SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9UM07

- PADI4_HUMAN

UniProt

Q9UM07 - PADI4_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Protein-arginine deiminase type-4
Gene
PADI4, PADI5, PDI5
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

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 (1 Publication). 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) (1 Publication). Strongly and specifically inhibited by Thr-Asp-F-amidine (TDFA); other members of the family are not inhibited (1 Publication).3 Publications

Kineticsi

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

Vmax=33.2 µmol/h/mg enzyme toward fibrinogen

Vmax=8.0 µmol/h/mg enzyme toward filaggrin

pH dependencei

Optimum pH is 6.5-9.0.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi153 – 1531Calcium 1
Metal bindingi155 – 1551Calcium 1
Metal bindingi155 – 1551Calcium 2
Metal bindingi157 – 1571Calcium 1
Metal bindingi157 – 1571Calcium 2
Metal bindingi165 – 1651Calcium 1
Metal bindingi165 – 1651Calcium 3; via carbonyl oxygen
Metal bindingi168 – 1681Calcium 3
Metal bindingi170 – 1701Calcium 3; via carbonyl oxygen
Metal bindingi176 – 1761Calcium 1
Metal bindingi179 – 1791Calcium 1
Metal bindingi179 – 1791Calcium 2
Binding sitei346 – 3461TDFA Inhibitor
Metal bindingi349 – 3491Calcium 4
Active sitei350 – 35011 Publication
Metal bindingi351 – 3511Calcium 5
Metal bindingi353 – 3531Calcium 4
Metal bindingi369 – 3691Calcium 5
Binding sitei369 – 3691TDFA Inhibitor
Metal bindingi370 – 3701Calcium 5; via carbonyl oxygen
Metal bindingi373 – 3731Calcium 5
Binding sitei374 – 3741Substrate
Binding sitei374 – 3741TDFA Inhibitor
Metal bindingi388 – 3881Calcium 2
Metal bindingi407 – 4071Calcium 4; via carbonyl oxygen
Metal bindingi410 – 4101Calcium 4; via carbonyl oxygen
Metal bindingi411 – 4111Calcium 4
Active sitei471 – 47111 Publication
Binding sitei471 – 4711TDFA Inhibitor
Active sitei473 – 47311 Publication
Binding sitei473 – 4731TDFA Inhibitor
Binding sitei639 – 6391Substrate; via carbonyl oxygen
Active sitei645 – 64511 Publication
Binding sitei645 – 6451TDFA Inhibitor

GO - Molecular functioni

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

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. chromatin modification Source: UniProtKB
  3. chromatin remodeling Source: UniProtKB
  4. histone H3-R26 citrullination Source: UniProtKB
  5. histone 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.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  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.
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 (1 Publication). 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 (1 Publication).1 Publication

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-4
PRO_0000220033Add
BLAST

Amino acid modifications

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

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.
STRINGi9606.ENSP00000364597.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ9UM07.

Family & Domainsi

Sequence similaritiesi

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

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. 3 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. 3 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. 3 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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti149 – 1491I → V in BAF83196. 1 Publication
Sequence conflicti247 – 2471M → T in BAG37357. 1 Publication
Sequence conflicti657 – 6571K → E in BAF83196. 1 Publication

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...

Protein-protein interaction databases

BioGridi 117111. 9 interactions.
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

« 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: July 9, 2014
This is version 125 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

Similar proteinsi