S2A4R_HUMAN
ID S2A4R_HUMAN Reviewed; 387 AA.
AC Q9NR83; Q2PHL5; Q6F6I6; Q6F6I7; Q6GTK5; Q8TAH5; Q8WVW7; Q96QD3; Q9BV85;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 4.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=SLC2A4 regulator;
DE AltName: Full=GLUT4 enhancer factor;
DE Short=GEF;
DE AltName: Full=Huntington disease gene regulatory region-binding protein 1;
DE Short=HDBP-1;
GN Name=SLC2A4RG; Synonyms=HDBP1;
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 ASP-233.
RC TISSUE=Skeletal muscle;
RX PubMed=10825161; DOI=10.1074/jbc.m001452200;
RA Oshel K.M., Knight J.B., Cao K.T., Thai M.V., Olson A.L.;
RT "Identification of a 30-base pair regulatory element and novel DNA binding
RT protein that regulates the human GLUT4 promoter in transgenic mice.";
RL J. Biol. Chem. 275:23666-23673(2000).
RN [2]
RP SEQUENCE REVISION.
RA Olson A.L., Oshel K.M.;
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), VARIANT ASP-233, FUNCTION,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-257;
RP LEU-260; PHE-273 AND LEU-276.
RC TISSUE=Testis;
RX PubMed=14625278; DOI=10.1074/jbc.m310726200;
RA Tanaka K., Shouguchi-Miyata J., Miyamoto N., Ikeda J.-E.;
RT "Novel nuclear shuttle proteins, HDBP1 and HDBP2, bind to neuronal cell-
RT specific cis-regulatory element in the promoter for the human Huntington's
RT disease gene.";
RL J. Biol. Chem. 279:7275-7286(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ASP-233.
RC TISSUE=Ovary, Placenta, and Prostate;
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 TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH MEF2A, AND
RP FUNCTION.
RX PubMed=14630949; DOI=10.1073/pnas.2432756100;
RA Knight J.B., Eyster C.A., Griesel B.A., Olson A.L.;
RT "Regulation of the human GLUT4 gene promoter: interaction between a
RT transcriptional activator and myocyte enhancer factor 2A.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:14725-14730(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-268, 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).
CC -!- FUNCTION: Transcription factor involved in SLC2A4 and HD gene
CC transactivation. Binds to the consensus sequence 5'-GCCGGCG-3'.
CC {ECO:0000269|PubMed:14625278, ECO:0000269|PubMed:14630949}.
CC -!- SUBUNIT: Interacts with MEF2A. {ECO:0000269|PubMed:14630949}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the
CC cytoplasm and the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NR83-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NR83-4; Sequence=VSP_055908;
CC Name=3;
CC IsoId=Q9NR83-3; Sequence=VSP_055909;
CC -!- TISSUE SPECIFICITY: According to PubMed:14630949, expressed in heart,
CC skeletal muscle, liver, kidney and pancreas; undetectable in lung,
CC placenta or brain. According to PubMed:14625278, ubiquitously
CC expressed, with lowest expression in brain and ileum.
CC {ECO:0000269|PubMed:14625278, ECO:0000269|PubMed:14630949}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17446.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD29732.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AF249267; AAF97516.2; -; mRNA.
DR EMBL; AB044777; BAE71373.1; -; mRNA.
DR EMBL; AB044786; BAD29732.1; ALT_SEQ; mRNA.
DR EMBL; AB052777; BAD29733.1; -; mRNA.
DR EMBL; AL121845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001402; AAH01402.2; -; mRNA.
DR EMBL; BC017446; AAH17446.1; ALT_INIT; mRNA.
DR EMBL; BC028349; AAH28349.2; -; mRNA.
DR EMBL; BC052306; AAH52306.1; -; mRNA.
DR CCDS; CCDS13537.1; -. [Q9NR83-1]
DR RefSeq; NP_064446.2; NM_020062.3. [Q9NR83-1]
DR PDB; 7DTA; NMR; -; A=355-387.
DR PDBsum; 7DTA; -.
DR AlphaFoldDB; Q9NR83; -.
DR SMR; Q9NR83; -.
DR BioGRID; 121193; 3.
DR STRING; 9606.ENSP00000266077; -.
DR iPTMnet; Q9NR83; -.
DR PhosphoSitePlus; Q9NR83; -.
DR BioMuta; SLC2A4RG; -.
DR DMDM; 85700401; -.
DR jPOST; Q9NR83; -.
DR MassIVE; Q9NR83; -.
DR PaxDb; Q9NR83; -.
DR PeptideAtlas; Q9NR83; -.
DR PRIDE; Q9NR83; -.
DR ProteomicsDB; 82304; -. [Q9NR83-1]
DR Antibodypedia; 15361; 280 antibodies from 25 providers.
DR DNASU; 56731; -.
DR Ensembl; ENST00000266077.5; ENSP00000266077.2; ENSG00000125520.14. [Q9NR83-1]
DR GeneID; 56731; -.
DR KEGG; hsa:56731; -.
DR MANE-Select; ENST00000266077.5; ENSP00000266077.2; NM_020062.4; NP_064446.2.
DR UCSC; uc002ygq.4; human. [Q9NR83-1]
DR CTD; 56731; -.
DR DisGeNET; 56731; -.
DR GeneCards; SLC2A4RG; -.
DR HGNC; HGNC:15930; SLC2A4RG.
DR HPA; ENSG00000125520; Tissue enhanced (liver).
DR MIM; 609493; gene.
DR neXtProt; NX_Q9NR83; -.
DR OpenTargets; ENSG00000125520; -.
DR PharmGKB; PA38052; -.
DR VEuPathDB; HostDB:ENSG00000125520; -.
DR eggNOG; ENOG502SCW3; Eukaryota.
DR GeneTree; ENSGT00940000162832; -.
DR HOGENOM; CLU_032989_0_0_1; -.
DR InParanoid; Q9NR83; -.
DR OMA; KEALVRP; -.
DR OrthoDB; 915379at2759; -.
DR PhylomeDB; Q9NR83; -.
DR TreeFam; TF326610; -.
DR PathwayCommons; Q9NR83; -.
DR BioGRID-ORCS; 56731; 18 hits in 1081 CRISPR screens.
DR ChiTaRS; SLC2A4RG; human.
DR GeneWiki; SLC2A4RG; -.
DR GenomeRNAi; 56731; -.
DR Pharos; Q9NR83; Tbio.
DR PRO; PR:Q9NR83; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NR83; protein.
DR Bgee; ENSG00000125520; Expressed in apex of heart and 172 other tissues.
DR Genevisible; Q9NR83; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA: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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:GO_Central.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..387
FT /note="SLC2A4 regulator"
FT /id="PRO_0000047208"
FT ZN_FING 200..225
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 253..263
FT /note="Nuclear export signal"
FT MOTIF 351..354
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305"
FT COMPBIAS 145..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..198
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055908"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14625278"
FT /id="VSP_055909"
FT VARIANT 233
FT /note="E -> D (in dbSNP:rs8957)"
FT /evidence="ECO:0000269|PubMed:10825161,
FT ECO:0000269|PubMed:14625278, ECO:0000269|PubMed:15489334"
FT /id="VAR_025005"
FT MUTAGEN 257
FT /note="L->A: Nuclear; when associated with A-260."
FT /evidence="ECO:0000269|PubMed:14625278"
FT MUTAGEN 260
FT /note="L->A: Nuclear; when associated with A-257."
FT /evidence="ECO:0000269|PubMed:14625278"
FT MUTAGEN 273
FT /note="F->A: Cytoplasmic; when associated with A-276."
FT /evidence="ECO:0000269|PubMed:14625278"
FT MUTAGEN 276
FT /note="L->A: Cytoplasmic; when associated with A-273."
FT /evidence="ECO:0000269|PubMed:14625278"
FT CONFLICT 117..121
FT /note="SPLLL -> KPSPS (in Ref. 1; AAF97516)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="A -> V (in Ref. 3; BAD29733)"
FT /evidence="ECO:0000305"
FT HELIX 360..364
FT /evidence="ECO:0007829|PDB:7DTA"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:7DTA"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:7DTA"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:7DTA"
SQ SEQUENCE 387 AA; 41267 MW; C12F8D1BF629EB3E CRC64;
MERPPPRAAG RDPSALRAEA PWLRAEGPGP RAAPVTVPTP PQGSSVGGGF AGLEFARPQE
SEPRASDLGA PRTWTGAAAG PRTPSAHIPV PAQRATPGKA RLDEVMAAAA LTSLSTSPLL
LGAPVAAFSP EPGLEPWKEA LVRPPGSYSS SSNSGDWGWD LASDQSSPST PSPPLPPEAA
HFLFGEPTLR KRKSPAQVMF QCLWKSCGKV LSTASAMQRH IRLVHLGRQA EPEQSDGEED
FYYTELDVGV DTLTDGLSSL TPVSPTASMP PAFPRLELPE LLEPPALPSP LRPPAPPLPP
PPVLSTVANP QSCHSDRVYQ GCLTPARLEP QPTEVGACPP ALSSRIGVTL RKPRGDAKKC
RKVYGMERRD LWCTACRWKK ACQRFLD
