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Telomere zinc finger-associated protein (TZAP) (Krueppel-related zinc finger protein 3) (hKR3) (Zinc finger and BTB domain-containing protein 48) (Zinc finger protein 855)

 TZAP_HUMAN              Reviewed;         688 AA.
P10074; Q5SY19;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
25-OCT-2017, entry version 183.
RecName: Full=Telomere zinc finger-associated protein {ECO:0000303|PubMed:28082411};
Short=TZAP {ECO:0000303|PubMed:28082411};
AltName: Full=Krueppel-related zinc finger protein 3 {ECO:0000303|PubMed:9516840};
Short=hKR3 {ECO:0000303|Ref.12};
AltName: Full=Zinc finger and BTB domain-containing protein 48 {ECO:0000312|HGNC:HGNC:4930};
AltName: Full=Zinc finger protein 855 {ECO:0000312|HGNC:HGNC:4930};
Name=ZBTB48 {ECO:0000312|HGNC:HGNC:4930};
Synonyms=HKR3 {ECO:0000303|PubMed:9516840},
TZAP {ECO:0000303|PubMed:28082411},
ZNF855 {ECO:0000312|HGNC:HGNC:4930};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], DNA-BINDING, AND FUNCTION.
PubMed=7969177; DOI=10.1128/MCB.14.12.8438;
Sugawara M., Scholl T., Ponath P.D., Strominger J.L.;
"A factor that regulates the class II major histocompatibility complex
gene DPA is a member of a subfamily of zinc finger proteins that
includes a Drosophila developmental control protein.";
Mol. Cell. Biol. 14:8438-8450(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=9516840; DOI=10.1016/S0959-8049(97)00279-7;
Maris J.M., Jensen J., Sulman E.P., Beltinger C.P., Allen C.,
Biegel J.A., Brodeur G.M., White P.S.;
"Human Kruppel-related 3 (HKR3): a candidate for the 1p36
neuroblastoma tumour suppressor gene?";
Eur. J. Cancer 33:1991-1996(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 461-488.
PubMed=2850480; DOI=10.1128/MCB.8.8.3104;
Ruppert J.M., Kinzler K.W., Wong A.J., Bigner S.H., Kao F.T.,
Law M.L., Seuanez H.N., O'Brien S.J., Vogelstein B.;
"The GLI-Kruppel family of human genes.";
Mol. Cell. Biol. 8:3104-3113(1988).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[7]
FUNCTION, AND INTERACTION WITH EP300.
PubMed=24382891; DOI=10.1074/jbc.M113.526855;
Yoon J.H., Choi W.I., Jeon B.N., Koh D.I., Kim M.K., Kim M.H., Kim J.,
Hur S.S., Kim K.S., Hur M.W.;
"Human Kruppel-related 3 (HKR3) is a novel transcription activator of
alternate reading frame (ARF) gene.";
J. Biol. Chem. 289:4018-4031(2014).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-171 AND
SER-179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[9]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF HIS-596.
PubMed=28500257; DOI=10.15252/embr.201744095;
Jahn A., Rane G., Paszkowski-Rogacz M., Sayols S., Bluhm A., Han C.T.,
Draskovic I., Londono-Vallejo J.A., Kumar A.P., Buchholz F.,
Butter F., Kappei D.;
"ZBTB48 is both a vertebrate telomere-binding protein and a
transcriptional activator.";
EMBO Rep. 18:929-946(2017).
[10]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-143 AND LYS-263, 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).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=28082411; DOI=10.1126/science.aah6752;
Li J.S., Miralles Fuste J., Simavorian T., Bartocci C., Tsai J.,
Karlseder J., Lazzerini Denchi E.;
"TZAP: A telomere-associated protein involved in telomere length
control.";
Science 355:638-641(2017).
[12]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 2-120.
Structural genomics consortium (SGC);
"Crystal structure of the human BTB domain of the krueppel-related
zinc finger protein 3 (hKR3).";
Submitted (NOV-2007) to the PDB data bank.
-!- FUNCTION: Telomere-binding protein that acts as a regulator of
telomere length (PubMed:28500257, PubMed:28082411). Directly binds
the telomeric double-stranded 5'-TTAGGG-3' repeat
(PubMed:28500257, PubMed:28082411). Preferentially binds to
telomeres that have a low concentration of shelterin complex and
acts as a regulator of telomere length by initiating telomere
trimming, a process that prevents the accumulation of aberrantly
long telomeres (PubMed:28082411). Also acts as a transcription
regulator that binds to promoter regions (PubMed:7969177,
PubMed:24382891, PubMed:28500257). Regulates expression of a small
subset of genes, including MTFP1 (PubMed:28500257). Regulates
expression the J and/or S elements in MHC II promoter
(PubMed:7969177). Acts as a negative regulator of cell
proliferation by specifically activating expression of ARF, a
tumor suppressor isoform of CDKN2A (PubMed:24382891).
{ECO:0000269|PubMed:24382891, ECO:0000269|PubMed:28082411,
ECO:0000269|PubMed:28500257, ECO:0000269|PubMed:7969177}.
-!- SUBUNIT: Interacts with EP300 (PubMed:24382891).
{ECO:0000269|PubMed:24382891}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-744864, EBI-744864;
Q92997:DVL3; NbExp=3; IntAct=EBI-744864, EBI-739789;
Q9NWQ4:GPATCH2L; NbExp=3; IntAct=EBI-744864, EBI-5666657;
P60370:KRTAP10-5; NbExp=3; IntAct=EBI-744864, EBI-10172150;
Q9Y5B8:NME7; NbExp=5; IntAct=EBI-744864, EBI-744782;
Q8WV44:TRIM41; NbExp=3; IntAct=EBI-744864, EBI-725997;
Q9H2G4:TSPYL2; NbExp=4; IntAct=EBI-744864, EBI-947459;
Q96BR9:ZBTB8A; NbExp=6; IntAct=EBI-744864, EBI-742740;
Q9H9D4:ZNF408; NbExp=4; IntAct=EBI-744864, EBI-347633;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere
{ECO:0000269|PubMed:28082411, ECO:0000269|PubMed:28500257}.
Note=Directly binds the telomeric double-stranded 5'-TTAGGG-3'
repeat (PubMed:28500257, PubMed:28082411). According to a report,
preferentially binds to long telomeres that have a low
concentration of shelterin complex, competing with the telomeric
repeat binding factors TERF1 and TERF2 (PubMed:28082411).
According to another report, binds telomeres regardless of their
length (PubMed:28500257). {ECO:0000269|PubMed:28082411,
ECO:0000269|PubMed:28500257}.
-!- TISSUE SPECIFICITY: Detected in adrenal gland and neuroblastoma.
{ECO:0000269|PubMed:9516840}.
-!- DOMAIN: The C2H2-type zinc fingers mediate binding to the
telomeric double-stranded 5'-TTAGGG-3' repeats (PubMed:28082411).
The last C2H2-type zinc finger is required for telomeric-binding
(PubMed:28500257). {ECO:0000269|PubMed:28082411,
ECO:0000269|PubMed:28500257}.
-!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- CAUTION: According to a study, preferentially binds to long
telomeres that have a low concentration of shelterin complex
(PubMed:28082411). According to another report, binds telomeres
regardless of their length (PubMed:28500257).
{ECO:0000269|PubMed:28082411, ECO:0000269|PubMed:28500257}.
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EMBL; L16896; AAA65124.1; -; mRNA.
EMBL; U45325; AAB08973.1; -; Genomic_DNA.
EMBL; U45324; AAB08973.1; JOINED; Genomic_DNA.
EMBL; AL591866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC013573; AAH13573.1; -; mRNA.
EMBL; M20677; AAA35989.1; -; Genomic_DNA.
CCDS; CCDS84.1; -.
PIR; A56360; A56360.
RefSeq; NP_001265576.1; NM_001278647.1.
RefSeq; NP_001265577.1; NM_001278648.1.
RefSeq; NP_005332.1; NM_005341.3.
UniGene; Hs.502330; -.
PDB; 3B84; X-ray; 1.74 A; A=4-120.
PDBsum; 3B84; -.
ProteinModelPortal; P10074; -.
SMR; P10074; -.
BioGrid; 109349; 106.
IntAct; P10074; 33.
MINT; MINT-8247379; -.
STRING; 9606.ENSP00000366902; -.
iPTMnet; P10074; -.
PhosphoSitePlus; P10074; -.
BioMuta; ZBTB48; -.
DMDM; 1708212; -.
EPD; P10074; -.
MaxQB; P10074; -.
PaxDb; P10074; -.
PeptideAtlas; P10074; -.
PRIDE; P10074; -.
DNASU; 3104; -.
Ensembl; ENST00000377674; ENSP00000366902; ENSG00000204859.
GeneID; 3104; -.
KEGG; hsa:3104; -.
UCSC; uc001anx.5; human.
CTD; 3104; -.
DisGeNET; 3104; -.
EuPathDB; HostDB:ENSG00000204859.11; -.
GeneCards; ZBTB48; -.
HGNC; HGNC:4930; ZBTB48.
HPA; HPA030417; -.
MIM; 165270; gene.
neXtProt; NX_P10074; -.
OpenTargets; ENSG00000204859; -.
PharmGKB; PA162409481; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00900000141025; -.
HOGENOM; HOG000049146; -.
HOVERGEN; HBG000087; -.
InParanoid; P10074; -.
KO; K10519; -.
OMA; NVIRKPC; -.
OrthoDB; EOG091G02KC; -.
PhylomeDB; P10074; -.
TreeFam; TF331310; -.
ChiTaRS; ZBTB48; human.
EvolutionaryTrace; P10074; -.
GenomeRNAi; 3104; -.
PRO; PR:P10074; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000204859; -.
CleanEx; HS_ZBTB48; -.
ExpressionAtlas; P10074; baseline and differential.
Genevisible; P10074; HS.
GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0010833; P:telomere maintenance via telomere lengthening; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR011333; SKP1/BTB/POZ.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00651; BTB; 1.
SMART; SM00225; BTB; 1.
SMART; SM00355; ZnF_C2H2; 11.
SUPFAM; SSF54695; SSF54695; 1.
SUPFAM; SSF57667; SSF57667; 6.
PROSITE; PS50097; BTB; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
1: Evidence at protein level;
3D-structure; Activator; Chromosome; Complete proteome; DNA-binding;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Telomere; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 688 Telomere zinc finger-associated protein.
/FTId=PRO_0000047272.
DOMAIN 26 89 BTB. {ECO:0000255|PROSITE-
ProRule:PRU00037}.
ZN_FING 291 313 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 319 341 C2H2-type 2; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 350 372 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 378 401 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 407 430 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 436 459 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 465 487 C2H2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 493 515 C2H2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 521 544 C2H2-type 9. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 550 572 C2H2-type 10. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 578 600 C2H2-type 11. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
MOD_RES 169 169 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 171 171 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CROSSLNK 143 143 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 263 263 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 675 675 S -> A (in dbSNP:rs2229330).
/FTId=VAR_052925.
MUTAGEN 596 596 H->A: Abolishes binding to the telomeric
double-stranded 5'-TTAGGG-3' repeat.
{ECO:0000269|PubMed:28500257}.
CONFLICT 201 201 P -> S (in Ref. 1; AAA65124).
{ECO:0000305}.
CONFLICT 244 244 D -> S (in Ref. 1; AAA65124).
{ECO:0000305}.
CONFLICT 350 351 FT -> LP (in Ref. 1; AAA65124).
{ECO:0000305}.
CONFLICT 607 607 N -> K (in Ref. 1; AAA65124).
{ECO:0000305}.
HELIX 5 22 {ECO:0000244|PDB:3B84}.
STRAND 28 32 {ECO:0000244|PDB:3B84}.
STRAND 35 39 {ECO:0000244|PDB:3B84}.
HELIX 41 47 {ECO:0000244|PDB:3B84}.
HELIX 49 55 {ECO:0000244|PDB:3B84}.
TURN 56 59 {ECO:0000244|PDB:3B84}.
STRAND 63 65 {ECO:0000244|PDB:3B84}.
HELIX 67 69 {ECO:0000244|PDB:3B84}.
HELIX 70 82 {ECO:0000244|PDB:3B84}.
TURN 89 91 {ECO:0000244|PDB:3B84}.
HELIX 92 101 {ECO:0000244|PDB:3B84}.
HELIX 105 113 {ECO:0000244|PDB:3B84}.
SEQUENCE 688 AA; 77054 MW; EBECCE3D6CBBD524 CRC64;
MDGSFVQHSV RVLQELNKQR EKGQYCDATL DVGGLVFKAH WSVLACCSHF FQSLYGDGSG
GSVVLPAGFA EIFGLLLDFF YTGHLALTSG NRDQVLLAAR ELRVPEAVEL CQSFKPKTSV
GQAAGGQSGL GPPASQNVNS HVKEPAGLEE EEVSRTLGLV PRDQEPRGSH SPQRPQLHSP
AQSEGPSSLC GKLKQALKPC PLEDKKPEDC KVPPRPLEAE GAQLQGGSNE WEVVVQVEDD
GDGDYMSEPE AVLTRRKSNV IRKPCAAEPA LSAGSLAAEP AENRKGTAVP VECPTCHKKF
LSKYYLKVHN RKHTGEKPFE CPKCGKCYFR KENLLEHEAR NCMNRSEQVF TCSVCQETFR
RRMELRVHMV SHTGEMPYKC SSCSQQFMQK KDLQSHMIKL HGAPKPHACP TCAKCFLSRT
ELQLHEAFKH RGEKLFVCEE CGHRASSRNG LQMHIKAKHR NERPHVCEFC SHAFTQKANL
NMHLRTHTGE KPFQCHLCGK TFRTQASLDK HNRTHTGERP FSCEFCEQRF TEKGPLLRHV
ASRHQEGRPH FCQICGKTFK AVEQLRVHVR RHKGVRKFEC TECGYKFTRQ AHLRRHMEIH
DRVENYNPRQ RKLRNLIIED EKMVVVALQP PAELEVGSAE VIVESLAQGG LASQLPGQRL
CAEESFTGPG VLEPSLIITA AVPEDCDT


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EIAAB48065 HKR2,Homo sapiens,Human,Krueppel-related zinc finger protein 2,Protein HKR2,Zinc finger and SCAN domain-containing protein 22,Zinc finger protein 50,ZNF50,ZSCAN22
EIAAB46812 Homo sapiens,Human,MIZ1,Miz-1,Myc-interacting zinc finger protein 1,ZBTB17,Zinc finger and BTB domain-containing protein 17,Zinc finger protein 151,Zinc finger protein 60,ZNF151,ZNF60
EIAAB47193 Mouse,Mus musculus,SCAN-KRAB-zinc finger protein,Skz1,Zf47,Zfp306,Zfp307,Zfp47,Zfp-47,Zinc finger protein 306,Zinc finger protein 307,Zinc finger protein 47 homolog,Zinc finger protein with KRAB and S
EIAAB47355 Homo sapiens,Human,Neurotrophin receptor-interacting factor homolog,SP2114,Zf2,Zinc finger protein 274,Zinc finger protein HFB101,Zinc finger protein with KRAB and SCAN domains 19,Zinc finger protein
EIAAB47401 Homo sapiens,Human,KIAA0065,KOX31,Zinc finger and ZAK-associated protein with KRAB domain,Zinc finger protein 11A,Zinc finger protein 33A,Zinc finger protein KOX31,ZNF11,ZNF11A,ZNF33,ZNF33A,ZZaPK
EIAAB47892 Homo sapiens,Human,KOX17,Retinoic acid suppression protein A,RSG-A,Zinc finger and SCAN domain-containing protein 3,Zinc finger protein 191,Zinc finger protein 24,Zinc finger protein KOX17,ZNF191,ZNF2
18-003-42388 Zinc finger protein 24 - Zinc finger protein 191; Zinc finger protein KOX17; Retinoic acid suppression protein A; RSG-A; Zinc finger and SCAN domain-containing protein 3 Polyclonal 0.05 mg Aff Pur
EIAAB47395 C2H2-like zinc finger protein rearranged in thyroid adenomas,Homo sapiens,Human,RITA,Zinc finger protein 331,Zinc finger protein 361,Zinc finger protein 463,ZNF331,ZNF361,ZNF463
EIAAB47457 Early B-cell factor-associated zinc finger protein,Ebfaz,Kiaa0760,Mouse,Mus musculus,Nur12,Oaz,Olf1_EBF-associated zinc finger protein,Smad- and Olf-interacting zinc finger protein,Zfp423,Zinc finger
EIAAB46813 LP-1,Mouse,Mus musculus,Polyomavirus late initiator promoter-binding protein,Zbtb17,Zfp100,Zfp-100,Zinc finger and BTB domain-containing protein 17,Zinc finger protein 100,Zinc finger protein 151,Zinc
EIAAB14743 Fez family zinc finger protein 2,FEZF2,FEZL,FKSG36,Forebrain embryonic zinc finger-like protein 2,Homo sapiens,Human,Zinc finger protein 312,Zinc finger protein Fez-like,ZNF312
EIAAB47275 Homo sapiens,Human,Zinc finger protein 167,Zinc finger protein 448,Zinc finger protein 64,Zinc finger protein with KRAB and SCAN domains 7,ZKSCAN7,ZNF167,ZNF448,ZNF64
EIAAB47047 Homo sapiens,Human,hZF5,ZBTB14,ZF5,ZFP161,Zfp-161,Zfp-5,Zinc finger and BTB domain-containing protein 14,Zinc finger protein 161 homolog,Zinc finger protein 478,Zinc finger protein 5 homolog,ZNF478
EIAAB46811 Homo sapiens,Human,PLZF,Promyelocytic leukemia zinc finger protein,ZBTB16,Zinc finger and BTB domain-containing protein 16,Zinc finger protein 145,Zinc finger protein PLZF,ZNF145


 

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