ID RFX7_HUMAN Reviewed; 1460 AA.
AC Q2KHR2; Q6ZRR1; Q6ZTY6; Q8N3J0; Q9H7A9; Q9H956;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2024, sequence version 2.
DT 27-MAR-2024, entry version 144.
DE RecName: Full=DNA-binding protein RFX7 {ECO:0000305};
DE AltName: Full=Regulatory factor X 7;
DE AltName: Full=Regulatory factor X domain-containing protein 2;
GN Name=RFX7 {ECO:0000312|HGNC:HGNC:25777}; Synonyms=RFXDC2;
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 NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 284-1460 (ISOFORM 3).
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1065-1460 (ISOFORM 3).
RC TISSUE=Melanoma;
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 IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=18673564; DOI=10.1186/1471-2148-8-226;
RA Aftab S., Semenec L., Chu J.S.-C., Chen N.;
RT "Identification and characterization of novel human tissue-specific RFX
RT transcription factors.";
RL BMC Evol. Biol. 8:226-226(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
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 [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 SER-379; SER-455; THR-988;
RP SER-1178 AND SER-1329, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-704, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1178, 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 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1178, AND IDENTIFICATION BY
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322; SER-379; SER-418;
RP SER-455; THR-564; SER-662; THR-988 AND SER-1178, AND IDENTIFICATION BY MASS
RP 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 [15]
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 [16]
RP FUNCTION.
RX PubMed=29967452; DOI=10.1038/s41590-018-0144-9;
RA Castro W., Chelbi S.T., Niogret C., Ramon-Barros C., Welten S.P.M.,
RA Osterheld K., Wang H., Rota G., Morgado L., Vivier E., Raeber M.E.,
RA Boyman O., Delorenzi M., Barras D., Ho P.C., Oxenius A., Guarda G.;
RT "The transcription factor Rfx7 limits metabolism of NK cells and promotes
RT their maintenance and immunity.";
RL Nat. Immunol. 19:809-820(2018).
RN [17]
RP FUNCTION.
RX PubMed=34197623; DOI=10.1093/nar/gkab575;
RA Coronel L., Riege K., Schwab K., Foerste S., Haeckes D., Semerau L.,
RA Bernhart S.H., Siebert R., Hoffmann S., Fischer M.;
RT "Transcription factor RFX7 governs a tumor suppressor network in response
RT to p53 and stress.";
RL Nucleic Acids Res. 49:7437-7456(2021).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 182-198 IN COMPLEX WITH RFXANK,
RP AND MOTIF.
RA Tempel W., Xu C., Dong A., Li Y., Bountra C., Arrowsmith C.H.,
RA Edwards A.M., Min J.;
RT "Crystal structure of RFXANK ankyrin repeats in complex with RFX7.";
RL Submitted (JUN-2014) to the PDB data bank.
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 182-198 IN COMPLEX WITH ANKRA2,
RP INTERACTION WITH ANKRA2 AND RFXANK, AND MOTIF.
RX PubMed=25752541; DOI=10.1016/j.str.2015.02.001;
RA Nie J., Xu C., Jin J., Aka J.A., Tempel W., Nguyen V., You L., Weist R.,
RA Min J., Pawson T., Yang X.J.;
RT "Ankyrin repeats of ANKRA2 recognize a PxLPxL motif on the 3M syndrome
RT protein CCDC8.";
RL Structure 23:700-712(2015).
RN [20]
RP INVOLVEMENT IN MRD71, VARIANTS MRD71 742-SER--GLY-1460 DEL;
RP 745-GLU--GLY-1460 DEL; 762-GLY--GLY-1460 DEL; 906-TYR--GLY-1460 DEL;
RP 964-PRO-THR-965 DEL; LEU-1028 AND VAL-1029, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=33658631; DOI=10.1038/s41436-021-01114-z;
RA Harris H.K., Nakayama T., Lai J., Zhao B., Argyrou N., Gubbels C.S.,
RA Soucy A., Genetti C.A., Suslovitch V., Rodan L.H., Tiller G.E., Lesca G.,
RA Gripp K.W., Asadollahi R., Hamosh A., Applegate C.D., Turnpenny P.D.,
RA Simon M.E.H., Volker-Touw C.M.L., Gassen K.L.I.V., Binsbergen E.V.,
RA Pfundt R., Gardeitchik T., Vries B.B.A., Immken L.L., Buchanan C.,
RA Willing M., Toler T.L., Fassi E., Baker L., Vansenne F., Wang X.,
RA Ambrus J.L. Jr., Fannemel M., Posey J.E., Agolini E., Novelli A., Rauch A.,
RA Boonsawat P., Fagerberg C.R., Larsen M.J., Kibaek M., Labalme A.,
RA Poisson A., Payne K.K., Walsh L.E., Aldinger K.A., Balciuniene J.,
RA Skraban C., Gray C., Murrell J., Bupp C.P., Pascolini G., Grammatico P.,
RA Broly M., Kuery S., Nizon M., Rasool I.G., Zahoor M.Y., Kraus C., Reis A.,
RA Iqbal M., Uguen K., Audebert-Bellanger S., Ferec C., Redon S., Baker J.,
RA Wu Y., Zampino G., Syrbe S., Brosse I., Jamra R.A., Dobyns W.B.,
RA Cohen L.L., Blomhoff A., Mignot C., Keren B., Courtin T., Agrawal P.B.,
RA Beggs A.H., Yu T.W.;
RT "Disruption of RFX family transcription factors causes autism, attention-
RT deficit/hyperactivity disorder, intellectual disability, and dysregulated
RT behavior.";
RL Genet. Med. 23:1028-1040(2021).
RN [21]
RP VARIANT MRD71 SER-1028.
RX PubMed=36334883; DOI=10.1016/j.ejmg.2022.104657;
RA Ledger M.L., Kaare M., Mailo J.A., Jain-Ghai S.;
RT "Phenotype expansion and neurological manifestations of neurobehavioural
RT disease caused by a variant in RFX7.";
RL Eur. J. Med. Genet. 66:104657-104657(2023).
CC -!- FUNCTION: Transcription factor (PubMed:29967452). Acts as a
CC transcriptional activator by binding to promoter regions of target
CC genes, such as PDCD4, PIK3IP1, MXD4, PNRC1, and RFX5 (PubMed:29967452,
CC PubMed:34197623). Plays a role in natural killer (NK) cell maintenance
CC and immunity (PubMed:29967452). May play a role in the process of
CC ciliogenesis in the neural tube and neural tube closure (By
CC similarity). {ECO:0000250|UniProtKB:A0A1L8H0H2,
CC ECO:0000269|PubMed:29967452, ECO:0000269|PubMed:34197623}.
CC -!- SUBUNIT: Interacts (via PxLPxI/L motif) with RFXANK (via ankyrin
CC repeats) (PubMed:25752541). Interacts (via PxLPxI/L motif) with ANKRA2
CC (via ankyrin repeats) (PubMed:25752541). {ECO:0000269|PubMed:25752541,
CC ECO:0000312|PDB:6MEW}.
CC -!- INTERACTION:
CC Q2KHR2; Q9H9E1: ANKRA2; NbExp=2; IntAct=EBI-1222187, EBI-10215533;
CC Q2KHR2; O14593: RFXANK; NbExp=2; IntAct=EBI-1222187, EBI-1057665;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q2KHR2-3; Sequence=Displayed;
CC Name=3;
CC IsoId=Q2KHR2-1; Sequence=VSP_062138;
CC Name=2;
CC IsoId=Q2KHR2-2; Sequence=VSP_062139;
CC -!- TISSUE SPECIFICITY: Widely expressed in many different tissue types
CC including thymus and placenta, with high expression in brain
CC (PubMed:18673564). Expressed in both inhibitory and excitatory neurons
CC in cortex (PubMed:33658631). {ECO:0000269|PubMed:18673564,
CC ECO:0000269|PubMed:33658631}.
CC -!- DEVELOPMENTAL STAGE: Expressed in interneurons from the medial
CC ganglionic eminence in developing cortex.
CC {ECO:0000269|PubMed:33658631}.
CC -!- DOMAIN: The PxLPxI/L motif mediates interaction with ankyrin repeats of
CC ANKRA2 and RFXANK. {ECO:0000269|PubMed:25752541, ECO:0000312|PDB:6MEW}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 71,
CC with behavioral abnormalities (MRD71) [MIM:620330]: An autosomal
CC dominant neurodevelopmental disorder characterized by global
CC developmental delay, hypotonia, speech delay, and impaired intellectual
CC development. Most patients manifest neurobehavioral features including
CC autism spectrum disorder and attention-deficit/hyperactivity disorder.
CC Other frequent features include hypersensitivity to sensory stimuli and
CC sleep problems. {ECO:0000269|PubMed:33658631,
CC ECO:0000269|PubMed:36334883}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the RFX family. {ECO:0000255|PROSITE-
CC ProRule:PRU00858}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14381.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14988.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC86441.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AK023056; BAB14381.1; ALT_INIT; mRNA.
DR EMBL; AK024757; BAB14988.1; ALT_INIT; mRNA.
DR EMBL; AK126103; BAC86441.1; ALT_INIT; mRNA.
DR EMBL; AK128045; BAC87248.1; -; mRNA.
DR EMBL; AC068726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC247040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC112936; AAI12937.1; -; mRNA.
DR EMBL; AL834302; CAD38972.1; -; mRNA.
DR CCDS; CCDS92003.1; -. [Q2KHR2-3]
DR CCDS; CCDS92004.1; -. [Q2KHR2-2]
DR CCDS; CCDS92005.1; -. [Q2KHR2-3]
DR RefSeq; NP_073752.5; NM_022841.5. [Q2KHR2-3]
DR RefSeq; XP_005254660.2; XM_005254603.3.
DR RefSeq; XP_011520227.1; XM_011521925.2.
DR RefSeq; XP_016877995.1; XM_017022506.1.
DR RefSeq; XP_016877996.1; XM_017022507.1.
DR RefSeq; XP_016877997.1; XM_017022508.1.
DR PDB; 4QQI; X-ray; 2.03 A; X=182-198.
DR PDB; 6MEW; X-ray; 1.78 A; B/D=182-198.
DR PDBsum; 4QQI; -.
DR PDBsum; 6MEW; -.
DR AlphaFoldDB; Q2KHR2; -.
DR SMR; Q2KHR2; -.
DR BioGRID; 122335; 20.
DR ELM; Q2KHR2; -.
DR IntAct; Q2KHR2; 15.
DR STRING; 9606.ENSP00000501317; -.
DR GlyCosmos; Q2KHR2; 1 site, 1 glycan.
DR GlyGen; Q2KHR2; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q2KHR2; -.
DR PhosphoSitePlus; Q2KHR2; -.
DR BioMuta; RFX7; -.
DR DMDM; 121946796; -.
DR EPD; Q2KHR2; -.
DR jPOST; Q2KHR2; -.
DR MassIVE; Q2KHR2; -.
DR MaxQB; Q2KHR2; -.
DR PaxDb; 9606-ENSP00000453281; -.
DR PeptideAtlas; Q2KHR2; -.
DR ProteomicsDB; 61305; -. [Q2KHR2-1]
DR ProteomicsDB; 61306; -. [Q2KHR2-2]
DR Pumba; Q2KHR2; -.
DR Antibodypedia; 25133; 59 antibodies from 11 providers.
DR DNASU; 64864; -.
DR Ensembl; ENST00000559447.8; ENSP00000453281.3; ENSG00000181827.16. [Q2KHR2-3]
DR Ensembl; ENST00000673997.1; ENSP00000501278.1; ENSG00000181827.16. [Q2KHR2-1]
DR Ensembl; ENST00000674082.1; ENSP00000501248.1; ENSG00000181827.16. [Q2KHR2-1]
DR GeneID; 64864; -.
DR KEGG; hsa:64864; -.
DR MANE-Select; ENST00000559447.8; ENSP00000453281.3; NM_022841.7; NP_073752.6.
DR UCSC; uc059jng.1; human. [Q2KHR2-3]
DR AGR; HGNC:25777; -.
DR CTD; 64864; -.
DR DisGeNET; 64864; -.
DR GeneCards; RFX7; -.
DR HGNC; HGNC:25777; RFX7.
DR HPA; ENSG00000181827; Low tissue specificity.
DR MalaCards; RFX7; -.
DR MIM; 612660; gene.
DR MIM; 620330; phenotype.
DR neXtProt; NX_Q2KHR2; -.
DR OpenTargets; ENSG00000181827; -.
DR PharmGKB; PA162401255; -.
DR VEuPathDB; HostDB:ENSG00000181827; -.
DR eggNOG; KOG3712; Eukaryota.
DR GeneTree; ENSGT01050000244970; -.
DR HOGENOM; CLU_252972_0_0_1; -.
DR InParanoid; Q2KHR2; -.
DR OMA; MSMNSSH; -.
DR OrthoDB; 2961139at2759; -.
DR PhylomeDB; Q2KHR2; -.
DR TreeFam; TF321340; -.
DR PathwayCommons; Q2KHR2; -.
DR SignaLink; Q2KHR2; -.
DR BioGRID-ORCS; 64864; 27 hits in 382 CRISPR screens.
DR ChiTaRS; RFX7; human.
DR GenomeRNAi; 64864; -.
DR Pharos; Q2KHR2; Tdark.
DR PRO; PR:Q2KHR2; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q2KHR2; Protein.
DR Bgee; ENSG00000181827; Expressed in skeletal muscle tissue of rectus abdominis and 184 other cell types or tissues.
DR ExpressionAtlas; Q2KHR2; baseline and differential.
DR Genevisible; Q2KHR2; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 6.10.140.1290; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR003150; DNA-bd_RFX.
DR InterPro; IPR039779; RFX-like.
DR InterPro; IPR040889; RFX5_N.
DR InterPro; IPR047009; RFX5_N_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12619:SF2; DNA-BINDING PROTEIN RFX7; 1.
DR PANTHER; PTHR12619; RFX TRANSCRIPTION FACTOR FAMILY; 1.
DR Pfam; PF18326; RFX5_N; 1.
DR Pfam; PF02257; RFX_DNA_binding; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51526; RFX_DBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Autism spectrum disorder;
KW Disease variant; DNA-binding; Intellectual disability; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1460
FT /note="DNA-binding protein RFX7"
FT /id="PRO_0000342186"
FT DNA_BIND 108..183
FT /note="RFX-type winged-helix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00858"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 188..193
FT /note="PxLPxI/L motif; mediates interaction with ANKRA2 and
FT RFXANK"
FT /evidence="ECO:0000269|PubMed:25752541,
FT ECO:0000312|PDB:6MEW"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..963
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 564
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 704
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 988
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..98
FT /note="MAEEQQQPPPQQPDAHQQLPPSAPNSGVALPALVPGLPGTEASALQHKIKNS
FT ICKTVQSKVDCILQEVEKFTDLEKLYLYLQLPSGLSNGEKSDQNAM -> M (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_062138"
FT VAR_SEQ 1366..1460
FT /note="VGQGASDLTNTASDFSSDIRLSSELSGSINDLNTLDPNLLFDPGRQQGQDDE
FT ATLEELKNDPLFQQICSESMNSMTSSGFEWIESKDHPTVEMLG -> CSCPSSLLAGMQ
FT M (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_062139"
FT VARIANT 531
FT /note="G -> V (in dbSNP:rs16976751)"
FT /id="VAR_044135"
FT VARIANT 742..1460
FT /note="Missing (in MRD71; likely pathogenic)"
FT /evidence="ECO:0000269|PubMed:33658631"
FT /id="VAR_088507"
FT VARIANT 745..1460
FT /note="Missing (in MRD71; likely pathogenic)"
FT /evidence="ECO:0000269|PubMed:33658631"
FT /id="VAR_088508"
FT VARIANT 762..1460
FT /note="Missing (in MRD71; likely pathogenic)"
FT /evidence="ECO:0000269|PubMed:33658631"
FT /id="VAR_088509"
FT VARIANT 774
FT /note="V -> L (in dbSNP:rs3803460)"
FT /id="VAR_044136"
FT VARIANT 906..1460
FT /note="Missing (in MRD71; likely pathogenic)"
FT /evidence="ECO:0000269|PubMed:33658631"
FT /id="VAR_088510"
FT VARIANT 964..965
FT /note="Missing (in MRD71; uncertain significance;
FT dbSNP:rs551989191)"
FT /evidence="ECO:0000269|PubMed:33658631"
FT /id="VAR_088511"
FT VARIANT 1028
FT /note="P -> L (in MRD71; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:33658631"
FT /id="VAR_088512"
FT VARIANT 1028
FT /note="P -> S (in MRD71; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:36334883"
FT /id="VAR_088513"
FT VARIANT 1029
FT /note="I -> V (in MRD71; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:33658631"
FT /id="VAR_088514"
FT VARIANT 1353
FT /note="L -> P (in dbSNP:rs33984059)"
FT /id="VAR_044137"
FT CONFLICT 608
FT /note="E -> K (in Ref. 1; BAC86441)"
FT /evidence="ECO:0000305"
FT CONFLICT 836
FT /note="H -> R (in Ref. 1; BAC87248)"
FT /evidence="ECO:0000305"
FT CONFLICT 1190
FT /note="R -> Q (in Ref. 1; BAC87248)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1460 AA; 157351 MW; 5C6656F47D4D33A8 CRC64;
MAEEQQQPPP QQPDAHQQLP PSAPNSGVAL PALVPGLPGT EASALQHKIK NSICKTVQSK
VDCILQEVEK FTDLEKLYLY LQLPSGLSNG EKSDQNAMSS SRAQQMHAFS WIRNTLEEHP
ETSLPKQEVY DEYKSYCDNL GYHPLSAADF GKIMKNVFPN MKARRLGTRG KSKYCYSGLR
KKAFVHMPTL PNLDFHKTGD GLEGAEPSGQ LQNIDEEVIS SACRLVCEWA QKVLSQPFDT
VLELARFLVK SHYIGTKSMA ALTVMAAAPA GMKGITQPSA FIPTAESNSF QPQVKTLPSP
IDAKQQLQRK IQKKQQEQKL QSPLPGESAA KKSESATSNG VTNLPNGNPS ILSPQPIGIV
VAAVPSPIPV QRTRQLVTSP SPMSSSDGKV LPLNVQVVTQ HMQSVKQAPK TPQNVPASPG
GDRSARHRYP QILPKPANTS ALTIRSPTTV LFTSSPIKTA VVPASHMSSL NVVKMTTISL
TPSNSNTPLK HSASVSSATG TTEESRSVPQ IKNGSVVSLQ SPGSRSSSAG GTSAVEVKVE
PETSSDEHPV QCQENSDEAK APQTPSALLG QKSNTDGALQ KPSNEGVIEI KATKVCDQRT
KCKSRCNEML PGTSTGNNQS TITLSVASQN LTFTSSSSPP NGDSINKDPK LCTKSPRKRL
SSTLQETQVP PVKKPIVEQL SAATIEGQKQ GSVKKDQKVP HSGKTEGSTA GAQIPSKVSV
NVSSHIGANQ PLNSSALVIS DSALEQQTTP SSSPDIKVKL EGSVFLLDSD SKSVGSFNPN
GWQQITKDSE FISASCEQQQ DISVMTIPEH SDINDLEKSV WELEGMPQDT YSQQLHSQIQ
ESSLNQIQAH SSDQLPLQSE LKEFEPSVSQ TNESYFPFDD ELTQDSIVEE LVLMEQQMSM
NNSHSYGNCL GMTLQSQSVT PGAPMSSHTS STHFYHPIHS NGTPIHTPTP TPTPTPTPTP
TPTPTSEMIA GSQSLSRESP CSRLAQTTPV DSALGSSRHT PIGTPHSNCS SSVPPSPVEC
RNPFAFTPIS SSMAYHDASI VSSSPVKPMQ RPMATHPDKT KLEWMNNGYS GVGNSSVSGH
GILPSYQELV EDRFRKPHAF AVPGQSYQSQ SRHHDTHFGR LTPVSPVQHQ GATVNNTNKQ
EGFAVPAPLD NKGTNSSASS NFRCRSVSPA VHRQRNLSGS TLYPVSNIPR SNVTPFGSPV
TPEVHVFTNV HTDACANNIA QRSQSVPLTV MMQTAFPNAL QKQANSKKIT NVLLSKLDSD
NDDAVRGLGM NNLPSNYTAR MNLTQILEPS TVFPSANPQN MIDSSTSVYE FQTPSYLTKS
NSTGQINFSP GDNQAQSEIG EQQLDFNSTV KDLLSGDSLQ TNQQLVGQGA SDLTNTASDF
SSDIRLSSEL SGSINDLNTL DPNLLFDPGR QQGQDDEATL EELKNDPLFQ QICSESMNSM
TSSGFEWIES KDHPTVEMLG
//
