MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
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
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
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
| Description | RecName: Full=Zinc finger protein 93; AltName: Full=Zinc finger protein 505; AltName: Full=Zinc finger protein HTF34; |
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| MyHits synonyms | ZNF93_HUMAN , P35789 , A6NMY2 , B9EGT2 , Q8N8Q4 , Q9H9X5 , Q9Y2N8 , 722A49B2EA82801A |
 Legends: 1, VARIANT D -> Y (in dbSNP:rs12151060). {ECO:0000269|PubMed:14702039}; 2, CONFLICT S -> SGP (in Ref. 5; AAA83548). {ECO:0000305}; 3, CONFLICT Q -> H (in Ref. 5; AAA83548). {ECO:0000305}; 4, CONFLICT S -> R (in Ref. 5; AAA83548). {ECO:0000305}; 5, CONFLICT C -> S (in Ref. 5; AAA83548). {ECO:0000305}; 6, CONFLICT V -> D (in Ref. 5; AAA83548). {ECO:0000305}; 7, CONFLICT G -> E (in Ref. 1; BAC04764). {ECO:0000305}; 8, CONFLICT K -> E (in Ref. 1; BAC04764). {ECO:0000305}; 9, KRAB. {ECO:0000255|PROSITE- ProRule:PRU00119}; 10, ZN_FING C2H2-type 1; degenerate. {ECO:0000255|PROSITE-ProRule:PRU00042}; 11, ZN_FING C2H2-type 2. {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. {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, VAR_SEQ Missing (in isoform 2). {ECO:0000303|PubMed:14702039}; 28, VAR_SEQ Missing (in isoform 3). {ECO:0000303|PubMed:14702039}; 29, ipat:ZINC_FINGER_C2H2_1 [T]; 30, ismart:ZnF_C2H2 [T]; 31, iprf:ZINC_FINGER_C2H2_2 [T]; 32, iprf:KRAB [T]; 33, ismart:KRAB [T]; 34, ipfam:KRAB [T].
| |
ID ZNF93_HUMAN Reviewed; 620 AA.
AC P35789; A6NMY2; B9EGT2; Q8N8Q4; Q9H9X5; Q9Y2N8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 4.
DT 02-NOV-2016, entry version 155.
DE RecName: Full=Zinc finger protein 93;
DE AltName: Full=Zinc finger protein 505;
DE AltName: Full=Zinc finger protein HTF34;
GN Name=ZNF93; Synonyms=ZNF505;
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 [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 307-620 (ISOFORM 3), AND VARIANT
RP TYR-93.
RC TISSUE=Teratocarcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-195.
RX PubMed=2023909; DOI=10.1073/pnas.88.9.3608;
RA Bellefroid E.J., Poncelet D.A., Lecocq P.J., Revelant O.,
RA Martial J.A.;
RT "The evolutionarily conserved Kruppel-associated box domain defines a
RT subfamily of eukaryotic multifingered proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3608-3612(1991).
RN [6]
RP RESISTANCE TO ET-743 AND PM00104 ANTITUMORS.
RX PubMed=19742314; DOI=10.1371/journal.pone.0006967;
RA Duan Z., Choy E., Harmon D., Yang C., Ryu K., Schwab J., Mankin H.,
RA Hornicek F.J.;
RT "ZNF93 increases resistance to ET-743 (Trabectedin; Yondelis) and
RT PM00104 (Zalypsis) in human cancer cell lines.";
RL PLoS ONE 4:E6967-E6967(2009).
RN [7]
RP FUNCTION.
RX PubMed=25274305; DOI=10.1038/nature13760;
RA Jacobs F.M., Greenberg D., Nguyen N., Haeussler M., Ewing A.D.,
RA Katzman S., Paten B., Salama S.R., Haussler D.;
RT "An evolutionary arms race between KRAB zinc-finger genes ZNF91/93 and
RT SVA/L1 retrotransposons.";
RL Nature 516:242-245(2014).
CC -!- FUNCTION: Transcription factor specifically required to repress
CC long interspersed nuclear element 1 (L1) retrotransposons:
CC recognizes and binds L1 sequences and repress their expression by
CC recruiting a repressive complex containing TRIM28/KAP1
CC (PubMed:25274305). Not able to repress expression of all subtypes
CC of L1 elements. Binds to the 5' end of L1PA4, L1PA5 and L1PA6
CC subtypes, and some L1PA3 subtypes. Does not bind to L1PA7 or older
CC subtypes nor at the most recently evolved L1PA2 and L1Hs. 50% of
CC L1PA3 elements have lost the ZNF93-binding site, explaining why
CC ZNF93 is not able to repress their expression (PubMed:25274305).
CC {ECO:0000269|PubMed:25274305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P35789-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35789-2; Sequence=VSP_016988;
CC Note=No experimental confirmation available.;
CC Name=3;
CC IsoId=P35789-3; Sequence=VSP_016989;
CC Note=No experimental confirmation available.;
CC -!- DEVELOPMENTAL STAGE: Expressed early during embryonic development.
CC -!- MISCELLANEOUS: ZNF93 is only present in primates and evolved to
CC repress the primate L1 lineage until 12.5 million years. Evolution
CC stopped when the L1PA3-subfamily of retrotransposons, that escape
CC repression by ZNF93 through the removal of the ZNF93-binding site,
CC appeared (PubMed:25274305). {ECO:0000269|PubMed:25274305}.
CC -!- MISCELLANEOUS: Confers resistance to ET-743 (trabectedin,
CC Yondelis) and PM00104 (Zalypsis), 2 marine derived compounds with
CC antitumor activity in cancer cell lines.
CC {ECO:0000305|PubMed:19742314}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 17 C2H2-type zinc fingers.
CC {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC -!- SIMILARITY: Contains 1 KRAB domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00119}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD22981.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB14093.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR EMBL; AK022550; BAB14093.1; ALT_INIT; mRNA.
DR EMBL; AK096342; BAC04764.1; -; mRNA.
DR EMBL; AC007204; AAD22981.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84866.1; -; Genomic_DNA.
DR EMBL; BC136718; AAI36719.1; -; mRNA.
DR EMBL; BC136719; AAI36720.1; -; mRNA.
DR EMBL; M61873; AAA83548.1; -; Genomic_DNA.
DR CCDS; CCDS32973.1; -. [P35789-1]
DR PIR; H39384; H39384.
DR RefSeq; NP_112495.2; NM_031218.3. [P35789-1]
DR UniGene; Hs.301059; -.
DR UniGene; Hs.723768; -.
DR ProteinModelPortal; P35789; -.
DR SMR; P35789; -.
DR BioGrid; 123631; 1.
DR STRING; 9606.ENSP00000342002; -.
DR iPTMnet; P35789; -.
DR PhosphoSitePlus; P35789; -.
DR BioMuta; ZNF93; -.
DR DMDM; 85681872; -.
DR MaxQB; P35789; -.
DR PaxDb; P35789; -.
DR PeptideAtlas; P35789; -.
DR PRIDE; P35789; -.
DR Ensembl; ENST00000343769; ENSP00000342002; ENSG00000184635. [P35789-1]
DR GeneID; 81931; -.
DR KEGG; hsa:81931; -.
DR UCSC; uc002non.4; human. [P35789-1]
DR CTD; 81931; -.
DR DisGeNET; 81931; -.
DR GeneCards; ZNF93; -.
DR HGNC; HGNC:13169; ZNF93.
DR MIM; 603975; gene.
DR neXtProt; NX_P35789; -.
DR OpenTargets; ENSG00000184635; -.
DR PharmGKB; PA37741; -.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; COG5048; LUCA.
DR GeneTree; ENSGT00790000122969; -.
DR HOGENOM; HOG000234617; -.
DR HOVERGEN; HBG018163; -.
DR InParanoid; P35789; -.
DR KO; K09228; -.
DR OMA; IHMGKKH; -.
DR OrthoDB; EOG091G02KC; -.
DR PhylomeDB; P35789; -.
DR TreeFam; TF342117; -.
DR ChiTaRS; ZNF93; human.
DR GenomeRNAi; 81931; -.
DR PRO; PR:P35789; -.
DR Proteomes; UP000005640; Chromosome 19.
DR Bgee; ENSG00000184635; -.
DR CleanEx; HS_ZNF93; -.
DR ExpressionAtlas; P35789; baseline and differential.
DR Genevisible; P35789; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0070895; P:negative regulation of transposon integration; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR CDD; cd07765; KRAB_A-box; 1.
DR Gene3D; 3.30.160.60; -; 17.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR Pfam; PF13912; zf-C2H2_6; 3.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 17.
DR SUPFAM; SSF109640; SSF109640; 1.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 17.
PE 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; DNA-binding; Metal-binding;
KW Nucleus; Polymorphism; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 620 Zinc finger protein 93.
FT /FTId=PRO_0000047402.
FT DOMAIN 4 75 KRAB. {ECO:0000255|PROSITE-
FT ProRule:PRU00119}.
FT ZN_FING 145 167 C2H2-type 1; degenerate.
FT {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT ZN_FING 173 195 C2H2-type 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 201 223 C2H2-type 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 229 251 C2H2-type 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 257 279 C2H2-type 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 285 307 C2H2-type 6. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 313 335 C2H2-type 7. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 341 363 C2H2-type 8. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 369 391 C2H2-type 9. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 397 419 C2H2-type 10. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 425 447 C2H2-type 11. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 453 475 C2H2-type 12. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 481 503 C2H2-type 13. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 509 531 C2H2-type 14. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 537 559 C2H2-type 15. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 565 587 C2H2-type 16. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 593 615 C2H2-type 17. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT VAR_SEQ 391 418 Missing (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_016988.
FT VAR_SEQ 499 582 Missing (in isoform 3).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_016989.
FT VARIANT 93 93 D -> Y (in dbSNP:rs12151060).
FT {ECO:0000269|PubMed:14702039}.
FT /FTId=VAR_052768.
FT CONFLICT 75 75 S -> SGP (in Ref. 5; AAA83548).
FT {ECO:0000305}.
FT CONFLICT 89 89 Q -> H (in Ref. 5; AAA83548).
FT {ECO:0000305}.
FT CONFLICT 119 119 S -> R (in Ref. 5; AAA83548).
FT {ECO:0000305}.
FT CONFLICT 136 136 C -> S (in Ref. 5; AAA83548).
FT {ECO:0000305}.
FT CONFLICT 153 153 V -> D (in Ref. 5; AAA83548).
FT {ECO:0000305}.
FT CONFLICT 337 337 G -> E (in Ref. 1; BAC04764).
FT {ECO:0000305}.
FT CONFLICT 597 597 K -> E (in Ref. 1; BAC04764).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 539 559 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 509 531 ismart:ZnF_C2H2 [T]
FT MYHIT 371 391 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 397 424 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 483 503 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 203 223 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 4 75 iprf:KRAB [T]
FT MYHIT 341 368 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 4 64 ismart:KRAB [T]
FT MYHIT 397 419 ismart:ZnF_C2H2 [T]
FT MYHIT 593 620 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 257 284 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 341 363 ismart:ZnF_C2H2 [T]
FT MYHIT 313 335 ismart:ZnF_C2H2 [T]
FT MYHIT 425 452 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 285 307 ismart:ZnF_C2H2 [T]
FT MYHIT 509 536 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 537 564 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 481 503 ismart:ZnF_C2H2 [T]
FT MYHIT 201 228 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 231 251 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 537 559 ismart:ZnF_C2H2 [T]
FT MYHIT 145 172 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 565 592 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 175 195 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 399 419 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 595 615 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 229 256 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 4 44 ipfam:KRAB [T]
FT MYHIT 565 587 ismart:ZnF_C2H2 [T]
FT MYHIT 229 251 ismart:ZnF_C2H2 [T]
FT MYHIT 369 391 ismart:ZnF_C2H2 [T]
FT MYHIT 425 447 ismart:ZnF_C2H2 [T]
FT MYHIT 453 480 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 315 335 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 173 200 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 313 340 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 343 363 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 259 279 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 287 307 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 453 475 ismart:ZnF_C2H2 [T]
FT MYHIT 593 615 ismart:ZnF_C2H2 [T]
FT MYHIT 455 475 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 201 223 ismart:ZnF_C2H2 [T]
FT MYHIT 511 531 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 427 447 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 285 312 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 145 167 ismart:ZnF_C2H2 [T]
FT MYHIT 173 195 ismart:ZnF_C2H2 [T]
FT MYHIT 567 587 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 257 279 ismart:ZnF_C2H2 [T]
FT MYHIT 369 396 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 481 508 iprf:ZINC_FINGER_C2H2_2 [T]
SQ SEQUENCE 620 AA; 70971 MW; 722A49B2EA82801A CRC64;
MGPLQFRDVA IEFSLEEWHC LDTAQRNLYR NVMLENYSNL VFLGIVVSKP DLIAHLEQGK
KPLTMKRHEM VANPSVICSH FAQDLWPEQN IKDSFQKVIL RRYEKRGHGN LQLIKRCESV
DECKVHTGGY NGLNQCSTTT QSKVFQCDKY GKVFHKFSNS NRHNIRHTEK KPFKCIECGK
AFNQFSTLIT HKKIHTGEKP YICEECGKAF KYSSALNTHK RIHTGEKPYK CDKCDKAFIA
SSTLSKHEII HTGKKPYKCE ECGKAFNQSS TLTKHKKIHT GEKPYKCEEC GKAFNQSSTL
TKHKKIHTGE KPYVCEECGK AFKYSRILTT HKRIHTGEKP YKCNKCGKAF IASSTLSRHE
FIHMGKKHYK CEECGKAFIW SSVLTRHKRV HTGEKPYKCE ECGKAFKYSS TLSSHKRSHT
GEKPYKCEEC GKAFVASSTL SKHEIIHTGK KPYKCEECGK AFNQSSSLTK HKKIHTGEKP
YKCEECGKAF NQSSSLTKHK KIHTGEKPYK CEECGKAFNQ SSTLIKHKKI HTREKPYKCE
ECGKAFHLST HLTTHKILHT GEKPYRCREC GKAFNHSATL SSHKKIHSGE KPYECDKCGK
AFISPSSLSR HEIIHTGEKP
//
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