GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Zinc finger CCCH-type antiviral protein 1 (ADP-ribosyltransferase diphtheria toxin-like 13) (ARTD13) (Zinc finger CCCH domain-containing protein 2) (Zinc finger antiviral protein) (ZAP)

 ZCCHV_HUMAN             Reviewed;         902 AA.
Q7Z2W4; A4D1R2; A4D1S4; Q8IW57; Q8TAJ3; Q96N79; Q9H8R9; Q9P0Y7;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 3.
13-FEB-2019, entry version 157.
RecName: Full=Zinc finger CCCH-type antiviral protein 1;
AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 13 {ECO:0000303|PubMed:20106667};
Short=ARTD13 {ECO:0000303|PubMed:20106667};
AltName: Full=Inactive Poly [ADP-ribose] polymerase 13 {ECO:0000305};
Short=PARP13 {ECO:0000303|PubMed:25043379};
AltName: Full=Zinc finger CCCH domain-containing protein 2;
AltName: Full=Zinc finger antiviral protein;
Short=ZAP;
Name=ZC3HAV1 {ECO:0000312|HGNC:HGNC:23721}; Synonyms=ZC3HDC2;
ORFNames=PRO1677;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT
GLN-565.
TISSUE=Fetal liver;
Zhang C., Yu Y., Zhang S., Zhou G., Wei H., Bi J., Xu W., Zai Y.,
Feng F., Liu M., He F.;
"Functional prediction of the coding sequences of 5 new genes deduced
by analysis of cDNA clones from human fetal liver.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
VARIANTS LYS-485; GLN-565 AND GLU-701.
TISSUE=Kidney, and Ovarian carcinoma;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
GLU-701 AND ILE-851.
TISSUE=Endometrium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS GLU-701 AND ILE-851.
TISSUE=Brain, and Uterus;
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
FUNCTION.
PubMed=18225958; DOI=10.1371/journal.pgen.0040021;
Kerns J.A., Emerman M., Malik H.S.;
"Positive selection and increased antiviral activity associated with
the PARP-containing isoform of human zinc-finger antiviral protein.";
PLoS Genet. 4:E21-E21(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; THR-273; SER-275;
SER-284; SER-302; SER-378; SER-387 AND THR-393, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
REVIEW.
PubMed=18418085; DOI=10.4161/rna.5.2.6044;
Zhu Y., Gao G.;
"ZAP-mediated mRNA degradation.";
RNA Biol. 5:65-67(2008).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-284; SER-335;
SER-387 AND THR-393, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES,
RNA-BINDING, AND DOMAIN N-TERMINAL.
PubMed=20451500; DOI=10.1016/j.bbrc.2010.04.164;
Jeong M.S., Kim E.J., Jang S.B.;
"Expression and RNA-binding of human zinc-finger antiviral protein.";
Biochem. Biophys. Res. Commun. 396:696-702(2010).
[17]
SUBUNIT.
PubMed=20181706; DOI=10.1128/JVI.02018-09;
Law L.M., Albin O.R., Carroll J.W., Jones C.T., Rice C.M.,
Macdonald M.R.;
"Identification of a dominant negative inhibitor of human zinc finger
antiviral protein reveals a functional endogenous pool and critical
homotypic interactions.";
J. Virol. 84:4504-4512(2010).
[18]
INTERACTION WITH DHX30.
PubMed=21204022; DOI=10.1007/s13238-010-0117-8;
Ye P., Liu S., Zhu Y., Chen G., Gao G.;
"DEXH-Box protein DHX30 is required for optimal function of the zinc-
finger antiviral protein.";
Protein Cell 1:956-964(2010).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; SER-302; SER-335;
SER-378; THR-393 AND SER-492, PHOSPHORYLATION [LARGE SCALE ANALYSIS]
AT SER-572 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
NOMENCLATURE.
PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
"Toward a unified nomenclature for mammalian ADP-
ribosyltransferases.";
Trends Biochem. Sci. 35:208-219(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
REVIEW.
PubMed=21169998; DOI=10.1038/ni0111-11;
Liu H.M., Gale M. Jr.;
"ZAPS electrifies RIG-I signaling.";
Nat. Immunol. 12:11-12(2011).
[23]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH
DDX58/RIG-I.
PubMed=21102435; DOI=10.1038/ni.1963;
Hayakawa S., Shiratori S., Yamato H., Kameyama T., Kitatsuji C.,
Kashigi F., Goto S., Kameoka S., Fujikura D., Yamada T., Mizutani T.,
Kazumata M., Sato M., Tanaka J., Asaka M., Ohba Y., Miyazaki T.,
Imamura M., Takaoka A.;
"ZAPS is a potent stimulator of signaling mediated by the RNA helicase
RIG-I during antiviral responses.";
Nat. Immunol. 12:37-44(2011).
[24]
FUNCTION, AND INTERACTION WITH EXOSC3; EXOSC7; PARN; DCP2; DCP1A AND
XRN1.
PubMed=21876179; DOI=10.1073/pnas.1101676108;
Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L.,
Zheng Y.T., Gao G.;
"Zinc-finger antiviral protein inhibits HIV-1 infection by selectively
targeting multiply spliced viral mRNAs for degradation.";
Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[27]
FUNCTION.
PubMed=22720057; DOI=10.1371/journal.pone.0039159;
Wang X., Tu F., Zhu Y., Gao G.;
"Zinc-finger antiviral protein inhibits XMRV infection.";
PLoS ONE 7:E39159-E39159(2012).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; THR-273; SER-275;
SER-284; SER-302; SER-335; SER-355; SER-378; THR-393; SER-407;
SER-469; SER-492; SER-494; THR-554 AND SER-590, 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).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-284 AND
SER-492, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
LACK OF ADP-RIBOSYLTRANSFERASE ACTIVITY, AND NOMENCLATURE.
PubMed=25043379; DOI=10.1038/ncomms5426;
Vyas S., Matic I., Uchima L., Rood J., Zaja R., Hay R.T., Ahel I.,
Chang P.;
"Family-wide analysis of poly(ADP-ribose) polymerase activity.";
Nat. Commun. 5:4426-4426(2014).
[31]
X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 724-896, DOMAIN, AND
MUTAGENESIS OF HIS-810 AND ASN-830.
PubMed=25635049; DOI=10.1074/jbc.M114.630160;
Karlberg T., Klepsch M., Thorsell A.G., Andersson C.D., Linusson A.,
Schuler H.;
"Structural basis for lack of ADP-ribosyltransferase activity in
poly(ADP-ribose) polymerase-13/zinc finger antiviral protein.";
J. Biol. Chem. 290:7336-7344(2015).
-!- FUNCTION: Antiviral protein which inhibits the replication of
viruses by recruiting the cellular RNA degradation machineries to
degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE)
present in the target viral mRNA, recruits cellular poly(A)-
specific ribonuclease PARN to remove the poly(A) tail, and the 3'-
5' exoribonuclease complex exosome to degrade the RNA body from
the 3'-end. It also recruits the decapping complex DCP1-DCP2
through RNA helicase p72 (DDX17) to remove the cap structure of
the viral mRNA to initiate its degradation from the 5'-end. Its
target viruses belong to families which include retroviridae:
human immunodeficiency virus type 1 (HIV-1), moloney and murine
leukemia virus (MoMLV) and xenotropic MuLV-related virus (XMRV),
filoviridae: ebola virus (EBOV) and marburg virus (MARV),
togaviridae: sindbis virus (SINV) and Ross river virus (RRV).
Specifically targets the multiply spliced but not unspliced or
singly spliced HIV-1 mRNAs for degradation. Isoform 1 is a more
potent viral inhibitor than isoform 2. Isoform 2 acts as a
positive regulator of DDX58/RIG-I signaling resulting in
activation of the downstream effector IRF3 leading to the
expression of type I IFNs and IFN stimulated genes (ISGs).
{ECO:0000269|PubMed:18225958, ECO:0000269|PubMed:21102435,
ECO:0000269|PubMed:21876179, ECO:0000269|PubMed:22720057}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Temperature dependence:
Thermostable. {ECO:0000269|PubMed:20451500};
-!- SUBUNIT: Homodimer or homooligomer. Homooligomerization is
essential for its antiviral activity. Interacts with EXOSC5 (By
similarity). Interacts (via N-terminal domain) with DDX17 in an
RNA-independent manner (By similarity). Interacts with EXOSC3,
EXOSC7, DCP2 and DCP1A. Interacts with PARN in an RNA-independent
manner. Interacts with XRN1 in an RNA-dependent manner. Isoform 2
interacts (via zinc-fingers) with DDX58/RIG-I in an RNA-dependent
manner. Interacts (via N-terminal domain) with DHX30 (via N-
terminus) in an RNA-independent manner. {ECO:0000250,
ECO:0000269|PubMed:20181706, ECO:0000269|PubMed:21102435,
ECO:0000269|PubMed:21204022, ECO:0000269|PubMed:21876179}.
-!- INTERACTION:
O95786:DDX58; NbExp=4; IntAct=EBI-922559, EBI-995350;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm
{ECO:0000250|UniProtKB:Q8K3Y6}. Nucleus
{ECO:0000250|UniProtKB:Q8K3Y6}. Note=Localizes in the cytoplasm at
steady state, but shuttles between nucleus and cytoplasm in a
XPO1-dependent manner. {ECO:0000250|UniProtKB:Q8K3Y6}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:21102435}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=ZAPL;
IsoId=Q7Z2W4-1; Sequence=Displayed;
Name=2; Synonyms=ZAPS {ECO:0000303|PubMed:21102435};
IsoId=Q7Z2W4-2; Sequence=VSP_010269;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q7Z2W4-3; Sequence=VSP_010270, VSP_010271;
Note=No experimental confirmation available. Contains a
phosphoserine at position 572. {ECO:0000244|PubMed:20068231};
Name=4;
IsoId=Q7Z2W4-4; Sequence=VSP_010268;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q7Z2W4-5; Sequence=VSP_010268, VSP_010269;
Note=No experimental confirmation available.;
-!- INDUCTION: By type I interferon (IFN) and viruses. Isoform 2 is
up-regulated by 3'-PPP-RNA. {ECO:0000269|PubMed:21102435}.
-!- DOMAIN: The N-terminal domain is sufficient to bind to viral RNAs
and promote their degradation. The second and fourth zinc fingers
are involved in binding to specific viral RNAs (PubMed:20451500).
Contains a divergent PARP homology ADP-ribosyltransferase domain
which lacks the structural requirements for NAD[+] binding
(PubMed:25635049). It is therefore inactive (PubMed:25043379,
PubMed:25635049). {ECO:0000269|PubMed:20451500,
ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:25635049}.
-!- PTM: Phosphorylation at Ser-275 is essential for sequential
phosphorylation of Ser-271, Ser-267, Ser-263 and Ser-257 by GSK3-
beta. Phosphorylation by GSK3-beta enhances its antiviral activity
(By similarity). {ECO:0000250|UniProtKB:Q8K3Y6}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF138863; AAF61195.1; -; mRNA.
EMBL; AK055851; BAB71028.1; -; mRNA.
EMBL; AK023350; BAB14537.1; -; mRNA.
EMBL; BX571742; CAE11868.1; -; mRNA.
EMBL; CH236950; EAL24040.1; -; Genomic_DNA.
EMBL; CH236950; EAL24041.1; -; Genomic_DNA.
EMBL; BC025308; AAH25308.1; -; mRNA.
EMBL; BC027462; AAH27462.1; -; mRNA.
EMBL; BC033105; AAH33105.1; -; mRNA.
EMBL; BC040956; AAH40956.1; -; mRNA.
CCDS; CCDS55171.1; -. [Q7Z2W4-2]
CCDS; CCDS5851.1; -. [Q7Z2W4-1]
RefSeq; NP_064504.2; NM_020119.3. [Q7Z2W4-1]
RefSeq; NP_078901.3; NM_024625.3. [Q7Z2W4-2]
UniGene; Hs.133512; -.
PDB; 2X5Y; X-ray; 1.05 A; A=724-896.
PDB; 4X52; X-ray; 2.08 A; A/B/C/D=726-896.
PDBsum; 2X5Y; -.
PDBsum; 4X52; -.
ProteinModelPortal; Q7Z2W4; -.
SMR; Q7Z2W4; -.
BioGrid; 121203; 170.
DIP; DIP-37896N; -.
IntAct; Q7Z2W4; 44.
MINT; Q7Z2W4; -.
STRING; 9606.ENSP00000242351; -.
iPTMnet; Q7Z2W4; -.
PhosphoSitePlus; Q7Z2W4; -.
SwissPalm; Q7Z2W4; -.
BioMuta; ZC3HAV1; -.
DMDM; 223634727; -.
EPD; Q7Z2W4; -.
jPOST; Q7Z2W4; -.
MaxQB; Q7Z2W4; -.
PaxDb; Q7Z2W4; -.
PeptideAtlas; Q7Z2W4; -.
PRIDE; Q7Z2W4; -.
ProteomicsDB; 68971; -.
ProteomicsDB; 68972; -. [Q7Z2W4-2]
ProteomicsDB; 68973; -. [Q7Z2W4-3]
ProteomicsDB; 68974; -. [Q7Z2W4-4]
ProteomicsDB; 68975; -. [Q7Z2W4-5]
Ensembl; ENST00000242351; ENSP00000242351; ENSG00000105939. [Q7Z2W4-1]
Ensembl; ENST00000471652; ENSP00000419855; ENSG00000105939. [Q7Z2W4-2]
GeneID; 56829; -.
KEGG; hsa:56829; -.
UCSC; uc003vun.4; human. [Q7Z2W4-1]
CTD; 56829; -.
DisGeNET; 56829; -.
EuPathDB; HostDB:ENSG00000105939.12; -.
GeneCards; ZC3HAV1; -.
H-InvDB; HIX0007129; -.
HGNC; HGNC:23721; ZC3HAV1.
HPA; HPA047818; -.
HPA; HPA059096; -.
MIM; 607312; gene.
neXtProt; NX_Q7Z2W4; -.
OpenTargets; ENSG00000105939; -.
PharmGKB; PA134944289; -.
eggNOG; ENOG410IEI4; Eukaryota.
eggNOG; ENOG410ZFB8; LUCA.
GeneTree; ENSGT00940000162001; -.
HOVERGEN; HBG050384; -.
InParanoid; Q7Z2W4; -.
KO; K15259; -.
OrthoDB; 782733at2759; -.
PhylomeDB; Q7Z2W4; -.
TreeFam; TF338389; -.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
ChiTaRS; ZC3HAV1; human.
EvolutionaryTrace; Q7Z2W4; -.
GeneWiki; ZC3HAV1; -.
GenomeRNAi; 56829; -.
PMAP-CutDB; Q7Z2W4; -.
PRO; PR:Q7Z2W4; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000105939; Expressed in 216 organ(s), highest expression level in blood.
ExpressionAtlas; Q7Z2W4; baseline and differential.
Genevisible; Q7Z2W4; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0032727; P:positive regulation of interferon-alpha production; IDA:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:UniProtKB.
GO; GO:0061014; P:positive regulation of mRNA catabolic process; IDA:UniProtKB.
GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; IMP:UniProtKB.
GO; GO:0006471; P:protein ADP-ribosylation; IEA:GOC.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 3.30.720.50; -; 1.
InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR004170; WWE-dom.
InterPro; IPR037197; WWE_dom_sf.
InterPro; IPR000571; Znf_CCCH.
Pfam; PF00644; PARP; 1.
Pfam; PF02825; WWE; 1.
SUPFAM; SSF117839; SSF117839; 1.
PROSITE; PS51059; PARP_CATALYTIC; 1.
PROSITE; PS50918; WWE; 1.
PROSITE; PS50103; ZF_C3H1; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Antiviral defense;
Complete proteome; Cytoplasm; Immunity; Innate immunity;
Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
CHAIN 2 902 Zinc finger CCCH-type antiviral protein
1.
/FTId=PRO_0000211343.
DOMAIN 594 681 WWE. {ECO:0000255|PROSITE-
ProRule:PRU00248}.
DOMAIN 716 902 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
ZN_FING 73 86 C3H1-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
ZN_FING 88 110 C3H1-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
ZN_FING 150 172 C3H1-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
ZN_FING 169 193 C3H1-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
REGION 2 254 N-terminal domain.
REGION 224 254 Binding to EXOSC5. {ECO:0000250}.
MOTIF 69 76 Nuclear localization signal.
{ECO:0000250}.
MOTIF 285 292 Nuclear export signal. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
MOD_RES 257 257 Phosphoserine; by GSK3-beta.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 263 263 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q8K3Y6}.
MOD_RES 267 267 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q8K3Y6}.
MOD_RES 271 271 Phosphoserine; by GSK3-beta.
{ECO:0000244|PubMed:18669648}.
MOD_RES 273 273 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UPF5}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 355 355 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 378 378 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 387 387 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 393 393 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 407 407 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 494 494 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 554 554 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 590 590 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 539 Missing (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.1}.
/FTId=VSP_010268.
VAR_SEQ 491 624 DSLSDVTSTTSSRVDDHDSEEICLDHLCKGCPLNGSCSKVH
FHLPYRWQMLIGKTWTDFEHMETIEKGYCNPGIHLCSVGSY
TINFRVMSCDSFPIRRLSTPSSVTKPANSVFTTKWIWYWKN
ESGTWIQYGEE -> GKYKGKTLWASTFVHDIPNGSSQVVD
KTTDVEKTGATGFGLTMAVKAEKDMLCTGSQSLRNLVPTTP
GESTAPAQVSTLPQSPAALSSSNRAAVWGAQGQNCTQVPVS
SASELTRKTTGSAQCKSLKDKGASVS (in isoform
3). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_010270.
VAR_SEQ 625 902 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_010271.
VAR_SEQ 699 902 DHQPAKTSSVSLTATFRPQEDFCFLSSKKYKLSEIHHLHPE
YVRVSEHFKASMKNFKIEKIKKIENSELLDKFTWKKSQMKE
EGKLLFYATSRAYVESICSNNFDSFLHETHENKYGKGIYFA
KDAIYSHKNCPYDAKNVVMFVAQVLVGKFTEGNITYTSPPP
QFDSCVDTRSNPSVFVIFQKDQVYPQYVIEYTEDKACVIS
-> E (in isoform 2 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.1}.
/FTId=VSP_010269.
VARIANT 485 485 R -> K (in dbSNP:rs2236426).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_018454.
VARIANT 565 565 H -> Q (in dbSNP:rs2297241).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.1}.
/FTId=VAR_018455.
VARIANT 701 701 Q -> E (in dbSNP:rs2297236).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_054319.
VARIANT 851 851 T -> I (in dbSNP:rs3735007).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_018456.
MUTAGEN 810 810 H->N: No effect on the structural
inability to bind NAD(+); when associated
with Y-830.
{ECO:0000269|PubMed:25635049}.
MUTAGEN 830 830 N->Y: No effect on the structural
inability to bind NAD(+); when associated
with N-810.
{ECO:0000269|PubMed:25635049}.
CONFLICT 245 245 A -> T (in Ref. 3; CAE11868).
{ECO:0000305}.
STRAND 729 732 {ECO:0000244|PDB:2X5Y}.
HELIX 738 748 {ECO:0000244|PDB:2X5Y}.
STRAND 754 763 {ECO:0000244|PDB:2X5Y}.
HELIX 765 778 {ECO:0000244|PDB:2X5Y}.
STRAND 783 790 {ECO:0000244|PDB:2X5Y}.
HELIX 791 793 {ECO:0000244|PDB:2X5Y}.
HELIX 794 800 {ECO:0000244|PDB:2X5Y}.
HELIX 804 807 {ECO:0000244|PDB:2X5Y}.
STRAND 812 814 {ECO:0000244|PDB:2X5Y}.
STRAND 816 823 {ECO:0000244|PDB:2X5Y}.
HELIX 824 830 {ECO:0000244|PDB:2X5Y}.
HELIX 835 837 {ECO:0000244|PDB:2X5Y}.
STRAND 838 845 {ECO:0000244|PDB:2X5Y}.
STRAND 849 852 {ECO:0000244|PDB:2X5Y}.
STRAND 866 869 {ECO:0000244|PDB:2X5Y}.
STRAND 871 873 {ECO:0000244|PDB:2X5Y}.
STRAND 876 879 {ECO:0000244|PDB:2X5Y}.
HELIX 882 884 {ECO:0000244|PDB:2X5Y}.
STRAND 885 895 {ECO:0000244|PDB:2X5Y}.
SEQUENCE 902 AA; 101431 MW; 72AB311D23658E24 CRC64;
MADPEVCCFI TKILCAHGGR MALDALLQEI ALSEPQLCEV LQVAGPDRFV VLETGGEAGI
TRSVVATTRA RVCRRKYCQR PCDNLHLCKL NLLGRCNYSQ SERNLCKYSH EVLSEENFKV
LKNHELSGLN KEELAVLLLQ SDPFFMPEIC KSYKGEGRQQ ICNQQPPCSR LHICDHFTRG
NCRFPNCLRS HNLMDRKVLA IMREHGLNPD VVQNIQDICN SKHMQKNPPG PRAPSSHRRN
MAYRARSKSR DRFFQGSQEF LASASASAER SCTPSPDQIS HRASLEDAPV DDLTRKFTYL
GSQDRARPPS GSSKATDLGG TSQAGTSQRF LENGSQEDLL HGNPGSTYLA SNSTSAPNWK
SLTSWTNDQG ARRKTVFSPT LPAARSSLGS LQTPEAVTTR KGTGLLSSDY RIINGKSGTQ
DIQPGPLFNN NADGVATDIT STRSLNYKST SSGHREISSP RIQDAGPASR DVQATGRIAD
DADPRVALVN DSLSDVTSTT SSRVDDHDSE EICLDHLCKG CPLNGSCSKV HFHLPYRWQM
LIGKTWTDFE HMETIEKGYC NPGIHLCSVG SYTINFRVMS CDSFPIRRLS TPSSVTKPAN
SVFTTKWIWY WKNESGTWIQ YGEEKDKRKN SNVDSSYLES LYQSCPRGVV PFQAGSRNYE
LSFQGMIQTN IASKTQKDVI RRPTFVPQWY VQQMKRGPDH QPAKTSSVSL TATFRPQEDF
CFLSSKKYKL SEIHHLHPEY VRVSEHFKAS MKNFKIEKIK KIENSELLDK FTWKKSQMKE
EGKLLFYATS RAYVESICSN NFDSFLHETH ENKYGKGIYF AKDAIYSHKN CPYDAKNVVM
FVAQVLVGKF TEGNITYTSP PPQFDSCVDT RSNPSVFVIF QKDQVYPQYV IEYTEDKACV
IS


Related products :

Catalog number Product name Quantity
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
EIAAB46919 Rat,Rattus norvegicus,rZAP,ZAP,Zap,Zc3hav1,Zinc finger antiviral protein,Zinc finger CCCH-type antiviral protein 1
5839 Zinc finger CCCH-type antiviral protein 1 0.5 mg
5839 Zinc finger CCCH-type antiviral protein 1 0.1 mg
I3152 Zinc finger CCCH-type antiviral protein 1 (ZC3HAV1), Rat, ELISA Kit 96T
CSB-EL026369RA Rat Zinc finger CCCH-type antiviral protein 1(ZC3HAV1) ELISA kit 96T
E1837r Human ELISA Kit FOR Zinc finger CCCH-type antiviral protein 1-like 96T
CSB-EL026369HU Human Zinc finger CCCH-type antiviral protein 1(ZC3HAV1) ELISA kit 96T
I3154 Zinc finger CCCH-type antiviral protein 1-like (ZC3HAV1L), Mouse, ELISA Kit 96T
I3153 Zinc finger CCCH-type antiviral protein 1-like (ZC3HAV1L), Human, ELISA Kit 96T
I3150 Zinc finger CCCH-type antiviral protein 1 (ZC3HAV1), Human, ELISA Kit 96T
CSB-EL026370HU Human Zinc finger CCCH-type antiviral protein 1-like(ZC3HAV1L) ELISA kit 96T
I3151 Zinc finger CCCH-type antiviral protein 1 (ZC3HAV1), Mouse, ELISA Kit 96T
CSB-EL026369RA Rat Zinc finger CCCH-type antiviral protein 1(ZC3HAV1) ELISA kit SpeciesRat 96T
CSB-EL026370MO Mouse Zinc finger CCCH-type antiviral protein 1-like(ZC3HAV1L) ELISA kit 96T
EIAAB46917 Mouse,Mus musculus,Zc3hav1l,Zinc finger CCCH-type antiviral protein 1-like
EIAAB46920 Mouse,Mus musculus,Zc3hav1,Zinc finger CCCH-type antiviral protein 1
CSB-EL026369MO Mouse Zinc finger CCCH-type antiviral protein 1(ZC3HAV1) ELISA kit 96T
CSB-EL026369MO Mouse Zinc finger CCCH-type antiviral protein 1(ZC3HAV1) ELISA kit SpeciesMouse 96T
ZCCHV_RAT ELISA Kit FOR Zinc finger CCCH-type antiviral protein 1; organism: Rat; gene name: Zc3hav1 96T
CSB-EL026370HU Human Zinc finger CCCH-type antiviral protein 1-like(ZC3HAV1L) ELISA kit SpeciesHuman 96T
CSB-EL026369HU Human Zinc finger CCCH-type antiviral protein 1(ZC3HAV1) ELISA kit SpeciesHuman 96T
CSB-EL026370MO Mouse Zinc finger CCCH-type antiviral protein 1-like(ZC3HAV1L) ELISA kit SpeciesMouse 96T
EIAAB46916 C7orf39,Homo sapiens,Human,ZC3HAV1L,Zinc finger CCCH-type antiviral protein 1-like
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

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP2199: Seed Development
WP1689: Porphyrin and chlorophyll metabolism
WP2272: Pathogenic Escherichia coli infection
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation

Related Genes :
[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)
[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)
[Zc3hav1] Zinc finger CCCH-type antiviral protein 1 (ADP-ribosyltransferase diphtheria toxin-like 13) (ARTD13) (Inactive Poly [ADP-ribose] polymerase 13) (PARP13)
[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)
[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)
[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)
[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)
[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)
[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)
[Zc3h8 Fliz1 Zc3hdc8] Zinc finger CCCH domain-containing protein 8 (Fetal liver zinc finger protein 1)
[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)
[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)
[oma-1 moe-1 C09G9.6] CCCH-type zinc finger protein oma-1 (Maturation oocyte expansion protein 1) (Oocyte maturation defective protein 1)
[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)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (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)]
[ZKSCAN3 ZFP47 ZNF306 ZNF309 ZSCAN13] Zinc finger protein with KRAB and SCAN domains 3 (Zinc finger and SCAN domain-containing protein 13) (Zinc finger protein 306) (Zinc finger protein 309) (Zinc finger protein 47 homolog) (Zf47) (Zfp-47)
[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)
[Zbtb17 Zfp100 Znf151] Zinc finger and BTB domain-containing protein 17 (LP-1) (Polyomavirus late initiator promoter-binding protein) (Zinc finger protein 100) (Zfp-100) (Zinc finger protein 151) (Zinc finger protein Z13)
[ZC3H13 KIAA0853] Zinc finger CCCH domain-containing protein 13
[RCHY1 ARNIP CHIMP PIRH2 RNF199 ZNF363] RING finger and CHY zinc finger domain-containing protein 1 (EC 2.3.2.27) (Androgen receptor N-terminal-interacting protein) (CH-rich-interacting match with PLAG1) (E3 ubiquitin-protein ligase Pirh2) (RING finger protein 199) (RING-type E3 ubiquitin transferase RCHY1) (Zinc finger protein 363) (p53-induced RING-H2 protein) (hPirh2)
[ZBTB7B ZBTB15 ZFP67 ZNF857B] Zinc finger and BTB domain-containing protein 7B (Krueppel-related zinc finger protein cKrox) (hcKrox) (T-helper-inducing POZ/Krueppel-like factor) (Zinc finger and BTB domain-containing protein 15) (Zinc finger protein 67 homolog) (Zfp-67) (Zinc finger protein 857B) (Zinc finger protein Th-POK)
[ZBTB18 RP58 TAZ1 ZNF238] Zinc finger and BTB domain-containing protein 18 (58 kDa repressor protein) (Transcriptional repressor RP58) (Translin-associated zinc finger protein 1) (TAZ-1) (Zinc finger protein 238) (Zinc finger protein C2H2-171)
[Zrsr1 Sp2 Sp2-7 U2af1-rs1 U2af1l1] U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1 (CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 1) (SP2) (U2(RNU2) small nuclear RNA auxiliary factor 1-like 1)
[Zfand5 Za20d2 Zfp216 Znf216] AN1-type zinc finger protein 5 (Zinc finger A20 domain-containing protein 2) (Zinc finger protein 216)
[ZBTB17 MIZ1 ZNF151 ZNF60] Zinc finger and BTB domain-containing protein 17 (Myc-interacting zinc finger protein 1) (Miz-1) (Zinc finger protein 151) (Zinc finger protein 60)
[ZC3H8 ZC3HDC8] Zinc finger CCCH domain-containing protein 8
[ZBTB16 PLZF ZNF145] Zinc finger and BTB domain-containing protein 16 (Promyelocytic leukemia zinc finger protein) (Zinc finger protein 145) (Zinc finger protein PLZF)
[Zfp36l3] mRNA decay activator protein ZFP36L3 (Zinc finger protein 36, C3H1 type-like 3) (zinc finger protein 36-like 3)
[Znf423 Ebfaz Kiaa0760 Nur12 Oaz Zfp423] Zinc finger protein 423 (Early B-cell factor-associated zinc finger protein) (Olf1/EBF-associated zinc finger protein) (Smad- and Olf-interacting zinc finger protein)
[Zbtb7b Thpok Zfp67] Zinc finger and BTB domain-containing protein 7B (Krueppel-related zinc finger protein cKrox) (c-Krox) (T-helper-inducing POZ/Krueppel-like factor) (Zinc finger protein 67) (Zfp-67) (Zinc finger protein Th-POK)

Bibliography :
?>