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Protein Wiz (Widely-interspaced zinc finger-containing protein)

 WIZ_MOUSE               Reviewed;        1684 AA.
O88286; O88287; Q1XG03; Q3UZX7; Q7TSJ4; Q9CT89;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 2.
12-SEP-2018, entry version 147.
RecName: Full=Protein Wiz;
AltName: Full=Widely-interspaced zinc finger-containing protein;
Name=Wiz;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS L AND S), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
TISSUE=Brain;
PubMed=9795207; DOI=10.1016/S0169-328X(98)00216-2;
Matsumoto K., Ishii N., Yoshida S., Shiosaka S., Wanaka A.,
Tohyama M.;
"Molecular cloning and distinct developmental expression pattern of
spliced forms of a novel zinc finger gene wiz in the mouse
cerebellum.";
Brain Res. Mol. Brain Res. 61:179-189(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM S), FUNCTION, TISSUE SPECIFICITY,
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH EHMT1; EHMT2;
CTBP1 AND CTBP2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-1631 AND
HIS-1651.
PubMed=16702210; DOI=10.1074/jbc.M603087200;
Ueda J., Tachibana M., Ikura T., Shinkai Y.;
"Zinc finger protein Wiz links G9a/GLP histone methyltransferases to
the co-repressor molecule CtBP.";
J. Biol. Chem. 281:20120-20128(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1525-1684 (ISOFORM L).
STRAIN=C57BL/6J; TISSUE=Embryo, and Pituitary;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
POLYMORPHISM.
PubMed=12226707; DOI=10.1007/s00335-002-2178-3;
Baust C., Baillie G.J., Mager D.L.;
"Insertional polymorphisms of ETn retrotransposons include a
disruption of the wiz gene in C57BL/6 mice.";
Mamm. Genome 13:423-428(2002).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1045 AND THR-1049, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1039; SER-1045;
THR-1049; SER-1050; SER-1179 AND SER-1184, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: May link EHMT1 and EHMT2 histone methyltransferases to
the CTBP corepressor machinery. May be involved in EHMT1-EHMT2
heterodimer formation and stabilization.
{ECO:0000269|PubMed:16702210}.
-!- SUBUNIT: Part of a complex containing at least CDYL, REST, WIZ,
SETB1, EHMT1 and EHMT2 (By similarity). Interacts with EHMT1,
EHMT2, CTBP1 and CTBP2. {ECO:0000250,
ECO:0000269|PubMed:16702210}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16702210}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=L;
IsoId=O88286-1; Sequence=Displayed;
Name=S;
IsoId=O88286-2; Sequence=VSP_024954;
Name=2;
IsoId=O88286-3; Sequence=VSP_024953, VSP_024956, VSP_024958;
Note=No experimental confirmation available.;
Name=3;
IsoId=O88286-4; Sequence=VSP_024955, VSP_024957;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: According to PubMed:9795207, isoform L and
isoform S are brain-specific. According to PubMed:16702210,
isoform S is ubiquitously expressed. {ECO:0000269|PubMed:16702210,
ECO:0000269|PubMed:9795207}.
-!- DEVELOPMENTAL STAGE: Isoform L and isoform S are expressed in
brain from E14 to adulthood, with highest levels in the perinatal
period. At embryonic stages, isoform L seems to be excluded from
cerebellum. {ECO:0000269|PubMed:9795207}.
-!- DOMAIN: The C2H2-type zinc finger 10 mediates interaction with
EHMT1 and EHMT2.
-!- POLYMORPHISM: C57BL/6J and C57BR/cdJ mice specifically present an
insertion of a type II early transposon in the opposite
orientation into exon 6. This results in a strong reduction in the
protein levels of isoform L. {ECO:0000269|PubMed:12226707}.
-!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
family. {ECO:0000305}.
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EMBL; AB012265; BAA32790.1; -; mRNA.
EMBL; AB012266; BAA32791.1; -; mRNA.
EMBL; AB255388; BAE93139.1; -; mRNA.
EMBL; AK004274; BAB23245.1; -; mRNA.
EMBL; AK133564; BAE21728.1; -; mRNA.
EMBL; BC053035; AAH53035.1; -; mRNA.
CCDS; CCDS28617.2; -. [O88286-2]
PIR; T00247; T00247.
PIR; T00248; T00248.
RefSeq; NP_035847.2; NM_011717.4.
RefSeq; NP_997603.3; NM_212438.3. [O88286-2]
RefSeq; XP_017172890.1; XM_017317401.1. [O88286-2]
UniGene; Mm.274948; -.
ProteinModelPortal; O88286; -.
BioGrid; 204563; 33.
IntAct; O88286; 27.
MINT; O88286; -.
STRING; 10090.ENSMUSP00000069443; -.
iPTMnet; O88286; -.
PhosphoSitePlus; O88286; -.
EPD; O88286; -.
MaxQB; O88286; -.
PaxDb; O88286; -.
PeptideAtlas; O88286; -.
PRIDE; O88286; -.
Ensembl; ENSMUST00000064694; ENSMUSP00000069443; ENSMUSG00000024050. [O88286-2]
GeneID; 22404; -.
KEGG; mmu:22404; -.
UCSC; uc008bwn.2; mouse. [O88286-2]
UCSC; uc008bwq.2; mouse. [O88286-3]
UCSC; uc008bwt.2; mouse. [O88286-4]
CTD; 58525; -.
MGI; MGI:1332638; Wiz.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00530000063587; -.
HOGENOM; HOG000154859; -.
HOVERGEN; HBG108678; -.
InParanoid; O88286; -.
OMA; HFGLECS; -.
PhylomeDB; O88286; -.
TreeFam; TF333705; -.
PRO; PR:O88286; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024050; Expressed in 262 organ(s), highest expression level in olfactory bulb.
CleanEx; MM_WIZ; -.
ExpressionAtlas; O88286; baseline and differential.
Genevisible; O88286; MM.
GO; GO:0030496; C:midbody; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0070984; F:SET domain binding; IPI:UniProtKB.
GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; ISO:MGI.
GO; GO:0070208; P:protein heterotrimerization; IMP:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 11.
SUPFAM; SSF57667; SSF57667; 5.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Isopeptide bond;
Metal-binding; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1684 Protein Wiz.
/FTId=PRO_0000286055.
ZN_FING 308 330 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 345 367 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 454 477 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 734 756 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 802 824 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 903 925 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1076 1098 C2H2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1260 1282 C2H2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1430 1452 C2H2-type 9. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1629 1655 C2H2-type 10. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 1063 1067 Interaction with CTBP1 and CTBP2 1.
{ECO:0000269|PubMed:16702210}.
REGION 1247 1251 Interaction with CTBP1 and CTBP2 2.
{ECO:0000269|PubMed:16702210}.
COMPBIAS 299 304 Poly-Glu.
COMPBIAS 601 608 Poly-Glu.
COMPBIAS 658 663 Poly-Gln.
COMPBIAS 786 790 Poly-Lys.
COMPBIAS 1174 1177 Poly-Pro.
MOD_RES 1029 1029 Phosphoserine.
{ECO:0000250|UniProtKB:O95785}.
MOD_RES 1031 1031 Phosphothreonine.
{ECO:0000250|UniProtKB:O95785}.
MOD_RES 1039 1039 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1045 1045 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1049 1049 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1050 1050 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1058 1058 Phosphoserine.
{ECO:0000250|UniProtKB:O95785}.
MOD_RES 1112 1112 Phosphoserine.
{ECO:0000250|UniProtKB:O95785}.
MOD_RES 1139 1139 Phosphoserine.
{ECO:0000250|UniProtKB:O95785}.
MOD_RES 1155 1155 Phosphoserine.
{ECO:0000250|UniProtKB:O95785}.
MOD_RES 1160 1160 Phosphoserine.
{ECO:0000250|UniProtKB:O95785}.
MOD_RES 1167 1167 Phosphoserine.
{ECO:0000250|UniProtKB:O95785}.
MOD_RES 1179 1179 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1184 1184 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1195 1195 N6,N6,N6-trimethyllysine; by EHMT2;
alternate.
{ECO:0000250|UniProtKB:O95785}.
MOD_RES 1195 1195 N6,N6-dimethyllysine; by EHMT2;
alternate.
{ECO:0000250|UniProtKB:O95785}.
MOD_RES 1296 1296 Phosphoserine.
{ECO:0000250|UniProtKB:O95785}.
MOD_RES 1342 1342 Phosphoserine.
{ECO:0000250|UniProtKB:O95785}.
MOD_RES 1347 1347 Phosphoserine.
{ECO:0000250|UniProtKB:O95785}.
MOD_RES 1550 1550 Phosphoserine.
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 916 916 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 972 972 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 988 988 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1000 1000 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1021 1021 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1033 1033 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1038 1038 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1089 1089 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1141 1141 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1145 1145 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1171 1171 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1172 1172 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1210 1210 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1273 1273 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1315 1315 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1376 1376 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1389 1389 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1403 1403 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1405 1405 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1415 1415 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1481 1481 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1497 1497 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1510 1510 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1556 1556 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1556 1556 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1567 1567 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1593 1593 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
CROSSLNK 1663 1663 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95785}.
VAR_SEQ 1 759 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_024953.
VAR_SEQ 63 790 Missing (in isoform S).
{ECO:0000303|PubMed:16702210,
ECO:0000303|PubMed:9795207}.
/FTId=VSP_024954.
VAR_SEQ 745 798 YGIGLANHVRGHLNRVGVSYNVRHFISAEEVKAIERRFSFQ
KKKKKVANFDPGT -> NGIVLRPPAARNVNGSTEKAARAV
REESRRGKRRNVAKTVTLIKAQILLLRHQL (in
isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_024955.
VAR_SEQ 760 789 VGVSYNVRHFISAEEVKAIERRFSFQKKKK -> MAEVAFL
MGSPILASAKPSPVPPPPPIGSA (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_024956.
VAR_SEQ 799 1684 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_024957.
VAR_SEQ 898 898 D -> DGLCSEENTMVAMDLGSPLLPKKSLPVSGTLEQVAS
RLSSKVAAEVPHGSKQELPDLK (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_024958.
MUTAGEN 1631 1631 C->A: Impairs interaction with EHMT1 and
EHMT2. {ECO:0000269|PubMed:16702210}.
MUTAGEN 1651 1651 H->A: Impairs interaction with EHMT1 and
EHMT2. {ECO:0000269|PubMed:16702210}.
CONFLICT 492 492 D -> G (in Ref. 1; BAA32790).
{ECO:0000305}.
CONFLICT 868 868 R -> G (in Ref. 1; BAA32790/BAA32791).
{ECO:0000305}.
CONFLICT 1020 1020 K -> N (in Ref. 3; AAH53035).
{ECO:0000305}.
CONFLICT 1052 1052 K -> R (in Ref. 1; BAA32790/BAA32791).
{ECO:0000305}.
CONFLICT 1055 1055 W -> C (in Ref. 1; BAA32790/BAA32791).
{ECO:0000305}.
CONFLICT 1252 1252 Missing (in Ref. 1; BAA32790/BAA32791).
{ECO:0000305}.
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


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