PIAS3_MOUSE
ID PIAS3_MOUSE Reviewed; 628 AA.
AC O54714; Q80WF8; Q8R598;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=E3 SUMO-protein ligase PIAS3;
DE EC=2.3.2.-;
DE AltName: Full=E3 SUMO-protein transferase PIAS3 {ECO:0000305};
DE AltName: Full=Protein inhibitor of activated STAT protein 3;
GN Name=Pias3;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor, and Retina;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-628 (ISOFORM 3), AND INTERACTION WITH
RP STAT3.
RC TISSUE=Thymus;
RX PubMed=9388184; DOI=10.1126/science.278.5344.1803;
RA Chung C.D., Liao J., Liu B., Rao X., Jay P., Berta P., Shuai K.;
RT "Specific inhibition of Stat3 signal transduction by PIAS3.";
RL Science 278:1803-1805(1997).
RN [4]
RP SEQUENCE REVISION.
RA Shuai K.;
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH GFI1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11060035; DOI=10.1093/emboj/19.21.5845;
RA Roedel B., Tavassoli K., Karsunky H., Schmidt T., Bachmann M., Schaper F.,
RA Heinrich P., Shuai K., Elsaesser H.-P., Moeroey T.;
RT "The zinc finger protein Gfi-1 can enhance STAT3 signaling by interacting
RT with the STAT3 inhibitor PIAS3.";
RL EMBO J. 19:5845-5855(2000).
RN [6]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10854042; DOI=10.1385/jmn:14:1-2:107;
RA Sturm S., Koch M., White F.A.;
RT "Cloning and analysis of a murine Pias family member, Pias-gamma, in
RT developing skin and neurons.";
RL J. Mol. Neurosci. 14:107-121(2000).
RN [7]
RP INTERACTION WITH AR.
RX PubMed=11117529; DOI=10.1210/mend.14.12.0569;
RA Kotaja N., Aittomaeki S., Silvennoinen O., Palvimo J.J., Jaenne O.A.;
RT "ARIP3 (androgen receptor-interacting protein 3) and other PIAS (protein
RT inhibitor of activated STAT) proteins differ in their ability to modulate
RT steroid receptor-dependent transcriptional activation.";
RL Mol. Endocrinol. 14:1986-2000(2000).
RN [8]
RP INTERACTION WITH HMGA2.
RX PubMed=11390395; DOI=10.1074/jbc.m103153200;
RA Zentner M.D., Lin H.H., Deng H.-T., Kim K.-J., Shih H.-M., Ann D.K.;
RT "Requirement for high mobility group protein HMGI-C interaction with STAT3
RT inhibitor PIAS3 in repression of alpha-subunit of epithelial Na+ channel
RT (alpha-ENaC) transcription by Ras activation in salivary epithelial
RT cells.";
RL J. Biol. Chem. 276:29805-29814(2001).
RN [9]
RP INTERACTION WITH NCOA2.
RX PubMed=12208521; DOI=10.1016/s0014-5793(02)03154-x;
RA Jimenez-Lara A.M., Heine M.J.S., Gronemeyer H.;
RT "PIAS3 (protein inhibitor of activated STAT-3) modulates the
RT transcriptional activation mediated by the nuclear receptor coactivator
RT TIF2.";
RL FEBS Lett. 526:142-146(2002).
RN [10]
RP INTERACTION WITH IRF1; SUMO1 AND UBE2I, SUMOYLATION, AND MUTAGENESIS OF
RP CYS-343.
RX PubMed=12387893; DOI=10.1016/s0014-5793(02)03486-5;
RA Nakagawa K., Yokosawa H.;
RT "PIAS3 induces SUMO-1 modification and transcriptional repression of IRF-
RT 1.";
RL FEBS Lett. 530:204-208(2002).
RN [11]
RP INTERACTION WITH MITF, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11709556; DOI=10.1074/jbc.m109236200;
RA Levy C., Nechushtan H., Razin E.;
RT "A new role for the STAT3 inhibitor, PIAS3: a repressor of microphthalmia
RT transcription factor.";
RL J. Biol. Chem. 277:1962-1966(2002).
RN [12]
RP INTERACTION WITH SUMO1 AND UBE2I, AND SUBCELLULAR LOCATION.
RX PubMed=12077349; DOI=10.1128/mcb.22.14.5222-5234.2002;
RA Kotaja N., Karvonen U., Jaenne O.A., Palvimo J.J.;
RT "PIAS proteins modulate transcription factors by functioning as SUMO-1
RT ligases.";
RL Mol. Cell. Biol. 22:5222-5234(2002).
RN [13]
RP STAT1 SUMOYLATION.
RX PubMed=12855578; DOI=10.1182/blood-2002-12-3816;
RA Ungureanu D., Vanhatupa S., Kotaja N., Yang J., Aittomaeki S., Jaenne O.A.,
RA Palvimo J.J., Silvennoinen O.;
RT "PIAS proteins promote SUMO-1 conjugation to STAT1.";
RL Blood 102:3311-3313(2003).
RN [14]
RP FUNCTION OF THE PINIT MOTIF, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 19-LEU--LEU-23; 242-PRO--THR-244 AND 343-CYS--SER-348.
RX PubMed=14596924; DOI=10.1016/s0014-5793(03)01116-5;
RA Duval D., Duval G., Kedinger C., Poch O., Boeuf H.;
RT "The 'PINIT' motif, of a newly identified conserved domain of the PIAS
RT protein family, is essential for nuclear retention of PIAS3L.";
RL FEBS Lett. 554:111-118(2003).
RN [15]
RP INTERACTION WITH BCL11A.
RX PubMed=18681895; DOI=10.1111/j.1365-2443.2008.01216.x;
RA Kuwata T., Nakamura T.;
RT "BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes in
RT its nuclear body.";
RL Genes Cells 13:931-940(2008).
CC -!- FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO)
CC ligase, stabilizing the interaction between UBE2I and the substrate,
CC and as a SUMO-tethering factor. Plays a crucial role as a
CC transcriptional coregulation in various cellular pathways, including
CC the STAT pathway and the steroid hormone signaling pathway. Repressor
CC of STAT3 signaling via inhibiting STAT3 DNA-binding and suppressing
CC cell growth. Repressor of MITF transcriptional activity. Enhances the
CC sumoylation of MTA1 and may participate in its paralog-selective
CC sumoylation. Sumoylates CCAR2 which promotes its interaction with SIRT1
CC (By similarity). Diminishes the sumoylation of ZFHX3 by preventing the
CC colocalization of ZFHX3 with SUMO1 in the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y6X2, ECO:0000269|PubMed:11060035,
CC ECO:0000269|PubMed:11709556, ECO:0000269|PubMed:14596924}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Monomer. Interacts with PLAG1 and ZFHX3. Interacts with
CC STAT5A; the interaction occurs on stimulation by PRL (By similarity).
CC Binds SUMO1 and UBE2I. Interacts with AR, BCL11A, HMGA2, IRF1 and
CC NCOA2. Interacts with MITF; the interaction inhibits the
CC transcriptional activity of MITF. Interacts with STAT3; the interaction
CC occurs on stimulation by IL6, CNTF or OSM and inhibits the DNA binding
CC activity of STAT3. Interacts with GFI1; the interaction relieves the
CC inhibitory effect of PIAS3 on STAT3-mediated transcriptional activity.
CC Interacts with MTA1. Interacts with CCAR2 (via N-terminus) (By
CC similarity). Interacts with TRIM8 (By similarity). Interacts with PRDM1
CC (By similarity). {ECO:0000250|UniProtKB:Q9Y6X2,
CC ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11117529,
CC ECO:0000269|PubMed:11390395, ECO:0000269|PubMed:11709556,
CC ECO:0000269|PubMed:12077349, ECO:0000269|PubMed:12208521,
CC ECO:0000269|PubMed:12387893, ECO:0000269|PubMed:18681895,
CC ECO:0000269|PubMed:9388184}.
CC -!- INTERACTION:
CC O54714; P70338: Gfi1; NbExp=6; IntAct=EBI-927969, EBI-3954754;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11060035,
CC ECO:0000269|PubMed:11709556}. Nucleus {ECO:0000269|PubMed:11060035,
CC ECO:0000269|PubMed:11709556, ECO:0000269|PubMed:14596924}. Nucleus
CC speckle {ECO:0000269|PubMed:12077349}. Note=Colocalizes with MITF in
CC the nucleus (PubMed:11709556). Colocalizes with GFI1 in nuclear dots
CC (PubMed:11060035). Colocalizes with SUMO1 in nuclear granules
CC (PubMed:12077349). {ECO:0000269|PubMed:11060035,
CC ECO:0000269|PubMed:11709556, ECO:0000269|PubMed:12077349}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O54714-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O54714-2; Sequence=VSP_012203;
CC Name=3;
CC IsoId=O54714-3; Sequence=VSP_012204;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, heart, spleen, brain and
CC cerebellum; weak expression, if any, in liver and lung.
CC {ECO:0000269|PubMed:10854042, ECO:0000269|PubMed:14596924}.
CC -!- DEVELOPMENTAL STAGE: Expressed as early as 7.6 dpc. Expression remains
CC high through 15.5 dpc. {ECO:0000269|PubMed:10854042}.
CC -!- DOMAIN: The LXXLL motif is a transcriptional coregulator signature.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:12387893}.
CC -!- SIMILARITY: Belongs to the PIAS family. {ECO:0000305}.
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DR EMBL; AK040619; BAC30647.1; -; mRNA.
DR EMBL; AK077551; BAC36858.1; -; mRNA.
DR EMBL; BC023128; AAH23128.1; -; mRNA.
DR EMBL; BC051252; AAH51252.1; -; mRNA.
DR EMBL; AF034080; AAB88902.3; -; mRNA.
DR CCDS; CCDS17645.2; -. [O54714-3]
DR CCDS; CCDS38559.1; -. [O54714-2]
DR CCDS; CCDS51007.1; -. [O54714-1]
DR RefSeq; NP_001159421.1; NM_001165949.1. [O54714-1]
DR RefSeq; NP_061282.2; NM_018812.2. [O54714-3]
DR RefSeq; NP_666247.1; NM_146135.2. [O54714-2]
DR RefSeq; XP_006501456.1; XM_006501393.1. [O54714-2]
DR AlphaFoldDB; O54714; -.
DR SMR; O54714; -.
DR BioGRID; 230874; 21.
DR IntAct; O54714; 2.
DR STRING; 10090.ENSMUSP00000069259; -.
DR PhosphoSitePlus; O54714; -.
DR EPD; O54714; -.
DR MaxQB; O54714; -.
DR PaxDb; O54714; -.
DR PRIDE; O54714; -.
DR ProteomicsDB; 288148; -. [O54714-1]
DR ProteomicsDB; 288149; -. [O54714-2]
DR ProteomicsDB; 288150; -. [O54714-3]
DR Antibodypedia; 20233; 261 antibodies from 39 providers.
DR DNASU; 229615; -.
DR Ensembl; ENSMUST00000064900; ENSMUSP00000069259; ENSMUSG00000028101. [O54714-1]
DR Ensembl; ENSMUST00000107076; ENSMUSP00000102691; ENSMUSG00000028101. [O54714-2]
DR Ensembl; ENSMUST00000107077; ENSMUSP00000102692; ENSMUSG00000028101. [O54714-3]
DR GeneID; 229615; -.
DR KEGG; mmu:229615; -.
DR UCSC; uc008qnt.2; mouse. [O54714-1]
DR UCSC; uc008qnu.2; mouse. [O54714-3]
DR CTD; 10401; -.
DR MGI; MGI:1913126; Pias3.
DR VEuPathDB; HostDB:ENSMUSG00000028101; -.
DR eggNOG; KOG2169; Eukaryota.
DR GeneTree; ENSGT01030000234539; -.
DR HOGENOM; CLU_020768_1_0_1; -.
DR InParanoid; O54714; -.
DR OMA; HYMSPLT; -.
DR OrthoDB; 1205949at2759; -.
DR PhylomeDB; O54714; -.
DR TreeFam; TF323787; -.
DR Reactome; R-MMU-3232118; SUMOylation of transcription factors.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-4755510; SUMOylation of immune response proteins.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 229615; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Pias3; mouse.
DR PRO; PR:O54714; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O54714; protein.
DR Bgee; ENSMUSG00000028101; Expressed in retinal neural layer and 260 other tissues.
DR ExpressionAtlas; O54714; baseline and differential.
DR Genevisible; O54714; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0015459; F:potassium channel regulator activity; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR GO; GO:0019789; F:SUMO transferase activity; IDA:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:MGI.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IDA:MGI.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0045838; P:positive regulation of membrane potential; ISO:MGI.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; ISS:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR GO; GO:0071847; P:TNFSF11-mediated signaling pathway; IDA:MGI.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.60.120.780; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR027226; PIAS3.
DR InterPro; IPR023321; PINIT.
DR InterPro; IPR038654; PINIT_sf.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782:SF10; PTHR10782:SF10; 1.
DR Pfam; PF14324; PINIT; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS51466; PINIT; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..628
FT /note="E3 SUMO-protein ligase PIAS3"
FT /id="PRO_0000218980"
FT DOMAIN 11..45
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 115..280
FT /note="PINIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00799"
FT ZN_FING 312..393
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT REGION 1..200
FT /note="Interaction with CCAR2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X2"
FT REGION 450..460
FT /note="SUMO1-binding"
FT /evidence="ECO:0000250"
FT REGION 571..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 19..23
FT /note="LXXLL motif"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X2"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X2"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X2"
FT CROSSLNK 307
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X2"
FT CROSSLNK 466
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X2"
FT CROSSLNK 482
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X2"
FT VAR_SEQ 1..9
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_012203"
FT VAR_SEQ 87..121
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9388184"
FT /id="VSP_012204"
FT MUTAGEN 19..23
FT /note="LQVLL->AQVAA: Nuclear and cytoplasmic location."
FT /evidence="ECO:0000269|PubMed:14596924"
FT MUTAGEN 141
FT /note="L->A: Greatly reduced interaction with STAT3."
FT MUTAGEN 143
FT /note="R->N: Abolishes interaction with STAT3."
FT MUTAGEN 143
FT /note="R->Q: Abolishes interaction with STAT3."
FT MUTAGEN 242..244
FT /note="INI->SDS: Nuclear and cytoplasmic location."
FT /evidence="ECO:0000269|PubMed:14596924"
FT MUTAGEN 343..348
FT /note="CAHLQS->GADLQG: Nuclear and cytoplasmic location."
FT /evidence="ECO:0000269|PubMed:14596924"
FT MUTAGEN 343
FT /note="C->S: Loss of promotion of IRF1 sumoylation, as well
FT as of autosumoylation; partial loss of suppression of IRF1
FT transcriptional activity."
FT /evidence="ECO:0000269|PubMed:12387893"
SQ SEQUENCE 628 AA; 68318 MW; 2827F52715F0E549 CRC64;
MAELGELKHM VMSFRVSELQ VLLGFAGRNK SGRKHELLAK ALHLLKSSCA PSVQMKIKEL
YRRRFPRKTL GPSDLSLLSL PPGTSPVGSP GPLAPIPPTL LTPGTLLGPK REVDMHPPLP
QPVHPDVTMK PLPFYEVYGE LIRPTTLAST SSQRFEEAHF TFALTPQQLQ QILTSREVLP
GAKCDYTIQV QLRFCLCETS CPQEDYFPPN LFVKVNGKLC PLPGYLPPTK NGAEPKRPSR
PINITPLARL SATVPNTIVV NWSSEFGRNY SLSVYLVRQL TAGTLLQKLR AKGIRNPDHS
RALIKEKLTA DPDSEVATTS LRVSLMCPLG KMRLTVPCRA LTCAHLQSFD AALYLQMNEK
KPTWTCPVCD KKAPYESLII DGLFMEILNS CSDCDEIQFM EDGSWCPMKP KKEASEVCPP
PGYGLDGLQY SAVQEGIQPE SKKRVEVIDL TIESSSDEED LPPTKKHCPV TSAAIPALPG
SKGALTSGHQ PSSVLRSPAM GTLGSDFLSS LPLHEYPPAF PLGADIQGLD LFSFLQTESQ
HYGPSVITSL DEQDTLGHFF QYRGTPSHFL GPLAPTLGSS HRSSTPAPPP GRVSSIVAPG
SSLREGHGGP LPSGPSLTGC RSDVISLD
