ID PHF6_HUMAN Reviewed; 365 AA. AC Q8IWS0; A8K230; B4E0G4; D3DTG3; E9PC97; Q5JRC7; Q5JRC8; Q96JK3; Q9BRU0; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 02-SEP-2026, entry version 194. DE RecName: Full=PHD finger protein 6; DE AltName: Full=PHD-like zinc finger protein; GN Name=PHF6; Synonyms=CENP-31, KIAA1823; 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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR RP LOCATION, ALTERNATIVE SPLICING, AND VARIANTS BFLS TYR-45; PHE-99; ARG-229; RP GLU-234 AND GLY-257. RX PubMed=12415272; DOI=10.1038/ng1040; RA Lower K.M., Turner G., Kerr B.A., Mathews K.D., Shaw M.A., Gedeon A.K., RA Schelley S., Hoyme H.E., White S.M., Delatycki M.B., Lampe A.K., RA Clayton-Smith J., Stewart H., van Ravenswaay C.M.A., de Vries B.B.A., RA Cox B., Grompe M., Ross S., Thomas P., Mulley J.C., Gecz J.; RT "Mutations in PHF6 are associated with Boerjeson-Forssman-Lehmann RT syndrome."; RL Nat. Genet. 32:661-665(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=11347906; DOI=10.1093/dnares/8.2.85; RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XX. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 8:85-95(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5). RC TISSUE=Subthalamic nucleus, and Thymus; 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]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Bone marrow; 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-358, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-145, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 (ISOFORM 2), AND 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 [11] 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY RP 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 [13] RP SUBCELLULAR LOCATION. RX PubMed=20813266; DOI=10.1016/j.cell.2010.07.047; RA Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L., RA Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T., RA Earnshaw W.C., Rappsilber J.; RT "The protein composition of mitotic chromosomes determined using RT multiclassifier combinatorial proteomics."; RL Cell 142:810-821(2010). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, AND IDENTIFICATION BY RP 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=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-199, AND 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 [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [18] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UBTF, AND CHARACTERIZATION RP OF VARIANTS BFLS TYR-45 AND PHE-99. RX PubMed=23229552; DOI=10.1074/jbc.m112.414839; RA Wang J., Leung J.W., Gong Z., Feng L., Shi X., Chen J.; RT "PHF6 regulates cell cycle progression by suppressing ribosomal RNA RT synthesis."; RL J. Biol. Chem. 288:3174-3183(2013). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-145; SER-155 AND RP SER-199, AND IDENTIFICATION BY 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 [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-173 AND LYS-227, AND RP IDENTIFICATION BY MASS 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 [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-227, 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 [22] RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 208-333, INTERACTION WITH RBBP4, RP ZINC-FINGERS, EXTENDED PHD DOMAIN, AND DNA-BINDING. RX PubMed=24554700; DOI=10.1074/jbc.m113.535351; RA Liu Z., Li F., Ruan K., Zhang J., Mei Y., Wu J., Shi Y.; RT "Structural and functional insights into the human Borjeson-Forssman- RT Lehmann syndrome-associated protein PHF6."; RL J. Biol. Chem. 289:10069-10083(2014). RN [23] RP VARIANT BFLS PHE-305. RX PubMed=23906836; DOI=10.1093/hmg/ddt366; RA Wieczorek D., Boegershausen N., Beleggia F., Steiner-Haldenstaett S., RA Pohl E., Li Y., Milz E., Martin M., Thiele H., Altmueller J., Alanay Y., RA Kayserili H., Klein-Hitpass L., Boehringer S., Wollstein A., Albrecht B., RA Boduroglu K., Caliebe A., Chrzanowska K., Cogulu O., Cristofoli F., RA Czeschik J.C., Devriendt K., Dotti M.T., Elcioglu N., Gener B., RA Goecke T.O., Krajewska-Walasek M., Guillen-Navarro E., Hayek J., Houge G., RA Kilic E., Simsek-Kiper P.O., Lopez-Gonzalez V., Kuechler A., Lyonnet S., RA Mari F., Marozza A., Mathieu Dramard M., Mikat B., Morin G., RA Morice-Picard F., Ozkinay F., Rauch A., Renieri A., Tinschert S., RA Utine G.E., Vilain C., Vivarelli R., Zweier C., Nuernberg P., Rahmann S., RA Vermeesch J., Luedecke H.J., Zeschnigk M., Wollnik B.; RT "A comprehensive molecular study on Coffin-Siris and Nicolaides-Baraitser RT syndromes identifies a broad molecular and clinical spectrum converging on RT altered chromatin remodeling."; RL Hum. Mol. Genet. 22:5121-5135(2013). CC -!- FUNCTION: Transcriptional regulator that associates with ribosomal RNA CC promoters and suppresses ribosomal RNA (rRNA) transcription. CC {ECO:0000269|PubMed:23229552}. CC -!- SUBUNIT: Interacts with UBTF. Interacts with the NuRD complex component CC RBBP4 (via the nucleolar localization motif), the interaction mediates CC transcriptional repression activity. {ECO:0000269|PubMed:23229552, CC ECO:0000269|PubMed:24554700}. CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Chromosome, CC centromere, kinetochore {ECO:0000269|PubMed:20813266}. Note=Nuclear, it CC particularly localizes to the nucleolus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=PHF6a, PHF6b; CC IsoId=Q8IWS0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IWS0-2; Sequence=VSP_009372, VSP_009373, VSP_009374; CC Name=3; CC IsoId=Q8IWS0-3; Sequence=VSP_053441; CC Name=4; CC IsoId=Q8IWS0-4; Sequence=VSP_053441, VSP_009373, VSP_009374; CC Name=5; CC IsoId=Q8IWS0-5; Sequence=VSP_054937; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:12415272}. CC -!- DOMAIN: The PHD-type zinc finger 1 mediates both nucleolar localization CC and interaction with UBTF. CC -!- DOMAIN: The ePHD2 domain folds as an integrated structural module CC comprizing the C2HC pre-PHD-type 2 zinc finger and the PHD-type 2 zinc CC finger. It mediates non-specific binding to dsDNA, but doesn't bind CC histones in contrast to many PHD-type zinc fingers. CC -!- DISEASE: Boerjeson-Forssman-Lehmann syndrome (BFLS) [MIM:301900]: An X- CC linked recessive disorder characterized by moderate to severe CC intellectual disability, epilepsy, hypogonadism, hypometabolism, CC obesity with marked gynecomastia, swelling of subcutaneous tissue of CC the face, narrow palpebral fissure and large but not deformed ears. CC {ECO:0000269|PubMed:12415272, ECO:0000269|PubMed:23229552, CC ECO:0000269|PubMed:23906836}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=BAB47452.1; 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; AY157622; AAO13214.1; -; mRNA. DR EMBL; AB058726; BAB47452.1; ALT_INIT; mRNA. DR EMBL; AK290095; BAF82784.1; -; mRNA. DR EMBL; AK303369; BAG64426.1; -; mRNA. DR EMBL; AC004383; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL591668; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471107; EAX11762.1; -; Genomic_DNA. DR EMBL; CH471107; EAX11763.1; -; Genomic_DNA. DR EMBL; CH471107; EAX11766.1; -; Genomic_DNA. DR EMBL; BC005994; AAH05994.1; -; mRNA. DR CCDS; CCDS14639.1; -. [Q8IWS0-1] DR CCDS; CCDS14640.1; -. [Q8IWS0-2] DR RefSeq; NP_001015877.1; NM_001015877.2. [Q8IWS0-1] DR RefSeq; NP_115711.2; NM_032335.3. [Q8IWS0-2] DR RefSeq; NP_115834.1; NM_032458.3. [Q8IWS0-1] DR PDB; 4NN2; X-ray; 1.47 A; A/B=208-333. DR PDB; 4R7A; X-ray; 1.85 A; A=157-171. DR AlphaFoldDB; Q8IWS0; -. DR SMR; Q8IWS0; -. DR BioGRID; 124022; 325. DR FunCoup; Q8IWS0; 2959. DR IntAct; Q8IWS0; 65. DR MINT; Q8IWS0; -. DR NDEx; IQUERY-CP-PHF6; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000329097; -. DR BindingDB; Q8IWS0; -. DR ChEMBL; CHEMBL5465329; -. DR GlyGen; Q8IWS0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8IWS0; -. DR PhosphoSitePlus; Q8IWS0; -. DR SwissPalm; Q8IWS0; -. DR BioMuta; PHF6; -. DR DMDM; 42559482; -. DR jPOST; Q8IWS0; -. DR MassIVE; Q8IWS0; -. DR PaxDb; 9606-ENSP00000329097; -. DR PeptideAtlas; Q8IWS0; -. DR ProteomicsDB; 19401; -. DR ProteomicsDB; 5670; -. DR ProteomicsDB; 70885; -. [Q8IWS0-1] DR ProteomicsDB; 70886; -. [Q8IWS0-2] DR Pumba; Q8IWS0; -. DR Antibodypedia; 426; 230 antibodies from 31 providers. DR DNASU; 84295; -. DR Ensembl; ENST00000332070.7; ENSP00000329097.3; ENSG00000156531.19. [Q8IWS0-1] DR Ensembl; ENST00000370800.4; ENSP00000359836.4; ENSG00000156531.19. [Q8IWS0-2] DR Ensembl; ENST00000370803.8; ENSP00000359839.4; ENSG00000156531.19. [Q8IWS0-1] DR Ensembl; ENST00000687496.1; ENSP00000509551.1; ENSG00000156531.19. [Q8IWS0-5] DR Ensembl; ENST00000688598.1; ENSP00000510410.1; ENSG00000156531.19. [Q8IWS0-5] DR Ensembl; ENST00000691812.1; ENSP00000510211.1; ENSG00000156531.19. [Q8IWS0-1] DR Ensembl; ENST00000908871.1; ENSP00000578930.1; ENSG00000156531.19. [Q8IWS0-1] DR Ensembl; ENST00000908872.1; ENSP00000578931.1; ENSG00000156531.19. [Q8IWS0-1] DR Ensembl; ENST00000934665.1; ENSP00000604724.1; ENSG00000156531.19. [Q8IWS0-1] DR Ensembl; ENST00000956399.1; ENSP00000626458.1; ENSG00000156531.19. [Q8IWS0-1] DR GeneID; 84295; -. DR KEGG; hsa:84295; -. DR MANE-Select; ENST00000370803.8; ENSP00000359839.4; NM_001015877.2; NP_001015877.1. DR UCSC; uc004exh.4; human. [Q8IWS0-1] DR AGR; HGNC:18145; -. DR ClinPGx; PA33263; -. DR CTD; 84295; -. DR DisGeNET; 84295; -. DR GeneCards; PHF6; -. DR HGNC; HGNC:18145; PHF6. DR HPA; ENSG00000156531; Low tissue specificity. DR MalaCards; PHF6; -. DR MIM; 300414; gene. DR MIM; 301900; phenotype. DR OpenTargets; ENSG00000156531; -. DR Orphanet; 127; Borjeson-Forssman-Lehmann syndrome. DR VEuPathDB; HostDB:ENSG00000156531; -. DR eggNOG; KOG1084; Eukaryota. DR GeneTree; ENSGT00950000182865; -. DR InParanoid; Q8IWS0; -. DR OMA; KHKKTPH; -. DR OrthoDB; 2384350at2759; -. DR PAN-GO; Q8IWS0; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q8IWS0; -. DR PathwayCommons; Q8IWS0; -. DR Reactome; R-HSA-9940951; Interaction of NuRD complexes with transcription factors. DR SignaLink; Q8IWS0; -. DR SIGNOR; Q8IWS0; -. DR Agora; ENSG00000156531; -. DR BioGRID-ORCS; 84295; 32 hits in 800 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR ChiTaRS; PHF6; human. DR EvolutionaryTrace; Q8IWS0; -. DR GeneWiki; PHF6; -. DR GenomeRNAi; 84295; -. DR Pharos; Q8IWS0; Tbio. DR PRO; PR:Q8IWS0; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q8IWS0; protein. DR Bgee; ENSG00000156531; Expressed in corpus epididymis and 197 other cell types or tissues. DR ExpressionAtlas; Q8IWS0; baseline and differential. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0042393; F:histone binding; IPI:UniProtKB. DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB. DR GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB. DR GO; GO:0043021; F:ribonucleoprotein complex binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0097110; F:scaffold protein binding; IPI:UniProtKB. DR GO; GO:0015631; F:tubulin binding; IPI:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd15710; ePHD1_PHF6; 1. DR CDD; cd15711; ePHD2_PHF6; 1. DR FunFam; 3.30.40.10:FF:000219; PHD finger protein 6 isoform X1; 1. DR FunFam; 3.30.40.10:FF:000167; PHD finger protein 6 X-linked; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2. DR IDEAL; IID00594; -. DR InterPro; IPR034732; EPHD. DR InterPro; IPR051188; PHD-type_Zinc_Finger. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR12420; PHD FINGER PROTEIN; 1. DR PANTHER; PTHR12420:SF15; PHD FINGER PROTEIN 6; 1. DR Pfam; PF13771; zf-HC5HC2H; 2. DR SMART; SM00249; PHD; 2. DR PROSITE; PS51805; EPHD; 2. DR PDBsum; 4NN2; -. DR PDBsum; 4R7A; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Centromere; Chromosome; KW Disease variant; DNA-binding; Epilepsy; Hypotrichosis; KW Intellectual disability; Isopeptide bond; Kinetochore; Metal-binding; KW Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..365 FT /note="PHD finger protein 6" FT /id="PRO_0000059293" FT ZN_FING 14..52 FT /note="C2HC pre-PHD-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146" FT ZN_FING 80..132 FT /note="PHD-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146" FT ZN_FING 209..249 FT /note="C2HC pre-PHD-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146" FT ZN_FING 278..330 FT /note="PHD-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146" FT REGION 14..132 FT /note="Extended PHD1 domain (ePHD1)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146" FT REGION 139..211 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 209..330 FT /note="Extended PHD2 domain (ePHD2)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146" FT REGION 330..365 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 13..16 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOTIF 129..133 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOTIF 157..169 FT /note="Nucleolar localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 157..171 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 342..352 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 354..365 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 138 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 145 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 155 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 183 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D4J7" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 358 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17525332" FT CROSSLNK 173 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447" FT CROSSLNK 227 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 47..80 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054937" FT VAR_SEQ 140 FT /note="A -> AA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_009372" FT VAR_SEQ 140 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053441" FT VAR_SEQ 279..311 FT /note="KCTLCSQPGATIGCEIKACVKTYHYHCGVQDKA -> VCSFYICYATLHLIC FT CFKFRVHPKFIQSSENLK (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_009373" FT VAR_SEQ 312..365 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_009374" FT VARIANT 45 FT /note="C -> Y (in BFLS; Loss of interaction with UBTF; FT dbSNP:rs132630299)" FT /evidence="ECO:0000269|PubMed:12415272, FT ECO:0000269|PubMed:23229552" FT /id="VAR_017633" FT VARIANT 99 FT /note="C -> F (in BFLS; Loss of interaction with UBTF; FT dbSNP:rs132630298)" FT /evidence="ECO:0000269|PubMed:12415272, FT ECO:0000269|PubMed:23229552" FT /id="VAR_017634" FT VARIANT 229 FT /note="H -> R (in BFLS; dbSNP:rs104894918)" FT /evidence="ECO:0000269|PubMed:12415272" FT /id="VAR_017635" FT VARIANT 234 FT /note="K -> E (in BFLS; dbSNP:rs104894917)" FT /evidence="ECO:0000269|PubMed:12415272" FT /id="VAR_017636" FT VARIANT 257 FT /note="R -> G (in BFLS; dbSNP:rs104894919)" FT /evidence="ECO:0000269|PubMed:12415272" FT /id="VAR_017637" FT VARIANT 305 FT /note="C -> F (in BFLS; dbSNP:rs587777489)" FT /evidence="ECO:0000269|PubMed:23906836" FT /id="VAR_076933" FT CONFLICT 126 FT /note="V -> A (in Ref. 6; AAH05994)" FT /evidence="ECO:0000305" FT TURN 213..215 FT /evidence="ECO:0007829|PDB:4NN2" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:4NN2" FT HELIX 222..225 FT /evidence="ECO:0007829|PDB:4NN2" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:4NN2" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:4NN2" FT HELIX 240..244 FT /evidence="ECO:0007829|PDB:4NN2" FT STRAND 257..259 FT /evidence="ECO:0007829|PDB:4NN2" FT HELIX 265..275 FT /evidence="ECO:0007829|PDB:4NN2" FT TURN 281..283 FT /evidence="ECO:0007829|PDB:4NN2" FT STRAND 290..294 FT /evidence="ECO:0007829|PDB:4NN2" FT HELIX 303..308 FT /evidence="ECO:0007829|PDB:4NN2" FT STRAND 312..316 FT /evidence="ECO:0007829|PDB:4NN2" FT TURN 317..320 FT /evidence="ECO:0007829|PDB:4NN2" FT STRAND 321..325 FT /evidence="ECO:0007829|PDB:4NN2" FT HELIX 327..329 FT /evidence="ECO:0007829|PDB:4NN2" FT MOD_RES Q8IWS0-2:146 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" SQ SEQUENCE 365 AA; 41290 MW; E8E587909EF9701D CRC64; MSSSVEQKKG PTRQRKCGFC KSNRDKECGQ LLISENQKVA AHHKCMLFSS ALVSSHSDNE SLGGFSIEDV QKEIKRGTKL MCSLCHCPGA TIGCDVKTCH RTYHYHCALH DKAQIREKPS QGIYMVYCRK HKKTAHNSEA DLEESFNEHE LEPSSPKSKK KSRKGRPRKT NFKGLSEDTR STSSHGTDEM ESSSYRDRSP HRSSPSDTRP KCGFCHVGEE ENEARGKLHI FNAKKAAAHY KCMLFSSGTV QLTTTSRAEF GDFDIKTVLQ EIKRGKRMKC TLCSQPGATI GCEIKACVKT YHYHCGVQDK AKYIENMSRG IYKLYCKNHS GNDERDEEDE ERESKSRGKV EIDQQQLTQQ QLNGN //