RWDD3_HUMAN
ID RWDD3_HUMAN Reviewed; 267 AA.
AC Q9Y3V2; A6NP44; A8K9F0; C9J9L7; C9JI45; Q08AJ7; Q6FID3; Q9BX35;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=RWD domain-containing protein 3;
DE AltName: Full=RWD domain-containing sumoylation enhancer;
DE Short=RSUME {ECO:0000303|PubMed:17956732};
GN Name=RWDD3; Synonyms=RSUME;
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 VARIANTS ALA-47 AND
RP LYS-86.
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANTS
RP ALA-47 AND LYS-86.
RC TISSUE=Thymus;
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 MRNA] (ISOFORM 2), AND VARIANTS ALA-47 AND
RP LYS-86.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ALA-47 AND
RP LYS-86.
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 FUNCTION, INTERACTION WITH UBE2I; SUMO1; NFKBIA AND HIF1A, INDUCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 61-TYR-PRO-62.
RX PubMed=17956732; DOI=10.1016/j.cell.2007.07.044;
RA Carbia-Nagashima A., Gerez J., Perez-Castro C., Paez-Pereda M.,
RA Silberstein S., Stalla G.K., Holsboer F., Arzt E.;
RT "RSUME, a small RWD-containing protein, enhances SUMO conjugation and
RT stabilizes HIF-1alpha during hypoxia.";
RL Cell 131:309-323(2007).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=22009797; DOI=10.1530/erc-11-0211;
RA Shan B., Gerez J., Haedo M., Fuertes M., Theodoropoulou M., Buchfelder M.,
RA Losa M., Stalla G.K., Arzt E., Renner U.;
RT "RSUME is implicated in HIF-1-induced VEGF-A production in pituitary tumour
RT cells.";
RL Endocr. Relat. Cancer 19:13-27(2012).
RN [8]
RP FUNCTION, INTERACTION WITH NR3C1 AND NCOA2, AND MUTAGENESIS OF
RP 61-TYR-PRO-62.
RX PubMed=23508108; DOI=10.1128/mcb.01470-12;
RA Druker J., Liberman A.C., Antunica-Noguerol M., Gerez J., Paez-Pereda M.,
RA Rein T., Iniguez-Lluhi J.A., Holsboer F., Arzt E.;
RT "RSUME enhances glucocorticoid receptor SUMOylation and transcriptional
RT activity.";
RL Mol. Cell. Biol. 33:2116-2127(2013).
RN [9]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORM 4), INTERACTION WITH UBE2I; NFKBIA
RP AND HIF1A, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=23469069; DOI=10.1371/journal.pone.0057795;
RA Gerez J., Fuertes M., Tedesco L., Silberstein S., Sevlever G.,
RA Paez-Pereda M., Holsboer F., Turjanski A.G., Arzt E.;
RT "In silico structural and functional characterization of the RSUME splice
RT variants.";
RL PLoS ONE 8:E57795-E57795(2013).
RN [10]
RP STRUCTURE BY NMR OF 1-121.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RWD domain of human RWD domain containing
RT protein 3.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [11] {ECO:0007744|PDB:4Y1L}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH UBC9, INTERACTION
RP WITH UBC9, DOMAIN, AND NMR.
RX PubMed=25918163; DOI=10.1074/jbc.m115.644047;
RA Alontaga A.Y., Ambaye N.D., Li Y.J., Vega R., Chen C.H., Bzymek K.P.,
RA Williams J.C., Hu W., Chen Y.;
RT "RWD domain as an E2 (Ubc9)-interaction module.";
RL J. Biol. Chem. 290:16550-16559(2015).
CC -!- FUNCTION: Enhancer of SUMO conjugation. Via its interaction with
CC UBE2I/UBC9, increases SUMO conjugation to proteins by promoting the
CC binding of E1 and E2 enzymes, thioester linkage between SUMO and
CC UBE2I/UBC9 and transfer of SUMO to specific target proteins which
CC include HIF1A, PIAS, NFKBIA, NR3C1 and TOP1. Isoform 1 and isoform 2
CC positively regulate the NF-kappa-B signaling pathway by enhancing the
CC sumoylation of NF-kappa-B inhibitor alpha (NFKBIA), promoting its
CC stabilization which consequently leads to an increased inhibition of
CC NF-kappa-B transcriptional activity. Isoform 1 and isoform 2 negatively
CC regulate the hypoxia-inducible factor-1 alpha (HIF1A) signaling pathway
CC by increasing the sumoylation of HIF1A, promoting its stabilization,
CC transcriptional activity and the expression of its target gene VEGFA
CC during hypoxia. Isoform 2 promotes the sumoylation and transcriptional
CC activity of the glucocorticoid receptor NR3C1 and enhances the
CC interaction of SUMO1 and NR3C1 with UBE2I/UBC9. Has no effect on
CC ubiquitination. {ECO:0000269|PubMed:17956732,
CC ECO:0000269|PubMed:22009797, ECO:0000269|PubMed:23469069,
CC ECO:0000269|PubMed:23508108}.
CC -!- SUBUNIT: Isoform 1 and isoform 2 interact with UBE2I/UBC9
CC (PubMed:17956732, PubMed:23469069, PubMed:25918163). Isoform 1 shows a
CC greater interaction with NFKBIA and HIF1A as compared to isoform 2
CC (PubMed:17956732, PubMed:23469069). Isoform 2 interacts with NCOA2 and
CC NR3C1 (PubMed:23508108). {ECO:0000269|PubMed:17956732,
CC ECO:0000269|PubMed:23469069, ECO:0000269|PubMed:23508108,
CC ECO:0000269|PubMed:25918163}.
CC -!- INTERACTION:
CC Q9Y3V2; P63165: SUMO1; NbExp=2; IntAct=EBI-1549885, EBI-80140;
CC Q9Y3V2; P63279: UBE2I; NbExp=5; IntAct=EBI-1549885, EBI-80168;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17956732}. Cytoplasm
CC {ECO:0000269|PubMed:17956732}. Note=Colocalizes with UBC9/UBE2I in
CC nuclear spots. {ECO:0000269|PubMed:17956732}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9Y3V2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3V2-2; Sequence=VSP_034176, VSP_034177;
CC Name=3;
CC IsoId=Q9Y3V2-3; Sequence=VSP_035411, VSP_035412;
CC Name=4;
CC IsoId=Q9Y3V2-4; Sequence=VSP_035412;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in glioma
CC tumors (at protein level). Expressed in a wide number of tissues with
CC highest expression in cerebellum, pituitary, heart, kidney, liver,
CC stomach, pancreas, prostate and spleen. Low levels in thalamus, spinal
CC cord, esophagus, thymus, lung and peripheral blood leukocytes. A higher
CC level expression seen in pituitary tumors as compared to the pituitary
CC gland. {ECO:0000269|PubMed:17956732, ECO:0000269|PubMed:22009797,
CC ECO:0000269|PubMed:23469069}.
CC -!- INDUCTION: Induced by hypoxia and heat shock.
CC {ECO:0000269|PubMed:17956732, ECO:0000269|PubMed:22009797,
CC ECO:0000269|PubMed:23469069}.
CC -!- DOMAIN: The RWD domain is required for the sumoylation enhancement
CC activity. {ECO:0000250}.
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; AL050062; CAB43254.2; -; mRNA.
DR EMBL; AK292665; BAF85354.1; -; mRNA.
DR EMBL; AK292699; BAF85388.1; -; mRNA.
DR EMBL; CR533493; CAG38524.1; -; mRNA.
DR EMBL; AC092802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010936; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC125142; AAI25143.1; -; mRNA.
DR CCDS; CCDS41357.1; -. [Q9Y3V2-1]
DR CCDS; CCDS44177.1; -. [Q9Y3V2-2]
DR RefSeq; NP_001121614.1; NM_001128142.1. [Q9Y3V2-2]
DR RefSeq; NP_001265176.1; NM_001278247.1. [Q9Y3V2-3]
DR RefSeq; NP_001265177.1; NM_001278248.1.
DR PDB; 2EBK; NMR; -; A=1-121.
DR PDB; 4Y1L; X-ray; 2.70 A; C=2-113.
DR PDBsum; 2EBK; -.
DR PDBsum; 4Y1L; -.
DR AlphaFoldDB; Q9Y3V2; -.
DR BMRB; Q9Y3V2; -.
DR SMR; Q9Y3V2; -.
DR BioGRID; 117445; 8.
DR IntAct; Q9Y3V2; 4.
DR STRING; 9606.ENSP00000359221; -.
DR iPTMnet; Q9Y3V2; -.
DR PhosphoSitePlus; Q9Y3V2; -.
DR BioMuta; RWDD3; -.
DR DMDM; 296453018; -.
DR EPD; Q9Y3V2; -.
DR MassIVE; Q9Y3V2; -.
DR MaxQB; Q9Y3V2; -.
DR PaxDb; Q9Y3V2; -.
DR PeptideAtlas; Q9Y3V2; -.
DR PRIDE; Q9Y3V2; -.
DR ProteomicsDB; 86080; -. [Q9Y3V2-1]
DR ProteomicsDB; 86081; -. [Q9Y3V2-2]
DR ProteomicsDB; 86082; -. [Q9Y3V2-3]
DR Antibodypedia; 33670; 141 antibodies from 23 providers.
DR DNASU; 25950; -.
DR Ensembl; ENST00000263893.10; ENSP00000263893.6; ENSG00000122481.17. [Q9Y3V2-2]
DR Ensembl; ENST00000370202.5; ENSP00000359221.4; ENSG00000122481.17. [Q9Y3V2-1]
DR GeneID; 25950; -.
DR KEGG; hsa:25950; -.
DR MANE-Select; ENST00000370202.5; ENSP00000359221.4; NM_015485.5; NP_056300.3.
DR UCSC; uc001drf.5; human. [Q9Y3V2-1]
DR CTD; 25950; -.
DR DisGeNET; 25950; -.
DR GeneCards; RWDD3; -.
DR HGNC; HGNC:21393; RWDD3.
DR HPA; ENSG00000122481; Low tissue specificity.
DR MIM; 615875; gene.
DR neXtProt; NX_Q9Y3V2; -.
DR OpenTargets; ENSG00000122481; -.
DR PharmGKB; PA134974302; -.
DR VEuPathDB; HostDB:ENSG00000122481; -.
DR eggNOG; ENOG502QSYH; Eukaryota.
DR GeneTree; ENSGT00390000000954; -.
DR HOGENOM; CLU_087636_0_0_1; -.
DR InParanoid; Q9Y3V2; -.
DR OMA; PMVHQLV; -.
DR OrthoDB; 1437243at2759; -.
DR PhylomeDB; Q9Y3V2; -.
DR TreeFam; TF324344; -.
DR PathwayCommons; Q9Y3V2; -.
DR Reactome; R-HSA-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR SignaLink; Q9Y3V2; -.
DR SIGNOR; Q9Y3V2; -.
DR BioGRID-ORCS; 25950; 7 hits in 1070 CRISPR screens.
DR ChiTaRS; RWDD3; human.
DR EvolutionaryTrace; Q9Y3V2; -.
DR GeneWiki; RWDD3; -.
DR GenomeRNAi; 25950; -.
DR Pharos; Q9Y3V2; Tbio.
DR PRO; PR:Q9Y3V2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y3V2; protein.
DR Bgee; ENSG00000122481; Expressed in endometrium and 95 other tissues.
DR Genevisible; Q9Y3V2; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:1902073; P:positive regulation of hypoxia-inducible factor-1alpha signaling pathway; IDA:UniProtKB.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; IDA:UniProtKB.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR038840; RWDD3.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR15628; PTHR15628; 1.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50908; RWD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..267
FT /note="RWD domain-containing protein 3"
FT /id="PRO_0000097545"
FT DOMAIN 7..114
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT REGION 13..15
FT /note="Interaction with UBE2I/UBC9"
FT /evidence="ECO:0000269|PubMed:25918163"
FT REGION 100..102
FT /note="Interaction with UBE2I/UBC9"
FT /evidence="ECO:0000269|PubMed:25918163"
FT VAR_SEQ 1..28
FT /note="MAEPVQEELSVLAAIFCRPHEWEVLSRS -> MFLSCGSLHQRGP (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035411"
FT VAR_SEQ 177..267
FT /note="KIILILLQGDRNNLKEYLILQKTSKVDVDSSGKKCKEKMISVLFETKVQTEH
FT KRFLAFEVKEYSALDELQKEFETAGLKKLFSEFVLALVK -> VLDSSENLQSRCGLKW
FT KEMQREND (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035412"
FT VAR_SEQ 192..195
FT /note="EYLI -> VPKS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.3"
FT /id="VSP_034176"
FT VAR_SEQ 196..267
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.3"
FT /id="VSP_034177"
FT VARIANT 47
FT /note="V -> A (in dbSNP:rs259358)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.3"
FT /id="VAR_034420"
FT VARIANT 86
FT /note="N -> K (in dbSNP:rs2296308)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.3"
FT /id="VAR_024346"
FT MUTAGEN 61..62
FT /note="YP->AA: Abolishes enhancement of NFKBIA and NR3C1
FT sumoylation. No effect on NR3C1 transcriptional activity."
FT /evidence="ECO:0000269|PubMed:17956732,
FT ECO:0000269|PubMed:23508108"
FT CONFLICT 79
FT /note="Q -> R (in Ref. 3; CAG38524)"
FT /evidence="ECO:0000305"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:4Y1L"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:4Y1L"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:4Y1L"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:4Y1L"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:2EBK"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:4Y1L"
FT TURN 59..63
FT /evidence="ECO:0007829|PDB:4Y1L"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2EBK"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:4Y1L"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:4Y1L"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2EBK"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:4Y1L"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4Y1L"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:2EBK"
SQ SEQUENCE 267 AA; 30543 MW; 00F6892F29A57CA7 CRC64;
MAEPVQEELS VLAAIFCRPH EWEVLSRSET DGTVFRIHTK AEGFMDVDIP LELVFHLPVN
YPSCLPGISI NSEQLTRAQC VTVKENLLEQ AESLLSEPMV HELVLWIQQN LRHILSQPET
GSGSEKCTFS TSTTMDDGLW ITLLHLDHMR AKTKYVKIVE KWASDLRLTG RLMFMGKIIL
ILLQGDRNNL KEYLILQKTS KVDVDSSGKK CKEKMISVLF ETKVQTEHKR FLAFEVKEYS
ALDELQKEFE TAGLKKLFSE FVLALVK
