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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.
17-JUN-2020, entry version 104.
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:AL449284}
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). Inhibits
cooperatively with ZC3H12A the differentiation of helper T cells Th17
in lungs. They repress target mRNA encoding the Th17 cell-promoting
factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The cooperation
requires RNA-binding by RC3H1 and the nuclease activity of ZC3H12A (By
similarity). Together with RC3H1, destabilizes TNFRSF4/OX40 mRNA by
binding to the conserved stem loop structure in its 3'UTR (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) Binds to Japanese encephalitis virus
(JEV) and Dengue virus (DEN) RNAs. {ECO:0000269|PubMed:23355615}.
-!- FUNCTION: (Microbial infection) Exhibits antiviral activity against
HIV-1 in lymphocytes by decreasing the abundance of HIV-1 viral RNA
species. {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:
Q5D1E8; Q9NZD4: AHSP; NbExp=4; IntAct=EBI-747793, EBI-720250;
Q5D1E8; Q9Y297: BTRC; NbExp=3; IntAct=EBI-747793, EBI-307461;
Q5D1E8; P59910: DNAJB13; NbExp=3; IntAct=EBI-747793, EBI-11514233;
Q5D1E8; Q9Y6K9: IKBKG; NbExp=2; IntAct=EBI-747793, EBI-81279;
Q5D1E8; O43187: IRAK2; NbExp=2; IntAct=EBI-747793, EBI-447733;
Q5D1E8; Q7Z4N8: P4HA3; NbExp=6; IntAct=EBI-747793, EBI-10181968;
Q5D1E8; P84022: SMAD3; NbExp=2; IntAct=EBI-747793, EBI-347161;
Q5D1E8; 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: 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}.
-!- 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 and Th17 cell differentiation.
{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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL449284; -; NOT_ANNOTATED_CDS; 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.
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; -.
SMR; Q5D1E8; -.
BioGRID; 123141; 29.
CORUM; Q5D1E8; -.
IntAct; Q5D1E8; 17.
MINT; Q5D1E8; -.
STRING; 9606.ENSP00000362179; -.
iPTMnet; Q5D1E8; -.
PhosphoSitePlus; Q5D1E8; -.
BioMuta; ZC3H12A; -.
DMDM; 190479827; -.
EPD; Q5D1E8; -.
jPOST; Q5D1E8; -.
MassIVE; Q5D1E8; -.
MaxQB; Q5D1E8; -.
PaxDb; Q5D1E8; -.
PeptideAtlas; Q5D1E8; -.
PRIDE; Q5D1E8; -.
ProteomicsDB; 62741; -.
Antibodypedia; 31721; 187 antibodies.
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; ENSG00000163874; Tissue enhanced (bone marrow, tongue).
MIM; 610562; gene.
neXtProt; NX_Q5D1E8; -.
OpenTargets; ENSG00000163874; -.
PharmGKB; PA142670537; -.
eggNOG; KOG3777; Eukaryota.
eggNOG; ENOG410ZNK1; LUCA.
GeneTree; ENSGT00940000155107; -.
HOGENOM; CLU_013020_2_1_1; -.
InParanoid; Q5D1E8; -.
KO; K18668; -.
OMA; SEHRKQP; -.
OrthoDB; 771251at2759; -.
PhylomeDB; Q5D1E8; -.
TreeFam; TF315783; -.
SIGNOR; Q5D1E8; -.
BioGRID-ORCS; 80149; 5 hits in 792 CRISPR screens.
ChiTaRS; ZC3H12A; human.
GenomeRNAi; 80149; -.
Pharos; Q5D1E8; Tbio.
PRO; PR:Q5D1E8; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; Q5D1E8; protein.
Bgee; ENSG00000163874; Expressed in right adrenal gland and 130 other tissues.
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:0032991; C:protein-containing 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: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:0002757; P:immune response-activating signal transduction; IDA:UniProtKB.
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:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
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:2000320; P:negative regulation of T-helper 17 cell differentiation; 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 by RNA polymerase II; IDA:UniProtKB.
GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; 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:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR040546; Rege-1_UBA-like.
InterPro; IPR040757; Regnase_1/ZC3H12_C.
InterPro; IPR021869; RNase_Zc3h12_NYN.
Pfam; PF18561; Regnase_1_C; 1.
Pfam; PF11977; RNase_Zc3h12a; 1.
Pfam; PF18039; UBA_6; 1.
1: Evidence at protein level;
3D-structure; Angiogenesis; Antiviral defense; Apoptosis; Cytoplasm;
Developmental protein; Differentiation; DNA damage; DNA-binding;
Endonuclease; Endoplasmic reticulum; Host-virus interaction; 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
/note="Endoribonuclease ZC3H12A"
/id="PRO_0000341512"
ZN_FING 301..324
/note="C3H1-type"
REGION 42..87
/note="Ubiquitin association domain"
/evidence="ECO:0000250|UniProtKB:Q5D1E7"
REGION 81..150
/note="Necessary for interaction with TANK"
/evidence="ECO:0000269|PubMed:25861989"
REGION 112..297
/note="RNase"
/evidence="ECO:0000305|PubMed:22561375"
REGION 214..220
/note="RNA binding"
/evidence="ECO:0000305|PubMed:22561375"
REGION 301..457
/note="Necessary for interaction with ZC3H12D"
/evidence="ECO:0000269|PubMed:26134560"
COMPBIAS 458..536
/note="Pro-rich"
/evidence="ECO:0000255"
METAL 226
/note="Magnesium"
/evidence="ECO:0000269|PubMed:22561375"
MOD_RES 99
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 344
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 438
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q5D1E7"
MOD_RES 442
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q5D1E7"
VARIANT 240
/note="V -> M (in dbSNP:rs16824179)"
/id="VAR_052968"
VARIANT 547
/note="G -> D (in dbSNP:rs17849897)"
/evidence="ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
/id="VAR_044082"
MUTAGEN 141
/note="D->N: Abolishes RNase activity."
/evidence="ECO:0000269|PubMed:22561375"
MUTAGEN 141
/note="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."
/evidence="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
/note="N->A: No change in RNase activity."
/evidence="ECO:0000269|PubMed:22561375"
MUTAGEN 157
/note="C->A: Does not inhibit antiviral effects."
/evidence="ECO:0000269|PubMed:23355615"
MUTAGEN 214
/note="R->A: Abolishes RNase activity."
/evidence="ECO:0000269|PubMed:22561375"
MUTAGEN 225
/note="D->A: Loss of pre-miRNA RNase activity, IL17A mRNA
instability and antiviral effects; when associated with A-
226."
/evidence="ECO:0000269|PubMed:23355615,
ECO:0000269|PubMed:24191027, ECO:0000269|PubMed:26320658"
MUTAGEN 226
/note="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."
/evidence="ECO:0000269|PubMed:19909337,
ECO:0000269|PubMed:23355615, ECO:0000269|PubMed:24191027,
ECO:0000269|PubMed:26320658"
MUTAGEN 306
/note="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."
/evidence="ECO:0000269|PubMed:22055188,
ECO:0000269|PubMed:23355615, ECO:0000269|PubMed:24191027,
ECO:0000269|PubMed:26320658"
MUTAGEN 311
/note="K->G: Inhibits transcriptional activity; when
associated with G-312."
/evidence="ECO:0000269|PubMed:16574901"
MUTAGEN 312
/note="C->G: Inhibits transcriptional activity; when
associated with G-311."
/evidence="ECO:0000269|PubMed:16574901"
MUTAGEN 317
/note="K->G: Inhibits transcriptional activity; when
associated with G-318."
/evidence="ECO:0000269|PubMed:16574901"
MUTAGEN 318
/note="C->G: Inhibits transcriptional activity; when
associated with G-317."
/evidence="ECO:0000269|PubMed:16574901"
CONFLICT 248
/note="D -> G (in Ref. 3; CAG33645)"
/evidence="ECO:0000305"
CONFLICT 599
/note="E -> D (in Ref. 3; CAG33645)"
/evidence="ECO:0000305"
STRAND 138..141
/evidence="ECO:0000244|PDB:3V32"
HELIX 142..149
/evidence="ECO:0000244|PDB:3V32"
TURN 150..153
/evidence="ECO:0000244|PDB:3V32"
STRAND 154..156
/evidence="ECO:0000244|PDB:3V32"
HELIX 157..169
/evidence="ECO:0000244|PDB:3V32"
STRAND 175..180
/evidence="ECO:0000244|PDB:3V32"
HELIX 181..184
/evidence="ECO:0000244|PDB:3V32"
STRAND 193..195
/evidence="ECO:0000244|PDB:3V33"
HELIX 197..204
/evidence="ECO:0000244|PDB:3V32"
STRAND 208..211
/evidence="ECO:0000244|PDB:3V32"
STRAND 213..216
/evidence="ECO:0000244|PDB:3V33"
STRAND 219..222
/evidence="ECO:0000244|PDB:3V33"
HELIX 225..235
/evidence="ECO:0000244|PDB:3V32"
STRAND 239..241
/evidence="ECO:0000244|PDB:3V32"
HELIX 247..252
/evidence="ECO:0000244|PDB:3V32"
HELIX 254..263
/evidence="ECO:0000244|PDB:3V32"
STRAND 268..270
/evidence="ECO:0000244|PDB:3V32"
STRAND 273..275
/evidence="ECO:0000244|PDB:3V32"
TURN 280..283
/evidence="ECO:0000244|PDB:3V32"
HELIX 288..291
/evidence="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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Catalog number Product name Quantity
EIAAB46883 MCP-induced protein 1,Mcpip,Mcpip1,Mouse,Mus musculus,Ribonuclease ZC3H12A,Zc3h12a,Zinc finger CCCH domain-containing protein 12A
EIAAB46881 Homo sapiens,Human,MCP-induced protein 1,MCPIP,MCPIP1,Ribonuclease ZC3H12A,ZC3H12A,Zinc finger CCCH domain-containing protein 12A
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
EIAAB43277 Homo sapiens,Human,OTU domain-containing protein 7C,OTUD7C,Putative DNA-binding protein A20,TNF alpha-induced protein 3,TNFAIP3,Tumor necrosis factor alpha-induced protein 3,Zinc finger protein A20
EIAAB46884 Rat,Rattus norvegicus,Ribonuclease ZC3H12A,Zc3h12a,Zinc finger CCCH domain-containing protein 12A
EIAAB46882 Bos taurus,Bovine,Ribonuclease ZC3H12A,ZC3H12A,Zinc finger CCCH domain-containing protein 12A
EIAAB46821 Bif1,Bone morphogenetic protein-induced factor 1,Brain-specific protein 1,Bsg1,Mouse,Mus musculus,Zbtb24,Zinc finger and BTB domain-containing protein 24,Zinc finger protein 450,Znf450
EIAAB46885 CXorf32,Homo sapiens,Human,MCP-induced protein 2,MCPIP2,Probable ribonuclease ZC3H12B,ZC3H12B,Zinc finger CCCH domain-containing protein 12B
EIAAB46887 Homo sapiens,Human,KIAA1726,MCP-induced protein 3,MCPIP3,Probable ribonuclease ZC3H12C,ZC3H12C,Zinc finger CCCH domain-containing protein 12C
EIAAB46889 MCP-induced protein 4,Mcpip4,Mouse,Mus musculus,Probable ribonuclease ZC3H12D,Tfl,Transformed follicular lymphoma homolog,Zc3h12d,Zinc finger CCCH domain-containing protein 12D
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
Pathways :
WP2199: Seed Development
WP1689: Porphyrin and chlorophyll metabolism
WP1049: G Protein Signaling Pathways
WP1700: Selenoamino acid metabolism
WP1657: Glycerolipid metabolism
WP232: G Protein Signaling Pathways
WP1663: Homologous recombination
WP2371: Parkinsons Disease Pathway
WP1371: G Protein Signaling Pathways
WP1888: Post-translational protein modification
WP1939: Unfolded Protein Response
WP1673: Naphthalene and anthracene degradation
WP346: Protein Modifications
WP1502: Mitochondrial biogenesis
WP73: G Protein Signaling Pathways
WP1613: 1,4-Dichlorobenzene degradation
WP211: BMP signaling pathway
WP1678: Nucleotide excision repair
WP1690: Propanoate metabolism
WP931: G Protein Signaling Pathways
WP1625: Base excision repair
WP2203: TSLP Signaling Pathway
WP1654: gamma-Hexachlorocyclohexane degradation
WP2292: Chemokine signaling pathway
WP1694: Pyrimidine metabolism

Related Genes :
[Zc3h12a Mcpip Mcpip1] 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)
[ZC3H12A MCPIP MCPIP1] 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)
[Zc3h12a] 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)
[ZC3H12A] Ribonuclease ZC3H12A (EC 3.1.-.-) (Zinc finger CCCH domain-containing protein 12A)
[Rc3h1 Gm551 Kiaa2025] Roquin-1 (Roquin) (EC 2.3.2.27) (Protein Sanroque) (RING finger and C3H zinc finger protein 1) (RING finger and CCCH-type zinc finger domain-containing protein 1)
[] Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[hchA AM465_15370 AWF59_019055 AZZ83_004235 B9N33_26475 BFD68_20845 C7B02_06890 C9Z28_17130 CCZ14_26645 CCZ17_22700 CRJUMX01_1140054 CRT43_11430 CUB99_23505 D3C88_02905 D3P02_16265 D9D33_15385 D9D94_15735 D9E49_19020 D9I20_10460 D9J46_03345 DJ487_18960 DJ492_13470 DL251_00505 DL979_00380 DMC44_18755 DMZ50_24495 DNR41_00375 DS966_16070 DU333_03260 DW236_02290 E0L04_20335 EA159_21345 EA167_21075 EA189_00370 EA191_21560 EA198_02280 EA200_00370 EA203_21510 EA222_02305 EA232_20265 EA233_11705 EA242_17410 EA245_13290 EA429_05770 EA435_21775 EA834_21700 ECTO124_02024 EGT48_04930 ELT23_21030 ELT33_08025 ELT34_19745 ELU82_24705 ELU96_05025 ELV13_26065 ELX79_15035 ELX83_25640 ELY23_20490 ELY24_19085 ELY50_24510 EPS76_06485 EPS91_17475 EPS94_00505 ERS085406_02591 EWK56_00075 ExPECSC065_02714 EYX99_25670 FNJ67_10775 FV295_16190 GFU40_00360 GFU45_09680 GFU47_04835 GJ638_18410 GKE92_23545 GKF28_00040 GKF34_00055 GKF47_00040 GKG08_13460 GKG09_11990 GKG11_12245 GKG22_12830 GKG29_13740 GQE47_24120 GQN33_12435 GQS26_09145 NCTC10766_03778 NCTC7928_05955 NCTC8450_02317 NCTC9007_02951 NCTC9075_02834 SY51_11150 U12A_02105 U14A_02105] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.124) (Maillard deglycase)
[RC3H1 KIAA2025 RNF198] Roquin-1 (Roquin) (EC 2.3.2.27) (RING finger and C3H zinc finger protein 1) (RING finger and CCCH-type zinc finger domain-containing protein 1) (RING finger protein 198)
[Rc3h2 Mnab] Roquin-2 (EC 2.3.2.27) (Membrane-associated nucleic acid-binding protein) (RING finger and CCCH-type zinc finger domain-containing protein 2) (RING-type E3 ubiquitin transferase Roquin-2)
[Ccl2 Je Mcp1 Scya2] C-C motif chemokine 2 (Monocyte chemoattractant protein 1) (Monocyte chemotactic protein 1) (MCP-1) (Platelet-derived growth factor-inducible protein JE) (Small-inducible cytokine A2)
[Ccl2 Je Mcp1 Scya2] C-C motif chemokine 2 (Immediate-early serum-responsive protein JE) (Monocyte chemoattractant protein 1) (Monocyte chemotactic protein 1) (MCP-1) (Small-inducible cytokine A2)
[CCL2 MCP1 SCYA2] C-C motif chemokine 2 (Monocyte chemoattractant protein 1) (Monocyte chemotactic protein 1) (MCP-1) (Small-inducible cytokine A2)
[CCL2 MCP1 SCYA2] C-C motif chemokine 2 (HC11) (Monocyte chemoattractant protein 1) (Monocyte chemotactic and activating factor) (MCAF) (Monocyte chemotactic protein 1) (MCP-1) (Monocyte secretory protein JE) (Small-inducible cytokine A2)
[CCL2 SCYA2] C-C motif chemokine 2 (Monocyte chemoattractant protein 1) (Monocyte chemotactic protein 1) (MCP-1) (Small-inducible cytokine A2)
[CCL2 SCYA2] C-C motif chemokine 2 (Acidic seminal fluid protein) (Monocyte chemotactic protein 1A) (MCP-1) (MCP-1A) (Small-inducible cytokine A2)
[Zfp36l1 Brf1 Cmg1 Tis11b] mRNA decay activator protein ZFP36L1 (Butyrate response factor 1) (EGF-inducible protein CMG1) (TPA-induced sequence 11b) (Zinc finger protein 36, C3H1 type-like 1) (ZFP36-like 1)
[ZFP36L1 BERG36 BRF1 ERF1 RNF162B TIS11B] mRNA decay activator protein ZFP36L1 (Butyrate response factor 1) (EGF-response factor 1) (ERF-1) (TPA-induced sequence 11b) (Zinc finger protein 36, C3H1 type-like 1) (ZFP36-like 1)
[Zfp36l1 Brf1 Tis11b] mRNA decay activator protein ZFP36L1 (Butyrate response factor 1) (TPA-induced sequence 11b) (Zinc finger protein 36, C3H1 type-like 1) (ZFP36-like 1)
[CCL2 MCP1 SCYA2] C-C motif chemokine 2 (Monocyte chemoattractant protein 1) (Monocyte chemotactic protein 1) (MCP-1) (Small-inducible cytokine A2)
[SAMHD1 MOP5] Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Dendritic cell-derived IFNG-induced protein) (DCIP) (Monocyte protein 5) (MOP-5) (SAM domain and HD domain-containing protein 1) (hSAMHD1)
[Prdm1 Blimp1] PR domain zinc finger protein 1 (EC 2.1.1.-) (B lymphocyte-induced maturation protein 1) (Blimp-1) (Beta-interferon gene positive regulatory domain I-binding factor) (PR domain-containing protein 1)
[CCL2 MCP1 SCYA2] C-C motif chemokine 2 (Monocyte chemoattractant protein 1) (Monocyte chemotactic protein 1) (MCP-1) (Small-inducible cytokine A2)
[Zfp36l2 Brf2 Tis11d] mRNA decay activator protein ZFP36L2 (Butyrate response factor 2) (TPA-induced sequence 11d) (Zinc finger protein 36, C3H1 type-like 2) (ZFP36-like 2)
[ZFP36L2 BRF2 ERF2 RNF162C TIS11D] mRNA decay activator protein ZFP36L2 (Butyrate response factor 2) (EGF-response factor 2) (ERF-2) (TPA-induced sequence 11d) (Zinc finger protein 36, C3H1 type-like 2) (ZFP36-like 2)
[IFI27] Interferon alpha-inducible protein 27, mitochondrial (p27) (Interferon alpha-induced 11.5 kDa protein) (Interferon-stimulated gene 12a protein) (ISG12(a)) (ISG12A)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.354) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[CCR2 CMKBR2] C-C chemokine receptor type 2 (C-C CKR-2) (CC-CKR-2) (CCR-2) (CCR2) (Monocyte chemoattractant protein 1 receptor) (MCP-1-R) (CD antigen CD192)
[Prdm9 Hst1 Meisetz] Histone-lysine N-methyltransferase PRDM9 (Hybrid sterility protein 1) (Meiosis-induced factor containing a PR/SET domain and zinc-finger motif) (PR domain zinc finger protein 9) (PR domain-containing protein 9) (Protein-lysine N-methyltransferase PRDM9) (EC 2.1.1.-) ([histone H3]-lysine36 N-trimethyltransferase PRDM9) (EC 2.1.1.359) ([histone H3]-lysine4 N-trimethyltransferase PRDM9) (EC 2.1.1.354) ([histone H3]-lysine9 N-trimethyltransferase PRDM9) (EC 2.1.1.355) ([histone H4]-N-methyl-L-lysine20 N-methyltransferase PRDM9) (EC 2.1.1.362) ([histone H4]-lysine20 N-methyltransferase PRDM9) (EC 2.1.1.361)
[CCL8 MCP2 SCYA10 SCYA8] C-C motif chemokine 8 (HC14) (Monocyte chemoattractant protein 2) (Monocyte chemotactic protein 2) (MCP-2) (Small-inducible cytokine A8) [Cleaved into: MCP-2(6-76)]
[IFIH1 MDA5 RH116] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Clinically amyopathic dermatomyositis autoantigen 140 kDa) (CADM-140 autoantigen) (Helicase with 2 CARD domains) (Helicard) (Interferon-induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (Murabutide down-regulated protein) (RIG-I-like receptor 2) (RLR-2) (RNA helicase-DEAD box protein 116)

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