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Q9UM07

- PADI4_HUMAN

UniProt

Q9UM07 - PADI4_HUMAN

Protein

Protein-arginine deiminase type-4

Gene

PADI4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    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

    Catalytic activityi

    Protein L-arginine + H2O = protein L-citrulline + NH3.2 Publications

    Cofactori

    Binds 5 calcium ions per subunit.3 Publications

    Enzyme 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-N(5)-(2-fluoro-1-iminoethyl)-L-ornithine amide (o-F-amidine) and N-alpha-(2-carboxyl)benzoyl-N(5)-(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

    Kineticsi

    1. KM=0.055 mM for fibrinogen1 Publication
    2. KM=0.064 mM for filaggrin1 Publication

    Vmax=33.2 µmol/h/mg enzyme toward fibrinogen1 Publication

    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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi153 – 1531Calcium 13 Publications
    Metal bindingi155 – 1551Calcium 13 Publications
    Metal bindingi155 – 1551Calcium 23 Publications
    Metal bindingi157 – 1571Calcium 13 Publications
    Metal bindingi157 – 1571Calcium 23 Publications
    Metal bindingi165 – 1651Calcium 13 Publications
    Metal bindingi165 – 1651Calcium 3; via carbonyl oxygen3 Publications
    Metal bindingi168 – 1681Calcium 33 Publications
    Metal bindingi170 – 1701Calcium 3; via carbonyl oxygen3 Publications
    Metal bindingi176 – 1761Calcium 13 Publications
    Metal bindingi179 – 1791Calcium 13 Publications
    Metal bindingi179 – 1791Calcium 23 Publications
    Binding sitei346 – 3461TDFA Inhibitor1 Publication
    Metal bindingi349 – 3491Calcium 43 Publications
    Active sitei350 – 35011 Publication
    Metal bindingi351 – 3511Calcium 53 Publications
    Metal bindingi353 – 3531Calcium 43 Publications
    Metal bindingi369 – 3691Calcium 53 Publications
    Binding sitei369 – 3691TDFA Inhibitor1 Publication
    Metal bindingi370 – 3701Calcium 5; via carbonyl oxygen3 Publications
    Metal bindingi373 – 3731Calcium 53 Publications
    Binding sitei374 – 3741Substrate
    Binding sitei374 – 3741TDFA Inhibitor1 Publication
    Metal bindingi388 – 3881Calcium 23 Publications
    Metal bindingi407 – 4071Calcium 4; via carbonyl oxygen3 Publications
    Metal bindingi410 – 4101Calcium 4; via carbonyl oxygen3 Publications
    Metal bindingi411 – 4111Calcium 43 Publications
    Active sitei471 – 47111 Publication
    Binding sitei471 – 4711TDFA Inhibitor1 Publication
    Active sitei473 – 47311 Publication
    Binding sitei473 – 4731TDFA Inhibitor1 Publication
    Binding sitei639 – 6391Substrate; via carbonyl oxygen
    Active sitei645 – 64511 Publication
    Binding sitei645 – 6451TDFA Inhibitor1 Publication

    GO - Molecular functioni

    1. arginine deiminase activity Source: UniProtKB
    2. calcium ion binding Source: UniProtKB
    3. protein-arginine deiminase activity Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular protein modification process Source: ProtInc
    2. chromatin modification Source: UniProtKB
    3. chromatin remodeling Source: UniProtKB
    4. histone citrullination Source: UniProtKB
    5. histone H3-R26 citrullination Source: UniProtKB
    6. innate immune response Source: UniProtKB-KW
    7. nucleosome assembly Source: UniProtKB
    8. protein citrullination Source: UniProtKB
    9. regulation of transcription, DNA-templated Source: UniProtKB-KW
    10. stem cell maintenance Source: UniProtKB
    11. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase

    Keywords - Biological processi

    Immunity, Innate immunity, Transcription, Transcription regulation

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08389-MONOMER.
    BRENDAi3.5.3.15. 2681.

    Names & Taxonomyi

    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
    Gene namesi
    Name:PADI4
    Synonyms:PADI5, PDI5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:18368. PADI4.

    Subcellular locationi

    Cytoplasm. Nucleus. Cytoplasmic granule
    Note: Cytoplasmic granules of eosinophils and neutrophils.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Rheumatoid arthritis (RA) [MIM:180300]: An 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.1 Publication
    Note: 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

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi346 – 3461Q → A: Impaired binding of TDFA Inhibitor. 1 Publication
    Mutagenesisi374 – 3741R → A: Strongly reduces enzymatic activity. 3 Publications
    Mutagenesisi374 – 3741R → Q: Impaired binding of TDFA Inhibitor. 3 Publications
    Mutagenesisi639 – 6391R → Q: Impaired binding of TDFA Inhibitor. 1 Publication
    Mutagenesisi645 – 6451C → A: Abolishes enzymatic activity. 1 Publication

    Organism-specific databases

    MIMi180300. phenotype.
    PharmGKBiPA32903.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 663663Protein-arginine deiminase type-4PRO_0000220033Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei205 – 2051Citrulline1 Publication
    Modified residuei212 – 2121Citrulline1 Publication
    Modified residuei218 – 2181Citrulline1 Publication
    Modified residuei372 – 3721Citrulline1 Publication
    Modified residuei374 – 3741Citrulline1 Publication
    Modified residuei383 – 3831Citrulline1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Citrullination

    Proteomic databases

    PaxDbiQ9UM07.
    PRIDEiQ9UM07.

    PTM databases

    PhosphoSiteiQ9UM07.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiQ9UM07.
    BgeeiQ9UM07.
    CleanExiHS_PADI4.
    GenevestigatoriQ9UM07.

    Organism-specific databases

    HPAiHPA017007.

    Interactioni

    Protein-protein interaction databases

    BioGridi117111. 9 interactions.
    IntActiQ9UM07. 1 interaction.
    STRINGi9606.ENSP00000364597.

    Structurei

    Secondary structure

    1
    663
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Beta strandi11 – 133
    Beta strandi15 – 206
    Beta strandi23 – 286
    Beta strandi39 – 446
    Beta strandi48 – 514
    Beta strandi77 – 826
    Beta strandi85 – 884
    Beta strandi90 – 989
    Beta strandi101 – 11818
    Beta strandi123 – 1264
    Beta strandi148 – 1503
    Beta strandi158 – 1603
    Helixi165 – 1673
    Beta strandi168 – 1703
    Helixi174 – 1796
    Beta strandi180 – 18910
    Helixi193 – 1953
    Beta strandi196 – 2027
    Turni205 – 2073
    Helixi208 – 2103
    Beta strandi211 – 2155
    Beta strandi226 – 2305
    Beta strandi233 – 2386
    Beta strandi242 – 25312
    Beta strandi263 – 27311
    Beta strandi277 – 2793
    Beta strandi282 – 29312
    Beta strandi305 – 3106
    Helixi317 – 32913
    Beta strandi333 – 3364
    Helixi339 – 3424
    Turni348 – 3503
    Beta strandi351 – 3599
    Beta strandi362 – 3698
    Turni375 – 3773
    Helixi378 – 3836
    Beta strandi389 – 3935
    Beta strandi397 – 3993
    Helixi403 – 4053
    Helixi407 – 4093
    Beta strandi410 – 4123
    Beta strandi415 – 4184
    Beta strandi421 – 4233
    Beta strandi428 – 4325
    Helixi445 – 4539
    Helixi455 – 4573
    Beta strandi460 – 4634
    Beta strandi467 – 4693
    Helixi472 – 4743
    Beta strandi476 – 4805
    Beta strandi482 – 4843
    Beta strandi486 – 4938
    Helixi494 – 50613
    Turni507 – 5115
    Turni515 – 5173
    Beta strandi519 – 5213
    Helixi526 – 5316
    Helixi533 – 55725
    Helixi561 – 5633
    Beta strandi564 – 5685
    Beta strandi571 – 5733
    Helixi575 – 5773
    Beta strandi579 – 5835
    Beta strandi590 – 5923
    Beta strandi595 – 5995
    Beta strandi607 – 6104
    Helixi611 – 62010
    Helixi621 – 6233
    Beta strandi626 – 6305
    Turni633 – 6364
    Helixi637 – 6393
    Turni643 – 6464
    Beta strandi647 – 6515
    Helixi658 – 6603

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    DisProtiDP00321.
    ProteinModelPortaliQ9UM07.
    SMRiQ9UM07. Positions 2-663.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UM07.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the protein arginine deiminase family.Curated

    Phylogenomic databases

    eggNOGiNOG42085.
    HOGENOMiHOG000220908.
    HOVERGENiHBG053016.
    InParanoidiQ9UM07.
    KOiK01481.
    OMAiVLGPQQP.
    OrthoDBiEOG7P5T09.
    PhylomeDBiQ9UM07.
    TreeFamiTF331952.

    Family and domain databases

    InterProiIPR008972. Cupredoxin.
    IPR004303. PAD.
    IPR013530. PAD_C.
    IPR013732. PAD_N.
    IPR013733. Prot_Arg_deaminase_cen_dom.
    IPR016296. Protein-arginine_deiminase_sub.
    [Graphical view]
    PANTHERiPTHR10837. PTHR10837. 1 hit.
    PfamiPF03068. PAD. 1 hit.
    PF08527. PAD_M. 1 hit.
    PF08526. PAD_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001247. Protein-arginine_deiminase. 1 hit.
    SUPFAMiSSF110083. SSF110083. 1 hit.
    SSF49503. SSF49503. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9UM07-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQGTLIRVT PEQPTHAVCV LGTLTQLDIC SSAPEDCTSF SINASPGVVV    50
    DIAHGPPAKK KSTGSSTWPL DPGVEVTLTM KVASGSTGDQ KVQISYYGPK 100
    TPPVKALLYL TGVEISLCAD ITRTGKVKPT RAVKDQRTWT WGPCGQGAIL 150
    LVNCDRDNLE SSAMDCEDDE VLDSEDLQDM SLMTLSTKTP KDFFTNHTLV 200
    LHVARSEMDK VRVFQATRGK LSSKCSVVLG PKWPSHYLMV PGGKHNMDFY 250
    VEALAFPDTD FPGLITLTIS LLDTSNLELP EAVVFQDSVV FRVAPWIMTP 300
    NTQPPQEVYA CSIFENEDFL KSVTTLAMKA KCKLTICPEE ENMDDQWMQD 350
    EMEIGYIQAP HKTLPVVFDS PRNRGLKEFP IKRVMGPDFG YVTRGPQTGG 400
    ISGLDSFGNL EVSPPVTVRG KEYPLGRILF GDSCYPSNDS RQMHQALQDF 450
    LSAQQVQAPV KLYSDWLSVG HVDEFLSFVP APDRKGFRLL LASPRSCYKL 500
    FQEQQNEGHG EALLFEGIKK KKQQKIKNIL SNKTLREHNS FVERCIDWNR 550
    ELLKRELGLA ESDIIDIPQL FKLKEFSKAE AFFPNMVNML VLGKHLGIPK 600
    PFGPVINGRC CLEEKVCSLL EPLGLQCTFI NDFFTYHIRH GEVHCGTNVR 650
    RKPFSFKWWN MVP 663
    Length:663
    Mass (Da):74,079
    Last modified:May 18, 2010 - v2
    Checksum:i79D7AF7B3D307A3B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti149 – 1491I → V in BAF83196. (PubMed:14702039)Curated
    Sequence conflicti247 – 2471M → T in BAG37357. (PubMed:14702039)Curated
    Sequence conflicti657 – 6571K → E in BAF83196. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81R → H.
    Corresponds to variant rs35381732 [ dbSNP | Ensembl ].
    VAR_053560
    Natural varianti55 – 551G → S Does not catalytic activity. 2 Publications
    Corresponds to variant rs11203366 [ dbSNP | Ensembl ].
    VAR_020639
    Natural varianti79 – 791T → M.
    Corresponds to variant rs35809521 [ dbSNP | Ensembl ].
    VAR_053561
    Natural varianti82 – 821V → A Does not catalytic activity. 2 Publications
    Corresponds to variant rs11203367 [ dbSNP | Ensembl ].
    VAR_020640
    Natural varianti89 – 891D → N.1 Publication
    VAR_027401
    Natural varianti102 – 1021P → T.1 Publication
    Corresponds to variant rs34309058 [ dbSNP | Ensembl ].
    VAR_027402
    Natural varianti112 – 1121G → A Does not catalytic activity. 2 Publications
    Corresponds to variant rs874881 [ dbSNP | Ensembl ].
    VAR_020641
    Natural varianti131 – 1311R → T.1 Publication
    Corresponds to variant rs12733102 [ dbSNP | Ensembl ].
    VAR_027403
    Natural varianti164 – 1641M → T.
    Corresponds to variant rs11588132 [ dbSNP | Ensembl ].
    VAR_027404
    Natural varianti260 – 2601D → N.
    Corresponds to variant rs35903413 [ dbSNP | Ensembl ].
    VAR_053562
    Natural varianti275 – 2751S → F.1 Publication
    Corresponds to variant rs1748020 [ dbSNP | Ensembl ].
    VAR_020642

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017919 mRNA. Translation: BAA84542.1.
    AJ549502 Genomic DNA. Translation: CAE47743.1.
    AK290507 mRNA. Translation: BAF83196.1.
    AK314839 mRNA. Translation: BAG37357.1.
    AL590644, AC004824 Genomic DNA. Translation: CAH73167.1.
    BC025718 mRNA. Translation: AAH25718.1.
    CCDSiCCDS180.1.
    RefSeqiNP_036519.2. NM_012387.2.
    UniGeneiHs.522969.

    Genome annotation databases

    EnsembliENST00000375448; ENSP00000364597; ENSG00000159339.
    GeneIDi23569.
    KEGGihsa:23569.
    UCSCiuc001baj.2. human.

    Polymorphism databases

    DMDMi296439260.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017919 mRNA. Translation: BAA84542.1 .
    AJ549502 Genomic DNA. Translation: CAE47743.1 .
    AK290507 mRNA. Translation: BAF83196.1 .
    AK314839 mRNA. Translation: BAG37357.1 .
    AL590644 , AC004824 Genomic DNA. Translation: CAH73167.1 .
    BC025718 mRNA. Translation: AAH25718.1 .
    CCDSi CCDS180.1.
    RefSeqi NP_036519.2. NM_012387.2.
    UniGenei Hs.522969.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WD8 X-ray 2.80 A 1-663 [» ]
    1WD9 X-ray 2.60 A 1-663 [» ]
    1WDA X-ray 2.30 A 1-663 [» ]
    2DEW X-ray 2.10 X 1-663 [» ]
    2DEX X-ray 2.10 X 1-663 [» ]
    2DEY X-ray 2.25 X 1-663 [» ]
    2DW5 X-ray 2.30 A 1-663 [» ]
    3APM X-ray 2.50 A 1-663 [» ]
    3APN X-ray 2.70 A 1-663 [» ]
    3B1T X-ray 2.50 A 1-663 [» ]
    3B1U X-ray 2.10 A 1-663 [» ]
    4DKT X-ray 2.98 A 1-663 [» ]
    DisProti DP00321.
    ProteinModelPortali Q9UM07.
    SMRi Q9UM07. Positions 2-663.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117111. 9 interactions.
    IntActi Q9UM07. 1 interaction.
    STRINGi 9606.ENSP00000364597.

    Chemistry

    BindingDBi Q9UM07.
    ChEMBLi CHEMBL6111.
    DrugBanki DB00155. L-Citrulline.

    PTM databases

    PhosphoSitei Q9UM07.

    Polymorphism databases

    DMDMi 296439260.

    Proteomic databases

    PaxDbi Q9UM07.
    PRIDEi Q9UM07.

    Protocols and materials databases

    DNASUi 23569.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375448 ; ENSP00000364597 ; ENSG00000159339 .
    GeneIDi 23569.
    KEGGi hsa:23569.
    UCSCi uc001baj.2. human.

    Organism-specific databases

    CTDi 23569.
    GeneCardsi GC01P017634.
    H-InvDB HIX0000182.
    HGNCi HGNC:18368. PADI4.
    HPAi HPA017007.
    MIMi 180300. phenotype.
    605347. gene.
    neXtProti NX_Q9UM07.
    PharmGKBi PA32903.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42085.
    HOGENOMi HOG000220908.
    HOVERGENi HBG053016.
    InParanoidi Q9UM07.
    KOi K01481.
    OMAi VLGPQQP.
    OrthoDBi EOG7P5T09.
    PhylomeDBi Q9UM07.
    TreeFami TF331952.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS08389-MONOMER.
    BRENDAi 3.5.3.15. 2681.

    Miscellaneous databases

    EvolutionaryTracei Q9UM07.
    GeneWikii PADI4.
    GenomeRNAii 23569.
    NextBioi 35463997.
    PROi Q9UM07.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UM07.
    Bgeei Q9UM07.
    CleanExi HS_PADI4.
    Genevestigatori Q9UM07.

    Family and domain databases

    InterProi IPR008972. Cupredoxin.
    IPR004303. PAD.
    IPR013530. PAD_C.
    IPR013732. PAD_N.
    IPR013733. Prot_Arg_deaminase_cen_dom.
    IPR016296. Protein-arginine_deiminase_sub.
    [Graphical view ]
    PANTHERi PTHR10837. PTHR10837. 1 hit.
    Pfami PF03068. PAD. 1 hit.
    PF08527. PAD_M. 1 hit.
    PF08526. PAD_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001247. Protein-arginine_deiminase. 1 hit.
    SUPFAMi SSF110083. SSF110083. 1 hit.
    SSF49503. SSF49503. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1alpha,25-dihydroxyvitamin D(3)."
      Nakashima K., Hagiwara T., Ishigami A., Nagata S., Asaga H., Kuramoto M., Senshu T., Yamada M.
      J. Biol. Chem. 274:27786-27792(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-55; ALA-82 AND ALA-112.
    2. "Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6."
      Chavanas S., Mechin M.-C., Takahara H., Kawada A., Nachat R., Serre G., Simon M.
      Gene 330:19-27(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-275.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS SER-55; ALA-82 AND ALA-112.
      Tissue: Pancreas and Spleen.
    6. "Immunocytochemical localization of peptidylarginine deiminase in human eosinophils and neutrophils."
      Asaga H., Nakashima K., Senshu T., Ishigami A., Yamada M.
      J. Leukoc. Biol. 70:46-51(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    7. Cited for: INVOLVEMENT IN RA.
    8. Cited for: FUNCTION.
    9. Cited for: FUNCTION.
    10. Cited for: SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
    11. "Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination."
      Lee Y.-H., Coonrod S.A., Kraus W.L., Jelinek M.A., Stallcup M.R.
      Proc. Natl. Acad. Sci. U.S.A. 102:3611-3616(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CITRULLINATION OF EP300.
    12. "Histone deimination as a response to inflammatory stimuli in neutrophils."
      Neeli I., Khan S.N., Radic M.
      J. Immunol. 180:1895-1902(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Autocitrullination of human peptidyl arginine deiminase type 4 regulates protein citrullination during cell activation."
      Andrade F., Darrah E., Gucek M., Cole R.N., Rosen A., Zhu X.
      Arthritis Rheum. 62:1630-1640(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CITRULLINATION AT ARG-205; ARG-212; ARG-218; ARG-372; ARG-374 AND ARG-383.
    14. "Structural basis for Ca(2+)-induced activation of human PAD4."
      Arita K., Hashimoto H., Shimizu T., Nakashima K., Yamada M., Sato M.
      Nat. Struct. Mol. Biol. 11:777-783(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH CALCIUM AND HISTONE H3 N-TERMINUS, X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CALCIUM AND HISTONE H4 N-TERMINUS, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CALCIUM AND BENZOYL-ARGININE AMIDE, ACTIVE SITE, MUTAGENESIS OF ARG-374 AND CYS-645.
    15. "Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4."
      Arita K., Shimizu T., Hashimoto H., Hidaka Y., Yamada M., Sato M.
      Proc. Natl. Acad. Sci. U.S.A. 103:5291-5296(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH CALCIUM AND HISTONE H3 AND H4 N-TERMINUS, COFACTOR, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-374.
    16. "Inhibitors and inactivators of protein arginine deiminase 4: functional and structural characterization."
      Luo Y., Arita K., Bhatia M., Knuckley B., Lee Y.H., Stallcup M.R., Sato M., Thompson P.R.
      Biochemistry 45:11727-11736(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CALCIUM, COFACTOR, ENZYME REGULATION.
    17. "Structural and biochemical analyses of the human PAD4 variant encoded by a functional haplotype gene."
      Horikoshi N., Tachiwana H., Saito K., Osakabe A., Sato M., Yamada M., Akashi S., Nishimura Y., Kagawa W., Kurumizaka H.
      Acta Crystallogr. D 67:112-118(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANTS SER-55; ALA-82 AND ALA-112.
    18. "The development of N-alpha-(2-carboxyl)benzoyl-N(5)-(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) as second generation protein arginine deiminase (PAD) inhibitors."
      Causey C.P., Jones J.E., Slack J.L., Kamei D., Jones L.E., Subramanian V., Knuckley B., Ebrahimi P., Chumanevich A.A., Luo Y., Hashimoto H., Sato M., Hofseth L.J., Thompson P.R.
      J. Med. Chem. 54:6919-6935(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH INHIBITOR, ENZYME REGULATION, MUTAGENESIS OF GLN-346; ARG-374 AND ARG-639.
    19. "Synthesis and screening of a haloacetamidine containing library to identify PAD4 selective inhibitors."
      Jones J.E., Slack J.L., Fang P., Zhang X., Subramanian V., Causey C.P., Coonrod S.A., Guo M., Thompson P.R.
      ACS Chem. Biol. 7:160-165(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.98 ANGSTROMS) IN COMPLEX WITH TDFA, ENZYME REGULATION.
    20. "High variability of peptidylarginine deiminase 4 (PADI4) in a healthy white population: characterization of six new variants of PADI4 exons 2-4 by a novel haplotype-specific sequencing-based approach."
      Hoppe B., Heymann G.A., Tolou F., Kiesewetter H., Doerner T., Salama A.
      J. Mol. Med. 82:762-767(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ASN-89; THR-102 AND THR-131.

    Entry informationi

    Entry nameiPADI4_HUMAN
    AccessioniPrimary (citable) accession number: Q9UM07
    Secondary accession number(s): A8K392
    , B2RBW0, Q5VTZ8, Q70SX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 of the sequence. [Complete history]
    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.

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

    External Data

    Dasty 3