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Protein

Protein-arginine deiminase type-4

Gene

PADI4

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

Catalyzes the citrullination/deimination of arginine residues of proteins such as histones, thereby playing a key role in histone code and regulation of stem cell maintenance. Citrullinates histone H1 at 'Arg-54' (to form H1R54ci), histone H3 at 'Arg-2', 'Arg-8', 'Arg-17' and/or 'Arg-26' (to form H3R2ci, H3R8ci, H3R17ci, H3R26ci, respectively) and histone H4 at 'Arg-3' (to form H4R3ci). Acts as a key regulator of stem cell maintenance by mediating citrullination of histone H1: citrullination of 'Arg-54' of histone H1 (H1R54ci) results in H1 displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. Promotes profound chromatin decondensation during the innate immune response to infection in neutrophils by mediating formation of H1R54ci. Citrullination of histone H3 prevents their methylation by CARM1 and HRMT1L2/PRMT1 and represses transcription. Citrullinates EP300/P300 at 'Arg-2142', which favors its interaction with NCOA2/GRIP1.6 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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+3 PublicationsNote: Binds 5 Ca2+ ions per subunit.3 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Strongly Inhibited by F-amidine and N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine amide (Cl-amidine). These inhibitors are however not specific to PADI4 and also inhibit other members of the family (PubMed:17002273). Incorporation of a carboxylate ortho to the backbone amide of Cl-amidine results in inhibitors with increased specificity for PADI4: N-alpha-(2-carboxyl)benzoyl-N5-(2-fluoro-1-iminoethyl)-L-ornithine amide (o-F-amidine) and N-alpha-(2-carboxyl)benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine amide (o-Cl-amidine) (PubMed:21882827). Strongly and specifically inhibited by Thr-Asp-F-amidine (TDFA); other members of the family are not inhibited (PubMed:22004374).3 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.055 mM for fibrinogen1 Publication
  2. KM=0.064 mM for filaggrin1 Publication
  1. Vmax=33.2 µmol/h/mg enzyme toward fibrinogen1 Publication
  2. Vmax=8.0 µmol/h/mg enzyme toward filaggrin1 Publication

pH dependencei

Optimum pH is 6.5-9.0.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi153Calcium 13 Publications1
Metal bindingi155Calcium 13 Publications1
Metal bindingi155Calcium 23 Publications1
Metal bindingi157Calcium 13 Publications1
Metal bindingi157Calcium 23 Publications1
Metal bindingi165Calcium 13 Publications1
Metal bindingi165Calcium 3; via carbonyl oxygen3 Publications1
Metal bindingi168Calcium 33 Publications1
Metal bindingi170Calcium 3; via carbonyl oxygen3 Publications1
Metal bindingi176Calcium 13 Publications1
Metal bindingi179Calcium 13 Publications1
Metal bindingi179Calcium 23 Publications1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei346TDFA Inhibitor1 Publication1
Metal bindingi349Calcium 43 Publications1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei3501 Publication1
Metal bindingi351Calcium 53 Publications1
Metal bindingi353Calcium 43 Publications1
Metal bindingi369Calcium 53 Publications1
Binding sitei369TDFA Inhibitor1 Publication1
Metal bindingi370Calcium 5; via carbonyl oxygen3 Publications1
Metal bindingi373Calcium 53 Publications1
Binding sitei374Substrate1
Binding sitei374TDFA Inhibitor1 Publication1
Metal bindingi388Calcium 23 Publications1
Metal bindingi407Calcium 4; via carbonyl oxygen3 Publications1
Metal bindingi410Calcium 4; via carbonyl oxygen3 Publications1
Metal bindingi411Calcium 43 Publications1
Active sitei4711 Publication1
Binding sitei471TDFA Inhibitor1 Publication1
Active sitei4731 Publication1
Binding sitei473TDFA Inhibitor1 Publication1
Binding sitei639Substrate; via carbonyl oxygen1
Active sitei6451 Publication1
Binding sitei645TDFA Inhibitor1 Publication1

<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

  • arginine binding Source: CAFA
  • arginine deiminase activity Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • protein-arginine deiminase activity Source: UniProtKB
  • protein homodimerization activity Source: CAFA

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 functionChromatin regulator, Hydrolase
Biological processImmunity, Innate immunity, Transcription, Transcription regulation
LigandCalcium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS08389-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.5.3.15 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-3247509 Chromatin modifying enzymes

<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:
Protein-arginine deiminase type-4 (EC:3.5.3.15)
Alternative name(s):
HL-60 PAD
Peptidylarginine deiminase IV
Protein-arginine deiminase type IV
<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:PADI4
Synonyms:PAD4, PADI5, PDI5
<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)
<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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000159339.13

Human Gene Nomenclature Database

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HGNCi
HGNC:18368 PADI4

Online Mendelian Inheritance in Man (OMIM)

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MIMi
605347 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9UM07

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, 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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Rheumatoid arthritis (RA)1 Publication
The gene represented in this entry may be involved in disease pathogenesis. The association to rheumatoid arthritis was initially thought to result from increased citrullination of target proteins (PubMed:12833157). However, variants that have been associated to rheumatoid arthritis (Ser-55, Ala-82 and Ala-112) do not affect the catalytic activity or the citrullination activity of PADI4, suggesting that these variants may affect the mRNA stability rather than the protein (PubMed:21245532).2 Publications
Disease descriptionAn inflammatory disease with autoimmune features and a complex genetic component. It primarily affects the joints and is characterized by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures.
See also OMIM:180300

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>Mutagenesisi346Q → A: Impaired binding of TDFA Inhibitor. 1 Publication1
Mutagenesisi374R → A: Strongly reduces enzymatic activity. 3 Publications1
Mutagenesisi374R → Q: Impaired binding of TDFA Inhibitor. 3 Publications1
Mutagenesisi639R → Q: Impaired binding of TDFA Inhibitor. 1 Publication1
Mutagenesisi645C → A: Abolishes enzymatic activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
23569

MalaCards human disease database

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MalaCardsi
PADI4
MIMi180300 phenotype

Open Targets

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OpenTargetsi
ENSG00000159339

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA32903

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL6111

Drug and drug target database

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DrugBanki
DB00207 Azithromycin
DB00254 Doxycycline
DB00155 L-Citrulline
DB07449 N-[(1S)-1-(AMINOCARBONYL)-4-(ETHANIMIDOYLAMINO)BUTYL]BENZAMIDE
DB01082 Streptomycin
DB00759 Tetracycline

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2877

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PADI4

Domain mapping of disease mutations (DMDM)

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DMDMi
296439260

<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 ‘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_00002200331 – 663Protein-arginine deiminase type-4Add BLAST663

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 residuei205Citrulline1 Publication1
Modified residuei212Citrulline1 Publication1
Modified residuei218Citrulline1 Publication1
Modified residuei372Citrulline1 Publication1
Modified residuei374Citrulline1 Publication1
Modified residuei383Citrulline1 Publication1

<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

Autocitrullination at Arg-372 and Arg-374 inactivates the enzyme.

Keywords - PTMi

Citrullination

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9UM07

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

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PaxDbi
Q9UM07

PeptideAtlas

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PeptideAtlasi
Q9UM07

PRoteomics IDEntifications database

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PRIDEi
Q9UM07

ProteomicsDB human proteome resource

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ProteomicsDBi
85166

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9UM07

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

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PhosphoSitePlusi
Q9UM07

<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 eosinophils and neutrophils, not expressed in peripheral monocytes or lymphocytes.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000159339 Expressed in 88 organ(s), highest expression level in blood

CleanEx database of gene expression profiles

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CleanExi
HS_PADI4

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9UM07 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9UM07 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA017007
HPA042825

<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%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

WithEntry#Exp.IntActNotes
ANXA4Q6LES25EBI-1042511,EBI-10250835

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
117111, 13 interactors

Database of interacting proteins

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DIPi
DIP-50397N

Protein interaction database and analysis system

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IntActi
Q9UM07, 4 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000364597

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q9UM07

<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

1663
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

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DisProti
DP00321

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q9UM07

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

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SMRi
Q9UM07

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...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q9UM07

<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

<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 protein arginine deiminase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IF3F Eukaryota
ENOG410ZKF3 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154565

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000220908

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG053016

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9UM07

KEGG Orthology (KO)

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KOi
K01481

Identification of Orthologs from Complete Genome Data

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OMAi
RVFQATR

Database of Orthologous Groups

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OrthoDBi
EOG091G02QG

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9UM07

TreeFam database of animal gene trees

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TreeFami
TF331952

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.1700, 1 hit
2.60.40.1860, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR008972 Cupredoxin
IPR004303 PAD
IPR013530 PAD_C
IPR036556 PAD_central_sf
IPR013732 PAD_N
IPR038685 PAD_N_sf
IPR013733 Prot_Arg_deaminase_cen_dom

The PANTHER Classification System

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PANTHERi
PTHR10837 PTHR10837, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF03068 PAD, 1 hit
PF08527 PAD_M, 1 hit
PF08526 PAD_N, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF001247 Protein-arginine_deiminase, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF110083 SSF110083, 1 hit
SSF49503 SSF49503, 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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q9UM07-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAQGTLIRVT PEQPTHAVCV LGTLTQLDIC SSAPEDCTSF SINASPGVVV
60 70 80 90 100
DIAHGPPAKK KSTGSSTWPL DPGVEVTLTM KVASGSTGDQ KVQISYYGPK
110 120 130 140 150
TPPVKALLYL TGVEISLCAD ITRTGKVKPT RAVKDQRTWT WGPCGQGAIL
160 170 180 190 200
LVNCDRDNLE SSAMDCEDDE VLDSEDLQDM SLMTLSTKTP KDFFTNHTLV
210 220 230 240 250
LHVARSEMDK VRVFQATRGK LSSKCSVVLG PKWPSHYLMV PGGKHNMDFY
260 270 280 290 300
VEALAFPDTD FPGLITLTIS LLDTSNLELP EAVVFQDSVV FRVAPWIMTP
310 320 330 340 350
NTQPPQEVYA CSIFENEDFL KSVTTLAMKA KCKLTICPEE ENMDDQWMQD
360 370 380 390 400
EMEIGYIQAP HKTLPVVFDS PRNRGLKEFP IKRVMGPDFG YVTRGPQTGG
410 420 430 440 450
ISGLDSFGNL EVSPPVTVRG KEYPLGRILF GDSCYPSNDS RQMHQALQDF
460 470 480 490 500
LSAQQVQAPV KLYSDWLSVG HVDEFLSFVP APDRKGFRLL LASPRSCYKL
510 520 530 540 550
FQEQQNEGHG EALLFEGIKK KKQQKIKNIL SNKTLREHNS FVERCIDWNR
560 570 580 590 600
ELLKRELGLA ESDIIDIPQL FKLKEFSKAE AFFPNMVNML VLGKHLGIPK
610 620 630 640 650
PFGPVINGRC CLEEKVCSLL EPLGLQCTFI NDFFTYHIRH GEVHCGTNVR
660
RKPFSFKWWN MVP
Length:663
Mass (Da):74,079
Last modified:May 18, 2010 - 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:i79D7AF7B3D307A3B
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B1AQ67B1AQ67_HUMAN
Protein-arginine deiminase type-4
PADI4
127Annotation 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 conflicti149I → V in BAF83196 (PubMed:14702039).Curated1
Sequence conflicti247M → T in BAG37357 (PubMed:14702039).Curated1
Sequence conflicti657K → E in BAF83196 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0535608R → H. Corresponds to variant dbSNP:rs35381732Ensembl.1
Natural variantiVAR_02063955G → S Does not affect catalytic activity. 3 PublicationsCorresponds to variant dbSNP:rs11203366Ensembl.1
Natural variantiVAR_05356179T → M. Corresponds to variant dbSNP:rs35809521Ensembl.1
Natural variantiVAR_02064082V → A Does not affect catalytic activity. 3 PublicationsCorresponds to variant dbSNP:rs11203367Ensembl.1
Natural variantiVAR_02740189D → N1 PublicationCorresponds to variant dbSNP:rs143187209Ensembl.1
Natural variantiVAR_027402102P → T1 PublicationCorresponds to variant dbSNP:rs34309058Ensembl.1
Natural variantiVAR_020641112G → A Does not affect catalytic activity. 3 PublicationsCorresponds to variant dbSNP:rs874881Ensembl.1
Natural variantiVAR_027403131R → T1 PublicationCorresponds to variant dbSNP:rs12733102Ensembl.1
Natural variantiVAR_027404164M → T. Corresponds to variant dbSNP:rs11588132Ensembl.1
Natural variantiVAR_053562260D → N. Corresponds to variant dbSNP:rs35903413Ensembl.1
Natural variantiVAR_020642275S → F1 PublicationCorresponds to variant dbSNP:rs1748020Ensembl.1

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

More...
DDBJi
Links Updated
AB017919 mRNA Translation: BAA84542.1
AJ549502 Genomic DNA Translation: CAE47743.1
AK290507 mRNA Translation: BAF83196.1
AK314839 mRNA Translation: BAG37357.1
AC004824 Genomic DNA No translation available.
AL590644 Genomic DNA No translation available.
BC025718 mRNA Translation: AAH25718.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS180.1

NCBI Reference Sequences

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RefSeqi
NP_036519.2, NM_012387.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.522969

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000375448; ENSP00000364597; ENSG00000159339
ENST00000628229; ENSP00000487021; ENSG00000280908

Database of genes from NCBI RefSeq genomes

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GeneIDi
23569

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:23569

UCSC genome browser

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UCSCi
uc001baj.3 human

Keywords - Coding sequence diversityi

Polymorphism

<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
AB017919 mRNA Translation: BAA84542.1
AJ549502 Genomic DNA Translation: CAE47743.1
AK290507 mRNA Translation: BAF83196.1
AK314839 mRNA Translation: BAG37357.1
AC004824 Genomic DNA No translation available.
AL590644 Genomic DNA No translation available.
BC025718 mRNA Translation: AAH25718.1
CCDSiCCDS180.1
RefSeqiNP_036519.2, NM_012387.2
UniGeneiHs.522969

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WD8X-ray2.80A1-663[»]
1WD9X-ray2.60A1-663[»]
1WDAX-ray2.30A1-663[»]
2DEWX-ray2.10X1-663[»]
2DEXX-ray2.10X1-663[»]
2DEYX-ray2.25X1-663[»]
2DW5X-ray2.30A1-663[»]
3APMX-ray2.50A1-663[»]
3APNX-ray2.70A1-663[»]
3B1TX-ray2.50A1-663[»]
3B1UX-ray2.10A1-663[»]
4DKTX-ray2.98A1-663[»]
4X8CX-ray3.10A1-663[»]
4X8GX-ray3.29A1-663[»]
5N0MX-ray2.18A1-663[»]
5N0YX-ray2.23A1-663[»]
5N0ZX-ray2.52A1-663[»]
5N1BX-ray2.90A1-663[»]
DisProtiDP00321
ProteinModelPortaliQ9UM07
SMRiQ9UM07
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117111, 13 interactors
DIPiDIP-50397N
IntActiQ9UM07, 4 interactors
STRINGi9606.ENSP00000364597

Chemistry databases

BindingDBiQ9UM07
ChEMBLiCHEMBL6111
DrugBankiDB00207 Azithromycin
DB00254 Doxycycline
DB00155 L-Citrulline
DB07449 N-[(1S)-1-(AMINOCARBONYL)-4-(ETHANIMIDOYLAMINO)BUTYL]BENZAMIDE
DB01082 Streptomycin
DB00759 Tetracycline
GuidetoPHARMACOLOGYi2877

PTM databases

iPTMnetiQ9UM07
PhosphoSitePlusiQ9UM07

Polymorphism and mutation databases

BioMutaiPADI4
DMDMi296439260

Proteomic databases

MaxQBiQ9UM07
PaxDbiQ9UM07
PeptideAtlasiQ9UM07
PRIDEiQ9UM07
ProteomicsDBi85166

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
23569
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375448; ENSP00000364597; ENSG00000159339
ENST00000628229; ENSP00000487021; ENSG00000280908
GeneIDi23569
KEGGihsa:23569
UCSCiuc001baj.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
23569
DisGeNETi23569
EuPathDBiHostDB:ENSG00000159339.13

GeneCards: human genes, protein and diseases

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GeneCardsi
PADI4

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0000182
HGNCiHGNC:18368 PADI4
HPAiHPA017007
HPA042825
MalaCardsiPADI4
MIMi180300 phenotype
605347 gene
neXtProtiNX_Q9UM07
OpenTargetsiENSG00000159339
PharmGKBiPA32903

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IF3F Eukaryota
ENOG410ZKF3 LUCA
GeneTreeiENSGT00940000154565
HOGENOMiHOG000220908
HOVERGENiHBG053016
InParanoidiQ9UM07
KOiK01481
OMAiRVFQATR
OrthoDBiEOG091G02QG
PhylomeDBiQ9UM07
TreeFamiTF331952

Enzyme and pathway databases

BioCyciMetaCyc:HS08389-MONOMER
BRENDAi3.5.3.15 2681
ReactomeiR-HSA-3247509 Chromatin modifying enzymes

Miscellaneous databases

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

More...
ChiTaRSi
PADI4 human
EvolutionaryTraceiQ9UM07

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
PADI4

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

More...
GenomeRNAii
23569

Protein Ontology

More...
PROi
PR:Q9UM07

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000159339 Expressed in 88 organ(s), highest expression level in blood
CleanExiHS_PADI4
ExpressionAtlasiQ9UM07 baseline and differential
GenevisibleiQ9UM07 HS

Family and domain databases

Gene3Di2.60.40.1700, 1 hit
2.60.40.1860, 1 hit
InterProiView protein in InterPro
IPR008972 Cupredoxin
IPR004303 PAD
IPR013530 PAD_C
IPR036556 PAD_central_sf
IPR013732 PAD_N
IPR038685 PAD_N_sf
IPR013733 Prot_Arg_deaminase_cen_dom
PANTHERiPTHR10837 PTHR10837, 1 hit
PfamiView protein in Pfam
PF03068 PAD, 1 hit
PF08527 PAD_M, 1 hit
PF08526 PAD_N, 1 hit
PIRSFiPIRSF001247 Protein-arginine_deiminase, 1 hit
SUPFAMiSSF110083 SSF110083, 1 hit
SSF49503 SSF49503, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
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 nameiPADI4_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: Q9UM07
Secondary accession number(s): A8K392
, B2RBW0, Q5VTZ8, Q70SX4
<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: January 11, 2001
Last sequence update: May 18, 2010
Last modified: December 5, 2018
This is version 170 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, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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