RREB1_HUMAN
ID RREB1_HUMAN Reviewed; 1687 AA.
AC Q92766; A2RRF5; E2GM80; E2GM81; O75567; O75568; Q5VYB2; Q6BEP5; Q6BEP6;
AC Q6BEP8; Q86SU2; Q9Y474;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Ras-responsive element-binding protein 1;
DE Short=RREB-1;
DE AltName: Full=Finger protein in nuclear bodies;
DE AltName: Full=Raf-responsive zinc finger protein LZ321;
DE AltName: Full=Zinc finger motif enhancer-binding protein 1;
DE Short=Zep-1;
GN Name=RREB1; Synonyms=FINB;
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 PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9305772; DOI=10.1016/s0378-1119(97)00172-8;
RA Fujimoto-Nishiyama A., Ishii S., Matsuda S., Inoue J., Yamamoto T.;
RT "A novel zinc finger protein, Finb, is a transcriptional activator and
RT localized in nuclear bodies.";
RL Gene 195:267-275(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), VARIANTS ARG-195; VAL-783
RP AND PRO-1467, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15067362;
RA Date S., Nibu Y., Yanai K., Hirata J., Yagami K., Fukamizu A.;
RT "Finb, a multiple zinc finger protein, represses transcription of the human
RT angiotensinogen gene.";
RL Int. J. Mol. Med. 13:637-642(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6), ALTERNATIVE SPLICING, AND
RP VARIANTS ARG-195 AND VAL-783.
RX PubMed=21703425; DOI=10.1016/j.ajpath.2011.03.038;
RA Nitz M.D., Harding M.A., Smith S.C., Thomas S., Theodorescu D.;
RT "RREB1 transcription factor splice variants in urologic cancer.";
RL Am. J. Pathol. 179:477-486(2011).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-324 (ISOFORM 1), AND VARIANTS ARG-195 AND PRO-1467.
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 849-1687 (ISOFORM 1), TISSUE SPECIFICITY, AND
RP FUNCTION.
RC TISSUE=Thyroid carcinoma;
RX PubMed=8816445; DOI=10.1128/mcb.16.10.5335;
RA Thiagalingam A., de Bustros A., Borges M., Jasti R., Compton D.,
RA Diamond L., Mabry M., Ball D.W., Baylin S.B., Nelkin B.D.;
RT "RREB-1, a novel zinc finger protein, is involved in the differentiation
RT response to Ras in human medullary thyroid carcinomas.";
RL Mol. Cell. Biol. 16:5335-5345(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1161-1687 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 1161-1633 (ISOFORM 2), VARIANT PRO-1467, AND FUNCTION.
RC TISSUE=Liver;
RX PubMed=10390538; DOI=10.1093/nar/27.14.2947;
RA Zhang L., Zhao J., Edenberg H.J.;
RT "A human Raf-responsive zinc-finger protein that binds to divergent
RT sequences.";
RL Nucleic Acids Res. 27:2947-2956(1999).
RN [8]
RP INTERACTION WITH NEUROD1, AND FUNCTION.
RX PubMed=12482979; DOI=10.1128/mcb.23.1.259-271.2003;
RA Ray S.K., Nishitani J., Petry M.W., Fessing M.Y., Leiter A.B.;
RT "Novel transcriptional potentiation of BETA2/NeuroD on the secretin gene
RT promoter by the DNA-binding protein Finb/RREB-1.";
RL Mol. Cell. Biol. 23:259-271(2003).
RN [9]
RP INTERACTION WITH AR, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17550981; DOI=10.1210/me.2006-0503;
RA Mukhopadhyay N.K., Cinar B., Mukhopadhyay L., Lutchman M., Ferdinand A.S.,
RA Kim J., Chung L.W.K., Adam R.M., Ray S.K., Leiter A.B., Richie J.P.,
RA Liu B.C.-S., Freeman M.R.;
RT "The zinc finger protein Ras-responsive element binding protein-1 is a
RT coregulator of the androgen receptor: implications for the role of the Ras
RT pathway in enhancing androgenic signaling in prostate cancer.";
RL Mol. Endocrinol. 21:2056-2070(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-231; SER-1167;
RP SER-1174; SER-1175; SER-1219; SER-1225; THR-1315 AND SER-1653, 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1167; SER-1174 AND SER-1175,
RP AND 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-161; SER-231;
RP SER-1122; SER-1167; SER-1174; SER-1175 AND SER-1653, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-42; SER-161 AND
RP SER-1475, AND 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-161; SER-175;
RP SER-180; SER-231; SER-1122; SER-1140; SER-1167; SER-1174; SER-1175 AND
RP SER-1320, AND 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161 AND SER-1219, 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-551 AND LYS-615, AND
RP IDENTIFICATION BY MASS 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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-615, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-615 AND LYS-885, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-203 AND LYS-615, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-203; LYS-435; LYS-502; LYS-551;
RP LYS-566; LYS-593; LYS-613; LYS-615; LYS-624; LYS-857; LYS-885 AND LYS-913,
RP AND 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: Transcription factor that binds specifically to the RAS-
CC responsive elements (RRE) of gene promoters (PubMed:9305772,
CC PubMed:15067362, PubMed:8816445, PubMed:10390538, PubMed:17550981).
CC Represses the angiotensinogen gene (PubMed:15067362). Negatively
CC regulates the transcriptional activity of AR (PubMed:17550981).
CC Potentiates the transcriptional activity of NEUROD1 (PubMed:12482979).
CC Promotes brown adipocyte differentiation (By similarity). May be
CC involved in Ras/Raf-mediated cell differentiation by enhancing
CC calcitonin expression (PubMed:8816445). {ECO:0000250|UniProtKB:Q3UH06,
CC ECO:0000269|PubMed:10390538, ECO:0000269|PubMed:12482979,
CC ECO:0000269|PubMed:15067362, ECO:0000269|PubMed:17550981,
CC ECO:0000269|PubMed:8816445, ECO:0000269|PubMed:9305772}.
CC -!- SUBUNIT: Interacts with NEUROD1 (PubMed:12482979). Interacts with AR
CC (PubMed:17550981). {ECO:0000269|PubMed:12482979,
CC ECO:0000269|PubMed:17550981}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15067362,
CC ECO:0000269|PubMed:17550981, ECO:0000269|PubMed:9305772}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=beta;
CC IsoId=Q92766-1; Sequence=Displayed;
CC Name=2; Synonyms=alpha;
CC IsoId=Q92766-2; Sequence=VSP_026706;
CC Name=3; Synonyms=gamma;
CC IsoId=Q92766-3; Sequence=VSP_026707;
CC Name=4;
CC IsoId=Q92766-4; Sequence=VSP_026704, VSP_026705;
CC Name=5; Synonyms=delta;
CC IsoId=Q92766-5; Sequence=VSP_053540;
CC Name=6; Synonyms=epsilon;
CC IsoId=Q92766-6; Sequence=VSP_053538, VSP_053539;
CC -!- TISSUE SPECIFICITY: Expressed in heart, placenta, lung, liver, skeletal
CC muscle, kidney and pancreas. Not found in the brain.
CC {ECO:0000269|PubMed:8816445}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB19094.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC25598.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC26118.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH42910.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH42910.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA23165.1; Type=Miscellaneous discrepancy; Note=Numerous sequencing errors.; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=AAC26118.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D49835; BAA23165.1; ALT_SEQ; mRNA.
DR EMBL; AB019254; BAD32776.1; -; mRNA.
DR EMBL; AB019351; BAD32778.1; -; mRNA.
DR EMBL; AB019352; BAD32779.1; -; mRNA.
DR EMBL; HM369360; ADO14468.1; -; mRNA.
DR EMBL; HM369361; ADO14469.1; -; mRNA.
DR EMBL; AL139095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042910; AAH42910.1; ALT_SEQ; mRNA.
DR EMBL; BC131599; AAI31600.1; -; mRNA.
DR EMBL; U26914; AAB19094.1; ALT_FRAME; mRNA.
DR EMBL; AF072825; AAC25598.1; ALT_FRAME; mRNA.
DR EMBL; AF072826; AAC26118.1; ALT_FRAME; mRNA.
DR CCDS; CCDS34335.1; -. [Q92766-2]
DR CCDS; CCDS34336.1; -. [Q92766-1]
DR CCDS; CCDS54963.1; -. [Q92766-3]
DR RefSeq; NP_001003698.1; NM_001003698.3. [Q92766-1]
DR RefSeq; NP_001003699.1; NM_001003699.3. [Q92766-2]
DR RefSeq; NP_001003700.1; NM_001003700.1. [Q92766-3]
DR RefSeq; NP_001161816.1; NM_001168344.1. [Q92766-1]
DR RefSeq; XP_006715220.1; XM_006715157.3.
DR RefSeq; XP_011513097.1; XM_011514795.2.
DR AlphaFoldDB; Q92766; -.
DR BioGRID; 112153; 65.
DR CORUM; Q92766; -.
DR IntAct; Q92766; 39.
DR STRING; 9606.ENSP00000369270; -.
DR iPTMnet; Q92766; -.
DR PhosphoSitePlus; Q92766; -.
DR SwissPalm; Q92766; -.
DR BioMuta; RREB1; -.
DR DMDM; 152031673; -.
DR EPD; Q92766; -.
DR jPOST; Q92766; -.
DR MassIVE; Q92766; -.
DR MaxQB; Q92766; -.
DR PeptideAtlas; Q92766; -.
DR PRIDE; Q92766; -.
DR ProteomicsDB; 75450; -. [Q92766-1]
DR ProteomicsDB; 75451; -. [Q92766-2]
DR ProteomicsDB; 75452; -. [Q92766-3]
DR ProteomicsDB; 75453; -. [Q92766-4]
DR Antibodypedia; 9691; 207 antibodies from 31 providers.
DR DNASU; 6239; -.
DR Ensembl; ENST00000334984.10; ENSP00000335574.6; ENSG00000124782.21. [Q92766-3]
DR Ensembl; ENST00000349384.10; ENSP00000305560.10; ENSG00000124782.21. [Q92766-1]
DR Ensembl; ENST00000379933.7; ENSP00000369265.3; ENSG00000124782.21. [Q92766-1]
DR Ensembl; ENST00000379938.7; ENSP00000369270.2; ENSG00000124782.21. [Q92766-2]
DR GeneID; 6239; -.
DR KEGG; hsa:6239; -.
DR MANE-Select; ENST00000379938.7; ENSP00000369270.2; NM_001003699.4; NP_001003699.1. [Q92766-2]
DR UCSC; uc003mxb.4; human. [Q92766-1]
DR CTD; 6239; -.
DR DisGeNET; 6239; -.
DR GeneCards; RREB1; -.
DR HGNC; HGNC:10449; RREB1.
DR HPA; ENSG00000124782; Low tissue specificity.
DR MalaCards; RREB1; -.
DR MIM; 602209; gene.
DR neXtProt; NX_Q92766; -.
DR OpenTargets; ENSG00000124782; -.
DR Orphanet; 567; 22q11.2 deletion syndrome.
DR PharmGKB; PA34864; -.
DR VEuPathDB; HostDB:ENSG00000124782; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157533; -.
DR HOGENOM; CLU_002702_0_0_1; -.
DR InParanoid; Q92766; -.
DR OMA; VHMRTHC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q92766; -.
DR TreeFam; TF332503; -.
DR PathwayCommons; Q92766; -.
DR SignaLink; Q92766; -.
DR SIGNOR; Q92766; -.
DR BioGRID-ORCS; 6239; 77 hits in 1112 CRISPR screens.
DR ChiTaRS; RREB1; human.
DR GeneWiki; RREB1; -.
DR GenomeRNAi; 6239; -.
DR Pharos; Q92766; Tbio.
DR PRO; PR:Q92766; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q92766; protein.
DR Bgee; ENSG00000124782; Expressed in buccal mucosa cell and 209 other tissues.
DR ExpressionAtlas; Q92766; baseline and differential.
DR Genevisible; Q92766; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; TAS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IMP:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; IMP:UniProtKB.
DR GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IMP:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:UniProtKB.
DR GO; GO:1903691; P:positive regulation of wound healing, spreading of epidermal cells; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1687
FT /note="Ras-responsive element-binding protein 1"
FT /id="PRO_0000047326"
FT ZN_FING 66..88
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 97..119
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 125..147
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 208..230
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 235..258
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 316..338
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 643..665
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 671..693
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 699..722
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 753..775
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 790..815
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1246..1268
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1393..1415
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1512..1534
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1540..1562
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 25..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1409..1513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1524..1543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1558..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..964
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UH06"
FT MOD_RES 1122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UH06"
FT MOD_RES 1135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UH06"
FT MOD_RES 1140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1315
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UH06"
FT MOD_RES 1598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UH06"
FT MOD_RES 1653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 435
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 502
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 551
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 566
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 593
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 613
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 615
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 615
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 624
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 857
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 885
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 913
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..1200
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026704"
FT VAR_SEQ 300..314
FT /note="AWCETNLRRCISEQH -> GKGHTNVRPASEPSP (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:21703425"
FT /id="VSP_053538"
FT VAR_SEQ 315..1687
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:21703425"
FT /id="VSP_053539"
FT VAR_SEQ 1201..1268
FT /note="EDNTQDEVAGAPADHHGPSDEEQGSPPEDKLLRAKRNSYTNCLQKITCPHCP
FT RVFPWASSLQRHMLTH -> MLTHTGQKPFPCQKCDAFFSTKSNCERHQLRKHGVTTCS
FT LRRNGLIPQSKESDVGSHDS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026705"
FT VAR_SEQ 1269
FT /note="T -> TGQKPFPCQKCDAFFSTKSNCERHQLRKHGVTTCSLRRNGLIPQSKE
FT SDVGSHDST (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10390538,
FT ECO:0000303|PubMed:15067362"
FT /id="VSP_026706"
FT VAR_SEQ 1270..1535
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:21703425"
FT /id="VSP_053540"
FT VAR_SEQ 1270..1534
FT /note="DSQSDAETAAAAGEVLDLTSRDREQPSEGATELRQVAGDAPVEQATAETASP
FT VHREEHGRGESHEPEEEHGTEESTGDADGAEEDASSNQSLDLDFATKLMDFKLAEGDGE
FT AGAGGAASQEQKLACDTCGKSFKFLGTLSRHRKAHGRQEPKDEKGDGASTAEEGPQPAP
FT EQEEKPPETPAEVVESAPGAGEAPAEKLAEETEGPSDGESAAEKRSSEKSDDDKKPKTD
FT SPKSVASKADKRKKVCSVCNKRFWSLQDLTRHMRSH -> GQKPFPCQKCDAFFSTKSN
FT CERHQLRKHGVTTCSLRRNGLIPQSKESDVGSHDS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15067362"
FT /id="VSP_026707"
FT VARIANT 195
FT /note="G -> R (in dbSNP:rs1334576)"
FT /evidence="ECO:0000269|PubMed:15067362,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:21703425"
FT /id="VAR_033197"
FT VARIANT 783
FT /note="G -> V (in dbSNP:rs9502564)"
FT /evidence="ECO:0000269|PubMed:15067362,
FT ECO:0000269|PubMed:21703425"
FT /id="VAR_033198"
FT VARIANT 1171
FT /note="D -> N (in dbSNP:rs9379084)"
FT /id="VAR_033199"
FT VARIANT 1384
FT /note="G -> R (in dbSNP:rs2281833)"
FT /id="VAR_033200"
FT VARIANT 1467
FT /note="L -> P (in dbSNP:rs2256596)"
FT /evidence="ECO:0000269|PubMed:10390538,
FT ECO:0000269|PubMed:15067362, ECO:0000269|PubMed:15489334"
FT /id="VAR_033201"
FT VARIANT 1499
FT /note="S -> Y (in dbSNP:rs35742417)"
FT /id="VAR_033202"
FT CONFLICT 574
FT /note="A -> T (in Ref. 3; ADO14469)"
FT /evidence="ECO:0000305"
FT CONFLICT 866
FT /note="Q -> K (in Ref. 6; AAB19094)"
FT /evidence="ECO:0000305"
FT CONFLICT 994
FT /note="A -> V (in Ref. 3; ADO14469)"
FT /evidence="ECO:0000305"
FT CONFLICT 1148
FT /note="G -> R (in Ref. 6; AAB19094)"
FT /evidence="ECO:0000305"
FT CONFLICT 1321
FT /note="P -> R (in Ref. 7; AAC25598/AAC26118)"
FT /evidence="ECO:0000305"
FT CONFLICT 1394..1395
FT /note="AC -> SS (in Ref. 7; AAC25598/AAC26118)"
FT /evidence="ECO:0000305"
FT CONFLICT 1429
FT /note="S -> T (in Ref. 6; AAB19094)"
FT /evidence="ECO:0000305"
FT CONFLICT 1436
FT /note="Q -> S (in Ref. 6; AAB19094)"
FT /evidence="ECO:0000305"
FT CONFLICT 1683
FT /note="L -> H (in Ref. 6; AAB19094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1687 AA; 181420 MW; 33B5755B0243C64F CRC64;
MTSSSPAGLE GSDLSSINTM MSAVMSVGKV TENGGSPQGI KSPSKPPGPN RIGRRNQETK
EEKSSYNCPL CEKICTTQHQ LTMHIRQHNT DTGGADHSCS ICGKSLSSAS SLDRHMLVHS
GERPYKCTVC GQSFTTNGNM HRHMKIHEKD PNSATATAPP SPLKRRRLSS KRKLSHDAES
EREDPAPAKK MVEDGQSGDL EKKADEVFHC PVCFKEFVCK YGLETHMETH SDNPLRCDIC
CVTFRTHRGL LRHNALVHKQ LPRDAMGRPF IQNNPSIPAG FHDLGFTDFS CRKFPRISQA
WCETNLRRCI SEQHRFVCDT CDKAFPMLCS LALHKQTHVA ADQGQEKPQA TPLPGDALDQ
KGFLALLGLQ HTKDVRPAPA EEPLPDDNQA IQLQTLKCQL PQDPGCTNLL SLSPFEAASL
GGSLTVLPAT KDSIKHLSLQ PFQKGFIIQP DSSIVVKPIS GESAIELADI QQILKMAASA
PPQISLPPFS KAPAAPLQAI FKHMPPLKPK PLVTPRTVVA TSTPPPLINA QQASPGCISP
SLPPPPLKLL KGSVEAASNA HLLQSKSGTQ PHAATRLSLQ QPRAELPGQP EMKTQLEQDS
IIEALLPLSM EAKIKQEITE GELKAFMTAP GGKKTPAMRK VLYPCRFCNQ VFAFSGVLRA
HVRSHLGISP YQCNICDYIA ADKAALIRHL RTHSGERPYI CKICHYPFTV KANCERHLRK
KHLKATRKDI EKNIEYVSSS AAELVDAFCA PDTVCRLCGE DLKHYRALRI HMRTHCGRGL
GGGHKGRKPF ECKECSAAFA AKRNCIHHIL KQHLHVPEQD IESYVLAADG LGPAEAPAAE
ASGRGEDSGC AALGDCKPLT AFLEPQNGFL HRGPTQPPPP HVSIKLEPAS SFAVDFNEPL
DFSQKGLALV QVKQENISFL SPSSLVPYDC SMEPIDLSIP KNFRKGDKDL ATPSEAKKPE
EEAGSSEQPS PCPAPGPSLP VTLGPSGILE SPMAPAPAAT PEPPAQPLQG PVQLAVPIYS
SALVSSPPLV GSSALLSGTA LLRPLRPKPP LLLPKPPVTE ELPPLASIAQ IISSVSSAPT
LLKTKVADPG PASTGSNTTA SDSLGGSVPK AATTATPAAT TSPKESSEPP APASSPEAAS
PTEQGPAGTS KKRGRKRGMR SRPRANSGGV DLDSSGEFAS IEKMLATTDT NKFSPFLQTA
EDNTQDEVAG APADHHGPSD EEQGSPPEDK LLRAKRNSYT NCLQKITCPH CPRVFPWASS
LQRHMLTHTD SQSDAETAAA AGEVLDLTSR DREQPSEGAT ELRQVAGDAP VEQATAETAS
PVHREEHGRG ESHEPEEEHG TEESTGDADG AEEDASSNQS LDLDFATKLM DFKLAEGDGE
AGAGGAASQE QKLACDTCGK SFKFLGTLSR HRKAHGRQEP KDEKGDGAST AEEGPQPAPE
QEEKPPETPA EVVESAPGAG EAPAEKLAEE TEGPSDGESA AEKRSSEKSD DDKKPKTDSP
KSVASKADKR KKVCSVCNKR FWSLQDLTRH MRSHTGERPY KCQTCERTFT LKHSLVRHQR
IHQKARHAKH HGKDSDKEER GEEDSENEST HSGNNAVSEN EAELAPNASN HMAVTRSRKE
GLASATKDCS HREEKVTAGW PSEPGQGDLN PESPAALGQD LLEPRSKRPA HPILATADGA
SQLVGME
