E2F6_HUMAN
ID E2F6_HUMAN Reviewed; 281 AA.
AC O75461; A8K2Z8; G5E936; O60544; Q53QY9; Q6Q9Z6; Q7Z2H6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Transcription factor E2F6 {ECO:0000305};
DE Short=E2F-6 {ECO:0000303|PubMed:9689056};
GN Name=E2F6 {ECO:0000303|PubMed:9689056, ECO:0000312|HGNC:HGNC:3120};
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, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF LEU-68.
RX PubMed=9689056; DOI=10.1073/pnas.95.16.9190;
RA Gaubatz S., Wood J.G., Livingston D.M.;
RT "Unusual proliferation arrest and transcriptional control properties of a
RT newly discovered E2F family member, E2F-6.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9190-9195(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9704927; DOI=10.1038/sj.onc.1201975;
RA Cartwright P., Mueller H., Wagener C., Holm K., Helin K.;
RT "E2F-6: a novel member of the E2F family is an inhibitor of E2F-dependent
RT transcription.";
RL Oncogene 17:611-623(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Heart;
RA Salih M., Tuana B.S.;
RT "Sequence for human E2F-6 alternative transcript.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=15081404; DOI=10.1016/j.bbrc.2004.03.099;
RA Kherrouche Z., De Launoit Y., Monte D.;
RT "Human E2F6 is alternatively spliced to generate multiple protein
RT isoforms.";
RL Biochem. Biophys. Res. Commun. 317:749-760(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schwertfeger N., Taudien S., Truss M., Morkel M., Pohlers M., Gruska I.,
RA Haaf T., Rosenthal A., Hagemeier C.;
RT "Cloning, genomic organisation and chromosomal mapping of the human
RT E2F6/EMA gene.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-281 (ISOFORM 1), AND FUNCTION.
RC TISSUE=Fetal brain;
RX PubMed=9501179; DOI=10.1073/pnas.95.6.2850;
RA Trimarchi J.M., Fairchild B., Verona R., Moberg K., Andon N., Lees J.A.;
RT "E2F-6, a member of the E2F family that can behave as a transcriptional
RT repressor.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:2850-2855(1998).
RN [11]
RP IDENTIFICATION IN COMPLEX WITH TFDP1; MAX; MGA; EUHMTASE1; BAT8; CBX3;
RP RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
RX PubMed=12004135; DOI=10.1126/science.1069861;
RA Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.;
RT "A complex with chromatin modifiers that occupies E2F- and Myc-responsive
RT genes in G0 cells.";
RL Science 296:1132-1136(2002).
RN [12]
RP IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT "Physical association and coordinate function of the H3 K4
RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL Cell 121:873-885(2005).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-9, AND IDENTIFICATION BY MASS
RP 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: Inhibitor of E2F-dependent transcription (PubMed:9689056,
CC PubMed:9704927, PubMed:9501179). Binds DNA cooperatively with DP
CC proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3'
CC (PubMed:9501179). Has a preference for the 5'-TTTCCCGC-3' E2F
CC recognition site (PubMed:9501179). E2F6 lacks the transcriptional
CC activation and pocket protein binding domains (PubMed:9704927,
CC PubMed:9501179). Appears to regulate a subset of E2F-dependent genes
CC whose products are required for entry into the cell cycle but not for
CC normal cell cycle progression (PubMed:9689056, PubMed:9501179).
CC Represses expression of some meiosis-specific genes, including
CC SLC25A31/ANT4 (By similarity). May silence expression via the
CC recruitment of a chromatin remodeling complex containing histone H3-K9
CC methyltransferase activity. Overexpression delays the exit of cells
CC from the S-phase (PubMed:9501179). {ECO:0000250|UniProtKB:O54917,
CC ECO:0000269|PubMed:9501179, ECO:0000269|PubMed:9689056,
CC ECO:0000269|PubMed:9704927}.
CC -!- SUBUNIT: Forms heterodimers with DP family members TFDP1 or TFDP2
CC (PubMed:9704927). Component of the DRTF1/E2F transcription factor
CC complex (PubMed:12004135). Part of the E2F6.com-1 complex in G0 phase
CC composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2,
CC MBLR, L3MBTL2 and YAF2 (PubMed:12004135). Component of some MLL1/MLL
CC complex, at least composed of the core components KMT2A/MLL1, ASH2L,
CC HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components
CC BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA,
CC KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15960975).
CC {ECO:0000269|PubMed:12004135, ECO:0000269|PubMed:15960975,
CC ECO:0000269|PubMed:9704927}.
CC -!- INTERACTION:
CC O75461; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-749694, EBI-10172290;
CC O75461; P61244: MAX; NbExp=4; IntAct=EBI-749694, EBI-751711;
CC O75461; Q14186: TFDP1; NbExp=22; IntAct=EBI-749694, EBI-749713;
CC O75461; Q14188: TFDP2; NbExp=9; IntAct=EBI-749694, EBI-752268;
CC O75461; Q14188-5: TFDP2; NbExp=11; IntAct=EBI-749694, EBI-12181237;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9689056,
CC ECO:0000269|PubMed:9704927}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75461-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75461-2; Sequence=VSP_008771;
CC Name=3;
CC IsoId=O75461-3; Sequence=VSP_054754;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Highest levels
CC in placenta, skeletal muscle, heart, ovary, kidney, small intestine and
CC spleen. {ECO:0000269|PubMed:9689056}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/E2F6ID521.html";
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; AF059292; AAC31426.1; -; mRNA.
DR EMBL; AY083996; AAM10783.1; -; mRNA.
DR EMBL; AY083997; AAM10784.1; -; Genomic_DNA.
DR EMBL; AY083997; AAM10785.1; -; Genomic_DNA.
DR EMBL; AY551347; AAT02637.1; -; mRNA.
DR EMBL; AJ493061; CAD37950.1; -; Genomic_DNA.
DR EMBL; AK290413; BAF83102.1; -; mRNA.
DR EMBL; AC099344; AAY14826.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00931.1; -; Genomic_DNA.
DR EMBL; BC008348; AAH08348.1; -; mRNA.
DR EMBL; BC107740; AAI07741.1; -; mRNA.
DR EMBL; AF041381; AAC14694.1; -; mRNA.
DR CCDS; CCDS1680.2; -. [O75461-1]
DR CCDS; CCDS62858.1; -. [O75461-2]
DR CCDS; CCDS62859.1; -. [O75461-3]
DR RefSeq; NP_001265204.1; NM_001278275.1. [O75461-3]
DR RefSeq; NP_001265205.1; NM_001278276.1. [O75461-2]
DR RefSeq; NP_001265206.1; NM_001278277.1. [O75461-2]
DR RefSeq; NP_001265207.1; NM_001278278.1. [O75461-2]
DR RefSeq; NP_937987.2; NM_198256.3. [O75461-1]
DR AlphaFoldDB; O75461; -.
DR SMR; O75461; -.
DR BioGRID; 108208; 187.
DR CORUM; O75461; -.
DR DIP; DIP-41699N; -.
DR IntAct; O75461; 81.
DR MINT; O75461; -.
DR STRING; 9606.ENSP00000370936; -.
DR ChEMBL; CHEMBL4630726; -.
DR GlyGen; O75461; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75461; -.
DR PhosphoSitePlus; O75461; -.
DR BioMuta; E2F6; -.
DR EPD; O75461; -.
DR jPOST; O75461; -.
DR MassIVE; O75461; -.
DR MaxQB; O75461; -.
DR PaxDb; O75461; -.
DR PeptideAtlas; O75461; -.
DR PRIDE; O75461; -.
DR ProteomicsDB; 33817; -.
DR ProteomicsDB; 50023; -. [O75461-1]
DR ProteomicsDB; 50024; -. [O75461-2]
DR Antibodypedia; 12671; 337 antibodies from 36 providers.
DR DNASU; 1876; -.
DR Ensembl; ENST00000307236.8; ENSP00000302159.4; ENSG00000169016.17. [O75461-3]
DR Ensembl; ENST00000381525.8; ENSP00000370936.3; ENSG00000169016.17. [O75461-1]
DR Ensembl; ENST00000542100.5; ENSP00000446315.1; ENSG00000169016.17. [O75461-2]
DR Ensembl; ENST00000546212.2; ENSP00000438864.1; ENSG00000169016.17. [O75461-2]
DR GeneID; 1876; -.
DR KEGG; hsa:1876; -.
DR MANE-Select; ENST00000381525.8; ENSP00000370936.3; NM_198256.4; NP_937987.2.
DR UCSC; uc002rbf.4; human. [O75461-1]
DR CTD; 1876; -.
DR DisGeNET; 1876; -.
DR GeneCards; E2F6; -.
DR HGNC; HGNC:3120; E2F6.
DR HPA; ENSG00000169016; Low tissue specificity.
DR MIM; 602944; gene.
DR neXtProt; NX_O75461; -.
DR OpenTargets; ENSG00000169016; -.
DR PharmGKB; PA27578; -.
DR VEuPathDB; HostDB:ENSG00000169016; -.
DR eggNOG; KOG2577; Eukaryota.
DR GeneTree; ENSGT00940000155734; -.
DR HOGENOM; CLU_032091_4_0_1; -.
DR InParanoid; O75461; -.
DR OMA; VEQNHSN; -.
DR OrthoDB; 1087250at2759; -.
DR PhylomeDB; O75461; -.
DR TreeFam; TF105566; -.
DR PathwayCommons; O75461; -.
DR Reactome; R-HSA-69205; G1/S-Specific Transcription.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; O75461; -.
DR SIGNOR; O75461; -.
DR BioGRID-ORCS; 1876; 178 hits in 1102 CRISPR screens.
DR GenomeRNAi; 1876; -.
DR Pharos; O75461; Tbio.
DR PRO; PR:O75461; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O75461; protein.
DR Bgee; ENSG00000169016; Expressed in gastrocnemius and 103 other tissues.
DR ExpressionAtlas; O75461; baseline and differential.
DR Genevisible; O75461; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:NTNU_SB.
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; IEA:Ensembl.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
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; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR CDD; cd14660; E2F_DD; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR015633; E2F.
DR InterPro; IPR037241; E2F-DP_heterodim.
DR InterPro; IPR032198; E2F_CC-MB.
DR InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
DR InterPro; IPR015635; Transcription_factor_E2F6.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12081; PTHR12081; 1.
DR PANTHER; PTHR12081:SF19; PTHR12081:SF19; 1.
DR Pfam; PF16421; E2F_CC-MB; 1.
DR Pfam; PF02319; E2F_TDP; 1.
DR SMART; SM01372; E2F_TDP; 1.
DR SUPFAM; SSF144074; SSF144074; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; DNA-binding; Isopeptide bond; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..281
FT /note="Transcription factor E2F6"
FT /id="PRO_0000219472"
FT DNA_BIND 50..129
FT /evidence="ECO:0000255"
FT REGION 130..222
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 143..164
FT /note="Leucine-zipper"
FT REGION 173..281
FT /note="Transcription repression"
FT REGION 241..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 95..129
FT /note="DEF box"
FT COMPBIAS 241..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 9
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..75
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_008771"
FT VAR_SEQ 1..36
FT /note="MSQQRPARKLPSLLLDPTEETVRRRCRDPINVEGLL -> MNPS (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15081404"
FT /id="VSP_054754"
FT MUTAGEN 68
FT /note="L->E: Reduction in repressor activity, little effect
FT on S-phase entry."
FT /evidence="ECO:0000269|PubMed:9689056"
FT CONFLICT 7..8
FT /note="AR -> HE (in Ref. 10; AAC14694)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="V -> A (in Ref. 4; AAT02637)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="I -> V (in Ref. 10; AAC14694)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="G -> E (in Ref. 10; AAC14694)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 281 AA; 31844 MW; 539E049C15AD3508 CRC64;
MSQQRPARKL PSLLLDPTEE TVRRRCRDPI NVEGLLPSKI RINLEDNVQY VSMRKALKVK
RPRFDVSLVY LTRKFMDLVR SAPGGILDLN KVATKLGVRK RRVYDITNVL DGIDLVEKKS
KNHIRWIGSD LSNFGAVPQQ KKLQEELSDL SAMEDALDEL IKDCAQQLFE LTDDKENERL
AYVTYQDIHS IQAFHEQIVI AVKAPAETRL DVPAPREDSI TVHIRSTNGP IDVYLCEVEQ
GQTSNKRSEG VGTSSSESTH PEGPEEEENP QQSEELLEVS N
