Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endoribonuclease ZC3H12A

Gene

ZC3H12A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity10 Publications
(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).2 Publications

Cofactori

Mg2+1 PublicationNote: Mg2+ is required for RNase activity (PubMed:22561375).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi226Magnesium1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri301 – 324C3H1-typeAdd BLAST24

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • endoribonuclease activity Source: UniProtKB
  • exoribonuclease activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • miRNA binding Source: UniProtKB
  • mRNA 3'-UTR AU-rich region binding Source: UniProtKB
  • mRNA 3'-UTR binding Source: UniProtKB
  • mRNA binding Source: UniProtKB
  • ribonuclease activity Source: UniProtKB
  • ribosome binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • RNA stem-loop binding Source: UniProtKB

GO - Biological processi

  • 3'-UTR-mediated mRNA destabilization Source: UniProtKB
  • angiogenesis Source: UniProtKB-KW
  • apoptotic process Source: UniProtKB-KW
  • cell differentiation Source: UniProtKB-KW
  • cellular response to chemokine Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to glucose starvation Source: UniProtKB
  • cellular response to interleukin-1 Source: UniProtKB
  • cellular response to ionomycin Source: UniProtKB
  • cellular response to lipopolysaccharide Source: UniProtKB
  • cellular response to oxidative stress Source: UniProtKB
  • cellular response to phorbol 13-acetate 12-myristate Source: UniProtKB
  • cellular response to sodium arsenite Source: UniProtKB
  • cellular response to tumor necrosis factor Source: UniProtKB
  • cellular response to virus Source: UniProtKB
  • defense response to virus Source: UniProtKB-KW
  • inflammatory response Source: UniProtKB-KW
  • negative regulation by host of viral genome replication Source: UniProtKB
  • negative regulation of cardiac muscle contraction Source: UniProtKB
  • negative regulation of cytokine production involved in inflammatory response Source: UniProtKB
  • negative regulation of gene expression Source: BHF-UCL
  • negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • negative regulation of interferon-gamma secretion Source: UniProtKB
  • negative regulation of interleukin-1 beta secretion Source: UniProtKB
  • negative regulation of interleukin-6 production Source: BHF-UCL
  • negative regulation of interleukin-6 secretion Source: UniProtKB
  • negative regulation of macrophage activation Source: BHF-UCL
  • negative regulation of muscle cell apoptotic process Source: UniProtKB
  • negative regulation of NF-kappaB import into nucleus Source: UniProtKB
  • negative regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  • negative regulation of nitric oxide biosynthetic process Source: BHF-UCL
  • negative regulation of production of miRNAs involved in gene silencing by miRNA Source: UniProtKB
  • negative regulation of protein phosphorylation Source: UniProtKB
  • negative regulation of tumor necrosis factor production Source: BHF-UCL
  • negative regulation of tumor necrosis factor secretion Source: UniProtKB
  • nervous system development Source: UniProtKB-KW
  • nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay Source: UniProtKB
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of autophagy Source: BHF-UCL
  • positive regulation of cell death Source: UniProtKB
  • positive regulation of defense response to virus by host Source: UniProtKB
  • positive regulation of endothelial cell migration Source: UniProtKB
  • positive regulation of execution phase of apoptosis Source: UniProtKB
  • positive regulation of fat cell differentiation Source: BHF-UCL
  • positive regulation of gene expression Source: BHF-UCL
  • positive regulation of lipid storage Source: BHF-UCL
  • positive regulation of miRNA catabolic process Source: UniProtKB
  • positive regulation of mRNA catabolic process Source: UniProtKB
  • positive regulation of p38MAPK cascade Source: UniProtKB
  • positive regulation of protein deubiquitination Source: UniProtKB
  • positive regulation of protein import into nucleus Source: UniProtKB
  • positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • protein deubiquitination Source: UniProtKB
  • protein oligomerization Source: UniProtKB
  • regulation of gene expression Source: UniProtKB
  • RNA phosphodiester bond hydrolysis Source: UniProtKB
  • RNA phosphodiester bond hydrolysis, endonucleolytic Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Endonuclease, Hydrolase, Nuclease, Repressor

Keywords - Biological processi

Angiogenesis, Antiviral defense, Apoptosis, Differentiation, DNA damage, Immunity, Inflammatory response, Neurogenesis, Stress response, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Endoribonuclease ZC3H12ACurated (EC:3.1.-.-1 Publication)
Alternative name(s):
Monocyte chemotactic protein-induced protein 11 Publication
Short name:
MCP-induced protein 11 Publication
Short name:
MCPIP-11 Publication
Regnase-11 Publication
Short name:
Reg1By similarity
Zinc finger CCCH domain-containing protein 12AImported
Gene namesi
Name:ZC3H12AImported
Synonyms:MCPIP1 Publication, MCPIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:26259. ZC3H12A.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytoskeleton Source: UniProtKB
  • extrinsic component of endoplasmic reticulum membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • plasma membrane Source: HPA
  • protein complex Source: UniProtKB
  • rough endoplasmic reticulum Source: UniProtKB
  • rough endoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Increased expression of ZC3H12A is associated with ischemic heart disease (PubMed:16574901).

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi141D → N: Abolishes RNase activity. 1 Publication1
Mutagenesisi141D → 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. 6 Publications1
Mutagenesisi144N → A: No change in RNase activity. 1 Publication1
Mutagenesisi157C → A: Does not inhibit antiviral effects. 1 Publication1
Mutagenesisi214R → A: Abolishes RNase activity. 1 Publication1
Mutagenesisi225D → A: Loss of pre-miRNA RNase activity, IL17A mRNA instability and antiviral effects; when associated with A-226. 3 Publications1
Mutagenesisi226D → 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. 4 Publications1
Mutagenesisi306C → 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. 4 Publications1
Mutagenesisi311K → G: Inhibits transcriptional activity; when associated with G-312. 1 Publication1
Mutagenesisi312C → G: Inhibits transcriptional activity; when associated with G-311. 1 Publication1
Mutagenesisi317K → G: Inhibits transcriptional activity; when associated with G-318. 1 Publication1
Mutagenesisi318C → G: Inhibits transcriptional activity; when associated with G-317. 1 Publication1

Organism-specific databases

DisGeNETi80149.
OpenTargetsiENSG00000163874.
PharmGKBiPA142670537.

Polymorphism and mutation databases

BioMutaiZC3H12A.
DMDMi190479827.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003415121 – 599Endoribonuclease ZC3H12AAdd BLAST599

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei99PhosphoserineCombined sources1
Modified residuei344PhosphoserineCombined sources1
Modified residuei438PhosphoserineBy similarity1
Modified residuei442PhosphoserineBy similarity1

Post-translational modificationi

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).By similarity
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).By similarity
(Microbial infection) Rapidly degraded in activated T-cells in response to phorbol 13-acetate 12-myristate (PMA) during HIV-1 viral infection (PubMed:24191027).1 Publication
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).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ5D1E8.
MaxQBiQ5D1E8.
PaxDbiQ5D1E8.
PeptideAtlasiQ5D1E8.
PRIDEiQ5D1E8.

PTM databases

iPTMnetiQ5D1E8.
PhosphoSitePlusiQ5D1E8.

Expressioni

Tissue specificityi

Expressed in heart, placenta, spleen, kidney, liver and lung (PubMed:19909337). Expressed in leukocytes (PubMed:19909337). Expressed in monocyte (PubMed:16574901).2 Publications

Inductioni

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).10 Publications
(Microbial infection) Up-regulated in response to Japanese encephalitis virus (JEV) and dengue virus (DEN) infections (PubMed:23355615).1 Publication

Gene expression databases

BgeeiENSG00000163874.
CleanExiHS_ZC3H12A.
ExpressionAtlasiQ5D1E8. baseline and differential.
GenevisibleiQ5D1E8. HS.

Organism-specific databases

HPAiHPA032052.
HPA032053.

Interactioni

Subunit structurei

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).By similarity5 Publications
(Microbial infection) Oligomerization is necessary for antiviral activity (PubMed:23355615).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AHSPQ9NZD44EBI-747793,EBI-720250
BTRCQ9Y2973EBI-747793,EBI-307461
IKBKGQ9Y6K92EBI-747793,EBI-81279
IRAK2O431872EBI-747793,EBI-447733
P4HA3Q7Z4N85EBI-747793,EBI-10181968
SMAD3P840222EBI-747793,EBI-347161
USP10Q146945EBI-747793,EBI-2510389

Protein-protein interaction databases

BioGridi123141. 19 interactors.
IntActiQ5D1E8. 16 interactors.
MINTiMINT-6776367.
STRINGi9606.ENSP00000362174.

Structurei

Secondary structure

1599
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi138 – 141Combined sources4
Helixi142 – 149Combined sources8
Turni150 – 153Combined sources4
Beta strandi154 – 156Combined sources3
Helixi157 – 169Combined sources13
Beta strandi175 – 180Combined sources6
Helixi181 – 184Combined sources4
Beta strandi193 – 195Combined sources3
Helixi197 – 204Combined sources8
Beta strandi208 – 211Combined sources4
Beta strandi213 – 216Combined sources4
Beta strandi219 – 222Combined sources4
Helixi225 – 235Combined sources11
Beta strandi239 – 241Combined sources3
Helixi247 – 252Combined sources6
Helixi254 – 263Combined sources10
Beta strandi268 – 270Combined sources3
Beta strandi273 – 275Combined sources3
Turni280 – 283Combined sources4
Helixi288 – 291Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3V32X-ray2.00A/B112-296[»]
3V33X-ray2.00A/B112-334[»]
3V34X-ray2.00A/B112-296[»]
ProteinModelPortaliQ5D1E8.
SMRiQ5D1E8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni42 – 87Ubiquitin association domainBy similarityAdd BLAST46
Regioni81 – 150Necessary for interaction with TANK1 PublicationAdd BLAST70
Regioni112 – 297RNase1 PublicationAdd BLAST186
Regioni214 – 220RNA binding1 Publication7
Regioni301 – 457Necessary for interaction with ZC3H12D1 PublicationAdd BLAST157

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi458 – 536Pro-richSequence analysisAdd BLAST79

Domaini

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).1 Publication
(Microbial infection) The C3H1-type zinc finger domain is necessary for JEV and DEN viral RNA-binding and antiviral activity (PubMed:23355615).1 Publication

Sequence similaritiesi

Belongs to the ZC3H12 family.Curated
Contains 1 C3H1-type zinc finger.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri301 – 324C3H1-typeAdd BLAST24

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3777. Eukaryota.
ENOG410ZNK1. LUCA.
GeneTreeiENSGT00750000117218.
HOGENOMiHOG000060218.
HOVERGENiHBG108758.
InParanoidiQ5D1E8.
KOiK18668.
OMAiAFPPREY.
OrthoDBiEOG091G03B2.
PhylomeDBiQ5D1E8.
TreeFamiTF315783.

Family and domain databases

InterProiIPR021869. RNase_Zc3h12_NYN.
[Graphical view]
PfamiPF11977. RNase_Zc3h12a. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5D1E8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGPCGEKPV LEASPTMSLW EFEDSHSRQG TPRPGQELAA EEASALELQM
60 70 80 90 100
KVDFFRKLGY SSTEIHSVLQ KLGVQADTNT VLGELVKHGT ATERERQTSP
110 120 130 140 150
DPCPQLPLVP RGGGTPKAPN LEPPLPEEEK EGSDLRPVVI DGSNVAMSHG
160 170 180 190 200
NKEVFSCRGI LLAVNWFLER GHTDITVFVP SWRKEQPRPD VPITDQHILR
210 220 230 240 250
ELEKKKILVF TPSRRVGGKR VVCYDDRFIV KLAYESDGIV VSNDTYRDLQ
260 270 280 290 300
GERQEWKRFI EERLLMYSFV NDKFMPPDDP LGRHGPSLDN FLRKKPLTLE
310 320 330 340 350
HRKQPCPYGR KCTYGIKCRF FHPERPSCPQ RSVADELRAN ALLSPPRAPS
360 370 380 390 400
KDKNGRRPSP SSQSSSLLTE SEQCSLDGKK LGAQASPGSR QEGLTQTYAP
410 420 430 440 450
SGRSLAPSGG SGSSFGPTDW LPQTLDSLPY VSQDCLDSGI GSLESQMSEL
460 470 480 490 500
WGVRGGGPGE PGPPRAPYTG YSPYGSELPA TAAFSAFGRA MGAGHFSVPA
510 520 530 540 550
DYPPAPPAFP PREYWSEPYP LPPPTSVLQE PPVQSPGAGR SPWGRAGSLA
560 570 580 590
KEQASVYTKL CGVFPPHLVE AVMGRFPQLL DPQQLAAEIL SYKSQHPSE
Length:599
Mass (Da):65,699
Last modified:February 5, 2008 - v1
Checksum:i9213139FA7DCA443
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti248D → G in CAG33645 (Ref. 3) Curated1
Sequence conflicti599E → D in CAG33645 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052968240V → M.Corresponds to variant rs16824179dbSNPEnsembl.1
Natural variantiVAR_044082547G → D.3 PublicationsCorresponds to variant rs17849897dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY920403 mRNA. Translation: AAX14017.1.
AK026884 mRNA. Translation: BAB15581.1.
CR457364 mRNA. Translation: CAG33645.1.
AL034379, AL449284 Genomic DNA. Translation: CAI20551.1.
AL449284, AL034379 Genomic DNA. Translation: CAH73689.1.
CH471059 Genomic DNA. Translation: EAX07346.1.
CH471059 Genomic DNA. Translation: EAX07347.1.
BC005001 mRNA. Translation: AAH05001.1.
CCDSiCCDS417.1.
RefSeqiNP_001310479.1. NM_001323550.1.
NP_079355.2. NM_025079.2.
UniGeneiHs.656294.

Genome annotation databases

EnsembliENST00000373087; ENSP00000362179; ENSG00000163874.
GeneIDi80149.
KEGGihsa:80149.
UCSCiuc001cbb.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY920403 mRNA. Translation: AAX14017.1.
AK026884 mRNA. Translation: BAB15581.1.
CR457364 mRNA. Translation: CAG33645.1.
AL034379, AL449284 Genomic DNA. Translation: CAI20551.1.
AL449284, AL034379 Genomic DNA. Translation: CAH73689.1.
CH471059 Genomic DNA. Translation: EAX07346.1.
CH471059 Genomic DNA. Translation: EAX07347.1.
BC005001 mRNA. Translation: AAH05001.1.
CCDSiCCDS417.1.
RefSeqiNP_001310479.1. NM_001323550.1.
NP_079355.2. NM_025079.2.
UniGeneiHs.656294.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3V32X-ray2.00A/B112-296[»]
3V33X-ray2.00A/B112-334[»]
3V34X-ray2.00A/B112-296[»]
ProteinModelPortaliQ5D1E8.
SMRiQ5D1E8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123141. 19 interactors.
IntActiQ5D1E8. 16 interactors.
MINTiMINT-6776367.
STRINGi9606.ENSP00000362174.

PTM databases

iPTMnetiQ5D1E8.
PhosphoSitePlusiQ5D1E8.

Polymorphism and mutation databases

BioMutaiZC3H12A.
DMDMi190479827.

Proteomic databases

EPDiQ5D1E8.
MaxQBiQ5D1E8.
PaxDbiQ5D1E8.
PeptideAtlasiQ5D1E8.
PRIDEiQ5D1E8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373087; ENSP00000362179; ENSG00000163874.
GeneIDi80149.
KEGGihsa:80149.
UCSCiuc001cbb.5. human.

Organism-specific databases

CTDi80149.
DisGeNETi80149.
GeneCardsiZC3H12A.
HGNCiHGNC:26259. ZC3H12A.
HPAiHPA032052.
HPA032053.
MIMi610562. gene.
neXtProtiNX_Q5D1E8.
OpenTargetsiENSG00000163874.
PharmGKBiPA142670537.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3777. Eukaryota.
ENOG410ZNK1. LUCA.
GeneTreeiENSGT00750000117218.
HOGENOMiHOG000060218.
HOVERGENiHBG108758.
InParanoidiQ5D1E8.
KOiK18668.
OMAiAFPPREY.
OrthoDBiEOG091G03B2.
PhylomeDBiQ5D1E8.
TreeFamiTF315783.

Miscellaneous databases

ChiTaRSiZC3H12A. human.
GenomeRNAii80149.
PROiQ5D1E8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163874.
CleanExiHS_ZC3H12A.
ExpressionAtlasiQ5D1E8. baseline and differential.
GenevisibleiQ5D1E8. HS.

Family and domain databases

InterProiIPR021869. RNase_Zc3h12_NYN.
[Graphical view]
PfamiPF11977. RNase_Zc3h12a. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiZC12A_HUMAN
AccessioniPrimary (citable) accession number: Q5D1E8
Secondary accession number(s): D3DPT0, Q6I9Z1, Q9H5P1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: February 5, 2008
Last modified: November 30, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Was originally proposed to bind to DNA and act as transcription factor.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.