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UniProtKB - O75925 (PIAS1_HUMAN)

Entry version 208 (25 May 2022)
Sequence version 2 (05 Mar 2002)
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Protein

E3 SUMO-protein ligase PIAS1

Gene

PIAS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation (By similarity).

Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (By similarity).

By similarity2 Publications

Caution

A paper showing that PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling has been retracted, because some of the data was found to be deliberately falsified.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi351ZincPROSITE-ProRule annotation1
Metal bindingi353ZincPROSITE-ProRule annotation1
Metal bindingi374ZincPROSITE-ProRule annotation1
Metal bindingi377ZincPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri320 – 405SP-RING-typePROSITE-ProRule annotationAdd BLAST86

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Transferase
Biological processHost-virus interaction, Transcription, Transcription regulation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		O75925

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-3108214, SUMOylation of DNA damage response and repair proteins
R-HSA-3232118, SUMOylation of transcription factors
R-HSA-3232142, SUMOylation of ubiquitinylation proteins
R-HSA-3899300, SUMOylation of transcription cofactors
R-HSA-4090294, SUMOylation of intracellular receptors
R-HSA-4551638, SUMOylation of chromatin organization proteins
R-HSA-5696395, Formation of Incision Complex in GG-NER
R-HSA-877312, Regulation of IFNG signaling

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		O75925

SIGNOR Signaling Network Open Resource

More...SIGNORi		O75925

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00886

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
E3 SUMO-protein ligase PIAS1 (EC:2.3.2.-)
Alternative name(s):
DEAD/H box-binding protein 1
E3 SUMO-protein transferase PIAS1Curated
Gu-binding protein
Short name:
GBP
Protein inhibitor of activated STAT protein 1
RNA helicase II-binding protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PIAS1
Synonyms:DDXBP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 15

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:2752, PIAS1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		603566, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_O75925

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000033800

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi351C → A or S: Loss of UBE2I-binding; almost complete loss of promotion of TP53 sumoylation; no loss of SUMO1- and TP53-binding. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		8554

Open Targets

More...OpenTargetsi		ENSG00000033800

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33285

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		O75925, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PIAS1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002189742 – 651E3 SUMO-protein ligase PIAS1Add BLAST650

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki40Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki238Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei467PhosphoserineCombined sources1
Modified residuei468PhosphoserineCombined sources1
Modified residuei483PhosphoserineBy similarity1
Modified residuei485PhosphoserineCombined sources1
Modified residuei487PhosphothreonineBy similarity1
Modified residuei488PhosphoserineCombined sources1
Cross-linki493Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei503PhosphoserineCombined sources1
Modified residuei510PhosphoserineCombined sources1
Modified residuei522PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Sumoylated.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O75925

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O75925

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		O75925

MaxQB - The MaxQuant DataBase

More...MaxQBi		O75925

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		O75925

PeptideAtlas

More...PeptideAtlasi		O75925

PRoteomics IDEntifications database

More...PRIDEi		O75925

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		3657
50293 [O75925-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O75925

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		O75925

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in numerous tissues with highest level in testis.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000033800, Expressed in bone marrow and 246 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O75925, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O75925, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000033800, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with NCOA2 and AR.

Interacts with NR2C1; the interaction promotes its sumoylation (By similarity).

Interacts with DDX21, CSRP2, AXIN1, JUN, UBE2I, SUMO1, SATB2, PLAG1, TP53 and STAT1 (dimer), following IFNA1-stimulation.

Interacts with SP3 (preferentially when SUMO-modified).

Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G1 phase.

Interacts with CHUK/IKKA; this interaction induces PIAS1 phosphorylation.

Interacts with PTK2/FAK1; the interaction promotes its sumoylation.

Interacts with DDX5.

Interacts with PML (By similarity).

Interacts with MTA1.

Interacts with SUMO1P1/SUMO5 (PubMed:27211601).

Interacts with PRDM1/Blimp-1 (PubMed:28842558).

By similarity17 Publications

(Microbial infection) Interacts with ebolavirus VP35; this interaction mediates the sumoylation of IRF7 and contributes to the viral inhibition of IFN-type I production.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details
O75925
With#Exp.IntAct
A2M [P01023]3EBI-629434,EBI-640741
ALS2 [A0A0S2Z5Q7]3EBI-629434,EBI-25928834
APBB2 - isoform 2 [Q92870-2]3EBI-629434,EBI-21535880
ASPA [P45381]3EBI-629434,EBI-750475
ATXN1 [P54253]7EBI-629434,EBI-930964
ATXN10 [Q9UBB4]3EBI-629434,EBI-702390
ATXN3 [P54252]9EBI-629434,EBI-946046
CASP8AP2 [Q9UKL3]4EBI-629434,EBI-2339650
CCT5 [P48643]3EBI-629434,EBI-355710
DMWD [G5E9A7]3EBI-629434,EBI-10976677
ELAVL4 - isoform 2 [P26378-2]3EBI-629434,EBI-21603100
ERCC8 - isoform 2 [Q13216-2]3EBI-629434,EBI-16466949
FXN [Q16595]3EBI-629434,EBI-949340
GLE1 [Q53GS7]3EBI-629434,EBI-1955541
GRN [P28799]3EBI-629434,EBI-747754
HEXB [P07686]3EBI-629434,EBI-7133736
HOXD10 [P28358]3EBI-629434,EBI-12690664
HSPB1 [P04792]3EBI-629434,EBI-352682
HTRA2 [O43464]3EBI-629434,EBI-517086
HTT [P42858]19EBI-629434,EBI-466029
KIF1B - isoform 2 [O60333-2]3EBI-629434,EBI-10975473
LMNA [P02545]3EBI-629434,EBI-351935
LMNA - isoform C [P02545-2]3EBI-629434,EBI-351953
MBD1 [Q9UIS9]3EBI-629434,EBI-867196
MECP2 [P51608]3EBI-629434,EBI-1189067
NDUFV2 [P19404]3EBI-629434,EBI-713665
NF2 [P35240]3EBI-629434,EBI-1014472
NF2 - isoform 4 [P35240-4]3EBI-629434,EBI-1014514
NOS3 [P29474]3EBI-629434,EBI-1391623
PEX1 [O43933]3EBI-629434,EBI-988601
PEX7 [O00628]3EBI-629434,EBI-5238811
PHYH [O14832]3EBI-629434,EBI-721853
PPT1 [P50897]3EBI-629434,EBI-1237011
PRDM1 [O75626]2EBI-629434,EBI-948789
PRKCG [P05129]3EBI-629434,EBI-949799
PRPH [P41219]3EBI-629434,EBI-752074
SMN2 [Q16637]3EBI-629434,EBI-395421
SNCA [P37840]3EBI-629434,EBI-985879
SNCB [Q16143]3EBI-629434,EBI-727106
SPRED1 [Q7Z699]3EBI-629434,EBI-5235340
SPTLC1 [Q6NUL7]3EBI-629434,EBI-25912847
TDP1 [Q9NUW8]3EBI-629434,EBI-2902553
TP53 [P04637]4EBI-629434,EBI-366083
WFS1 [O76024]3EBI-629434,EBI-720609
YARS1 [P54577]3EBI-629434,EBI-1048893
Q9P1N43EBI-629434,EBI-25878161
RNA-directed RNA polymerase NS5 (PRO_0000037946) from Dengue virus type 2 (strain 16681-PDK53).3EBI-629434,EBI-8826488

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		114124, 144 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		O75925

Database of interacting proteins

More...DIPi		DIP-5970N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		O75925

Protein interaction database and analysis system

More...IntActi		O75925, 111 interactors

Molecular INTeraction database

More...MINTi		O75925

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000249636

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O75925, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1651
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		O75925

Biological Magnetic Resonance Data Bank

More...BMRBi		O75925

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		O75925

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		O75925

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini11 – 45SAPPROSITE-ProRule annotationAdd BLAST35
Domaini124 – 288PINITPROSITE-ProRule annotationAdd BLAST165
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati520 – 52314
Repeati557 – 56024
Repeati598 – 6013; approximate4
Repeati612 – 6154; approximate4

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni462 – 473SUMO1-bindingBy similarityAdd BLAST12
Regioni465 – 511DisorderedSequence analysisAdd BLAST47
Regioni520 – 6154 X 4 AA repeats of N-T-S-LAdd BLAST96
Regioni599 – 632DisorderedSequence analysisAdd BLAST34

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi19 – 23LXXLL motif5
Motifi56 – 64Nuclear localization signalSequence analysis9
Motifi368 – 380Nuclear localization signalSequence analysisAdd BLAST13

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi480 – 511Polar residuesSequence analysisAdd BLAST32

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The LXXLL motif is a transcriptional coregulator signature.
The SP-RING-type domain is required for promoting EKLF sumoylation.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the PIAS family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri320 – 405SP-RING-typePROSITE-ProRule annotationAdd BLAST86

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2169, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT01030000234539

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_020768_3_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O75925

Identification of Orthologs from Complete Genome Data

More...OMAi		CFVSKQM

Database of Orthologous Groups

More...OrthoDBi		1205949at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O75925

TreeFam database of animal gene trees

More...TreeFami		TF323787

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.720.30, 1 hit
2.60.120.780, 1 hit
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR027227, PIAS1
IPR023321, PINIT
IPR038654, PINIT_sf
IPR003034, SAP_dom
IPR036361, SAP_dom_sf
IPR004181, Znf_MIZ
IPR013083, Znf_RING/FYVE/PHD

The PANTHER Classification System

More...PANTHERi		PTHR10782:SF11, PTHR10782:SF11, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF14324, PINIT, 1 hit
PF02891, zf-MIZ, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00513, SAP, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF68906, SSF68906, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51466, PINIT, 1 hit
PS50800, SAP, 1 hit
PS51044, ZF_SP_RING, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O75925-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS 
        60         70         80         90        100
PAVQMKIKEL YRRRFPQKIM TPADLSIPNV HSSPMPATLS PSTIPQLTYD 
       110        120        130        140        150
GHPASSPLLP VSLLGPKHEL ELPHLTSALH PVHPDIKLQK LPFYDLLDEL 
       160        170        180        190        200
IKPTSLASDN SQRFRETCFA FALTPQQVQQ ISSSMDISGT KCDFTVQVQL 
       210        220        230        240        250
RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG VEPKRPSRPI 
       260        270        280        290        300
NITSLVRLST TVPNTIVVSW TAEIGRNYSM AVYLVKQLSS TVLLQRLRAK 
       310        320        330        340        350
GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT 
       360        370        380        390        400
CSHLQCFDAT LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT 
       410        420        430        440        450
DCDEIQFKED GTWAPMRSKK EVQEVSASYN GVDGCLSSTL EHQVASHHQS 
       460        470        480        490        500
SNKNKKVEVI DLTIDSSSDE EEEEPSAKRT CPSLSPTSPL NNKGILSLPH 
       510        520        530        540        550
QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL QGLDFFPFLS 
       560        570        580        590        600
GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS 
       610        620        630        640        650
LPTTNGSSSG SNSSLVSSNS LRESHSHTVT NRSSTDTASI FGIIPDIISL 

D
Length:651
Mass (Da):71,836
Last modified:March 5, 2002 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iAA69338221124119
GO
Isoform 2 (identifier: O75925-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MADSAEL → MFTLQDSYV

Show »
Length:653
Mass (Da):72,203
Checksum:i585370DA0FBDC926
GO
Isoform 3 (identifier: O75925-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     312-325: IKEKLTADPDSEIA → STYDKLISLIQLFC
     326-651: Missing.

Show »
Length:325
Mass (Da):36,204
Checksum:iF0A265377BDCADC2
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BSI8H3BSI8_HUMAN
E3 SUMO-protein ligase PIAS1
PIAS1
160Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BS65H3BS65_HUMAN
E3 SUMO-protein ligase PIAS1
PIAS1
64Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BUL7H3BUL7_HUMAN
E3 SUMO-protein ligase PIAS1
PIAS1
20Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti119E → K in AAC36702 (PubMed:9724754).Curated1
Sequence conflicti266 – 268IVV → MC in AAC36702 (PubMed:9724754).Curated3
Sequence conflicti613S → T in AAB58488 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0562191 – 7MADSAEL → MFTLQDSYV in isoform 2. 1 Publication7
Alternative sequenceiVSP_057195312 – 325IKEKL…DSEIA → STYDKLISLIQLFC in isoform 3. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_057196326 – 651Missing in isoform 3. 1 PublicationAdd BLAST326

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF077951 mRNA Translation: AAC36702.1
AF167160 mRNA Translation: AAD49722.1
FJ997900 mRNA Translation: ACR77525.1
AK094641 mRNA Translation: BAG52901.1
AK314515 mRNA Translation: BAG37114.1
AC107871 Genomic DNA No translation available.
AC135628 Genomic DNA No translation available.
BC118587 mRNA Translation: AAI18588.1
BC121797 mRNA Translation: AAI21798.1
U78524 mRNA Translation: AAB58488.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS45290.1 [O75925-1]
CCDS81902.1 [O75925-2]

NCBI Reference Sequences

More...RefSeqi		NP_001307616.1, NM_001320687.1 [O75925-2]
NP_057250.1, NM_016166.2 [O75925-1]
XP_016878177.1, XM_017022688.1 [O75925-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000249636.11; ENSP00000249636.6; ENSG00000033800.14
ENST00000545237.1; ENSP00000438574.1; ENSG00000033800.14 [O75925-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		8554

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:8554

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000249636.11; ENSP00000249636.6; NM_016166.3; NP_057250.1

UCSC genome browser

More...UCSCi		uc002aqz.4, human [O75925-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077951 mRNA Translation: AAC36702.1
AF167160 mRNA Translation: AAD49722.1
FJ997900 mRNA Translation: ACR77525.1
AK094641 mRNA Translation: BAG52901.1
AK314515 mRNA Translation: BAG37114.1
AC107871 Genomic DNA No translation available.
AC135628 Genomic DNA No translation available.
BC118587 mRNA Translation: AAI18588.1
BC121797 mRNA Translation: AAI21798.1
U78524 mRNA Translation: AAB58488.1
CCDSiCCDS45290.1 [O75925-1]
CCDS81902.1 [O75925-2]
RefSeqiNP_001307616.1, NM_001320687.1 [O75925-2]
NP_057250.1, NM_016166.2 [O75925-1]
XP_016878177.1, XM_017022688.1 [O75925-2]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V66NMR-A1-65[»]
AlphaFoldDBiO75925
BMRBiO75925
SMRiO75925
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi114124, 144 interactors
CORUMiO75925
DIPiDIP-5970N
ELMiO75925
IntActiO75925, 111 interactors
MINTiO75925
STRINGi9606.ENSP00000249636

PTM databases

iPTMnetiO75925
PhosphoSitePlusiO75925

Genetic variation databases

BioMutaiPIAS1

Proteomic databases

EPDiO75925
jPOSTiO75925
MassIVEiO75925
MaxQBiO75925
PaxDbiO75925
PeptideAtlasiO75925
PRIDEiO75925
ProteomicsDBi3657
50293 [O75925-1]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		26284, 368 antibodies from 35 providers

The DNASU plasmid repository

More...DNASUi		8554

Genome annotation databases

EnsembliENST00000249636.11; ENSP00000249636.6; ENSG00000033800.14
ENST00000545237.1; ENSP00000438574.1; ENSG00000033800.14 [O75925-2]
GeneIDi8554
KEGGihsa:8554
MANE-SelectiENST00000249636.11; ENSP00000249636.6; NM_016166.3; NP_057250.1
UCSCiuc002aqz.4, human [O75925-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8554
DisGeNETi8554

GeneCards: human genes, protein and diseases

More...GeneCardsi		PIAS1
HGNCiHGNC:2752, PIAS1
HPAiENSG00000033800, Low tissue specificity
MIMi603566, gene
neXtProtiNX_O75925
OpenTargetsiENSG00000033800
PharmGKBiPA33285
VEuPathDBiHostDB:ENSG00000033800

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2169, Eukaryota
GeneTreeiENSGT01030000234539
HOGENOMiCLU_020768_3_0_1
InParanoidiO75925
OMAiCFVSKQM
OrthoDBi1205949at2759
PhylomeDBiO75925
TreeFamiTF323787

Enzyme and pathway databases

UniPathwayiUPA00886
PathwayCommonsiO75925
ReactomeiR-HSA-3108214, SUMOylation of DNA damage response and repair proteins
R-HSA-3232118, SUMOylation of transcription factors
R-HSA-3232142, SUMOylation of ubiquitinylation proteins
R-HSA-3899300, SUMOylation of transcription cofactors
R-HSA-4090294, SUMOylation of intracellular receptors
R-HSA-4551638, SUMOylation of chromatin organization proteins
R-HSA-5696395, Formation of Incision Complex in GG-NER
R-HSA-877312, Regulation of IFNG signaling
SignaLinkiO75925
SIGNORiO75925

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		8554, 78 hits in 1057 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		PIAS1, human
EvolutionaryTraceiO75925

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PIAS1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		8554
PharosiO75925, Tbio

Protein Ontology

More...PROi		PR:O75925
RNActiO75925, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000033800, Expressed in bone marrow and 246 other tissues
ExpressionAtlasiO75925, baseline and differential
GenevisibleiO75925, HS

Family and domain databases

Gene3Di1.10.720.30, 1 hit
2.60.120.780, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR027227, PIAS1
IPR023321, PINIT
IPR038654, PINIT_sf
IPR003034, SAP_dom
IPR036361, SAP_dom_sf
IPR004181, Znf_MIZ
IPR013083, Znf_RING/FYVE/PHD
PANTHERiPTHR10782:SF11, PTHR10782:SF11, 1 hit
PfamiView protein in Pfam
PF14324, PINIT, 1 hit
PF02891, zf-MIZ, 1 hit
SMARTiView protein in SMART
SM00513, SAP, 1 hit
SUPFAMiSSF68906, SSF68906, 1 hit
PROSITEiView protein in PROSITE
PS51466, PINIT, 1 hit
PS50800, SAP, 1 hit
PS51044, ZF_SP_RING, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPIAS1_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O75925
Secondary accession number(s): B2RB67
, B3KSY9, C5J4B4, Q147X4, Q99751, Q9UN02
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: May 25, 2022
This is version 208 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families
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