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ZN689_MOUSE
ID   ZN689_MOUSE             Reviewed;         500 AA.
AC   Q8BKK5; Q8C1C6;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Zinc finger protein 689;
GN   Name=Znf689; Synonyms=Zfp689;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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).
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; AK028417; BAC25939.1; -; mRNA.
DR   EMBL; AK051667; BAC34710.1; -; mRNA.
DR   EMBL; BC052084; AAH52084.1; -; mRNA.
DR   CCDS; CCDS21867.1; -.
DR   RefSeq; NP_780372.2; NM_175163.3.
DR   AlphaFoldDB; Q8BKK5; -.
DR   SMR; Q8BKK5; -.
DR   STRING; 10090.ENSMUSP00000056610; -.
DR   iPTMnet; Q8BKK5; -.
DR   PhosphoSitePlus; Q8BKK5; -.
DR   PaxDb; Q8BKK5; -.
DR   PRIDE; Q8BKK5; -.
DR   ProteomicsDB; 302092; -.
DR   Antibodypedia; 27365; 79 antibodies from 19 providers.
DR   DNASU; 71131; -.
DR   Ensembl; ENSMUST00000053392; ENSMUSP00000056610; ENSMUSG00000048921.
DR   GeneID; 71131; -.
DR   KEGG; mmu:71131; -.
DR   UCSC; uc009jvl.2; mouse.
DR   CTD; 71131; -.
DR   MGI; MGI:1918381; Zfp689.
DR   VEuPathDB; HostDB:ENSMUSG00000048921; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162326; -.
DR   HOGENOM; CLU_002678_13_1_1; -.
DR   InParanoid; Q8BKK5; -.
DR   OMA; QSHKCAQ; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q8BKK5; -.
DR   TreeFam; TF336948; -.
DR   Reactome; R-MMU-212436; Generic Transcription Pathway.
DR   BioGRID-ORCS; 71131; 0 hits in 72 CRISPR screens.
DR   PRO; PR:Q8BKK5; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q8BKK5; protein.
DR   Bgee; ENSMUSG00000048921; Expressed in cortical plate and 131 other tissues.
DR   ExpressionAtlas; Q8BKK5; baseline and differential.
DR   Genevisible; Q8BKK5; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
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; 6.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE   2: Evidence at transcript 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_0000234009"
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..483
FT                   /note="C2H2-type 12; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          105..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..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:0000250|UniProtKB:Q96CS4"
FT   CONFLICT        450
FT                   /note="L -> V (in Ref. 1; BAC25939)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   500 AA;  57082 MW;  5BF3B828B151E4D2 CRC64;
     MAPPSAPLLL RAVGEAGPTR KRGRRPRALK FVDVAVYFSS EEWGCLQPAQ RTLYRDVMRE
     TYGLLGALGC AGPKPALISW LERNTDDWEP AALDPQEYRR WVTFQRKTRS KQKTEEKDVF
     PPKEAPRKGK RGRKPSKPRL IPRQTSGGPI CPDCGCTFPD HLALESHKCA QNLKKPYPCP
     DCGRRFSYPS LLVSHRRAHS GECPYVCDQC GKRFSQRKNL SQHQVIHTGE KPYHCPDCGR
     CFRRSRSLAN HRTTHTGEKP HQCPSCGRRF AYPSLLAIHQ RTHTGEKPYT CLECSRRFRQ
     RTALVIHQRI HTGEKPYPCP DCERRFSSSS RLVSHRRVHS GERPYACENC EARFSQRSTL
     LQHQLLHTGE KPYPCPDCGR AFRRSGSLAI HRSTHTEEKL HACDDCGRRF AYPSLLASHR
     RVHSGERPYA CDLCSKRFAQ WSHLSQHQLL HTGEKPFPCL ECGRCFRQRW SLAVHKCCPN
     TPNGSPRPLI GGPSQRSSAL
 
 
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