ZNF41_HUMAN
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 03-AUG-2022, entry version 211.
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}.
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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 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 PRIDE; 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; 237 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 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; CNKDENI; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; P51814; -.
DR TreeFam; TF350810; -.
DR PathwayCommons; P51814; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; P51814; -.
DR BioGRID-ORCS; 7592; 14 hits in 732 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 113 other tissues.
DR ExpressionAtlas; P51814; baseline and differential.
DR Genevisible; P51814; HS.
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 InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 17.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 17.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 17.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 18.
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 (rare variant found in patients with X-linked
FT intellectual disability; unknown pathological significance;
FT 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
