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E3 SUMO-protein ligase PIAS4 (EC 2.3.2.27) (PIASy) (Protein inhibitor of activated STAT protein 4) (Protein inhibitor of activated STAT protein gamma) (PIAS-gamma) (RING-type E3 ubiquitin transferase PIAS4)

 PIAS4_MOUSE             Reviewed;         507 AA.
Q9JM05; Q8R165;
19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 2.
22-NOV-2017, entry version 153.
RecName: Full=E3 SUMO-protein ligase PIAS4;
EC=2.3.2.27;
AltName: Full=PIASy;
AltName: Full=Protein inhibitor of activated STAT protein 4;
AltName: Full=Protein inhibitor of activated STAT protein gamma;
Short=PIAS-gamma;
AltName: Full=RING-type E3 ubiquitin transferase PIAS4 {ECO:0000305};
Name=Pias4; Synonyms=Piasg;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:AAF72040.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
TISSUE=Brain;
PubMed=10854042; DOI=10.1385/JMN:14:1-2:107;
Sturm S., Koch M., White F.A.;
"Cloning and analysis of a murine Pias family member, Pias-gamma, in
developing skin and neurons.";
J. Mol. Neurosci. 14:107-121(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
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] {ECO:0000305}
INTERACTION WITH LEF1, DNA-BINDING, SUMOYLATION, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF CYS-330; CYS-335; HIS-337; CYS-340 AND
470-SER--SER-474.
PubMed=11731474; DOI=10.1101/gad.944801;
Sachdev S., Bruhn L., Sieber H., Pichler A., Melchior F.,
Grosschedl R.;
"PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1
activity by sequestration into nuclear bodies.";
Genes Dev. 15:3088-3103(2001).
[4]
TISSUE SPECIFICITY.
PubMed=12750312; DOI=10.1161/01.RES.0000076893.70898.36;
Chun T.-H., Itoh H., Subramanian L., Iniguez-Lluhi J.A., Nakao K.;
"Modification of GATA-2 transcriptional activity in endothelial cells
by the SUMO E3 ligase PIASy.";
Circ. Res. 92:1201-1208(2003).
[5]
SUBCELLULAR LOCATION, INTERACTION WITH TRIM32, AND UBIQUITINATION.
PubMed=16816390; DOI=10.1074/jbc.M601655200;
Albor A., El-Hizawi S., Horn E.J., Laederich M., Frosk P.,
Wrogemann K., Kulesz-Martin M.;
"The interaction of Piasy with Trim32, an E3-ubiquitin ligase mutated
in limb-girdle muscular dystrophy type 2H, promotes Piasy degradation
and regulates UVB-induced keratinocyte apoptosis through NFkappaB.";
J. Biol. Chem. 281:25850-25866(2006).
[6]
INTERACTION WITH MOMLV CA.
PubMed=16352559; DOI=10.1128/JVI.80.1.342-352.2006;
Yueh A., Leung J., Bhattacharyya S., Perrone L.A., de los Santos K.,
Pu S.-Y., Goff S.P.;
"Interaction of moloney murine leukemia virus capsid with Ubc9 and
PIASy mediates SUMO-1 addition required early in infection.";
J. Virol. 80:342-352(2006).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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: Functions as an E3-type small ubiquitin-like modifier
(SUMO) ligase, stabilizing the interaction between UBE2I and the
substrate, and as a SUMO-tethering factor. Plays a crucial role as
a transcriptional coregulation in various cellular pathways,
including the STAT pathway, the p53/TP53 pathway, the Wnt pathway
and the steroid hormone signaling pathway. Involved in gene
silencing. Mediates sumoylation of CEBPA, PARK7, HERC2, MYB, TCF4
and RNF168. In Wnt signaling, represses LEF1 and enhances TCF4
transcriptional activities through promoting their sumoylations.
Enhances the sumoylation of MTA1 and may participate in its
paralog-selective sumoylation (By similarity). {ECO:0000250}.
-!- 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 sumoylation.
-!- SUBUNIT: Interacts with AR, AXIN1, GATA2, LEF1, TP53 and STAT1,
after treatment with IFNG. Binds to AT-rich DNA sequences, known
as matrix or scaffold attachment regions (MARs/SARs) (By
similarity). Interacts with TICAM1 (By similarity). Interacts with
Moloney murine leukemia virus CA. Interacts with KLF8; the
interaction results in SUMO ligation and repression of KLF8
transcriptional activity and of its cell cycle progression into
G(1) phase. Interacts with MTA1 (By similarity). Interacts with
TRIM32 upon treatment with UVB and TNF-alpha. {ECO:0000250,
ECO:0000269|PubMed:11731474, ECO:0000269|PubMed:16352559,
ECO:0000269|PubMed:16816390}.
-!- SUBCELLULAR LOCATION: Nucleus, PML body
{ECO:0000269|PubMed:11731474, ECO:0000269|PubMed:16816390}.
Note=Colocalizes with SUMO1 and TCF7L2/TCF4 and LEF1 in a subset
of PML (promyelocytic leukemia) nuclear bodies. Accumulates in the
cytoplasm upon treatment with UVB and TNF-alpha.
-!- TISSUE SPECIFICITY: Widely expressed, with highest levels in
testis. Also expressed in vascular endothelial cells, in primary
keratinocytes and in the CNS, including cortex, olfactory bulb,
spinal cord, thalamus and trigeminal ganglion. Low expression, if
any, in liver and lung. {ECO:0000269|PubMed:10854042,
ECO:0000269|PubMed:12750312}.
-!- DEVELOPMENTAL STAGE: At 8.5 dpc, expressed primarily in the
anterior part of the neural tube. At 10.5 dpc, expressed in the
neuroepithelium of the forebrain and hindbrain. At 11.5 dpc,
detected in the neural tube, eye, limb buds and brachial arches.
At 12.5 dpc, expressed in the hindlimbs and forelimbs, as well as
in the forebrain. At 12.5 and 13.5 dpc, detected in single cells
in the marginal zone of the developing cortex, as well as in other
developing tissues and organs. At 13.5 dpc, expressed in the
developing limb buds, in single cells in the mesenchyme
surrounding future digit structures. At 15.5 dpc, detected in the
inner root sheath of vibrissa hair follicle. Expression in the
inner root sheath of the hair follicle continues later in life as
it can also be detected in the back skin of newborn at postnatal
day 3. At 16.5 dpc, expressed in the epithelium of olfactory and
in the retina. {ECO:0000269|PubMed:10854042}.
-!- DOMAIN: The LXXLL motif is a coregulator signature that is
essential for transcriptional corepression.
-!- PTM: Sumoylated. Lys-35 is the main site of sumoylation.
Sumoylation is required for TCF4 sumoylation and transcriptional
activation. Represses LEF1 transcriptional activity. SUMO1 is the
preferred conjugate. {ECO:0000269|PubMed:11731474}.
-!- PTM: Ubiquitinated by TRIM32 upon treatment with UVB and TNF-
alpha. {ECO:0000269|PubMed:16816390}.
-!- SIMILARITY: Belongs to the PIAS family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF109174; AAF72040.1; -; mRNA.
EMBL; BC025159; AAH25159.1; -; mRNA.
CCDS; CCDS35992.1; -.
RefSeq; NP_067476.2; NM_021501.4.
UniGene; Mm.34428; -.
ProteinModelPortal; Q9JM05; -.
SMR; Q9JM05; -.
BioGrid; 208475; 7.
DIP; DIP-60971N; -.
IntAct; Q9JM05; 2.
STRING; 10090.ENSMUSP00000005064; -.
iPTMnet; Q9JM05; -.
PhosphoSitePlus; Q9JM05; -.
EPD; Q9JM05; -.
MaxQB; Q9JM05; -.
PaxDb; Q9JM05; -.
PRIDE; Q9JM05; -.
Ensembl; ENSMUST00000005064; ENSMUSP00000005064; ENSMUSG00000004934.
GeneID; 59004; -.
KEGG; mmu:59004; -.
UCSC; uc007ggc.3; mouse.
CTD; 51588; -.
MGI; MGI:2136940; Pias4.
eggNOG; KOG2169; Eukaryota.
eggNOG; ENOG410XQ2E; LUCA.
GeneTree; ENSGT00550000074410; -.
HOGENOM; HOG000230594; -.
HOVERGEN; HBG053598; -.
InParanoid; Q9JM05; -.
KO; K16065; -.
OMA; LRICYTD; -.
OrthoDB; EOG091G08G5; -.
PhylomeDB; Q9JM05; -.
TreeFam; TF323787; -.
Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-MMU-3232118; SUMOylation of transcription factors.
Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
UniPathway; UPA00886; -.
PRO; PR:Q9JM05; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000004934; -.
CleanEx; MM_PIAS4; -.
ExpressionAtlas; Q9JM05; baseline and differential.
Genevisible; Q9JM05; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0016363; C:nuclear matrix; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:1990234; C:transferase complex; IDA:BHF-UCL.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0061665; F:SUMO ligase activity; IDA:BHF-UCL.
GO; GO:0019789; F:SUMO transferase activity; IDA:MGI.
GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
GO; GO:0007259; P:JAK-STAT cascade; ISA:MGI.
GO; GO:0007275; P:multicellular organism development; NAS:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IMP:MGI.
GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI.
GO; GO:1902174; P:positive regulation of keratinocyte apoptotic process; IDA:BHF-UCL.
GO; GO:0033235; P:positive regulation of protein sumoylation; ISS:UniProtKB.
GO; GO:0016925; P:protein sumoylation; IDA:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
Gene3D; 1.10.720.30; -; 1.
InterPro; IPR027224; PIAS4.
InterPro; IPR023321; PINIT.
InterPro; IPR003034; SAP_dom.
InterPro; IPR036361; SAP_dom_sf.
InterPro; IPR004181; Znf_MIZ.
PANTHER; PTHR10782:SF9; PTHR10782:SF9; 1.
Pfam; PF14324; PINIT; 1.
Pfam; PF02891; zf-MIZ; 1.
SMART; SM00513; SAP; 1.
SUPFAM; SSF68906; SSF68906; 1.
PROSITE; PS51466; PINIT; 1.
PROSITE; PS50800; SAP; 1.
PROSITE; PS51044; ZF_SP_RING; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; DNA-binding; Host-virus interaction;
Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
Repressor; Transcription; Transcription regulation; Transferase;
Ubl conjugation; Ubl conjugation pathway; Wnt signaling pathway; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q8N2W9}.
CHAIN 2 507 E3 SUMO-protein ligase PIAS4.
/FTId=PRO_0000218983.
DOMAIN 12 46 SAP. {ECO:0000255|PROSITE-
ProRule:PRU00186, ECO:0000305}.
DOMAIN 112 272 PINIT. {ECO:0000255|PROSITE-
ProRule:PRU00799}.
ZN_FING 304 381 SP-RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00452}.
MOTIF 20 24 LXXLL motif.
COMPBIAS 462 488 Asp/Glu-rich (acidic).
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q8N2W9}.
MOD_RES 107 107 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8N2W9}.
CROSSLNK 9 9 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q8N2W9}.
CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q8N2W9}.
CROSSLNK 56 56 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q8N2W9}.
CROSSLNK 59 59 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q8N2W9}.
CROSSLNK 68 68 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q8N2W9}.
CROSSLNK 69 69 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q8N2W9}.
CROSSLNK 118 118 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q8N2W9}.
CROSSLNK 128 128 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
MUTAGEN 330 330 C->S: Abrogates sumoylation of LEF1 and
increases LEF1-mediated transcriptional
activity; when associated with S-335; A-
337 and S-340.
{ECO:0000269|PubMed:11731474}.
MUTAGEN 335 335 C->S: Abrogates sumoylation of LEF1 and
increases LEF1-mediated transcriptional
activity; when associated with S-330; A-
337 and S-340.
{ECO:0000269|PubMed:11731474}.
MUTAGEN 337 337 H->A: Abrogates sumoylation of LEF1 and
increases LEF1-mediated transcriptional
activity; when associated with S-330; S-
335 and S-340.
{ECO:0000269|PubMed:11731474}.
MUTAGEN 340 340 C->S: Abrogates sumoylation of LEF1 and
increases LEF1-mediated transcriptional
activity; when associated with S-330; S-
335 and A-337.
{ECO:0000269|PubMed:11731474}.
MUTAGEN 470 474 SSSSS->AAAAA: No effect on sumoylation of
LEF1, nor on LEF1-binding.
{ECO:0000269|PubMed:11731474}.
CONFLICT 230 230 K -> N (in Ref. 1; AAF72040).
{ECO:0000305}.
CONFLICT 417 417 L -> H (in Ref. 1; AAF72040).
{ECO:0000305}.
CONFLICT 494 494 K -> N (in Ref. 1; AAF72040).
{ECO:0000305}.
SEQUENCE 507 AA; 55570 MW; A8E5E6E3BAC76426 CRC64;
MAAELVEAKN MVMSFRVSDL QMLLGFVGRS KSGLKHELVT RALQLVQFDC SPELFKKIKE
LYETRYAKKS AEPGPQAPRP LDPLALHSMP RTPLSGPTVD YPVLYGKYLN GLGRLPTKTL
KPEVRLVKLP FFNMLDELLK PTELVPQSAE KLQESPCIFA LTPRQVEMIR NSRELQPGVK
AVQVVLRICY SDTSCPQEDQ YPPNIAVKVN HSYCSVPGYY PSNKPGVEPK RPCRPINLTH
LMYLSSATNR ITVTWGNYGK SYSVALYLVR QLTSSDLLQR LKTIGVKHPE LCKALVKEKL
RLDPDSEIAT TGVRVSLICP LVKMRLSVPC RAETCAHLQC FDAVFYLQMN EKKPTWMCPV
CDKPAAYDQL IIDGLLSKIL SECEGADEIE FLAEGSWRPI RAEKEPSCSP QGPILVLGTS
DANGLAPASS TPGIGSGLSG PGSAGSGAGA AGSLENGKTG ADVVDLTLDS SSSSEDEDED
EDDDEDEDEG PRPKRRCPFQ KGLVPAC


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