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Entry version 169 (10 Apr 2019)
Sequence version 1 (01 Oct 2002)
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Protein

E3 SUMO-protein ligase PIAS4

Gene

PIAS4

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/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.6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'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.7 Publications
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 fingeri311 – 388SP-RING-typePROSITE-ProRule annotationAdd BLAST78

<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

GO - Biological processi

<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, Repressor, Transferase
Biological processTranscription, Transcription regulation, Ubl conjugation pathway, Wnt signaling pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-196791 Vitamin D (calciferol) metabolism
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-4085377 SUMOylation of SUMOylation proteins
R-HSA-4090294 SUMOylation of intracellular receptors
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-4755510 SUMOylation of immune response proteins
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693571 Nonhomologous End-Joining (NHEJ)
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-69473 G2/M DNA damage checkpoint

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

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SignaLinki
Q8N2W9

SIGNOR Signaling Network Open Resource

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SIGNORi
Q8N2W9

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_and_taxonomy_section">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 PIAS4 (EC:2.3.2.276 Publications)
Alternative name(s):
PIASy
Protein inhibitor of activated STAT protein 4
Protein inhibitor of activated STAT protein gamma
Short name:
PIAS-gamma
RING-type E3 ubiquitin transferase PIAS4Curated
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:PIAS4
Synonyms:PIASG
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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 19

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000105229.6

Human Gene Nomenclature Database

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HGNCi
HGNC:17002 PIAS4

Online Mendelian Inheritance in Man (OMIM)

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MIMi
605989 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q8N2W9

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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_and_biotech_section">'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>Mutagenesisi23 – 24LL → AA: Loss of repression of AR- and STAT1-induced transcription; no effect on AR- and STAT1-binding. 2 Publications2
Mutagenesisi35K → R: Complete loss of sumoylation. No enhancement of TCF4 sumoylation. No effect on interaction with TCF4. Colocalizes with SUMO1 in nucleus but concentrated into nuclear granules. 2 Publications1
Mutagenesisi128K → R: Some loss of sumoylation. 2 Publications1
Mutagenesisi342C → A: Inhibits TCF4 sumoylation. Inhibits beta-catenin-mediated TCF7L2/TCF4 activity. No colocalization with TCF7L2/TCF4 in nuclear punctate structures; when associated with A-347. 1
Mutagenesisi347C → A: Inhibits TCF4 sumoylation. Inhibits beta-catenin-mediated TCF7L2/TCF4 activity. No colocalization with TCF7L2/TCF4 in nuclear punctate structures; when associated with A-342. AR- and STAT1-binding. 1

Organism-specific databases

DisGeNET

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DisGeNETi
51588

Open Targets

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OpenTargetsi
ENSG00000105229

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA134945903

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PIAS4

Domain mapping of disease mutations (DMDM)

More...
DMDMi
34922831

<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_processing_section">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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002189822 – 510E3 SUMO-protein ligase PIAS4Add BLAST509

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_processing_section">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-linki9Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki68Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki69Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei114N6-acetyllysineCombined sources1
Cross-linki125Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki128Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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. 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.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q8N2W9

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q8N2W9

MaxQB - The MaxQuant DataBase

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MaxQBi
Q8N2W9

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

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PaxDbi
Q8N2W9

PeptideAtlas

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PeptideAtlasi
Q8N2W9

PRoteomics IDEntifications database

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PRIDEi
Q8N2W9

ProteomicsDB human proteome resource

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ProteomicsDBi
71739

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q8N2W9

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

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PhosphoSitePlusi
Q8N2W9

<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

Highly expressed in testis and, at lower levels, in spleen, prostate, ovary, colon and peripheral blood leukocytes.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000105229 Expressed in 182 organ(s), highest expression level in testis

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q8N2W9 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA010598

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with AR, AXIN1, GATA2, LEF1, TP53 and STAT1 (IFNG-induced). Binds to AT-rich DNA sequences, known as matrix or scaffold attachment regions (MARs/SARs) (By similarity). Interacts with TICAM1. 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 MTA1.By similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
119624, 133 interactors

Database of interacting proteins

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DIPi
DIP-32499N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q8N2W9

Protein interaction database and analysis system

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IntActi
Q8N2W9, 65 interactors

Molecular INTeraction database

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MINTi
Q8N2W9

STRING: functional protein association networks

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STRINGi
9606.ENSP00000262971

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q8N2W9

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

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SMRi
Q8N2W9

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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_and_domains_section">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>Domaini12 – 46SAPPROSITE-ProRule annotationAdd BLAST35
Domaini119 – 279PINITPROSITE-ProRule annotationAdd BLAST161

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>Motifi20 – 24LXXLL motif1 Publication5

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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi464 – 492Asp/Glu-rich (acidic)Add BLAST29

<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 coregulator signature that is essential for transcriptional corepression.1 Publication

<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 fingeri311 – 388SP-RING-typePROSITE-ProRule annotationAdd BLAST78

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2169 Eukaryota
ENOG410XQ2E LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000182717

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000230594

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG053598

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q8N2W9

KEGG Orthology (KO)

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KOi
K16065

Identification of Orthologs from Complete Genome Data

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OMAi
LRICYTD

Database of Orthologous Groups

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OrthoDBi
1205949at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q8N2W9

TreeFam database of animal gene trees

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TreeFami
TF323787

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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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

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InterProi
View protein in InterPro
IPR027224 PIAS4
IPR023321 PINIT
IPR038654 PINIT_sf
IPR003034 SAP_dom
IPR036361 SAP_dom_sf
IPR004181 Znf_MIZ
IPR013083 Znf_RING/FYVE/PHD

The PANTHER Classification System

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PANTHERi
PTHR10782:SF9 PTHR10782:SF9, 1 hit

Pfam protein domain database

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

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00513 SAP, 1 hit

Superfamily database of structural and functional annotation

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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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

Q8N2W9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAAELVEAKN MVMSFRVSDL QMLLGFVGRS KSGLKHELVT RALQLVQFDC
60 70 80 90 100
SPELFKKIKE LYETRYAKKN SEPAPQPHRP LDPLTMHSTY DRAGAVPRTP
110 120 130 140 150
LAGPNIDYPV LYGKYLNGLG RLPAKTLKPE VRLVKLPFFN MLDELLKPTE
160 170 180 190 200
LVPQNNEKLQ ESPCIFALTP RQVELIRNSR ELQPGVKAVQ VVLRICYSDT
210 220 230 240 250
SCPQEDQYPP NIAVKVNHSY CSVPGYYPSN KPGVEPKRPC RPINLTHLMY
260 270 280 290 300
LSSATNRITV TWGNYGKSYS VALYLVRQLT SSELLQRLKT IGVKHPELCK
310 320 330 340 350
ALVKEKLRLD PDSEIATTGV RVSLICPLVK MRLSVPCRAE TCAHLQCFDA
360 370 380 390 400
VFYLQMNEKK PTWMCPVCDK PAPYDQLIID GLLSKILSEC EDADEIEYLV
410 420 430 440 450
DGSWCPIRAE KERSCSPQGA ILVLGPSDAN GLLPAPSVNG SGALGSTGGG
460 470 480 490 500
GPVGSMENGK PGADVVDLTL DSSSSSEDEE EEEEEEEDED EEGPRPKRRC
510
PFQKGLVPAC
Length:510
Mass (Da):56,504
Last modified:October 1, 2002 - v1
<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:i26AAA18246E1ACE3
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAD45155 differs from that shown. Reason: Erroneous initiation.Curated

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 conflicti178N → K (PubMed:9724754).Curated1
Sequence conflicti179 – 182SREL → FQGM (PubMed:9724754).Curated4
Sequence conflicti179 – 182SREL → FQGM (PubMed:11388671).Curated4
Sequence conflicti482E → G in AAH66895 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF077952 mRNA Translation: AAC36703.1
BC010047 mRNA Translation: AAH10047.2
BC029874 mRNA Translation: AAH29874.1
BC066895 mRNA Translation: AAH66895.1
AF164437 mRNA Translation: AAD45155.1 Different initiation.

The Consensus CDS (CCDS) project

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CCDSi
CCDS12118.1

NCBI Reference Sequences

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RefSeqi
NP_056981.2, NM_015897.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.105779

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000262971; ENSP00000262971; ENSG00000105229

Database of genes from NCBI RefSeq genomes

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GeneIDi
51588

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:51588

UCSC genome browser

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UCSCi
uc002lzg.4 human

<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
AF077952 mRNA Translation: AAC36703.1
BC010047 mRNA Translation: AAH10047.2
BC029874 mRNA Translation: AAH29874.1
BC066895 mRNA Translation: AAH66895.1
AF164437 mRNA Translation: AAD45155.1 Different initiation.
CCDSiCCDS12118.1
RefSeqiNP_056981.2, NM_015897.3
UniGeneiHs.105779

3D structure databases

ProteinModelPortaliQ8N2W9
SMRiQ8N2W9
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119624, 133 interactors
DIPiDIP-32499N
ELMiQ8N2W9
IntActiQ8N2W9, 65 interactors
MINTiQ8N2W9
STRINGi9606.ENSP00000262971

PTM databases

iPTMnetiQ8N2W9
PhosphoSitePlusiQ8N2W9

Polymorphism and mutation databases

BioMutaiPIAS4
DMDMi34922831

Proteomic databases

EPDiQ8N2W9
jPOSTiQ8N2W9
MaxQBiQ8N2W9
PaxDbiQ8N2W9
PeptideAtlasiQ8N2W9
PRIDEiQ8N2W9
ProteomicsDBi71739

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
51588
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262971; ENSP00000262971; ENSG00000105229
GeneIDi51588
KEGGihsa:51588
UCSCiuc002lzg.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
51588
DisGeNETi51588
EuPathDBiHostDB:ENSG00000105229.6

GeneCards: human genes, protein and diseases

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GeneCardsi
PIAS4
HGNCiHGNC:17002 PIAS4
HPAiHPA010598
MIMi605989 gene
neXtProtiNX_Q8N2W9
OpenTargetsiENSG00000105229
PharmGKBiPA134945903

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2169 Eukaryota
ENOG410XQ2E LUCA
GeneTreeiENSGT00950000182717
HOGENOMiHOG000230594
HOVERGENiHBG053598
InParanoidiQ8N2W9
KOiK16065
OMAiLRICYTD
OrthoDBi1205949at2759
PhylomeDBiQ8N2W9
TreeFamiTF323787

Enzyme and pathway databases

UniPathwayi
UPA00886

ReactomeiR-HSA-196791 Vitamin D (calciferol) metabolism
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-4085377 SUMOylation of SUMOylation proteins
R-HSA-4090294 SUMOylation of intracellular receptors
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-4755510 SUMOylation of immune response proteins
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693571 Nonhomologous End-Joining (NHEJ)
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-69473 G2/M DNA damage checkpoint
SignaLinkiQ8N2W9
SIGNORiQ8N2W9

Miscellaneous databases

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

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ChiTaRSi
PIAS4 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
PIAS4

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

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GenomeRNAii
51588

Protein Ontology

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PROi
PR:Q8N2W9

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000105229 Expressed in 182 organ(s), highest expression level in testis
GenevisibleiQ8N2W9 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
IPR027224 PIAS4
IPR023321 PINIT
IPR038654 PINIT_sf
IPR003034 SAP_dom
IPR036361 SAP_dom_sf
IPR004181 Znf_MIZ
IPR013083 Znf_RING/FYVE/PHD
PANTHERiPTHR10782:SF9 PTHR10782:SF9, 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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 nameiPIAS4_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: Q8N2W9
Secondary accession number(s): O75926, Q96G19, Q9UN16
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: October 1, 2002
Last modified: April 10, 2019
This is version 169 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
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