ZBED4_MOUSE
ID ZBED4_MOUSE Reviewed; 1168 AA.
AC Q80WQ9; Q3UPJ9; Q80TV3; Q8R329;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Zinc finger BED domain-containing protein 4;
GN Name=Zbed4; Synonyms=Kiaa0637;
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 TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Limb, and Mammary tumor;
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19369242; DOI=10.1167/iovs.08-2751;
RA Saghizadeh M., Akhmedov N.B., Yamashita C.K., Gribanova Y., Theendakara V.,
RA Mendoza E., Nelson S.F., Ljubimov A.V., Farber D.B.;
RT "ZBED4, a BED-type zinc-finger protein in the cones of the human retina.";
RL Invest. Ophthalmol. Vis. Sci. 50:3580-3588(2009).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22693546; DOI=10.1371/journal.pone.0035317;
RA Mokhonov V.V., Theendakara V.P., Gribanova Y.E., Ahmedli N.B., Farber D.B.;
RT "Sequence-specific binding of recombinant Zbed4 to DNA: insights into Zbed4
RT participation in gene transcription and its association with other
RT proteins.";
RL PLoS ONE 7:e35317-e35317(2012).
CC -!- FUNCTION: Transcriptional regulator that binds to poly-guanine tracts
CC in gene promoters and activates transcription (By similarity). Able to
CC bind single- and double-stranded DNA and RNA (PubMed:22693546).
CC {ECO:0000250|UniProtKB:O75132, ECO:0000269|PubMed:22693546}.
CC -!- SUBUNIT: Homodimer; via C-terminus (By similarity). Interacts with MYH9
CC (By similarity). Interacts with SAFB/SAFB1 (By similarity).
CC {ECO:0000250|UniProtKB:O75132}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75132}. Nucleus
CC {ECO:0000269|PubMed:19369242}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:O75132}.
CC -!- TISSUE SPECIFICITY: Expressed in the thymus (PubMed:19369242). In the
CC retina, expressed in the cone photoreceptors (PubMed:19369242,
CC PubMed:22693546). {ECO:0000269|PubMed:19369242,
CC ECO:0000269|PubMed:22693546}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65617.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305};
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DR EMBL; AK122335; BAC65617.1; ALT_SEQ; Transcribed_RNA.
DR EMBL; AK143488; BAE25396.1; -; mRNA.
DR EMBL; BC026763; AAH26763.1; -; mRNA.
DR EMBL; BC052174; AAH52174.1; -; mRNA.
DR CCDS; CCDS27731.1; -.
DR RefSeq; NP_852077.1; NM_181412.3.
DR RefSeq; XP_006520903.1; XM_006520840.3.
DR RefSeq; XP_006520904.1; XM_006520841.3.
DR AlphaFoldDB; Q80WQ9; -.
DR SMR; Q80WQ9; -.
DR STRING; 10090.ENSMUSP00000035437; -.
DR iPTMnet; Q80WQ9; -.
DR PhosphoSitePlus; Q80WQ9; -.
DR EPD; Q80WQ9; -.
DR jPOST; Q80WQ9; -.
DR PaxDb; Q80WQ9; -.
DR PeptideAtlas; Q80WQ9; -.
DR PRIDE; Q80WQ9; -.
DR ProteomicsDB; 275336; -.
DR Antibodypedia; 59180; 12 antibodies from 7 providers.
DR Ensembl; ENSMUST00000041297; ENSMUSP00000035437; ENSMUSG00000034333.
DR GeneID; 223773; -.
DR KEGG; mmu:223773; -.
DR UCSC; uc007xem.1; mouse.
DR CTD; 9889; -.
DR MGI; MGI:2682302; Zbed4.
DR VEuPathDB; HostDB:ENSMUSG00000034333; -.
DR eggNOG; KOG1121; Eukaryota.
DR GeneTree; ENSGT00940000161365; -.
DR HOGENOM; CLU_006260_0_0_1; -.
DR InParanoid; Q80WQ9; -.
DR OMA; HMWRAHK; -.
DR OrthoDB; 223749at2759; -.
DR PhylomeDB; Q80WQ9; -.
DR TreeFam; TF322818; -.
DR BioGRID-ORCS; 223773; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Zbed4; mouse.
DR PRO; PR:Q80WQ9; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q80WQ9; protein.
DR Bgee; ENSMUSG00000034333; Expressed in dorsal pancreas and 246 other tissues.
DR Genevisible; Q80WQ9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR InterPro; IPR008906; HATC_C_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR003656; Znf_BED.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR Pfam; PF02892; zf-BED; 4.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50808; ZF_BED; 4.
PE 2: Evidence at transcript level;
KW Activator; Cytoplasm; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1168
FT /note="Zinc finger BED domain-containing protein 4"
FT /id="PRO_0000391794"
FT ZN_FING 114..171
FT /note="BED-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT ZN_FING 284..341
FT /note="BED-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT ZN_FING 456..512
FT /note="BED-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT ZN_FING 557..614
FT /note="BED-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT REGION 22..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1168
FT /note="Required for homodimerization and nuclear
FT accumulation"
FT /evidence="ECO:0000250|UniProtKB:O75132"
FT COMPBIAS 372..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 477
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 480
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 500
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 578
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 581
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 602
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 607
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75132"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75132"
FT CROSSLNK 489
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75132"
FT CONFLICT 743
FT /note="L -> P (in Ref. 1; BAC65617)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1168 AA; 130402 MW; 57A65CC20B6FE0BC CRC64;
MEDKQETCPK GDSDFVSDKV NFKTEEDDDQ TPCHSLEQVD FKSESEDMRQ TDSGDEQADI
RAASCACQPS GKFLAAESED DYGSLFSQYS STLYSVAMEA VTQSLLSSRH ISSRKKSPAW
KHFFISPRDS TKAICTYCMK EFSRGKNEKD LSTSCLMRHV RRAHPTKLIQ ENGSLSAGSS
FSPPSLLLPP QPADVGDLST VLSPVRLVQK MAPKIPSPDQ IMEESVTVVS SEELSSDVSV
TEKYSREEAL AGSSPNLSML HYDDASETMA DRNLSLPKST SGSRRRSAVW KHFYLSPLDS
SKAVCVHCMN EFSRGKNGKD LGTSCLIRHM WRAHRSIVLQ ENGGNTGIPP LYPMPPTLLP
ALLPPEGDLN SASLSPGKQV KESPSASSSP ERLPEDLSSH TNPGDVSRED VSMLSSSDDL
GEASVVSSPE KQPADTVNPR FESGTVFQQN KKVMRRLKSE VWHHFSLAPM DSLKAVCRYC
SCVISRGKKG DVGTSCLMRH LYRRHPEVVG NQKDFLGASL ANSPYATLAS AESSSKLTDL
PAVVRKNHQG VFPTNSKKTS KLWNHFSICS ADSTKVVCLH CGRTISRGKK PTNLGTSCLL
RHLQRFHGHV LKNDVSEATL SRSPGIRRPL GIELSGPSSF RDSTEKFYDS HPVAKKITSL
IAEMIALDLQ PYSLVDNVGF NRLLEYLKPQ YSLPSPSYFS RTAIPGMYDN VKQIIMSHLK
EAESGVVHFT SGIWMSSQTR EYLTLTAHWV TFASAVRPHC EDHHCSALLD VSQIDCDYSG
NSIQKQLECW WEAWVTSIGL QIGITVTDNP SIGKMLSEGE HSSVQCFSHT VNLIVSEAIK
SQRMVQNLLS IARKLCERVH RSPRAREKLA ELQKEYELPQ HQLIQDVPSK WSTSFHMLER
LIEQKRAVNE VSIECNFREL ISCDQWEVMQ SVCHVLRPFD AASREMSAHM STLSQVIPMI
HILSRKVEML FGETMGIDTM LKSLKEAMAS RLSATLHDPR YIFATLLDPR YKASLFTEEE
AEQYRQDLIR ELEILNSTSE DTATSNGCDS GSPLKDTGTE ESLWSLAPIK RDQREKLPED
MVLAYLEEEV LEHSCDPLTY WNLKRSSWPG LSTLAVRFLG CPPSTVPSEK LFSTPMDAGS
FGQPRLMMEH FEKLIFLKVN LPLICFQY
