BEND3_HUMAN
ID BEND3_HUMAN Reviewed; 828 AA.
AC Q5T5X7; A2RRH2; Q9HCL9;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=BEN domain-containing protein 3;
GN Name=BEND3; Synonyms=KIAA1553;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 159-828.
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND SER-379, AND
RP IDENTIFICATION BY 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 [7]
RP FUNCTION, INTERACTION WITH HDAC2; HDAC3 AND SALL4, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DOMAIN, SUMOYLATION AT LYS-20 AND LYS-512, AND
RP MUTAGENESIS OF LYS-20 AND LYS-512.
RX PubMed=21914818; DOI=10.1242/jcs.086603;
RA Sathyan K.M., Shen Z., Tripathi V., Prasanth K.V., Prasanth S.G.;
RT "A BEN-domain-containing protein associates with heterochromatin and
RT represses transcription.";
RL J. Cell Sci. 124:3149-3163(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; SER-379 AND SER-489, AND
RP 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 [9]
RP TISSUE SPECIFICITY.
RX PubMed=25400923; DOI=10.1002/iid3.17;
RA Shiheido H., Kitagori K., Sasaki C., Kobayashi S., Aoyama T., Urata K.,
RA Oku T., Hirayama Y., Yoshitomi H., Hikida M., Yoshifuji H., Mimori T.,
RA Watanabe T., Shimizu J.;
RT "Human T cells expressing BEND3 on their surface represent a novel
RT subpopulation that preferentially produces IL-6 and IL-8.";
RL Immun. Inflammation. Dis. 2:35-43(2014).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-129 AND LYS-427, 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 [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20, 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 [12]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-56; ARG-57 AND LYS-58.
RX PubMed=25600804; DOI=10.1016/j.bbrc.2015.01.029;
RA Shiheido H., Shimizu J.;
RT "Basic amino acid residues located in the N-terminal region of BEND3 are
RT essential for its nuclear localization.";
RL Biochem. Biophys. Res. Commun. 457:589-594(2015).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-56 AND LYS-142, 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20, AND IDENTIFICATION BY MASS
RP 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 [15]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMARCA5; BAZ2A AND USP21,
RP AND MUTAGENESIS OF LYS-20 AND LYS-512.
RX PubMed=26100909; DOI=10.1073/pnas.1424705112;
RA Khan A., Giri S., Wang Y., Chakraborty A., Ghosh A.K., Anantharaman A.,
RA Aggarwal V., Sathyan K.M., Ha T., Prasanth K.V., Prasanth S.G.;
RT "BEND3 represses rDNA transcription by stabilizing a NoRC component via
RT USP21 deubiquitinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:8338-8343(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-41; LYS-56; LYS-58;
RP LYS-73; LYS-128; LYS-129; LYS-137; LYS-142; LYS-158; LYS-176; LYS-427;
RP LYS-512; LYS-528 AND LYS-700, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [17]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 236-347 IN COMPLEX WITH ERCC6L,
RP FUNCTION, INTERACTION WITH ERCC6L, SUBUNIT, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=28977671; DOI=10.1093/nar/gkx792;
RA Pitchai G.P., Kaulich M., Bizard A.H., Mesa P., Yao Q., Sarlos K.,
RA Streicher W.W., Nigg E.A., Montoya G., Hickson I.D.;
RT "A novel TPR-BEN domain interaction mediates PICH-BEND3 association.";
RL Nucleic Acids Res. 45:11413-11424(2017).
CC -!- FUNCTION: Transcriptional repressor which associates with the NoRC
CC (nucleolar remodeling complex) complex and plays a key role in
CC repressing rDNA transcription. The sumoylated form modulates the
CC stability of the NoRC complex component BAZ2A/TIP5 by controlling its
CC USP21-mediated deubiquitination (PubMed:21914818, PubMed:26100909).
CC Binds to unmethylated major satellite DNA and is involved in the
CC recruitment of the Polycomb repressive complex 2 (PRC2) to major
CC satellites (By similarity). Stimulates the ERCC6L translocase and
CC ATPase activities (PubMed:28977671). {ECO:0000250|UniProtKB:Q6PAL0,
CC ECO:0000269|PubMed:21914818, ECO:0000269|PubMed:26100909,
CC ECO:0000269|PubMed:28977671}.
CC -!- SUBUNIT: Homooligomer, probably a homooctamer (PubMed:28977671).
CC Interacts with HDAC2 and HDAC3, but not HDAC1. Interacts with SALL4
CC (PubMed:21914818). Interacts with SMARCA5/SNF2H, BAZ2A/TIP5 and USP21
CC (PubMed:26100909). Interacts with the nucleosome remodeling and histone
CC deacetylase (NuRD) repressor complex (By similarity). Interacts (via
CC BEN domains 1 and 3) with ERCC6L (via N-terminal TPR repeat); the
CC interaction is direct (PubMed:28977671). {ECO:0000250|UniProtKB:Q6PAL0,
CC ECO:0000269|PubMed:21914818, ECO:0000269|PubMed:26100909,
CC ECO:0000269|PubMed:28977671}.
CC -!- INTERACTION:
CC Q5T5X7; Q9C005: DPY30; NbExp=3; IntAct=EBI-1211496, EBI-744973;
CC Q5T5X7; Q3B820: FAM161A; NbExp=3; IntAct=EBI-1211496, EBI-719941;
CC Q5T5X7; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-1211496, EBI-348259;
CC Q5T5X7; Q8NDC4: MORN4; NbExp=6; IntAct=EBI-1211496, EBI-10269566;
CC Q5T5X7; P0CB47: UBTFL1; NbExp=3; IntAct=EBI-1211496, EBI-17208936;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21914818,
CC ECO:0000269|PubMed:25600804}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:26100909}. Note=In the nucleus, observed in
CC heterochromatic foci containing CBX1, CBX3, CBX5 and histone H3
CC trimethylated at 'Lys-9'. Released from chromatin during
CC decondensation. Association with heterochromatin does not depend on
CC sumoylation. {ECO:0000269|PubMed:21914818}.
CC -!- TISSUE SPECIFICITY: Expressed at least in heart, kidney, liver, ovary
CC and spleen, with highest levels in spleen and lowest in heart.
CC Expressed on the surface of T-cells. {ECO:0000269|PubMed:21914818,
CC ECO:0000269|PubMed:25400923}.
CC -!- DOMAIN: The BEN domain 4 is necessary and sufficient for the
CC localization of BEND3 to heterochromatic regions.
CC {ECO:0000269|PubMed:21914818}.
CC -!- PTM: Sumoylated at Lys-20 by SUMO1 and at Lys-512 by SUMO1, SUMO2 and
CC SUMO3. Sumoylation probably occurs sequentially, with that of Lys-20
CC preceding that of Lys-512. It does not alter association with
CC heterochromatin, but is required for the repression of transcription.
CC {ECO:0000269|PubMed:21914818}.
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DR EMBL; AL355586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC131628; AAI31629.1; -; mRNA.
DR EMBL; AB046773; BAB13379.1; -; mRNA.
DR CCDS; CCDS34507.1; -.
DR RefSeq; NP_001073919.1; NM_001080450.2.
DR RefSeq; XP_005267136.1; XM_005267079.3.
DR RefSeq; XP_005267137.1; XM_005267080.3.
DR RefSeq; XP_011534307.1; XM_011536005.2.
DR RefSeq; XP_016866627.1; XM_017011138.1.
DR PDB; 5JNO; X-ray; 2.20 A; A=236-347.
DR PDB; 7W27; X-ray; 1.49 A; C=715-825.
DR PDBsum; 5JNO; -.
DR PDBsum; 7W27; -.
DR AlphaFoldDB; Q5T5X7; -.
DR SMR; Q5T5X7; -.
DR BioGRID; 121704; 105.
DR IntAct; Q5T5X7; 31.
DR MINT; Q5T5X7; -.
DR STRING; 9606.ENSP00000411268; -.
DR GlyGen; Q5T5X7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5T5X7; -.
DR PhosphoSitePlus; Q5T5X7; -.
DR BioMuta; BEND3; -.
DR DMDM; 74745144; -.
DR EPD; Q5T5X7; -.
DR jPOST; Q5T5X7; -.
DR MassIVE; Q5T5X7; -.
DR MaxQB; Q5T5X7; -.
DR PaxDb; Q5T5X7; -.
DR PeptideAtlas; Q5T5X7; -.
DR PRIDE; Q5T5X7; -.
DR ProteomicsDB; 64557; -.
DR Antibodypedia; 2976; 123 antibodies from 21 providers.
DR DNASU; 57673; -.
DR Ensembl; ENST00000369042.6; ENSP00000358038.1; ENSG00000178409.14.
DR Ensembl; ENST00000429433.3; ENSP00000411268.2; ENSG00000178409.14.
DR GeneID; 57673; -.
DR KEGG; hsa:57673; -.
DR MANE-Select; ENST00000369042.6; ENSP00000358038.1; NM_001367314.1; NP_001354243.1.
DR UCSC; uc003prs.3; human.
DR CTD; 57673; -.
DR DisGeNET; 57673; -.
DR GeneCards; BEND3; -.
DR HGNC; HGNC:23040; BEND3.
DR HPA; ENSG00000178409; Low tissue specificity.
DR MIM; 616374; gene.
DR neXtProt; NX_Q5T5X7; -.
DR OpenTargets; ENSG00000178409; -.
DR PharmGKB; PA164716540; -.
DR VEuPathDB; HostDB:ENSG00000178409; -.
DR eggNOG; ENOG502QQWG; Eukaryota.
DR GeneTree; ENSGT00390000010827; -.
DR HOGENOM; CLU_017582_0_0_1; -.
DR InParanoid; Q5T5X7; -.
DR OMA; QCAQRLN; -.
DR OrthoDB; 168652at2759; -.
DR PhylomeDB; Q5T5X7; -.
DR TreeFam; TF300204; -.
DR PathwayCommons; Q5T5X7; -.
DR SignaLink; Q5T5X7; -.
DR BioGRID-ORCS; 57673; 32 hits in 1077 CRISPR screens.
DR ChiTaRS; BEND3; human.
DR GenomeRNAi; 57673; -.
DR Pharos; Q5T5X7; Tbio.
DR PRO; PR:Q5T5X7; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5T5X7; protein.
DR Bgee; ENSG00000178409; Expressed in ileal mucosa and 153 other tissues.
DR Genevisible; Q5T5X7; HS.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000182; F:rDNA binding; IDA:UniProtKB.
DR GO; GO:0006306; P:DNA methylation; IMP:UniProtKB.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IDA:UniProtKB.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
DR GO; GO:0036124; P:histone H3-K9 trimethylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:1903580; P:positive regulation of ATP metabolic process; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IMP:UniProtKB.
DR InterPro; IPR018379; BEN_domain.
DR InterPro; IPR033583; BEND3.
DR PANTHER; PTHR28665; PTHR28665; 1.
DR Pfam; PF10523; BEN; 4.
DR SMART; SM01025; BEN; 4.
DR PROSITE; PS51457; BEN; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..828
FT /note="BEN domain-containing protein 3"
FT /id="PRO_0000290200"
FT DOMAIN 242..343
FT /note="BEN 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT DOMAIN 387..487
FT /note="BEN 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT DOMAIN 548..650
FT /note="BEN 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT DOMAIN 715..816
FT /note="BEN 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT REGION 164..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 56..58
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:25600804"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:21914818"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 41
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 56
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 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 73
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 129
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 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 142
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 158
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 176
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 427
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 512
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:21914818"
FT CROSSLNK 512
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 528
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 700
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 20
FT /note="K->R: Partial loss of sumoylation. Almost complete
FT loss of sumoylation, partial loss of transcription
FT repression, no effect on subcellular location, loss of rDNA
FT silencing; when associated with R-512."
FT /evidence="ECO:0000269|PubMed:21914818,
FT ECO:0000269|PubMed:26100909"
FT MUTAGEN 56
FT /note="K->A: Loss of nuclear localization."
FT /evidence="ECO:0000269|PubMed:25600804"
FT MUTAGEN 57
FT /note="R->A: Loss of nuclear localization."
FT /evidence="ECO:0000269|PubMed:25600804"
FT MUTAGEN 58
FT /note="K->A: Loss of nuclear localization."
FT /evidence="ECO:0000269|PubMed:25600804"
FT MUTAGEN 512
FT /note="K->R: Partial loss of sumoylation. Almost complete
FT loss of sumoylation, partial loss of transcription
FT repression, no effect on subcellular location, loss of rDNA
FT silencing; when associated with R-20."
FT /evidence="ECO:0000269|PubMed:21914818,
FT ECO:0000269|PubMed:26100909"
FT CONFLICT 409
FT /note="E -> D (in Ref. 3; BAB13379)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="N -> S (in Ref. 2; AAI31629)"
FT /evidence="ECO:0000305"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:5JNO"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:5JNO"
FT HELIX 263..274
FT /evidence="ECO:0007829|PDB:5JNO"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:5JNO"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:5JNO"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:5JNO"
FT HELIX 321..326
FT /evidence="ECO:0007829|PDB:5JNO"
FT HELIX 328..346
FT /evidence="ECO:0007829|PDB:5JNO"
SQ SEQUENCE 828 AA; 94475 MW; 28D8F39112DB7EAE CRC64;
MNSTEFTEDV EEVLKSITVK VETEAEDAAL DCSVNSRTSE KHSVDSVLTA LQDSSKRKQL
VSDGLLDSVP GVKRRRLIPE ALLAGMRNRE NSSPCQGNGE QAGRGRSLGN VWPGEEEPCN
DATTPSYKKP LYGISHKIME KKNPPSGDLL NVYELFEKAN ASNSPSSLRL LNEPQKRDCG
STGAGTDNDP NIYFLIQKMF YMLNTLTSNM SQLHSKVDLL SLEVSRIKKQ VSPTEMVAKF
QPPPEYQLTA AELKQIVDQS LSGGDLACRL LVQLFPELFS DVDFSRGCSA CGFAAKRKLE
SLHLQLIRNY VEVYYPSVKD TAVWQAECLP QLNDFFSRFW AQREMEDSQP SGQVASFFEA
EQVDPGHFLD NKDQEEALSL DRSSTIASDH VVDTQDLTEF LDEASSPGEF AVFLLHRLFP
ELFDHRKLGE QYSCYGDGGK QELDPQRLQI IRNYTEIYFP DMQEEEAWLQ QCAQRINDEL
EGLGLDAGSE GDPPRDDCYD SSSLPDDISV VKVEDSFEGE RPGRRSKKIW LVPIDFDKLE
IPQPDFEVPG ADCLLSKEQL RSIYESSLSI GNFASRLLVH LFPELFTHEN LRKQYNCSGS
LGKKQLDPSR IKLIRHYVQL LYPRAKNDRV WTLEFVGKLD ERCRRRDTEQ RRSYQQQRKV
HVPGPECRDL TSYAINPERF REEFEGPPLP PERSSKDFCK IPLDELVVPS PDFPVPSPYL
LSDKEVREIV QQSLSVGNFA ARLLVRLFPE LFTAENLRLQ YNHSGACNKK QLDPTRLRLI
RHYVEAVYPV EKMEEVWHYE CIPSIDERCR RPNRKKCDIL KKAKKVEK
