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Zinc finger protein castor homolog 1 (Castor-related protein) (Putative survival-related protein) (Zinc finger protein 693)

 CASZ1_HUMAN             Reviewed;        1759 AA.
Q86V15; Q078S9; Q2EN02; Q5T9S1; Q6ZNM8; Q8WX49; Q8WX50; Q9BT16;
Q9NXC6;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
13-JUL-2010, sequence version 4.
07-NOV-2018, entry version 137.
RecName: Full=Zinc finger protein castor homolog 1;
AltName: Full=Castor-related protein;
AltName: Full=Putative survival-related protein;
AltName: Full=Zinc finger protein 693;
Name=CASZ1; Synonyms=CST, SRG, ZNF693;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
PubMed=16322216; DOI=10.1158/0008-5472.CAN-05-2176;
Yuan Z.-R., Wang R., Solomon J., Luo X., Sun H., Zhang L., Shi Y.;
"Identification and characterization of survival-related gene, a novel
cell survival gene controlling apoptosis and tumorigenesis.";
Cancer Res. 65:10716-10724(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=16631614; DOI=10.1016/j.bbrc.2006.03.207;
Liu Z., Yang X., Tan F., Cullion K., Thiele C.J.;
"Molecular cloning and characterization of human Castor, a novel human
gene upregulated during cell differentiation.";
Biochem. Biophys. Res. Commun. 344:834-844(2006).
[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] (ISOFORM 2).
TISSUE=Pancreas, and 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 [LARGE SCALE MRNA] OF 115-1759 (ISOFORM 2).
TISSUE=Hepatoma, and Rectum;
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-981, 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).
[7]
FUNCTION, AND MISCELLANEOUS.
PubMed=23639441; DOI=10.1016/j.devcel.2013.03.003;
Charpentier M.S., Christine K.S., Amin N.M., Dorr K.M., Kushner E.J.,
Bautch V.L., Taylor J.M., Conlon F.L.;
"CASZ1 promotes vascular assembly and morphogenesis through the direct
regulation of an EGFL7/RhoA-mediated pathway.";
Dev. Cell 25:132-143(2013).
[8]
FUNCTION, VARIANT PRO-38, AND CHARACTERIZATION OF VARIANT PRO-38.
PubMed=27693370; DOI=10.1016/j.gene.2016.09.044;
Huang R.T., Xue S., Wang J., Gu J.Y., Xu J.H., Li Y.J., Li N.,
Yang X.X., Liu H., Zhang X.D., Qu X.K., Xu Y.J., Qiu X.B., Li R.G.,
Yang Y.Q.;
"CASZ1 loss-of-function mutation associated with congenital heart
disease.";
Gene 595:62-68(2016).
[9]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-288 AND LYS-975, 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).
-!- FUNCTION: Transcriptional activator (PubMed:23639441,
PubMed:27693370). Involved in vascular assembly and morphogenesis
through direct transcriptional regulation of EGFL7
(PubMed:23639441). {ECO:0000269|PubMed:23639441,
ECO:0000269|PubMed:27693370}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16631614}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=hCASZ11;
IsoId=Q86V15-1; Sequence=Displayed;
Name=2; Synonyms=hCASZ5;
IsoId=Q86V15-2; Sequence=VSP_027093, VSP_027094;
-!- TISSUE SPECIFICITY: Expressed in heart, lung, skeletal muscle,
pancreas, testis, small intestine, and stomach, but it is not
detectable in the adult brain. {ECO:0000269|PubMed:16631614}.
-!- MISCELLANEOUS: Endothelial cells depleted in CASZ1 by siRNAs
display dramatic alterations in adhesion, morphology and
sprouting; normal behavior can be rescued by restoration of EGFL7
expression. The defects are in part due to diminished RhoA
expression and impaired focal adhesion localization.
-!- CAUTION: According to PubMed:16322216, another protein (SRG) is
encoded on the 3'-UTR of the CASZ1 gene. The existence of this
protein that may play a role in apoptosis is extremely dubious
despite the fact it was localized in the cytoplasm with the help
of a polyclonal antibody. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABD14411.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
Sequence=BAA91089.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC85474.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CASZ1ID45989ch1p36.html";
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EMBL; DQ372703; ABD14411.1; ALT_SEQ; mRNA.
EMBL; DQ217660; ABB29845.1; -; mRNA.
EMBL; AL139423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004410; AAH04410.2; -; mRNA.
EMBL; BC051883; AAH51883.2; -; mRNA.
EMBL; AK000328; BAA91089.1; ALT_INIT; mRNA.
EMBL; AK130996; BAC85474.1; ALT_SEQ; mRNA.
CCDS; CCDS120.2; -. [Q86V15-2]
CCDS; CCDS41246.1; -. [Q86V15-1]
RefSeq; NP_001073312.1; NM_001079843.2. [Q86V15-1]
RefSeq; NP_060236.3; NM_017766.4. [Q86V15-2]
UniGene; Hs.439894; -.
ProteinModelPortal; Q86V15; -.
BioGrid; 120243; 13.
IntAct; Q86V15; 10.
MINT; Q86V15; -.
STRING; 9606.ENSP00000366221; -.
iPTMnet; Q86V15; -.
PhosphoSitePlus; Q86V15; -.
DMDM; 300669712; -.
EPD; Q86V15; -.
MaxQB; Q86V15; -.
PaxDb; Q86V15; -.
PeptideAtlas; Q86V15; -.
PRIDE; Q86V15; -.
ProteomicsDB; 69945; -.
ProteomicsDB; 69946; -. [Q86V15-2]
DNASU; 54897; -.
Ensembl; ENST00000344008; ENSP00000339445; ENSG00000130940. [Q86V15-2]
Ensembl; ENST00000377022; ENSP00000366221; ENSG00000130940. [Q86V15-1]
GeneID; 54897; -.
KEGG; hsa:54897; -.
UCSC; uc001aro.6; human. [Q86V15-1]
CTD; 54897; -.
DisGeNET; 54897; -.
EuPathDB; HostDB:ENSG00000130940.14; -.
GeneCards; CASZ1; -.
HGNC; HGNC:26002; CASZ1.
HPA; HPA028222; -.
HPA; HPA029927; -.
MIM; 609895; gene.
neXtProt; NX_Q86V15; -.
OpenTargets; ENSG00000130940; -.
PharmGKB; PA142672203; -.
eggNOG; KOG4377; Eukaryota.
eggNOG; ENOG410XRBA; LUCA.
GeneTree; ENSGT00390000008187; -.
HOVERGEN; HBG080122; -.
InParanoid; Q86V15; -.
OMA; FLHKVHF; -.
OrthoDB; EOG091G0364; -.
PhylomeDB; Q86V15; -.
TreeFam; TF324787; -.
ChiTaRS; CASZ1; human.
GeneWiki; CASZ1; -.
GenomeRNAi; 54897; -.
PRO; PR:Q86V15; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000130940; Expressed in 198 organ(s), highest expression level in skin of leg.
CleanEx; HS_CASZ1; -.
ExpressionAtlas; Q86V15; baseline and differential.
Genevisible; Q86V15; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 11.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Developmental protein;
Disease mutation; DNA-binding; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1759 Zinc finger protein castor homolog 1.
/FTId=PRO_0000046912.
ZN_FING 551 575 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 610 634 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 668 692 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1031 1055 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1300 1324 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1457 1481 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1515 1537 C2H2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1571 1595 C2H2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
COMPBIAS 384 417 Pro-rich.
COMPBIAS 1080 1143 Pro-rich.
COMPBIAS 1635 1670 Ala-rich.
COMPBIAS 1672 1729 Glu-rich.
COMPBIAS 1691 1718 Asp-rich.
MOD_RES 720 720 Phosphoserine.
{ECO:0000250|UniProtKB:Q9CWL2}.
MOD_RES 721 721 Phosphoserine.
{ECO:0000250|UniProtKB:Q9CWL2}.
MOD_RES 981 981 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
CROSSLNK 288 288 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 975 975 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1166 1166 N -> K (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_027093.
VAR_SEQ 1167 1759 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_027094.
VARIANT 38 38 L -> P (probable disease-associated
mutation found in a patient with
congenital heart defect; severe decrease
of positive regulation of transcription
from TH promoter).
{ECO:0000269|PubMed:27693370}.
/FTId=VAR_077466.
CONFLICT 192 192 D -> N (in Ref. 2; ABB29845).
{ECO:0000305}.
CONFLICT 273 273 L -> P (in Ref. 2; ABB29845).
{ECO:0000305}.
CONFLICT 408 408 S -> N (in Ref. 4; BAA91089).
{ECO:0000305}.
CONFLICT 486 486 Y -> H (in Ref. 2; ABB29845).
{ECO:0000305}.
CONFLICT 650 650 K -> E (in Ref. 2; ABB29845).
{ECO:0000305}.
CONFLICT 813 813 L -> P (in Ref. 3; AAH51883).
{ECO:0000305}.
CONFLICT 961 961 M -> T (in Ref. 2; ABB29845).
{ECO:0000305}.
CONFLICT 989 989 F -> S (in Ref. 2; ABB29845).
{ECO:0000305}.
CONFLICT 1061 1061 G -> E (in Ref. 4; BAA91089).
{ECO:0000305}.
CONFLICT 1297 1297 N -> S (in Ref. 2; ABB29845).
{ECO:0000305}.
CONFLICT 1501 1501 C -> R (in Ref. 2; ABB29845).
{ECO:0000305}.
CONFLICT 1549 1549 C -> R (in Ref. 2; ABB29845).
{ECO:0000305}.
SEQUENCE 1759 AA; 190069 MW; 4F5146BE72606654 CRC64;
MDLGTAEGTR CTDPPAGKPA MAPKRKGGLK LNAICAKLSR QVVVEKRADA GSHTEGSPSQ
PRDQERSGPE SGAARAPRSE EDKRRAVIEK WVNGEYSEEP APTPVLGRIA REGLELPPEG
VYMVQPQGCS DEEDHAEEPS KDGGALEEKD SDGAASKEDS GPSTRQASGE ASSLRDYAAS
TMTEFLGMFG YDDQNTRDEL ARKISFEKLH AGSTPEAATS SMLPTSEDTL SKRARFSKYE
EYIRKLKAGE QLSWPAPSTK TEERVGKEVV GTLPGLRLPS STAHLETKAT ILPLPSHSSV
QMQNLVARAS KYDFFIQKLK TGENLRPQNG STYKKPSKYD LENVKYLHLF KPGEGSPDMG
GAIAFKTGKV GRPSKYDVRG IQKPGPAKVP PTPSLAPAPL ASVPSAPSAP GPGPEPPASL
SFNTPEYLKS TFSKTDSITT GTVSTVKNGL PTDKPAVTED VNIYQKYIAR FSGSQHCGHI
HCAYQYREHY HCLDPECNYQ RFTSKQDVIR HYNMHKKRDN SLQHGFMRFS PLDDCSVYYH
GCHLNGKSTH YHCMQVGCNK VYTSTSDVMT HENFHKKNTQ LINDGFQRFR ATEDCGTADC
QFYGQKTTHF HCRRPGCTFT FKNKCDIEKH KSYHIKDDAY AKDGFKKFYK YEECKYEGCV
YSKATNHFHC IRAGCGFTFT STSQMTSHKR KHERRHIRSS GALGLPPSLL GAKDTEHEES
SNDDLVDFSA LSSKNSSLSA SPTSQQSSAS LAAATAATEA GPSATKPPNS KISGLLPQGL
PGSIPLALAL SNSGLPTPTP YFPILAGRGS TSLPVGTPSL LGAVSSGSAA SATPDTPTLV
ASGAGDSAPV AAASVPAPPA SIMERISASK GLISPMMARL AAAALKPSAT FDPGSGQQVT
PARFPPAQVK PEPGESTGAP GPHEASQDRS LDLTVKEPSN ESNGHAVPAN SSLLSSLMNK
MSQGNPGLGS LLNIKAEAEG SPAAEPSPFL GKAVKALVQE KLAEPWKVYL RRFGTKDFCD
GQCDFLHKAH FHCVVEECGA LFSTLDGAIK HANFHFRTEG GAAKGNTEAA FPASAAETKP
PMAPSSPPVP PVTTATVSSL EGPAPSPASV PSTPTLLAWK QLASTIPQMP QIPASVPHLP
ASPLATTSLE NAKPQVKPGF LQFQENDPCL ATDCKYANKF HFHCLFGNCK YVCKTSGKAE
SHCLDHINPN NNLVNVRDQF AYYSLQCLCP NQHCEFRMRG HYHCLRTGCY FVTNITTKLP
WHIKKHEKAE RRAANGFKYF TKREECGRLG CKYNQVNSHF HCIREGCQFS FLLKHQMTSH
ARKHMRRMLG KNFDRVPPSQ GPPGLMDAET DECMDYTGCS PGAMSSESST MDRSCSSTPV
GNESTAAGNT ISMPTASGAK KRFWIIEDMS PFGKRRKTAS SRKMLDEGMM LEGFRRFDLY
EDCKDAACQF SLKVTHYHCT RENCGYKFCG RTHMYKHAQH HDRVDNLVLD DFKRFKASLS
CHFADCPFSG TSTHFHCLRC RFRCTDSTKV TAHRKHHGKQ DVISAAGFCQ FSSSADCAVP
DCKYKLKCSH FHCTFPGCRH TVVGMSQMDS HKRKHEKQER GEPAAEGPAP GPPISLDGSL
SLGAEPGSLL FLQSAAAGLG LALGDAGDPG PPDAAAPGPR EGAAAAAAAA GESSQEDEEE
ELELPEEEAE DDEDEDDDED DDDEDDDEDD DDEDLRTDSE ESLPEAAAEA AGAGARTPAL
AALAALGAPG PAPTAASSP


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I4007 Zinc finger protein castor homolog 1 (CASZ1), Mouse, ELISA Kit 96T
I4006 Zinc finger protein castor homolog 1 (CASZ1), Human, ELISA Kit 96T
EIAAB47325 Homo sapiens,Human,ZFP93,Zfp-93,Zinc finger protein 235,Zinc finger protein 270,Zinc finger protein 93 homolog,Zinc finger protein HZF6,ZNF235,ZNF270
EIAAB47314 BMZF2,BMZF-2,Bone marrow zinc finger 2,Homo sapiens,Human,KOX22,Zinc finger protein 224,Zinc finger protein 233,Zinc finger protein 255,Zinc finger protein 27,Zinc finger protein KOX22,ZNF224,ZNF233,Z
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
EIAAB47352 CT-ZFP48,EBV-induced zinc finger protein,Epstein-Barr virus-induced zinc finger protein,Homo sapiens,Human,Zinc finger protein 271,Zinc finger protein dp,Zinc finger protein HZF7,Zinc finger protein Z
EIAAB46856 c-Krox,Krueppel-related zinc finger protein cKrox,Mouse,Mus musculus,T-helper-inducing POZ_Krueppel-like factor,Thpok,Zbtb7b,Zfp67,Zfp-67,Zinc finger and BTB domain-containing protein 7B,Zinc finger p
CSB-EL004562MO Mouse Zinc finger protein castor homolog 1(CASZ1) ELISA kit SpeciesMouse 96T
CSB-EL004562HU Human Zinc finger protein castor homolog 1(CASZ1) ELISA kit SpeciesHuman 96T
EIAAB46847 HKR3,Homo sapiens,Human,Krueppel-related zinc finger protein 3,Protein HKR3,ZBTB48,Zinc finger and BTB domain-containing protein 48,Zinc finger protein 855,ZNF855
EIAAB46855 hcKrox,Homo sapiens,Human,Krueppel-related zinc finger protein cKrox,T-helper-inducing POZ_Krueppel-like factor,ZBTB15,ZBTB7B,ZFP67,Zfp-67,Zinc finger and BTB domain-containing protein 15,Zinc finger
EIAAB46826 FANCC-interacting protein,Fanconi anemia zinc finger protein,FAZF,Homo sapiens,Human,Testis zinc finger protein,TZFP,ZBTB32,Zinc finger and BTB domain-containing protein 32,Zinc finger protein 538,ZNF
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
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


 

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