ID PF21A_HUMAN Reviewed; 680 AA. AC Q96BD5; D3DQP5; Q6AWA2; Q9C0G7; Q9H8V9; Q9HAK6; Q9NZE9; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 186. DE RecName: Full=PHD finger protein 21A; DE AltName: Full=BHC80a; DE AltName: Full=BRAF35-HDAC complex protein BHC80; GN Name=PHF21A; Synonyms=BHC80, KIAA1696; ORFNames=BM-006; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), IDENTIFICATION BY MASS RP SPECTROMETRY, IDENTIFICATION IN THE BHC COMPLEX WITH HDAC1; HDAC2; HMG20B; RP KDM1A AND RCOR1, TISSUE SPECIFICITY, AND VARIANT HIS-347. RX PubMed=12032298; DOI=10.1073/pnas.112008599; RA Hakimi M.-A., Bochar D.A., Chenoweth J., Lane W.S., Mandel G., RA Shiekhattar R.; RT "A core-BRAF35 complex containing histone deacetylase mediates repression RT of neuronal-specific genes."; RL Proc. Natl. Acad. Sci. U.S.A. 99:7420-7425(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=11214970; DOI=10.1093/dnares/7.6.347; RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIX. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:347-355(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-456 (ISOFORM 3), AND VARIANT HIS-347. RC TISSUE=Embryo, and Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Uterus; 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 [LARGE SCALE MRNA] OF 121-680 (ISOFORM 1). RC TISSUE=Fetal kidney; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-672 (ISOFORMS 2/3). RC TISSUE=Bone marrow; RA Zhao M., Song H., Li N., Peng Y., Han Z., Chen Z.; RT "A novel gene expressed in human bone marrow."; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE BHC COMPLEX RP WITH GSE1; GTF2I; HDAC1; HDAC2; HMG20B; KDM1A; RCOR1; ZMYM2; ZMYM3 AND RP ZNF217. RX PubMed=12493763; DOI=10.1074/jbc.m208992200; RA Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.; RT "A candidate X-linked mental retardation gene is a component of a new RT family of histone deacetylase-containing complexes."; RL J. Biol. Chem. 278:7234-7239(2003). RN [9] RP INTERACTION WITH HDAC1; HDAC2; HMG20B; KDM1A AND RCOR1. 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 [10] RP FUNCTION. RX PubMed=16140033; DOI=10.1016/j.molcel.2005.08.027; RA Shi Y.-J., Matson C., Lan F., Iwase S., Baba T., Shi Y.; RT "Regulation of LSD1 histone demethylase activity by its associated RT factors."; RL Mol. Cell 19:857-864(2005). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-444 AND SER-447, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-350, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-65, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-65, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [19] RP STRUCTURE BY NMR OF 487-535. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the PHD domain in PHD finger protein 21A."; RL Submitted (MAR-2008) to the PDB data bank. RN [20] RP VARIANT IDDBCS 580-ARG--LYS-680 DEL, AND INVOLVEMENT IN IDDBCS. RX PubMed=30487643; DOI=10.1038/s41431-018-0289-x; RA Hamanaka K., Sugawara Y., Shimoji T., Nordtveit T.I., Kato M., RA Nakashima M., Saitsu H., Suzuki T., Yamakawa K., Aukrust I., Houge G., RA Mitsuhashi S., Takata A., Iwama K., Alkanaq A., Fujita A., Imagawa E., RA Mizuguchi T., Miyake N., Miyatake S., Matsumoto N.; RT "De novo truncating variants in PHF21A cause intellectual disability and RT craniofacial anomalies."; RL Eur. J. Hum. Genet. 27:378-383(2019). RN [21] RP VARIANTS IDDBCS SER-429 AND 580-ARG--LYS-680 DEL, INVOLVEMENT IN IDDBCS, RP AND TISSUE SPECIFICITY. RX PubMed=31649809; DOI=10.1186/s13229-019-0286-0; RA Kim H.G., Rosenfeld J.A., Scott D.A., Benedicte G., Labonne J.D., Brown J., RA McGuire M., Mahida S., Naidu S., Gutierrez J., Lesca G., des Portes V., RA Bruel A.L., Sorlin A., Xia F., Capri Y., Muller E., McKnight D., Torti E., RA Rueschendorf F., Hummel O., Islam Z., Kolatkar P.R., Layman L.C., Ryu D., RA Kong I.K., Madan-Khetarpal S., Kim C.H.; RT "Disruption of PHF21A causes syndromic intellectual disability with RT craniofacial anomalies, epilepsy, hypotonia, and neurobehavioral problems RT including autism."; RL Mol. Autism 10:35-35(2019). 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. CC {ECO:0000269|PubMed:16140033}. 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. {ECO:0000269|PubMed:12032298, CC ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:15325272}. CC -!- INTERACTION: CC Q96BD5; Q8N9N5: BANP; NbExp=4; IntAct=EBI-745085, EBI-744695; CC Q96BD5; Q8N9N5-2: BANP; NbExp=4; IntAct=EBI-745085, EBI-11524452; CC Q96BD5; Q96B26: EXOSC8; NbExp=3; IntAct=EBI-745085, EBI-371922; CC Q96BD5; Q14192: FHL2; NbExp=3; IntAct=EBI-745085, EBI-701903; CC Q96BD5; Q13643: FHL3; NbExp=7; IntAct=EBI-745085, EBI-741101; CC Q96BD5; Q6A162: KRT40; NbExp=3; IntAct=EBI-745085, EBI-10171697; CC Q96BD5; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-745085, EBI-11985629; CC Q96BD5; P37198: NUP62; NbExp=7; IntAct=EBI-745085, EBI-347978; CC Q96BD5; Q02447: SP3; NbExp=3; IntAct=EBI-745085, EBI-348158; CC Q96BD5; Q13077: TRAF1; NbExp=4; IntAct=EBI-745085, EBI-359224; CC Q96BD5; Q15942: ZYX; NbExp=6; IntAct=EBI-745085, EBI-444225; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96BD5-1; Sequence=Displayed; CC Name=2; Synonyms=hBHC80-4; CC IsoId=Q96BD5-2; Sequence=VSP_017448, VSP_017449; CC Name=3; CC IsoId=Q96BD5-3; Sequence=VSP_017448; CC -!- TISSUE SPECIFICITY: Highly expressed in brain (PubMed:31649809). CC Expressed at lower level in other tissues, including heart, kidney, CC liver, lung and skeletal muscle (PubMed:31649809). Abundantly expressed CC in fetal brain (PubMed:31649809). {ECO:0000269|PubMed:12032298, CC ECO:0000269|PubMed:31649809}. CC -!- DISEASE: Intellectual developmental disorder with behavioral CC abnormalities and craniofacial dysmorphism with or without seizures CC (IDDBCS) [MIM:618725]: An autosomal dominant neurodevelopmental CC disorder characterized by impaired intellectual development, CC developmental delay of varying severity, impaired motor skills and CC language delay. Additional clinical features include macrocephaly, CC obesity, overgrowth, craniofacial dysmorphism, epilepsy, and variable CC behavioral manifestations including autism and attention deficit CC hyperactivity disorder. {ECO:0000269|PubMed:30487643, CC ECO:0000269|PubMed:31649809}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAF64262.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB21787.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY090777; AAM09095.1; -; mRNA. DR EMBL; AB051483; BAB21787.1; ALT_INIT; mRNA. DR EMBL; AK021530; BAB13839.1; -; mRNA. DR EMBL; AK023258; BAB14492.1; -; mRNA. DR EMBL; CH471064; EAW68012.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68013.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68015.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68017.1; -; Genomic_DNA. DR EMBL; BC015714; AAH15714.1; -; mRNA. DR EMBL; BX648236; CAH10542.1; -; mRNA. DR EMBL; AF208848; AAF64262.1; ALT_FRAME; mRNA. DR CCDS; CCDS31474.1; -. [Q96BD5-2] DR CCDS; CCDS44578.1; -. [Q96BD5-1] DR CCDS; CCDS91465.1; -. [Q96BD5-3] DR RefSeq; NP_001095272.1; NM_001101802.1. [Q96BD5-1] DR RefSeq; NP_057705.3; NM_016621.3. [Q96BD5-2] DR RefSeq; XP_005253022.1; XM_005252965.4. [Q96BD5-3] DR RefSeq; XP_011518475.1; XM_011520173.2. DR RefSeq; XP_011518476.1; XM_011520174.2. [Q96BD5-3] DR RefSeq; XP_011518481.1; XM_011520179.2. [Q96BD5-2] DR RefSeq; XP_016873380.1; XM_017017891.1. [Q96BD5-1] DR PDB; 2PUY; X-ray; 1.43 A; A/B=486-543. DR PDB; 2YQL; NMR; -; A=487-535. DR PDBsum; 2PUY; -. DR PDBsum; 2YQL; -. DR AlphaFoldDB; Q96BD5; -. DR BMRB; Q96BD5; -. DR SMR; Q96BD5; -. DR BioGRID; 119468; 338. DR CORUM; Q96BD5; -. DR DIP; DIP-60252N; -. DR IntAct; Q96BD5; 46. DR MINT; Q96BD5; -. DR STRING; 9606.ENSP00000398824; -. DR GlyCosmos; Q96BD5; 8 sites, 2 glycans. DR GlyGen; Q96BD5; 13 sites, 2 O-linked glycans (13 sites). DR iPTMnet; Q96BD5; -. DR PhosphoSitePlus; Q96BD5; -. DR BioMuta; PHF21A; -. DR DMDM; 74731224; -. DR EPD; Q96BD5; -. DR jPOST; Q96BD5; -. DR MassIVE; Q96BD5; -. DR MaxQB; Q96BD5; -. DR PaxDb; 9606-ENSP00000398824; -. DR PeptideAtlas; Q96BD5; -. DR ProteomicsDB; 76065; -. [Q96BD5-1] DR ProteomicsDB; 76066; -. [Q96BD5-2] DR ProteomicsDB; 76067; -. [Q96BD5-3] DR Pumba; Q96BD5; -. DR Antibodypedia; 26236; 256 antibodies from 29 providers. DR DNASU; 51317; -. DR Ensembl; ENST00000323180.10; ENSP00000323152.6; ENSG00000135365.17. [Q96BD5-2] DR Ensembl; ENST00000418153.6; ENSP00000398824.2; ENSG00000135365.17. [Q96BD5-1] DR Ensembl; ENST00000676320.1; ENSP00000502222.1; ENSG00000135365.17. [Q96BD5-3] DR Ensembl; ENST00000690620.1; ENSP00000508589.1; ENSG00000135365.17. [Q96BD5-2] DR GeneID; 51317; -. DR KEGG; hsa:51317; -. DR MANE-Select; ENST00000676320.1; ENSP00000502222.1; NM_001352027.3; NP_001338956.1. [Q96BD5-3] DR UCSC; uc001ncb.5; human. [Q96BD5-1] DR AGR; HGNC:24156; -. DR CTD; 51317; -. DR DisGeNET; 51317; -. DR GeneCards; PHF21A; -. DR HGNC; HGNC:24156; PHF21A. DR HPA; ENSG00000135365; Low tissue specificity. DR MalaCards; PHF21A; -. DR MIM; 608325; gene. DR MIM; 618725; phenotype. DR neXtProt; NX_Q96BD5; -. DR OpenTargets; ENSG00000135365; -. DR Orphanet; 52022; Potocki-Shaffer syndrome. DR PharmGKB; PA134977844; -. DR VEuPathDB; HostDB:ENSG00000135365; -. DR eggNOG; KOG0383; Eukaryota. DR GeneTree; ENSGT00940000156124; -. DR HOGENOM; CLU_020260_1_0_1; -. DR InParanoid; Q96BD5; -. DR OMA; SHQTGGD; -. DR OrthoDB; 4547516at2759; -. DR PhylomeDB; Q96BD5; -. DR TreeFam; TF331518; -. DR PathwayCommons; Q96BD5; -. DR Reactome; R-HSA-3214815; HDACs deacetylate histones. DR Reactome; R-HSA-9679191; Potential therapeutics for SARS. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; Q96BD5; -. DR SIGNOR; Q96BD5; -. DR BioGRID-ORCS; 51317; 24 hits in 1166 CRISPR screens. DR ChiTaRS; PHF21A; human. DR EvolutionaryTrace; Q96BD5; -. DR GeneWiki; PHF21A; -. DR GenomeRNAi; 51317; -. DR Pharos; Q96BD5; Tbio. DR PRO; PR:Q96BD5; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q96BD5; Protein. DR Bgee; ENSG00000135365; Expressed in tendon of biceps brachii and 192 other cell types or tissues. DR ExpressionAtlas; Q96BD5; baseline and differential. DR GO; GO:1990391; C:DNA repair complex; IDA:MGI. DR GO; GO:0000118; C:histone deacetylase complex; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central. 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; IDA:MGI. DR CDD; cd15523; PHD_PHF21A; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 PANTHER; PTHR24102; PHD FINGER PROTEIN; 1. DR PANTHER; PTHR24102:SF6; PHD FINGER PROTEIN 21A; 1. DR Pfam; PF00628; PHD; 1. DR SMART; SM00249; PHD; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. DR Genevisible; Q96BD5; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromatin regulator; Coiled coil; KW Disease variant; DNA-binding; Epilepsy; Intellectual disability; KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repressor; Transcription; Transcription regulation; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..680 FT /note="PHD finger protein 21A" FT /id="PRO_0000226767" FT DNA_BIND 425..437 FT /note="A.T hook" FT ZN_FING 488..535 FT /note="PHD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT REGION 82..118 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 318..363 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 440..463 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 486..680 FT /note="Required for transcriptional repression" FT REGION 639..680 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 558..603 FT /evidence="ECO:0000255" FT COMPBIAS 331..345 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 442..463 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 650..680 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 350 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 444 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 447 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT CROSSLNK 65 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 204 FT /note="L -> LQ (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:11214970, FT ECO:0000303|PubMed:12032298, ECO:0000303|PubMed:14702039" FT /id="VSP_017448" FT VAR_SEQ 429..483 FT /note="GRPPKYNAVLGFGALTPTSPQSSHPDSPENEKTETTFTFPAPVQPVSLPSPT FT STD -> ANEEHWPK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11214970, FT ECO:0000303|PubMed:12032298, ECO:0000303|PubMed:14702039" FT /id="VSP_017449" FT VARIANT 347 FT /note="R -> H (in dbSNP:rs3736508)" FT /evidence="ECO:0000269|PubMed:12032298, FT ECO:0000269|PubMed:14702039" FT /id="VAR_025515" FT VARIANT 429 FT /note="G -> S (in IDDBCS; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31649809" FT /id="VAR_083199" FT VARIANT 580..680 FT /note="Missing (in IDDBCS)" FT /evidence="ECO:0000269|PubMed:30487643, FT ECO:0000269|PubMed:31649809" FT /id="VAR_083200" FT CONFLICT 447 FT /note="S -> P (in Ref. 3; BAB13839)" FT /evidence="ECO:0000305" FT CONFLICT 662..680 FT /note="PSPSSQSCTANCNQGEETK -> LCSLPELHSEL (in Ref. 7)" FT /evidence="ECO:0000305" FT TURN 492..494 FT /evidence="ECO:0007829|PDB:2PUY" FT STRAND 504..507 FT /evidence="ECO:0007829|PDB:2PUY" FT HELIX 512..514 FT /evidence="ECO:0007829|PDB:2PUY" FT STRAND 515..517 FT /evidence="ECO:0007829|PDB:2PUY" FT HELIX 530..538 FT /evidence="ECO:0007829|PDB:2PUY" FT TURN 539..542 FT /evidence="ECO:0007829|PDB:2PUY" SQ SEQUENCE 680 AA; 74854 MW; C7AF87EB2984A796 CRC64; MELQTLQEAL KVEIQVHQKL VAQMKQDPQN ADLKKQLHEL QAKITALSEK QKRVVEQLRK NLIVKQEQPD KFQIQPLPQS ENKLQTAQQQ PLQQLQQQQQ YHHHHAQQSA AASPNLTASQ KTVTTASMIT TKTLPLVLKA ATATMPASVV GQRPTIAMVT AINSQKAVLS TDVQNTPVNL QTSSKVTGPG AEAVQIVAKN TVTLVQATPP QPIKVPQFIP PPRLTPRPNF LPQVRPKPVA QNNIPIAPAP PPMLAAPQLI QRPVMLTKFT PTTLPTSQNS IHPVRVVNGQ TATIAKTFPM AQLTSIVIAT PGTRLAGPQT VQLSKPSLEK QTVKSHTETD EKQTESRTIT PPAAPKPKRE ENPQKLAFMV SLGLVTHDHL EEIQSKRQER KRRTTANPVY SGAVFEPERK KSAVTYLNST MHPGTRKRGR PPKYNAVLGF GALTPTSPQS SHPDSPENEK TETTFTFPAP VQPVSLPSPT STDGDIHEDF CSVCRKSGQL LMCDTCSRVY HLDCLDPPLK TIPKGMWICP RCQDQMLKKE EAIPWPGTLA IVHSYIAYKA AKEEEKQKLL KWSSDLKQER EQLEQKVKQL SNSISKCMEM KNTILARQKE MHSSLEKVKQ LIRLIHGIDL SKPVDSEATV GAISNGPDCT PPANAATSTP APSPSSQSCT ANCNQGEETK //