Full text data of ZNF346
ZNF346
(JAZ)
[Confidence: low (only semi-automatic identification from reviews)]
Zinc finger protein 346 (Just another zinc finger protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Zinc finger protein 346 (Just another zinc finger protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UL40
ID ZN346_HUMAN Reviewed; 294 AA.
AC Q9UL40; Q68CV9; Q6ZMW1;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Zinc finger protein 346;
DE AltName: Full=Just another zinc finger protein;
GN Name=ZNF346; Synonyms=JAZ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=10488071; DOI=10.1074/jbc.274.39.27399;
RA Yang M., May W.S., Ito T.;
RT "JAZ requires the double-stranded RNA-binding zinc finger motifs for
RT nuclear localization.";
RL J. Biol. Chem. 274:27399-27406(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN;
RP ILF3 AND DOUBLE-STRANDED RNA, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH XPO5 AND ILF3.
RX PubMed=15254228; DOI=10.1128/MCB.24.15.6608-6619.2004;
RA Chen T., Brownawell A.M., Macara I.G.;
RT "Nucleocytoplasmic shuttling of JAZ, a new cargo protein for exportin-
RT 5.";
RL Mol. Cell. Biol. 24:6608-6619(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Binds to dsRNA and DNA (By similarity).
CC -!- SUBUNIT: Forms a heteromeric complex with XPO5 and ILF3. Found in
CC a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and double-
CC stranded RNA. Interacts with XPO5. Interacts with ILF3 in an RNA-
CC independent manner.
CC -!- INTERACTION:
CC P19525:EIF2AK2; NbExp=2; IntAct=EBI-2462313, EBI-640775;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Note=Nuclear
CC at steady state, primarily in the nucleolus. Shuttles between the
CC nucleus and cytoplasm when associated with XPO5.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UL40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UL40-2; Sequence=VSP_015971;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The zinc-finger domains are required for binding to dsRNA,
CC and also for nuclear localization (By similarity).
CC -!- SIMILARITY: Contains 4 matrin-type zinc fingers.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF083340; AAD52018.1; -; mRNA.
DR EMBL; AK131469; BAD18614.1; -; mRNA.
DR EMBL; CR749692; CAH18475.1; -; mRNA.
DR EMBL; BC007775; AAH07775.1; -; mRNA.
DR RefSeq; NP_036411.1; NM_012279.2.
DR RefSeq; XP_005265918.1; XM_005265861.1.
DR UniGene; Hs.484259; -.
DR ProteinModelPortal; Q9UL40; -.
DR SMR; Q9UL40; 53-167.
DR IntAct; Q9UL40; 6.
DR STRING; 9606.ENSP00000350869; -.
DR DMDM; 74735051; -.
DR PaxDb; Q9UL40; -.
DR PRIDE; Q9UL40; -.
DR DNASU; 23567; -.
DR Ensembl; ENST00000261948; ENSP00000261948; ENSG00000113761.
DR Ensembl; ENST00000358149; ENSP00000350869; ENSG00000113761.
DR Ensembl; ENST00000503039; ENSP00000424495; ENSG00000113761.
DR GeneID; 23567; -.
DR KEGG; hsa:23567; -.
DR UCSC; uc003mfi.3; human.
DR CTD; 23567; -.
DR GeneCards; GC05P176382; -.
DR HGNC; HGNC:16403; ZNF346.
DR HPA; HPA018485; -.
DR MIM; 605308; gene.
DR neXtProt; NX_Q9UL40; -.
DR PharmGKB; PA134898181; -.
DR eggNOG; NOG85918; -.
DR HOGENOM; HOG000008682; -.
DR HOVERGEN; HBG061007; -.
DR OMA; EEVEHMI; -.
DR PhylomeDB; Q9UL40; -.
DR ChiTaRS; ZNF346; human.
DR GeneWiki; ZNF346; -.
DR GenomeRNAi; 23567; -.
DR NextBio; 46164; -.
DR PRO; PR:Q9UL40; -.
DR ArrayExpress; Q9UL40; -.
DR Bgee; Q9UL40; -.
DR CleanEx; HS_ZNF346; -.
DR Genevestigator; Q9UL40; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR InterPro; IPR003604; Znf_U1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SMART; SM00451; ZnF_U1; 4.
DR PROSITE; PS50171; ZF_MATRIN; FALSE_NEG.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Metal-binding; Nucleus; Reference proteome; Repeat; RNA-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1 294 Zinc finger protein 346.
FT /FTId=PRO_0000191809.
FT ZN_FING 70 104 Matrin-type 1.
FT ZN_FING 131 165 Matrin-type 2.
FT ZN_FING 182 216 Matrin-type 3.
FT ZN_FING 236 270 Matrin-type 4.
FT METAL 75 75 Zinc 1 (By similarity).
FT METAL 78 78 Zinc 1 (By similarity).
FT METAL 91 91 Zinc 1; via tele nitrogen (By
FT similarity).
FT METAL 97 97 Zinc 1; via pros nitrogen (By
FT similarity).
FT METAL 136 136 Zinc 2 (By similarity).
FT METAL 139 139 Zinc 2 (By similarity).
FT METAL 152 152 Zinc 2; via tele nitrogen (By
FT similarity).
FT METAL 158 158 Zinc 2; via pros nitrogen (By
FT similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 58 58 E -> EAQFFPHSRTVIPILVLSETYSLCHP (in
FT isoform 2).
FT /FTId=VSP_015971.
FT CONFLICT 152 152 H -> Y (in Ref. 3; CAH18475).
SQ SEQUENCE 294 AA; 32933 MW; 095F02E19FBCFBE0 CRC64;
MEYPAPATVQ AADGGAAGPY SSSELLEGQE PDGVRFDRER ARRLWEAVSG AQPVGREEVE
HMIQKNQCLF TNTQCKVCCA LLISESQKLA HYQSKKHANK VKRYLAIHGM ETLKGETKKL
DSDQKSSRSK DKNQCCPICN MTFSSPVVAQ SHYLGKTHAK NLKLKQQSTK VEALHQNREM
IDPDKFCSLC HATFNDPVMA QQHYVGKKHR KQETKLKLMA RYGRLADPAV TDFPAGKGYP
CKTCKIVLNS IEQYQAHVSG FKHKNQSPKT VASSLGQIPM QRQPIQKDST TLED
//
ID ZN346_HUMAN Reviewed; 294 AA.
AC Q9UL40; Q68CV9; Q6ZMW1;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Zinc finger protein 346;
DE AltName: Full=Just another zinc finger protein;
GN Name=ZNF346; Synonyms=JAZ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=10488071; DOI=10.1074/jbc.274.39.27399;
RA Yang M., May W.S., Ito T.;
RT "JAZ requires the double-stranded RNA-binding zinc finger motifs for
RT nuclear localization.";
RL J. Biol. Chem. 274:27399-27406(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN;
RP ILF3 AND DOUBLE-STRANDED RNA, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH XPO5 AND ILF3.
RX PubMed=15254228; DOI=10.1128/MCB.24.15.6608-6619.2004;
RA Chen T., Brownawell A.M., Macara I.G.;
RT "Nucleocytoplasmic shuttling of JAZ, a new cargo protein for exportin-
RT 5.";
RL Mol. Cell. Biol. 24:6608-6619(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Binds to dsRNA and DNA (By similarity).
CC -!- SUBUNIT: Forms a heteromeric complex with XPO5 and ILF3. Found in
CC a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and double-
CC stranded RNA. Interacts with XPO5. Interacts with ILF3 in an RNA-
CC independent manner.
CC -!- INTERACTION:
CC P19525:EIF2AK2; NbExp=2; IntAct=EBI-2462313, EBI-640775;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Note=Nuclear
CC at steady state, primarily in the nucleolus. Shuttles between the
CC nucleus and cytoplasm when associated with XPO5.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UL40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UL40-2; Sequence=VSP_015971;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The zinc-finger domains are required for binding to dsRNA,
CC and also for nuclear localization (By similarity).
CC -!- SIMILARITY: Contains 4 matrin-type zinc fingers.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF083340; AAD52018.1; -; mRNA.
DR EMBL; AK131469; BAD18614.1; -; mRNA.
DR EMBL; CR749692; CAH18475.1; -; mRNA.
DR EMBL; BC007775; AAH07775.1; -; mRNA.
DR RefSeq; NP_036411.1; NM_012279.2.
DR RefSeq; XP_005265918.1; XM_005265861.1.
DR UniGene; Hs.484259; -.
DR ProteinModelPortal; Q9UL40; -.
DR SMR; Q9UL40; 53-167.
DR IntAct; Q9UL40; 6.
DR STRING; 9606.ENSP00000350869; -.
DR DMDM; 74735051; -.
DR PaxDb; Q9UL40; -.
DR PRIDE; Q9UL40; -.
DR DNASU; 23567; -.
DR Ensembl; ENST00000261948; ENSP00000261948; ENSG00000113761.
DR Ensembl; ENST00000358149; ENSP00000350869; ENSG00000113761.
DR Ensembl; ENST00000503039; ENSP00000424495; ENSG00000113761.
DR GeneID; 23567; -.
DR KEGG; hsa:23567; -.
DR UCSC; uc003mfi.3; human.
DR CTD; 23567; -.
DR GeneCards; GC05P176382; -.
DR HGNC; HGNC:16403; ZNF346.
DR HPA; HPA018485; -.
DR MIM; 605308; gene.
DR neXtProt; NX_Q9UL40; -.
DR PharmGKB; PA134898181; -.
DR eggNOG; NOG85918; -.
DR HOGENOM; HOG000008682; -.
DR HOVERGEN; HBG061007; -.
DR OMA; EEVEHMI; -.
DR PhylomeDB; Q9UL40; -.
DR ChiTaRS; ZNF346; human.
DR GeneWiki; ZNF346; -.
DR GenomeRNAi; 23567; -.
DR NextBio; 46164; -.
DR PRO; PR:Q9UL40; -.
DR ArrayExpress; Q9UL40; -.
DR Bgee; Q9UL40; -.
DR CleanEx; HS_ZNF346; -.
DR Genevestigator; Q9UL40; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR InterPro; IPR003604; Znf_U1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SMART; SM00451; ZnF_U1; 4.
DR PROSITE; PS50171; ZF_MATRIN; FALSE_NEG.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Metal-binding; Nucleus; Reference proteome; Repeat; RNA-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1 294 Zinc finger protein 346.
FT /FTId=PRO_0000191809.
FT ZN_FING 70 104 Matrin-type 1.
FT ZN_FING 131 165 Matrin-type 2.
FT ZN_FING 182 216 Matrin-type 3.
FT ZN_FING 236 270 Matrin-type 4.
FT METAL 75 75 Zinc 1 (By similarity).
FT METAL 78 78 Zinc 1 (By similarity).
FT METAL 91 91 Zinc 1; via tele nitrogen (By
FT similarity).
FT METAL 97 97 Zinc 1; via pros nitrogen (By
FT similarity).
FT METAL 136 136 Zinc 2 (By similarity).
FT METAL 139 139 Zinc 2 (By similarity).
FT METAL 152 152 Zinc 2; via tele nitrogen (By
FT similarity).
FT METAL 158 158 Zinc 2; via pros nitrogen (By
FT similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 58 58 E -> EAQFFPHSRTVIPILVLSETYSLCHP (in
FT isoform 2).
FT /FTId=VSP_015971.
FT CONFLICT 152 152 H -> Y (in Ref. 3; CAH18475).
SQ SEQUENCE 294 AA; 32933 MW; 095F02E19FBCFBE0 CRC64;
MEYPAPATVQ AADGGAAGPY SSSELLEGQE PDGVRFDRER ARRLWEAVSG AQPVGREEVE
HMIQKNQCLF TNTQCKVCCA LLISESQKLA HYQSKKHANK VKRYLAIHGM ETLKGETKKL
DSDQKSSRSK DKNQCCPICN MTFSSPVVAQ SHYLGKTHAK NLKLKQQSTK VEALHQNREM
IDPDKFCSLC HATFNDPVMA QQHYVGKKHR KQETKLKLMA RYGRLADPAV TDFPAGKGYP
CKTCKIVLNS IEQYQAHVSG FKHKNQSPKT VASSLGQIPM QRQPIQKDST TLED
//
MIM
605308
*RECORD*
*FIELD* NO
605308
*FIELD* TI
*605308 ZINC FINGER PROTEIN 346; ZNF346
;;DOUBLE-STRANDED RNA-BINDING ZINC FINGER PROTEIN;;
read moreJUST ANOTHER ZINC FINGER PROTEIN; JAZ
*FIELD* TX
CLONING
Double-stranded (ds) RNA binding is frequently mediated by a 65-amino
acid motif, while other nuclear localization signals are required for
proteins to move selectively from the cytoplasm across the nuclear
envelope and into the nucleus. Using a yeast 2-hybrid screen of a mouse
NFS/N1.H7 cDNA library with dsRNA-dependent protein kinase PKR (176871)
as bait, followed by searching an EST database and 5-prime RACE of a
human placental library, Yang et al. (1999) obtained a cDNA encoding JAZ
(just another zinc finger protein). Sequence analysis predicted that the
294-amino acid JAZ protein, which is 89% homologous to the mouse
sequence, contains 4 homologous C2H2-type zinc finger domains that are
connected by unusually long helix-loop linker sequences beginning with
basic residues. Northern blot analysis of multiple mouse tissues
detected ubiquitous expression of a 3.6-kb transcript. Gel shift
analysis showed that JAZ binds preferentially to dsRNA or RNA/DNA
hybrids rather than dsDNA. Western blot analysis determined that JAZ is
expressed as a 36-kD nuclear protein. Immunofluorescence microscopy
demonstrated that JAZ localizes to the nucleus, primarily to the
nucleolus. Immunoblot and immunofluorescence analysis indicated that the
zinc finger domains and the linker length are both required for binding
to dsRNA and for nuclear localization. Exogenous overexpression of JAZ
induced apoptosis, which also required intact zinc fingers.
*FIELD* RF
1. Yang, M.; May, W. S.; Ito, T.: JAZ requires the double-stranded
RNA-binding zinc finger motifs for nuclear localization. J. Biol.
Chem. 274: 27399-27406, 1999.
*FIELD* CD
Paul J. Converse: 9/29/2000
*FIELD* ED
alopez: 07/06/2010
mgross: 9/29/2000
*RECORD*
*FIELD* NO
605308
*FIELD* TI
*605308 ZINC FINGER PROTEIN 346; ZNF346
;;DOUBLE-STRANDED RNA-BINDING ZINC FINGER PROTEIN;;
read moreJUST ANOTHER ZINC FINGER PROTEIN; JAZ
*FIELD* TX
CLONING
Double-stranded (ds) RNA binding is frequently mediated by a 65-amino
acid motif, while other nuclear localization signals are required for
proteins to move selectively from the cytoplasm across the nuclear
envelope and into the nucleus. Using a yeast 2-hybrid screen of a mouse
NFS/N1.H7 cDNA library with dsRNA-dependent protein kinase PKR (176871)
as bait, followed by searching an EST database and 5-prime RACE of a
human placental library, Yang et al. (1999) obtained a cDNA encoding JAZ
(just another zinc finger protein). Sequence analysis predicted that the
294-amino acid JAZ protein, which is 89% homologous to the mouse
sequence, contains 4 homologous C2H2-type zinc finger domains that are
connected by unusually long helix-loop linker sequences beginning with
basic residues. Northern blot analysis of multiple mouse tissues
detected ubiquitous expression of a 3.6-kb transcript. Gel shift
analysis showed that JAZ binds preferentially to dsRNA or RNA/DNA
hybrids rather than dsDNA. Western blot analysis determined that JAZ is
expressed as a 36-kD nuclear protein. Immunofluorescence microscopy
demonstrated that JAZ localizes to the nucleus, primarily to the
nucleolus. Immunoblot and immunofluorescence analysis indicated that the
zinc finger domains and the linker length are both required for binding
to dsRNA and for nuclear localization. Exogenous overexpression of JAZ
induced apoptosis, which also required intact zinc fingers.
*FIELD* RF
1. Yang, M.; May, W. S.; Ito, T.: JAZ requires the double-stranded
RNA-binding zinc finger motifs for nuclear localization. J. Biol.
Chem. 274: 27399-27406, 1999.
*FIELD* CD
Paul J. Converse: 9/29/2000
*FIELD* ED
alopez: 07/06/2010
mgross: 9/29/2000