RBAK_MOUSE
ID RBAK_MOUSE Reviewed; 711 AA.
AC Q8BQC8; Q6PB38; Q9JKU4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=RB-associated KRAB zinc finger protein;
DE AltName: Full=RB-associated KRAB repressor;
DE AltName: Full=Zinc finger protein 769;
GN Name=Rbak; Synonyms=Znf769;
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=Embryo;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-689, AND INTERACTION WITH RB1.
RX PubMed=10702291; DOI=10.1074/jbc.275.10.7212;
RA Skapek S.X., Jansen D., Wei T.-F., McDermott T., Huang W., Olson E.N.,
RA Lee E.Y.-H.P.;
RT "Cloning and characterization of a novel Kruppel-associated box family
RT transcriptional repressor that interacts with the retinoblastoma gene
RT product, RB.";
RL J. Biol. Chem. 275:7212-7223(2000).
CC -!- FUNCTION: May repress E2F-dependent transcription. May promote AR-
CC dependent transcription. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with AR (By similarity). May also interact with
CC other nuclear hormone receptors such as NR3C1/GR (By similarity).
CC Interacts with RB1. {ECO:0000250, ECO:0000269|PubMed:10702291}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK051009; BAC34495.1; -; mRNA.
DR EMBL; AF226870; AAF43390.1; -; mRNA.
DR CCDS; CCDS19835.1; -.
DR RefSeq; NP_001038947.1; NM_001045482.2.
DR RefSeq; NP_067301.1; NM_021326.3.
DR RefSeq; XP_006504787.1; XM_006504724.3.
DR AlphaFoldDB; Q8BQC8; -.
DR SMR; Q8BQC8; -.
DR BioGRID; 208328; 25.
DR STRING; 10090.ENSMUSP00000128731; -.
DR iPTMnet; Q8BQC8; -.
DR PhosphoSitePlus; Q8BQC8; -.
DR MaxQB; Q8BQC8; -.
DR PaxDb; Q8BQC8; -.
DR PRIDE; Q8BQC8; -.
DR ProteomicsDB; 255113; -.
DR Antibodypedia; 11262; 153 antibodies from 27 providers.
DR DNASU; 57782; -.
DR Ensembl; ENSMUST00000049861; ENSMUSP00000059273; ENSMUSG00000061898.
DR Ensembl; ENSMUST00000165318; ENSMUSP00000128731; ENSMUSG00000061898.
DR GeneID; 57782; -.
DR KEGG; mmu:57782; -.
DR UCSC; uc009ajp.2; mouse.
DR CTD; 57786; -.
DR MGI; MGI:1927369; Rbak.
DR VEuPathDB; HostDB:ENSMUSG00000061898; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154303; -.
DR HOGENOM; CLU_002678_0_12_1; -.
DR InParanoid; Q8BQC8; -.
DR OMA; YECNQNG; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8BQC8; -.
DR TreeFam; TF350803; -.
DR BioGRID-ORCS; 57782; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q8BQC8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BQC8; protein.
DR Bgee; ENSMUSG00000061898; Expressed in metanephric cortical collecting duct and 223 other tissues.
DR Genevisible; Q8BQC8; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:0000977; F:RNA polymerase II transcription 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 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; 14.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE 1: Evidence at protein level;
KW Activator; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..711
FT /note="RB-associated KRAB zinc finger protein"
FT /id="PRO_0000316977"
FT DOMAIN 8..79
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 258..280
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 286..308
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 314..336
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 342..364
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 370..392
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 398..420
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 426..448
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 454..476
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 508..530
FT /note="C2H2-type 9; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 536..558
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 564..586
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 592..614
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 620..642
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 648..670
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 676..698
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 170..257
FT /note="Required for interaction with RB1"
FT /evidence="ECO:0000250"
FT REGION 414..711
FT /note="Interaction with AR"
FT /evidence="ECO:0000250"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYW8"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYW8"
FT CROSSLNK 312
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYW8"
FT CROSSLNK 354
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYW8"
FT CROSSLNK 534
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYW8"
SQ SEQUENCE 711 AA; 81675 MW; 62896A7C42A105E9 CRC64;
MSRSKGPLSF KDVAVAFSQE EWQQLDPEER TTYRDVMLET YSNLVSVGYD VTKPNMIIKL
EQGEEPWTVE GDRHAQRHLE ISKVYDPREG IEEIGEKHLQ CDDDPYCWRA EKGAAFDEAY
TLETALISPS SGAHSCVSCG ETLESVSELI SSDGSYALEK PSMCFECGKA YGESLEDFNQ
DEGNSSQHDE NILQKVTILE KPFAYECMEA LDSESVFMAR ERAYMGEKPY DWGDSGPDFI
QMSDFSTYPR SQMELKPFEC TQCGKSFCKK SKFIIHQRAH TGEKPYACSV CGKSFSQKGT
LTVHRRSHLE EKPYKCNECG KTFCQKLHLT QHQRTHSGEK PYECSECGKS FCQKTHLTLH
QRNHSGERPY PCNECGKSFS RKSALNDHQR THTGEKLYKC NECGKSYYRK STLITHQRTH
TGEKPYQCSE CGKFFSRVSY LTIHYRSHLE EKPYECTECG KTFNLNSAFI RHWKVHAEER
VQECGECGKP SPLQCAPDHT GDLGEKRYEC NECGKTFLDS SAFHRHQSVP EGEKTYECNI
CGKSFSDSSC YTVHYRGHSE EKPFGCSECG KTFSHNSSLF RHQRVHTGEK PYECYECGKF
FSQKSYLTIH HRIHSGEKPY ECSKCGKVFS RMSNLTVHYR SHSGEKPYEC NECGKVFSQK
SYLTVHYRTH SGEKPYECNE CGKKFHHRSA FNSHQRIHKR GTVNVLTVEK L
