ID ZN561_HUMAN Reviewed; 486 AA. AC Q8N587; B4E2Q8; Q6PJS0; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 2. DT 27-MAR-2024, entry version 172. DE RecName: Full=Zinc finger protein 561; GN Name=ZNF561; 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 MRNA] (ISOFORM 2). RC TISSUE=Trachea; 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 [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon, and Skin; 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 [4] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-273 AND LYS-424, 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). CC -!- FUNCTION: May be involved in transcriptional regulation. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8N587-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N587-2; Sequence=VSP_055964; CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH12144.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAH32668.1; Type=Erroneous initiation; Evidence={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; AK304383; BAG65220.1; -; mRNA. DR EMBL; AC008759; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC012144; AAH12144.1; ALT_SEQ; mRNA. DR EMBL; BC032668; AAH32668.1; ALT_INIT; mRNA. DR CCDS; CCDS12216.2; -. [Q8N587-1] DR RefSeq; NP_001317294.1; NM_001330365.1. DR RefSeq; NP_689502.2; NM_152289.2. [Q8N587-1] DR RefSeq; XP_005260207.1; XM_005260150.2. [Q8N587-1] DR RefSeq; XP_016882968.1; XM_017027479.1. DR RefSeq; XP_016882970.1; XM_017027481.1. DR RefSeq; XP_016882971.1; XM_017027482.1. DR AlphaFoldDB; Q8N587; -. DR SMR; Q8N587; -. DR BioGRID; 125005; 11. DR IntAct; Q8N587; 2. DR STRING; 9606.ENSP00000303915; -. DR GlyGen; Q8N587; 1 site. DR iPTMnet; Q8N587; -. DR PhosphoSitePlus; Q8N587; -. DR BioMuta; ZNF561; -. DR DMDM; 82582592; -. DR EPD; Q8N587; -. DR jPOST; Q8N587; -. DR MassIVE; Q8N587; -. DR MaxQB; Q8N587; -. DR PaxDb; 9606-ENSP00000303915; -. DR PeptideAtlas; Q8N587; -. DR ProteomicsDB; 5846; -. DR ProteomicsDB; 72021; -. [Q8N587-1] DR Antibodypedia; 25053; 42 antibodies from 15 providers. DR DNASU; 93134; -. DR Ensembl; ENST00000302851.8; ENSP00000303915.3; ENSG00000171469.11. [Q8N587-1] DR GeneID; 93134; -. DR KEGG; hsa:93134; -. DR MANE-Select; ENST00000302851.8; ENSP00000303915.3; NM_152289.3; NP_689502.2. DR UCSC; uc002mlu.4; human. [Q8N587-1] DR AGR; HGNC:28684; -. DR CTD; 93134; -. DR DisGeNET; 93134; -. DR GeneCards; ZNF561; -. DR HGNC; HGNC:28684; ZNF561. DR HPA; ENSG00000171469; Low tissue specificity. DR neXtProt; NX_Q8N587; -. DR OpenTargets; ENSG00000171469; -. DR PharmGKB; PA134935834; -. DR VEuPathDB; HostDB:ENSG00000171469; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000162984; -. DR InParanoid; Q8N587; -. DR OMA; IKSYKCV; -. DR OrthoDB; 4746561at2759; -. DR PhylomeDB; Q8N587; -. DR TreeFam; TF341966; -. DR PathwayCommons; Q8N587; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR SignaLink; Q8N587; -. DR BioGRID-ORCS; 93134; 14 hits in 1142 CRISPR screens. DR ChiTaRS; ZNF561; human. DR GenomeRNAi; 93134; -. DR Pharos; Q8N587; Tdark. DR PRO; PR:Q8N587; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q8N587; Protein. DR Bgee; ENSG00000171469; Expressed in buccal mucosa cell and 187 other cell types or tissues. DR ExpressionAtlas; Q8N587; 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; 9. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23226; ZINC FINGER AND SCAN DOMAIN-CONTAINING; 1. DR PANTHER; PTHR23226:SF411; ZINC FINGER PROTEIN 426; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 8. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 9. 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; 8. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10. DR Genevisible; Q8N587; HS. 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..486 FT /note="Zinc finger protein 561" FT /id="PRO_0000047650" FT DOMAIN 41..112 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 118..140 FT /note="C2H2-type 1; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 169..191 FT /note="C2H2-type 2; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 197..219 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 223..247 FT /note="C2H2-type 4; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 253..275 FT /note="C2H2-type 5; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 281..303 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 309..331 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 337..359 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 365..387 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 393..415 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 421..443 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 449..471 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT CROSSLNK 273 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 424 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..136 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055964" SQ SEQUENCE 486 AA; 55197 MW; 108E8C7BBAEC764C CRC64; MAAIYLSRGF FSREPICPFE EKTKVERMVE DYLASGYQDS VTFDDVAVDF TPEEWALLDT TEKYLYRDVM LENYMNLASV EWEIQPRTKR SSLQQGFLKN QIFSGIQMTR GYSGWKLCDC KNCGEVFREQ FCLKTHMRVQ NGGNTSEGNC YGKDTLSVHK EASTGQELSK FNPCGKVFTL TPGLAVHLEV LNARQPYKCK ECGKGFKYFA SLDNHMGIHT DEKLCEFQEY GRAVTASSHL KQCVAVHTGK KSKKTKKCGK SFTNFSQLYA PVKTHKGEKS FECKECGRSF RNSSCLNDHI QIHTGIKPHK CTYCGKAFTR STQLTEHVRT HTGIKPYECK ECGQAFAQYS GLSIHIRSHS GKKPYQCKEC GKAFTTSTSL IQHTRIHTGE KPYECVECGK TFITSSRRSK HLKTHSGEKP FVCKICGKAF LYSSRLNVHL RTHTGEKPFV CKECGKAFAV SSRLSRHERI HTGEKPYECK DMSVTI //