euk:ZN473

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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

MyHits
UniProt

Description	RecName: Full=Zinc finger protein 473; AltName: Full=Zinc finger protein 100 homolog; Short=Zfp-100;
	query by protein blastp
MyHits synonyms	ZN473_HUMAN , Q8WTR7 , A8K8T7 , Q9ULS9 , Q9Y4Q7 , 959AFB7C3C2D5456
Legends: 1, VARIANT S -> G (in dbSNP:rs10419876); 2, VARIANT S -> G (in dbSNP:rs10419911); 3, VARIANT T -> M (in dbSNP:rs16981705); 4, VARIANT E -> G (in dbSNP:rs16981706); 5, VARIANT T -> I (in dbSNP:rs10424809); 6, VARIANT S -> A (in dbSNP:rs10426374); 7, CONFLICT P -> A (in Ref. 6). {ECO:0000305}; 8, CONFLICT V -> M (in Ref. 2; BAA86455). {ECO:0000305}; 9, KRAB. {ECO:0000255\|PROSITE- ProRule:PRU00119}; 10, ZN_FING C2H2-type 1. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 11, ZN_FING C2H2-type 2; degenerate. {ECO:0000255\|PROSITE-ProRule:PRU00042}; 12, ZN_FING C2H2-type 3. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 13, ZN_FING C2H2-type 4. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 14, ZN_FING C2H2-type 5. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 15, ZN_FING C2H2-type 6; degenerate. {ECO:0000255\|PROSITE-ProRule:PRU00042}; 16, ZN_FING C2H2-type 7. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 17, ZN_FING C2H2-type 8. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 18, ZN_FING C2H2-type 9. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 19, ZN_FING C2H2-type 10. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 20, ZN_FING C2H2-type 11. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 21, ZN_FING C2H2-type 12. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 22, ZN_FING C2H2-type 13. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 23, ZN_FING C2H2-type 14. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 24, ZN_FING C2H2-type 15. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 25, ZN_FING C2H2-type 16. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 26, ZN_FING C2H2-type 17. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 27, ZN_FING C2H2-type 18. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 28, ZN_FING C2H2-type 19. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 29, ZN_FING C2H2-type 20. {ECO:0000255\|PROSITE- ProRule:PRU00042}; 30, REGION Interaction with SLBP/pre-mRNA complex; 31, iprf:ZINC_FINGER_C2H2_2 [T]; 32, ismart:ZnF_C2H2 [T]; 33, ipat:ZINC_FINGER_C2H2_1 [T]; 34, iprf:KRAB [T]; 35, ipfam:KRAB [T]; 36, ismart:KRAB [T]; 37, STRAND {ECO:0000244\|PDB:2YTT}; 38, HELIX {ECO:0000244\|PDB:2YTT}; 39, STRAND {ECO:0000244\|PDB:2EOX}; 40, TURN {ECO:0000244\|PDB:2EOX}; 41, HELIX {ECO:0000244\|PDB:2EOX}; 42, STRAND {ECO:0000244\|PDB:2EMB}; 43, TURN {ECO:0000244\|PDB:2EMB}; 44, HELIX {ECO:0000244\|PDB:2EMB}; 45, STRAND {ECO:0000244\|PDB:2EOU}; 46, TURN {ECO:0000244\|PDB:2EOU}; 47, HELIX {ECO:0000244\|PDB:2EOU}; 48, STRAND {ECO:0000244\|PDB:2YTD}; 49, HELIX {ECO:0000244\|PDB:2YTD}; 50, TURN {ECO:0000244\|PDB:2YTE}; 51, HELIX {ECO:0000244\|PDB:2YTE}; 52, STRAND {ECO:0000244\|PDB:2EOY}; 53, HELIX {ECO:0000244\|PDB:2EOY}; 54, STRAND {ECO:0000244\|PDB:2EMC}; 55, HELIX {ECO:0000244\|PDB:2EMC}; 56, TURN {ECO:0000244\|PDB:2EMC}; 57, STRAND {ECO:0000244\|PDB:2YU5}; 58, HELIX {ECO:0000244\|PDB:2YU5}; 59, TURN {ECO:0000244\|PDB:2YRH}; 60, STRAND {ECO:0000244\|PDB:2YRH}; 61, HELIX {ECO:0000244\|PDB:2YRH}; 62, STRAND {ECO:0000244\|PDB:2EME}; 63, HELIX {ECO:0000244\|PDB:2EME}; 64, STRAND {ECO:0000244\|PDB:2YSV}; 65, HELIX {ECO:0000244\|PDB:2YSV}; 66, STRAND {ECO:0000244\|PDB:2YRJ}; 67, HELIX {ECO:0000244\|PDB:2YRJ}; 68, TURN {ECO:0000244\|PDB:2YRJ}; 69, STRAND {ECO:0000244\|PDB:2EOZ}; 70, TURN {ECO:0000244\|PDB:2EOZ}; 71, HELIX {ECO:0000244\|PDB:2EOZ}.
ID ZN473_HUMAN Reviewed; 871 AA. AC Q8WTR7; A8K8T7; Q9ULS9; Q9Y4Q7; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 10-MAY-2017, entry version 140. DE RecName: Full=Zinc finger protein 473; DE AltName: Full=Zinc finger protein 100 homolog; DE Short=Zfp-100; GN Name=ZNF473; Synonyms=KIAA1141, ZFP100; 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], FUNCTION, AND INTERACTION WITH RP SLBP/PRE-MRNA COMPLEX. RX PubMed=11782445; DOI=10.1101/gad.932302; RA Dominski Z., Erkmann J.A., Yang X., Sanchez R., Marzluff W.F.; RT "A novel zinc finger protein is associated with U7 snRNP and interacts RT with the stem-loop binding protein in the histone pre-mRNP to RT stimulate 3'-end processing."; RL Genes Dev. 16:58-71(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=10574461; DOI=10.1093/dnares/6.5.329; RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.; RT "Characterization of cDNA clones selected by the GeneMark analysis RT from size-fractionated cDNA libraries from human brain."; RL DNA Res. 6:329-336(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 486-871. RC TISSUE=Testis; 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 [7] RP INTERACTION WITH LSM11. RC TISSUE=Cervix carcinoma; RX PubMed=12975319; DOI=10.1101/gad.274403; RA Pillai R.S., Grimmler M., Meister G., Will C.L., Luehrmann R., RA Fischer U., Schuemperli D.; RT "Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN RT complex and the role of a new component, Lsm11, in histone RNA RT processing."; RL Genes Dev. 17:2321-2333(2003). RN [8] RP INTERACTION WITH LSM11. RX PubMed=15824063; DOI=10.1093/nar/gki516; RA Azzouz T.N., Gruber A., Schuemperli D.; RT "U7 snRNP-specific Lsm11 protein: dual binding contacts with the 100 RT kDa zinc finger processing factor (ZFP100) and a ZFP100-independent RT function in histone RNA 3'-end processing."; RL Nucleic Acids Res. 33:2106-2117(2005). RN [9] RP FUNCTION. RX PubMed=16914750; DOI=10.1128/MCB.00391-06; RA Wagner E.J., Marzluff W.F.; RT "ZFP100, a component of the active U7 snRNP limiting for histone pre- RT mRNA processing, is required for entry into S phase."; RL Mol. Cell. Biol. 26:6702-6712(2006). RN [10] RP FUNCTION, INTERACTION WITH LSM11, AND SUBCELLULAR LOCATION. RX PubMed=16714279; DOI=10.1261/rna.2606; RA Wagner E.J., Ospina J.K., Hu Y., Dundr M., Matera A.G., Marzluff W.F.; RT "Conserved zinc fingers mediate multiple functions of ZFP100, a RT U7snRNP associated protein."; RL RNA 12:1206-1218(2006). RN [11] RP STRUCTURE BY NMR OF 205-841. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the C2H2 type zinc finger region of human zinc RT finger protein 473."; RL Submitted (OCT-2007) to the PDB data bank. CC -!- FUNCTION: Involved in histone 3'-end pre-mRNA processing by CC associating with U7 snRNP and interacting with SLBP/pre-mRNA CC complex. Increases histone 3'-end pre-mRNA processing but has no CC effect on U7 snRNP levels, when overexpressed. Required for cell CC cycle progression from G1 to S phases. CC {ECO:0000269\|PubMed:11782445, ECO:0000269\|PubMed:16714279, CC ECO:0000269\|PubMed:16914750}. CC -!- SUBUNIT: Interacts with the SLBP/pre-mRNA complex but not with CC SLBP alone. Interacts with LSM11 in a U7 snRNP-dependent manner. CC {ECO:0000269\|PubMed:11782445, ECO:0000269\|PubMed:12975319, CC ECO:0000269\|PubMed:15824063, ECO:0000269\|PubMed:16714279}. CC -!- INTERACTION: CC Q8WTP8:AEN; NbExp=3; IntAct=EBI-751409, EBI-8637627; CC P49760:CLK2; NbExp=3; IntAct=EBI-751409, EBI-750020; CC Q6P158:DHX57; NbExp=3; IntAct=EBI-751409, EBI-1051531; CC Q9NWQ4:GPATCH2L; NbExp=3; IntAct=EBI-751409, EBI-5666657; CC P60410:KRTAP10-8; NbExp=5; IntAct=EBI-751409, EBI-10171774; CC P60411:KRTAP10-9; NbExp=3; IntAct=EBI-751409, EBI-10172052; CC Q8WWY3:PRPF31; NbExp=3; IntAct=EBI-751409, EBI-1567797; CC D3DU92:RNPS1; NbExp=3; IntAct=EBI-751409, EBI-10176640; CC Q8WV44:TRIM41; NbExp=3; IntAct=EBI-751409, EBI-725997; CC P15622-3:ZNF250; NbExp=3; IntAct=EBI-751409, EBI-10177272; CC Q3KQV3:ZNF792; NbExp=3; IntAct=EBI-751409, EBI-10240849; CC O43309:ZSCAN12; NbExp=3; IntAct=EBI-751409, EBI-1210440; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269\|PubMed:16714279}. CC Note=Stable component of Cajal bodies (CBs). Colocalizes with SMN, CC coilin and U7 snRNA. CC -!- DOMAIN: The C2H2-type zinc finger 2 to 6 are necessary and CC sufficient for discrete Cajal bodies localization. The C2H2-type CC zinc finger 5 to 10 are necessary and sufficient for interaction CC with LSM11. The C2H2-type zinc finger 2 to 8 are necessary for CC interaction with the SLBP/RNA complex in the histone pre-mRNAs. CC The C2H2-type zinc finger 2 to 10 confer activity in histone pre- CC mRNA processing. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA86455.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AF454744; AAL51029.1; -; mRNA. DR EMBL; AB032967; BAA86455.1; ALT_INIT; mRNA. DR EMBL; AK292452; BAF85141.1; -; mRNA. DR EMBL; CH471177; EAW52593.1; -; Genomic_DNA. DR EMBL; BC018612; AAH18612.1; -; mRNA. DR EMBL; AL080143; CAB45736.1; -; mRNA. DR CCDS; CCDS33077.1; -. DR PIR; T12527; T12527. DR RefSeq; NP_001006657.1; NM_001006656.3. DR RefSeq; NP_001295353.1; NM_001308424.2. DR RefSeq; NP_056243.1; NM_015428.3. DR UniGene; Hs.440553; -. DR PDB; 2EMB; NMR; -; A=342-372. DR PDB; 2EMC; NMR; -; A=641-673. DR PDB; 2EME; NMR; -; A=725-757. DR PDB; 2EOU; NMR; -; A=370-400. DR PDB; 2EOX; NMR; -; A=315-345. DR PDB; 2EOY; NMR; -; A=557-589. DR PDB; 2EOZ; NMR; -; A=809-841. DR PDB; 2YRH; NMR; -; A=699-729. DR PDB; 2YRJ; NMR; -; A=781-813. DR PDB; 2YSV; NMR; -; A=755-783. DR PDB; 2YTD; NMR; -; A=426-458. DR PDB; 2YTE; NMR; -; A=484-512. DR PDB; 2YTT; NMR; -; A=204-236. DR PDB; 2YU5; NMR; -; A=669-699. DR PDBsum; 2EMB; -. DR PDBsum; 2EMC; -. DR PDBsum; 2EME; -. DR PDBsum; 2EOU; -. DR PDBsum; 2EOX; -. DR PDBsum; 2EOY; -. DR PDBsum; 2EOZ; -. DR PDBsum; 2YRH; -. DR PDBsum; 2YRJ; -. DR PDBsum; 2YSV; -. DR PDBsum; 2YTD; -. DR PDBsum; 2YTE; -. DR PDBsum; 2YTT; -. DR PDBsum; 2YU5; -. DR ProteinModelPortal; Q8WTR7; -. DR SMR; Q8WTR7; -. DR BioGrid; 117398; 15. DR IntAct; Q8WTR7; 20. DR MINT; MINT-1441474; -. DR STRING; 9606.ENSP00000270617; -. DR iPTMnet; Q8WTR7; -. DR PhosphoSitePlus; Q8WTR7; -. DR BioMuta; ZNF473; -. DR DMDM; 51702187; -. DR EPD; Q8WTR7; -. DR PaxDb; Q8WTR7; -. DR PeptideAtlas; Q8WTR7; -. DR PRIDE; Q8WTR7; -. DR DNASU; 25888; -. DR Ensembl; ENST00000270617; ENSP00000270617; ENSG00000142528. DR Ensembl; ENST00000391821; ENSP00000375697; ENSG00000142528. DR Ensembl; ENST00000595661; ENSP00000472808; ENSG00000142528. DR GeneID; 25888; -. DR KEGG; hsa:25888; -. DR UCSC; uc002prm.4; human. DR CTD; 25888; -. DR DisGeNET; 25888; -. DR GeneCards; ZNF473; -. DR HGNC; HGNC:23239; ZNF473. DR HPA; HPA004191; -. DR HPA; HPA073309; -. DR neXtProt; NX_Q8WTR7; -. DR OpenTargets; ENSG00000142528; -. DR PharmGKB; PA134987987; -. DR eggNOG; KOG1721; Eukaryota. DR eggNOG; COG5048; LUCA. DR GeneTree; ENSGT00840000130048; -. DR HOGENOM; HOG000234617; -. DR HOVERGEN; HBG018163; -. DR InParanoid; Q8WTR7; -. DR KO; K09228; -. DR OMA; CAECKET; -. DR OrthoDB; EOG091G02KC; -. DR PhylomeDB; Q8WTR7; -. DR TreeFam; TF350932; -. DR Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region. DR Reactome; R-HSA-111367; SLBP independent Processing of Histone Pre-mRNAs. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR Reactome; R-HSA-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs. DR EvolutionaryTrace; Q8WTR7; -. DR GeneWiki; ZNF473; -. DR GenomeRNAi; 25888; -. DR PRO; PR:Q8WTR7; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000142528; -. DR CleanEx; HS_ZNF473; -. DR ExpressionAtlas; Q8WTR7; baseline and differential. DR Genevisible; Q8WTR7; HS. DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008334; P:histone mRNA metabolic process; TAS:Reactome. DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome. DR CDD; cd07765; KRAB_A-box; 1. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR001909; KRAB. DR InterPro; IPR013087; Znf_C2H2_type. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF01352; KRAB; 1. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 20. DR SUPFAM; SSF109640; SSF109640; 1. DR SUPFAM; SSF57667; SSF57667; 11. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 18. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 20. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA-binding; Metal-binding; Nucleus; KW Polymorphism; Reference proteome; Repeat; Zinc; Zinc-finger. FT CHAIN 1 871 Zinc finger protein 473. FT /FTId=PRO_0000047604. FT DOMAIN 6 75 KRAB. {ECO:0000255\|PROSITE- FT ProRule:PRU00119}. FT ZN_FING 209 231 C2H2-type 1. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 265 286 C2H2-type 2; degenerate. FT {ECO:0000255\|PROSITE-ProRule:PRU00042}. FT ZN_FING 320 342 C2H2-type 3. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 347 369 C2H2-type 4. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 375 397 C2H2-type 5. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 403 425 C2H2-type 6; degenerate. FT {ECO:0000255\|PROSITE-ProRule:PRU00042}. FT ZN_FING 431 453 C2H2-type 7. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 459 481 C2H2-type 8. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 487 509 C2H2-type 9. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 515 537 C2H2-type 10. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 562 584 C2H2-type 11. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 591 613 C2H2-type 12. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 646 668 C2H2-type 13. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 674 696 C2H2-type 14. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 702 724 C2H2-type 15. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 730 752 C2H2-type 16. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 758 780 C2H2-type 17. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 786 808 C2H2-type 18. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 814 836 C2H2-type 19. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 842 864 C2H2-type 20. {ECO:0000255\|PROSITE- FT ProRule:PRU00042}. FT REGION 312 552 Interaction with SLBP/pre-mRNA complex. FT VARIANT 59 59 S -> G (in dbSNP:rs10419876). FT /FTId=VAR_052839. FT VARIANT 74 74 S -> G (in dbSNP:rs10419911). FT /FTId=VAR_052840. FT VARIANT 164 164 T -> M (in dbSNP:rs16981705). FT /FTId=VAR_052841. FT VARIANT 309 309 E -> G (in dbSNP:rs16981706). FT /FTId=VAR_052842. FT VARIANT 654 654 T -> I (in dbSNP:rs10424809). FT /FTId=VAR_052843. FT VARIANT 662 662 S -> A (in dbSNP:rs10426374). FT /FTId=VAR_052844. FT CONFLICT 486 486 P -> A (in Ref. 6). {ECO:0000305}. FT CONFLICT 588 588 V -> M (in Ref. 2; BAA86455). FT {ECO:0000305}. FT STRAND 212 214 {ECO:0000244\|PDB:2YTT}. FT HELIX 221 228 {ECO:0000244\|PDB:2YTT}. FT HELIX 230 233 {ECO:0000244\|PDB:2YTT}. FT STRAND 320 322 {ECO:0000244\|PDB:2EOX}. FT TURN 323 326 {ECO:0000244\|PDB:2EOX}. FT STRAND 327 332 {ECO:0000244\|PDB:2EOX}. FT HELIX 333 336 {ECO:0000244\|PDB:2EOX}. FT HELIX 339 342 {ECO:0000244\|PDB:2EOX}. FT STRAND 345 348 {ECO:0000244\|PDB:2EMB}. FT TURN 350 352 {ECO:0000244\|PDB:2EMB}. FT STRAND 355 357 {ECO:0000244\|PDB:2EMB}. FT HELIX 359 365 {ECO:0000244\|PDB:2EMB}. FT HELIX 366 369 {ECO:0000244\|PDB:2EMB}. FT STRAND 370 372 {ECO:0000244\|PDB:2EOU}. FT TURN 378 380 {ECO:0000244\|PDB:2EOU}. FT HELIX 387 397 {ECO:0000244\|PDB:2EOU}. FT STRAND 430 432 {ECO:0000244\|PDB:2YTD}. FT STRAND 434 436 {ECO:0000244\|PDB:2YTD}. FT STRAND 439 442 {ECO:0000244\|PDB:2YTD}. FT HELIX 443 453 {ECO:0000244\|PDB:2YTD}. FT TURN 490 492 {ECO:0000244\|PDB:2YTE}. FT HELIX 499 508 {ECO:0000244\|PDB:2YTE}. FT STRAND 565 567 {ECO:0000244\|PDB:2EOY}. FT STRAND 570 574 {ECO:0000244\|PDB:2EOY}. FT HELIX 575 581 {ECO:0000244\|PDB:2EOY}. FT STRAND 645 647 {ECO:0000244\|PDB:2EMC}. FT STRAND 649 651 {ECO:0000244\|PDB:2EMC}. FT STRAND 654 657 {ECO:0000244\|PDB:2EMC}. FT HELIX 658 665 {ECO:0000244\|PDB:2EMC}. FT TURN 666 670 {ECO:0000244\|PDB:2EMC}. FT STRAND 673 675 {ECO:0000244\|PDB:2YU5}. FT STRAND 677 680 {ECO:0000244\|PDB:2YU5}. FT STRAND 682 686 {ECO:0000244\|PDB:2YU5}. FT HELIX 687 695 {ECO:0000244\|PDB:2YU5}. FT TURN 705 707 {ECO:0000244\|PDB:2YRH}. FT STRAND 710 713 {ECO:0000244\|PDB:2YRH}. FT HELIX 714 721 {ECO:0000244\|PDB:2YRH}. FT TURN 722 724 {ECO:0000244\|PDB:2YRH}. FT STRAND 729 731 {ECO:0000244\|PDB:2EME}. FT STRAND 733 735 {ECO:0000244\|PDB:2EME}. FT STRAND 738 741 {ECO:0000244\|PDB:2EME}. FT HELIX 742 749 {ECO:0000244\|PDB:2EME}. FT HELIX 750 752 {ECO:0000244\|PDB:2EME}. FT STRAND 761 763 {ECO:0000244\|PDB:2YSV}. FT STRAND 768 771 {ECO:0000244\|PDB:2YSV}. FT HELIX 772 778 {ECO:0000244\|PDB:2YSV}. FT STRAND 789 791 {ECO:0000244\|PDB:2YRJ}. FT STRAND 794 797 {ECO:0000244\|PDB:2YRJ}. FT HELIX 798 805 {ECO:0000244\|PDB:2YRJ}. FT TURN 806 808 {ECO:0000244\|PDB:2YRJ}. FT STRAND 813 816 {ECO:0000244\|PDB:2EOZ}. FT TURN 817 820 {ECO:0000244\|PDB:2EOZ}. FT STRAND 821 825 {ECO:0000244\|PDB:2EOZ}. FT HELIX 826 836 {ECO:0000244\|PDB:2EOZ}. CC -------------------------------------------------------------------------- CC The following FT lines are automated annotations from the MyHits database. CC -------------------------------------------------------------------------- FT MYHIT 674 701 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 591 618 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 487 514 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 758 785 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 730 752 ismart:ZnF_C2H2 [T] FT MYHIT 816 836 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 6 75 iprf:KRAB [T] FT MYHIT 760 780 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 209 231 ismart:ZnF_C2H2 [T] FT MYHIT 320 342 ismart:ZnF_C2H2 [T] FT MYHIT 403 430 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 403 425 ismart:ZnF_C2H2 [T] FT MYHIT 702 724 ismart:ZnF_C2H2 [T] FT MYHIT 564 584 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 347 374 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 265 286 ismart:ZnF_C2H2 [T] FT MYHIT 375 397 ismart:ZnF_C2H2 [T] FT MYHIT 349 369 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 515 542 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 788 808 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 489 509 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 842 864 ismart:ZnF_C2H2 [T] FT MYHIT 377 397 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 433 453 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 322 342 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 459 486 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 646 673 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 461 481 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 562 584 ismart:ZnF_C2H2 [T] FT MYHIT 844 864 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 730 757 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 211 231 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 786 813 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 786 808 ismart:ZnF_C2H2 [T] FT MYHIT 591 613 ismart:ZnF_C2H2 [T] FT MYHIT 842 869 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 347 369 ismart:ZnF_C2H2 [T] FT MYHIT 674 696 ismart:ZnF_C2H2 [T] FT MYHIT 814 841 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 676 696 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 6 46 ipfam:KRAB [T] FT MYHIT 704 724 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 265 291 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 320 347 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 814 836 ismart:ZnF_C2H2 [T] FT MYHIT 758 780 ismart:ZnF_C2H2 [T] FT MYHIT 648 668 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 646 668 ismart:ZnF_C2H2 [T] FT MYHIT 6 64 ismart:KRAB [T] FT MYHIT 209 236 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 431 458 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 487 509 ismart:ZnF_C2H2 [T] FT MYHIT 562 585 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 459 481 ismart:ZnF_C2H2 [T] FT MYHIT 431 453 ismart:ZnF_C2H2 [T] FT MYHIT 375 402 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 732 752 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 517 537 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 702 729 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 593 613 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 515 537 ismart:ZnF_C2H2 [T] SQ SEQUENCE 871 AA; 100182 MW; 959AFB7C3C2D5456 CRC64; MAEEFVTLKD VGMDFTLGDW EQLGLEQGDT FWDTALDNCQ DLFLLDPPRP NLTSHPDGSE DLEPLAGGSP EATSPDVTET KNSPLMEDFF EEGFSQEIIE MLSKDGFWNS NFGEACIEDT WLDSLLGDPE SLLRSDIATN GESPTECKSH ELKRGLSPVS TVSTGEDSMV HNVSEKTLTP AKSKEYRGEF FSYSDHSQQD SVQEGEKPYQ CSECGKSFSG SYRLTQHWIT HTREKPTVHQ ECEQGFDRNA SLSVYPKTHT GYKFYVCNEY GTTFSQSTYL WHQKTHTGEK PCKSQDSDHP PSHDTQPGEH QKTHTDSKSY NCNECGKAFT RIFHLTRHQK IHTRKRYECS KCQATFNLRK HLIQHQKTHA AKTTSECQEC GKIFRHSSLL IEHQALHAGE EPYKCNERGK SFRHNSTLKI HQRVHSGEKP YKCSECGKAF HRHTHLNEHR RIHTGYRPHK CQECVRSFSR PSHLMRHQAI HTAEKPYSCA ECKETFSDNN RLVQHQKMHT VKTPYECQEC GERFICGSTL KCHESVHARE KQGFFVSGKI LDQNPEQKEK CFKCNKCEKT FSCSKYLTQH ERIHTRGVKP FECDQCGKAF GQSTRLIHHQ RIHSRVRLYK WGEQGKAISS ASLIKLQSFH TKEHPFKCNE CGKTFSHSAH LSKHQLIHAG ENPFKCSKCD RVFTQRNYLV QHERTHARKK PLVCNECGKT FRQSSCLSKH QRIHSGEKPY VCDYCGKAFG LSAELVRHQR IHTGEKPYVC QECGKAFTQS SCLSIHRRVH TGEKPYRCGE CGKAFAQKAN LTQHQRIHTG EKPYSCNVCG KAFVLSAHLN QHLRVHTQET LYQCQRCQKA FRCHSSLSRH QRVHNKQQYC L //

Entry euk:ZN473_HUMAN