ID ZN181_HUMAN Reviewed; 571 AA. AC Q2M3W8; B7ZKX3; Q49A75; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2006, sequence version 1. DT 27-MAR-2024, entry version 153. DE RecName: Full=Zinc finger protein 181; DE AltName: Full=HHZ181; GN Name=ZNF181; 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 [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Lung, 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109, AND IDENTIFICATION BY MASS RP 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 [4] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-126, AND IDENTIFICATION BY MASS RP 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). CC -!- FUNCTION: May be involved in transcriptional regulation. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q2M3W8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q2M3W8-2; Sequence=VSP_017824; CC Name=3; CC IsoId=Q2M3W8-3; Sequence=VSP_043416; CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. 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; AC020910; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC043228; AAH43228.1; -; mRNA. DR EMBL; BC104759; AAI04760.1; -; mRNA. DR EMBL; BC143442; AAI43443.1; -; mRNA. DR CCDS; CCDS32990.2; -. [Q2M3W8-1] DR CCDS; CCDS46043.1; -. [Q2M3W8-3] DR RefSeq; NP_001025168.2; NM_001029997.3. [Q2M3W8-1] DR RefSeq; NP_001139137.1; NM_001145665.1. [Q2M3W8-3] DR RefSeq; XP_005258906.1; XM_005258849.2. [Q2M3W8-1] DR RefSeq; XP_005258907.1; XM_005258850.2. [Q2M3W8-3] DR RefSeq; XP_006723246.1; XM_006723183.3. [Q2M3W8-1] DR RefSeq; XP_016882228.1; XM_017026739.1. [Q2M3W8-3] DR AlphaFoldDB; Q2M3W8; -. DR SMR; Q2M3W8; -. DR BioGRID; 130866; 6. DR IntAct; Q2M3W8; 8. DR STRING; 9606.ENSP00000420727; -. DR iPTMnet; Q2M3W8; -. DR PhosphoSitePlus; Q2M3W8; -. DR BioMuta; ZNF181; -. DR DMDM; 91208389; -. DR jPOST; Q2M3W8; -. DR MassIVE; Q2M3W8; -. DR PaxDb; 9606-ENSP00000420727; -. DR PeptideAtlas; Q2M3W8; -. DR ProteomicsDB; 61384; -. [Q2M3W8-1] DR ProteomicsDB; 61385; -. [Q2M3W8-2] DR ProteomicsDB; 61386; -. [Q2M3W8-3] DR Antibodypedia; 29203; 87 antibodies from 14 providers. DR DNASU; 339318; -. DR Ensembl; ENST00000459757.6; ENSP00000419435.1; ENSG00000197841.15. [Q2M3W8-3] DR Ensembl; ENST00000492450.3; ENSP00000420727.1; ENSG00000197841.15. [Q2M3W8-1] DR GeneID; 339318; -. DR KEGG; hsa:339318; -. DR MANE-Select; ENST00000492450.3; ENSP00000420727.1; NM_001029997.4; NP_001025168.2. DR UCSC; uc002nvu.4; human. [Q2M3W8-1] DR AGR; HGNC:12971; -. DR CTD; 339318; -. DR DisGeNET; 339318; -. DR GeneCards; ZNF181; -. DR HGNC; HGNC:12971; ZNF181. DR HPA; ENSG00000197841; Low tissue specificity. DR MIM; 606741; gene. DR neXtProt; NX_Q2M3W8; -. DR OpenTargets; ENSG00000197841; -. DR PharmGKB; PA37553; -. DR VEuPathDB; HostDB:ENSG00000197841; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000161431; -. DR HOGENOM; CLU_002678_44_5_1; -. DR InParanoid; Q2M3W8; -. DR OMA; KEDICDE; -. DR OrthoDB; 3120634at2759; -. DR PhylomeDB; Q2M3W8; -. DR TreeFam; TF341817; -. DR PathwayCommons; Q2M3W8; -. DR SignaLink; Q2M3W8; -. DR BioGRID-ORCS; 339318; 23 hits in 1175 CRISPR screens. DR ChiTaRS; ZNF181; human. DR GenomeRNAi; 339318; -. DR Pharos; Q2M3W8; Tdark. DR PRO; PR:Q2M3W8; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q2M3W8; Protein. DR Bgee; ENSG00000197841; Expressed in calcaneal tendon and 100 other cell types or tissues. DR ExpressionAtlas; Q2M3W8; 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; 11. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24381:SF390; B-CELL CLL_LYMPHOMA 6 MEMBER B PROTEIN; 1. DR PANTHER; PTHR24381; ZINC FINGER PROTEIN; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 11. DR SMART; SM00349; KRAB; 1. DR SMART; SM00614; ZnF_BED; 3. DR SMART; SM00355; ZnF_C2H2; 11. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11. PE 1: Evidence at protein level; KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..571 FT /note="Zinc finger protein 181" FT /id="PRO_0000230666" FT DOMAIN 4..76 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 237..259 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 265..287 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 293..315 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 321..343 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 349..371 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 377..399 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 405..427 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 433..455 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 461..483 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 489..511 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 517..539 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT CROSSLNK 109 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447" FT CROSSLNK 126 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..64 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017824" FT VAR_SEQ 44 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043416" SQ SEQUENCE 571 AA; 65842 MW; 8E69CEBA9B0E9720 CRC64; MPQVTFNDVA IDFTHEEWGW LSSAQRDLYK DVMVQNYENL VSVAGLSVTK PYVITLLEDG KEPWMMEKKL SKGMIPDWES RWENKELSTK KDNYDEDSPQ TVIIEKVVKQ SYEFSNSKKN LEYIEKLEGK HGSQVDHFRP AILTSRESPT ADSVYKYNIF RSTFHSKSTL SEPQKISAEG NSHKYDILKK NLPKKSVIKN EKVNGGKKLL NSNKSGAAFS QGKSLTLPQT CNREKIYTCS ECGKAFGKQS ILNRHWRIHT GEKPYECREC GKTFSHGSSL TRHLISHSGE KPYKCIECGK AFSHVSSLTN HQSTHTGEKP YECMNCGKSF SRVSHLIEHL RIHTQEKLYE CRICGKAFIH RSSLIHHQKI HTGEKPYECR ECGKAFCCSS HLTRHQRIHT MEKQYECNKC LKVFSSLSFL VQHQSIHTEE KPFECQKCRK SFNQLESLNM HLRNHIRLKP YECSICGKAF SHRSSLLQHH RIHTGEKPYE CIKCGKTFSC SSNLTVHQRI HTGEKPYKCN ECGKAFSKGS NLTAHQRVHN GEKPNSVVSV EKPLDYMNHY TCEKSYRRET V //