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 217; |
 |
|
| MyHits synonyms | ZN217_HUMAN , O75362 , E1P5Y6 , Q14DB8 , 797FC620817D1E1F |
 Legends: 1, Phosphoserine. {ECO:0000244|PubMed:23186163}; 2, Phosphoserine. {ECO:0000244|PubMed:18669648}; 3, Phosphothreonine. {ECO:0000244|PubMed:18669648}; 4, Phosphoserine. {ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163}; 5, Phosphoserine. {ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:23186163}; 6, Phosphoserine. {ECO:0000244|PubMed:21406692}; 7, VARIANT D -> N (in a colorectal cancer sample; somatic mutation; dbSNP:rs767530299). {ECO:0000269|PubMed:16959974}; 8, VARIANT V -> I (in dbSNP:rs6063966); 9, VARIANT D -> G (in dbSNP:rs34323943); 10, ZN_FING C2H2-type 1. {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, ismart:ZnF_C2H2 [T]; 18, ipat:ZINC_FINGER_C2H2_1 [T]; 19, iprf:ZINC_FINGER_C2H2_2 [T]; 20, TURN {ECO:0000244|PDB:3UK3}; 21, HELIX {ECO:0000244|PDB:3UK3}; 22, STRAND {ECO:0000244|PDB:3UK3}.
| |
ID ZN217_HUMAN Reviewed; 1048 AA.
AC O75362; E1P5Y6; Q14DB8;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 30-NOV-2016, entry version 155.
DE RecName: Full=Zinc finger protein 217;
GN Name=ZNF217; Synonyms=ZABC1;
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].
RX PubMed=9671742; DOI=10.1073/pnas.95.15.8703;
RA Collins C., Rommens J.M., Kowbel D., Godfrey T., Tanner M.,
RA Hwang S.-I., Polikoff D., Nonet G., Cochran J., Myambo K., Jay K.E.,
RA Froula J., Cloutier T., Kuo W.-L., Yaswen P., Dairkee S.,
RA Giovanola J., Hutchinson G.B., Isola J., Kallioniemi O.-P.,
RA Palazzolo M., Martin C., Ericsson C., Pinkel D., Albertson D.,
RA Li W.-B., Gray J.W.;
RT "Positional cloning of ZNF217 and NABC1: genes amplified at 20q13.2
RT and overexpressed in breast carcinoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8703-8708(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 THE BHC COMPLEX WITH GSE1; GTF2I; HDAC1; HDAC2;
RP HMG20B; KDM1A; PHF21A; RCOR1; ZMYM2 AND ZMYM3.
RX PubMed=12493763; DOI=10.1074/jbc.M208992200;
RA Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
RT "A candidate X-linked mental retardation gene is a component of a new
RT family of histone deacetylase-containing complexes.";
RL J. Biol. Chem. 278:7234-7239(2003).
RN [6]
RP FUNCTION.
RX PubMed=16203743; DOI=10.1093/hmg/ddi352;
RA Huang G., Krig S., Kowbel D., Xu H., Hyun B., Volik S., Feuerstein B.,
RA Mills G.B., Stokoe D., Yaswen P., Collins C.;
RT "ZNF217 suppresses cell death associated with chemotherapy and
RT telomere dysfunction.";
RL Hum. Mol. Genet. 14:3219-3225(2005).
RN [7]
RP FUNCTION.
RX PubMed=17259635; DOI=10.1074/jbc.M611752200;
RA Krig S.R., Jin V.X., Bieda M.C., O'Geen H., Yaswen P., Green R.,
RA Farnham P.J.;
RT "Identification of genes directly regulated by the oncogene ZNF217
RT using chromatin immunoprecipitation (ChIP)-chip assays.";
RL J. Biol. Chem. 282:9703-9712(2007).
RN [8]
RP SUBUNIT, IDENTIFICATION IN A COMPLEX WITH HDAC2; KDM1A AND CTBP1, AND
RP FUNCTION.
RX PubMed=18625718; DOI=10.1128/MCB.00246-08;
RA Thillainadesan G., Isovic M., Loney E., Andrews J., Tini M.,
RA Torchia J.;
RT "Genome analysis identifies the p15ink4b tumor suppressor as a direct
RT target of the ZNF217/CoREST complex.";
RL Mol. Cell. Biol. 28:6066-6077(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; THR-322; THR-648
RP AND SER-662, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-795, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-407; SER-593
RP AND SER-662, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 752-760 IN COMPLEX WITH
RP CTBP1, INTERACTION WITH CTBP1 AND CTBP2, AND FUNCTION.
RX PubMed=16940172; DOI=10.1128/MCB.00680-06;
RA Quinlan K.G.R., Nardini M., Verger A., Francescato P., Yaswen P.,
RA Corda D., Bolognesi M., Crossley M.;
RT "Specific recognition of ZNF217 and other zinc finger proteins at a
RT surface groove of C-terminal binding proteins.";
RL Mol. Cell. Biol. 26:8159-8172(2006).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-323.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Binds to the promoters of target genes and functions as
CC repressor. Promotes cell proliferation and antagonizes cell death.
CC Promotes phosphorylation of AKT1 at 'Ser-473'.
CC {ECO:0000269|PubMed:16203743, ECO:0000269|PubMed:16940172,
CC ECO:0000269|PubMed:17259635, ECO:0000269|PubMed:18625718}.
CC -!- SUBUNIT: Component of a histone deacetylase complex that contains
CC HDAC2, KDM1A, CTBP1 and ZNF217. May be a component of a BHC
CC histone deacetylase complex that contains HDAC1, HDAC2,
CC HMG20B/BRAF35, KDM1A, RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217,
CC ZMYM3, GSE1 and GTF2I. Interacts with CTBP1 and CTBP2.
CC {ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:16940172,
CC ECO:0000269|PubMed:18625718}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 7 C2H2-type zinc fingers.
CC {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ZNF217ID42875ch20q13.html";
DR EMBL; AF041259; AAC39895.1; -; mRNA.
DR EMBL; AL157838; CAC08433.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75580.1; -; Genomic_DNA.
DR EMBL; BC113427; AAI13428.1; -; mRNA.
DR CCDS; CCDS13443.1; -.
DR RefSeq; NP_006517.1; NM_006526.2.
DR RefSeq; XP_016883548.1; XM_017028059.1.
DR UniGene; Hs.155040; -.
DR UniGene; Hs.711564; -.
DR PDB; 2HU2; X-ray; 2.85 A; B=752-760.
DR PDB; 3UK3; X-ray; 2.10 A; C/D=469-523.
DR PDB; 4F2J; X-ray; 2.64 A; C=469-523.
DR PDB; 4IS1; X-ray; 2.10 A; C/D=469-523.
DR PDBsum; 2HU2; -.
DR PDBsum; 3UK3; -.
DR PDBsum; 4F2J; -.
DR PDBsum; 4IS1; -.
DR ProteinModelPortal; O75362; -.
DR SMR; O75362; -.
DR BioGrid; 113547; 12.
DR IntAct; O75362; 6.
DR MINT; MINT-7970236; -.
DR STRING; 9606.ENSP00000304308; -.
DR iPTMnet; O75362; -.
DR PhosphoSitePlus; O75362; -.
DR BioMuta; ZNF217; -.
DR EPD; O75362; -.
DR MaxQB; O75362; -.
DR PaxDb; O75362; -.
DR PeptideAtlas; O75362; -.
DR PRIDE; O75362; -.
DR Ensembl; ENST00000302342; ENSP00000304308; ENSG00000171940.
DR Ensembl; ENST00000371471; ENSP00000360526; ENSG00000171940.
DR GeneID; 7764; -.
DR KEGG; hsa:7764; -.
DR UCSC; uc002xwq.5; human.
DR CTD; 7764; -.
DR DisGeNET; 7764; -.
DR GeneCards; ZNF217; -.
DR HGNC; HGNC:13009; ZNF217.
DR HPA; HPA051857; -.
DR MIM; 602967; gene.
DR neXtProt; NX_O75362; -.
DR OpenTargets; ENSG00000171940; -.
DR PharmGKB; PA37588; -.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; COG5048; LUCA.
DR GeneTree; ENSGT00530000063100; -.
DR HOGENOM; HOG000276541; -.
DR HOVERGEN; HBG061769; -.
DR InParanoid; O75362; -.
DR OMA; EHSKVHT; -.
DR OrthoDB; EOG091G010T; -.
DR PhylomeDB; O75362; -.
DR TreeFam; TF332241; -.
DR BioCyc; ZFISH:ENSG00000171940-MONOMER; -.
DR SIGNOR; O75362; -.
DR ChiTaRS; ZNF217; human.
DR EvolutionaryTrace; O75362; -.
DR GeneWiki; ZNF217; -.
DR GenomeRNAi; 7764; -.
DR PRO; PR:O75362; -.
DR Proteomes; UP000005640; Chromosome 20.
DR Bgee; ENSG00000171940; -.
DR CleanEx; HS_ZNF217; -.
DR ExpressionAtlas; O75362; baseline and differential.
DR Genevisible; O75362; HS.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
DR GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
DR GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; TAS:ProtInc.
DR Gene3D; 3.30.160.60; -; 6.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR SMART; SM00355; ZnF_C2H2; 8.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 1048 Zinc finger protein 217.
FT /FTId=PRO_0000047460.
FT ZN_FING 65 88 C2H2-type 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 128 150 C2H2-type 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 156 178 C2H2-type 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 216 238 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 471 493 C2H2-type 6. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 499 521 C2H2-type 7. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT MOD_RES 106 106 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 321 321 Phosphoserine.
FT {ECO:0000244|PubMed:18669648}.
FT MOD_RES 322 322 Phosphothreonine.
FT {ECO:0000244|PubMed:18669648}.
FT MOD_RES 407 407 Phosphoserine.
FT {ECO:0000244|PubMed:21406692,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 593 593 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 648 648 Phosphothreonine.
FT {ECO:0000244|PubMed:18669648}.
FT MOD_RES 662 662 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 795 795 Phosphoserine.
FT {ECO:0000244|PubMed:21406692}.
FT VARIANT 323 323 D -> N (in a colorectal cancer sample;
FT somatic mutation; dbSNP:rs767530299).
FT {ECO:0000269|PubMed:16959974}.
FT /FTId=VAR_035572.
FT VARIANT 739 739 V -> I (in dbSNP:rs6063966).
FT /FTId=VAR_052795.
FT VARIANT 889 889 D -> G (in dbSNP:rs34323943).
FT /FTId=VAR_061939.
FT TURN 474 476 {ECO:0000244|PDB:3UK3}.
FT HELIX 483 494 {ECO:0000244|PDB:3UK3}.
FT STRAND 502 505 {ECO:0000244|PDB:3UK3}.
FT STRAND 507 510 {ECO:0000244|PDB:3UK3}.
FT HELIX 511 521 {ECO:0000244|PDB:3UK3}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 128 150 ismart:ZnF_C2H2 [T]
FT MYHIT 65 88 ismart:ZnF_C2H2 [T]
FT MYHIT 67 88 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 377 397 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 710 733 ismart:ZnF_C2H2 [T]
FT MYHIT 218 238 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 499 521 ismart:ZnF_C2H2 [T]
FT MYHIT 375 397 ismart:ZnF_C2H2 [T]
FT MYHIT 158 178 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 216 238 ismart:ZnF_C2H2 [T]
FT MYHIT 471 493 ismart:ZnF_C2H2 [T]
FT MYHIT 375 402 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 499 526 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 216 243 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 473 493 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 471 498 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 156 183 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 130 150 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 65 88 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 156 178 ismart:ZnF_C2H2 [T]
FT MYHIT 128 155 iprf:ZINC_FINGER_C2H2_2 [T]
SQ SEQUENCE 1048 AA; 115272 MW; 797FC620817D1E1F CRC64;
MQSKVTGNMP TQSLLMYMDG PEVIGSSLGS PMEMEDALSM KGTAVVPFRA TQEKNVIQIE
GYMPLDCMFC SQTFTHSEDL NKHVLMQHRP TLCEPAVLRV EAEYLSPLDK SQVRTEPPKE
KNCKENEFSC EVCGQTFRVA FDVEIHMRTH KDSFTYGCNM CGRRFKEPWF LKNHMRTHNG
KSGARSKLQQ GLESSPATIN EVVQVHAAES ISSPYKICMV CGFLFPNKES LIEHRKVHTK
KTAFGTSSAQ TDSPQGGMPS SREDFLQLFN LRPKSHPETG KKPVRCIPQL DPFTTFQAWQ
LATKGKVAIC QEVKESGQEG STDNDDSSSE KELGETNKGS CAGLSQEKEK CKHSHGEAPS
VDADPKLPSS KEKPTHCSEC GKAFRTYHQL VLHSRVHKKD RRAGAESPTM SVDGRQPGTC
SPDLAAPLDE NGAVDRGEGG SEDGSEDGLP EGIHLDKNDD GGKIKHLTSS RECSYCGKFF
RSNYYLNIHL RTHTGEKPYK CEFCEYAAAQ KTSLRYHLER HHKEKQTDVA AEVKNDGKNQ
DTEDALLTAD SAQTKNLKRF FDGAKDVTGS PPAKQLKEMP SVFQNVLGSA VLSPAHKDTQ
DFHKNAADDS ADKVNKNPTP AYLDLLKKRS AVETQANNLI CRTKADVTPP PDGSTTHNLE
VSPKEKQTET AADCRYRPSV DCHEKPLNLS VGALHNCPAI SLSKSLIPSI TCPFCTFKTF
YPEVLMMHQR LEHKYNPDVH KNCRNKSLLR SRRTGCPPAL LGKDVPPLSS FCKPKPKSAF
PAQSKSLPSA KGKQSPPGPG KAPLTSGIDS STLAPSNLKS HRPQQNVGVQ GAATRQQQSE
MFPKTSVSPA PDKTKRPETK LKPLPVAPSQ PTLGSSNING SIDYPAKNDS PWAPPGRDYF
CNRSASNTAA EFGEPLPKRL KSSVVALDVD QPGANYRRGY DLPKYHMVRG ITSLLPQDCV
YPSQALPPKP RFLSSSEVDS PNVLTVQKPY GGSGPLYTCV PAGSPASSST LEGKRPVSYQ
HLSNSMAQKR NYENFIGNAH YRPNDKKT
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