ID PHF14_HUMAN Reviewed; 948 AA.
AC O94880; A0A0U1RRH6; A7MCZ3; B4DI82;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-OCT-2022, sequence version 3.
DT 27-MAR-2024, entry version 174.
DE RecName: Full=PHD finger protein 14;
GN Name=PHF14; Synonyms=KIAA0783;
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), AND VARIANT ARG-115.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Hippocampus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208; THR-287 AND SER-290, 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287 AND SER-290, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; THR-287; SER-290;
RP SER-294; SER-298; SER-302 AND SER-530, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-651 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-84; SER-196; THR-287;
RP SER-290; SER-294; SER-298; SER-302 AND SER-530, AND IDENTIFICATION BY MASS
RP 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 [12]
RP FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND ALTERNATIVE SPLICING
RP (ISOFORMS 1; 2 AND 3).
RX PubMed=23688586; DOI=10.1093/abbs/gmt055;
RA Huang Q., Zhang L., Wang Y., Zhang C., Zhou S., Yang G., Li Z., Gao X.,
RA Chen Z., Zhang Z.;
RT "Depletion of PHF14, a novel histone-binding protein gene, causes neonatal
RT lethality in mice due to respiratory failure.";
RL Acta Biochim. Biophys. Sin. 45:622-633(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; THR-287; SER-290;
RP SER-294; SER-298; SER-302; SER-308; SER-530 AND SER-835, AND IDENTIFICATION
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-206; SER-208 AND SER-359, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-648 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: Histone-binding protein (PubMed:23688586). Binds
CC preferentially to unmodified histone H3 but can also bind to a lesser
CC extent to histone H3 trimethylated at 'Lys-9' (H3K9me3) as well as to
CC histone H3 monomethylated at 'Lys-27' (H3K27ac) and trimethylated at
CC 'Lys-27' (H3K27me3) (By similarity). Represses PDGFRA expression, thus
CC playing a role in regulation of mesenchymal cell proliferation (By
CC similarity). Suppresses the expression of CDKN1A/p21 by reducing the
CC level of trimethylation of histone H3 'Lys-4', leading to enhanced
CC proliferation of germinal center B cells (By similarity).
CC {ECO:0000250|UniProtKB:A0A286Y9D1, ECO:0000250|UniProtKB:Q9D4H9,
CC ECO:0000269|PubMed:23688586}.
CC -!- INTERACTION:
CC O94880; O95239: KIF4A; NbExp=4; IntAct=EBI-2680164, EBI-1057516;
CC O94880-1; O95239: KIF4A; NbExp=3; IntAct=EBI-16716857, EBI-1057516;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:23688586}. Chromosome
CC {ECO:0000269|PubMed:23688586}. Note=Mainly localized in the nucleus of
CC interphase cells. In mitotic cells, colocalizes with condensed
CC chromatin during metaphase and anaphase. {ECO:0000269|PubMed:23688586}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:23688586}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=1; Synonyms=PHF14-alpha {ECO:0000303|PubMed:23688586};
CC IsoId=O94880-3; Sequence=Displayed;
CC Name=2; Synonyms=PHF14-beta {ECO:0000303|PubMed:23688586};
CC IsoId=O94880-1; Sequence=VSP_061646, VSP_061647;
CC Name=3; Synonyms=PHF14-gamma {ECO:0000303|PubMed:23688586};
CC IsoId=O94880-2; Sequence=VSP_061645;
CC -!- DOMAIN: The N-terminal region, including the PHD-type 1 and 2 zinc
CC fingers and the C2HC pre-PHD-type zinc finger, is required for binding
CC to histone H3. {ECO:0000250|UniProtKB:A0A286Y9D1}.
CC -!- MISCELLANEOUS: [Isoform 3]: Dubious isoform. Alternative initiation
CC from a downstream AUG is supported by ribosome profiling data.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34503.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB018326; BAA34503.2; ALT_INIT; mRNA.
DR EMBL; AK295461; BAG58394.1; -; mRNA.
DR EMBL; AC005007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC080064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF458374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471073; EAW93634.1; -; Genomic_DNA.
DR EMBL; BC152414; AAI52415.1; -; mRNA.
DR CCDS; CCDS47542.1; -. [O94880-1]
DR RefSeq; NP_055475.2; NM_014660.3. [O94880-1]
DR RefSeq; XP_016868303.1; XM_017012814.1.
DR AlphaFoldDB; O94880; -.
DR SMR; O94880; -.
DR BioGRID; 115032; 104.
DR IntAct; O94880; 30.
DR MINT; O94880; -.
DR STRING; 9606.ENSP00000385795; -.
DR GlyCosmos; O94880; 1 site, 1 glycan.
DR GlyGen; O94880; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O94880; -.
DR PhosphoSitePlus; O94880; -.
DR SwissPalm; O94880; -.
DR BioMuta; PHF14; -.
DR EPD; O94880; -.
DR jPOST; O94880; -.
DR MassIVE; O94880; -.
DR MaxQB; O94880; -.
DR PaxDb; 9606-ENSP00000385795; -.
DR PeptideAtlas; O94880; -.
DR ProteomicsDB; 50520; -. [O94880-1]
DR ProteomicsDB; 50521; -. [O94880-2]
DR Pumba; O94880; -.
DR Antibodypedia; 629; 93 antibodies from 25 providers.
DR DNASU; 9678; -.
DR Ensembl; ENST00000403050.7; ENSP00000385795.3; ENSG00000106443.17. [O94880-1]
DR Ensembl; ENST00000634607.2; ENSP00000489535.1; ENSG00000106443.17. [O94880-3]
DR GeneID; 9678; -.
DR KEGG; hsa:9678; -.
DR MANE-Select; ENST00000634607.2; ENSP00000489535.1; NM_001007157.2; NP_001007158.1.
DR UCSC; uc003sry.3; human. [O94880-3]
DR AGR; HGNC:22203; -.
DR CTD; 9678; -.
DR DisGeNET; 9678; -.
DR GeneCards; PHF14; -.
DR HGNC; HGNC:22203; PHF14.
DR HPA; ENSG00000106443; Low tissue specificity.
DR MIM; 619907; gene.
DR neXtProt; NX_O94880; -.
DR OpenTargets; ENSG00000106443; -.
DR PharmGKB; PA134867397; -.
DR VEuPathDB; HostDB:ENSG00000106443; -.
DR eggNOG; KOG0957; Eukaryota.
DR GeneTree; ENSGT00940000156923; -.
DR HOGENOM; CLU_006506_0_0_1; -.
DR InParanoid; O94880; -.
DR OMA; LVMCDEC; -.
DR OrthoDB; 163389at2759; -.
DR PhylomeDB; O94880; -.
DR TreeFam; TF316118; -.
DR PathwayCommons; O94880; -.
DR SignaLink; O94880; -.
DR BioGRID-ORCS; 9678; 12 hits in 1160 CRISPR screens.
DR ChiTaRS; PHF14; human.
DR GenomeRNAi; 9678; -.
DR Pharos; O94880; Tbio.
DR PRO; PR:O94880; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O94880; Protein.
DR Bgee; ENSG00000106443; Expressed in sural nerve and 186 other cell types or tissues.
DR ExpressionAtlas; O94880; baseline and differential.
DR Genevisible; O94880; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0140566; F:histone reader activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0002314; P:germinal center B cell differentiation; ISS:UniProtKB.
DR GO; GO:0048286; P:lung alveolus development; ISS:UniProtKB.
DR GO; GO:0010463; P:mesenchymal cell proliferation; ISS:UniProtKB.
DR GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0072201; P:negative regulation of mesenchymal cell proliferation; ISS:UniProtKB.
DR GO; GO:2000791; P:negative regulation of mesenchymal cell proliferation involved in lung development; ISS:UniProtKB.
DR GO; GO:2000584; P:negative regulation of platelet-derived growth factor receptor-alpha signaling pathway; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd15674; ePHD_PHF14; 1.
DR CDD; cd15561; PHD1_PHF14; 1.
DR CDD; cd15562; PHD2_PHF14; 1.
DR CDD; cd15563; PHD3_PHF14; 1.
DR Gene3D; 2.30.30.1150; -; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR034732; EPHD.
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; PTHR13793:SF150; PHD FINGER PROTEIN 14; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00249; PHD; 4.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 3.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 1: Evidence at protein level;
KW Alternative initiation; Alternative splicing; Chromosome; Coiled coil;
KW Cytoplasm; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..948
FT /note="PHD finger protein 14"
FT /id="PRO_0000059306"
FT ZN_FING 319..380
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 382..415
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 439..499
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 725..779
FT /note="PHD-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 868..921
FT /note="PHD-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 22..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 630..678
FT /evidence="ECO:0000255"
FT COMPBIAS 70..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..256
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A286Y9D1"
FT BINDING 388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A286Y9D1"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A286Y9D1"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A286Y9D1"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:A0A286Y9D1"
FT BINDING 444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:A0A286Y9D1"
FT BINDING 458
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:A0A286Y9D1"
FT BINDING 463
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:A0A286Y9D1"
FT BINDING 468
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:A0A286Y9D1"
FT BINDING 471
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:A0A286Y9D1"
FT BINDING 495
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:A0A286Y9D1"
FT BINDING 498
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:A0A286Y9D1"
FT BINDING 728
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 731
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 743
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 746
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 751
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 754
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 773
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 776
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 871
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 874
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 886
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 897
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 915
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 918
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 206
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D4H9"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D4H9"
FT MOD_RES 835
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..300
FT /note="MDRSSKRRQVKPLAASLLEALDYDSSDDSDFKVGDASDSEGSGNGSEDASKD
FT SGEGSCSDSEENILEEELNEDIKVKEEQLKNSAEEEVLSSEKQLIKMEKKEEEENGERP
FT RKKKEKEKEKEKEKEKEKEREKEKEKATVSENVAASAAATTPATSPPAVNTSPSVPTTT
FT TATEEQVSEPKKWNLRRNRPLLDFVSMEELNDMDDYDSEDDNDWRPTVVKRKGRSASQK
FT EGSDGDNEDDEDEGSGSDEDENDEGNDEDHSSPASEGGCKKKKSKVLSRNSADDEELTN
FT DSLTLSQSKSNE -> MIVQMTVILKLEMPQ (in isoform 3)"
FT /id="VSP_061645"
FT VAR_SEQ 886..888
FT /note="CDE -> YPS (in isoform 2)"
FT /id="VSP_061646"
FT VAR_SEQ 889..948
FT /note="Missing (in isoform 2)"
FT /id="VSP_061647"
FT VARIANT 115
FT /note="K -> R (in dbSNP:rs218966)"
FT /evidence="ECO:0000269|PubMed:9872452"
FT /id="VAR_018480"
FT CONFLICT 395
FT /note="F -> S (in Ref. 2; BAG58394)"
FT /evidence="ECO:0000305"
FT MOD_RES O94880-2:651
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK O94880-2:648
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 948 AA; 106986 MW; D0CFDB1BAF0BC653 CRC64;
MDRSSKRRQV KPLAASLLEA LDYDSSDDSD FKVGDASDSE GSGNGSEDAS KDSGEGSCSD
SEENILEEEL NEDIKVKEEQ LKNSAEEEVL SSEKQLIKME KKEEEENGER PRKKKEKEKE
KEKEKEKEKE REKEKEKATV SENVAASAAA TTPATSPPAV NTSPSVPTTT TATEEQVSEP
KKWNLRRNRP LLDFVSMEEL NDMDDYDSED DNDWRPTVVK RKGRSASQKE GSDGDNEDDE
DEGSGSDEDE NDEGNDEDHS SPASEGGCKK KKSKVLSRNS ADDEELTNDS LTLSQSKSNE
DSLILEKSQN WSSQKMDHIL ICCVCLGDNS EDADEIIQCD NCGITVHEGC YGVDGESDSI
MSSASENSTE PWFCDACKCG VSPSCELCPN QDGIFKETDA GRWVHIVCAL YVPGVAFGDI
DKLRPVTLTE MNYSKYGAKE CSFCEDPRFA RTGVCISCDA GMCRAYFHVT CAQKEGLLSE
AAAEEDIADP FFAYCKQHAD RLDRKWKRKN YLALQSYCKM SLQEREKQLS PEAQARINAR
LQQYRAKAEL ARSTRPQAWV PREKLPRPLT SSASAIRKLM RKAELMGIST DIFPVDNSDT
SSSVDGRRKH KQPALTADFV NYYFERNMRM IQIQENMAEQ KNIKDKLENE QEKLHVEYNK
LCESLEELQN LNGKLRSEGQ GIWALLGRIT GQKLNIPAIL RAPKERKPSK KEGGTQKTST
LPAVLYSCGI CKKNHDQHLL LLCDTCKLHY HLGCLDPPLT RMPRKTKNSY WQCSECDQAG
SSDMEADMAM ETLPDGTKRS RRQIKEPVKF VPQDVPPEPK KIPIRNTRTR GRKRSFVPEE
EKHEERVPRE RRQRQSVLQK KPKAEDLRTE CATCKGTGDN ENLVRCDECR LCYHFGCLDP
PLKKSPKQTG YGWICQECDS SSSKEDENEA ERKNISQELN MEQKNPKK
//
