ZN827_HUMAN
ID ZN827_HUMAN Reviewed; 1081 AA.
AC Q17R98; B7ZL52; Q7Z4S7; Q8N279;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Zinc finger protein 827;
GN Name=ZNF827;
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 3).
RC TISSUE=Lymph;
RA Zan Q., Guo J.H., Yu L.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Tongue;
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 1).
RC TISSUE=Liver;
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 [4]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, CAUTION, MOTIF, AND MUTAGENESIS OF
RP 3-ARG--LYS-5.
RX PubMed=25150861; DOI=10.1038/nsmb.2877;
RA Conomos D., Reddel R.R., Pickett H.A.;
RT "NuRD-ZNF827 recruitment to telomeres creates a molecular scaffold for
RT homologous recombination.";
RL Nat. Struct. Mol. Biol. 21:760-770(2014).
RN [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-466; LYS-523 AND LYS-673, 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 [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-673, 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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-466 AND LYS-523, 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 [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-466; LYS-597; LYS-673 AND
RP LYS-704, AND IDENTIFICATION BY MASS 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 [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-176; LYS-216; LYS-226; LYS-360;
RP LYS-372; LYS-466; LYS-475; LYS-549; LYS-580; LYS-587; LYS-634; LYS-639;
RP LYS-658; LYS-673; LYS-704; LYS-710; LYS-742; LYS-778; LYS-798; LYS-870;
RP LYS-891; LYS-958 AND LYS-1014, 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 [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=33174841; DOI=10.7554/elife.58478;
RA Hollensen A.K., Thomsen H.S., Lloret-Llinares M., Kamstrup A.B.,
RA Jensen J.M., Luckmann M., Birkmose N., Palmfeldt J., Jensen T.H.,
RA Hansen T.B., Damgaard C.K.;
RT "circZNF827 nucleates a transcription inhibitory complex to balance
RT neuronal differentiation.";
RL Elife 9:0-0(2020).
RN [11] {ECO:0007744|PDB:5XXQ}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-14 IN COMPLEX WITH RBBP4,
RP SUBUNIT, SUBCELLULAR LOCATION, REGION, AND MUTAGENESIS OF ARG-4; LYS-5;
RP GLN-6; PRO-9 AND ARG-11.
RX PubMed=30045876; DOI=10.1042/bcj20180310;
RA Yang S.F., Sun A.A., Shi Y., Li F., Pickett H.A.;
RT "Structural and functional characterization of the RBBP4-ZNF827 interaction
RT and its role in NuRD recruitment to telomeres.";
RL Biochem. J. 475:2667-2679(2018).
CC -!- FUNCTION: As part of a ribonucleoprotein complex composed at least of
CC HNRNPK, HNRNPL and the circular RNA circZNF827 that nucleates the
CC complex on chromatin, may negatively regulate the transcription of
CC genes involved in neuronal differentiation (PubMed:33174841). Could
CC also recruit the nucleosome remodeling and histone deacetylase/NuRD
CC complex to telomeric regions of chromosomes to regulate chromatin
CC remodeling as part of telomere maintenance (PubMed:25150861).
CC {ECO:0000269|PubMed:25150861, ECO:0000269|PubMed:33174841}.
CC -!- SUBUNIT: Part of a transcription inhibitory ribonucleoprotein complex
CC composed at least of the circular RNA circZNF827, HNRNPK and HNRNPL
CC (PubMed:33174841). Interacts with the nucleosome remodeling and histone
CC deacetylase/NuRD complex (PubMed:25150861). Interacts with RBBP4; the
CC interaction is direct and recruits RBBP4, a component of the NuRD
CC complex, to telomeres (PubMed:30045876). {ECO:0000269|PubMed:25150861,
CC ECO:0000269|PubMed:30045876, ECO:0000269|PubMed:33174841}.
CC -!- INTERACTION:
CC Q17R98; Q14839: CHD4; NbExp=2; IntAct=EBI-5564776, EBI-372916;
CC Q17R98; Q8WXI9: GATAD2B; NbExp=2; IntAct=EBI-5564776, EBI-923440;
CC Q17R98; Q92769: HDAC2; NbExp=2; IntAct=EBI-5564776, EBI-301821;
CC Q17R98; Q14696: MESD; NbExp=3; IntAct=EBI-5564776, EBI-6165891;
CC Q17R98; O94776: MTA2; NbExp=2; IntAct=EBI-5564776, EBI-1783035;
CC Q17R98; Q16576: RBBP7; NbExp=2; IntAct=EBI-5564776, EBI-352227;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:25150861}.
CC Chromosome, telomere {ECO:0000269|PubMed:25150861,
CC ECO:0000269|PubMed:30045876}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q17R98-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q17R98-2; Sequence=VSP_032464, VSP_032465;
CC Name=3;
CC IsoId=Q17R98-3; Sequence=VSP_032463;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- CAUTION: The function in telomere maintenance is inferred from
CC experiments in cells displaying alternative lengthening of
CC telomeres/ALT a process specific of cancer cells.
CC {ECO:0000269|PubMed:25150861}.
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DR EMBL; AF450485; AAP97679.1; -; mRNA.
DR EMBL; AK091130; BAC03591.1; -; mRNA.
DR EMBL; BC117407; AAI17408.1; -; mRNA.
DR EMBL; BC143577; AAI43578.1; -; mRNA.
DR CCDS; CCDS34072.1; -. [Q17R98-2]
DR CCDS; CCDS77968.1; -. [Q17R98-1]
DR RefSeq; NP_001293144.1; NM_001306215.1. [Q17R98-1]
DR RefSeq; NP_849157.2; NM_178835.4. [Q17R98-2]
DR RefSeq; XP_016863261.1; XM_017007772.1. [Q17R98-2]
DR RefSeq; XP_016863262.1; XM_017007773.1. [Q17R98-2]
DR RefSeq; XP_016863263.1; XM_017007774.1. [Q17R98-2]
DR RefSeq; XP_016863264.1; XM_017007775.1. [Q17R98-2]
DR PDB; 5XXQ; X-ray; 1.90 A; C/D=1-14.
DR PDBsum; 5XXQ; -.
DR AlphaFoldDB; Q17R98; -.
DR SMR; Q17R98; -.
DR BioGRID; 127447; 25.
DR DIP; DIP-61048N; -.
DR IntAct; Q17R98; 17.
DR MINT; Q17R98; -.
DR STRING; 9606.ENSP00000368761; -.
DR GlyGen; Q17R98; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q17R98; -.
DR PhosphoSitePlus; Q17R98; -.
DR SwissPalm; Q17R98; -.
DR BioMuta; ZNF827; -.
DR DMDM; 121945543; -.
DR EPD; Q17R98; -.
DR jPOST; Q17R98; -.
DR MassIVE; Q17R98; -.
DR MaxQB; Q17R98; -.
DR PaxDb; Q17R98; -.
DR PeptideAtlas; Q17R98; -.
DR PRIDE; Q17R98; -.
DR ProteomicsDB; 61138; -. [Q17R98-1]
DR ProteomicsDB; 61139; -. [Q17R98-2]
DR ProteomicsDB; 61140; -. [Q17R98-3]
DR Antibodypedia; 56760; 26 antibodies from 11 providers.
DR DNASU; 152485; -.
DR Ensembl; ENST00000379448.9; ENSP00000368761.4; ENSG00000151612.18. [Q17R98-2]
DR Ensembl; ENST00000508784.6; ENSP00000421863.1; ENSG00000151612.18. [Q17R98-1]
DR Ensembl; ENST00000656985.1; ENSP00000499364.1; ENSG00000151612.18. [Q17R98-2]
DR GeneID; 152485; -.
DR KEGG; hsa:152485; -.
DR MANE-Select; ENST00000508784.6; ENSP00000421863.1; NM_001306215.2; NP_001293144.1.
DR UCSC; uc003ikm.4; human. [Q17R98-1]
DR CTD; 152485; -.
DR DisGeNET; 152485; -.
DR GeneCards; ZNF827; -.
DR HGNC; HGNC:27193; ZNF827.
DR HPA; ENSG00000151612; Low tissue specificity.
DR MIM; 617962; gene.
DR neXtProt; NX_Q17R98; -.
DR OpenTargets; ENSG00000151612; -.
DR PharmGKB; PA162410714; -.
DR VEuPathDB; HostDB:ENSG00000151612; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156063; -.
DR HOGENOM; CLU_005602_0_0_1; -.
DR InParanoid; Q17R98; -.
DR OMA; DYACMEE; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q17R98; -.
DR TreeFam; TF333046; -.
DR PathwayCommons; Q17R98; -.
DR SignaLink; Q17R98; -.
DR BioGRID-ORCS; 152485; 12 hits in 1095 CRISPR screens.
DR ChiTaRS; ZNF827; human.
DR GenomeRNAi; 152485; -.
DR Pharos; Q17R98; Tdark.
DR PRO; PR:Q17R98; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q17R98; protein.
DR Bgee; ENSG00000151612; Expressed in buccal mucosa cell and 196 other tissues.
DR ExpressionAtlas; Q17R98; baseline and differential.
DR Genevisible; Q17R98; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0120325; F:NuRD complex binding; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
DR GO; GO:0070200; P:establishment of protein localization to telomere; IMP:UniProtKB.
DR GO; GO:1904791; P:negative regulation of shelterin complex assembly; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Telomere; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1081
FT /note="Zinc finger protein 827"
FT /id="PRO_0000325889"
FT ZN_FING 374..396
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 402..424
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 433..455
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 817..839
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 845..867
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 897..919
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 929..952
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1019..1041
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1047..1069
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..14
FT /note="Mediates direct interaction with RBBP4"
FT /evidence="ECO:0000269|PubMed:30045876"
FT REGION 259..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..5
FT /note="RRK motif; mediates NuRD recruitment to telomeres"
FT /evidence="ECO:0000269|PubMed:25150861"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..348
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 360
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 372
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 466
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 475
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 523
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364"
FT CROSSLNK 549
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 580
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 587
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 597
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297"
FT CROSSLNK 634
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 639
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 658
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 673
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 673
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 704
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 710
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 742
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 778
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 798
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 870
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 891
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 958
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1014
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 16..365
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_032463"
FT VAR_SEQ 1077
FT /note="N -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032464"
FT VAR_SEQ 1078..1081
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032465"
FT MUTAGEN 3..5
FT /note="Missing: Loss of function in NuRD complex
FT recruitment to telomeric regions."
FT /evidence="ECO:0000269|PubMed:25150861"
FT MUTAGEN 4
FT /note="R->A,K: Decreased interaction with RBBP4."
FT /evidence="ECO:0000269|PubMed:30045876"
FT MUTAGEN 5
FT /note="K->A,R: Decreased interaction with RBBP4."
FT /evidence="ECO:0000269|PubMed:30045876"
FT MUTAGEN 6
FT /note="Q->A: Decreased interaction with RBBP4."
FT /evidence="ECO:0000269|PubMed:30045876"
FT MUTAGEN 9
FT /note="P->A: Decreased interaction with RBBP4."
FT /evidence="ECO:0000269|PubMed:30045876"
FT MUTAGEN 11
FT /note="R->A: Decreased interaction with RBBP4."
FT /evidence="ECO:0000269|PubMed:30045876"
FT CONFLICT 15
FT /note="H -> P (in Ref. 1; AAP97679)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="T -> A (in Ref. 2; BAC03591)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="Q -> R (in Ref. 2; BAC03591)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="F -> L (in Ref. 2; BAC03591)"
FT /evidence="ECO:0000305"
FT CONFLICT 859
FT /note="N -> D (in Ref. 1; AAP97679)"
FT /evidence="ECO:0000305"
FT CONFLICT 905
FT /note="E -> G (in Ref. 2; BAC03591)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1081 AA; 119165 MW; BA32DF19FE700EFA CRC64;
MPRRKQEQPK RLPSHVSRQE EAEGELSEGE HWYGNSSETP SEASYGEVQE NYKLSLEDRI
QEQSTSPDTS LGSTTPSSHT LELVALDSEV LRDSLQCQDH LSPGVSSLCD DDPGSNKPLS
SNLRRLLEAG SLKLDAAATA NGRVESPVNV GSNLSFSPPS HHAQQLSVLA RKLAEKQEQN
DQYTPSNRFI WNQGKWLPNS TTTCSLSPDS AILKLKAAAN AVLQDKSLTR TEETMRFESF
SSPFSSQSAS STLAALSKKV SERSLTPGQE HPPPASSFLS LASMTSSAAL LKEVAARAAG
SLLAEKSSLL PEDPLPPPPS EKKPEKVTPP PPPPPPPPPP PPPQSLELLL LPVPKGRVSK
PSNSASEEES GKPFQCPICG LVIKRKSYWK RHMVIHTGLK SHQCPLCPFR CARKDNLKSH
MKVHQHQDRG ETFQCQLCPF TSSRHFSLKL HMRCHQHFLR TEAKVKEEIP DPDVKGSPHL
SDSACLGQQR EGGGTELVGT MMTSNTPERT SQGGAGVSPL LVKEEPKEDN GLPTSFTLNA
ADRPANHTKL KDPSEYVANS ASALFSQDIS VKMASDFLMK LSAANQKEPM NLNFKVKEEP
KEGESLSTTL PRSSYVFSPE SEVSAPGVSE DALKPQEGKG SVLRRDVSVK AASELLMKLS
AESYKETQMV KIKEEPMEVD IQDSHVSISP SRNVGYSTLI GREKTEPLQK MPEGRVPPER
NLFSQDISVK MASELLFQLS EKVSKEHNHT KENTIRTTTS PFFSEDTFRQ SPFTSNSKEL
LPSDSVLHGR ISAPETEKIV LEAGNGLPSW KFNDQLFPCD VCGKVFGRQQ TLSRHLSLHT
EERKYKCHLC PYAAKCRANL NQHLTVHSVK LVSTDTEDIV SAVTSEGSDG KKHPYYYSCH
VCGFETELNV QFVSHMSLHV DKEQWMFSIC CTACDFVTME EAEIKTHIGT KHTGEDRKTP
SESNSPSSSS LSALSDSANS KDDSDGSQKN KGGNNLLVIS VMPGSQPSLN SEEKPEKGFE
CVFCNFVCKT KNMFERHLQI HLITRMFECD VCHKFMKTPE QLLEHKKCHT VPTGGLNSGQ
W
