMed=12450794; DOI=10.1016/S1535-6108(02)00182-4;
Bruno T., De Angelis R., De Nicola F., Barbato C., Di Padova M.,
Corbi N., Libri V., Benassi B., Mattei E., Chersi A., Soddu S.,
Floridi A., Passananti C., Fanciulli M.;
"Che-1 affects cell growth by interfering with the recruitment of
HDAC1 by Rb.";
Cancer Cell 2:387-399(2002).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
Greco A., Hochstrasser D.F., Diaz J.-J.;
"Functional proteomic analysis of human nucleolus.";
Mol. Biol. Cell 13:4100-4109(2002).
[10]
FUNCTION, AND INTERACTION WITH SP1.
PubMed=12847090; DOI=10.1074/jbc.M306694200;
Di Padova M., Bruno T., De Nicola F., Iezzi S., D'Angelo C., Gallo R.,
Nicosia D., Corbi N., Biroccio A., Floridi A., Passananti C.,
Fanciulli M.;
"Che-1 arrests human colon carcinoma cell proliferation by displacing
HDAC1 from the p21WAF1/CIP1 promoter.";
J. Biol. Chem. 278:36496-36504(2003).
[11]
INTERACTION WITH MAPT.
PubMed=14697667; DOI=10.1016/j.mcn.2003.08.002;
Barbato C., Corbi N., Canu N., Fanciulli M., Serafino A., Ciotti M.,
Libri V., Bruno T., Amadoro G., De Angelis R., Calissano P.,
Passananti C.;
"Rb binding protein Che-1 interacts with Tau in cerebellar granule
neurons. Modulation during neuronal apoptosis.";
Mol. Cell. Neurosci. 24:1038-1050(2003).
[12]
FUNCTION, AND INTERACTION WITH PAWR.
PubMed=14627703; DOI=10.1074/jbc.M309811200;
Guo Q., Xie J.;
"AATF inhibits aberrant production of amyloid beta peptide 1-42 by
interacting directly with Par-4.";
J. Biol. Chem. 279:4596-4603(2004).
[13]
FUNCTION.
PubMed=15207272; DOI=10.1016/j.nbd.2004.02.003;
Xie J., Guo Q.;
"AATF protects neural cells against oxidative damage induced by
amyloid beta-peptide.";
Neurobiol. Dis. 16:150-157(2004).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-320 AND
SER-321, 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).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-320 AND
SER-321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-316; SER-320
AND SER-321, 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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-316; SER-320
AND SER-321, 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-63; SER-150;
SER-155; SER-203 AND SER-273, 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).
-!- FUNCTION: May function as a general inhibitor of the histone
deacetylase HDAC1. Binding to the pocket region of RB1 may
displace HDAC1 from RB1/E2F complexes, leading to activation of
E2F target genes and cell cycle progression. Conversely,
displacement of HDAC1 from SP1 bound to the CDKN1A promoter leads
to increased expression of this CDK inhibitor and blocks cell
cycle progression. Also antagonizes PAWR mediated induction of
aberrant amyloid peptide production in Alzheimer disease
(presenile and senile dementia), although the molecular basis for
this phenomenon has not been described to date.
{ECO:0000269|PubMed:12450794, ECO:0000269|PubMed:12847090,
ECO:0000269|PubMed:14627703, ECO:0000269|PubMed:15207272}.
-!- SUBUNIT: Binds PAWR, POLR2J, RB1/RB, RBL1/P107, RBL2/P130, and
SP1. May also bind MAPT.
-!- INTERACTION:
Q13315:ATM; NbExp=3; IntAct=EBI-372428, EBI-495465;
O96017:CHEK2; NbExp=4; IntAct=EBI-372428, EBI-1180783;
Q6ZWQ9:Myl12a (xeno); NbExp=3; IntAct=EBI-372428, EBI-8034418;
Q8NEJ9:NGDN; NbExp=3; IntAct=EBI-372428, EBI-9995414;
Q04206:RELA; NbExp=3; IntAct=EBI-372428, EBI-73886;
P08047:SP1; NbExp=2; IntAct=EBI-372428, EBI-298336;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:12429849}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at high
levels in brain, heart, kidney, placenta and thymus.
{ECO:0000269|PubMed:10783144, ECO:0000269|PubMed:11027528}.
-!- PTM: Hyperphosphorylated during the G1/S phase transition.
-!- SIMILARITY: Belongs to the AATF family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD52016.1; Type=Frameshift; Positions=355, 365, 487, 498, 503; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/AATFID534ch17q11.html";
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EMBL; AJ249940; CAB57451.2; -; mRNA.
EMBL; AF083208; AAD52016.1; ALT_FRAME; mRNA.
EMBL; AK057229; BAG51888.1; -; mRNA.
EMBL; AC003103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471199; EAW57575.1; -; Genomic_DNA.
EMBL; BC000591; AAH00591.1; -; mRNA.
EMBL; AF161395; AAF28955.1; -; mRNA.
CCDS; CCDS32632.1; -.
RefSeq; NP_036270.1; NM_012138.3.
UniGene; Hs.195740; -.
ProteinModelPortal; Q9NY61; -.
SMR; Q9NY61; -.
BioGrid; 117743; 74.
CORUM; Q9NY61; -.
ELM; Q9NY61; -.
IntAct; Q9NY61; 27.
MINT; MINT-131397; -.
STRING; 9606.ENSP00000225402; -.
iPTMnet; Q9NY61; -.
PhosphoSitePlus; Q9NY61; -.
BioMuta; AATF; -.
DMDM; 71152211; -.
SWISS-2DPAGE; Q9NY61; -.
EPD; Q9NY61; -.
MaxQB; Q9NY61; -.
PaxDb; Q9NY61; -.
PeptideAtlas; Q9NY61; -.
PRIDE; Q9NY61; -.
TopDownProteomics; Q9NY61; -.
DNASU; 26574; -.
Ensembl; ENST00000619387; ENSP00000477848; ENSG00000275700.
Ensembl; ENST00000620004; ENSP00000481894; ENSG00000276072.
GeneID; 26574; -.
KEGG; hsa:26574; -.
UCSC; uc002hni.3; human.
CTD; 26574; -.
DisGeNET; 26574; -.
EuPathDB; HostDB:ENSG00000275700.4; -.
GeneCards; AATF; -.
HGNC; HGNC:19235; AATF.
HPA; HPA004940; -.
MIM; 608463; gene.
neXtProt; NX_Q9NY61; -.
OpenTargets; ENSG00000275700; -.
PharmGKB; PA128395780; -.
eggNOG; KOG2773; Eukaryota.
eggNOG; ENOG410XWGK; LUCA.
GeneTree; ENSGT00390000000288; -.
HOGENOM; HOG000007555; -.
HOVERGEN; HBG080805; -.
InParanoid; Q9NY61; -.
KO; K14782; -.
OMA; EVLLKWD; -.
OrthoDB; EOG091G0F1H; -.
PhylomeDB; Q9NY61; -.
TreeFam; TF324341; -.
Reactome; R-HSA-193648; NRAGE signals death through JNK.
SIGNOR; Q9NY61; -.
ChiTaRS; AATF; human.
GeneWiki; Apoptosis-antagonizing_transcription_factor; -.
GenomeRNAi; 26574; -.
PRO; PR:Q9NY61; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000275700; -.
CleanEx; HS_AATF; -.
ExpressionAtlas; Q9NY61; baseline and differential.
Genevisible; Q9NY61; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043522; F:leucine zipper domain binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0048156; F:tau protein binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:UniProtKB.
GO; GO:0040016; P:embryonic cleavage; IEA:Ensembl.
GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IDA:UniProtKB.
GO; GO:0032929; P:negative regulation of superoxide anion generation; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0042254; P:ribosome biogenesis; IEA:Ensembl.
InterPro; IPR025160; AATF.
InterPro; IPR012617; AATF_C.
Pfam; PF13339; AATF-Che1; 1.
Pfam; PF08164; TRAUB; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Nucleus; Phosphoprotein;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 560 Protein AATF.
/FTId=PRO_0000056616.
REGION 273 315 POLR2J binding.
REGION 316 372 RB1 binding.
REGION 373 472 RB1 and SP1 binding.
COMPBIAS 96 195 Glu-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 61 61 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 63 63 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 155 155 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 273 273 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 316 316 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CONFLICT 2 3 AG -> GR (in Ref. 2; AAD52016).
{ECO:0000305}.
CONFLICT 4 5 Missing (in Ref. 2; AAD52016).
{ECO:0000305}.
CONFLICT 139 139 S -> T (in Ref. 2; AAD52016).
{ECO:0000305}.
CONFLICT 262 262 L -> V (in Ref. 2; AAD52016).
{ECO:0000305}.
CONFLICT 272 272 S -> A (in Ref. 2; AAD52016).
{ECO:0000305}.
CONFLICT 306 306 L -> V (in Ref. 2; AAD52016).
{ECO:0000305}.
CONFLICT 402 402 D -> C (in Ref. 2; AAD52016).
{ECO:0000305}.
SEQUENCE 560 AA; 63133 MW; EC493EF3B4C3A199 CRC64;
MAGPQPLALQ LEQLLNPRPS EADPEADPEE ATAARVIDRF DEGEDGEGDF LVVGSIRKLA
SASLLDTDKR YCGKTTSRKA WNEDHWEQTL PGSSDEEISD EEGSGDEDSE GLGLEEYDED
DLGAAEEQEC GDHRESKKSR SHSAKTPGFS VQSISDFEKF TKGMDDLGSS EEEEDEESGM
EEGDDAEDSQ GESEEDRAGD RNSEDDGVVM TFSSVKVSEE VEKGRAVKNQ IALWDQLLEG
RIKLQKALLT TNQLPQPDVF PLFKDKGGPE FSSALKNSHK ALKALLRSLV GLQEELLFQY
PDTRYLVDGT KPNAGSEEIS SEDDELVEEK KQQRRRVPAK RKLEMEDYPS FMAKRFADFT
VYRNRTLQKW HDKTKLASGK LGKGFGAFER SILTQIDHIL MDKERLLRRT QTKRSVYRVL
GKPEPAAQPV PESLPGEPEI LPQAPANAHL KDLDEEIFDD DDFYHQLLRE LIERKTSSLD
PNDQVAMGRQ WLAIQKLRSK IHKKVDRKAS KGRKLRFHVL SKLLSFMAPI DHTTMNDDAR
TELYRSLFGQ LHPPDEGHGD


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E04A0531 Rabbit Apoptosis Antagonizing Transcription Factor ELISA , AATF
E08A0531 Canine Apoptosis Antagonizing Transcription Factor Elisa Kit (AATF) 96 Tests/kit
E-EL-H0477 Human AATF (Apoptosis Antagonizing Transcription Factor) ELISA Kit 96T
E05A0531 Guinea Apoptosis Antagonizing Transcription Factor Elisa Kit (AATF) 96 Tests/kit
E07A0531 Porcine Apoptosis Antagonizing Transcription Factor Elisa Kit (AATF) 96 Tests/kit
E06A0531 Goat Apoptosis Antagonizing Transcription Factor ELISA , AATF
E07A0531 Porcine Apoptosis Antagonizing Transcription Factor ELISA , AATF 96 Tests/kit
E01A0531 Human Apoptosis Antagonizing Transcription Factor Elisa Kit (AATF) 96 Tests/kit
GWB-E1AACE Anti- AATF (apoptosis antagonizing transcription factor) Antibody
E04A0531 Rabbit Apoptosis Antagonizing Transcription Factor ELISA , AATF 96 Tests/kit
E-EL-P1367 Porcine AATF (Apoptosis Antagonizing Transcription Factor) ELISA Kit 96T
E12A0531 Chicken Apoptosis Antagonizing Transcription Factor ELISA , AATF 96 Tests/kit


 

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