ID   PRD10_HUMAN             Reviewed;        1147 AA.
AC   Q9NQV6; B7ZL71; G3XAE5; J3KP23; Q17R90; Q2KHR4; Q863Z2; Q9NXI4; Q9ULI9;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 3.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=PR domain zinc finger protein 10;
DE            EC=2.1.1.-;
DE   AltName: Full=PR domain-containing protein 10;
DE   AltName: Full=Tristanin;
GN   Name=PRDM10; Synonyms=KIAA1231, PFM7, TRIS;
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 2).
RC   TISSUE=Brain;
RX   PubMed=12175877; DOI=10.1016/s0736-5748(02)00055-2;
RA   Siegel D.A., Huang M.K., Becker S.F.;
RT   "Ectopic dendrite initiation: CNS pathogenesis as a model of CNS
RT   development.";
RL   Int. J. Dev. Neurosci. 20:373-389(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=10668202; DOI=10.14670/hh-15.109;
RA   Jiang G.L., Huang S.;
RT   "The yin-yang of PR-domain family genes in tumorigenesis.";
RL   Histol. Histopathol. 15:109-117(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA   Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:337-345(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7), AND VARIANT ALA-573.
RC   TISSUE=Amygdala;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND VARIANT
RP   ALA-573.
RC   TISSUE=Brain, and 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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 268-1147 (ISOFORM 6), AND VARIANT
RP   ALA-573.
RC   TISSUE=Colon mucosa;
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428, 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   [10]
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424 AND THR-428, 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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, 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   [14]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-380, 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   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 188-339.
RG   Structural genomics consortium (SGC);
RT   "Methyltransferase domain of human PR domain-containing protein 10.";
RL   Submitted (JUL-2011) to the PDB data bank.
RN   [16]
RP   VARIANT BHD2 TYR-677, INVOLVEMENT IN BHD2, CHARACTERIZATION OF VARIANT BHD2
RP   TYR-677, AND FUNCTION.
RX   PubMed=36440963; DOI=10.1093/hmg/ddac288;
RA   van de Beek I., Glykofridis I.E., Oosterwijk J.C., van den Akker P.C.,
RA   Diercks G.F.H., Bolling M.C., Waisfisz Q., Mensenkamp A.R., Balk J.A.,
RA   Zwart R., Postma A.V., Meijers-Heijboer H.E.J., van Moorselaar R.J.A.,
RA   Wolthuis R.M.F., Houweling A.C.;
RT   "PRDM10 directs FLCN expression in a novel disorder overlapping with Birt-
RT   Hogg-Dube syndrome and familial lipomatosis.";
RL   Hum. Mol. Genet. 32:1223-1235(2023).
CC   -!- FUNCTION: Acts as a transcriptional activator of FLNC expression.
CC       {ECO:0000269|PubMed:36440963}.
CC   -!- INTERACTION:
CC       Q9NQV6; Q04864: REL; NbExp=3; IntAct=EBI-10312448, EBI-307352;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:36440963}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=3;
CC         IsoId=Q9NQV6-3; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NQV6-2; Sequence=VSP_036351, VSP_035655, VSP_035656;
CC       Name=1;
CC         IsoId=Q9NQV6-1; Sequence=VSP_036351;
CC       Name=4;
CC         IsoId=Q9NQV6-4; Sequence=VSP_035655, VSP_036352;
CC       Name=5;
CC         IsoId=Q9NQV6-5; Sequence=VSP_036351, VSP_036352;
CC       Name=6;
CC         IsoId=Q9NQV6-6; Sequence=VSP_035655, VSP_036352, VSP_036353;
CC       Name=7;
CC         IsoId=Q9NQV6-7; Sequence=VSP_036352;
CC   -!- DOMAIN: The SET domain is degenerated, suggesting that it has lost
CC       methyltransferase activity.
CC   -!- DISEASE: Birt-Hogg-Dube syndrome 2 (BHD2) [MIM:620459]: A form of Birt-
CC       Hogg-Dube syndrome, a rare genodermatosis usually manifesting in
CC       adulthood and characterized by multiple fibrofolliculomas,
CC       trichodiscomas, and acrochordons. Patients with this syndrome have an
CC       increased susceptibility to develop renal cell carcinoma, lung cysts,
CC       and spontaneous pneumothorax. BHD2 inheritance is autosomal dominant.
CC       {ECO:0000269|PubMed:36440963}. Note=The disease may be caused by
CC       variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA91026.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF503171; AAP30847.1; -; mRNA.
DR   EMBL; AF275817; AAF87243.1; -; mRNA.
DR   EMBL; AB033057; BAA86545.2; -; mRNA.
DR   EMBL; BX648944; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AP003041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP003326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP003327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471065; EAW67761.1; -; Genomic_DNA.
DR   EMBL; BC112934; AAI12935.1; -; mRNA.
DR   EMBL; BC117415; AAI17416.1; -; mRNA.
DR   EMBL; BC143612; AAI43613.1; -; mRNA.
DR   EMBL; AK000234; BAA91026.1; ALT_INIT; mRNA.
DR   CCDS; CCDS44771.1; -. [Q9NQV6-7]
DR   CCDS; CCDS44772.1; -. [Q9NQV6-1]
DR   CCDS; CCDS8484.1; -. [Q9NQV6-4]
DR   CCDS; CCDS8485.1; -. [Q9NQV6-2]
DR   CCDS; CCDS91624.1; -. [Q9NQV6-5]
DR   RefSeq; NP_064613.2; NM_020228.2. [Q9NQV6-7]
DR   RefSeq; NP_955469.1; NM_199437.1. [Q9NQV6-4]
DR   RefSeq; NP_955470.1; NM_199438.1. [Q9NQV6-1]
DR   RefSeq; NP_955471.1; NM_199439.1. [Q9NQV6-2]
DR   PDB; 3IHX; X-ray; 2.50 A; A/B/C/D=188-339.
DR   PDBsum; 3IHX; -.
DR   AlphaFoldDB; Q9NQV6; -.
DR   SMR; Q9NQV6; -.
DR   BioGRID; 121298; 70.
DR   IntAct; Q9NQV6; 23.
DR   MINT; Q9NQV6; -.
DR   STRING; 9606.ENSP00000351686; -.
DR   ChEMBL; CHEMBL5214863; -.
DR   GlyCosmos; Q9NQV6; 6 sites, 2 glycans.
DR   GlyGen; Q9NQV6; 6 sites, 2 O-linked glycans (6 sites).
DR   iPTMnet; Q9NQV6; -.
DR   PhosphoSitePlus; Q9NQV6; -.
DR   BioMuta; PRDM10; -.
DR   DMDM; 442570289; -.
DR   EPD; Q9NQV6; -.
DR   jPOST; Q9NQV6; -.
DR   MassIVE; Q9NQV6; -.
DR   MaxQB; Q9NQV6; -.
DR   PaxDb; 9606-ENSP00000351686; -.
DR   PeptideAtlas; Q9NQV6; -.
DR   ProteomicsDB; 33727; -.
DR   ProteomicsDB; 82192; -. [Q9NQV6-3]
DR   ProteomicsDB; 82193; -. [Q9NQV6-1]
DR   ProteomicsDB; 82194; -. [Q9NQV6-2]
DR   ProteomicsDB; 82195; -. [Q9NQV6-4]
DR   ProteomicsDB; 82196; -. [Q9NQV6-5]
DR   ProteomicsDB; 82197; -. [Q9NQV6-6]
DR   Pumba; Q9NQV6; -.
DR   ABCD; Q9NQV6; 1 sequenced antibody.
DR   Antibodypedia; 19222; 271 antibodies from 33 providers.
DR   DNASU; 56980; -.
DR   Ensembl; ENST00000304538.10; ENSP00000302669.6; ENSG00000170325.16. [Q9NQV6-2]
DR   Ensembl; ENST00000358825.9; ENSP00000351686.5; ENSG00000170325.16. [Q9NQV6-7]
DR   Ensembl; ENST00000360871.8; ENSP00000354118.3; ENSG00000170325.16. [Q9NQV6-4]
DR   Ensembl; ENST00000423662.6; ENSP00000398431.2; ENSG00000170325.16. [Q9NQV6-1]
DR   Ensembl; ENST00000526082.5; ENSP00000432237.1; ENSG00000170325.16. [Q9NQV6-5]
DR   GeneID; 56980; -.
DR   KEGG; hsa:56980; -.
DR   MANE-Select; ENST00000360871.8; ENSP00000354118.3; NM_199437.2; NP_955469.1. [Q9NQV6-4]
DR   UCSC; uc001qfj.4; human. [Q9NQV6-3]
DR   AGR; HGNC:13995; -.
DR   CTD; 56980; -.
DR   DisGeNET; 56980; -.
DR   GeneCards; PRDM10; -.
DR   HGNC; HGNC:13995; PRDM10.
DR   HPA; ENSG00000170325; Low tissue specificity.
DR   MalaCards; PRDM10; -.
DR   MIM; 618319; gene.
DR   MIM; 620459; phenotype.
DR   neXtProt; NX_Q9NQV6; -.
DR   OpenTargets; ENSG00000170325; -.
DR   PharmGKB; PA33708; -.
DR   VEuPathDB; HostDB:ENSG00000170325; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000158740; -.
DR   InParanoid; Q9NQV6; -.
DR   OMA; IRVIFQN; -.
DR   OrthoDB; 5394783at2759; -.
DR   TreeFam; TF350894; -.
DR   PathwayCommons; Q9NQV6; -.
DR   SignaLink; Q9NQV6; -.
DR   BioGRID-ORCS; 56980; 346 hits in 1162 CRISPR screens.
DR   ChiTaRS; PRDM10; human.
DR   EvolutionaryTrace; Q9NQV6; -.
DR   GenomeRNAi; 56980; -.
DR   Pharos; Q9NQV6; Tbio.
DR   PRO; PR:Q9NQV6; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9NQV6; Protein.
DR   Bgee; ENSG00000170325; Expressed in secondary oocyte and 182 other cell types or tissues.
DR   ExpressionAtlas; Q9NQV6; baseline and differential.
DR   GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0017053; C:transcription repressor complex; IDA:ARUK-UCL.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR   CDD; cd19194; PR-SET_PRDM10; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 7.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR044403; PRDM10_PR/SET.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24403:SF48; PR DOMAIN ZINC FINGER PROTEIN 10; 1.
DR   PANTHER; PTHR24403; ZINC FINGER PROTEIN; 1.
DR   Pfam; PF21549; PRDM2_PR; 1.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   Pfam; PF12874; zf-met; 2.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
DR   Genevisible; Q9NQV6; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Disease variant; DNA-binding;
KW   Isopeptide bond; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..1147
FT                   /note="PR domain zinc finger protein 10"
FT                   /id="PRO_0000047767"
FT   DOMAIN          208..326
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   ZN_FING         355..377
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         530..552
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         560..582
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         588..610
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         616..639
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         644..666
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         672..695
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         727..750
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         772..795
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         834..857
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          110..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          953..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          988..1031
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1088..1147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..160
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..404
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        953..967
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1088..1103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1112..1147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         424
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         428
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17525332,
FT                   ECO:0007744|PubMed:21406692"
FT   CROSSLNK        380
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..97
FT                   /note="MDSKDESSHVWPTSAEHEQNAAQVHFVPDTGTVAQIVYTDDQVRPPQQVVYT
FT                   ADGASYTSVDGPEHTLVYIHPVEAAQTLFTDPGQVAYVQQDATAQ -> MSAYSVPSTF
FT                   A (in isoform 1, isoform 2 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10574462,
FT                   ECO:0000303|PubMed:10668202, ECO:0000303|PubMed:12175877,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_036351"
FT   VAR_SEQ         511..514
FT                   /note="Missing (in isoform 2, isoform 4 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:12175877,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035655"
FT   VAR_SEQ         952..985
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12175877"
FT                   /id="VSP_035656"
FT   VAR_SEQ         984
FT                   /note="I -> IQVSEPTASAPSSA (in isoform 4, isoform 5,
FT                   isoform 6 and isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT                   /id="VSP_036352"
FT   VAR_SEQ         1132..1147
FT                   /note="TTTNGNGSSEVHITKP -> AGSKVIQNEFTVGEECELETMTGEKVKTVVQL
FT                   EGDNKLVTTFKNIKSVTELNGDIITNTMTLGDIVFKRISKRI (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_036353"
FT   VARIANT         22
FT                   /note="A -> T (in dbSNP:rs11221912)"
FT                   /id="VAR_054418"
FT   VARIANT         573
FT                   /note="T -> A (in dbSNP:rs2241571)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT                   /id="VAR_019984"
FT   VARIANT         677
FT                   /note="C -> Y (in BHD2; likely pathogenic; results in
FT                   reduced FLCN promoter binding and severely decreased FLCN
FT                   expression)"
FT                   /evidence="ECO:0000269|PubMed:36440963"
FT                   /id="VAR_088741"
FT   CONFLICT        46
FT                   /note="P -> S (in Ref. 6; AAI12935)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        387
FT                   /note="T -> A (in Ref. 8; BAA91026)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        569
FT                   /note="F -> L (in Ref. 4; BX648944)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        621
FT                   /note="C -> Y (in Ref. 4; BX648944)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1112
FT                   /note="S -> N (in Ref. 4; BX648944)"
FT                   /evidence="ECO:0000305"
FT   HELIX           203..206
FT                   /evidence="ECO:0007829|PDB:3IHX"
FT   STRAND          212..214
FT                   /evidence="ECO:0007829|PDB:3IHX"
FT   TURN            216..218
FT                   /evidence="ECO:0007829|PDB:3IHX"
FT   STRAND          220..225
FT                   /evidence="ECO:0007829|PDB:3IHX"
FT   STRAND          248..250
FT                   /evidence="ECO:0007829|PDB:3IHX"
FT   TURN            278..280
FT                   /evidence="ECO:0007829|PDB:3IHX"
FT   HELIX           283..286
FT                   /evidence="ECO:0007829|PDB:3IHX"
FT   TURN            293..295
FT                   /evidence="ECO:0007829|PDB:3IHX"
FT   STRAND          298..302
FT                   /evidence="ECO:0007829|PDB:3IHX"
FT   STRAND          304..313
FT                   /evidence="ECO:0007829|PDB:3IHX"
FT   STRAND          323..325
FT                   /evidence="ECO:0007829|PDB:3IHX"
FT   HELIX           327..332
FT                   /evidence="ECO:0007829|PDB:3IHX"
SQ   SEQUENCE   1147 AA;  130136 MW;  E565CA8822CB2934 CRC64;
     MDSKDESSHV WPTSAEHEQN AAQVHFVPDT GTVAQIVYTD DQVRPPQQVV YTADGASYTS
     VDGPEHTLVY IHPVEAAQTL FTDPGQVAYV QQDATAQQAS LPVHNQVLPS IESVDGSDPL
     ATLQTPLGRL EAKEEEDEDE DEDTEEDEEE DGEDTDLDDW EPDPPRPFDP HDLWCEECNN
     AHASVCPKHG PLHPIPNRPV LTRARASLPL VLYIDRFLGG VFSKRRIPKR TQFGPVEGPL
     VRGSELKDCY IHLKVSLDKG DRKERDLHED LWFELSDETL CNWMMFVRPA QNHLEQNLVA
     YQYGHHVYYT TIKNVEPKQE LKVWYAASYA EFVNQKIHDI SEEERKVLRE QEKNWPCYEC
     NRRFISSEQL QQHLNSHDEK LDVFSRTRGR GRGRGKRRFG PGRRPGRPPK FIRLEITSEN
     GEKSDDGTQD LLHFPTKEQF DEAEPATLNG LDQPEQTTIP IPQLPQETQS SLEHEPETHT
     LHLQPQHEES VVPTQSTLTA DDMRRAKRIR LELQNAALQH LFIRKSFRPF KCLQCGKAFR
     EKDKLDQHLR FHGREGNCPL TCDLCNKGFI SSTSLESHMK LHSDQKTYSC IFCPESFDRL
     DLLKDHVAIH INDGYFTCPT CKKRFPDFIQ VKKHVRSFHS EKIYQCTECD KAFCRPDKLR
     LHMLRHSDRK DFLCSTCGKQ FKRKDKLREH MQRMHNPERE AKKADRISRS KTFKPRITST
     DYDSFTFKCR LCMMGFRRRG MLVNHLSKRH PDMKIEEVPE LTLPIIKPNR DYFCQYCDKV
     YKSASKRKAH ILKNHPGAEL PPSIRKLRPA GPGEPDPMLS THTQLTGTIA TPPVCCPHCS
     KQYSSKTKMV QHIRKKHPEF AQLSNTIHTP LTTAVISATP AVLTTDSATG ETVVTTDLLT
     QAMTELSQTL TTDYRTPQGD YQRIQYIPVS QSASGLQQPQ HIQLQVVQVA SATSPHQSQQ
     STVDVGQLHD PQPYPQHAIQ VQHIQVSGQP LSPSAQQAQQ GLSPSHIQGS SSTQGQALQQ
     QQQQQQNSSV QHTYLPSAWN SFRGYSSEIQ MMTLPPGQFV ITDSGVATPV TTGQVKAVTS
     GHYVLSESQS ELEEKQTSAL SGGVQVEPPA HSDSLDPQTN SQQQTTQYII TTTTNGNGSS
     EVHITKP
//