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Zinc finger protein 385A (Hematopoietic zinc finger protein) (Retinal zinc finger protein)

 Z385A_HUMAN             Reviewed;         386 AA.
Q96PM9; B2RDN5; B4DKH2; F1T0F1; J3KNS3; Q5VH53; Q9H7R6; Q9UFU3;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
24-JUL-2013, sequence version 2.
12-SEP-2018, entry version 140.
RecName: Full=Zinc finger protein 385A;
AltName: Full=Hematopoietic zinc finger protein;
AltName: Full=Retinal zinc finger protein;
Name=ZNF385A; Synonyms=HZF, RZF, ZNF385;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
TISSUE=Retina;
PubMed=15527981; DOI=10.1016/j.gene.2004.08.015;
Sharma S., Dimasi D., Higginson K., Della N.G.;
"RZF, a zinc-finger protein in the photoreceptors of human retina.";
Gene 342:219-229(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Qu X., Zhai Y., Zhang C., Wu S., Zhang Y., Xing G., Wei H., Yu Y.,
Wang M., He F.;
"Homo sapiens hematopoietic zinc finger protein mRNA.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Thyroid, and Umbilical cord blood;
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 MRNA] (ISOFORM 3).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=21697133; DOI=10.1167/iovs.11-7479;
Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M.,
Toyama S., Usami R., Ohtoko K., Kato S.;
"Full-length transcriptome analysis of human retina-derived cell lines
ARPE-19 and Y79 using the vector-capping method.";
Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[7]
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Prostate;
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-386 (ISOFORMS 1/4).
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[10]
FUNCTION IN TP53-DEPENDENT CELL CYCLE ARREST, INTERACTION WITH TP53,
INDUCTION, AND UBIQUITINATION.
PubMed=17719541; DOI=10.1016/j.cell.2007.06.013;
Das S., Raj L., Zhao B., Kimura Y., Bernstein A., Aaronson S.A.,
Lee S.W.;
"Hzf Determines cell survival upon genotoxic stress by modulating p53
transactivation.";
Cell 130:624-637(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND THR-248, 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: RNA-binding protein that affects the localization and
the translation of a subset of mRNA. May play a role in
adipogenesis through binding to the 3'-UTR of CEBPA mRNA and
regulation of its translation. Targets ITPR1 mRNA to dendrites in
Purkinje cells, and may regulate its activity-dependent
translation. With ELAVL1, binds the 3'-UTR of p53/TP53 mRNAs to
control their nuclear export induced by CDKN2A. Hence, may
regulate p53/TP53 expression and mediate in part the CDKN2A anti-
proliferative activity. May also bind CCNB1 mRNA. Alternatively,
may also regulate p53/TP53 activity through direct protein-protein
interaction. Interacts with p53/TP53 and promotes cell-cycle
arrest over apoptosis enhancing preferentially the DNA binding and
transactivation of p53/TP53 on cell-cycle arrest target genes over
proapoptotic target genes. May also regulate the ubiquitination
and stability of CDKN1A promoting DNA damage-induced cell cycle
arrest. Also plays a role in megakaryocytes differentiation.
{ECO:0000269|PubMed:17719541}.
-!- SUBUNIT: Interacts with ELAVL1; the interaction is indirect, mRNA-
dependent and may regulate p53/TP53 expression (By similarity).
Interacts with p53/TP53; the interaction is direct and enhances
p53/TP53 transactivation functions on cell-cycle arrest target
genes, resulting in growth arrest. {ECO:0000250,
ECO:0000269|PubMed:17719541}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15527981}.
Nucleus, nucleolus {ECO:0000269|PubMed:15527981}. Cell projection,
dendrite {ECO:0000250}. Note=Detected in dendrites of Purkinje
cells and hippocampal neurons. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=4;
IsoId=Q96PM9-4; Sequence=Displayed;
Name=1;
IsoId=Q96PM9-1; Sequence=VSP_047448;
Name=2;
IsoId=Q96PM9-2; Sequence=VSP_047448, VSP_047449;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q96PM9-3; Sequence=VSP_047449;
-!- TISSUE SPECIFICITY: Expressed predominantly in the retina.
{ECO:0000269|PubMed:15527981}.
-!- INDUCTION: Up-regulated by p53/TP53 in response to DNA damage and
oxidative stress. {ECO:0000269|PubMed:17719541}.
-!- PTM: Ubiquitinated upon prolonged exposure to genotoxic stress,
which leads to proteasomal degradation of ZNF385A and releases
p53/TP53 from cell-cycle arrest target gene promoters.
{ECO:0000269|PubMed:17719541}.
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EMBL; AY461717; AAS19275.1; -; mRNA.
EMBL; AF304052; AAL08625.1; -; mRNA.
EMBL; AK024404; BAB14910.1; -; mRNA.
EMBL; AK296564; BAG59184.1; -; mRNA.
EMBL; AK315613; BAG37982.1; -; mRNA.
EMBL; CR457327; CAG33608.1; -; mRNA.
EMBL; AB593085; BAJ84025.1; -; mRNA.
EMBL; AC078778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC079313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW96777.1; -; Genomic_DNA.
EMBL; BC029752; AAH29752.1; -; mRNA.
EMBL; AL117462; CAB55938.1; -; mRNA.
CCDS; CCDS44910.1; -. [Q96PM9-3]
CCDS; CCDS44911.1; -. [Q96PM9-4]
CCDS; CCDS76563.1; -. [Q96PM9-2]
CCDS; CCDS8879.1; -. [Q96PM9-1]
PIR; T17248; T17248.
RefSeq; NP_001124439.1; NM_001130967.2. [Q96PM9-4]
RefSeq; NP_001124440.1; NM_001130968.2. [Q96PM9-3]
RefSeq; NP_001276930.1; NM_001290001.1. [Q96PM9-2]
RefSeq; NP_001276931.1; NM_001290002.1. [Q96PM9-1]
RefSeq; NP_001276933.1; NM_001290004.1. [Q96PM9-1]
RefSeq; NP_056296.1; NM_015481.2. [Q96PM9-1]
RefSeq; XP_005268840.1; XM_005268783.4. [Q96PM9-1]
RefSeq; XP_006719405.1; XM_006719342.2. [Q96PM9-1]
RefSeq; XP_016874663.1; XM_017019174.1. [Q96PM9-1]
UniGene; Hs.505653; -.
ProteinModelPortal; Q96PM9; -.
BioGrid; 117442; 11.
IntAct; Q96PM9; 2.
STRING; 9606.ENSP00000338927; -.
iPTMnet; Q96PM9; -.
PhosphoSitePlus; Q96PM9; -.
BioMuta; ZNF385A; -.
DMDM; 527504071; -.
EPD; Q96PM9; -.
PaxDb; Q96PM9; -.
PeptideAtlas; Q96PM9; -.
PRIDE; Q96PM9; -.
ProteomicsDB; 77713; -.
ProteomicsDB; 77714; -. [Q96PM9-2]
Ensembl; ENST00000338010; ENSP00000338927; ENSG00000161642. [Q96PM9-4]
Ensembl; ENST00000352268; ENSP00000293385; ENSG00000161642. [Q96PM9-3]
Ensembl; ENST00000394313; ENSP00000377849; ENSG00000161642. [Q96PM9-1]
Ensembl; ENST00000546970; ENSP00000446913; ENSG00000161642. [Q96PM9-1]
Ensembl; ENST00000551109; ENSP00000449161; ENSG00000161642. [Q96PM9-1]
Ensembl; ENST00000551771; ENSP00000447162; ENSG00000161642. [Q96PM9-2]
GeneID; 25946; -.
KEGG; hsa:25946; -.
UCSC; uc001sfw.2; human. [Q96PM9-4]
CTD; 25946; -.
DisGeNET; 25946; -.
EuPathDB; HostDB:ENSG00000161642.17; -.
GeneCards; ZNF385A; -.
HGNC; HGNC:17521; ZNF385A.
HPA; HPA039799; -.
MIM; 609124; gene.
neXtProt; NX_Q96PM9; -.
OpenTargets; ENSG00000161642; -.
PharmGKB; PA162410095; -.
eggNOG; ENOG410IHAD; Eukaryota.
eggNOG; ENOG410Y1ZH; LUCA.
GeneTree; ENSGT00390000002371; -.
HOGENOM; HOG000231865; -.
HOVERGEN; HBG054524; -.
InParanoid; Q96PM9; -.
OMA; RRHRDGM; -.
OrthoDB; EOG091G08IG; -.
PhylomeDB; Q96PM9; -.
TreeFam; TF326622; -.
Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
Reactome; R-HSA-6804759; Regulation of TP53 Activity through Association with Co-factors.
Reactome; R-HSA-69895; Transcriptional activation of cell cycle inhibitor p21.
ChiTaRS; ZNF385A; human.
GenomeRNAi; 25946; -.
PRO; PR:Q96PM9; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000161642; Expressed in 193 organ(s), highest expression level in skin of abdomen.
CleanEx; HS_ZNF385A; -.
ExpressionAtlas; Q96PM9; baseline and differential.
Genevisible; Q96PM9; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; NAS:NTNU_SB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0007599; P:hemostasis; IEA:Ensembl.
GO; GO:0007611; P:learning or memory; IEA:Ensembl.
GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
GO; GO:0035855; P:megakaryocyte development; ISS:UniProtKB.
GO; GO:0010609; P:mRNA localization resulting in posttranscriptional regulation of gene expression; ISS:UniProtKB.
GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:UniProtKB.
GO; GO:0070889; P:platelet alpha granule organization; IEA:Ensembl.
GO; GO:0030220; P:platelet formation; IEA:Ensembl.
GO; GO:1902164; P:positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IMP:UniProtKB.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:2000765; P:regulation of cytoplasmic translation; ISS:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 3.
SMART; SM00451; ZnF_U1; 3.
SUPFAM; SSF57667; SSF57667; 3.
1: Evidence at protein level;
Alternative splicing; Cell projection; Complete proteome; Cytoplasm;
DNA damage; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; Transcription;
Transcription regulation; Translation regulation; Ubl conjugation;
Zinc; Zinc-finger.
CHAIN 1 386 Zinc finger protein 385A.
/FTId=PRO_0000047554.
ZN_FING 74 98 Matrin-type 1.
ZN_FING 201 225 Matrin-type 2.
ZN_FING 261 285 Matrin-type 3.
REGION 145 351 Necessary for binding to ITPR1, CEBPA and
p53/TP53 mRNAs. {ECO:0000250}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 248 248 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 21 MILGSLSRAGPLPLLRQPPIM -> M (in isoform 1
and isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15527981,
ECO:0000303|PubMed:21697133,
ECO:0000303|Ref.2}.
/FTId=VSP_047448.
VAR_SEQ 141 221 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.4}.
/FTId=VSP_047449.
SEQUENCE 386 AA; 40454 MW; 21290C79D95CD620 CRC64;
MILGSLSRAG PLPLLRQPPI MQPPLDLKQI LPFPLEPAPT LGLFSNYSTM DPVQKAVLSH
TFGGPLLKTK RPVISCNICQ IRFNSQSQAE AHYKGNRHAR RVKGIEAAKT RGREPGVREP
GDPAPPGSTP TNGDGVAPRP VSMENGLGPA PGSPEKQPGS PSPPSIPETG QGVTKGEGGT
PAPASLPGGS KEEEEKAKRL LYCALCKVAV NSLSQLEAHN KGTKHKTILE ARSGLGPIKA
YPRLGPPTPG EPEAPAQDRT FHCEICNVKV NSEVQLKQHI SSRRHRDGVA GKPNPLLSRH
KKSRGAGELA GTLTFSKELP KSLAGGLLPS PLAVAAVMAA AAGSPLSLRP APAAPLLQGP
PITHPLLHPA PGPIRTAHGP ILFSPY


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EIAAB47194 Homo sapiens,Human,Zf47,ZFP47,Zfp-47,Zinc finger and SCAN domain-containing protein 13,Zinc finger protein 306,Zinc finger protein 309,Zinc finger protein 47 homolog,Zinc finger protein with KRAB and
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
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
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
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
18-003-42237 Zinc finger protein 385 - Hematopoietic zinc finger protein; Retinal zinc finger protein Polyclonal 0.05 mg Aff Pur
18-003-42091 Zinc finger protein 385 - Hematopoietic zinc finger protein; Retinal zinc finger protein Polyclonal 0.05 mg Aff Pur
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
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
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
EIAAB47878 HDSG1,Heart development-specific gene 1 protein,Homo sapiens,Human,KOX11,Zinc finger protein 18,Zinc finger protein 535,Zinc finger protein KOX11,Zinc finger protein with KRAB and SCAN domains 6,ZKSCA
EIAAB47384 Homo sapiens,Human,Zinc finger protein 322,Zinc finger protein 322A,Zinc finger protein 388,Zinc finger protein 489,ZNF322,ZNF322A,ZNF388,ZNF489
EIAAB14741 Fez,Fez family zinc finger protein 2,Fezf2,Fezl,Forebrain embryonic zinc finger-like protein 2,Mouse,Mus musculus,Zfp312,Zinc finger protein 312,Zinc finger protein Fez-like
EIAAB14742 Bos taurus,Bovine,Fez family zinc finger protein 2,FEZF2,FEZL,Forebrain embryonic zinc finger-like protein 2,Zinc finger protein 312,Zinc finger protein Fez-like,ZNF312
18-003-42276 Zinc finger and BTB domain-containing protein 7B - Zinc finger protein 67 homolog; Zfp-67; Zinc finger protein Th-POK; T-helper-inducing POZ_Krueppel-like factor; Krueppel-related zinc finger protein 0.1 mg Protein A
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
EIAAB47907 GIOT2,GIOT-2,Gonadotropin-inducible ovary transcription repressor 2,Homo sapiens,Human,KOX7,Zinc finger protein 44,Zinc finger protein 55,Zinc finger protein 58,Zinc finger protein KOX7,ZNF44,ZNF55,ZN
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


 

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