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Q9UM07

- PADI4_HUMAN

UniProt

Q9UM07 - PADI4_HUMAN

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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

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

Ca2+3 PublicationsNote: Binds 5 Ca(2+) 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

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
Complete GO annotation...

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-KW
  2. nucleus Source: UniProtKB
Complete GO annotation...

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

BgeeiQ9UM07.
CleanExiHS_PADI4.
ExpressionAtlasiQ9UM07. baseline and differential.
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 – 85Combined sources
Beta strandi11 – 133Combined sources
Beta strandi15 – 206Combined sources
Beta strandi23 – 286Combined sources
Beta strandi39 – 446Combined sources
Beta strandi48 – 514Combined sources
Beta strandi77 – 826Combined sources
Beta strandi85 – 884Combined sources
Beta strandi90 – 989Combined sources
Beta strandi101 – 11818Combined sources
Beta strandi123 – 1264Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi158 – 1603Combined sources
Helixi165 – 1673Combined sources
Beta strandi168 – 1703Combined sources
Helixi174 – 1796Combined sources
Beta strandi180 – 18910Combined sources
Helixi193 – 1953Combined sources
Beta strandi196 – 2027Combined sources
Turni205 – 2073Combined sources
Helixi208 – 2103Combined sources
Beta strandi211 – 2155Combined sources
Beta strandi226 – 2305Combined sources
Beta strandi233 – 2386Combined sources
Beta strandi242 – 25312Combined sources
Beta strandi263 – 27311Combined sources
Beta strandi277 – 2793Combined sources
Beta strandi282 – 29312Combined sources
Beta strandi305 – 3106Combined sources
Helixi317 – 32913Combined sources
Beta strandi333 – 3364Combined sources
Helixi339 – 3424Combined sources
Turni348 – 3503Combined sources
Beta strandi351 – 3599Combined sources
Beta strandi362 – 3698Combined sources
Turni375 – 3773Combined sources
Helixi378 – 3836Combined sources
Beta strandi389 – 3935Combined sources
Beta strandi397 – 3993Combined sources
Helixi403 – 4053Combined sources
Helixi407 – 4093Combined sources
Beta strandi410 – 4123Combined sources
Beta strandi415 – 4184Combined sources
Beta strandi421 – 4233Combined sources
Beta strandi428 – 4325Combined sources
Helixi445 – 4539Combined sources
Helixi455 – 4573Combined sources
Beta strandi460 – 4634Combined sources
Beta strandi467 – 4693Combined sources
Helixi472 – 4743Combined sources
Beta strandi476 – 4805Combined sources
Beta strandi482 – 4843Combined sources
Beta strandi486 – 4938Combined sources
Helixi494 – 50613Combined sources
Turni507 – 5115Combined sources
Turni515 – 5173Combined sources
Beta strandi519 – 5213Combined sources
Helixi526 – 5316Combined sources
Helixi533 – 55725Combined sources
Helixi561 – 5633Combined sources
Beta strandi564 – 5685Combined sources
Beta strandi571 – 5733Combined sources
Helixi575 – 5773Combined sources
Beta strandi579 – 5835Combined sources
Beta strandi590 – 5923Combined sources
Beta strandi595 – 5995Combined sources
Beta strandi607 – 6104Combined sources
Helixi611 – 62010Combined sources
Helixi621 – 6233Combined sources
Beta strandi626 – 6305Combined sources
Turni633 – 6364Combined sources
Helixi637 – 6393Combined sources
Turni643 – 6464Combined sources
Beta strandi647 – 6515Combined sources
Helixi658 – 6603Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000008680.
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

        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
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:
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.
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:
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 .
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00390000008680.
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

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

Gene expression databases

Bgeei Q9UM07.
CleanExi HS_PADI4.
ExpressionAtlasi Q9UM07. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 128 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