ID ZN689_HUMAN Reviewed; 500 AA. AC Q96CS4; Q658J5; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 164. DE RecName: Full=Zinc finger protein 689; GN Name=ZNF689; 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]. RC TISSUE=Teratocarcinoma; 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 MRNA]. RC TISSUE=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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-500. RC TISSUE=Melanoma; 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., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-455, 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 -!- 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; AK074896; BAC11275.1; -; mRNA. DR EMBL; BC014000; AAH14000.1; -; mRNA. DR EMBL; AL834299; CAH56363.1; -; mRNA. DR CCDS; CCDS10686.1; -. DR RefSeq; NP_612456.1; NM_138447.2. DR AlphaFoldDB; Q96CS4; -. DR SMR; Q96CS4; -. DR BioGRID; 125436; 100. DR IntAct; Q96CS4; 17. DR STRING; 9606.ENSP00000287461; -. DR iPTMnet; Q96CS4; -. DR PhosphoSitePlus; Q96CS4; -. DR BioMuta; ZNF689; -. DR DMDM; 74760770; -. DR EPD; Q96CS4; -. DR MassIVE; Q96CS4; -. DR MaxQB; Q96CS4; -. DR PaxDb; 9606-ENSP00000287461; -. DR PeptideAtlas; Q96CS4; -. DR ProteomicsDB; 76215; -. DR Pumba; Q96CS4; -. DR Antibodypedia; 27365; 91 antibodies from 19 providers. DR DNASU; 115509; -. DR Ensembl; ENST00000287461.8; ENSP00000287461.3; ENSG00000156853.13. DR GeneID; 115509; -. DR KEGG; hsa:115509; -. DR MANE-Select; ENST00000287461.8; ENSP00000287461.3; NM_138447.3; NP_612456.1. DR UCSC; uc002dyx.5; human. DR AGR; HGNC:25173; -. DR CTD; 115509; -. DR DisGeNET; 115509; -. DR GeneCards; ZNF689; -. DR HGNC; HGNC:25173; ZNF689. DR HPA; ENSG00000156853; Tissue enhanced (testis). DR MIM; 618033; gene. DR neXtProt; NX_Q96CS4; -. DR OpenTargets; ENSG00000156853; -. DR PharmGKB; PA142670488; -. DR VEuPathDB; HostDB:ENSG00000156853; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000162326; -. DR HOGENOM; CLU_002678_13_1_1; -. DR InParanoid; Q96CS4; -. DR OMA; QSHKCAQ; -. DR OrthoDB; 5250811at2759; -. DR PhylomeDB; Q96CS4; -. DR TreeFam; TF336948; -. DR PathwayCommons; Q96CS4; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR SignaLink; Q96CS4; -. DR BioGRID-ORCS; 115509; 26 hits in 1178 CRISPR screens. DR ChiTaRS; ZNF689; human. DR GenomeRNAi; 115509; -. DR Pharos; Q96CS4; Tdark. DR PRO; PR:Q96CS4; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q96CS4; Protein. DR Bgee; ENSG00000156853; Expressed in oocyte and 173 other cell types or tissues. 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 GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl. 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; PTHR23232; KRAB DOMAIN C2H2 ZINC FINGER; 1. DR PANTHER; PTHR23232:SF69; ZINC FINGER PROTEIN 688; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 10. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 12. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 7. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11. DR Genevisible; Q96CS4; HS. PE 1: Evidence at protein level; KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome; KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..500 FT /note="Zinc finger protein 689" FT /id="PRO_0000234008" FT DOMAIN 29..100 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 149..171 FT /note="C2H2-type 1; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 177..199 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 205..227 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 233..255 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 261..283 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 289..311 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 317..339 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 345..367 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 373..395 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 401..423 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 429..451 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 457..477 FT /note="C2H2-type 12; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 90..146 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 109..126 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CROSSLNK 455 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" SQ SEQUENCE 500 AA; 56907 MW; 921B675BBD40EBAE CRC64; MAPPSAPLPA QGPGKARPSR KRGRRPRALK FVDVAVYFSP EEWGCLRPAQ RALYRDVMRE TYGHLGALGC AGPKPALISW LERNTDDWEP AALDPQEYPR GLTVQRKSRT RKKNGEKEVF PPKEAPRKGK RGRRPSKPRL IPRQTSGGPI CPDCGCTFPD HQALESHKCA QNLKKPYPCP DCGRRFSYPS LLVSHRRAHS GECPYVCDQC GKRFSQRKNL SQHQVIHTGE KPYHCPDCGR CFRRSRSLAN HRTTHTGEKP HQCPSCGRRF AYPSLLAIHQ RTHTGEKPYT CLECNRRFRQ RTALVIHQRI HTGEKPYPCP DCERRFSSSS RLVSHRRVHS GERPYACEHC EARFSQRSTL LQHQLLHTGE KPYPCPDCGR AFRRSGSLAI HRSTHTEEKL HACDDCGRRF AYPSLLASHR RVHSGERPYA CDLCSKRFAQ WSHLAQHQLL HTGEKPFPCL ECGRCFRQRW SLAVHKCSPK APNCSPRSAI GGSSQRGNAH //