REQU_MOUSE
ID REQU_MOUSE Reviewed; 391 AA.
AC Q61103; Q3UNP5; Q60663; Q9QYA3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Zinc finger protein ubi-d4;
DE AltName: Full=Apoptosis response zinc finger protein;
DE AltName: Full=BRG1-associated factor 45D;
DE Short=BAF45D;
DE AltName: Full=D4, zinc and double PHD fingers family 2;
DE AltName: Full=Protein requiem;
GN Name=Dpf2; Synonyms=Baf45d, Req, Ubid4;
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 [GENOMIC DNA / MRNA].
RC STRAIN=CD-1;
RX PubMed=10602997; DOI=10.1007/s003350010014;
RA Mertsalov I.B., Kulikova D.A., Alimova-Kost M.V., Ninkina N.N.,
RA Korochkin L.I., Buchman V.L.;
RT "Structure and expression of two members of the d4 gene family in mouse.";
RL Mamm. Genome 11:72-74(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung, Mammary gland, Pancreas, and Thymus;
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 TISSUE=Colon, 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 NUCLEOTIDE SEQUENCE [MRNA] OF 6-391, AND FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=7961935; DOI=10.1016/s0021-9258(18)43910-5;
RA Gabig T.G., Mantel P.L., Rosli R., Crean C.D.;
RT "Requiem: a novel zinc finger gene essential for apoptosis in myeloid
RT cells.";
RL J. Biol. Chem. 269:29515-29519(1994).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=9680388; DOI=10.1007/s003359900840;
RA Gabig T.G., Crean C.D., Klenk A., Long H., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Quincey D., Parente F., Lespinasse F., Carle G.F.,
RA Gaudray P., Zhang C.X., Calender A., Hoeppener J., Kas K., Thakker R.V.,
RA Farnebo F., Teh B.T., Larsson C., Piehl F., Lagercrantz J., Khodaei S.,
RA Carson E., Weber G.;
RT "Expression and chromosomal localization of the Requiem gene.";
RL Mamm. Genome 9:660-665(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE.
RX PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T., Wu H.,
RA Aebersold R., Graef I.A., Crabtree G.R.;
RT "An essential switch in subunit composition of a chromatin remodeling
RT complex during neural development.";
RL Neuron 55:201-215(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND THR-176, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays an active role in transcriptional regulation by binding
CC modified histones H3 and H4. Is a negative regulator of myeloid
CC differentiation of hematopoietic progenitor cells (By similarity).
CC Might also have a role in the development and maturation of lymphoid
CC cells (PubMed:7961935). Involved in the regulation of non-canonical NF-
CC kappa-B pathway (By similarity). {ECO:0000250|UniProtKB:Q92785,
CC ECO:0000269|PubMed:7961935}.
CC -!- SUBUNIT: Interacts with the nucleosomes, in particular nucleosomes
CC bearing histone H3 crotonylated at 'Lys-14' (H3K14cr) for which DPF2
CC has high affinity. Also interacts (via PHD-type zinc finger domains)
CC with histone H3 butyrylated at 'Lys-14' (H3K14bu), histone H3
CC propionylated at 'Lys-14' (H3K14pr), and histone H3 acetylated at 'Lys-
CC 14' (H3K14ac). Interacts with histone H3 acetylated at 'Lys-9'
CC (H3K9ac), histone H3 di-methylated at 'Lys-9' (H3K9me2), and histone H3
CC tri-methylated at 'Lys-9' (H3K9me3). Interacts with histone H4
CC acetylated at 'Lys-12' (H4K12ac). Interacts with histone H4 acetylated
CC at 'Lys-16' (H4K16ac). Interacts with SWI/SNF complex components.
CC Interacts with SMARCA2, SMARCA4, SMARCB1 and SMARCD1. Interacts with
CC SMARCC1, SMARCC2 and ACTL6A. Interacts with RUNX1.
CC {ECO:0000250|UniProtKB:Q92785}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92785}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q92785}.
CC -!- TISSUE SPECIFICITY: In embryo, highest levels are seen in brain, eyes,
CC thymus and olfactory epithelium in nose, whereas several other tissues,
CC including the musculoskeletal system, show moderate expression. In
CC adult, higher expression in testis, medium in thymus and spleen, lower
CC in certain parts of the brain as the hippocampus. No expression in
CC adult heart, lung, liver, duodenum and kidney.
CC {ECO:0000269|PubMed:9680388}.
CC -!- DEVELOPMENTAL STAGE: Already detected at embryonic day 8.5. Expressed
CC ubiquitously throughout the developing spinal cord, brain and other
CC embryonic tissues at 10.5 dpc-16.5 dpc. {ECO:0000269|PubMed:17640523}.
CC -!- SIMILARITY: Belongs to the requiem/DPF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA64637.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH07188.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U43921; AAC52783.1; -; mRNA.
DR EMBL; AF108134; AAF21306.1; -; Genomic_DNA.
DR EMBL; AK004812; BAB23583.1; -; mRNA.
DR EMBL; AK138047; BAE23543.1; -; mRNA.
DR EMBL; AK144106; BAE25702.1; -; mRNA.
DR EMBL; AK144848; BAE26098.1; -; mRNA.
DR EMBL; AK144954; BAE26153.1; -; mRNA.
DR EMBL; BC007188; AAH07188.1; ALT_INIT; mRNA.
DR EMBL; BC012709; AAH12709.1; -; mRNA.
DR EMBL; U10435; AAA64637.1; ALT_INIT; mRNA.
DR CCDS; CCDS37892.1; -.
DR RefSeq; NP_001278007.1; NM_001291078.1.
DR RefSeq; NP_035392.1; NM_011262.5.
DR AlphaFoldDB; Q61103; -.
DR SMR; Q61103; -.
DR BioGRID; 202862; 10.
DR ComplexPortal; CPX-1251; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
DR DIP; DIP-59247N; -.
DR IntAct; Q61103; 7.
DR MINT; Q61103; -.
DR STRING; 10090.ENSMUSP00000120125; -.
DR iPTMnet; Q61103; -.
DR PhosphoSitePlus; Q61103; -.
DR SwissPalm; Q61103; -.
DR EPD; Q61103; -.
DR jPOST; Q61103; -.
DR MaxQB; Q61103; -.
DR PaxDb; Q61103; -.
DR PeptideAtlas; Q61103; -.
DR PRIDE; Q61103; -.
DR ProteomicsDB; 253212; -.
DR Antibodypedia; 15846; 333 antibodies from 38 providers.
DR DNASU; 19708; -.
DR Ensembl; ENSMUST00000136983; ENSMUSP00000120125; ENSMUSG00000024826.
DR GeneID; 19708; -.
DR KEGG; mmu:19708; -.
DR UCSC; uc008gfw.3; mouse.
DR CTD; 5977; -.
DR MGI; MGI:109529; Dpf2.
DR VEuPathDB; HostDB:ENSMUSG00000024826; -.
DR eggNOG; KOG1244; Eukaryota.
DR GeneTree; ENSGT00940000155070; -.
DR HOGENOM; CLU_038980_0_1_1; -.
DR InParanoid; Q61103; -.
DR OrthoDB; 708781at2759; -.
DR PhylomeDB; Q61103; -.
DR TreeFam; TF318971; -.
DR BioGRID-ORCS; 19708; 12 hits in 79 CRISPR screens.
DR ChiTaRS; Dpf2; mouse.
DR PRO; PR:Q61103; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q61103; protein.
DR Bgee; ENSMUSG00000024826; Expressed in embryonic post-anal tail and 288 other tissues.
DR ExpressionAtlas; Q61103; baseline and differential.
DR Genevisible; Q61103; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0071565; C:nBAF complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016514; C:SWI/SNF complex; IC:ComplexPortal.
DR GO; GO:0062072; F:H3K9me3 modified histone binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:1905454; P:negative regulation of myeloid progenitor cell differentiation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR025750; DPF1-3_N.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF14051; Requiem_N; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00355; ZnF_C2H2; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Chromatin regulator; Cytoplasm; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q92785"
FT CHAIN 2..391
FT /note="Zinc finger protein ubi-d4"
FT /id="PRO_0000168150"
FT ZN_FING 209..232
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 270..330
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 327..377
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 79..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q92785"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 172
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q92785"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92785"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92785"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92785"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92785"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92785"
FT CROSSLNK 107
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92785"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92785"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92785"
FT CROSSLNK 196
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92785"
FT CROSSLNK 281
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92785"
FT CONFLICT 176
FT /note="T -> R (in Ref. 4; AAA64637)"
FT /evidence="ECO:0000305"
FT CONFLICT 187..188
FT /note="Missing (in Ref. 3; AAH07188)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 44230 MW; 25598DBC80915BF2 CRC64;
MAAVVENVVK LLGEQYYKDA MEQCHNYNAR LCAERSVRLP FLDSQTGVAQ SNCYIWMEKR
HRGPGLASGQ LYSYPARRWR KKRRAHPPED PRLSFPSIKP DTDQTLKKEG LISQDGSSLE
ALLRTDPLEK RGAPDPRVDD DSLGEFPVSN SRARKRIIEP DDFLDDLDDE DYEEDTPKRR
GKGKSKSKGV SSARKKLDAS ILEDRDKPYA CDICGKRYKN RPGLSYHYAH SHLAEEEGED
KEDSRPPTPV SQRSEEQKSK KGPDGLALPN NYCDFCLGDS KINKKTGQPE ELVSCSDCGR
SGHPSCLQFT PVMMAAVKTY RWQCIECKCC NLCGTSENDD QLLFCDDCDR GYHMYCLTPS
MSEPPEGSWS CHLCLDLLKE KASIYQNQNS S
