RFX2_HUMAN
ID RFX2_HUMAN Reviewed; 723 AA.
AC P48378; A8K581; B3KNC4; Q6IQ44; Q8SNA2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=DNA-binding protein RFX2;
DE AltName: Full=Regulatory factor X 2;
GN Name=RFX2;
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), AND VARIANT THR-86.
RX PubMed=8289803; DOI=10.1128/mcb.14.2.1230-1244.1994;
RA Reith W., Ucla C., Barras E., Gaud A., Durand B., Herrero-Sanchez C.,
RA Kobr M., Mach B.;
RT "RFX1, a transactivator of hepatitis B virus enhancer I, belongs to a novel
RT family of homodimeric and heterodimeric DNA-binding proteins.";
RL Mol. Cell. Biol. 14:1230-1244(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-86.
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].
RC TISSUE=Brain;
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-610.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [6]
RP VARIANTS [LARGE SCALE ANALYSIS] GLY-37 AND LYS-110.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [7]
RP SUBUNIT, AND DNA-BINDING.
RX PubMed=10330134; DOI=10.1128/mcb.19.6.3940;
RA Iwama A., Pan J., Zhang P., Reith W., Mach B., Tenen D.G., Sun Z.;
RT "Dimeric RFX proteins contribute to the activity and lineage specificity of
RT the interleukin-5 receptor alpha promoter through activation and repression
RT domains.";
RL Mol. Cell. Biol. 19:3940-3950(1999).
CC -!- FUNCTION: Transcription factor that acts as a key regulator of
CC spermatogenesis. Acts by regulating expression of genes required for
CC the haploid phase during spermiogenesis, such as genes required for
CC cilium assembly and function (By similarity). Recognizes and binds the
CC X-box, a regulatory motif with DNA sequence 5'-GTNRCC(0-3N)RGYAAC-3'
CC present on promoters (PubMed:10330134). Probably activates
CC transcription of the testis-specific histone gene H1-6 (By similarity).
CC {ECO:0000250|UniProtKB:P48379, ECO:0000269|PubMed:10330134}.
CC -!- SUBUNIT: Homodimer; probably only forms homodimers in testis (By
CC similarity). Heterodimer; heterodimerizes with RFX1 and RFX3
CC (PubMed:10330134). {ECO:0000250|UniProtKB:P48379,
CC ECO:0000269|PubMed:10330134}.
CC -!- INTERACTION:
CC P48378; O00167-2: EYA2; NbExp=3; IntAct=EBI-746731, EBI-12807776;
CC P48378; Q92949: FOXJ1; NbExp=5; IntAct=EBI-746731, EBI-1760377;
CC P48378; Q96NZ1: FOXN4; NbExp=3; IntAct=EBI-746731, EBI-11749712;
CC P48378; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-746731, EBI-10271199;
CC P48378; O75928-2: PIAS2; NbExp=3; IntAct=EBI-746731, EBI-348567;
CC P48378; Q8HWS3: RFX6; NbExp=4; IntAct=EBI-746731, EBI-746118;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B2GV50,
CC ECO:0000255|PROSITE-ProRule:PRU00858}. Cytoplasm
CC {ECO:0000250|UniProtKB:B2GV50}. Note=Mainly expressed in the nucleus
CC and at lower level in cytoplasm. {ECO:0000250|UniProtKB:B2GV50}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P48378-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48378-2; Sequence=VSP_037811;
CC -!- SIMILARITY: Belongs to the RFX family. {ECO:0000255|PROSITE-
CC ProRule:PRU00858}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG51286.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X76091; CAA53705.1; -; mRNA.
DR EMBL; AK024288; BAG51286.1; ALT_INIT; mRNA.
DR EMBL; AK291196; BAF83885.1; -; mRNA.
DR EMBL; AC011444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028579; AAH28579.1; -; mRNA.
DR EMBL; BC071571; AAH71571.1; -; mRNA.
DR CCDS; CCDS12157.1; -. [P48378-1]
DR CCDS; CCDS12158.1; -. [P48378-2]
DR PIR; B55926; B55926.
DR RefSeq; NP_000626.2; NM_000635.3. [P48378-1]
DR RefSeq; NP_602309.1; NM_134433.2. [P48378-2]
DR RefSeq; XP_011526473.1; XM_011528171.2.
DR AlphaFoldDB; P48378; -.
DR SMR; P48378; -.
DR BioGRID; 111922; 21.
DR IntAct; P48378; 12.
DR MINT; P48378; -.
DR STRING; 9606.ENSP00000306335; -.
DR iPTMnet; P48378; -.
DR PhosphoSitePlus; P48378; -.
DR BioMuta; RFX2; -.
DR DMDM; 254763325; -.
DR EPD; P48378; -.
DR jPOST; P48378; -.
DR MassIVE; P48378; -.
DR MaxQB; P48378; -.
DR PaxDb; P48378; -.
DR PeptideAtlas; P48378; -.
DR PRIDE; P48378; -.
DR ProteomicsDB; 55881; -. [P48378-1]
DR ProteomicsDB; 55882; -. [P48378-2]
DR Antibodypedia; 24073; 157 antibodies from 25 providers.
DR DNASU; 5990; -.
DR Ensembl; ENST00000303657.10; ENSP00000306335.4; ENSG00000087903.13. [P48378-1]
DR Ensembl; ENST00000359161.7; ENSP00000352076.3; ENSG00000087903.13. [P48378-1]
DR Ensembl; ENST00000592546.5; ENSP00000467166.1; ENSG00000087903.13. [P48378-2]
DR GeneID; 5990; -.
DR KEGG; hsa:5990; -.
DR MANE-Select; ENST00000303657.10; ENSP00000306335.4; NM_000635.4; NP_000626.2.
DR UCSC; uc002meb.4; human. [P48378-1]
DR CTD; 5990; -.
DR DisGeNET; 5990; -.
DR GeneCards; RFX2; -.
DR HGNC; HGNC:9983; RFX2.
DR HPA; ENSG00000087903; Tissue enhanced (testis).
DR MIM; 142765; gene.
DR neXtProt; NX_P48378; -.
DR OpenTargets; ENSG00000087903; -.
DR PharmGKB; PA34353; -.
DR VEuPathDB; HostDB:ENSG00000087903; -.
DR eggNOG; KOG3712; Eukaryota.
DR GeneTree; ENSGT01050000244879; -.
DR HOGENOM; CLU_010393_1_1_1; -.
DR InParanoid; P48378; -.
DR OMA; QYMAIRQ; -.
DR OrthoDB; 346630at2759; -.
DR PhylomeDB; P48378; -.
DR TreeFam; TF321340; -.
DR PathwayCommons; P48378; -.
DR SignaLink; P48378; -.
DR SIGNOR; P48378; -.
DR BioGRID-ORCS; 5990; 9 hits in 1099 CRISPR screens.
DR ChiTaRS; RFX2; human.
DR GeneWiki; RFX2; -.
DR GenomeRNAi; 5990; -.
DR Pharos; P48378; Tbio.
DR PRO; PR:P48378; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P48378; protein.
DR Bgee; ENSG00000087903; Expressed in right uterine tube and 174 other tissues.
DR ExpressionAtlas; P48378; baseline and differential.
DR Genevisible; P48378; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; 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; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0001675; P:acrosome assembly; ISS:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR003150; DNA-bd_RFX.
DR InterPro; IPR039779; RFX-like.
DR InterPro; IPR007668; RFX1_trans_act.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12619; PTHR12619; 1.
DR Pfam; PF04589; RFX1_trans_act; 1.
DR Pfam; PF02257; RFX_DNA_binding; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51526; RFX_DBD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cilium biogenesis/degradation; Cytoplasm;
KW Differentiation; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Spermatogenesis; Transcription; Transcription regulation.
FT CHAIN 1..723
FT /note="DNA-binding protein RFX2"
FT /id="PRO_0000215288"
FT DNA_BIND 199..274
FT /note="RFX-type winged-helix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00858"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2GV50"
FT VAR_SEQ 175..199
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037811"
FT VARIANT 37
FT /note="A -> G (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036530"
FT VARIANT 86
FT /note="A -> T (in dbSNP:rs2288846)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:8289803"
FT /id="VAR_057151"
FT VARIANT 110
FT /note="E -> K (in a breast cancer sample; somatic mutation;
FT dbSNP:rs748493309)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036531"
FT VARIANT 610
FT /note="R -> Q (in dbSNP:rs17852566)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_058416"
FT CONFLICT 44
FT /note="A -> S (in Ref. 1; CAA53705)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="S -> P (in Ref. 2; BAF83885)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="P -> H (in Ref. 4; AAH71571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 723 AA; 79987 MW; 0F299954977A9218 CRC64;
MQNSEGGADS PASVALRPSA AAPPVPASPQ RVLVQAASSN PKGAQMQPIS LPRVQQVPQQ
VQPVQHVYPA QVQYVEGGDA VYTNGAIRTA YTYNPEPQMY APSSTASYFE APGGAQVTVA
ASSPPAVPSH SMVGITMDVG GSPIVSSAGA YLIHGGMDST RHSLAHTSRS SPATLEMAIE
NLQKSEGITS HKSGLLNSHL QWLLDNYETA EGVSLPRSSL YNHYLRHCQE HKLDPVNAAS
FGKLIRSVFM GLRTRRLGTR GNSKYHYYGI RLKPDSPLNR LQEDTQYMAM RQQPMHQKPR
YRPAQKTDSL GDSGSHSGLH STPEQTMAVQ SQHHQQYIDV SHVFPEFPAP DLGSFLLQDG
VTLHDVKALQ LVYRRHCEAT VDVVMNLQFH YIEKLWLSFW NSKASSSDGP TSLPASDEDP
EGAVLPKDKL ISLCQCDPIL RWMRSCDHIL YQALVEILIP DVLRPVPSTL TQAIRNFAKS
LEGWLTNAMS DFPQQVIQTK VGVVSAFAQT LRRYTSLNHL AQAARAVLQN TSQINQMLSD
LNRVDFANVQ EQASWVCQCE ESVVQRLEQD FKLTLQQQSS LDQWASWLDS VVTQVLKQHA
GSPSFPKAAR QFLLKWSFYS SMVIRDLTLR SAASFGSFHL IRLLYDEYMF YLVEHRVAEA
TGETPIAVMG EFNDLASLSL TLLDKDDMGD EQRGSEAGPD ARSLGEPLVK RERSDPNHSL
QGI
