FOXP4_HUMAN
ID FOXP4_HUMAN Reviewed; 680 AA.
AC Q8IVH2; Q5W098; Q7Z7F8; Q8IW55; Q96E19;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Forkhead box protein P4;
DE AltName: Full=Fork head-related protein-like A;
GN Name=FOXP4; Synonyms=FKHLA;
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).
RA Daigo Y., Takayama I., Fujino M.A.;
RT "Isolation, mapping, and characterization of a novel human cDNA
RT differentially expressed in the fundus of W/Wv mutant mice.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Lung, and Skin;
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 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 [6]
RP IDENTIFICATION BY 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-86 AND SER-554, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-246, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-175; LYS-246 AND LYS-378, 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).
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] THR-464.
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).
CC -!- FUNCTION: Transcriptional repressor that represses lung-specific
CC expression. {ECO:0000250}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with FOXP1 and FOXP2.
CC Dimerization is required for DNA-binding (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q8IVH2; Q9H334: FOXP1; NbExp=6; IntAct=EBI-1054619, EBI-983809;
CC Q8IVH2; O15409: FOXP2; NbExp=6; IntAct=EBI-1054619, EBI-983612;
CC Q8IVH2-2; Q92993: KAT5; NbExp=3; IntAct=EBI-25885364, EBI-399080;
CC Q8IVH2-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-25885364, EBI-11742507;
CC Q8IVH2-2; P17252: PRKCA; NbExp=3; IntAct=EBI-25885364, EBI-1383528;
CC Q8IVH2-2; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-25885364, EBI-9090795;
CC Q8IVH2-2; P61981: YWHAG; NbExp=3; IntAct=EBI-25885364, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IVH2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IVH2-2; Sequence=VSP_043034;
CC Name=3;
CC IsoId=Q8IVH2-3; Sequence=VSP_043465, VSP_043466;
CC -!- DOMAIN: The leucine-zipper is required for dimerization and
CC transcriptional repression. {ECO:0000250}.
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DR EMBL; AB080747; BAC53809.1; -; mRNA.
DR EMBL; AL139331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04047.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04048.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04049.1; -; Genomic_DNA.
DR EMBL; BC013030; AAH13030.2; -; mRNA.
DR EMBL; BC040962; AAH40962.1; -; mRNA.
DR EMBL; BC052803; AAH52803.1; -; mRNA.
DR CCDS; CCDS34447.1; -. [Q8IVH2-1]
DR CCDS; CCDS34448.1; -. [Q8IVH2-2]
DR CCDS; CCDS4856.1; -. [Q8IVH2-3]
DR RefSeq; NP_001012426.1; NM_001012426.1. [Q8IVH2-1]
DR RefSeq; NP_001012427.1; NM_001012427.1. [Q8IVH2-2]
DR RefSeq; NP_612466.1; NM_138457.2. [Q8IVH2-3]
DR PDB; 6XAT; X-ray; 2.20 A; A=464-550.
DR PDBsum; 6XAT; -.
DR AlphaFoldDB; Q8IVH2; -.
DR SMR; Q8IVH2; -.
DR BioGRID; 125474; 62.
DR DIP; DIP-59301N; -.
DR IntAct; Q8IVH2; 57.
DR MINT; Q8IVH2; -.
DR STRING; 9606.ENSP00000362151; -.
DR iPTMnet; Q8IVH2; -.
DR PhosphoSitePlus; Q8IVH2; -.
DR BioMuta; FOXP4; -.
DR DMDM; 46395887; -.
DR EPD; Q8IVH2; -.
DR jPOST; Q8IVH2; -.
DR MassIVE; Q8IVH2; -.
DR MaxQB; Q8IVH2; -.
DR PaxDb; Q8IVH2; -.
DR PeptideAtlas; Q8IVH2; -.
DR PRIDE; Q8IVH2; -.
DR ProteomicsDB; 70705; -. [Q8IVH2-1]
DR ProteomicsDB; 70706; -. [Q8IVH2-2]
DR ProteomicsDB; 70707; -. [Q8IVH2-3]
DR ABCD; Q8IVH2; 2 sequenced antibodies.
DR Antibodypedia; 1453; 272 antibodies from 35 providers.
DR DNASU; 116113; -.
DR Ensembl; ENST00000307972.10; ENSP00000309823.4; ENSG00000137166.17. [Q8IVH2-1]
DR Ensembl; ENST00000373057.7; ENSP00000362148.3; ENSG00000137166.17. [Q8IVH2-2]
DR Ensembl; ENST00000373063.7; ENSP00000362154.3; ENSG00000137166.17. [Q8IVH2-3]
DR GeneID; 116113; -.
DR KEGG; hsa:116113; -.
DR MANE-Select; ENST00000307972.10; ENSP00000309823.4; NM_001012426.2; NP_001012426.1.
DR UCSC; uc003oql.4; human. [Q8IVH2-1]
DR CTD; 116113; -.
DR DisGeNET; 116113; -.
DR GeneCards; FOXP4; -.
DR HGNC; HGNC:20842; FOXP4.
DR HPA; ENSG00000137166; Low tissue specificity.
DR MIM; 608924; gene.
DR neXtProt; NX_Q8IVH2; -.
DR OpenTargets; ENSG00000137166; -.
DR PharmGKB; PA134943098; -.
DR VEuPathDB; HostDB:ENSG00000137166; -.
DR eggNOG; KOG4385; Eukaryota.
DR GeneTree; ENSGT00940000158700; -.
DR HOGENOM; CLU_019502_3_1_1; -.
DR InParanoid; Q8IVH2; -.
DR OMA; NGQNHTP; -.
DR OrthoDB; 836427at2759; -.
DR PhylomeDB; Q8IVH2; -.
DR TreeFam; TF326978; -.
DR PathwayCommons; Q8IVH2; -.
DR SignaLink; Q8IVH2; -.
DR BioGRID-ORCS; 116113; 24 hits in 1101 CRISPR screens.
DR ChiTaRS; FOXP4; human.
DR GeneWiki; FOXP4; -.
DR GenomeRNAi; 116113; -.
DR Pharos; Q8IVH2; Tbio.
DR PRO; PR:Q8IVH2; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8IVH2; protein.
DR Bgee; ENSG00000137166; Expressed in kidney epithelium and 164 other tissues.
DR ExpressionAtlas; Q8IVH2; baseline and differential.
DR Genevisible; Q8IVH2; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR032354; FOXP-CC.
DR InterPro; IPR030456; TF_fork_head_CS_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00250; Forkhead; 1.
DR Pfam; PF16159; FOXP-CC; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..680
FT /note="Forkhead box protein P4"
FT /id="PRO_0000091889"
FT ZN_FING 307..332
FT /note="C2H2-type"
FT DNA_BIND 467..559
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..370
FT /note="Leucine-zipper"
FT REGION 407..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 141..142
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043034"
FT VAR_SEQ 220
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043465"
FT VAR_SEQ 384..395
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043466"
FT VARIANT 464
FT /note="A -> T (in a breast cancer sample; somatic mutation;
FT dbSNP:rs867245225)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036219"
FT HELIX 472..482
FT /evidence="ECO:0007829|PDB:6XAT"
FT HELIX 490..500
FT /evidence="ECO:0007829|PDB:6XAT"
FT HELIX 502..506
FT /evidence="ECO:0007829|PDB:6XAT"
FT HELIX 509..521
FT /evidence="ECO:0007829|PDB:6XAT"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:6XAT"
FT STRAND 535..538
FT /evidence="ECO:0007829|PDB:6XAT"
SQ SEQUENCE 680 AA; 73488 MW; A63826ED85B24752 CRC64;
MMVESASETI RSAPSGQNGV GSLSGQADGS SGGATGTTAS GTGREVTTGA DSNGEMSPAE
LLHFQQQQAL QVARQFLLQQ ASGLSSPGNN DSKQSASAVQ VPVSVAMMSP QMLTPQQMQQ
ILSPPQLQAL LQQQQALMLQ QLQEYYKKQQ EQLHLQLLTQ QQAGKPQPKE ALGNKQLAFQ
QQLLQMQQLQ QQHLLNLQRQ GLVSLQPNQA SGPLQTLPQA AVCPTDLPQL WKGEGAPGQP
AEDSVKQEGL DLTGTAATAT SFAAPPKVSP PLSHHTLPNG QPTVLTSRRD SSSHEETPGS
HPLYGHGECK WPGCETLCED LGQFIKHLNT EHALDDRSTA QCRVQMQVVQ QLEIQLAKES
ERLQAMMAHL HMRPSEPKPF SQPLNPVPGS SSFSKVTVSA ADSFPDGLVH PPTSAAAPVT
PLRPPGLGSA SLHGGGPARR RSSDKFCSPI SSELAQNHEF YKNADVRPPF TYASLIRQAI
LETPDRQLTL NEIYNWFTRM FAYFRRNTAT WKNAVRHNLS LHKCFVRVEN VKGAVWTVDE
REYQKRRPPK MTGSPTLVKN MISGLSYGAL NASYQAALAE SSFPLLNSPG MLNPGSASSL
LPLSHDDVGA PVEPLPSNGS SSPPRLSPPQ YSHQVQVKEE PAEAEEDRQP GPPLGAPNPS
ASGPPEDRDL EEELPGEELS
