ZN689_HUMAN
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 03-AUG-2022, entry version 155.
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}.
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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; 98.
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; Q96CS4; -.
DR PeptideAtlas; Q96CS4; -.
DR PRIDE; Q96CS4; -.
DR ProteomicsDB; 76215; -.
DR Antibodypedia; 27365; 79 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 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; 1318335at2759; -.
DR PhylomeDB; Q96CS4; -.
DR TreeFam; TF336948; -.
DR PathwayCommons; Q96CS4; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q96CS4; -.
DR BioGRID-ORCS; 115509; 25 hits in 1100 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 172 other tissues.
DR Genevisible; Q96CS4; 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 GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
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; 9.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
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
