PIAS1 | ENSG00000033800 | NCBI 8554

Details for: PIAS1

Gene ID: 8554

Symbol: PIAS1

Ensembl ID: ENSG00000033800

Description: protein inhibitor of activated STAT 1

Associated with

Cytokine signaling in immune system
(R-HSA-1280215)
Dna repair
(R-HSA-73894)
Formation of incision complex in gg-ner
(R-HSA-5696395)
Global genome nucleotide excision repair (gg-ner)
(R-HSA-5696399)
Immune system
(R-HSA-168256)
Interferon gamma signaling
(R-HSA-877300)
Interferon signaling
(R-HSA-913531)
Metabolism of proteins
(R-HSA-392499)
Nucleotide excision repair
(R-HSA-5696398)
Post-translational protein modification
(R-HSA-597592)
Regulation of ifng signaling
(R-HSA-877312)
Sumo e3 ligases sumoylate target proteins
(R-HSA-3108232)
Sumoylation
(R-HSA-2990846)
Sumoylation of chromatin organization proteins
(R-HSA-4551638)
Sumoylation of dna damage response and repair proteins
(R-HSA-3108214)
Sumoylation of intracellular receptors
(R-HSA-4090294)
Sumoylation of transcription cofactors
(R-HSA-3899300)
Sumoylation of transcription factors
(R-HSA-3232118)
Sumoylation of ubiquitinylation proteins
(R-HSA-3232142)
Cell surface receptor signaling pathway via jak-stat
(GO:0007259)
Chromatin
(GO:0000785)
Cytoskeleton
(GO:0005856)
Dna-binding transcription factor binding
(GO:0140297)
Dna damage response
(GO:0006974)
Enzyme binding
(GO:0019899)
Fat cell differentiation
(GO:0045444)
G1/s transition of mitotic cell cycle
(GO:0000082)
Glutamatergic synapse
(GO:0098978)
Negative regulation of apoptotic process
(GO:0043066)
Negative regulation of transcription by rna polymerase ii
(GO:0000122)
Nuclear periphery
(GO:0034399)
Nuclear speck
(GO:0016607)
Nucleoplasm
(GO:0005654)
Nucleus
(GO:0005634)
Pml body
(GO:0016605)
Positive regulation of dna-templated transcription
(GO:0045893)
Positive regulation of proteasomal ubiquitin-dependent protein catabolic process
(GO:0032436)
Positive regulation of protein localization to cell periphery
(GO:1904377)
Positive regulation of protein sumoylation
(GO:0033235)
Positive regulation of smooth muscle cell differentiation
(GO:0051152)
Postsynaptic cytosol
(GO:0099524)
Presynaptic cytosol
(GO:0099523)
Protein-dna complex assembly
(GO:0065004)
Protein binding
(GO:0005515)
Protein domain specific binding
(GO:0019904)
Protein sumoylation
(GO:0016925)
Regulation of cell population proliferation
(GO:0042127)
Regulation of transcription by rna polymerase ii
(GO:0006357)
Spermatogenesis
(GO:0007283)
Sumo ligase activity
(GO:0061665)
Sumo transferase activity
(GO:0019789)
Transcription cis-regulatory region binding
(GO:0000976)
Transcription coregulator activity
(GO:0003712)
Transcription corepressor activity
(GO:0003714)
Ubiquitin protein ligase binding
(GO:0031625)
Visual learning
(GO:0008542)
Zinc ion binding
(GO:0008270)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 505.7050
Cell Significance Index: -78.6600
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 305.4485
Cell Significance Index: -77.4800
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 205.6572
Cell Significance Index: -84.7200
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 172.7252
Cell Significance Index: -81.5500
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 165.2340
Cell Significance Index: -67.1300
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 146.8160
Cell Significance Index: -75.5200
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 70.4954
Cell Significance Index: -67.3100
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 66.3122
Cell Significance Index: -81.7600
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 27.2541
Cell Significance Index: -73.0100
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 26.0762
Cell Significance Index: -57.0700
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 25.0240
Cell Significance Index: -76.8600
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 20.9488
Cell Significance Index: -82.6700
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 4.4644
Cell Significance Index: 250.5200
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 2.6174
Cell Significance Index: 525.0600
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 2.5296
Cell Significance Index: 194.1200
Cell Name: leptomeningeal cell (CL0000708)
Fold Change: 2.4634
Cell Significance Index: 52.6600
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 2.4618
Cell Significance Index: 68.8000
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: 2.3163
Cell Significance Index: 59.5400
Cell Name: neoplastic cell (CL0001063)
Fold Change: 2.2081
Cell Significance Index: 438.2100
Cell Name: skeletal muscle fibroblast (CL0011027)
Fold Change: 2.1105
Cell Significance Index: 14.3000
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 2.0472
Cell Significance Index: 734.3000
Cell Name: preadipocyte (CL0002334)
Fold Change: 1.9455
Cell Significance Index: 37.9700
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: 1.6512
Cell Significance Index: 111.0300
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 1.2444
Cell Significance Index: 860.6600
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: 1.2166
Cell Significance Index: 74.7800
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: 1.1076
Cell Significance Index: 48.9900
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 1.1027
Cell Significance Index: 1697.6500
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: 1.0800
Cell Significance Index: 40.9000
Cell Name: anterior lens cell (CL0002223)
Fold Change: 1.0520
Cell Significance Index: 1940.2100
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 1.0189
Cell Significance Index: 110.8200
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.7790
Cell Significance Index: 95.7900
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.7264
Cell Significance Index: 130.9500
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.6929
Cell Significance Index: 1304.6400
Cell Name: basal epithelial cell of prostatic duct (CL0002236)
Fold Change: 0.5982
Cell Significance Index: 5.3100
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 0.5694
Cell Significance Index: 258.4200
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.5511
Cell Significance Index: 75.6900
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 0.5452
Cell Significance Index: 346.2300
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.4744
Cell Significance Index: 55.9500
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 0.4636
Cell Significance Index: 12.3800
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.4169
Cell Significance Index: 227.7100
Cell Name: cortical interneuron (CL0008031)
Fold Change: 0.4134
Cell Significance Index: 9.9100
Cell Name: hippocampal pyramidal neuron (CL1001571)
Fold Change: 0.4075
Cell Significance Index: 11.6300
Cell Name: retinal rod cell (CL0000604)
Fold Change: 0.3750
Cell Significance Index: 4.4700
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.3508
Cell Significance Index: 155.0900
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: 0.3122
Cell Significance Index: 5.3500
Cell Name: early pro-B cell (CL0002046)
Fold Change: 0.2671
Cell Significance Index: 17.2400
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.2174
Cell Significance Index: 41.3700
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.2155
Cell Significance Index: 194.6100
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 0.2010
Cell Significance Index: 273.2800
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.1059
Cell Significance Index: 4.8000
Cell Name: cardiac muscle cell (CL0000746)
Fold Change: 0.1014
Cell Significance Index: 1.5000
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: 0.0441
Cell Significance Index: 2.7800
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 0.0419
Cell Significance Index: 2.2000
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.0078
Cell Significance Index: 0.1700
Cell Name: fibroblast of cardiac tissue (CL0002548)
Fold Change: 0.0021
Cell Significance Index: 0.0300
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.0199
Cell Significance Index: -2.0700
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0698
Cell Significance Index: -51.1600
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0811
Cell Significance Index: -60.0600
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0862
Cell Significance Index: -65.2400
Cell Name: odontoblast (CL0000060)
Fold Change: -0.1093
Cell Significance Index: -14.0100
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.1336
Cell Significance Index: -75.3500
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.1412
Cell Significance Index: -14.4300
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.1494
Cell Significance Index: -93.3100
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: -0.1790
Cell Significance Index: -30.5700
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: -0.1952
Cell Significance Index: -13.5000
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: -0.2005
Cell Significance Index: -7.0400
Cell Name: colon goblet cell (CL0009039)
Fold Change: -0.2129
Cell Significance Index: -21.0600
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.2261
Cell Significance Index: -32.8700
Cell Name: lung endothelial cell (CL1001567)
Fold Change: -0.2437
Cell Significance Index: -12.7000
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.2487
Cell Significance Index: -71.5600
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: -0.2597
Cell Significance Index: -7.0700
Cell Name: lactocyte (CL0002325)
Fold Change: -0.2771
Cell Significance Index: -35.8000
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: -0.3843
Cell Significance Index: -18.0600
Cell Name: cardiac endothelial cell (CL0010008)
Fold Change: -0.3908
Cell Significance Index: -5.6200
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.4088
Cell Significance Index: -86.1000
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: -0.4142
Cell Significance Index: -67.3700
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.4303
Cell Significance Index: -32.0700
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: -0.4399
Cell Significance Index: -20.5100
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.4723
Cell Significance Index: -55.0400
Cell Name: type I muscle cell (CL0002211)
Fold Change: -0.4836
Cell Significance Index: -11.8000
Cell Name: sebum secreting cell (CL0000317)
Fold Change: -0.5683
Cell Significance Index: -40.1900
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.5716
Cell Significance Index: -65.4900
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -0.5848
Cell Significance Index: -15.6700
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.6841
Cell Significance Index: -21.9100
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: -0.8370
Cell Significance Index: -29.0900
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: -0.8424
Cell Significance Index: -24.2700
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: -0.8636
Cell Significance Index: -44.8600
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.8689
Cell Significance Index: -68.8200
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.8809
Cell Significance Index: -18.7600
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: -1.0001
Cell Significance Index: -25.0000
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -1.1458
Cell Significance Index: -70.2500
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -1.1636
Cell Significance Index: -7.0300
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: -1.2141
Cell Significance Index: -22.4400
Cell Name: kidney capillary endothelial cell (CL1000892)
Fold Change: -1.2445
Cell Significance Index: -12.8900
Cell Name: centrilobular region hepatocyte (CL0019029)
Fold Change: -1.3939
Cell Significance Index: -23.4800
Cell Name: Purkinje cell (CL0000121)
Fold Change: -1.4244
Cell Significance Index: -31.1900
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -1.4358
Cell Significance Index: -19.5900
Cell Name: periportal region hepatocyte (CL0019026)
Fold Change: -1.4621
Cell Significance Index: -21.5800
Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
Fold Change: -1.4698
Cell Significance Index: -46.8100
Cell Name: L6b glutamatergic cortical neuron (CL4023038)
Fold Change: -1.4777
Cell Significance Index: -48.3800

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics:** 1. **E3 SUMO-protein ligase activity**: PIAS1 possesses E3 SUMO-protein ligase activity, which enables it to catalyze the transfer of sumoylation units to target proteins. 2. **Specificity for STAT1**: PIAS1 is specifically involved in the regulation of STAT1, which is a critical transcription factor in the interferon signaling pathway. 3. **Inhibition of STAT1 activation**: PIAS1 inhibits the activation of STAT1, which modulates the immune response and prevents excessive inflammation. 4. **Regulation of various cellular processes**: PIAS1 is involved in the regulation of cell proliferation, differentiation, and survival, as well as the formation of incision complexes in GG-NER (Global Genome Nucleotide Excision Repair) and G1/S transition of the mitotic cell cycle. **Pathways and Functions:** 1. **Cytokine signaling in the immune system**: PIAS1 regulates the interferon signaling pathway by inhibiting the activation of STAT1, which is a key transcription factor in this pathway. 2. **DNA repair**: PIAS1 is involved in the regulation of GG-NER and G1/S transition of the mitotic cell cycle, which are critical processes in DNA repair and cell cycle regulation. 3. **Cell proliferation and differentiation**: PIAS1 regulates cell proliferation and differentiation by modulating the activity of transcription factors and signaling pathways. 4. **Apoptosis and transcriptional regulation**: PIAS1 regulates apoptosis and transcriptional regulation by modulating the activity of transcription factors and signaling pathways. **Clinical Significance:** 1. **Immunological disorders**: PIAS1 dysregulation has been implicated in various immunological disorders, including autoimmune diseases and cancer. 2. **Cancer**: PIAS1 has been shown to be overexpressed in certain types of cancer, including lung and colon cancer, and is associated with poor prognosis. 3. **Neurological disorders**: PIAS1 has been implicated in the regulation of neuroinflammation and is associated with various neurological disorders, including multiple sclerosis and Alzheimer's disease. 4. **Gene therapy**: PIAS1 has been identified as a potential target for gene therapy in the treatment of immunological disorders and cancer. In conclusion, PIAS1 is a critical regulator of the immune response and various cellular processes, and its dysregulation has been implicated in various immunological disorders and cancers. Further research is needed to fully understand the role of PIAS1 in regulating immune response and cellular processes, and to explore its potential as a therapeutic target.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

E3 SUMO-protein ligase PIAS1

Genular Protein ID: 1855041927

Symbol: PIAS1_HUMAN

Name: E3 SUMO-protein ligase PIAS1

UniProtKB Accession Codes:

O75925 B2RB67 B3KSY9 C5J4B4 Q147X4 Q99751 Q9UN02

Database IDs:

Citations:

PubMed ID: 9724754

Title: Inhibition of Stat1-mediated gene activation by PIAS1.

PubMed ID: 9724754

DOI: 10.1073/pnas.95.18.10626

PubMed ID: 10628744

Title: Protein inhibitor of activated STAT-1 (signal transducer and activator of transcription-1) is a nuclear receptor coregulator expressed in human testis.

PubMed ID: 10628744

DOI: 10.1210/mend.14.1.0408

PubMed ID: 19906316

Title: Discovery of novel human transcript variants by analysis of intronic single-block EST with polyadenylation site.

PubMed ID: 19906316

DOI: 10.1186/1471-2164-10-518

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16572171

Title: Analysis of the DNA sequence and duplication history of human chromosome 15.

PubMed ID: 16572171

DOI: 10.1038/nature04601

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 9177271

Title: Cloning and characterization of Gu/RH-II binding protein.

PubMed ID: 9177271

DOI: 10.1006/bbrc.1997.6642

PubMed ID: 11672422

Title: LIM-domain protein cysteine- and glycine-rich protein 2 (CRP2) is a novel marker of hepatic stellate cells and binding partner of the protein inhibitor of activated STAT1.

PubMed ID: 11672422

DOI: 10.1042/0264-6021:3590485

PubMed ID: 11583632

Title: Involvement of PIAS1 in the sumoylation of tumor suppressor p53.

PubMed ID: 11583632

DOI: 10.1016/s1097-2765(01)00349-5

PubMed ID: 11439351

Title: Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells.

PubMed ID: 11439351

DOI: 10.1038/sj.onc.1204489

PubMed ID: 12223491

Title: SUMO-1 modification of the C-terminal KVEKVD of Axin is required for JNK activation but has no effect on Wnt signaling.

PubMed ID: 12223491

DOI: 10.1074/jbc.m208099200

PubMed ID: 12393906

Title: Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes.

PubMed ID: 12393906

DOI: 10.1074/jbc.m208319200

PubMed ID: 12356736

Title: Transcription factor Sp3 is silenced through SUMO modification by PIAS1.

PubMed ID: 12356736

DOI: 10.1093/emboj/cdf510

PubMed ID: 11867732

Title: Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity.

PubMed ID: 11867732

DOI: 10.1073/pnas.052559499

PubMed ID: 14701874

Title: SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin mu gene expression.

PubMed ID: 14701874

DOI: 10.1101/gad.1153003

PubMed ID: 14500712

Title: PIAS1-mediated sumoylation of focal adhesion kinase activates its autophosphorylation.

PubMed ID: 14500712

DOI: 10.1074/jbc.m308562200

PubMed ID: 15208321

Title: Repression of the transactivating capacity of the oncoprotein PLAG1 by SUMOylation.

PubMed ID: 15208321

DOI: 10.1074/jbc.m401753200

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16600910

Title: PIAS1 confers DNA-binding specificity on the Msx1 homeoprotein.

PubMed ID: 16600910

DOI: 10.1101/gad.1392006

PubMed ID: 16617055

Title: Sumoylation delimits KLF8 transcriptional activity associated with the cell cycle regulation.

PubMed ID: 16617055

DOI: 10.1074/jbc.m513135200

PubMed ID: 17540171

Title: Proinflammatory stimuli induce IKKalpha-mediated phosphorylation of PIAS1 to restrict inflammation and immunity.

PubMed ID: 17540171

DOI: 10.1016/j.cell.2007.03.056

PubMed ID: 17369852

Title: SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1.

PubMed ID: 17369852

DOI: 10.1038/sj.onc.1210387

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19136629

Title: PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling.

PubMed ID: 19136629

DOI: 10.1101/gad.489409

PubMed ID: 21724836

Title: Retraction. PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling.

PubMed ID: 21724836

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19557165

Title: Ebola Zaire virus blocks type I interferon production by exploiting the host SUMO modification machinery.

PubMed ID: 19557165

DOI: 10.1371/journal.ppat.1000493

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21965678

Title: SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function.

PubMed ID: 21965678

DOI: 10.1074/jbc.m111.267237

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 27211601

Title: SUMO5, a novel poly-sumo isoform, regulates pml nuclear bodies.

PubMed ID: 27211601

DOI: 10.1038/srep26509

PubMed ID: 28842558

Title: HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal misfolded Blimp-1s in lymphoma cells.

PubMed ID: 28842558

DOI: 10.1038/s41467-017-00476-w

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 29262325

Title: B Cell Receptor Activation and Chemical Induction Trigger Caspase-Mediated Cleavage of PIAS1 to Facilitate Epstein-Barr Virus Reactivation.

PubMed ID: 29262325

DOI: 10.1016/j.celrep.2017.11.071

PubMed ID: 36050397

Title: Crosstalk between SUMOylation and ubiquitylation controls DNA end resection by maintaining MRE11 homeostasis on chromatin.

PubMed ID: 36050397

DOI: 10.1038/s41467-022-32920-x

PubMed ID: 15133049

Title: NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers.

PubMed ID: 15133049

DOI: 10.1074/jbc.m403561200

Sequence Information:

Length: 651
Mass: 71836
Checksum: AA69338221124119
Sequence:

MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS PAVQMKIKEL 
YRRRFPQKIM TPADLSIPNV HSSPMPATLS PSTIPQLTYD GHPASSPLLP VSLLGPKHEL 
ELPHLTSALH PVHPDIKLQK LPFYDLLDEL IKPTSLASDN SQRFRETCFA FALTPQQVQQ 
ISSSMDISGT KCDFTVQVQL RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG 
VEPKRPSRPI NITSLVRLST TVPNTIVVSW TAEIGRNYSM AVYLVKQLSS TVLLQRLRAK 
GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT CSHLQCFDAT 
LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT DCDEIQFKED GTWAPMRSKK 
EVQEVSASYN GVDGCLSSTL EHQVASHHQS SNKNKKVEVI DLTIDSSSDE EEEEPSAKRT 
CPSLSPTSPL NNKGILSLPH QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL 
QGLDFFPFLS GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS 
LPTTNGSSSG SNSSLVSSNS LRESHSHTVT NRSSTDTASI FGIIPDIISL D

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: PIAS1

Associated with

Cells (max top 100)

Other Information

Inhibition of Stat1-mediated gene activation by PIAS1. PubMed ID: 9724754

Protein inhibitor of activated STAT-1 (signal transducer and activator of transcription-1) is a nuclear receptor coregulator expressed in human testis. PubMed ID: 10628744

Discovery of novel human transcript variants by analysis of intronic single-block EST with polyadenylation site. PubMed ID: 19906316

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

Analysis of the DNA sequence and duplication history of human chromosome 15. PubMed ID: 16572171

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Cloning and characterization of Gu/RH-II binding protein. PubMed ID: 9177271

LIM-domain protein cysteine- and glycine-rich protein 2 (CRP2) is a novel marker of hepatic stellate cells and binding partner of the protein inhibitor of activated STAT1. PubMed ID: 11672422

Involvement of PIAS1 in the sumoylation of tumor suppressor p53. PubMed ID: 11583632

Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells. PubMed ID: 11439351

SUMO-1 modification of the C-terminal KVEKVD of Axin is required for JNK activation but has no effect on Wnt signaling. PubMed ID: 12223491

Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes. PubMed ID: 12393906

Transcription factor Sp3 is silenced through SUMO modification by PIAS1. PubMed ID: 12356736

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity. PubMed ID: 11867732

SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin mu gene expression. PubMed ID: 14701874

PIAS1-mediated sumoylation of focal adhesion kinase activates its autophosphorylation. PubMed ID: 14500712

Repression of the transactivating capacity of the oncoprotein PLAG1 by SUMOylation. PubMed ID: 15208321

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

PIAS1 confers DNA-binding specificity on the Msx1 homeoprotein. PubMed ID: 16600910

Sumoylation delimits KLF8 transcriptional activity associated with the cell cycle regulation. PubMed ID: 16617055

Proinflammatory stimuli induce IKKalpha-mediated phosphorylation of PIAS1 to restrict inflammation and immunity. PubMed ID: 17540171

SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1. PubMed ID: 17369852

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling. PubMed ID: 19136629

Retraction. PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling. PubMed ID: 21724836

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Ebola Zaire virus blocks type I interferon production by exploiting the host SUMO modification machinery. PubMed ID: 19557165

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function. PubMed ID: 21965678

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Uncovering global SUMOylation signaling networks in a site-specific manner. PubMed ID: 25218447

SUMO-2 orchestrates chromatin modifiers in response to DNA damage. PubMed ID: 25772364

System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability. PubMed ID: 25755297

SUMO5, a novel poly-sumo isoform, regulates pml nuclear bodies. PubMed ID: 27211601

HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal misfolded Blimp-1s in lymphoma cells. PubMed ID: 28842558

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

B Cell Receptor Activation and Chemical Induction Trigger Caspase-Mediated Cleavage of PIAS1 to Facilitate Epstein-Barr Virus Reactivation. PubMed ID: 29262325

Crosstalk between SUMOylation and ubiquitylation controls DNA end resection by maintaining MRE11 homeostasis on chromatin. PubMed ID: 36050397

NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers. PubMed ID: 15133049