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Ribonuclease ZC3H12A (EC 3.1.-.-) (Zinc finger CCCH domain-containing protein 12A)

 ZC12A_BOVIN             Reviewed;         583 AA.
A6QQJ8;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
21-AUG-2007, sequence version 1.
02-JUN-2021, entry version 88.
RecName: Full=Ribonuclease ZC3H12A;
EC=3.1.-.-;
AltName: Full=Zinc finger CCCH domain-containing protein 12A;
Name=ZC3H12A {ECO:0000250|UniProtKB:Q5D1E8};
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
Bovinae; Bos.
NCBI_TaxID=9913;
[1] {ECO:0000312|EMBL:AAI49868.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford {ECO:0000312|EMBL:AAI49868.1};
TISSUE=Hippocampus {ECO:0000312|EMBL:AAI49868.1};
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
-!- 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. 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. 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). 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. 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 (By similarity). Plays a role in the inhibition of
microRNAs (miRNAs) biogenesis (By similarity). 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 (By similarity).
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 (By similarity). Affects the overall
ubiquitination of cellular proteins. 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. 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 (By
similarity). Prevents stress granules (SGs) formation and promotes
macrophage apoptosis under stress conditions, including arsenite-
induced oxidative stress, heat shock, and energy deprivation. Plays a
role in the regulation of macrophage polarization; promotes IL4-induced
polarization of macrophages M1 into anti-inflammatory M2 state. May
also act as a transcription factor that regulates the expression of
multiple genes involved in inflammatory response, angiogenesis,
adipogenesis and apoptosis (By similarity). Functions as a positive
regulator of glial differentiation of neuroprogenitor cells through an
amyloid precursor protein (APP)-dependent signaling pathway (By
similarity). 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:0000250|UniProtKB:Q5D1E8}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q5D1E8};
Note=Mg(2+) is required for RNase activity.
{ECO:0000250|UniProtKB:Q5D1E8};
-!- SUBUNIT: Oligomer. 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. Interacts with IKBKG; this interaction increases in
response to DNA damage. 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. Interacts with TRAF6; this
interaction increases in response to DNA damage and is stimulated by
TANK. 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. Interacts with ZC3H12D. Interacts with
TNRC6A. Interacts with IKBKB/IKKB (By similarity). 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:0000250|UniProtKB:Q5D1E8}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5D1E8}. Cytoplasm
{ECO:0000250|UniProtKB:Q5D1E8}. Cytoplasm, P-body
{ECO:0000250|UniProtKB:Q5D1E8}. 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) (By similarity). {ECO:0000250|UniProtKB:Q5D1E8}.
-!- DOMAIN: The C3H1-type zinc finger domain and C-terminal region are
necessary for pre-miRNA binding. The C-terminal region and proline-rich
domain are necessary for oligomerization.
{ECO:0000250|UniProtKB:Q5D1E8}.
-!- 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-422 and Ser-426; 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, ECO:0000250|UniProtKB:Q5D1E8}.
-!- 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, ECO:0000250|UniProtKB:Q5D1E8}.
-!- PTM: Proteolytically cleaved between Arg-95 and Arg-198 by MALT1 in
activated T-cells; cleavage at Arg-95 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}.
-!- SIMILARITY: Belongs to the ZC3H12 family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; BC149867; AAI49868.1; -; mRNA.
RefSeq; NP_001095657.1; NM_001102187.1.
RefSeq; XP_005204850.1; XM_005204793.3.
SMR; A6QQJ8; -.
STRING; 9913.ENSBTAP00000015041; -.
PaxDb; A6QQJ8; -.
PRIDE; A6QQJ8; -.
Ensembl; ENSBTAT00000015041; ENSBTAP00000015041; ENSBTAG00000011316.
GeneID; 535344; -.
KEGG; bta:535344; -.
CTD; 80149; -.
VGNC; VGNC:37097; ZC3H12A.
eggNOG; KOG3777; Eukaryota.
GeneTree; ENSGT00940000155107; -.
HOGENOM; CLU_013020_2_1_1; -.
InParanoid; A6QQJ8; -.
OMA; SEHRKQP; -.
OrthoDB; 771251at2759; -.
TreeFam; TF315783; -.
Proteomes; UP000009136; Chromosome 3.
Bgee; ENSBTAG00000011316; Expressed in vertebral column and 99 other tissues.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IBA:GO_Central.
GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0000932; C:P-body; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
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; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS: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; ISS: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; ISS:UniProtKB.
GO; GO:0004518; F:nuclease activity; ISS:UniProtKB.
GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
GO; GO:0004843; F:thiol-dependent deubiquitinase; IEA:Ensembl.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS: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; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:1904637; P:cellular response to ionomycin; ISS:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
GO; GO:1903936; P:cellular response to sodium arsenite; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
GO; GO:0002757; P:immune response-activating signal transduction; ISS:UniProtKB.
GO; GO:0044828; P:negative regulation by host of viral genome replication; IEA:Ensembl.
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:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0032689; P:negative regulation of interferon-gamma production; ISS:UniProtKB.
GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISS:UniProtKB.
GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:UniProtKB.
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; IEA:Ensembl.
GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; ISS:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
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; ISS:UniProtKB.
GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; IBA:GO_Central.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
GO; GO:0010942; P:positive regulation of cell death; ISS:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IEA:Ensembl.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IEA:Ensembl.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0010884; P:positive regulation of lipid storage; IEA:Ensembl.
GO; GO:2000627; P:positive regulation of miRNA catabolic process; ISS:UniProtKB.
GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; IEA:Ensembl.
GO; GO:1903003; P:positive regulation of protein deubiquitination; IEA:Ensembl.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IEA:Ensembl.
GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; ISS:UniProtKB.
GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; ISS:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
InterPro; IPR040546; Rege-1_UBA-like.
InterPro; IPR040757; Regnase_1/ZC3H12_C.
InterPro; IPR021869; RNase_Zc3h12_NYN.
InterPro; IPR041367; Znf-CCCH_4.
InterPro; IPR000571; Znf_CCCH.
Pfam; PF18561; Regnase_1_C; 1.
Pfam; PF11977; RNase_Zc3h12a; 1.
Pfam; PF18039; UBA_6; 1.
Pfam; PF18044; zf-CCCH_4; 1.
PROSITE; PS50103; ZF_C3H1; 1.
2: Evidence at transcript level;
Angiogenesis; Apoptosis; Cytoplasm; Developmental protein; Differentiation;
Endonuclease; Endoplasmic reticulum; Hydrolase; Magnesium; Membrane;
Metal-binding; Nuclease; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1..583
/note="Ribonuclease ZC3H12A"
/id="PRO_0000341511"
DOMAIN 119..274
/note="RNase NYN"
/evidence="ECO:0000255"
ZN_FING 284..309
/note="C3H1-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
REGION 1..29
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 26..71
/note="Ubiquitin association domain"
/evidence="ECO:0000250|UniProtKB:Q5D1E7"
REGION 65..134
/note="Necessary for interaction with TANK"
/evidence="ECO:0000250|UniProtKB:Q5D1E8"
REGION 73..119
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 96..281
/note="RNase"
/evidence="ECO:0000250|UniProtKB:Q5D1E8"
REGION 198..204
/note="RNA binding"
/evidence="ECO:0000250|UniProtKB:Q5D1E8"
REGION 262..290
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 285..441
/note="Necessary for interaction with ZC3H12D"
/evidence="ECO:0000250|UniProtKB:Q5D1E8"
REGION 323..404
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 503..530
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 272..290
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 339..354
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 385..404
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
METAL 210
/note="Magnesium"
/evidence="ECO:0000250|UniProtKB:Q5D1E8"
MOD_RES 83
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q5D1E8"
MOD_RES 422
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q5D1E7"
MOD_RES 426
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q5D1E7"
SEQUENCE 583 AA; 64263 MW; A9258510092CD5D3 CRC64;
MSLWELEDRR SCQGTPRPAQ EPTAEEATTA ELQMKVDFFR KLGYSSAEIH SVLQKLGIQA
DTNTVLGELV KHGSAAERER QASPDPCPQL PLVPRGGGTP KAPTVETYPP EEDKEGSDLR
PIVIDGSNVA MSHGNKDVFS CRGILLAVNW FLERGHTDIT VFVPSWRKEQ PRPDVPITDQ
HILRDLEKKK ILVFTPSRRV GGKRVVCYDD RFIVKLAFES DGIVVSNDTY RDLQGERQEW
KRFIEERLLM YSFVNDKFMP PDDPLGRHGP SLDNFLRKKP LTSEHKKQPC PYGRKCTYGI
KCRFLHPERP SRPQRSVADE LRANALLPPS RAASKDKNSR RPSPSSQPGS LPTEHEQCSP
DRKKLGAQAS PGTPREGLMQ TFAPTGRSLP PSGSSGGSFG PSEWFPQTLD SLPYASQDCL
DSGIGSLESQ MSELWGVRGG GPGEPGPPRG PYAGYCTYGA ELPATPAFSA FSRALGAGHF
SVPADYAPPP AAFPPREYWS EPYQLPPPTQ RLQEPQAPGP GADRGPWGGA GRLAKERASV
YTKLCGVFPP HLVEAVMSRF PQLLDPQQLA AEILSYKSQH LSE


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Pathways :
WP2199: Seed Development
WP1689: Porphyrin and chlorophyll metabolism
WP1659: Glycine, serine and threonine metabolism
WP2371: Parkinsons Disease Pathway
WP1049: G Protein Signaling Pathways
WP1713: Two-component system
WP1438: Influenza A virus infection
WP1892: Protein folding
WP1665: Limonene and pinene degradation
WP525: Mitochondrial Unfolded-Protein Response
WP1675: Nitrogen metabolism
WP813: G Protein Signaling Pathways
WP1531: Vitamin D synthesis
WP2032: TSH signaling pathway
WP1616: ABC transporters
WP1685: Peptidoglycan biosynthesis
WP1692: Protein export
WP1644: DNA replication
WP2272: Pathogenic Escherichia coli infection
WP1657: Glycerolipid metabolism
WP2324: AGE/RAGE pathway
WP1700: Selenoamino acid metabolism
WP1888: Post-translational protein modification
WP1663: Homologous recombination
WP35: G Protein Signaling Pathways

Related Genes :
[ZC3H12A] Ribonuclease ZC3H12A (EC 3.1.-.-) (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 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)
[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)
[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)
[] 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)]
[ZC3HAV1 ZC3HDC2 PRO1677] Zinc finger CCCH-type antiviral protein 1 (ADP-ribosyltransferase diphtheria toxin-like 13) (ARTD13) (Inactive Poly [ADP-ribose] polymerase 13) (PARP13) (Zinc finger CCCH domain-containing protein 2) (Zinc finger antiviral protein) (ZAP)
[cas12a cpf1 HMPREF1246_0236] CRISPR-associated endonuclease Cas12a (EC 3.1.21.1) (EC 4.6.1.22) (AsCpf1) (CRISPR-associated endonuclease Cpf1)
[cas12a cpf1 FTN_1397] CRISPR-associated endonuclease Cas12a (EC 3.1.21.1) (EC 4.6.1.22) (CRISPR-associated endonuclease Cpf1) (FnCas12a) (FnCpf1)
[Zc3hav1 Zap] Zinc finger CCCH-type antiviral protein 1 (ADP-ribosyltransferase diphtheria toxin-like 13) (ARTD13) (Inactive Poly [ADP-ribose] polymerase 13) (PARP13) (Zinc finger antiviral protein) (ZAP) (rZAP)
[zfp36l2-A] mRNA decay activator protein ZFP36L2-A (CCCH zinc finger protein 3-A) (XC3H-3) (Zinc finger protein 36, C3H1 type-like 2-A)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[TRAF6 RNF85] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (Interleukin-1 signal transducer) (RING finger protein 85) (RING-type E3 ubiquitin transferase TRAF6)
[CPSF30 OXT6 At1g30460 F26G16.5 F26G16.6] 30-kDa cleavage and polyadenylation specificity factor 30 (EC 3.1.21.-) (Protein OXIDATIVE STRESS TOLERANT 6) (Zinc finger CCCH domain-containing protein 11) (AtC3H11)
[Zc3h8 Fliz1 Zc3hdc8] Zinc finger CCCH domain-containing protein 8 (Fetal liver zinc finger protein 1)
[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) (Cysteine methyltransferase KMT2A) (EC 2.1.1.-) (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)]
[RC3H2 MNAB RNF164] 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 finger protein 164) (RING-type E3 ubiquitin transferase Roquin-2)
[UNKL C16orf28 ZC3H5L ZC3HDC5L] Putative E3 ubiquitin-protein ligase UNKL (EC 2.3.2.-) (RING finger protein unkempt-like) (Zinc finger CCCH domain-containing protein 5-like)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[wee-1.3 let-37 myt-1 spe-37 Y53C12A.1] Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase wee-1.3 (EC 2.7.11.1) (Lethal protein 37) (Myt1 kinase)
[Zc3hav1] Zinc finger CCCH-type antiviral protein 1 (ADP-ribosyltransferase diphtheria toxin-like 13) (ARTD13) (Inactive Poly [ADP-ribose] polymerase 13) (PARP13)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[zfp36l2-B zfp36l2] mRNA decay activator protein ZFP36L2-B (CCCH zinc finger protein 3-B) (XC3H-3b) (Zinc finger protein 36, C3H1 type-like 2-B)
[PLA2G12A PLA2G12 FKSG38 UNQ2519/PRO6012] Group XIIA secretory phospholipase A2 (GXII sPLA2) (sPLA2-XII) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase 12A)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; 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); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)] (Fragment)
[orf1ab] 3C-like proteinase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.6.4.12) (EC 3.6.4.13) (Exoribonuclease) (Growth factor-like peptide) (Helicase) (M-PRO) (NendoU) (Non-structural protein 1) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (Peptide HD2) (Putative 2'-O-methyl transferase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (nsp12) (nsp13) (nsp14) (nsp15) (nsp16) (nsp5) (p12) (p195) (p23) (p34) (p5) (p87) (p9)
[] 49 kDa proteinase (EC 2.7.7.48) (EC 3.4.22.44) (EC 3.4.22.45) (6 kDa protein 1) (6 kDa protein 2) (Coat protein) (Cytoplasmic inclusion protein) (Genome polyprotein) (Helper component proteinase) (N-terminal protein) (NIa-pro) (Nuclear inclusion protein A) (Nuclear inclusion protein B) (P1 proteinase) (RNA-directed RNA polymerase) (VPg) (Viral genome-linked protein) (protein P3)

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