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B-cell lymphoma/leukemia 11A (BCL-11A) (B-cell CLL/lymphoma 11A) (COUP-TF-interacting protein 1) (Ecotropic viral integration site 9 protein) (EVI-9)

 BC11A_MOUSE             Reviewed;         773 AA.
Q9QYE3; Q80T89; Q8BLC7; Q8BLR4; Q8BWX3; Q921V4; Q9D0V2; Q9JIT4;
Q9JLK8; Q9JLK9;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 150.
RecName: Full=B-cell lymphoma/leukemia 11A;
Short=BCL-11A;
AltName: Full=B-cell CLL/lymphoma 11A;
AltName: Full=COUP-TF-interacting protein 1;
AltName: Full=Ecotropic viral integration site 9 protein;
Short=EVI-9;
Name=Bcl11a; Synonyms=Ctip1, Evi9, Kiaa1809;
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 1; 2 AND 3).
STRAIN=BXH/2;
PubMed=10757802; DOI=10.1128/MCB.20.9.3178-3186.2000;
Nakamura T., Yamazaki Y., Saiki Y., Moriyama M., Largaespada D.A.,
Jenkins N.A., Copeland N.G.;
"Evi9 encodes a novel zinc finger protein that physically interacts
with BCL6, a known human B-cell proto-oncogene product.";
Mol. Cell. Biol. 20:3178-3186(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH TFCOUP1;
EAR2 AND ARP1.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=10744719; DOI=10.1074/jbc.275.14.10315;
Avram D., Fields A., Pretty On Top K., Nevrivy D.J., Ishmael J.E.,
Leid M.;
"Isolation of a novel family of C(2)H(2) zinc finger proteins
implicated in transcriptional repression mediated by chicken ovalbumin
upstream promoter transcription factor (COUP-TF) orphan nuclear
receptors.";
J. Biol. Chem. 275:10315-10322(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
STRAIN=C57BL/6J;
TISSUE=Brain, Brain cortex, Corpora quadrigemina, Embryo, and
Spinal cord;
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 7).
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 8).
STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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).
[6]
FUNCTION.
PubMed=12717432; DOI=10.1038/ni925;
Liu P., Keller J.R., Ortiz M., Tessarollo L., Rachel R.A.,
Nakamura T., Jenkins N.A., Copeland N.G.;
"Bcl11a is essential for normal lymphoid development.";
Nat. Immunol. 4:525-532(2003).
[7]
SUMOYLATION AT LYS-634, INTERACTION WITH PIAS3, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF LYS-123 AND LYS-637.
PubMed=18681895; DOI=10.1111/j.1365-2443.2008.01216.x;
Kuwata T., Nakamura T.;
"BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes
in its nuclear body.";
Genes Cells 13:931-940(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-332; SER-337;
SER-446; SER-447; SER-608; SER-625; SER-630 AND THR-701,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-214 (ISOFORM 5),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-162 (ISOFORM 6), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Spleen;
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).
[9]
FUNCTION.
PubMed=23644491; DOI=10.1038/ng.2628;
Kadoch C., Hargreaves D.C., Hodges C., Elias L., Ho L., Ranish J.,
Crabtree G.R.;
"Proteomic and bioinformatic analysis of mammalian SWI/SNF complexes
identifies extensive roles in human malignancy.";
Nat. Genet. 45:592-601(2013).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-271, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[11]
DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND FUNCTION.
PubMed=27453576; DOI=10.1016/j.ajhg.2016.05.030;
DDD Study;
Dias C., Estruch S.B., Grmaham S.A., McRae J., Sawiak S.J.,
Hurst J.A., Joss S.K., Holder S.E., Morton J.E., Turner C.,
Thevenon J., Mellul K., Sanchez-Andrade G., Ibarra-Soria X.,
Deriziotis P., Santos R.F., Lee S.C., Faivre L., Kleefstra T., Liu P.,
Hurles M.E., Fisher S.E., Logan D.W.;
"BCL11A haploinsufficiency causes an intellectual disability syndrome
and dysregulates transcription.";
Am. J. Hum. Genet. 99:253-274(2016).
-!- FUNCTION: Functions as a myeloid and B-cell proto-oncogene. May
play important roles in leukemogenesis and hematopoiesis. An
essential factor in lymphopoiesis, is required for B-cell
formation in fetal liver. May function as a modulator of the
transcriptional repression activity of ARP1.
{ECO:0000269|PubMed:12717432}.
-!- SUBUNIT: Interacts with TFCOUP1, PIAS3, ARP1 and EAR2.
{ECO:0000269|PubMed:10744719, ECO:0000269|PubMed:18681895}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18681895}.
Nucleus {ECO:0000269|PubMed:18681895}. Note=Associates with the
nuclear body. Colocalizes with SUMO1 and SENP2 in nuclear
speckles.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1; Synonyms=a;
IsoId=Q9QYE3-1; Sequence=Displayed;
Name=2; Synonyms=b;
IsoId=Q9QYE3-10; Sequence=VSP_009557, VSP_009563;
Name=3; Synonyms=c;
IsoId=Q9QYE3-11; Sequence=VSP_009560;
Name=4;
IsoId=Q9QYE3-12; Sequence=VSP_009556, VSP_009564;
Name=5;
IsoId=Q9QYE3-13; Sequence=VSP_009561, VSP_009562;
Note=Contains a phosphothreonine at position 214.
{ECO:0000244|PubMed:21183079};
Name=6;
IsoId=Q9QYE3-14; Sequence=VSP_009558, VSP_009561, VSP_009562;
Note=Contains a phosphothreonine at position 162.
{ECO:0000244|PubMed:21183079};
Name=7;
IsoId=Q9QYE3-15; Sequence=VSP_009559;
Name=8;
IsoId=Q9QYE3-16; Sequence=VSP_009557;
-!- TISSUE SPECIFICITY: Isoforms are expressed in a tissue-specific
fashion. Isoforms 1, isoform 2, and isoform 3 are expressed at
similar levels in testis, kidney and spleen. Isoform 1 is
expressed in the stomach, and isoform 2 is expressed exclusively
in the lung. Overexpression following proviral integration in
hematopoietic cells results in the generation of myeloid leukemia.
-!- DEVELOPMENTAL STAGE: Highly expressed in the developing embryo.
Expressed in developing brain from embryonic day E10.5, with
highest expression in the forebrain between E12.5 and E14.5.
Central nervous system expression persists throughout the post-
natal period in the cortex, hippocampus, olfactory buld, and, to a
lesser extent, in the cerebellum. {ECO:0000269|PubMed:27453576}.
-!- DOMAIN: The N-terminus is involved in protein dimerization and in
transactivation of transcription. {ECO:0000250|UniProtKB:Q9H165}.
-!- PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:18681895}.
-!- DISRUPTION PHENOTYPE: Germline biallelic loss of Bcl11a leads to
perinatal lethality. Bcl11a +/- mice have a significantly
decreased brain volume, affecting both gray and white matter. The
limbic system (hippocampus and amygdala) is among the brain
regions that are more severely affected. Bcl11a +/- mice display
normal novelty-seeking behavior but show long-term social memory
defects, impaired sociability, and increased physical activity.
Bcl11a +/- mice show dynamic postnatal transcriptional
dysregulation in the brain. {ECO:0000269|PubMed:27453576}.
-!- SEQUENCE CAUTION:
Sequence=AAF63682.1; Type=Frameshift; Positions=744; Evidence={ECO:0000305};
Sequence=BAC65839.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF051525; AAF22430.1; -; mRNA.
EMBL; AF169036; AAF65928.1; -; mRNA.
EMBL; AF169037; AAF65929.1; -; mRNA.
EMBL; AF186018; AAF63682.1; ALT_FRAME; mRNA.
EMBL; AK004395; BAB23285.1; -; mRNA.
EMBL; AK043677; BAC31616.1; -; mRNA.
EMBL; AK045556; BAC32416.1; -; mRNA.
EMBL; AK049700; BAC33881.1; -; mRNA.
EMBL; AK122557; BAC65839.1; ALT_INIT; mRNA.
EMBL; BC010585; AAH10585.1; -; mRNA.
EMBL; BC051418; AAH51418.1; -; mRNA.
CCDS; CCDS24483.1; -. [Q9QYE3-1]
CCDS; CCDS48758.1; -. [Q9QYE3-13]
CCDS; CCDS48759.1; -. [Q9QYE3-14]
PIR; PT0706; PT0706.
RefSeq; NP_001152761.1; NM_001159289.1.
RefSeq; NP_001152762.1; NM_001159290.1. [Q9QYE3-14]
RefSeq; NP_001229863.1; NM_001242934.1.
RefSeq; NP_057916.1; NM_016707.3. [Q9QYE3-1]
UniGene; Mm.53687; -.
ProteinModelPortal; Q9QYE3; -.
SMR; Q9QYE3; -.
BioGrid; 199546; 2.
STRING; 10090.ENSMUSP00000105140; -.
iPTMnet; Q9QYE3; -.
PhosphoSitePlus; Q9QYE3; -.
PaxDb; Q9QYE3; -.
PeptideAtlas; Q9QYE3; -.
PRIDE; Q9QYE3; -.
Ensembl; ENSMUST00000000881; ENSMUSP00000000881; ENSMUSG00000000861. [Q9QYE3-1]
Ensembl; ENSMUST00000109516; ENSMUSP00000105142; ENSMUSG00000000861. [Q9QYE3-13]
Ensembl; ENSMUST00000118955; ENSMUSP00000112948; ENSMUSG00000000861. [Q9QYE3-14]
GeneID; 14025; -.
KEGG; mmu:14025; -.
UCSC; uc007ifs.2; mouse. [Q9QYE3-15]
UCSC; uc007ifu.2; mouse. [Q9QYE3-1]
UCSC; uc007ifv.2; mouse. [Q9QYE3-13]
UCSC; uc007ifw.2; mouse. [Q9QYE3-14]
CTD; 53335; -.
MGI; MGI:106190; Bcl11a.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00530000063542; -.
HOVERGEN; HBG050673; -.
InParanoid; Q9QYE3; -.
KO; K22045; -.
PhylomeDB; Q9QYE3; -.
TreeFam; TF318131; -.
PRO; PR:Q9QYE3; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000000861; -.
CleanEx; MM_BCL11A; -.
ExpressionAtlas; Q9QYE3; baseline and differential.
Genevisible; Q9QYE3; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
GO; GO:0030183; P:B cell differentiation; IMP:MGI.
GO; GO:0048671; P:negative regulation of collateral sprouting; ISO:MGI.
GO; GO:2000171; P:negative regulation of dendrite development; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0022008; P:neurogenesis; IBA:GO_Central.
GO; GO:0048672; P:positive regulation of collateral sprouting; ISO:MGI.
GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
GO; GO:0016925; P:protein sumoylation; IMP:UniProtKB.
GO; GO:0050773; P:regulation of dendrite development; ISO:MGI.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
GO; GO:0030217; P:T cell differentiation; IMP:MGI.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IBA:GO_Central.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 3.
SUPFAM; SSF57667; SSF57667; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Isopeptide bond;
Metal-binding; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 773 B-cell lymphoma/leukemia 11A.
/FTId=PRO_0000047103.
ZN_FING 170 193 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 377 399 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 405 429 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 1 210 Required for nuclear body formation and
for SUMO1 recruitment.
COMPBIAS 260 373 Pro-rich.
COMPBIAS 481 509 Glu-rich.
MOD_RES 86 86 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H165}.
MOD_RES 271 271 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 446 446 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 608 608 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 625 625 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 630 630 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 701 701 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 123 123 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H165}.
CROSSLNK 164 164 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H165}.
CROSSLNK 620 620 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H165}.
CROSSLNK 634 634 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:18681895}.
VAR_SEQ 1 423 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_009556.
VAR_SEQ 1 286 Missing (in isoform 2 and isoform 8).
{ECO:0000303|PubMed:10757802,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_009557.
VAR_SEQ 1 52 Missing (in isoform 6).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_009558.
VAR_SEQ 131 773 Missing (in isoform 7).
{ECO:0000303|PubMed:12693553}.
/FTId=VSP_009559.
VAR_SEQ 212 744 Missing (in isoform 3).
{ECO:0000303|PubMed:10757802}.
/FTId=VSP_009560.
VAR_SEQ 212 243 GIPSGLGAECPSQPPLHGIHIADNNPFNLLRI -> LHTPP
FGVVPRELKMCGSFRMEAQEPLSSEKL (in isoform 5
and isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_009561.
VAR_SEQ 244 773 Missing (in isoform 5 and isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_009562.
VAR_SEQ 726 773 Missing (in isoform 2).
{ECO:0000303|PubMed:10757802}.
/FTId=VSP_009563.
VAR_SEQ 745 773 PSHTPVRRSTPRAQDVWQFSDGSSRTLKF -> EYCGKVFK
NCSNLTVHRRSHTGERPYKCELCNYACAQSSKLTRHMKTHG
QVGKDVYKCEICKMPFSVYSTLEKHMKKWHSDRVLNNDIKT
E (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_009564.
MUTAGEN 123 123 K->R: No effect on sumoylation.
{ECO:0000269|PubMed:18681895}.
MUTAGEN 637 637 K->R: Abolishes sumoylation. No effect on
nuclear body location.
{ECO:0000269|PubMed:18681895}.
CONFLICT 104 104 Q -> K (in Ref. 3; BAB23285).
{ECO:0000305}.
CONFLICT 129 129 D -> G (in Ref. 4; BAC65839).
{ECO:0000305}.
CONFLICT 211 211 V -> G (in Ref. 1; AAF65929).
{ECO:0000305}.
CONFLICT 673 673 F -> L (in Ref. 2; AAF63682).
{ECO:0000305}.
CONFLICT 699 699 F -> L (in Ref. 1; AAF65928).
{ECO:0000305}.
CONFLICT 743 743 T -> I (in Ref. 2; AAF63682).
{ECO:0000305}.
CONFLICT 773 773 F -> L (in Ref. 2; AAF63682).
{ECO:0000305}.
SEQUENCE 773 AA; 83855 MW; 3BD10B7F14AA9EC4 CRC64;
MSRRKQGKPQ HLSKREFSPE PLEAILTDDE PDHGPLGAPE GDHDLLTCGQ CQMNFPLGDI
LIFIEHKRKQ CNGSLCLEKG VDKPPSPSPI EMKKASNPVE VGIQVTPEDD DCLSTSSRGI
CPKQEHIADK LLHWRGLSSP RSAHGALIPT PGMSAEYAPQ GICKDEPSSY TCTTCKQPFT
SAWFLLQHAQ NTHGLRIYLE SEHGSPLTPR VGIPSGLGAE CPSQPPLHGI HIADNNPFNL
LRIPGSVSRE ASGLAEGRFP PTPPLFSPPP RHHLDPHRIE RLGAEEMALA THHPSAFDRV
LRLNPMAMEP PAMDFSRRLR ELAGNTSSPP LSPGRPSPMQ RLLQPFQPGS KPPFLATPPL
PPLQSAPPPS QPPVKSKSCE FCGKTFKFQS NLVVHRRSHT GEKPYKCNLC DHACTQASKL
KRHMKTHMHK SSPMTVKSDD GLSTASSPEP GTSDLVGSAS SALKSVVAKF KSENDPNLIP
ENGDEEEEED DEEEEEEEEE EEEELTESER VDYGFGLSLE AARHHENSSR GAVVGVGDEG
RALPDVMQGM VLSSMQHFSE AFHQVLGEKH KRSHLAEAEG HRDTCDEDSV AGESDRIDDG
TVNGRGCSPG ESASGGLSKK LLLGSPSSLS PFSKRIKLEK EFDLPPAAMP NTENVYSQWL
AGYAASRQLK DPFLTFGDSR QSPFASSSEH SSENGSLRFS TPPGELDGGI SGRSGTGSGG
STPHISGPGP GRPSSKEGRR SDTCPSHTPV RRSTPRAQDV WQFSDGSSRT LKF


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