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PIAS4

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

PIAS4

Identifiers

Aliases

PIAS4, PIASY, Piasg, ZMIZ6, PIAS-gamma, protein inhibitor of activated STAT 4

External IDs

OMIM:605989;MGI:2136940;HomoloGene:104136;GeneCards:PIAS4;OMA:PIAS4 - orthologs

Gene location (Human)

Chr.	Chromosome 19 (human)^[1]

Band	19p13.3	Start	4,007,736bp^[1]
Band	19p13.3	End	4,039,386bp^[1]

Gene location (Mouse)

Chr.	Chromosome 10 (mouse)^[2]

Band	10\|10 C1	Start	80,989,100bp^[2]
Band	10\|10 C1	End	81,003,757bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

left testis

right testis

right hemisphere of cerebellum

stromal cell of endometrium

oocyte

sural nerve

islet of Langerhans

muscle of thigh

muscle layer of sigmoid colon

monocyte

Top expressed in

seminiferous tubule

internal carotid artery

spermatid

external carotid artery

tibiofemoral joint

primary oocyte

crypt of lieberkuhn of small intestine

secondary oocyte

granulocyte

zygote

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	DNA binding transcription corepressor activity zinc ion binding metal ion binding SUMO ligase activity protein binding ubiquitin protein ligase binding SUMO transferase activity transferase activity protein C-terminus binding
Cellular component	cytoplasm PML body nuclear matrix transferase complex nucleus nucleoplasm
Biological process	regulation of transcription, DNA-templated positive regulation of keratinocyte apoptotic process negative regulation of tumor necrosis factor-mediated signaling pathway negative regulation of transcription by RNA polymerase II Wnt signaling pathway positive regulation of protein sumoylation protein sumoylation transcription, DNA-templated positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage negative regulation of transcription, DNA-templated double-strand break repair via nonhomologous end joining negative regulation of NF-kappaB transcription factor activity vitamin D metabolic process
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


51588


59004

Ensembl


ENSG00000105229


ENSMUSG00000004934

UniProt


Q8N2W9


Q9JM05

RefSeq (mRNA)


NM_015897 NM_016149


NM_021501

RefSeq (protein)


NP_056981


NP_067476

Location (UCSC)

Chr 19: 4.01 – 4.04 Mb

Chr 10: 80.99 – 81 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

E3 SUMO-protein ligase PIAS4 is one of severalprotein inhibitor of activated STAT (PIAS) proteins. It is also known as aprotein inhibitor of activated STAT protein gamma (PIASg or PIASy), and is anenzyme that in humans is encoded by thePIAS4gene.^[5]^[6]

Interactions

[edit]

PIAS4 has been shown tointeract withMothers against decapentaplegic homolog 6,^[7]Mothers against decapentaplegic homolog 7^[7] andLymphoid enhancer-binding factor 1.^[8] PIAS4 has been shown to be responsible for the SUMOylation of inhibitedWerner syndrome helicase (WRN) trapped on DNA in microsatellite unstable cancer cells.^[9]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000105229 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000004934 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^Liu B, Liao J, Rao X, Kushner SA, Chung CD, Chang DD, Shuai K (Sep 1998)."Inhibition of Stat1-mediated gene activation by PIAS1".Proc Natl Acad Sci U S A.95 (18):10626–31.Bibcode:1998PNAS...9510626L.doi:10.1073/pnas.95.18.10626.PMC 27945.PMID 9724754.
^"Entrez Gene: PIAS4 Protein inhibitor of activated STAT, 4".
^^a ^bImoto, Seiyu; Sugiyama Kenji; Muromoto Ryuta; Sato Noriko; Yamamoto Tetsuya; Matsuda Tadashi (Sep 2003)."Regulation of transforming growth factor-beta signaling by protein inhibitor of activated STAT, PIASy through Smad3".J. Biol. Chem.278 (36):34253–8.doi:10.1074/jbc.M304961200.hdl:2115/28123.ISSN 0021-9258.PMID 12815042.
^Sachdev, S; Bruhn L; Sieber H; Pichler A; Melchior F; Grosschedl R (Dec 2001)."PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies".Genes Dev.15 (23):3088–103.doi:10.1101/gad.944801.ISSN 0890-9369.PMC 312834.PMID 11731474.
^Rodríguez Pérez F, Natwick D, Schiff L, McSwiggen D, Heckert A, Huey M, Morrison H, Loo M, Miranda RG, Filbin J, Ortega J, Van Buren K, Murnock D, Tao A, Butler R, Cheng K, Tarvestad W, Zhang Z, Gonzalez E, Miller RM, Kelly M, Tang Y, Ho J, Anderson D, Bashore C, Basham S (July 2024)."WRN inhibition leads to its chromatin-associated degradation via the PIAS4-RNF4-p97/VCP axis".Nat. Commun.15 (6059) 6059.Bibcode:2024NatCo..15.6059R.doi:10.1038/s41467-024-50178-3.PMC 11258360.PMID 39025847.

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides".Gene.138 (1–2):171–4.doi:10.1016/0378-1119(94)90802-8.PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library".Gene.200 (1–2):149–56.doi:10.1016/S0378-1119(97)00411-3.PMID 9373149.
Liu B, Gross M, ten Hoeve J, Shuai K (2001)."A transcriptional corepressor of Stat1 with an essential LXXLL signature motif".Proc. Natl. Acad. Sci. U.S.A.98 (6):3203–7.Bibcode:2001PNAS...98.3203L.doi:10.1073/pnas.051489598.PMC 30631.PMID 11248056.
Nelson V, Davis GE, Maxwell SA (2001). "A putative protein inhibitor of activated STAT (PIASy) interacts with p53 and inhibits p53-mediated transactivation but not apoptosis".Apoptosis.6 (3):221–34.doi:10.1023/A:1011392811628.PMID 11388671.S2CID 13435653.
Gross M, Liu B, Tan J, et al. (2001)."Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells".Oncogene.20 (29):3880–7.doi:10.1038/sj.onc.1204489.PMID 11439351.
Sachdev S, Bruhn L, Sieber H, et al. (2001)."PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies".Genes Dev.15 (23):3088–103.doi:10.1101/gad.944801.PMC 312834.PMID 11731474.
Ohmine K, Ota J, Ueda M, et al. (2002)."Characterization of stage progression in chronic myeloid leukemia by DNA microarray with purified hematopoietic stem cells".Oncogene.20 (57):8249–57.doi:10.1038/sj.onc.1205029.PMID 11781839.
Tan JA, Hall SH, Hamil KG, et al. (2002)."Protein inhibitors of activated STAT resemble scaffold attachment factors and function as interacting nuclear receptor coregulators".J. Biol. Chem.277 (19):16993–7001.doi:10.1074/jbc.M109217200.PMID 11877418.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003)."Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences".Proc. Natl. Acad. Sci. U.S.A.99 (26):16899–903.Bibcode:2002PNAS...9916899M.doi:10.1073/pnas.242603899.PMC 139241.PMID 12477932.
Subramanian L, Benson MD, Iñiguez-Lluhí JA (2003)."A synergy control motif within the attenuator domain of CCAAT/enhancer-binding protein alpha inhibits transcriptional synergy through its PIASy-enhanced modification by SUMO-1 or SUMO-3".J. Biol. Chem.278 (11):9134–41.doi:10.1074/jbc.M210440200.PMID 12511558.
Dahle Ø, Andersen TØ, Nordgård O, et al. (2003)."Transactivation properties of c-Myb are critically dependent on two SUMO-1 acceptor sites that are conjugated in a PIASy enhanced manner".Eur. J. Biochem.270 (6):1338–48.doi:10.1046/j.1432-1033.2003.03504.x.PMID 12631292.
Yamamoto H, Ihara M, Matsuura Y, Kikuchi A (2003)."Sumoylation is involved in beta-catenin-dependent activation of Tcf-4".EMBO J.22 (9):2047–59.doi:10.1093/emboj/cdg204.PMC 156076.PMID 12727872.
Lee PS, Chang C, Liu D, Derynck R (2003)."Sumoylation of Smad4, the common Smad mediator of transforming growth factor-beta family signaling".J. Biol. Chem.278 (30):27853–63.doi:10.1074/jbc.M301755200.PMID 12740389.
Chun TH, Itoh H, Subramanian L, et al. (2003)."Modification of GATA-2 transcriptional activity in endothelial cells by the SUMO E3 ligase PIASy".Circ. Res.92 (11):1201–8.doi:10.1161/01.RES.0000076893.70898.36.PMID 12750312.
Imoto S, Sugiyama K, Muromoto R, et al. (2003)."Regulation of transforming growth factor-beta signaling by protein inhibitor of activated STAT, PIASy through Smad3".J. Biol. Chem.278 (36):34253–8.doi:10.1074/jbc.M304961200.hdl:2115/28123.PMID 12815042.
Galleguillos D, Vecchiola A, Fuentealba JA, et al. (2004)."PIASgamma represses the transcriptional activation induced by the nuclear receptor Nurr1".J. Biol. Chem.279 (3):2005–11.doi:10.1074/jbc.M308113200.hdl:10533/175295.PMID 14559918.
Gross M, Yang R, Top I, et al. (2004)."PIASy-mediated repression of the androgen receptor is independent of sumoylation".Oncogene.23 (17):3059–66.doi:10.1038/sj.onc.1207443.PMID 14981544.
Zoumpoulidou G, Jones MC, Fernandez de Mattos S, et al. (2005)."Convergence of interferon-gamma and progesterone signaling pathways in human endometrium: role of PIASy (protein inhibitor of activated signal transducer and activator of transcription-y)".Mol. Endocrinol.18 (8):1988–99.doi:10.1210/me.2003-0467.PMID 15155784.
Imoto S, Sugiyama K, Yamamoto T, Matsuda T (2004). "The RING domain of PIASy is involved in the suppression of bone morphogenetic protein-signaling pathway".Biochem. Biophys. Res. Commun.319 (1):275–82.Bibcode:2004BBRC..319..275I.doi:10.1016/j.bbrc.2004.04.161.hdl:2115/28116.PMID 15158472.

JAK-STAT signaling pathway

Ligand

Cytokine

Cytokine receptor

Janus kinase

Adaptor proteins

STAT	STAT1 STAT2 STAT3 STAT4 STAT5 STAT6
PIAS	PIAS1 PIAS2 PIAS3 PIAS4
SOCS	1 2 3 4 5 6 7 CISH
IRF	IRF1 IRF2 IRF3 IRF4 IRF5 IRF6 IRF7 IRF8

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