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Endoribonuclease ZC3H12A (EC 3.1.-.-) (Monocyte chemotactic protein-induced protein 1) (MCP-induced protein 1) (MCPIP-1) (Regnase-1) (Reg1) (Zinc finger CCCH domain-containing protein 12A)

 ZC12A_HUMAN             Reviewed;         599 AA.
Q5D1E8; D3DPT0; Q6I9Z1; Q9H5P1;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 1.
25-OCT-2017, entry version 84.
RecName: Full=Endoribonuclease ZC3H12A {ECO:0000305};
EC=3.1.-.- {ECO:0000269|PubMed:22055188};
AltName: Full=Monocyte chemotactic protein-induced protein 1 {ECO:0000303|PubMed:16574901};
Short=MCP-induced protein 1 {ECO:0000303|PubMed:16574901};
Short=MCPIP-1 {ECO:0000303|PubMed:16574901};
AltName: Full=Regnase-1 {ECO:0000303|PubMed:22037600};
Short=Reg1 {ECO:0000250|UniProtKB:Q5D1E7};
AltName: Full=Zinc finger CCCH domain-containing protein 12A {ECO:0000312|HGNC:HGNC:26259};
Name=ZC3H12A {ECO:0000312|HGNC:HGNC:26259};
Synonyms=MCPIP {ECO:0000303|PubMed:16574901}, MCPIP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAX14017.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION AS A TRANSCRIPTION FACTOR,
SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY, MUTAGENESIS OF
LYS-311; CYS-312; LYS-317 AND CYS-318, AND POSSIBLE INVOLVEMENT IN
ISCHEMIC HEART DISEASE.
PubMed=16574901; DOI=10.1161/01.RES.0000220106.64661.71;
Zhou L., Azfer A., Niu J., Graham S., Choudhury M., Adamski F.M.,
Younce C., Binkley P.F., Kolattukudy P.E.;
"Monocyte chemoattractant protein-1 induces a novel transcription
factor that causes cardiac myocyte apoptosis and ventricular
dysfunction.";
Circ. Res. 98:1177-1185(2006).
[2] {ECO:0000305, ECO:0000312|EMBL:BAB15581.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-547.
TISSUE=Artery {ECO:0000312|EMBL:BAB15581.1};
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).
[3] {ECO:0000305, ECO:0000312|EMBL:CAG33645.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-547.
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.
[4] {ECO:0000312|EMBL:CAH73689.1}
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).
[5] {ECO:0000305, ECO:0000312|EMBL:CAG33645.1}
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305, ECO:0000312|EMBL:AAH05001.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-547.
TISSUE=Kidney {ECO:0000312|EMBL:AAH05001.1};
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]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=18178554; DOI=10.1074/jbc.M707861200;
Liang J., Wang J., Azfer A., Song W., Tromp G., Kolattukudy P.E.,
Fu M.;
"A novel CCCH-zinc finger protein family regulates proinflammatory
activation of macrophages.";
J. Biol. Chem. 283:6337-6346(2008).
[8] {ECO:0000305}
FUNCTION AS A TRANSCRIPTION FACTOR, INDUCTION, CHROMATIN BINDING, AND
DNA-BINDING.
PubMed=18364357; DOI=10.1074/jbc.M802139200;
Niu J., Azfer A., Zhelyabovska O., Fatma S., Kolattukudy P.E.;
"Monocyte chemotactic protein (MCP)-1 promotes angiogenesis via a
novel transcription factor, MCP-1-induced protein (MCPIP).";
J. Biol. Chem. 283:14542-14551(2008).
[9]
FUNCTION, AND INDUCTION.
PubMed=19185603; DOI=10.1016/j.brainresbull.2009.01.004;
Vrotsos E.G., Kolattukudy P.E., Sugaya K.;
"MCP-1 involvement in glial differentiation of neuroprogenitor cells
through APP signaling.";
Brain Res. Bull. 79:97-103(2009).
[10]
INDUCTION.
PubMed=19747262; DOI=10.1111/j.1742-4658.2009.07273.x;
Skalniak L., Mizgalska D., Zarebski A., Wyrzykowska P., Koj A.,
Jura J.;
"Regulatory feedback loop between NF-kappaB and MCP-1-induced protein
1 RNase.";
FEBS J. 276:5892-5905(2009).
[11]
FUNCTION AS AN ENDORIBONUCLEASE, SUBCELLULAR LOCATION, INDUCTION,
TISSUE SPECIFICITY, AND MUTAGENESIS OF ASP-141 AND ASP-226.
PubMed=19909337; DOI=10.1111/j.1742-4658.2009.07452.x;
Mizgalska D., Wegrzyn P., Murzyn K., Kasza A., Koj A., Jura J.,
Jarzab B., Jura J.;
"Interleukin-1-inducible MCPIP protein has structural and functional
properties of RNase and participates in degradation of IL-1beta
mRNA.";
FEBS J. 276:7386-7399(2009).
[12]
INDUCTION.
PubMed=20137095; DOI=10.1186/1471-2199-11-14;
Kasza A., Wyrzykowska P., Horwacik I., Tymoszuk P., Mizgalska D.,
Palmer K., Rokita H., Sharrocks A.D., Jura J.;
"Transcription factors Elk-1 and SRF are engaged in IL1-dependent
regulation of ZC3H12A expression.";
BMC Mol. Biol. 11:14-14(2010).
[13]
FUNCTION AS AN ENDORIBONUCLEASE, CATALYTIC ACTIVITY, SUBUNIT,
RNA-BINDING, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF ASP-141
AND CYS-306.
PubMed=22055188; DOI=10.1016/j.molcel.2011.09.012;
Suzuki H.I., Arase M., Matsuyama H., Choi Y.L., Ueno T., Mano H.,
Sugimoto K., Miyazono K.;
"MCPIP1 ribonuclease antagonizes dicer and terminates microRNA
biogenesis through precursor microRNA degradation.";
Mol. Cell 44:424-436(2011).
[14]
INTERACTION WITH IKBKB, AND INDUCTION.
PubMed=22037600; DOI=10.1038/ni.2137;
Iwasaki H., Takeuchi O., Teraguchi S., Matsushita K., Uehata T.,
Kuniyoshi K., Satoh T., Saitoh T., Matsushita M., Standley D.M.,
Akira S.;
"The IkappaB kinase complex regulates the stability of cytokine-
encoding mRNA induced by TLR-IL-1R by controlling degradation of
regnase-1.";
Nat. Immunol. 12:1167-1175(2011).
[15]
INDUCTION.
PubMed=23185455; DOI=10.1371/journal.pone.0049841;
Li M., Cao W., Liu H., Zhang W., Liu X., Cai Z., Guo J., Wang X.,
Hui Z., Zhang H., Wang J., Wang L.;
"MCPIP1 down-regulates IL-2 expression through an ARE-independent
pathway.";
PLoS ONE 7:E49841-E49841(2012).
[16]
FUNCTION AS AN ENDORIBONUCLEASE.
PubMed=24048733; DOI=10.1152/ajpcell.00203.2013;
Roy A., Zhang M., Saad Y., Kolattukudy P.E.;
"Antidicer RNase activity of monocyte chemotactic protein-induced
protein-1 is critical for inducing angiogenesis.";
Am. J. Physiol. 305:C1021-C1032(2013).
[17]
REVIEW.
PubMed=23500036; DOI=10.1016/j.bbagrm.2013.03.001;
Uehata T., Akira S.;
"mRNA degradation by the endoribonuclease Regnase-1/ZC3H12a/MCPIP-1.";
Biochim. Biophys. Acta 1829:708-713(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-344, 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).
[19]
FUNCTION AS AN ENDORIBONUCLEASE (MICROBIAL INFECTION), SUBUNIT
(MICROBIAL INFECTION), RNA-BINDING, DOMAIN (MICROBIAL INFECTION),
INDUCTION (MICROBIAL INFECTION), AND MUTAGENESIS OF ASP-141; CYS-157;
ASP-225; ASP-226 AND CYS-306.
PubMed=23355615; DOI=10.1093/nar/gkt019;
Lin R.J., Chien H.L., Lin S.Y., Chang B.L., Yu H.P., Tang W.C.,
Lin Y.L.;
"MCPIP1 ribonuclease exhibits broad-spectrum antiviral effects through
viral RNA binding and degradation.";
Nucleic Acids Res. 41:3314-3326(2013).
[20]
FUNCTION AS AN ENDORIBONUCLEASE (MICROBIAL INFECTION), DEGRADATION
(MICROBIAL INFECTION), AND MUTAGENESIS OF ASP-141; ASP-225; ASP-226
AND CYS-306.
PubMed=24191027; DOI=10.1073/pnas.1316208110;
Liu S., Qiu C., Miao R., Zhou J., Lee A., Liu B., Lester S.N., Fu W.,
Zhu L., Zhang L., Xu J., Fan D., Li K., Fu M., Wang T.;
"MCPIP1 restricts HIV infection and is rapidly degraded in activated
CD4+ T cells.";
Proc. Natl. Acad. Sci. U.S.A. 110:19083-19088(2013).
[21]
FUNCTION AS AN ENDORIBONUCLEASE IN INFLAMMATION, INDUCTION, AND
MUTAGENESIS OF ASP-141; ASP-225; ASP-226 AND CYS-306.
PubMed=26320658; DOI=10.1016/j.immuni.2015.07.021;
Garg A.V., Amatya N., Chen K., Cruz J.A., Grover P., Whibley N.,
Conti H.R., Hernandez Mir G., Sirakova T., Childs E.C.,
Smithgall T.E., Biswas P.S., Kolls J.K., McGeachy M.J.,
Kolattukudy P.E., Gaffen S.L.;
"MCPIP1 endoribonuclease activity negatively regulates interleukin-17-
mediated signaling and inflammation.";
Immunity 43:475-487(2015).
[22]
FUNCTION, IDENTIFICATION IN A DEUBIQUITINATION COMPLEX WITH TANK AND
USP10, AND INTERACTION WITH IKBKG; TANK; TRAF6 AND USP10.
PubMed=25861989; DOI=10.1074/jbc.M115.643767;
Wang W., Huang X., Xin H.B., Fu M., Xue A., Wu Z.H.;
"TRAF family member-associated NF-kappaB activator (TANK) inhibits
genotoxic nuclear factor kappaB activation by facilitating
deubiquitinase USP10-dependent deubiquitination of TRAF6 ligase.";
J. Biol. Chem. 290:13372-13385(2015).
[23]
FUNCTION AS AN ENDORIBONUCLEASE, INTERACTION WITH TNRC6A AND ZC3H12D,
SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF ASP-141.
PubMed=26134560; DOI=10.1074/jbc.M114.635870;
Huang S., Liu S., Fu J.J., Tony Wang T., Yao X., Kumar A., Liu G.,
Fu M.;
"Monocyte chemotactic protein-induced protein 1 and 4 form a complex
but act independently in regulation of interleukin-6 mRNA
degradation.";
J. Biol. Chem. 290:20782-20792(2015).
[24]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 112-334, FUNCTION AS AN
ENDORIBONUCLEASE, CATALYTIC REGION, COFACTOR, DOMAIN, MUTAGENESIS OF
ASP-141; ASN-144 AND ARG-214, AND MAGNESIUM-BINDING SITE.
PubMed=22561375; DOI=10.1093/nar/gks359;
Xu J., Peng W., Sun Y., Wang X., Xu Y., Li X., Gao G., Rao Z.;
"Structural study of MCPIP1 N-terminal conserved domain reveals a PIN-
like RNase.";
Nucleic Acids Res. 40:6957-6965(2012).
-!- FUNCTION: Endoribonuclease involved in various biological
functions such as cellular inflammatory response and immune
homeostasis, glial differentiation of neuroprogenitor cells, cell
death of cardiomyocytes, adipogenesis and angiogenesis. Functions
as an endoribonuclease involved in mRNA decay (PubMed:19909337).
Modulates the inflammatory response by promoting the degradation
of a set of translationally active cytokine-induced inflammation-
related mRNAs, such as IL6 and IL12B, during the early phase of
inflammation (PubMed:26320658). Prevents aberrant T-cell-mediated
immune reaction by degradation of multiple mRNAs controlling T-
cell activation, such as those encoding cytokines (IL6 and IL2),
cell surface receptors (ICOS, TNFRSF4 and TNFR2) and transcription
factor (REL) (By similarity). Self regulates by destabilizing its
own mRNA (By similarity). Cleaves mRNA harboring a stem-loop (SL),
often located in their 3'-UTRs, during the early phase of
inflammation in a helicase UPF1-dependent manner (PubMed:19909337,
PubMed:26320658, PubMed:26134560, PubMed:22561375). Plays a role
in the inhibition of microRNAs (miRNAs) biogenesis
(PubMed:22055188). Cleaves the terminal loop of a set of precursor
miRNAs (pre-miRNAs) important for the regulation of the
inflammatory response leading to their degradation, and thus
preventing the biosynthesis of mature miRNAs (PubMed:22055188).
Plays also a role in promoting angiogenesis in response to
inflammatory cytokines by inhibiting the production of
antiangiogenic microRNAs via its anti-dicer RNase activity
(PubMed:24048733). Affects the overall ubiquitination of cellular
proteins (By similarity). Positively regulates deubiquitinase
activity promoting the cleavage at 'Lys-48'- and 'Lys-63'-linked
polyubiquitin chains on TNF receptor-associated factors (TRAFs),
preventing JNK and NF-kappa-B signaling pathway activation, and
hence negatively regulating macrophage-mediated inflammatory
response and immune homeostasis (By similarity). Induces also
deubiquitination of the transcription factor HIF1A, probably
leading to its stabilization and nuclear import, thereby
positively regulating the expression of proangiogenic HIF1A-
targeted genes (PubMed:24048733). Involved in a TANK-dependent
negative feedback response to attenuate NF-kappaB activation
through the deubiquitination of IKBKG or TRAF6 in response to
interleukin-1-beta (IL1B) stimulation or upon DNA damage
(PubMed:25861989). Prevents stress granule (SGs) formation and
promotes macrophage apoptosis under stress conditions, including
arsenite-induced oxidative stress, heat shock and energy
deprivation (By similarity). Plays a role in the regulation of
macrophage polarization; promotes IL4-induced polarization of
macrophages M1 into anti-inflammatory M2 state (By similarity).
May also act as a transcription factor that regulates the
expression of multiple genes involved in inflammatory response,
angiogenesis, adipogenesis and apoptosis (PubMed:16574901,
PubMed:18364357). Functions as a positive regulator of glial
differentiation of neuroprogenitor cells through an amyloid
precursor protein (APP)-dependent signaling pathway
(PubMed:19185603). Attenuates septic myocardial contractile
dysfunction in response to lipopolysaccharide (LPS) by reducing I-
kappa-B-kinase (IKK)-mediated NF-kappa-B activation, and hence
myocardial proinflammatory cytokine production (By similarity).
{ECO:0000250|UniProtKB:Q5D1E7, ECO:0000269|PubMed:16574901,
ECO:0000269|PubMed:18364357, ECO:0000269|PubMed:19185603,
ECO:0000269|PubMed:19909337, ECO:0000269|PubMed:22055188,
ECO:0000269|PubMed:22561375, ECO:0000269|PubMed:24048733,
ECO:0000269|PubMed:25861989, ECO:0000269|PubMed:26134560,
ECO:0000269|PubMed:26320658}.
-!- FUNCTION: (Microbial infection) Exhibits broad antiviral activity
by cleaving viral RNAs (PubMed:23355615). Binds to Japanese
encephalitis virus (JEV) and dengue virus (DEN) RNAs
(PubMed:23355615). Exhibits antiviral activity against HIV-1 in
lymphocytes by decreasing the abundance of HIV-1 viral RNA species
(PubMed:24191027). {ECO:0000269|PubMed:23355615,
ECO:0000269|PubMed:24191027}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:22561375};
Note=Mg(2+) is required for RNase activity (PubMed:22561375).
{ECO:0000269|PubMed:22561375};
-!- SUBUNIT: Oligomer (PubMed:22055188, PubMed:23355615). Found in a
deubiquitination complex with TANK, USP10 and ZC3H12A; this
complex inhibits genotoxic stress- or interleukin-1-beta-mediated
NF-kappaB activation by promoting IKBKG or TRAF6 deubiquitination
(PubMed:25861989). Interacts with IKBKG; this interaction
increases in response to DNA damage (PubMed:25861989). Interacts
with TANK; this interaction increases in response to DNA damage
and serves as a bridge to anchor both TANK and USP10 into a
deubiquitinating complex (PubMed:25861989). Interacts with TRAF6;
this interaction increases in response to DNA damage and is
stimulated by TANK (PubMed:25861989). Interacts with USP10; this
interaction increases in response to DNA damage and serves as a
bridge to anchor both TANK and USP10 into a deubiquitinating
complex (PubMed:25861989). Interacts with ZC3H12D
(PubMed:26134560). Interacts with TNRC6A (PubMed:26134560).
Interacts with IKBKB/IKKB (PubMed:22037600). Interacts with
IKBKB/IKKB. Interacts with BTRC; the interaction occurs when
ZC3H12A is phosphorylated in a IKBKB/IKKB-dependent manner (By
similarity). Interacts with IRAK1; this interaction increases the
interaction between ZC3H12A and IKBKB/IKKB (By similarity).
Interacts with UPF1; this interaction occurs in a mRNA
translationally active- and termination-dependent manner and is
essential for ZC3H12A-mediated degradation of target mRNAs (By
similarity). Associates with ribosomes (By similarity). Interacts
with ubiquitin (By similarity). {ECO:0000250|UniProtKB:Q5D1E7,
ECO:0000269|PubMed:22037600, ECO:0000269|PubMed:22055188,
ECO:0000269|PubMed:23355615, ECO:0000269|PubMed:25861989,
ECO:0000269|PubMed:26134560}.
-!- SUBUNIT: (Microbial infection) Oligomerization is necessary for
antiviral activity (PubMed:23355615).
{ECO:0000269|PubMed:23355615}.
-!- INTERACTION:
Q9NZD4:AHSP; NbExp=4; IntAct=EBI-747793, EBI-720250;
Q9Y297:BTRC; NbExp=3; IntAct=EBI-747793, EBI-307461;
Q9Y6K9:IKBKG; NbExp=2; IntAct=EBI-747793, EBI-81279;
O43187:IRAK2; NbExp=2; IntAct=EBI-747793, EBI-447733;
Q7Z4N8:P4HA3; NbExp=5; IntAct=EBI-747793, EBI-10181968;
P84022:SMAD3; NbExp=2; IntAct=EBI-747793, EBI-347161;
Q14694:USP10; NbExp=5; IntAct=EBI-747793, EBI-2510389;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16574901}.
Cytoplasm {ECO:0000269|PubMed:18178554,
ECO:0000269|PubMed:19909337, ECO:0000269|PubMed:22055188}.
Cytoplasm, P-body {ECO:0000269|PubMed:22055188,
ECO:0000269|PubMed:26134560}. Rough endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q5D1E7}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q5D1E7}; Cytoplasmic side
{ECO:0000250|UniProtKB:Q5D1E7}. Cytoplasmic granule
{ECO:0000250|UniProtKB:Q5D1E7}. Note=Predominantly localized in
the cytoplasm. Colocalizes with GW182 on many granule-like
structures, probably corresponding to cytoplasmic GW bodies
(GWBs), also called processing bodies (P bodies). Colocalizes with
calnexin on the surface of the rough endoplasmic reticulum (RER)
membrane and with translationally active polysomes (By
similarity). Colocalizes with ZC3H12D in cytoplasmic mRNA
processing P-body, also known as GW bodies (GWBs)
(PubMed:22055188, PubMed:26134560). {ECO:0000269|PubMed:22055188,
ECO:0000269|PubMed:26134560}.
-!- TISSUE SPECIFICITY: Expressed in heart, placenta, spleen, kidney,
liver and lung (PubMed:19909337). Expressed in leukocytes
(PubMed:19909337). Expressed in monocyte (PubMed:16574901).
{ECO:0000269|PubMed:16574901, ECO:0000269|PubMed:19909337}.
-!- INDUCTION: Up-regulated by the transcription factor ELK1 in a
interleukin IL1B-dependent manner through activation of the NF-
kappa-B and ERK signaling pathways (PubMed:19747262,
PubMed:20137095, PubMed:22037600). Up-regulated by chemokine CCL2
in endothelial cells and in peripheral blood monocytes
(PubMed:16574901, PubMed:18364357). Up-regulated in activated T
lymphocytes (PubMed:23185455). Up-regulated by phorbol 12-
myristate 13-acetate (PMA) in primary T lymphocytes
(PubMed:19909337, PubMed:23185455). Up-regulated by interleukin
IL17 in keratinocytes (PubMed:26320658). Up-regulated by
lipopolysaccharide (LPS) (PubMed:19909337). Up-regulated by tumor
necrosis factor TNF-alpha and interleukin IL1 in acute monocytic
leukemia cell line THP-1 cells (PubMed:18178554, PubMed:19909337).
Up-regulated by amyloid precursor protein (APP) (PubMed:19185603).
{ECO:0000269|PubMed:16574901, ECO:0000269|PubMed:18178554,
ECO:0000269|PubMed:18364357, ECO:0000269|PubMed:19185603,
ECO:0000269|PubMed:19747262, ECO:0000269|PubMed:19909337,
ECO:0000269|PubMed:20137095, ECO:0000269|PubMed:22037600,
ECO:0000269|PubMed:23185455, ECO:0000269|PubMed:26320658}.
-!- INDUCTION: (Microbial infection) Up-regulated in response to
Japanese encephalitis virus (JEV) and dengue virus (DEN)
infections (PubMed:23355615). {ECO:0000269|PubMed:23355615}.
-!- DOMAIN: The C3H1-type zinc finger domain and C-terminal region are
necessary for pre-miRNA binding (PubMed:22055188). The C-terminal
region and proline-rich domain are necessary for oligomerization
(PubMed:22055188). {ECO:0000269|PubMed:22055188}.
-!- DOMAIN: (Microbial infection) The C3H1-type zinc finger domain is
necessary for JEV and DEN viral RNA-binding and antiviral activity
(PubMed:23355615). {ECO:0000269|PubMed:23355615}.
-!- PTM: Proteolytically cleaved between Arg-111 and Arg-214 by MALT1
in activated T-cells; cleavage at Arg-111 is critical for
promoting ZC3H12A degradation in response to T-cell receptor (TCR)
stimulation, and hence is necessary for prolonging the stability
of a set of mRNAs controlling T-cell activation (By similarity).
{ECO:0000250|UniProtKB:Q5D1E7}.
-!- PTM: Phosphorylated by IRAK1; phosphorylation is necessary for
subsequent phosphorylation by the I-kappa-B-kinase (IKK) complex.
Phosphorylated by I-kappa-B-kinase (IKK) subunits IKBKB/IKKB and
CHUK/IKKA at Ser-438 and Ser-442; these phosphorylations promote
ubiquitin proteasome-mediated degradation of ZC3H12A and hence
facilitates rapid and robust production of IL-6 mRNA in response
to toll-like receptor (TLR) or IL-1 receptor stimuli (By
similarity). {ECO:0000250|UniProtKB:Q5D1E7}.
-!- PTM: (Microbial infection) Rapidly degraded in activated T-cells
in response to phorbol 13-acetate 12-myristate (PMA) during HIV-1
viral infection (PubMed:24191027). {ECO:0000269|PubMed:24191027}.
-!- PTM: Ubiquitinated; ubiquitination is induced in response to
interleukin IL1 receptor stimuli in a IKBKB/IKKB and IRAK1-
dependent manner, leading to proteasome-mediated degradation (By
similarity). {ECO:0000250|UniProtKB:Q5D1E7}.
-!- DISEASE: Note=Increased expression of ZC3H12A is associated with
ischemic heart disease (PubMed:16574901).
{ECO:0000269|PubMed:16574901}.
-!- SIMILARITY: Belongs to the ZC3H12 family. {ECO:0000305}.
-!- CAUTION: Was originally proposed to bind to DNA and act as
transcription factor. {ECO:0000305|PubMed:18364357}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AY920403; AAX14017.1; -; mRNA.
EMBL; AK026884; BAB15581.1; -; mRNA.
EMBL; CR457364; CAG33645.1; -; mRNA.
EMBL; AL034379; CAI20551.1; -; Genomic_DNA.
EMBL; AL449284; CAI20551.1; JOINED; Genomic_DNA.
EMBL; AL449284; CAH73689.1; -; Genomic_DNA.
EMBL; AL034379; CAH73689.1; JOINED; Genomic_DNA.
EMBL; CH471059; EAX07346.1; -; Genomic_DNA.
EMBL; CH471059; EAX07347.1; -; Genomic_DNA.
EMBL; BC005001; AAH05001.1; -; mRNA.
CCDS; CCDS417.1; -.
RefSeq; NP_001310479.1; NM_001323550.1.
RefSeq; NP_079355.2; NM_025079.2.
UniGene; Hs.656294; -.
PDB; 3V32; X-ray; 2.00 A; A/B=112-296.
PDB; 3V33; X-ray; 2.00 A; A/B=112-334.
PDB; 3V34; X-ray; 2.00 A; A/B=112-296.
PDBsum; 3V32; -.
PDBsum; 3V33; -.
PDBsum; 3V34; -.
ProteinModelPortal; Q5D1E8; -.
SMR; Q5D1E8; -.
BioGrid; 123141; 19.
CORUM; Q5D1E8; -.
IntAct; Q5D1E8; 16.
MINT; MINT-6776367; -.
STRING; 9606.ENSP00000362174; -.
iPTMnet; Q5D1E8; -.
PhosphoSitePlus; Q5D1E8; -.
BioMuta; ZC3H12A; -.
DMDM; 190479827; -.
EPD; Q5D1E8; -.
MaxQB; Q5D1E8; -.
PaxDb; Q5D1E8; -.
PeptideAtlas; Q5D1E8; -.
PRIDE; Q5D1E8; -.
Ensembl; ENST00000373087; ENSP00000362179; ENSG00000163874.
GeneID; 80149; -.
KEGG; hsa:80149; -.
UCSC; uc001cbb.5; human.
CTD; 80149; -.
DisGeNET; 80149; -.
EuPathDB; HostDB:ENSG00000163874.8; -.
GeneCards; ZC3H12A; -.
HGNC; HGNC:26259; ZC3H12A.
HPA; HPA032052; -.
HPA; HPA032053; -.
MIM; 610562; gene.
neXtProt; NX_Q5D1E8; -.
OpenTargets; ENSG00000163874; -.
PharmGKB; PA142670537; -.
eggNOG; KOG3777; Eukaryota.
eggNOG; ENOG410ZNK1; LUCA.
GeneTree; ENSGT00750000117218; -.
HOGENOM; HOG000060218; -.
HOVERGEN; HBG108758; -.
InParanoid; Q5D1E8; -.
KO; K18668; -.
OMA; FPPREYW; -.
OrthoDB; EOG091G03B2; -.
PhylomeDB; Q5D1E8; -.
TreeFam; TF315783; -.
ChiTaRS; ZC3H12A; human.
GenomeRNAi; 80149; -.
PRO; PR:Q5D1E8; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000163874; -.
CleanEx; HS_ZC3H12A; -.
ExpressionAtlas; Q5D1E8; baseline and differential.
Genevisible; Q5D1E8; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000932; C:P-body; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
GO; GO:0004532; F:exoribonuclease activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:1990869; P:cellular response to chemokine; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
GO; GO:1904637; P:cellular response to ionomycin; ISS:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; IDA:UniProtKB.
GO; GO:1903936; P:cellular response to sodium arsenite; ISS:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
GO; GO:0098586; P:cellular response to virus; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0044828; P:negative regulation by host of viral genome replication; IDA:UniProtKB.
GO; GO:0055118; P:negative regulation of cardiac muscle contraction; ISS:UniProtKB.
GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:1902714; P:negative regulation of interferon-gamma secretion; ISS:UniProtKB.
GO; GO:0050713; P:negative regulation of interleukin-1 beta secretion; ISS:UniProtKB.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:1900165; P:negative regulation of interleukin-6 secretion; ISS:UniProtKB.
GO; GO:0043031; P:negative regulation of macrophage activation; IC:BHF-UCL.
GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; ISS:UniProtKB.
GO; GO:0042347; P:negative regulation of NF-kappaB import into nucleus; ISS:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IDA:BHF-UCL.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; IDA:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:1904468; P:negative regulation of tumor necrosis factor secretion; ISS:UniProtKB.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; ISS:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; IDA:BHF-UCL.
GO; GO:0010942; P:positive regulation of cell death; IDA:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISS:UniProtKB.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
GO; GO:0010884; P:positive regulation of lipid storage; IDA:BHF-UCL.
GO; GO:2000627; P:positive regulation of miRNA catabolic process; IDA:UniProtKB.
GO; GO:0061014; P:positive regulation of mRNA catabolic process; IDA:UniProtKB.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA:UniProtKB.
GO; GO:1903003; P:positive regulation of protein deubiquitination; IMP:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:UniProtKB.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IDA:UniProtKB.
GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; ISS:UniProtKB.
GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR021869; RNase_Zc3h12_NYN.
Pfam; PF11977; RNase_Zc3h12a; 1.
1: Evidence at protein level;
3D-structure; Angiogenesis; Antiviral defense; Apoptosis;
Complete proteome; Cytoplasm; Developmental protein; Differentiation;
DNA damage; DNA-binding; Endonuclease; Endoplasmic reticulum;
Hydrolase; Immunity; Inflammatory response; Magnesium; Membrane;
Metal-binding; Neurogenesis; Nuclease; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repressor; RNA-binding;
Stress response; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 599 Endoribonuclease ZC3H12A.
/FTId=PRO_0000341512.
ZN_FING 301 324 C3H1-type.
REGION 42 87 Ubiquitin association domain.
{ECO:0000250|UniProtKB:Q5D1E7}.
REGION 81 150 Necessary for interaction with TANK.
{ECO:0000269|PubMed:25861989}.
REGION 112 297 RNase. {ECO:0000305|PubMed:22561375}.
REGION 214 220 RNA binding.
{ECO:0000305|PubMed:22561375}.
REGION 301 457 Necessary for interaction with ZC3H12D.
{ECO:0000269|PubMed:26134560}.
COMPBIAS 458 536 Pro-rich. {ECO:0000255}.
METAL 226 226 Magnesium. {ECO:0000269|PubMed:22561375}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 438 438 Phosphoserine.
{ECO:0000250|UniProtKB:Q5D1E7}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000250|UniProtKB:Q5D1E7}.
VARIANT 240 240 V -> M (in dbSNP:rs16824179).
/FTId=VAR_052968.
VARIANT 547 547 G -> D (in dbSNP:rs17849897).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3}.
/FTId=VAR_044082.
MUTAGEN 141 141 D->N: Abolishes RNase activity.
{ECO:0000269|PubMed:22561375}.
MUTAGEN 141 141 D->N: Loss of pre-miRNA RNase activity.
Attenuates strongly miRNA silencing
activity. Loss of interleukin IL17A and
IL6 mRNA instabilities. Reduces
angiogenic differentiation. Loss of RNase
activity on JEV and DEN viral RNAs and
antiviral effects. Loss of HIV-1
antiviral activity. Loss of IL1B mRNA
instability; when associated with A-226.
{ECO:0000269|PubMed:19909337,
ECO:0000269|PubMed:22055188,
ECO:0000269|PubMed:23355615,
ECO:0000269|PubMed:24191027,
ECO:0000269|PubMed:26134560,
ECO:0000269|PubMed:26320658}.
MUTAGEN 144 144 N->A: No change in RNase activity.
{ECO:0000269|PubMed:22561375}.
MUTAGEN 157 157 C->A: Does not inhibit antiviral effects.
{ECO:0000269|PubMed:23355615}.
MUTAGEN 214 214 R->A: Abolishes RNase activity.
{ECO:0000269|PubMed:22561375}.
MUTAGEN 225 225 D->A: Loss of pre-miRNA RNase activity,
IL17A mRNA instability and antiviral
effects; when associated with A-226.
{ECO:0000269|PubMed:23355615,
ECO:0000269|PubMed:24191027,
ECO:0000269|PubMed:26320658}.
MUTAGEN 226 226 D->A: Loss of pre-miRNA RNase activity,
IL17A mRNA instability and antiviral
effects; when associated with A-225. Loss
of IL1B mRNA instability; when associated
with N-141. {ECO:0000269|PubMed:19909337,
ECO:0000269|PubMed:23355615,
ECO:0000269|PubMed:24191027,
ECO:0000269|PubMed:26320658}.
MUTAGEN 306 306 C->R: Loss of interleukin IL17A mRNA
instability. Reduces weakly pre-miRNA
RNase activity. Attenuates miRNA
silencing activity. Does not inhibits
binding to Japanese encephalitis virus
(JEV) and dengue virus (DEN) RNAs and
weakly attenuates antiviral effects. Loss
of HIV-1 antiviral activity.
{ECO:0000269|PubMed:22055188,
ECO:0000269|PubMed:23355615,
ECO:0000269|PubMed:24191027,
ECO:0000269|PubMed:26320658}.
MUTAGEN 311 311 K->G: Inhibits transcriptional activity;
when associated with G-312.
{ECO:0000269|PubMed:16574901}.
MUTAGEN 312 312 C->G: Inhibits transcriptional activity;
when associated with G-311.
{ECO:0000269|PubMed:16574901}.
MUTAGEN 317 317 K->G: Inhibits transcriptional activity;
when associated with G-318.
{ECO:0000269|PubMed:16574901}.
MUTAGEN 318 318 C->G: Inhibits transcriptional activity;
when associated with G-317.
{ECO:0000269|PubMed:16574901}.
CONFLICT 248 248 D -> G (in Ref. 3; CAG33645).
{ECO:0000305}.
CONFLICT 599 599 E -> D (in Ref. 3; CAG33645).
{ECO:0000305}.
STRAND 138 141 {ECO:0000244|PDB:3V32}.
HELIX 142 149 {ECO:0000244|PDB:3V32}.
TURN 150 153 {ECO:0000244|PDB:3V32}.
STRAND 154 156 {ECO:0000244|PDB:3V32}.
HELIX 157 169 {ECO:0000244|PDB:3V32}.
STRAND 175 180 {ECO:0000244|PDB:3V32}.
HELIX 181 184 {ECO:0000244|PDB:3V32}.
STRAND 193 195 {ECO:0000244|PDB:3V33}.
HELIX 197 204 {ECO:0000244|PDB:3V32}.
STRAND 208 211 {ECO:0000244|PDB:3V32}.
STRAND 213 216 {ECO:0000244|PDB:3V33}.
STRAND 219 222 {ECO:0000244|PDB:3V33}.
HELIX 225 235 {ECO:0000244|PDB:3V32}.
STRAND 239 241 {ECO:0000244|PDB:3V32}.
HELIX 247 252 {ECO:0000244|PDB:3V32}.
HELIX 254 263 {ECO:0000244|PDB:3V32}.
STRAND 268 270 {ECO:0000244|PDB:3V32}.
STRAND 273 275 {ECO:0000244|PDB:3V32}.
TURN 280 283 {ECO:0000244|PDB:3V32}.
HELIX 288 291 {ECO:0000244|PDB:3V32}.
SEQUENCE 599 AA; 65699 MW; 9213139FA7DCA443 CRC64;
MSGPCGEKPV LEASPTMSLW EFEDSHSRQG TPRPGQELAA EEASALELQM KVDFFRKLGY
SSTEIHSVLQ KLGVQADTNT VLGELVKHGT ATERERQTSP DPCPQLPLVP RGGGTPKAPN
LEPPLPEEEK EGSDLRPVVI DGSNVAMSHG NKEVFSCRGI LLAVNWFLER GHTDITVFVP
SWRKEQPRPD VPITDQHILR ELEKKKILVF TPSRRVGGKR VVCYDDRFIV KLAYESDGIV
VSNDTYRDLQ GERQEWKRFI EERLLMYSFV NDKFMPPDDP LGRHGPSLDN FLRKKPLTLE
HRKQPCPYGR KCTYGIKCRF FHPERPSCPQ RSVADELRAN ALLSPPRAPS KDKNGRRPSP
SSQSSSLLTE SEQCSLDGKK LGAQASPGSR QEGLTQTYAP SGRSLAPSGG SGSSFGPTDW
LPQTLDSLPY VSQDCLDSGI GSLESQMSEL WGVRGGGPGE PGPPRAPYTG YSPYGSELPA
TAAFSAFGRA MGAGHFSVPA DYPPAPPAFP PREYWSEPYP LPPPTSVLQE PPVQSPGAGR
SPWGRAGSLA KEQASVYTKL CGVFPPHLVE AVMGRFPQLL DPQQLAAEIL SYKSQHPSE


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EIAAB46888 C6orf95,Homo sapiens,Human,MCP-induced protein 4,MCPIP4,p34,Probable ribonuclease ZC3H12D,TFL,Transformed follicular lymphoma,ZC3H12D,Zinc finger CCCH domain-containing protein 12D
EIAAB46820 Bif1,Bone morphogenetic protein-induced factor 1,Rat,Rattus norvegicus,Zbtb24,Zinc finger and BTB domain-containing protein 24,Zinc finger protein 450,Znf450
EIAAB43276 Mouse,Mus musculus,Putative DNA-binding protein A20,TNF alpha-induced protein 3,Tnfaip3,Tnfip3,Tumor necrosis factor alpha-induced protein 3,Zinc finger protein A20
EIAAB46918 Homo sapiens,Human,PRO1677,ZAP,ZC3HAV1,ZC3HDC2,Zinc finger antiviral protein,Zinc finger CCCH domain-containing protein 2,Zinc finger CCCH-type antiviral protein 1
EIAAB47160 G patch domain-containing protein 6,GPATC6,GPATCH6,Homo sapiens,Human,KIAA1847,ZC3H9,ZC3HDC9,ZGPAT,Zinc finger and G patch domain-containing protein,Zinc finger CCCH domain-containing protein 9,Zinc f
EIAAB32305 B lymphocyte-induced maturation protein 1,Beta-interferon gene positive regulatory domain I-binding factor,Blimp1,Blimp-1,Mouse,Mus musculus,PR domain zinc finger protein 1,PR domain-containing protei
EIAAB47213 Mouse,Mus musculus,PIAS-like protein Zimp10,Rai17,Retinoic acid-induced protein 17,Zimp10,Zinc finger MIZ domain-containing protein 1,Zmiz1
EIAAB47212 Homo sapiens,Human,KIAA1224,PIAS-like protein Zimp10,RAI17,Retinoic acid-induced protein 17,ZIMP10,Zinc finger MIZ domain-containing protein 1,ZMIZ1
EIAAB37259 DCIP,Dendritic cell-derived IFNG-induced protein,Homo sapiens,Human,Monocyte protein 5,MOP5,MOP-5,SAM domain and HD domain-containing protein 1,SAMHD1
27-526 Early Growth Response Protein 1 (EGR1, Krox-24 protein, nerve growth factor-induced protein A, Transcription factor ETR103, Zinc finger protein 225) belongs to the EGR family of C2H2-type zinc-finger 0.05 mg
28-572 Early Growth Response Protein 1 (EGR1, Krox-24 protein, nerve growth factor-induced protein A, Transcription factor ETR103, Zinc finger protein 225) belongs to the EGR family of C2H2-type zinc-finger 0.1 mg
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
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
EIAAB47204 Mouse,Mus musculus,p53-activated gene 608 protein,Pag608,Wig1,Wild-type p53-induced gene 1 protein,Zinc finger matrin-type protein 3,Zinc finger protein WIG-1,Zmat3
EIAAB32320 Histone-lysine N-methyltransferase PRDM9,Hst1,Hybrid sterility protein 1,Meiosis-induced factor containing a PR_SET domain and zinc-finger motif,Meisetz,Mouse,Mus musculus,PR domain zinc finger protei


 

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