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Transcription intermediary factor 1-alpha (TIF1-alpha) (EC 2.3.2.27) (E3 ubiquitin-protein ligase Trim24) (RING-type E3 ubiquitin transferase TIF1-alpha) (Tripartite motif-containing protein 24)

 TIF1A_MOUSE             Reviewed;        1051 AA.
Q64127; Q64126;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 173.
RecName: Full=Transcription intermediary factor 1-alpha;
Short=TIF1-alpha;
EC=2.3.2.27;
AltName: Full=E3 ubiquitin-protein ligase Trim24;
AltName: Full=RING-type E3 ubiquitin transferase TIF1-alpha {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 24;
Name=Trim24; Synonyms=Tif1, Tif1a;
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], FUNCTION, INTERACTION WITH ESTROGEN
RECEPTOR, AND SUBCELLULAR LOCATION.
TISSUE=Carcinoma;
PubMed=7744009;
le Douarin B., Zechel C., Garnier J.-M., Lutz Y., Tora L., Pierrat B.,
Heery D., Gronemeyer H., Chambon P., Losson R.;
"The N-terminal part of TIF1, a putative mediator of the ligand-
dependent activation function (AF-2) of nuclear receptors, is fused to
B-raf in the oncogenic protein T18.";
EMBO J. 14:2020-2033(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
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).
[3]
INTERACTION WITH CBX1 AND CBX3.
PubMed=8978696;
le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H.,
Jeanmougin F., Losson R., Chambon P.;
"A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic
control of transcription by nuclear receptors.";
EMBO J. 15:6701-6715(1996).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PML.
PubMed=10610177; DOI=10.1038/15463;
Zhong S., Delva L., Rachez C., Cenciarelli C., Gandini D., Zhang H.,
Kalantry S., Freedman L.P., Pandolfi P.P.;
"A RA-dependent, tumour-growth suppressive transcription complex is
the target of the PML-RARalpha and T18 oncoproteins.";
Nat. Genet. 23:287-295(1999).
[5]
SUMOYLATION, SUBCELLULAR LOCATION, INTERACTION WITH CBX5, AND
MUTAGENESIS OF LYS-724 AND LYS-742.
PubMed=11313457; DOI=10.1128/MCB.21.10.3314-3324.2001;
Seeler J.-S., Marchio A., Losson R., Desterro J.M.P., Hay R.T.,
Chambon P., Dejean A.;
"Common properties of nuclear protein SP100 and TIF1alpha chromatin
factor: role of SUMO modification.";
Mol. Cell. Biol. 21:3314-3324(2001).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16880268; DOI=10.1083/jcb.200603146;
Torres-Padilla M.E., Zernicka-Goetz M.;
"Role of TIF1alpha as a modulator of embryonic transcription in the
mouse zygote.";
J. Cell Biol. 174:329-338(2006).
[7]
FUNCTION, INTERACTION WITH CARM1, AND IDENTIFICATION IN A COACTIVATOR
COMPLEX WITH CARM1 AND NCOA2/GRIP1.
PubMed=16322096; DOI=10.1210/me.2005-0393;
Teyssier C., Ou C.Y., Khetchoumian K., Losson R., Stallcup M.R.;
"Transcriptional intermediary factor 1alpha mediates physical
interaction and functional synergy between the coactivator-associated
arginine methyltransferase 1 and glucocorticoid receptor-interacting
protein 1 nuclear receptor coactivators.";
Mol. Endocrinol. 20:1276-1286(2006).
[8]
INDUCTION, AND TISSUE SPECIFICITY.
PubMed=17412818; DOI=10.1210/en.2006-1192;
Laz E.V., Holloway M.G., Chen C.S., Waxman D.J.;
"Characterization of three growth hormone-responsive transcription
factors preferentially expressed in adult female liver.";
Endocrinology 148:3327-3337(2007).
[9]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=18026104; DOI=10.1038/ng.2007.15;
Khetchoumian K., Teletin M., Tisserand J., Mark M., Herquel B.,
Ignat M., Zucman-Rossi J., Cammas F., Lerouge T., Thibault C.,
Metzger D., Chambon P., Losson R.;
"Loss of Trim24 (Tif1alpha) gene function confers oncogenic activity
to retinoic acid receptor alpha.";
Nat. Genet. 39:1500-1506(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1026, 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).
[11]
DISRUPTION PHENOTYPE.
PubMed=18287084; DOI=10.1073/pnas.0712030105;
Ignat M., Teletin M., Tisserand J., Khetchoumian K., Dennefeld C.,
Chambon P., Losson R., Mark M.;
"Arterial calcifications and increased expression of vitamin D
receptor targets in mice lacking TIF1alpha.";
Proc. Natl. Acad. Sci. U.S.A. 105:2598-2603(2008).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AR; KAT5/TIP60
AND BRD7.
PubMed=19909775; DOI=10.1016/j.bbamcr.2009.11.001;
Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N.,
Tanaka J., Imamura M., Hatakeyama S.;
"TRIM24 mediates ligand-dependent activation of androgen receptor and
is repressed by a bromodomain-containing protein, BRD7, in prostate
cancer cells.";
Biochim. Biophys. Acta 1793:1828-1836(2009).
[13]
FUNCTION, INTERACTION WITH TP53, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=19556538; DOI=10.1073/pnas.0813177106;
Allton K., Jain A.K., Herz H.M., Tsai W.W., Jung S.Y., Qin J.,
Bergmann A., Johnson R.L., Barton M.C.;
"Trim24 targets endogenous p53 for degradation.";
Proc. Natl. Acad. Sci. U.S.A. 106:11612-11616(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661; SER-668; SER-812
AND SER-1026, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, 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).
[15]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-469, 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).
-!- FUNCTION: Transcriptional coactivator that interacts with numerous
nuclear receptors and coactivators and modulates the transcription
of target genes. Interacts with chromatin depending on histone H3
modifications, having the highest affinity for histone H3 that is
both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23'
(H3K23ac) (By similarity). Has E3 protein-ubiquitin ligase
activity. Promotes ubiquitination and proteasomal degradation of
p53/TP53. Plays a role in the regulation of cell proliferation and
apoptosis via its effects on p53/TP53 levels. Up-regulates ligand-
dependent transcription activation by AR, GCR/NR3C1, thyroid
hormone receptor (TR) and ESR1. Modulates transcription activation
by retinoic acid (RA) receptors, such as RARA. Plays a role in
regulating retinoic acid-dependent proliferation of hepatocytes.
Required for normal transition from proliferating neonatal
hepatocytes to quiescent adult hepatocytes. {ECO:0000250,
ECO:0000269|PubMed:10610177, ECO:0000269|PubMed:16322096,
ECO:0000269|PubMed:16880268, ECO:0000269|PubMed:18026104,
ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:19909775,
ECO:0000269|PubMed:7744009}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts (via bromo domain) with histone H3 (via N-
terminus), provided that it is not methylated at 'Lys-4'
(H3K4me0). Does not interact with histone H3 that is methylated at
'Lys-4' (H3K4me1, H3K4me2 or H3K4me3). Interacts (via bromo
domain) with histone H3 (via N-terminus) that is acetylated at
'Lys-23' (H3K23ac). Has the highest affinity for histone H3 that
is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23'
(H3K23ac). Has very low affinity for histone H3 that is methylated
at 'Lys-9' (H3K9me), or acetylated at both 'Lys-9' (H3K9ac) and
'Lys-14' (H3K14ac), or acetylated at 'Lys-27' (H3K27ac) (in
vitro). Interacts with NR3C2/MCR (By similarity). Interacts with
the ligand-binding domain of estrogen receptors (in vitro).
Interaction with DNA-bound estrogen receptors requires the
presence of estradiol (By similarity). Interacts with AR, CARM1,
KAT5/TIP60, NCOA2/GRIP1, BRD7, CBX1, CBX3 and CBX5. Part of a
coactivator complex containing TRIM24, NCOA2/GRIP1 and CARM1.
Interacts with p53/TP53 and PML. {ECO:0000250,
ECO:0000269|PubMed:10610177, ECO:0000269|PubMed:11313457,
ECO:0000269|PubMed:16322096, ECO:0000269|PubMed:19556538,
ECO:0000269|PubMed:19909775, ECO:0000269|PubMed:7744009,
ECO:0000269|PubMed:8978696}.
-!- INTERACTION:
P83917:Cbx1; NbExp=4; IntAct=EBI-307947, EBI-78119;
Q61686:Cbx5; NbExp=4; IntAct=EBI-307947, EBI-307973;
P02340:Tp53; NbExp=2; IntAct=EBI-307947, EBI-474016;
Q99PP7:Trim33; NbExp=2; IntAct=EBI-307947, EBI-3043980;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Detected in the
cytoplasm of the zygote. Translocates into the pronucleus at the
time of genome activation. Colocalizes with sites of active
transcription.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=Q64127-1; Sequence=Displayed;
Name=Short;
IsoId=Q64127-2; Sequence=VSP_005773;
-!- TISSUE SPECIFICITY: Detected in embryonic and adult liver.
Detected in zygote and throughout embryogenesis (at protein
level). Detected in all adult tissues, with the highest expression
level in testis. {ECO:0000269|PubMed:17412818,
ECO:0000269|PubMed:18026104}.
-!- INDUCTION: Before puberty, highly expressed in liver from males
and females. After puberty, expression is considerably higher in
liver from females compared to males. Up-regulated in males by
continuous exposure to growth hormone.
{ECO:0000269|PubMed:17412818}.
-!- PTM: Sumoylated. {ECO:0000269|PubMed:11313457}.
-!- DISEASE: Note=A chromosomal aberration involving TRIM24 produces a
TRIM24-BRAF (T18) oncogene originally isolated from a furfural-
induced hepatoma.
-!- DISRUPTION PHENOTYPE: No visible phenotype during the first few
months. Impaired transition from proliferating neonatal
hepatocytes to quiescent adult hepatocytes. Hepatocytes continue
to proliferate throughout adulthood. High incidence hypertrophic
hepatocytes with enlarged nuclei after three months. After nine
months, about half of the mice have hepatocellular adenomas. Very
high incidence of hepatocarcinoma in 13 to 29 month old mice,
increasing from 40% to 80%. When one copy of Rara is disrupted,
mice do not develop liver tumors or liver dysplasia.
{ECO:0000269|PubMed:18026104, ECO:0000269|PubMed:18287084}.
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EMBL; S78221; AAB34290.1; -; mRNA.
EMBL; S78219; AAB34289.1; -; mRNA.
EMBL; BC056959; AAH56959.1; -; mRNA.
CCDS; CCDS20008.1; -. [Q64127-1]
CCDS; CCDS71751.1; -. [Q64127-2]
PIR; S55259; S55259.
RefSeq; NP_001258993.1; NM_001272064.1. [Q64127-2]
RefSeq; NP_001259005.1; NM_001272076.1.
RefSeq; NP_659542.3; NM_145076.4. [Q64127-1]
UniGene; Mm.41063; -.
ProteinModelPortal; Q64127; -.
SMR; Q64127; -.
BioGrid; 204196; 11.
DIP; DIP-31476N; -.
IntAct; Q64127; 13.
MINT; MINT-4137892; -.
STRING; 10090.ENSMUSP00000031859; -.
iPTMnet; Q64127; -.
PhosphoSitePlus; Q64127; -.
PaxDb; Q64127; -.
PeptideAtlas; Q64127; -.
PRIDE; Q64127; -.
Ensembl; ENSMUST00000031859; ENSMUSP00000031859; ENSMUSG00000029833. [Q64127-1]
Ensembl; ENSMUST00000120428; ENSMUSP00000113063; ENSMUSG00000029833. [Q64127-2]
GeneID; 21848; -.
KEGG; mmu:21848; -.
UCSC; uc009bjk.2; mouse. [Q64127-1]
UCSC; uc009bjl.2; mouse. [Q64127-2]
CTD; 8805; -.
MGI; MGI:109275; Trim24.
eggNOG; ENOG410ITFE; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00890000139374; -.
HOGENOM; HOG000252971; -.
HOVERGEN; HBG054599; -.
InParanoid; Q64127; -.
KO; K08881; -.
OMA; FWAQNIF; -.
OrthoDB; EOG091G01KK; -.
PhylomeDB; Q64127; -.
TreeFam; TF106455; -.
UniPathway; UPA00143; -.
ChiTaRS; Trim24; mouse.
PRO; PR:Q64127; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000029833; -.
CleanEx; MM_TRIM24; -.
ExpressionAtlas; Q64127; baseline and differential.
Genevisible; Q64127; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005719; C:nuclear euchromatin; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005726; C:perichromatin fibrils; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0034056; F:estrogen response element binding; ISS:UniProtKB.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; IDA:MGI.
GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0055074; P:calcium ion homeostasis; IMP:MGI.
GO; GO:0071391; P:cellular response to estrogen stimulus; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:MGI.
GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
GO; GO:0030163; P:protein catabolic process; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IGI:MGI.
GO; GO:0070562; P:regulation of vitamin D receptor signaling pathway; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00021; BBOX; 1.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 3.30.40.10; -; 3.
InterPro; IPR003649; Bbox_C.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF00628; PHD; 1.
Pfam; PF00643; zf-B_box; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00502; BBC; 1.
SMART; SM00336; BBOX; 2.
SMART; SM00297; BROMO; 1.
SMART; SM00249; PHD; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS50119; ZF_BBOX; 2.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Alternative splicing; Bromodomain; Chromosomal rearrangement;
Coiled coil; Complete proteome; Cytoplasm; DNA-binding;
Isopeptide bond; Metal-binding; Methylation; Nucleus; Phosphoprotein;
Proto-oncogene; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Transferase; Tumor suppressor;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 1051 Transcription intermediary factor 1-
alpha.
/FTId=PRO_0000056391.
DOMAIN 933 988 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
ZN_FING 52 77 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 158 211 B box-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
ZN_FING 218 259 B box-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
ZN_FING 827 874 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
REGION 755 780 Nuclear receptor binding site (NRBS).
REGION 835 841 Interaction with histone H3 that is not
methylated at 'Lys-4' (H3K4me0).
{ECO:0000250}.
COILED 289 359 {ECO:0000255}.
MOTIF 892 908 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 8 15 Poly-Ala.
COMPBIAS 19 22 Poly-Ala.
COMPBIAS 344 347 Poly-Gln.
COMPBIAS 583 587 Poly-Ser.
SITE 332 333 Breakpoint for translocation to form
TRIM24-BRAF oncogene.
SITE 828 828 Interaction with histone H3 that is not
methylated at 'Lys-4' (H3K4me0).
{ECO:0000250}.
MOD_RES 97 97 Phosphothreonine.
{ECO:0000250|UniProtKB:O15164}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000250|UniProtKB:O15164}.
MOD_RES 469 469 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 655 655 Phosphoserine.
{ECO:0000250|UniProtKB:O15164}.
MOD_RES 661 661 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 668 668 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 745 745 Phosphoserine.
{ECO:0000250|UniProtKB:O15164}.
MOD_RES 769 769 Phosphoserine.
{ECO:0000250|UniProtKB:O15164}.
MOD_RES 809 809 Phosphoserine.
{ECO:0000250|UniProtKB:O15164}.
MOD_RES 812 812 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 819 819 Phosphothreonine.
{ECO:0000250|UniProtKB:O15164}.
MOD_RES 1026 1026 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1029 1029 Phosphoserine.
{ECO:0000250|UniProtKB:O15164}.
MOD_RES 1043 1043 Phosphoserine.
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 205 205 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 276 276 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 436 436 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 458 458 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 553 553 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 642 642 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 703 703 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 712 712 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 724 724 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000305}.
CROSSLNK 724 724 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 724 724 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 742 742 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000305}.
CROSSLNK 742 742 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 802 802 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 811 811 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 876 876 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 950 950 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 993 993 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15164}.
CROSSLNK 1042 1042 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O15164}.
VAR_SEQ 477 510 Missing (in isoform Short).
{ECO:0000305}.
/FTId=VSP_005773.
MUTAGEN 724 724 K->R: Loss of sumoylation; when
associated with R-742.
{ECO:0000269|PubMed:11313457}.
MUTAGEN 742 742 K->R: Loss of sumoylation; when
associated with R-724.
{ECO:0000269|PubMed:11313457}.
SEQUENCE 1051 AA; 116657 MW; 610584C1C6885972 CRC64;
MEVAVEKAAA AAAPAGGPAA AAPSGENEAE SRQGPDSESG GEASRLNLLD TCAVCHQNIQ
SRVPKLLPCL HSFCQRCLPA PQRYLMLTAP ALGSAETPPP APAPAPAPGS PAGGPSPFAT
QVGVIRCPVC SQECAERHII DNFFVKDTTE VPSSTVEKSN QVCTSCEDNA EANGFCVECV
EWLCKTCIRA HQRVKFTKDH TVRQKEEVSP EAVGVTSQRP VFCPFHKKEQ LKLYCETCDK
LTCRDCQLLE HKEHRYQFIE EAFQNQKVII DTLITKLMEK TKYIKYTGNQ IQNRIIEINQ
NQKQVEQDIK VAIFTLMVEI NKKGKALLHQ LESLAKDHRM KLMQQQQEVA GLSKQLEHVM
HFSKWAVSSG SSTALLYSKR LITYRLRHLL RARCDASPVT NTTIQFHCDP SFWAQNIINL
GSLVIEDKES QPQMPKQNPV VEQSSQPPGG LPSNQLSKFP TQISLAQLRL QHIQQQVMAQ
RQQVQRRPAP VGLPNPRMQG PIQQPSISHQ HPPPRLINFQ NHSPKPNGPV LPPYPQQLRY
SPSQNVPRQT TIKPNPLQMA FLAQQAIKQW QISSVQAPPT TASSSSSTPS SPTITSAAGY
DGKAFSSPMI DLSAPVGGSY NLPSLPDIDC SSTIMLDNIA RKDTGVDHAQ PRPPSNRTVQ
SPNSSVPSPG LAGPVTMTSV HPPIRSPSAS SVGSRGSSGS SSKPAGADST HKVPVVMLEP
IRIKQENSGP PENYDFPVVI VKQESDEESR PQNTNYPRSI LTSLLLNSSQ SSASEETVLR
SDAPDSTGDQ PGLHQENSSN GKSEWSDASQ KSPVHVGETR KEDDPNEDWC AVCQNGGELL
CCEKCPKVFH LTCHVPTLTN FPSGEWICTF CRDLSKPEVD YDCDVPSHHS EKRKSEGLTK
LTPIDKRKCE RLLLFLYCHE MSLAFQDPVP LTVPDYYKII KNPMDLSTIK KRLQEDYCMY
TKPEDFVADF RLIFQNCAEF NEPDSEVANA GIKLESYFEE LLKNLYPEKR FPKVEFRHEA
EDCKFSDDSD DDFVQPRKKR LKSTEDRQLL K


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