PF21A_HUMAN
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 03-AUG-2022, entry version 177.
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};
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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 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; 82.
DR CORUM; Q96BD5; -.
DR DIP; DIP-60252N; -.
DR IntAct; Q96BD5; 45.
DR MINT; Q96BD5; -.
DR STRING; 9606.ENSP00000398824; -.
DR GlyGen; Q96BD5; 8 sites, 2 O-linked glycans (8 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; Q96BD5; -.
DR PeptideAtlas; Q96BD5; -.
DR PRIDE; Q96BD5; -.
DR ProteomicsDB; 76065; -. [Q96BD5-1]
DR ProteomicsDB; 76066; -. [Q96BD5-2]
DR ProteomicsDB; 76067; -. [Q96BD5-3]
DR Antibodypedia; 26236; 235 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 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; QKEMHGS; -.
DR OrthoDB; 1185408at2759; -.
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; 21 hits in 1087 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 191 other tissues.
DR ExpressionAtlas; Q96BD5; baseline and differential.
DR Genevisible; Q96BD5; HS.
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 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 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; unknown pathological
FT 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
