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 with KRAB and SCAN domains 1; AltName: Full=Zinc finger protein 139; AltName: Full=Zinc finger protein 36; AltName: Full=Zinc finger protein KOX18; |
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MyHits synonyms | ZKSC1_HUMAN , P17029 , A4D294 , P52745 , Q2M1U1 , Q8TBW5 , Q8TEK7 , 9960C9E320554352 |
![]() Legends: 1, Phosphoserine. {ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569}; 2, Phosphoserine. {ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569}; 3, CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2). {ECO:0000244|PubMed:25218447}; 4, CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2). {ECO:0000244|PubMed:25218447, ECO:0000244|PubMed:25772364}; 5, CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2). {ECO:0000244|PubMed:25772364}; 6, VARIANT V -> A (in dbSNP:rs17851996). {ECO:0000269|PubMed:15489334}; 7, SCAN box. {ECO:0000255|PROSITE- ProRule:PRU00187}; 8, KRAB. {ECO:0000255|PROSITE- ProRule:PRU00119}; 9, ZN_FING C2H2-type 1. {ECO:0000255|PROSITE- ProRule:PRU00042}; 10, ZN_FING C2H2-type 2. {ECO:0000255|PROSITE- ProRule:PRU00042}; 11, ZN_FING C2H2-type 3. {ECO:0000255|PROSITE- ProRule:PRU00042}; 12, ZN_FING C2H2-type 4. {ECO:0000255|PROSITE- ProRule:PRU00042}; 13, ZN_FING C2H2-type 5. {ECO:0000255|PROSITE- ProRule:PRU00042}; 14, ZN_FING C2H2-type 6. {ECO:0000255|PROSITE- ProRule:PRU00042}; 15, iprf:ZINC_FINGER_C2H2_2 [T]; 16, ismart:ZnF_C2H2 [T]; 17, ipat:ZINC_FINGER_C2H2_1 [T]; 18, iprf:SCAN_BOX [T]; 19, ismart:KRAB [T]; 20, ipfam:KRAB [T].
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ID ZKSC1_HUMAN Reviewed; 563 AA. AC P17029; A4D294; P52745; Q2M1U1; Q8TBW5; Q8TEK7; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2006, sequence version 3. DT 10-MAY-2017, entry version 169. DE RecName: Full=Zinc finger protein with KRAB and SCAN domains 1; DE AltName: Full=Zinc finger protein 139; DE AltName: Full=Zinc finger protein 36; DE AltName: Full=Zinc finger protein KOX18; GN Name=ZKSCAN1; Synonyms=KOX18, ZNF139, ZNF36; 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]. RC TISSUE=Spleen; RX PubMed=12693554; DOI=10.1093/dnares/10.1.49; RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., RA Ohara O.; RT "Characterization of long cDNA clones from human adult spleen. II. The RT complete sequences of 81 cDNA clones."; RL DNA Res. 10:49-57(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Fetal kidney; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., RA Mural R.J., Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-26. RC TISSUE=Brain, and Lung; 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 [MRNA] OF 240-563. RC TISSUE=Insulinoma; RX PubMed=7557990; DOI=10.1006/geno.1995.1040; RA Tommerup N., Vissing H.; RT "Isolation and fine mapping of 16 novel human zinc finger-encoding RT cDNAs identify putative candidate genes for developmental and RT malignant disorders."; RL Genomics 27:259-264(1995). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 405-460. RC TISSUE=Lymphoid tissue; RX PubMed=2288909; RA Thiesen H.-J.; RT "Multiple genes encoding zinc finger domains are expressed in human T RT cells."; RL New Biol. 2:363-374(1990). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE 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-13, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-208, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-208, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-280 AND LYS-339, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-339 AND LYS-560, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). CC -!- FUNCTION: May be involved in transcriptional regulation. CC -!- INTERACTION: CC I3L3J2:ZSCAN32; NbExp=3; IntAct=EBI-10199654, EBI-10178206; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE- CC ProRule:PRU00187}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC50264.1; Type=Frameshift; Positions=241; 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; AK074116; BAB84942.1; -; mRNA. DR EMBL; BX640646; CAE45792.1; -; mRNA. DR EMBL; CH236956; EAL23861.1; -; Genomic_DNA. DR EMBL; CH471091; EAW76613.1; -; Genomic_DNA. DR EMBL; BC022378; AAH22378.1; -; mRNA. DR EMBL; BC112224; AAI12225.1; -; mRNA. DR EMBL; BC113697; AAI13698.1; -; mRNA. DR EMBL; U09848; AAC50264.1; ALT_FRAME; mRNA. DR EMBL; X52349; CAA36575.1; -; mRNA. DR CCDS; CCDS34698.1; -. DR PIR; I38616; I38616. DR RefSeq; NP_001333510.1; NM_001346581.1. DR RefSeq; NP_003430.1; NM_003439.3. DR RefSeq; XP_011514861.1; XM_011516559.2. DR UniGene; Hs.615360; -. DR UniGene; Hs.633338; -. DR UniGene; Hs.743424; -. DR ProteinModelPortal; P17029; -. DR SMR; P17029; -. DR BioGrid; 113414; 27. DR IntAct; P17029; 2. DR STRING; 9606.ENSP00000323148; -. DR iPTMnet; P17029; -. DR PhosphoSitePlus; P17029; -. DR DMDM; 85681856; -. DR EPD; P17029; -. DR MaxQB; P17029; -. DR PaxDb; P17029; -. DR PeptideAtlas; P17029; -. DR PRIDE; P17029; -. DR DNASU; 7586; -. DR Ensembl; ENST00000324306; ENSP00000323148; ENSG00000106261. DR GeneID; 7586; -. DR KEGG; hsa:7586; -. DR UCSC; uc003usk.3; human. DR CTD; 7586; -. DR DisGeNET; 7586; -. DR GeneCards; ZKSCAN1; -. DR HGNC; HGNC:13101; ZKSCAN1. DR HPA; HPA006672; -. DR MIM; 601260; gene. DR neXtProt; NX_P17029; -. DR OpenTargets; ENSG00000106261; -. DR PharmGKB; PA37676; -. DR eggNOG; KOG1721; Eukaryota. DR eggNOG; COG5048; LUCA. DR GeneTree; ENSGT00760000118881; -. DR HOGENOM; HOG000234619; -. DR HOVERGEN; HBG018163; -. DR InParanoid; P17029; -. DR KO; K09229; -. DR OMA; EKREQQG; -. DR OrthoDB; EOG091G046Q; -. DR PhylomeDB; P17029; -. DR TreeFam; TF350830; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR ChiTaRS; ZKSCAN1; human. DR GeneWiki; ZKSCAN1; -. DR GenomeRNAi; 7586; -. DR PRO; PR:P17029; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000106261; -. DR CleanEx; HS_ZKSCAN1; -. DR ExpressionAtlas; P17029; baseline and differential. DR Genevisible; P17029; HS. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR CDD; cd07765; KRAB_A-box; 1. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR001909; KRAB. DR InterPro; IPR008916; Retrov_capsid_C. DR InterPro; IPR003309; SCAN_dom. DR InterPro; IPR013087; Znf_C2H2_type. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF02023; SCAN; 1. DR SMART; SM00349; KRAB; 1. DR SMART; SM00431; SCAN; 1. DR SMART; SM00355; ZnF_C2H2; 6. DR SUPFAM; SSF109640; SSF109640; 1. DR SUPFAM; SSF47353; SSF47353; 1. DR SUPFAM; SSF57667; SSF57667; 4. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS50804; SCAN_BOX; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6. PE 1: Evidence at protein level; KW Complete proteome; DNA-binding; Isopeptide bond; Metal-binding; KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; KW Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1 563 Zinc finger protein with KRAB and SCAN FT domains 1. FT /FTId=PRO_0000047753. FT DOMAIN 56 138 SCAN box. {ECO:0000255|PROSITE- FT ProRule:PRU00187}. FT DOMAIN 227 300 KRAB. {ECO:0000255|PROSITE- FT ProRule:PRU00119}. FT ZN_FING 377 399 C2H2-type 1. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 405 427 C2H2-type 2. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 433 455 C2H2-type 3. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 461 483 C2H2-type 4. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 489 511 C2H2-type 5. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 517 539 C2H2-type 6. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT MOD_RES 13 13 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:19369195, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 208 208 Phosphoserine. FT {ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569}. FT CROSSLNK 280 280 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 339 339 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:25772364}. FT CROSSLNK 560 560 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25772364}. FT VARIANT 26 26 V -> A (in dbSNP:rs17851996). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_024839. CC -------------------------------------------------------------------------- CC The following FT lines are automated annotations from the MyHits database. CC -------------------------------------------------------------------------- FT MYHIT 405 432 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 489 516 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 377 404 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 405 427 ismart:ZnF_C2H2 [T] FT MYHIT 379 399 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 461 483 ismart:ZnF_C2H2 [T] FT MYHIT 56 138 iprf:SCAN_BOX [T] FT MYHIT 52 162 ismart:SCAN [T] FT MYHIT 491 511 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 435 455 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 433 460 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 517 544 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 517 539 ismart:ZnF_C2H2 [T] FT MYHIT 489 511 ismart:ZnF_C2H2 [T] FT MYHIT 377 399 ismart:ZnF_C2H2 [T] FT MYHIT 52 138 ipfam:SCAN [T] FT MYHIT 407 427 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 433 455 ismart:ZnF_C2H2 [T] FT MYHIT 227 300 iprf:KRAB [T] FT MYHIT 519 539 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 463 483 ipat:ZINC_FINGER_C2H2_1 [T] FT MYHIT 227 287 ismart:KRAB [T] FT MYHIT 461 488 iprf:ZINC_FINGER_C2H2_2 [T] FT MYHIT 227 262 ipfam:KRAB [T] SQ SEQUENCE 563 AA; 63630 MW; 9960C9E320554352 CRC64; MMTAESREAT GLSPQAAQEK DGIVIVKVEE EDEEDHMWGQ DSTLQDTPPP DPEIFRQRFR RFCYQNTFGP REALSRLKEL CHQWLRPEIN TKEQILELLV LEQFLSILPK ELQVWLQEYR PDSGEEAVTL LEDLELDLSG QQVPGQVHGP EMLARGMVPL DPVQESSSFD LHHEATQSHF KHSSRKPRLL QSRALPAAHI PAPPHEGSPR DQAMASALFT ADSQAMVKIE DMAVSLILEE WGCQNLARRN LSRDNRQENY GSAFPQGGEN RNENEESTSK AETSEDSASR GETTGRSQKE FGEKRDQEGK TGERQQKNPE EKTRKEKRDS GPAIGKDKKT ITGERGPREK GKGLGRSFSL SSNFTTPEEV PTGTKSHRCD ECGKCFTRSS SLIRHKIIHT GEKPYECSEC GKAFSLNSNL VLHQRIHTGE KPHECNECGK AFSHSSNLIL HQRIHSGEKP YECNECGKAF SQSSDLTKHQ RIHTGEKPYE CSECGKAFNR NSYLILHRRI HTREKPYKCT KCGKAFTRSS TLTLHHRIHA RERASEYSPA SLDAFGAFLK SCV // |