NKRF_HUMAN
ID NKRF_HUMAN Reviewed; 690 AA.
AC O15226; G3V1N1; Q4VC41; Q9UJ91;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=NF-kappa-B-repressing factor;
DE Short=NFkB-repressing factor {ECO:0000303|PubMed:10562553};
DE Short=NRF {ECO:0000303|PubMed:10562553};
DE AltName: Full=Protein ITBA4;
GN Name=NKRF {ECO:0000303|PubMed:32179686, ECO:0000312|HGNC:HGNC:19374};
GN Synonyms=ITBA4, NRF {ECO:0000303|PubMed:10562553};
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), FUNCTION, AND INTERACTION WITH
RP NF-KAPPA-B.
RC TISSUE=Cervix carcinoma;
RX PubMed=10562553; DOI=10.1093/emboj/18.22.6415;
RA Nourbakhsh M., Hauser H.;
RT "Constitutive silencing of IFN-beta promoter is mediated by NRF (NF-kB-
RT repressing factor), a nuclear inhibitor of NF-kB.";
RL EMBO J. 18:6415-6425(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Mao Y., Xie Y., Dai J.;
RT "Cloning and identification of human transcription factor NRF complete
RT cDNA.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas, 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-258 (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 453-690 (ISOFORM 1/2).
RC TISSUE=Brain;
RX PubMed=9224902; DOI=10.1016/s0378-1119(97)00108-x;
RA Frattini A., Faranda S., Bagnasco L., Patrosso C., Nulli P., Zucchi I.,
RA Vezzoni P.;
RT "Identification of a new member (ZNF183) of the Ring finger gene family in
RT Xq24-25.";
RL Gene 192:291-298(1997).
RN [8]
RP FUNCTION.
RX PubMed=12381793; DOI=10.1073/pnas.212306199;
RA Feng X., Guo Z., Nourbakhsh M., Hauser H., Ganster R., Shao L.,
RA Geller D.A.;
RT "Identification of a negative response element in the human inducible
RT nitric-oxide synthase (hiNOS) promoter: the role of NF-kappa B-repressing
RT factor (NRF) in basal repression of the hiNOS gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14212-14217(2002).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-618, AND IDENTIFICATION BY
RP 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 [12]
RP INTERACTION WITH XRN2.
RX PubMed=24462208; DOI=10.1016/j.molcel.2014.01.001;
RA Miki T.S., Richter H., Rueegger S., Grosshans H.;
RT "PAXT-1 promotes XRN2 activity by stabilizing it through a conserved
RT domain.";
RL Mol. Cell 53:351-360(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-500 AND LYS-674, 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-666 AND LYS-674, 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 [15] {ECO:0007744|PDB:6SH6, ECO:0007744|PDB:6SH7}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 541-603 IN COMPLEX WITH DHX15,
RP FUNCTION, INTERACTION WITH DHX15, AND MUTAGENESIS OF GLY-555; LEU-559;
RP TRP-564; LEU-569; GLY-590 AND LEU-591.
RX PubMed=32179686; DOI=10.1073/pnas.1913880117;
RA Studer M.K., Ivanovic L., Weber M.E., Marti S., Jonas S.;
RT "Structural basis for DEAH-helicase activation by G-patch proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:7159-7170(2020).
CC -!- FUNCTION: Enhances the ATPase activity of DHX15 by acting like a brace
CC that tethers mobile sections of DHX15 together, stabilizing a
CC functional conformation with high RNA affinity of DHX15
CC (PubMed:12381793). Involved in the constitutive silencing of the
CC interferon beta promoter, independently of the virus-induced signals,
CC and in the inhibition of the basal and cytokine-induced iNOS promoter
CC activity (PubMed:12381793). Also involved in the regulation of IL-8
CC transcription (PubMed:12381793). May also act as a DNA-binding
CC transcription regulator: interacts with a specific negative regulatory
CC element (NRE) 5'-AATTCCTCTGA-3' to mediate transcriptional repression
CC of certain NK-kappa-B responsive genes (PubMed:10562553).
CC {ECO:0000269|PubMed:10562553, ECO:0000269|PubMed:12381793}.
CC -!- SUBUNIT: Interacts with NF-kappa-B (PubMed:10562553). Interacts with
CC XRN2 (PubMed:24462208). Interacts (via G-patch domain) with DHX15;
CC promoting the RNA helicase activity of DHX15 (PubMed:32179686).
CC {ECO:0000269|PubMed:10562553, ECO:0000269|PubMed:24462208,
CC ECO:0000269|PubMed:32179686}.
CC -!- INTERACTION:
CC O15226; P78563-4: ADARB1; NbExp=3; IntAct=EBI-766011, EBI-12002366;
CC O15226; O43143: DHX15; NbExp=4; IntAct=EBI-766011, EBI-1237044;
CC O15226; Q96C10: DHX58; NbExp=2; IntAct=EBI-766011, EBI-744193;
CC O15226; O75569: PRKRA; NbExp=4; IntAct=EBI-766011, EBI-713955;
CC O15226; O95793: STAU1; NbExp=3; IntAct=EBI-766011, EBI-358174;
CC O15226; Q9UL40: ZNF346; NbExp=3; IntAct=EBI-766011, EBI-2462313;
CC O15226; P0DTC9: N; Xeno; NbExp=3; IntAct=EBI-766011, EBI-25475856;
CC O15226; PRO_0000449628 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-766011, EBI-25475880;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15226-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15226-2; Sequence=VSP_047377;
CC -!- TISSUE SPECIFICITY: Widely and constitutively expressed
CC (PubMed:10562553). Expressed at lower level in colon, peripheral blood
CC lymphocytes, lung and kidney (PubMed:10562553).
CC {ECO:0000269|PubMed:10562553}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AL539002; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=CAB56459.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ011812; CAB56459.1; ALT_FRAME; mRNA.
DR EMBL; AY208891; AAP43025.1; -; mRNA.
DR EMBL; AC004913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471161; EAW89859.1; -; Genomic_DNA.
DR EMBL; BC040379; AAH40379.1; -; mRNA.
DR EMBL; BC047878; AAH47878.1; -; mRNA.
DR EMBL; AL539002; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; Y07707; CAA68976.1; -; mRNA.
DR RefSeq; NP_001166958.1; NM_001173487.1.
DR RefSeq; NP_001166959.1; NM_001173488.1.
DR RefSeq; NP_060014.2; NM_017544.3.
DR RefSeq; XP_011529667.1; XM_011531365.2.
DR PDB; 6SH6; X-ray; 1.85 A; B=541-603.
DR PDB; 6SH7; X-ray; 2.21 A; B=541-603.
DR PDBsum; 6SH6; -.
DR PDBsum; 6SH7; -.
DR AlphaFoldDB; O15226; -.
DR SMR; O15226; -.
DR BioGRID; 121002; 213.
DR DIP; DIP-34570N; -.
DR IntAct; O15226; 66.
DR MINT; O15226; -.
DR STRING; 9606.ENSP00000442308; -.
DR ChEMBL; CHEMBL3163; -.
DR GlyGen; O15226; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15226; -.
DR MetOSite; O15226; -.
DR PhosphoSitePlus; O15226; -.
DR SwissPalm; O15226; -.
DR BioMuta; NKRF; -.
DR SWISS-2DPAGE; O15226; -.
DR EPD; O15226; -.
DR jPOST; O15226; -.
DR MassIVE; O15226; -.
DR MaxQB; O15226; -.
DR PaxDb; O15226; -.
DR PeptideAtlas; O15226; -.
DR PRIDE; O15226; -.
DR ProteomicsDB; 32386; -.
DR ProteomicsDB; 48517; -. [O15226-1]
DR Antibodypedia; 462; 211 antibodies from 30 providers.
DR DNASU; 55922; -.
DR Ensembl; ENST00000304449.8; ENSP00000304803.5; ENSG00000186416.18. [O15226-1]
DR Ensembl; ENST00000542113.3; ENSP00000442308.1; ENSG00000186416.18. [O15226-2]
DR GeneID; 55922; -.
DR KEGG; hsa:55922; -.
DR UCSC; uc004erq.3; human. [O15226-1]
DR CTD; 55922; -.
DR DisGeNET; 55922; -.
DR GeneCards; NKRF; -.
DR HGNC; HGNC:19374; NKRF.
DR HPA; ENSG00000186416; Low tissue specificity.
DR MIM; 300440; gene.
DR neXtProt; NX_O15226; -.
DR OpenTargets; ENSG00000186416; -.
DR PharmGKB; PA134990602; -.
DR VEuPathDB; HostDB:ENSG00000186416; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157256; -.
DR HOGENOM; CLU_025268_0_0_1; -.
DR InParanoid; O15226; -.
DR OrthoDB; 1179335at2759; -.
DR PhylomeDB; O15226; -.
DR TreeFam; TF326321; -.
DR PathwayCommons; O15226; -.
DR SignaLink; O15226; -.
DR SIGNOR; O15226; -.
DR BioGRID-ORCS; 55922; 11 hits in 708 CRISPR screens.
DR ChiTaRS; NKRF; human.
DR GeneWiki; NKRF_(gene); -.
DR GenomeRNAi; 55922; -.
DR Pharos; O15226; Tbio.
DR PRO; PR:O15226; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O15226; protein.
DR Bgee; ENSG00000186416; Expressed in postcentral gyrus and 175 other tissues.
DR ExpressionAtlas; O15226; baseline and differential.
DR Genevisible; O15226; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR CDD; cd02640; R3H_NRF; 1.
DR Gene3D; 3.30.1370.50; -; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR034071; R3H_NRF.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF01424; R3H; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00393; R3H; 1.
DR SUPFAM; SSF82708; SSF82708; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS51061; R3H; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..690
FT /note="NF-kappa-B-repressing factor"
FT /id="PRO_0000096869"
FT DOMAIN 551..596
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT DOMAIN 600..664
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT DNA_BIND 296..388
FT /evidence="ECO:0000269|PubMed:10562553"
FT REGION 1..296
FT /note="Active repression domain"
FT /evidence="ECO:0000269|PubMed:10562553"
FT REGION 27..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 25..45
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:10562553"
FT COMPBIAS 29..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 500
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 666
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 674
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 VAR_SEQ 1
FT /note="M -> MGFMLPLIFRYSPRLM (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_047377"
FT MUTAGEN 555
FT /note="G->E: Abolished interaction with DHX15."
FT /evidence="ECO:0000269|PubMed:32179686"
FT MUTAGEN 559
FT /note="L->E: Abolished interaction with DHX15."
FT /evidence="ECO:0000269|PubMed:32179686"
FT MUTAGEN 564
FT /note="W->A: Abolished interaction with DHX15."
FT /evidence="ECO:0000269|PubMed:32179686"
FT MUTAGEN 569
FT /note="L->E: Abolished interaction with DHX15."
FT /evidence="ECO:0000269|PubMed:32179686"
FT MUTAGEN 590
FT /note="G->E: Decreased, but not abolished interaction, with
FT DHX15."
FT /evidence="ECO:0000269|PubMed:32179686"
FT MUTAGEN 591
FT /note="L->E: Decreased, but not abolished interaction, with
FT DHX15."
FT /evidence="ECO:0000269|PubMed:32179686"
FT CONFLICT 71
FT /note="R -> G (in Ref. 1; CAB56459)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="C -> G (in Ref. 7; CAA68976)"
FT /evidence="ECO:0000305"
FT CONFLICT 614..615
FT /note="AR -> ES (in Ref. 1; CAB56459)"
FT /evidence="ECO:0000305"
FT HELIX 554..561
FT /evidence="ECO:0007829|PDB:6SH6"
FT STRAND 570..573
FT /evidence="ECO:0007829|PDB:6SH7"
FT TURN 591..595
FT /evidence="ECO:0007829|PDB:6SH7"
SQ SEQUENCE 690 AA; 77673 MW; 3067A52671A7AE8F CRC64;
MEKILQMAEG IDIGEMPSYD LVLSKPSKGQ KRHLSTCDGQ NPPKKQAGSK FHARPRFEPV
HFVASSSKDE RQEDPYGPQT KEVNEQTHFA SMPRDIYQDY TQDSFSIQDG NSQYCDSSGF
ILTKDQPVTA NMYFDSGNPA PSTTSQQANS QSTPEPSPSQ TFPESVVAEK QYFIEKLTAT
IWKNLSNPEM TSGSDKINYT YMLTRCIQAC KTNPEYIYAP LKEIPPADIP KNKKLLTDGY
ACEVRCQNIY LTTGYAGSKN GSRDRATELA VKLLQKRIEV RVVRRKFKHT FGEDLVVCQI
GMSSYEFPPA LKPPEDLVVL GKDASGQPIF NASAKHWTNF VITENANDAI GILNNSASFN
KMSIEYKYEM MPNRTWRCRV FLQDHCLAEG YGTKKTSKHA AADEALKILQ KTQPTYPSVK
SSQCHTGSSP RGSGKKKDIK DLVVYENSSN PVCTLNDTAQ FNRMTVEYVY ERMTGLRWKC
KVILESEVIA EAVGVKKTVK YEAAGEAVKT LKKTQPTVIN NLKKGAVEDV ISRNEIQGRS
AEEAYKQQIK EDNIGNQLLR KMGWTGGGLG KSGEGIREPI SVKEQHKREG LGLDVERVNK
IAKRDIEQII RNYARSESHT DLTFSRELTN DERKQIHQIA QKYGLKSKSH GVGHDRYLVV
GRKRRKEDLL DQLKQEGQVG HYELVMPQAN
