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Transcriptional activator GLI3 (GLI3 form of 190 kDa) (GLI3-190) (GLI3 full-length protein) (GLI3FL) [Cleaved into: Transcriptional repressor GLI3R (GLI3 C-terminally truncated form) (GLI3 form of 83 kDa) (GLI3-83)]

 GLI3_MOUSE              Reviewed;        1583 AA.
Q61602;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 2.
25-OCT-2017, entry version 156.
RecName: Full=Transcriptional activator GLI3;
AltName: Full=GLI3 form of 190 kDa;
Short=GLI3-190;
AltName: Full=GLI3 full-length protein;
Short=GLI3FL;
Contains:
RecName: Full=Transcriptional repressor GLI3R;
AltName: Full=GLI3 C-terminally truncated form;
AltName: Full=GLI3 form of 83 kDa;
Short=GLI3-83;
Name=Gli3;
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].
STRAIN=NIH Swiss;
PubMed=8688459; DOI=10.1016/0167-4781(96)00079-6;
Thien H., Buescher D., Ruether U.;
"Cloning and sequence analysis of the murine Gli3 cDNA.";
Biochim. Biophys. Acta 1307:267-269(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
DISEASE.
PubMed=1983115;
Pohl T.M., Mattei M.G., Ruether U.;
"Evidence for allelism of the recessive insertional mutation add and
the dominant mouse mutation extra-toes (Xt).";
Development 110:1153-1157(1990).
[4]
DISEASE.
PubMed=10051311; DOI=10.1007/s003359900973;
Thien H., Ruether U.;
"The mouse mutation Pdn (Polydactyly Nagoya) is caused by the
integration of a retrotransposon into the Gli3 gene.";
Mamm. Genome 10:205-209(1999).
[5]
FUNCTION, AND PROTEOLYTIC PROCESSING.
PubMed=10693759; DOI=10.1016/S0092-8674(00)80678-9;
Wang B., Fallon J.F., Beachy P.A.;
"Hedgehog-regulated processing of Gli3 produces an anterior/posterior
repressor gradient in the developing vertebrate limb.";
Cell 100:423-434(2000).
[6]
FUNCTION, AND DNA-BINDING.
PubMed=11053430; DOI=10.1074/jbc.M004430200;
Mizugishi K., Aruga J., Nakata K., Mikoshiba K.;
"Molecular properties of Zic proteins as transcriptional regulators
and their relationship to GLI proteins.";
J. Biol. Chem. 276:2180-2188(2001).
[7]
FUNCTION.
PubMed=17400206; DOI=10.1016/j.ydbio.2007.02.029;
Wang C., Ruther U., Wang B.;
"The Shh-independent activator function of the full-length Gli3
protein and its role in vertebrate limb digit patterning.";
Dev. Biol. 305:460-469(2007).
[8]
PROTEOLYTIC PROCESSING.
PubMed=19592253; DOI=10.1016/j.cub.2009.06.046;
Endoh-Yamagami S., Evangelista M., Wilson D., Wen X., Theunissen J.W.,
Phamluong K., Davis M., Scales S.J., Solloway M.J., de Sauvage F.J.,
Peterson A.S.;
"The mammalian Cos2 homolog Kif7 plays an essential role in modulating
Hh signal transduction during development.";
Curr. Biol. 19:1320-1326(2009).
[9]
FUNCTION, AND INTERACTION WITH TRPS1.
PubMed=19389374; DOI=10.1016/j.ydbio.2009.01.012;
Wuelling M., Kaiser F.J., Buelens L.A., Braunholz D., Shivdasani R.A.,
Depping R., Vortkamp A.;
"Trps1, a regulator of chondrocyte proliferation and differentiation,
interacts with the activator form of Gli3.";
Dev. Biol. 328:40-53(2009).
[10]
INTERACTION WITH KIF7.
PubMed=19549984; DOI=10.1126/scisignal.2000405;
Cheung H.O., Zhang X., Ribeiro A., Mo R., Makino S., Puviindran V.,
Law K.K., Briscoe J., Hui C.C.;
"The kinesin protein Kif7 is a critical regulator of Gli transcription
factors in mammalian hedgehog signaling.";
Sci. Signal. 2:RA29-RA29(2009).
[11]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
SUFU.
PubMed=20360384; DOI=10.1101/gad.1902910;
Humke E.W., Dorn K.V., Milenkovic L., Scott M.P., Rohatgi R.;
"The output of Hedgehog signaling is controlled by the dynamic
association between Suppressor of Fused and the Gli proteins.";
Genes Dev. 24:670-682(2010).
[12]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-175, 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: Has a dual function as a transcriptional activator and a
repressor of the sonic hedgehog (Shh) pathway, and plays a role in
limb development. The full-length GLI3 form (GLI3FL) after
phosphorylation and nuclear translocation, acts as an activator
(GLI3A) while GLI3R, its C-terminally truncated form, acts as a
repressor. A proper balance between the GLI3 activator and the
repressor GLI3R, rather than the repressor gradient itself or the
activator/repressor ratio gradient, specifies limb digit number
and identity. In concert with TRPS1, plays a role in regulating
the size of the zone of distal chondrocytes, in restricting the
zone of PTHLH expression in distal cells and in activating
chondrocyte proliferation. Binds to the minimal GLI-consensus
sequence 5'-GGGTGGTC-3'. {ECO:0000269|PubMed:10693759,
ECO:0000269|PubMed:11053430, ECO:0000269|PubMed:17400206,
ECO:0000269|PubMed:19389374, ECO:0000269|PubMed:20360384}.
-!- SUBUNIT: The phosphorylated form interacts with BTRC (By
similarity). The full-length GLI3 form (GLI3FL) interacts with
SUFU and this interaction regulates the formation of either
repressor or activator forms of GLI3. Its association with SUFU is
regulated by Hh signaling and dissociation of the SUFU-GLI3
interaction requires the presence of the ciliary motor KIF3A.
Interacts with KIF7. The activator form of GLI3 (GLI3A) but not
the repressor form (GLI3R) can interact with TRPS1. Interacts with
ZIC1. Interacts with ZIC3 (via C2H2-type domains 3, 4 and 5); the
interaction enhances its transcriptional activity (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20360384}.
Cytoplasm {ECO:0000269|PubMed:20360384}. Cell projection, cilium
{ECO:0000269|PubMed:20360384}. Note=Translocation to the nucleus
is promoted by interaction with ZIC1 (By similarity). GLI3FL is
localized predominantly in the cytoplasm while GLI3R resides
mainly in the nucleus. Ciliary accumulation requires the presence
of KIF7 and SMO. {ECO:0000250}.
-!- PTM: Phosphorylated by DYRK2 (in vitro) (By similarity).
Phosphorylated on multiple sites by protein kinase A (PKA) and
phosphorylation by PKA primes further phosphorylation by CK1 and
GSK3. Phosphorylation is essential for its proteolytic processing.
{ECO:0000250, ECO:0000269|PubMed:20360384}.
-!- PTM: Transcriptional repressor GLI3R, a C-terminally truncated
form, is generated from the full-length GLI3 protein (GLI3FL/GLI3-
190) through proteolytic processing. This process requires PKA-
primed phosphorylation of GLI3, ubiquitination of GLI3 and the
presence of BTRC. GLI3FL is complexed with SUFU in the cytoplasm
and is maintained in a neutral state. Without the Hh signal, the
SUFU-GLI3 complex is recruited to cilia, leading to the efficient
processing of GLI3FL into GLI3R. GLI3R formation leads to its
dissociation from SUFU, allowing it to translocate into the
nucleus, and repress Hh target genes. When Hh signaling is
initiated, SUFU dissociates from GLI3FL and this has two
consequences. First, GLI3R production is halted. Second, free
GLI3FL translocates to the nucleus, where it is phosphorylated,
destabilized, and converted to a transcriptional activator
(GLI3A). Phosphorylated in vitro by ULK3.
{ECO:0000269|PubMed:20360384}.
-!- DISEASE: Note=Several mutations result in developmental defects of
cranofacial and limb structures. In particular the add (anterior
digit-pattern deformity) and pdn (polydactyly Nagoya) alleles.
{ECO:0000269|PubMed:10051311, ECO:0000269|PubMed:1983115}.
-!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA64543.1; Type=Frameshift; Positions=1552; Evidence={ECO:0000305};
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EMBL; X95255; CAA64543.1; ALT_FRAME; mRNA.
EMBL; AC163610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC173115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC173210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS36603.1; -.
RefSeq; NP_032156.2; NM_008130.2.
UniGene; Mm.5098; -.
ProteinModelPortal; Q61602; -.
SMR; Q61602; -.
BioGrid; 199944; 8.
CORUM; Q61602; -.
STRING; 10090.ENSMUSP00000106137; -.
iPTMnet; Q61602; -.
PhosphoSitePlus; Q61602; -.
MaxQB; Q61602; -.
PaxDb; Q61602; -.
PRIDE; Q61602; -.
Ensembl; ENSMUST00000110510; ENSMUSP00000106137; ENSMUSG00000021318.
GeneID; 14634; -.
KEGG; mmu:14634; -.
UCSC; uc007pns.1; mouse.
CTD; 2737; -.
MGI; MGI:95729; Gli3.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00900000140802; -.
HOGENOM; HOG000290688; -.
HOVERGEN; HBG005844; -.
InParanoid; Q61602; -.
KO; K06230; -.
OMA; MHNKRSK; -.
OrthoDB; EOG091G01XS; -.
PhylomeDB; Q61602; -.
TreeFam; TF350216; -.
Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-MMU-5610787; Hedgehog 'off' state.
Reactome; R-MMU-5632684; Hedgehog 'on' state.
PRO; PR:Q61602; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021318; -.
CleanEx; MM_GLI3; -.
ExpressionAtlas; Q61602; baseline and differential.
Genevisible; Q61602; MM.
GO; GO:0005930; C:axoneme; IDA:CACAO.
GO; GO:0005929; C:cilium; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0016592; C:mediator complex; IEA:Ensembl.
GO; GO:0016607; C:nuclear speck; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0017053; C:transcriptional repressor complex; IDA:MGI.
GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IGI:MGI.
GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0048856; P:anatomical structure development; IGI:MGI.
GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IGI:MGI.
GO; GO:0060873; P:anterior semicircular canal development; IMP:MGI.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
GO; GO:0060840; P:artery development; IGI:MGI.
GO; GO:0007411; P:axon guidance; IMP:MGI.
GO; GO:0007420; P:brain development; IMP:MGI.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IGI:MGI.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
GO; GO:0043010; P:camera-type eye development; IGI:MGI.
GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
GO; GO:0061005; P:cell differentiation involved in kidney development; IGI:MGI.
GO; GO:0007417; P:central nervous system development; IMP:MGI.
GO; GO:0021801; P:cerebral cortex radial glia guided migration; IMP:MGI.
GO; GO:0048589; P:developmental growth; IMP:MGI.
GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
GO; GO:0048566; P:embryonic digestive tract development; IMP:MGI.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:MGI.
GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
GO; GO:0048598; P:embryonic morphogenesis; IMP:MGI.
GO; GO:0048704; P:embryonic skeletal system morphogenesis; IGI:MGI.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0021798; P:forebrain dorsal/ventral pattern formation; IMP:MGI.
GO; GO:0021861; P:forebrain radial glial cell differentiation; IMP:MGI.
GO; GO:0060364; P:frontal suture morphogenesis; IMP:MGI.
GO; GO:0007507; P:heart development; IGI:MGI.
GO; GO:0007442; P:hindgut morphogenesis; IGI:MGI.
GO; GO:0021766; P:hippocampus development; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0048839; P:inner ear development; IGI:MGI.
GO; GO:0001822; P:kidney development; IGI:MGI.
GO; GO:0060366; P:lambdoid suture morphogenesis; IMP:MGI.
GO; GO:0022018; P:lateral ganglionic eminence cell proliferation; IMP:MGI.
GO; GO:0060875; P:lateral semicircular canal development; IMP:MGI.
GO; GO:0021819; P:layer formation in cerebral cortex; IMP:MGI.
GO; GO:0060173; P:limb development; IMP:UniProtKB.
GO; GO:0035108; P:limb morphogenesis; IMP:MGI.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0030324; P:lung development; IMP:MGI.
GO; GO:0030879; P:mammary gland development; IMP:MGI.
GO; GO:0060594; P:mammary gland specification; IGI:MGI.
GO; GO:0030318; P:melanocyte differentiation; IMP:MGI.
GO; GO:0001656; P:metanephros development; IGI:MGI.
GO; GO:0046639; P:negative regulation of alpha-beta T cell differentiation; IMP:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0045596; P:negative regulation of cell differentiation; IGI:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0045060; P:negative thymic T cell selection; IMP:BHF-UCL.
GO; GO:0021915; P:neural tube development; IMP:MGI.
GO; GO:0048663; P:neuron fate commitment; IMP:MGI.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IGI:MGI.
GO; GO:0048709; P:oligodendrocyte differentiation; IGI:MGI.
GO; GO:0021631; P:optic nerve morphogenesis; IMP:MGI.
GO; GO:0060021; P:palate development; IMP:MGI.
GO; GO:0021543; P:pallium development; IMP:MGI.
GO; GO:0007389; P:pattern specification process; IGI:MGI.
GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IMP:BHF-UCL.
GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:MGI.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:MGI.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IGI:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030850; P:prostate gland development; IEA:Ensembl.
GO; GO:0016485; P:protein processing; IDA:MGI.
GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
GO; GO:1903010; P:regulation of bone development; IMP:MGI.
GO; GO:0045595; P:regulation of cell differentiation; IGI:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0060367; P:sagittal suture morphogenesis; IMP:MGI.
GO; GO:0007224; P:smoothened signaling pathway; IGI:MGI.
GO; GO:0060831; P:smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IGI:MGI.
GO; GO:0021776; P:smoothened signaling pathway involved in spinal cord motor neuron cell fate specification; IGI:MGI.
GO; GO:0021775; P:smoothened signaling pathway involved in ventral spinal cord interneuron specification; IGI:MGI.
GO; GO:0021513; P:spinal cord dorsal/ventral patterning; IGI:MGI.
GO; GO:0021522; P:spinal cord motor neuron differentiation; IGI:MGI.
GO; GO:0021544; P:subpallium development; IMP:MGI.
GO; GO:0033077; P:T cell differentiation in thymus; IMP:BHF-UCL.
GO; GO:0021537; P:telencephalon development; IMP:MGI.
GO; GO:0070242; P:thymocyte apoptotic process; IMP:BHF-UCL.
GO; GO:0043586; P:tongue development; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0035295; P:tube development; IGI:MGI.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR032851; GLI3.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR19818:SF5; PTHR19818:SF5; 1.
SMART; SM00355; ZnF_C2H2; 5.
SUPFAM; SSF57667; SSF57667; 3.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
1: Evidence at protein level;
Acetylation; Activator; Cell projection; Cilium; Complete proteome;
Cytoplasm; DNA-binding; Isopeptide bond; Metal-binding; Methylation;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 1583 Transcriptional activator GLI3.
/FTId=PRO_0000047203.
CHAIN 1 ? Transcriptional repressor GLI3R.
/FTId=PRO_0000406138.
ZN_FING 480 505 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 513 540 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 546 570 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 576 601 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 607 632 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
COMPBIAS 120 199 Pro-rich.
COMPBIAS 849 910 Ser-rich.
COMPBIAS 1494 1514 Asp/Glu-rich (acidic).
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P10071}.
MOD_RES 175 175 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 664 664 Phosphoserine.
{ECO:0000250|UniProtKB:P10071}.
MOD_RES 849 849 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P10071}.
MOD_RES 865 865 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P10071}.
MOD_RES 877 877 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P10071}.
MOD_RES 907 907 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P10071}.
MOD_RES 980 980 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P10071}.
MOD_RES 1006 1006 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P10071}.
CROSSLNK 438 438 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P10071}.
CROSSLNK 462 462 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P10071}.
CROSSLNK 773 773 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P10071}.
CROSSLNK 779 779 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P10071}.
CROSSLNK 779 779 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P10071}.
CROSSLNK 784 784 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P10071}.
CROSSLNK 800 800 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P10071}.
CONFLICT 209 209 S -> C (in Ref. 1; CAA64543).
{ECO:0000305}.
CONFLICT 428 428 D -> G (in Ref. 1; CAA64543).
{ECO:0000305}.
CONFLICT 928 928 R -> A (in Ref. 1; CAA64543).
{ECO:0000305}.
CONFLICT 936 936 A -> P (in Ref. 1; CAA64543).
{ECO:0000305}.
CONFLICT 1005 1005 A -> D (in Ref. 1; CAA64543).
{ECO:0000305}.
CONFLICT 1185 1186 SA -> R (in Ref. 1; CAA64543).
{ECO:0000305}.
CONFLICT 1475 1476 NG -> TC (in Ref. 1; CAA64543).
{ECO:0000305}.
SEQUENCE 1583 AA; 171655 MW; 37ECC0C3ACF26C24 CRC64;
MEAQAHSSTA TERKKAENSI GKCPTRTDVS EKAVASSTTS NEDESPGQIY HRERRNAITM
QPQSVQGLNK ISEEPSTSSD ERASLIKKEI HGSLPHLAEP SLPYRGTVFA MDPRNGYMEP
HYHPPHLFPA FHPPVPIDAR HHEGRYHYDP SPIPPLHVPS ALSSSPTYPD LPFIRISPHR
NPTAASESPF SPPHPYINPY MDYIRSLHSS PSLSMISAAR GLSPTDAPHA GVSPAEYYHQ
MALLTGQRSP YADILPSAAT AGAGAIHMEY LHAMDSTRFP SPRLSARPSR KRTLSISPLS
DHSFDLQTMI RTSPNSLVTI LNNSRSSSSA SGSYGHLSAS AISPALSFTY PSAPVSLHMH
QQILSRQQSL GSAFGHSPPL IHPAPTFPTQ RPIPGIPTVL NPVQVSSGPS ESSQSKPTSE
SAVSSTGDPM HNKRSKIKPD EDLPSPGSRG QQEQPEGTTL VKEEADKDES KQEPEVIYET
NCHWEGCTRE FDTQDQLVHH INNDHIHGEK KEFVCRWLDC SREQKPFKAQ YMLVVHMRRH
TGEKPHKCTF EGCTKAYSRL ENLKTHLRSH TGEKPYVCEH EGCNKAFSNA SDRAKHQNRT
HSNEKPYVCK IPGCTKRYTD PSSLRKHVKT VHGPEAHVTK KQRGDMHPRP PPPRDSGSHS
QSRSPGRPTQ GAFGEQKELS NTTSKREECL QVKTVKAEKP MTSQPSPGGQ SSCSSQQSPI
SNYSNSGLEL PLTDGGSVAD LSAIDETPIM DSTISTATTA LALQARRNPA GTKWMEHIKL
ERLKQVNGMF PRLNPILPSK APAVSPLIGN GTQSNNNYSS GGPGTLLPSR SDLSGVDFTV
LNTLNRRDSN TSTISSAYLS SRRSSGISPC FSSRRSSEAS QAEGRPQNVS VADSYDPIST
DASRRSSEAS QGDGLPSLLS LTPVQQYRLK AKYAAATGGP PPTPLPHMER LSLKTKMALL
GEGRDSGVTL PPVHPPRRCS DGGGHTYRGR HLMPHDALAN SVRRASDPVR TVSENMSLAR
VQRFSSLNSF NPPNLPPSVE KRSLVLQNYT RQESSQPRYF QASPCPPSIT ENVALEALTM
DADANLNDED LLPDDVVQYL NSQNQTGYGQ QLQSGISEDS KVAHEPEDLD LAGLPDSHVG
QEYPALEQPC SEGSKTDLPI QWNEVSSGTS DLSSSKLKCG QQRPSAQQPR GFGLYNNMVV
HPHNLWKVGT GPAGGYQTLG ENSSTYNGPE HFAIHSGDGL GTNGNTFHEQ PFKTQQYGSQ
LNRQPLTSSA LDHACGTGIQ GSKLKGNSLQ ENGGLLDFSL SVAPNELAGN TVNGMQTQDQ
MGQGYIAHQL LSGSMQHQGP SRPGQQVLGQ VGATSHINIY QGTESCLPGT QDNSSQPSSM
AAIRGYQPCA SYGGNRRQAM PRGNLTLQQG QLSDMSQSSR VNSIKMEAQG QSQQLCSTVQ
NYSGQFYDQT MGFSQQDRKA GSFSLSDANC LLQGNGTENS ELLSPGANQV TSTVDSFESH
DLEGVQIDFD AIIDDGDHTS LMSGALSPSI IQNLSHSSSR LTTPRASLPF PSLSMGTTNM
AIGDMSSLLT SLAEESKFLA VMQ


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