WIZ_MOUSE
ID WIZ_MOUSE Reviewed; 1684 AA.
AC O88286; O88287; Q1XG03; Q3UZX7; Q7TSJ4; Q9CT89;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Protein Wiz;
DE AltName: Full=Widely-interspaced zinc finger-containing protein;
GN Name=Wiz;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS L AND S), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=9795207; DOI=10.1016/s0169-328x(98)00216-2;
RA Matsumoto K., Ishii N., Yoshida S., Shiosaka S., Wanaka A., Tohyama M.;
RT "Molecular cloning and distinct developmental expression pattern of spliced
RT forms of a novel zinc finger gene wiz in the mouse cerebellum.";
RL Brain Res. Mol. Brain Res. 61:179-189(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM S), FUNCTION, TISSUE SPECIFICITY,
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH EHMT1; EHMT2; CTBP1
RP AND CTBP2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-1631 AND HIS-1651.
RX PubMed=16702210; DOI=10.1074/jbc.m603087200;
RA Ueda J., Tachibana M., Ikura T., Shinkai Y.;
RT "Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the
RT co-repressor molecule CtBP.";
RL J. Biol. Chem. 281:20120-20128(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1525-1684 (ISOFORM L).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; 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 [5]
RP POLYMORPHISM.
RX PubMed=12226707; DOI=10.1007/s00335-002-2178-3;
RA Baust C., Baillie G.J., Mager D.L.;
RT "Insertional polymorphisms of ETn retrotransposons include a disruption of
RT the wiz gene in C57BL/6 mice.";
RL Mamm. Genome 13:423-428(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1045 AND THR-1049, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1039; SER-1045; THR-1049;
RP SER-1050; SER-1179 AND SER-1184, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May link EHMT1 and EHMT2 histone methyltransferases to the
CC CTBP corepressor machinery. May be involved in EHMT1-EHMT2 heterodimer
CC formation and stabilization. {ECO:0000269|PubMed:16702210}.
CC -!- SUBUNIT: Part of a complex containing at least CDYL, REST, WIZ, SETB1,
CC EHMT1 and EHMT2 (By similarity). Interacts with EHMT1, EHMT2, CTBP1 and
CC CTBP2. {ECO:0000250, ECO:0000269|PubMed:16702210}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16702210}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=L;
CC IsoId=O88286-1; Sequence=Displayed;
CC Name=S;
CC IsoId=O88286-2; Sequence=VSP_024954;
CC Name=2;
CC IsoId=O88286-3; Sequence=VSP_024953, VSP_024956, VSP_024958;
CC Name=3;
CC IsoId=O88286-4; Sequence=VSP_024955, VSP_024957;
CC -!- TISSUE SPECIFICITY: According to PubMed:9795207, isoform L and isoform
CC S are brain-specific. According to PubMed:16702210, isoform S is
CC ubiquitously expressed. {ECO:0000269|PubMed:16702210,
CC ECO:0000269|PubMed:9795207}.
CC -!- DEVELOPMENTAL STAGE: Isoform L and isoform S are expressed in brain
CC from 14 dpc to adulthood, with highest levels in the perinatal period.
CC At embryonic stages, isoform L seems to be excluded from cerebellum.
CC {ECO:0000269|PubMed:9795207}.
CC -!- DOMAIN: The C2H2-type zinc finger 10 mediates interaction with EHMT1
CC and EHMT2.
CC -!- POLYMORPHISM: C57BL/6J and C57BR/cdJ mice specifically present an
CC insertion of a type II early transposon in the opposite orientation
CC into exon 6. This results in a strong reduction in the protein levels
CC of isoform L. {ECO:0000269|PubMed:12226707}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AB012265; BAA32790.1; -; mRNA.
DR EMBL; AB012266; BAA32791.1; -; mRNA.
DR EMBL; AB255388; BAE93139.1; -; mRNA.
DR EMBL; AK004274; BAB23245.1; -; mRNA.
DR EMBL; AK133564; BAE21728.1; -; mRNA.
DR EMBL; BC053035; AAH53035.1; -; mRNA.
DR CCDS; CCDS28617.2; -. [O88286-2]
DR PIR; T00247; T00247.
DR PIR; T00248; T00248.
DR RefSeq; NP_035847.2; NM_011717.4.
DR RefSeq; NP_997603.3; NM_212438.3. [O88286-2]
DR RefSeq; XP_017172890.1; XM_017317401.1.
DR AlphaFoldDB; O88286; -.
DR BioGRID; 204563; 36.
DR IntAct; O88286; 27.
DR MINT; O88286; -.
DR STRING; 10090.ENSMUSP00000069443; -.
DR iPTMnet; O88286; -.
DR PhosphoSitePlus; O88286; -.
DR EPD; O88286; -.
DR jPOST; O88286; -.
DR MaxQB; O88286; -.
DR PaxDb; O88286; -.
DR PeptideAtlas; O88286; -.
DR PRIDE; O88286; -.
DR ProteomicsDB; 299982; -. [O88286-1]
DR ProteomicsDB; 299983; -. [O88286-2]
DR ProteomicsDB; 299984; -. [O88286-3]
DR ProteomicsDB; 299985; -. [O88286-4]
DR Antibodypedia; 7541; 100 antibodies from 26 providers.
DR DNASU; 22404; -.
DR Ensembl; ENSMUST00000064694; ENSMUSP00000069443; ENSMUSG00000024050. [O88286-2]
DR GeneID; 22404; -.
DR KEGG; mmu:22404; -.
DR UCSC; uc008bwn.2; mouse. [O88286-2]
DR UCSC; uc008bwq.2; mouse. [O88286-3]
DR UCSC; uc008bwt.2; mouse. [O88286-4]
DR CTD; 58525; -.
DR MGI; MGI:1332638; Wiz.
DR VEuPathDB; HostDB:ENSMUSG00000024050; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159979; -.
DR InParanoid; O88286; -.
DR OrthoDB; 434804at2759; -.
DR PhylomeDB; O88286; -.
DR TreeFam; TF333705; -.
DR BioGRID-ORCS; 22404; 9 hits in 71 CRISPR screens.
DR ChiTaRS; Wiz; mouse.
DR PRO; PR:O88286; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O88286; protein.
DR Bgee; ENSMUSG00000024050; Expressed in embryonic brain and 238 other tissues.
DR ExpressionAtlas; O88286; baseline and differential.
DR Genevisible; O88286; MM.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:1990226; F:histone methyltransferase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0070984; F:SET domain binding; IPI:UniProtKB.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1684
FT /note="Protein Wiz"
FT /id="PRO_0000286055"
FT ZN_FING 308..330
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 345..367
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 454..477
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 734..756
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 802..824
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 903..925
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1076..1098
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1260..1282
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1430..1452
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1629..1655
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1067
FT /note="Interaction with CTBP1 and CTBP2 1"
FT /evidence="ECO:0000269|PubMed:16702210"
FT REGION 1127..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1251
FT /note="Interaction with CTBP1 and CTBP2 2"
FT /evidence="ECO:0000269|PubMed:16702210"
FT REGION 1320..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1496..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1662..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1560..1576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT MOD_RES 1031
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT MOD_RES 1039
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1045
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1049
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1050
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1058
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT MOD_RES 1112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT MOD_RES 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT MOD_RES 1155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT MOD_RES 1167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT MOD_RES 1179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1195
FT /note="N6,N6,N6-trimethyllysine; by EHMT2; alternate"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT MOD_RES 1195
FT /note="N6,N6-dimethyllysine; by EHMT2; alternate"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT MOD_RES 1296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT MOD_RES 1342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT MOD_RES 1347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT MOD_RES 1550
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 916
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 972
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 988
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1000
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1021
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1033
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1038
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1089
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1172
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1315
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1376
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1389
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1403
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1405
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1415
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1481
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1497
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1510
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1556
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1556
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1567
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1593
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT CROSSLNK 1663
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95785"
FT VAR_SEQ 1..759
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024953"
FT VAR_SEQ 63..790
FT /note="Missing (in isoform S)"
FT /evidence="ECO:0000303|PubMed:16702210,
FT ECO:0000303|PubMed:9795207"
FT /id="VSP_024954"
FT VAR_SEQ 745..798
FT /note="YGIGLANHVRGHLNRVGVSYNVRHFISAEEVKAIERRFSFQKKKKKVANFDP
FT GT -> NGIVLRPPAARNVNGSTEKAARAVREESRRGKRRNVAKTVTLIKAQILLLRHQ
FT L (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024955"
FT VAR_SEQ 760..789
FT /note="VGVSYNVRHFISAEEVKAIERRFSFQKKKK -> MAEVAFLMGSPILASAKP
FT SPVPPPPPIGSA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024956"
FT VAR_SEQ 799..1684
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024957"
FT VAR_SEQ 898
FT /note="D -> DGLCSEENTMVAMDLGSPLLPKKSLPVSGTLEQVASRLSSKVAAEVP
FT HGSKQELPDLK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024958"
FT MUTAGEN 1631
FT /note="C->A: Impairs interaction with EHMT1 and EHMT2."
FT /evidence="ECO:0000269|PubMed:16702210"
FT MUTAGEN 1651
FT /note="H->A: Impairs interaction with EHMT1 and EHMT2."
FT /evidence="ECO:0000269|PubMed:16702210"
FT CONFLICT 492
FT /note="D -> G (in Ref. 1; BAA32790)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="R -> G (in Ref. 1; BAA32790/BAA32791)"
FT /evidence="ECO:0000305"
FT CONFLICT 1020
FT /note="K -> N (in Ref. 3; AAH53035)"
FT /evidence="ECO:0000305"
FT CONFLICT 1052
FT /note="K -> R (in Ref. 1; BAA32790/BAA32791)"
FT /evidence="ECO:0000305"
FT CONFLICT 1055
FT /note="W -> C (in Ref. 1; BAA32790/BAA32791)"
FT /evidence="ECO:0000305"
FT CONFLICT 1252
FT /note="Missing (in Ref. 1; BAA32790/BAA32791)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1684 AA; 184291 MW; 67BA8AC25A97DDEB CRC64;
MEGLLAGGLA APDHPRGPAP REDIESGAEA AEGEGDIFPS SHYLPITKEG PRDILDGRSG
ISDGQPHPGL SEALPRATSA THRISSCYWD GDSLDFQPGS PPPHLLGPFP ASLDVQGSWE
HPMVQEAREG TPSEQRFKDS VIVRTMKPYA KLKGSRKFLH HQGEVKFLEK YSPSHHKFDW
LQDTDEQGPL KDTGLHLDLP AQPPTVTSFR RVIVPVDNTP KTLDMEVMGT REDLEDFGQV
AQPSEWGLHT SASEVATQTW TVNSEASVER LQPLLSPVQT GPYLCELLQE VAGGVDSNEE
EEEEPAVFPC IECSIYFKHK EHLLEHMSQH RRAPGQEPPA DLAPLACSEC GWAFTEPTAL
EQHWQLHQAS REKIIEEIQK LKQFPGDEGR EARLQCSKCV FGTNSSRAFM QHAKLHVRGS
LPSRQATEPF RGGSPVLDVS TLVYPSYGDS SGLNTCVHCG FTAPSKSLLR EHTRLVHAHH
AHWEEVGEAF EDLTSQPCTS QDAYTHSPDT ATVDYFSKSE PLLASVWQEN PSGYDPDLAF
GPDYQQPGMR NFPLLNSGQQ SLGKLAFPSP MASASYSIQR NRNKSTVHLQ RMEDKSHLWS
EEEEEEDEDV VLTSERDFTP ENGAFPPLAI PSLIPQPALE LKQTFQDALQ AVDASETQQQ
QLQGMVPIVL MAKLRPQVIA ATTRASPQLP PEEPELRSTH PLDFLLLDAP LGGSLGLNTL
LEGDPAMALK HEERKCPYCP DRFHYGIGLA NHVRGHLNRV GVSYNVRHFI SAEEVKAIER
RFSFQKKKKK VANFDPGTFS LMRCDFCGAG FDTRAGLSSH ARAHLRDFGI TNWELTISPI
NILQELLATS AAELPPSPLG REPGGPPRSF LTSRRPRLPL TMPFPPTWAE DPGPIYGDAQ
SLTTCEVCGA CFETRKGLSS HARSHLRQLG VAESESSGAP IDLLYELVKQ KGLPDAPLGL
TPSLTKKSNS PKEFLAGAAR PGLLTLAKPM DAPAVNKAIK SPPGFSAKGL THPSSSPLLK
KAPLTLAGSP TPKNPEDKSP QLSLSPRPTS PKAQWPQSED EGPLNLTSGP EPTRDIRCEF
CGEFFENRKG LSSHARSHLR QMGVTEWYVN GSPIDTLREI LKRRTQSRPG GHLHPPGPSP
KALAKVLSTG GPGSSLEARS PSDLHISPLT KKLPPPPGSP LGHSPTASPP PTARKMFSGL
ATPSLPKKLK PEHMRVEIKR EMLPGTLHGE PHPSEGPWGT PREDMAPLNL SARAEPVRDI
RCEFCGEFFE NRKGLSSHAR SHLRQMGVTE WSVNGSPIDT LREILKKKSK LCLIKKEPPA
GDLAPALTED GSPTAAPGAL HSPLPLSPLA SRPGKPGAGP TQVPRELSLS PITGSKPSAA
SYLGPVATKR PLQEDRFLPA EVKAKTYIQT ELPFKAKTLH EKTSHSSTEA CCELCGLYFE
NRKALASHAR AHLRQFGVTE WCVNGSPIET LSEWIKHRPQ KVGAYRSYIQ GGRPFTKKFR
SAGHGRDSDK RPPLGLAPGG LSLVGRSAGG EPGLEAGRAA DSGERPLATS PPGTVKSEEH
QRQNINKFER RQARPSDASA ARGGEEVNDL QQKLEEVRQP PPRVRPVPSL VPRPPQTSLV
KFVGNIYTLK CRFCEVEFQG PLSIQEEWVR HLQRHILEMN FSKADPPPEE PQAPQAQTAA
VEAP
