PF21A_MOUSE
ID PF21A_MOUSE Reviewed; 688 AA.
AC Q6ZPK0; A2AHG2; Q6XVG0; Q80Z33; Q8CAZ4; Q8VEC8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=PHD finger protein 21A {ECO:0000305};
DE AltName: Full=BHC80a;
DE AltName: Full=BRAF35-HDAC complex protein BHC80;
DE Short=mBHC80;
GN Name=Phf21a {ECO:0000312|MGI:MGI:2384756}; Synonyms=Bhc80, Kiaa1696, Pftf1;
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] (ISOFORMS 3; 4; 5; 6; 7; 8 AND 9),
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=15325272; DOI=10.1016/j.bbrc.2004.07.163;
RA Iwase S., Januma A., Miyamoto K., Shono N., Honda A., Yanagisawa J.,
RA Baba T.;
RT "Characterization of BHC80 in BRAF-HDAC complex, involved in neuron-
RT specific gene repression.";
RL Biochem. Biophys. Res. Commun. 322:601-608(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=FVB/N-3; TISSUE=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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 119-303 (ISOFORMS 3/6/8).
RC STRAIN=C57BL/6J;
RA Herrera L., Ottolenghi C., Forabosco A., Schlessinger D.;
RT "Mouse ovary and testis gene cohorts and RNA and protein developmental
RT markers from microarray expression profiling.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the BHC complex, a corepressor complex that
CC represses transcription of neuron-specific genes in non-neuronal cells.
CC The BHC complex is recruited at RE1/NRSE sites by REST and acts by
CC deacetylating and demethylating specific sites on histones, thereby
CC acting as a chromatin modifier. In the BHC complex, it may act as a
CC scaffold. Inhibits KDM1A-mediated demethylation of 'Lys-4' of histone
CC H3 in vitro, suggesting a role in demethylation regulation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a BHC histone deacetylase complex that contains
CC HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The
CC BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. In
CC the complex, it interacts directly with HDAC1, HDAC2, HMG20B/BRAF35,
CC KDM1A and RCOR1/CoREST (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15325272}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=Q6ZPK0-10; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZPK0-2; Sequence=VSP_060157;
CC Name=3; Synonyms=BHC80-6(AIF2+5);
CC IsoId=Q6ZPK0-3; Sequence=VSP_060158, VSP_060159;
CC Name=4;
CC IsoId=Q6ZPK0-4; Sequence=VSP_060156, VSP_060160;
CC Name=5; Synonyms=BHC80-1(AIF1+3);
CC IsoId=Q6ZPK0-5; Sequence=VSP_060156, VSP_060159, VSP_060160;
CC Name=6; Synonyms=BHC80-4(AIF2+3);
CC IsoId=Q6ZPK0-6; Sequence=VSP_060158, VSP_060159, VSP_060160;
CC Name=7; Synonyms=BHC80-2(AIF1+4);
CC IsoId=Q6ZPK0-7; Sequence=VSP_060156, VSP_060159, VSP_060161;
CC Name=8; Synonyms=BHC80-5(AIF2+4);
CC IsoId=Q6ZPK0-8; Sequence=VSP_060158, VSP_060159, VSP_060161;
CC Name=9; Synonyms=BHC80-3(AIF1+5);
CC IsoId=Q6ZPK0-9; Sequence=VSP_060156, VSP_060159;
CC -!- TISSUE SPECIFICITY: Expressed in the brain and testis. Weakly or not
CC expressed in other tissues tested. Localized throughout the central
CC nervous system (CNS) in brain, including the cerebellum, hippocampus,
CC and cortex. Notably present in neuronal cells of granular cell layer
CC and dentate gyrus in cerebellum and hippocampus, respectively. In the
CC seminiferous tubules, the signals it is present strongly in
CC spermatocytes, and weakly in spermatogonia and round spermatids. In
CC some cases, it is also observed solely in spermatocytes (at protein
CC level). {ECO:0000269|PubMed:15325272}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98234.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB105178; BAC65327.1; -; mRNA.
DR EMBL; AK129424; BAC98234.1; ALT_FRAME; Transcribed_RNA.
DR EMBL; AK037174; BAC29735.1; -; mRNA.
DR EMBL; AL691462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019181; AAH19181.1; -; mRNA.
DR EMBL; AY206982; AAP43962.1; -; mRNA.
DR CCDS; CCDS16442.1; -. [Q6ZPK0-4]
DR CCDS; CCDS50644.1; -. [Q6ZPK0-10]
DR CCDS; CCDS50645.1; -. [Q6ZPK0-2]
DR RefSeq; NP_001103161.1; NM_001109691.1.
DR RefSeq; NP_620094.2; NM_138755.2.
DR RefSeq; XP_006499043.1; XM_006498980.3.
DR RefSeq; XP_017172037.1; XM_017316548.1.
DR AlphaFoldDB; Q6ZPK0; -.
DR BMRB; Q6ZPK0; -.
DR SMR; Q6ZPK0; -.
DR BioGRID; 228685; 3.
DR STRING; 10090.ENSMUSP00000088074; -.
DR iPTMnet; Q6ZPK0; -.
DR PhosphoSitePlus; Q6ZPK0; -.
DR jPOST; Q6ZPK0; -.
DR MaxQB; Q6ZPK0; -.
DR PeptideAtlas; Q6ZPK0; -.
DR PRIDE; Q6ZPK0; -.
DR ProteomicsDB; 287676; -. [Q6ZPK0-10]
DR ProteomicsDB; 287677; -. [Q6ZPK0-2]
DR ProteomicsDB; 287678; -. [Q6ZPK0-3]
DR ProteomicsDB; 287679; -. [Q6ZPK0-4]
DR ProteomicsDB; 287680; -. [Q6ZPK0-5]
DR ProteomicsDB; 287681; -. [Q6ZPK0-6]
DR ProteomicsDB; 287682; -. [Q6ZPK0-7]
DR ProteomicsDB; 287683; -. [Q6ZPK0-8]
DR ProteomicsDB; 287684; -. [Q6ZPK0-9]
DR ProteomicsDB; 329183; -.
DR DNASU; 192285; -.
DR GeneID; 192285; -.
DR KEGG; mmu:192285; -.
DR UCSC; uc008kxl.2; mouse.
DR CTD; 51317; -.
DR MGI; MGI:2384756; Phf21a.
DR eggNOG; KOG0383; Eukaryota.
DR InParanoid; Q6ZPK0; -.
DR TreeFam; TF331518; -.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 192285; 3 hits in 111 CRISPR screens.
DR ChiTaRS; Phf21a; mouse.
DR PRO; PR:Q6ZPK0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6ZPK0; protein.
DR GO; GO:1990391; C:DNA repair complex; ISO:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0001967; P:suckling behavior; IMP:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
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 SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Coiled coil; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..688
FT /note="PHD finger protein 21A"
FT /id="PRO_0000226768"
FT DNA_BIND 434..446
FT /note="A.T hook"
FT /evidence="ECO:0000250"
FT ZN_FING 497..544
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 78..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 571..609
FT /evidence="ECO:0000255"
FT COMPBIAS 340..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 453
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96BD5"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BD5"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96BD5"
FT VAR_SEQ 129..213
FT /note="Missing (in isoform 4, isoform 5, isoform 7 and
FT isoform 9)"
FT /id="VSP_060156"
FT VAR_SEQ 129..212
FT /note="Missing (in isoform 2)"
FT /id="VSP_060157"
FT VAR_SEQ 129
FT /note="Missing (in isoform 3, isoform 6 and isoform 8)"
FT /id="VSP_060158"
FT VAR_SEQ 341..381
FT /note="Missing (in isoform 3, isoform 5, isoform 6, isoform
FT 7, isoform 9 and isoform 8)"
FT /id="VSP_060159"
FT VAR_SEQ 438..492
FT /note="GRPPKYNAVLGFGALTPTSPPSSHPDSPENEKTETTFTFPAPVQPVSLPSPT
FT STD -> ANEEHWPK (in isoform 6, isoform 5 and isoform 4)"
FT /id="VSP_060160"
FT VAR_SEQ 438..481
FT /note="GRPPKYNAVLGFGALTPTSPPSSHPDSPENEKTETTFTFPAPVQ -> ANEE
FT HWPK (in isoform 7 and isoform 8)"
FT /id="VSP_060161"
FT CONFLICT 325
FT /note="A -> P (in Ref. 1; BAC65327 and 3; BAC29735)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="Missing (in Ref. 2; BAC98234)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="A -> T (in Ref. 1; BAC65327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 688 AA; 75597 MW; 187A2BC69E7E2A5C CRC64;
MELQTLQEAL KVEIQVHQKL VAQMKQDPQN ADLKKQLHEL QAKITALSEK QKRVVEQLRK
NLIVKQEQPD KFQIQPLSQS ENKLQTAQQQ PLQPLQQQQP QQPQQQQQQQ QQHAQQSAAA
PPSLTASQKT VTTASMITTK TLPLVLKAAT ATMPASVVGQ RPTIAMVTAI NSQKAVLSTD
VQNTPVNLQT SSKVTGPGAE AVQIVAKNTV TLQVQATPPQ PIKVPQFIPP PRLTPRPNFL
PQVRPKPVAQ NNIPIAPAPP PMLAAPQLIQ RPVMLTKFTP TTLPTSQNSI HPVRVVNGQT
ATIAKTFPMA QLTSIVIATP GTRLAGPQTV QLSKPSLEKQ TVKSHPEAEE KQAESRTVTP
PAAPKPKREE NPQKLAFMVS LGLVTHDHLE EIQSKRQERK RRTTANPVYS GAVFEPERKK
SAVTYLNSTM HPGTRKRGRP PKYNAVLGFG ALTPTSPPSS HPDSPENEKT ETTFTFPAPV
QPVSLPSPTS TDGDIHEDFC SVCRKSGQLL MCDTCSRVYH LDCLEPPLKT IPKGMWICPR
CQDQMLKKEE AIPWPGTLAI VHSYIAYKAA KEEEKQKLLK WSSDLKQERE QLEQKVKELS
SSISKCMEMK SSILARQKEM RSSLDKVKRL IRLVHGVDLC RPVDSEATAG ALSNGPDCTP
PANAASTPAP SPSSQSCTAN CNQGEETK
