ID ZNF41_HUMAN Reviewed; 821 AA. AC P51814; A8K1V6; B4DH01; Q96LE8; Q9UMC4; Q9UMV5; Q9UMV6; Q9UMV7; Q9UMV8; AC Q9UMV9; Q9UMW0; Q9UMW1; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 27-MAR-2024, entry version 220. DE RecName: Full=Zinc finger protein 41; GN Name=ZNF41; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING. RX PubMed=10449920; DOI=10.1159/000015315; RA Rosati M., Franze A., Matarazzo M.R., Grimaldi G.; RT "Coding region intron/exon organization, alternative splicing and X- RT chromosome inactivation of the KRAB/FPB-domain-containing human zinc finger RT gene ZNF41."; RL Cytogenet. Cell Genet. 85:291-296(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6). RC TISSUE=Brain, and Hippocampus; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 280-821. RX PubMed=2037297; DOI=10.1016/0888-7543(91)90367-n; RA Franze A., Archidiacono N., Rocchi M., Marino M., Grimaldi G.; RT "Isolation and expression analysis of a human zinc finger gene (ZNF41) RT located on the short arm of the X chromosome."; RL Genomics 9:728-736(1991). RN [7] RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION, RP VARIANTS LEU-153; ARG-167 AND GLU-357, AND POSSIBLE ASSOCIATION OF VARIANT RP LEU-153 WITH X-LINKED INTELLECTUAL DISABILITY. RX PubMed=14628291; DOI=10.1086/380309; RA Shoichet S.A., Hoffmann K., Menzel C., Trautmann U., Moser B., RA Hoeltzenbein M., Echenne B., Partington M., Van Bokhoven H., Moraine C., RA Fryns J.-P., Chelly J., Rott H.-D., Ropers H.-H., Kalscheuer V.M.; RT "Mutations in the ZNF41 gene are associated with cognitive deficits: RT identification of a new candidate for X-linked mental retardation."; RL Am. J. Hum. Genet. 73:1341-1354(2003). RN [8] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-120 AND LYS-647, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [9] RP LACK OF ASSOCIATION OF VARIANT LEU-153 WITH X-LINKED INTELLECTUAL RP DISABILITY. RX PubMed=23871722; DOI=10.1016/j.ajhg.2013.06.013; RA Piton A., Redin C., Mandel J.L.; RT "XLID-causing mutations and associated genes challenged in light of data RT from large-scale human exome sequencing."; RL Am. J. Hum. Genet. 93:368-383(2013). CC -!- FUNCTION: May be involved in transcriptional regulation. CC -!- INTERACTION: CC P51814; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-2681830, EBI-10175124; CC P51814; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-2681830, EBI-10172290; CC P51814-6; Q8IZU0: FAM9B; NbExp=6; IntAct=EBI-12700258, EBI-10175124; CC P51814-6; P55081: MFAP1; NbExp=3; IntAct=EBI-12700258, EBI-1048159; CC P51814-6; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-12700258, EBI-3920396; CC P51814-6; Q15287: RNPS1; NbExp=3; IntAct=EBI-12700258, EBI-395959; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=P51814-1; Sequence=Displayed; CC Name=2; CC IsoId=P51814-2; Sequence=VSP_006883; CC Name=3; CC IsoId=P51814-3; Sequence=VSP_006884; CC Name=4; CC IsoId=P51814-4; Sequence=VSP_006887; CC Name=5; CC IsoId=P51814-5; Sequence=VSP_006886; CC Name=6; CC IsoId=P51814-6; Sequence=VSP_006885; CC Name=7; CC IsoId=P51814-7; Sequence=VSP_006883, VSP_006888; CC Name=8; CC IsoId=P51814-8; Sequence=VSP_006885, VSP_006888; CC -!- TISSUE SPECIFICITY: Expressed in the heart, brain, placenta, lung, CC liver, skeletal muscle, kidney and pancreas. CC {ECO:0000269|PubMed:14628291}. CC -!- DISEASE: Note=A chromosomal aberration involving ZNF41 has been found CC in a patient with severe intellectual disability. Translocation CC t(X;7)(p11.3;q11.21). {ECO:0000269|PubMed:14628291}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- CAUTION: Although ZNF41 has been reported to be involved in X-linked CC intellectual disability (PubMed:14628291), its pathological role is CC questionable (PubMed:23871722). {ECO:0000305|PubMed:14628291, CC ECO:0000305|PubMed:23871722}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X60155; CAB51740.1; -; mRNA. DR EMBL; AJ010017; CAB53035.1; -; mRNA. DR EMBL; AJ010018; CAB53036.1; -; mRNA. DR EMBL; AJ010019; CAB53037.1; -; mRNA. DR EMBL; AJ010020; CAB53038.1; -; mRNA. DR EMBL; AJ010021; CAB53039.1; -; mRNA. DR EMBL; AJ010022; CAB53040.1; -; mRNA. DR EMBL; AJ010023; CAB53041.1; -; mRNA. DR EMBL; AK290021; BAF82710.1; -; mRNA. DR EMBL; AK294858; BAG57962.1; -; mRNA. DR EMBL; AL590223; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590283; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471164; EAW59303.1; -; Genomic_DNA. DR EMBL; BC015023; AAH15023.1; -; mRNA. DR EMBL; M92443; AAA61312.1; -; Genomic_DNA. DR CCDS; CCDS14279.1; -. [P51814-6] DR PIR; A54661; A54661. DR RefSeq; NP_001311068.1; NM_001324139.1. [P51814-4] DR RefSeq; NP_001311069.1; NM_001324140.1. [P51814-6] DR RefSeq; NP_001311070.1; NM_001324141.1. [P51814-4] DR RefSeq; NP_001311071.1; NM_001324142.1. [P51814-2] DR RefSeq; NP_001311072.1; NM_001324143.1. [P51814-4] DR RefSeq; NP_001311073.1; NM_001324144.1. [P51814-6] DR RefSeq; NP_001311074.1; NM_001324145.1. [P51814-4] DR RefSeq; NP_001311076.1; NM_001324147.1. [P51814-6] DR RefSeq; NP_001311077.1; NM_001324148.1. [P51814-2] DR RefSeq; NP_001311078.1; NM_001324149.1. [P51814-4] DR RefSeq; NP_001311079.1; NM_001324150.1. [P51814-6] DR RefSeq; NP_001311080.1; NM_001324151.1. [P51814-3] DR RefSeq; NP_001311081.1; NM_001324152.1. [P51814-4] DR RefSeq; NP_001311082.1; NM_001324153.1. [P51814-3] DR RefSeq; NP_001311083.1; NM_001324154.1. [P51814-5] DR RefSeq; NP_001311084.1; NM_001324155.1. [P51814-1] DR RefSeq; NP_001311085.1; NM_001324156.1. [P51814-7] DR RefSeq; NP_001311086.1; NM_001324157.1. [P51814-8] DR RefSeq; NP_009061.1; NM_007130.3. [P51814-6] DR RefSeq; NP_700359.1; NM_153380.3. [P51814-6] DR RefSeq; XP_006724613.1; XM_006724550.3. [P51814-5] DR RefSeq; XP_006724618.1; XM_006724555.3. [P51814-3] DR RefSeq; XP_016885299.1; XM_017029810.1. [P51814-5] DR RefSeq; XP_016885300.1; XM_017029811.1. [P51814-5] DR RefSeq; XP_016885301.1; XM_017029812.1. [P51814-5] DR RefSeq; XP_016885302.1; XM_017029813.1. [P51814-5] DR RefSeq; XP_016885303.1; XM_017029814.1. [P51814-5] DR RefSeq; XP_016885304.1; XM_017029815.1. [P51814-5] DR RefSeq; XP_016885305.1; XM_017029816.1. [P51814-3] DR RefSeq; XP_016885306.1; XM_017029817.1. [P51814-6] DR AlphaFoldDB; P51814; -. DR SMR; P51814; -. DR BioGRID; 113418; 8. DR IntAct; P51814; 9. DR MINT; P51814; -. DR STRING; 9606.ENSP00000366265; -. DR iPTMnet; P51814; -. DR PhosphoSitePlus; P51814; -. DR BioMuta; ZNF41; -. DR DMDM; 20141930; -. DR EPD; P51814; -. DR jPOST; P51814; -. DR MassIVE; P51814; -. DR MaxQB; P51814; -. DR PeptideAtlas; P51814; -. DR ProteomicsDB; 56410; -. [P51814-1] DR ProteomicsDB; 56411; -. [P51814-2] DR ProteomicsDB; 56412; -. [P51814-3] DR ProteomicsDB; 56413; -. [P51814-4] DR ProteomicsDB; 56414; -. [P51814-5] DR ProteomicsDB; 56415; -. [P51814-6] DR ProteomicsDB; 56416; -. [P51814-7] DR ProteomicsDB; 56417; -. [P51814-8] DR ABCD; P51814; 1 sequenced antibody. DR Antibodypedia; 25429; 245 antibodies from 20 providers. DR DNASU; 7592; -. DR Ensembl; ENST00000313116.11; ENSP00000315173.7; ENSG00000147124.13. [P51814-6] DR Ensembl; ENST00000377065.8; ENSP00000366265.4; ENSG00000147124.13. [P51814-6] DR Ensembl; ENST00000684689.1; ENSP00000508254.1; ENSG00000147124.13. [P51814-6] DR GeneID; 7592; -. DR KEGG; hsa:7592; -. DR MANE-Select; ENST00000684689.1; ENSP00000508254.1; NM_001324144.2; NP_001311073.1. [P51814-6] DR UCSC; uc004dhx.5; human. [P51814-1] DR AGR; HGNC:13107; -. DR CTD; 7592; -. DR DisGeNET; 7592; -. DR GeneCards; ZNF41; -. DR HGNC; HGNC:13107; ZNF41. DR HPA; ENSG00000147124; Low tissue specificity. DR MalaCards; ZNF41; -. DR MIM; 314995; gene. DR neXtProt; NX_P51814; -. DR OpenTargets; ENSG00000147124; -. DR Orphanet; 777; X-linked non-syndromic intellectual disability. DR PharmGKB; PA37682; -. DR VEuPathDB; HostDB:ENSG00000147124; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000163107; -. DR HOGENOM; CLU_002678_17_1_1; -. DR InParanoid; P51814; -. DR OMA; SIHQKSH; -. DR OrthoDB; 5253872at2759; -. DR PhylomeDB; P51814; -. DR TreeFam; TF350810; -. DR PathwayCommons; P51814; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR SignaLink; P51814; -. DR BioGRID-ORCS; 7592; 15 hits in 804 CRISPR screens. DR ChiTaRS; ZNF41; human. DR GeneWiki; ZNF41; -. DR GenomeRNAi; 7592; -. DR Pharos; P51814; Tbio. DR PRO; PR:P51814; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P51814; Protein. DR Bgee; ENSG00000147124; Expressed in muscle of leg and 115 other cell types or tissues. DR ExpressionAtlas; P51814; baseline and differential. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd07765; KRAB_A-box; 1. DR Gene3D; 6.10.140.140; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 17. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24377; IP01015P-RELATED; 1. DR PANTHER; PTHR24377:SF669; ZINC FINGER PROTEIN 41; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 17. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 17. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 10. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 17. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 18. DR Genevisible; P51814; HS. PE 1: Evidence at protein level; KW Alternative splicing; Chromosomal rearrangement; DNA-binding; KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat; KW Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..821 FT /note="Zinc finger protein 41" FT /id="PRO_0000047374" FT DOMAIN 69..140 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 313..335 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 341..364 FT /note="C2H2-type 2; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 369..391 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 397..419 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 425..447 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 453..475 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 481..503 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 509..531 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 537..559 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 565..587 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 593..615 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 621..643 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 649..671 FT /note="C2H2-type 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 677..699 FT /note="C2H2-type 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 705..727 FT /note="C2H2-type 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 733..755 FT /note="C2H2-type 16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 761..783 FT /note="C2H2-type 17" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 789..811 FT /note="C2H2-type 18" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..55 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 21..39 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CROSSLNK 120 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 647 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..128 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_006887" FT VAR_SEQ 1..60 FT /note="MAANGDSPPWSPALAAEGRGSSCEVRRERTPEARIHSVKRYPDLSPGPKGRS FT SADHAALN -> MGTLPHGPRPWLQRDVAAHV (in isoform 7 and isoform FT 2)" FT /evidence="ECO:0000305" FT /id="VSP_006883" FT VAR_SEQ 1..52 FT /note="MAANGDSPPWSPALAAEGRGSSCEVRRERTPEARIHSVKRYPDLSPGPKGRS FT -> MGTLPHGPRPWLQRDVAAHV (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_006884" FT VAR_SEQ 25..66 FT /note="Missing (in isoform 6 and isoform 8)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_006885" FT VAR_SEQ 53..60 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_006886" FT VAR_SEQ 141..176 FT /note="Missing (in isoform 7 and isoform 8)" FT /evidence="ECO:0000305" FT /id="VSP_006888" FT VARIANT 153 FT /note="P -> L (found in patients with X-linked intellectual FT disability; uncertain significance; dbSNP:rs104894955)" FT /evidence="ECO:0000269|PubMed:14628291" FT /id="VAR_021785" FT VARIANT 167 FT /note="I -> R (in dbSNP:rs17147624)" FT /evidence="ECO:0000269|PubMed:14628291" FT /id="VAR_021786" FT VARIANT 357 FT /note="D -> E (in dbSNP:rs2498170)" FT /evidence="ECO:0000269|PubMed:14628291" FT /id="VAR_021787" FT CONFLICT 111 FT /note="Q -> R (in Ref. 1; CAB53039)" FT /evidence="ECO:0000305" SQ SEQUENCE 821 AA; 93728 MW; F44B7808C9A8AF13 CRC64; MAANGDSPPW SPALAAEGRG SSCEVRRERT PEARIHSVKR YPDLSPGPKG RSSADHAALN SIVSLQASVS FEDVTVDFSK EEWQHLDPAQ RRLYWDVTLE NYSHLLSVGY QIPKSEAAFK LEQGEGPWML EGEAPHQSCS GEAIGKMQQQ GIPGGIFFHC ERFDQPIGED SLCSILEELW QDNDQLEQRQ ENQNNLLSHV KVLIKERGYE HKNIEKIIHV TTKLVPSIKR LHNCDTILKH TLNSHNHNRN SATKNLGKIF GNGNNFPHSP SSTKNENAKT GANSCEHDHY EKHLSHKQAP THHQKIHPEE KLYVCTECVM GFTQKSHLFE HQRIHAGEKS RECDKSNKVF PQKPQVDVHP SVYTGEKPYL CTQCGKVFTL KSNLITHQKI HTGQKPYKCS ECGKAFFQRS DLFRHLRIHT GEKPYECSEC GKGFSQNSDL SIHQKTHTGE KHYECNECGK AFTRKSALRM HQRIHTGEKP YVCADCGKAF IQKSHFNTHQ RIHTGEKPYE CSDCGKSFTK KSQLHVHQRI HTGEKPYICT ECGKVFTHRT NLTTHQKTHT GEKPYMCAEC GKAFTDQSNL IKHQKTHTGE KPYKCNGCGK AFIWKSRLKI HQKSHIGERH YECKDCGKAF IQKSTLSVHQ RIHTGEKPYV CPECGKAFIQ KSHFIAHHRI HTGEKPYECS DCGKCFTKKS QLRVHQKIHT GEKPNICAEC GKAFTDRSNL ITHQKIHTRE KPYECGDCGK TFTWKSRLNI HQKSHTGERH YECSKCGKAF IQKATLSMHQ IIHTGKKPYA CTECQKAFTD RSNLIKHQKM HSGEKRYKAS D //