Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein-arginine deiminase type-4 (EC 3.5.3.15) (HL-60 PAD) (Peptidylarginine deiminase IV) (Protein-arginine deiminase type IV)

 PADI4_HUMAN             Reviewed;         663 AA.
Q9UM07; A8K392; B2RBW0; Q5VTZ8; Q70SX4;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
22-NOV-2017, entry version 161.
RecName: Full=Protein-arginine deiminase type-4;
EC=3.5.3.15;
AltName: Full=HL-60 PAD;
AltName: Full=Peptidylarginine deiminase IV;
AltName: Full=Protein-arginine deiminase type IV;
Name=PADI4; Synonyms=PAD4, PADI5, PDI5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-55; ALA-82 AND ALA-112.
PubMed=10488123; DOI=10.1074/jbc.274.39.27786;
Nakashima K., Hagiwara T., Ishigami A., Nagata S., Asaga H.,
Kuramoto M., Senshu T., Yamada M.;
"Molecular characterization of peptidylarginine deiminase in HL-60
cells induced by retinoic acid and 1alpha,25-dihydroxyvitamin D(3).";
J. Biol. Chem. 274:27786-27792(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-275.
PubMed=15087120; DOI=10.1016/j.gene.2003.12.038;
Chavanas S., Mechin M.-C., Takahara H., Kawada A., Nachat R.,
Serre G., Simon M.;
"Comparative analysis of the mouse and human peptidylarginine
deiminase gene clusters reveals highly conserved non-coding segments
and a new human gene, PADI6.";
Gene 330:19-27(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-55; ALA-82
AND ALA-112.
TISSUE=Pancreas, and Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=11435484;
Asaga H., Nakashima K., Senshu T., Ishigami A., Yamada M.;
"Immunocytochemical localization of peptidylarginine deiminase in
human eosinophils and neutrophils.";
J. Leukoc. Biol. 70:46-51(2001).
[7]
INVOLVEMENT IN RA.
PubMed=12833157; DOI=10.1038/ng1206;
Suzuki A., Yamada R., Chang X., Tokuhiro S., Sawada T., Suzuki M.,
Nagasaki M., Nakayama-Hamada M., Kawaida R., Ono M., Ohtsuki M.,
Furukawa H., Yoshino S., Yukioka M., Tohma S., Matsubara T.,
Wakitani S., Teshima R., Nishioka Y., Sekine A., Iida A.,
Takahashi A., Tsunoda T., Nakamura Y., Yamamoto K.;
"Functional haplotypes of PADI4, encoding citrullinating enzyme
peptidylarginine deiminase 4, are associated with rheumatoid
arthritis.";
Nat. Genet. 34:395-402(2003).
[8]
FUNCTION.
PubMed=15339660; DOI=10.1016/j.cell.2004.08.020;
Cuthbert G.L., Daujat S., Snowden A.W., Erdjument-Bromage H.,
Hagiwara T., Yamada M., Schneider R., Gregory P.D., Tempst P.,
Bannister A.J., Kouzarides T.;
"Histone deimination antagonizes arginine methylation.";
Cell 118:545-553(2004).
[9]
FUNCTION.
PubMed=15345777; DOI=10.1126/science.1101400;
Wang Y., Wysocka J., Sayegh J., Lee Y.-H., Perlin J.R., Leonelli L.,
Sonbuchner L.S., McDonald C.H., Cook R.G., Dou Y., Roeder R.G.,
Clarke S., Stallcup M.R., Allis C.D., Coonrod S.A.;
"Human PAD4 regulates histone arginine methylation levels via
demethylimination.";
Science 306:279-283(2004).
[10]
SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
PubMed=15629448; DOI=10.1016/j.bbrc.2004.11.152;
Nakayama-Hamada M., Suzuki A., Kubota K., Takazawa T., Ohsaka M.,
Kawaida R., Ono M., Kasuya A., Furukawa H., Yamada R., Yamamoto K.;
"Comparison of enzymatic properties between hPADI2 and hPADI4.";
Biochem. Biophys. Res. Commun. 327:192-200(2005).
[11]
FUNCTION IN CITRULLINATION OF EP300.
PubMed=15731352; DOI=10.1073/pnas.0407159102;
Lee Y.-H., Coonrod S.A., Kraus W.L., Jelinek M.A., Stallcup M.R.;
"Regulation of coactivator complex assembly and function by protein
arginine methylation and demethylimination.";
Proc. Natl. Acad. Sci. U.S.A. 102:3611-3616(2005).
[12]
FUNCTION.
PubMed=18209087; DOI=10.4049/jimmunol.180.3.1895;
Neeli I., Khan S.N., Radic M.;
"Histone deimination as a response to inflammatory stimuli in
neutrophils.";
J. Immunol. 180:1895-1902(2008).
[13]
CITRULLINATION AT ARG-205; ARG-212; ARG-218; ARG-372; ARG-374 AND
ARG-383.
PubMed=20201080; DOI=10.1002/art.27439;
Andrade F., Darrah E., Gucek M., Cole R.N., Rosen A., Zhu X.;
"Autocitrullination of human peptidyl arginine deiminase type 4
regulates protein citrullination during cell activation.";
Arthritis Rheum. 62:1630-1640(2010).
[14]
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, AND MUTAGENESIS OF ARG-374 AND CYS-645.
PubMed=15247907; DOI=10.1038/nsmb799;
Arita K., Hashimoto H., Shimizu T., Nakashima K., Yamada M., Sato M.;
"Structural basis for Ca(2+)-induced activation of human PAD4.";
Nat. Struct. Mol. Biol. 11:777-783(2004).
[15]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH CALCIUM AND
HISTONE H3 AND H4 N-TERMINUS, COFACTOR, FUNCTION, CATALYTIC ACTIVITY,
AND MUTAGENESIS OF ARG-374.
PubMed=16567635; DOI=10.1073/pnas.0509639103;
Arita K., Shimizu T., Hashimoto H., Hidaka Y., Yamada M., Sato M.;
"Structural basis for histone N-terminal recognition by human
peptidylarginine deiminase 4.";
Proc. Natl. Acad. Sci. U.S.A. 103:5291-5296(2006).
[16]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CALCIUM,
COFACTOR, AND ENZYME REGULATION.
PubMed=17002273; DOI=10.1021/bi061180d;
Luo Y., Arita K., Bhatia M., Knuckley B., Lee Y.H., Stallcup M.R.,
Sato M., Thompson P.R.;
"Inhibitors and inactivators of protein arginine deiminase 4:
functional and structural characterization.";
Biochemistry 45:11727-11736(2006).
[17]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
AND CHARACTERIZATION OF VARIANTS SER-55; ALA-82 AND ALA-112.
PubMed=21245532; DOI=10.1107/S0907444910051711;
Horikoshi N., Tachiwana H., Saito K., Osakabe A., Sato M., Yamada M.,
Akashi S., Nishimura Y., Kagawa W., Kurumizaka H.;
"Structural and biochemical analyses of the human PAD4 variant encoded
by a functional haplotype gene.";
Acta Crystallogr. D 67:112-118(2011).
[18]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH INHIBITOR,
ENZYME REGULATION, AND MUTAGENESIS OF GLN-346; ARG-374 AND ARG-639.
PubMed=21882827; DOI=10.1021/jm2008985;
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.;
"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.";
J. Med. Chem. 54:6919-6935(2011).
[19]
X-RAY CRYSTALLOGRAPHY (2.98 ANGSTROMS) IN COMPLEX WITH TDFA, AND
ENZYME REGULATION.
PubMed=22004374; DOI=10.1021/cb200258q;
Jones J.E., Slack J.L., Fang P., Zhang X., Subramanian V.,
Causey C.P., Coonrod S.A., Guo M., Thompson P.R.;
"Synthesis and screening of a haloacetamidine containing library to
identify PAD4 selective inhibitors.";
ACS Chem. Biol. 7:160-165(2012).
[20]
VARIANTS ASN-89; THR-102 AND THR-131.
PubMed=15338034; DOI=10.1007/s00109-004-0584-6;
Hoppe B., Heymann G.A., Tolou F., Kiesewetter H., Doerner T.,
Salama A.;
"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.";
J. Mol. Med. 82:762-767(2004).
-!- FUNCTION: 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. {ECO:0000269|PubMed:15339660,
ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:15731352,
ECO:0000269|PubMed:16567635, ECO:0000269|PubMed:18209087,
ECO:0000269|PubMed:21245532}.
-!- CATALYTIC ACTIVITY: Protein L-arginine + H(2)O = protein L-
citrulline + NH(3). {ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:21245532}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:15629448,
ECO:0000269|PubMed:16567635, ECO:0000269|PubMed:17002273};
Note=Binds 5 Ca(2+) ions per subunit.
{ECO:0000269|PubMed:15629448, ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273};
-!- ENZYME REGULATION: 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). {ECO:0000269|PubMed:17002273,
ECO:0000269|PubMed:21882827, ECO:0000269|PubMed:22004374}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.055 mM for fibrinogen {ECO:0000269|PubMed:15629448};
KM=0.064 mM for filaggrin {ECO:0000269|PubMed:15629448};
Vmax=33.2 umol/h/mg enzyme toward fibrinogen
{ECO:0000269|PubMed:15629448};
Vmax=8.0 umol/h/mg enzyme toward filaggrin
{ECO:0000269|PubMed:15629448};
pH dependence:
Optimum pH is 6.5-9.0. {ECO:0000269|PubMed:15629448};
-!- INTERACTION:
Q6LES2:ANXA4; NbExp=5; IntAct=EBI-1042511, EBI-10250835;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasmic granule.
Note=Cytoplasmic granules of eosinophils and neutrophils.
-!- TISSUE SPECIFICITY: Expressed in eosinophils and neutrophils, not
expressed in peripheral monocytes or lymphocytes.
{ECO:0000269|PubMed:11435484}.
-!- PTM: Autocitrullination at Arg-372 and Arg-374 inactivates the
enzyme.
-!- DISEASE: 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. {ECO:0000269|PubMed:12833157}. 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).
{ECO:0000269|PubMed:12833157, ECO:0000269|PubMed:21245532}.
-!- SIMILARITY: Belongs to the protein arginine deiminase family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB017919; BAA84542.1; -; mRNA.
EMBL; AJ549502; CAE47743.1; -; Genomic_DNA.
EMBL; AK290507; BAF83196.1; -; mRNA.
EMBL; AK314839; BAG37357.1; -; mRNA.
EMBL; AL590644; CAH73167.1; -; Genomic_DNA.
EMBL; AC004824; CAH73167.1; JOINED; Genomic_DNA.
EMBL; BC025718; AAH25718.1; -; mRNA.
CCDS; CCDS180.1; -.
RefSeq; NP_036519.2; NM_012387.2.
UniGene; Hs.522969; -.
PDB; 1WD8; X-ray; 2.80 A; A=1-663.
PDB; 1WD9; X-ray; 2.60 A; A=1-663.
PDB; 1WDA; X-ray; 2.30 A; A=1-663.
PDB; 2DEW; X-ray; 2.10 A; X=1-663.
PDB; 2DEX; X-ray; 2.10 A; X=1-663.
PDB; 2DEY; X-ray; 2.25 A; X=1-663.
PDB; 2DW5; X-ray; 2.30 A; A=1-663.
PDB; 3APM; X-ray; 2.50 A; A=1-663.
PDB; 3APN; X-ray; 2.70 A; A=1-663.
PDB; 3B1T; X-ray; 2.50 A; A=1-663.
PDB; 3B1U; X-ray; 2.10 A; A=1-663.
PDB; 4DKT; X-ray; 2.98 A; A=1-663.
PDB; 4X8C; X-ray; 3.10 A; A=1-663.
PDB; 4X8G; X-ray; 3.29 A; A=1-663.
PDB; 5N0M; X-ray; 2.18 A; A=1-663.
PDB; 5N0Y; X-ray; 2.23 A; A=1-663.
PDB; 5N0Z; X-ray; 2.52 A; A=1-663.
PDB; 5N1B; X-ray; 2.90 A; A=1-663.
PDBsum; 1WD8; -.
PDBsum; 1WD9; -.
PDBsum; 1WDA; -.
PDBsum; 2DEW; -.
PDBsum; 2DEX; -.
PDBsum; 2DEY; -.
PDBsum; 2DW5; -.
PDBsum; 3APM; -.
PDBsum; 3APN; -.
PDBsum; 3B1T; -.
PDBsum; 3B1U; -.
PDBsum; 4DKT; -.
PDBsum; 4X8C; -.
PDBsum; 4X8G; -.
PDBsum; 5N0M; -.
PDBsum; 5N0Y; -.
PDBsum; 5N0Z; -.
PDBsum; 5N1B; -.
DisProt; DP00321; -.
ProteinModelPortal; Q9UM07; -.
SMR; Q9UM07; -.
BioGrid; 117111; 13.
DIP; DIP-50397N; -.
IntAct; Q9UM07; 3.
STRING; 9606.ENSP00000364597; -.
BindingDB; Q9UM07; -.
ChEMBL; CHEMBL6111; -.
DrugBank; DB00207; Azithromycin.
DrugBank; DB00254; Doxycycline.
DrugBank; DB00155; L-Citrulline.
DrugBank; DB07449; N-[(1S)-1-(AMINOCARBONYL)-4-(ETHANIMIDOYLAMINO)BUTYL]BENZAMIDE.
DrugBank; DB01082; Streptomycin.
DrugBank; DB00759; Tetracycline.
GuidetoPHARMACOLOGY; 2877; -.
iPTMnet; Q9UM07; -.
PhosphoSitePlus; Q9UM07; -.
BioMuta; PADI4; -.
DMDM; 296439260; -.
MaxQB; Q9UM07; -.
PaxDb; Q9UM07; -.
PeptideAtlas; Q9UM07; -.
PRIDE; Q9UM07; -.
DNASU; 23569; -.
Ensembl; ENST00000375448; ENSP00000364597; ENSG00000159339.
Ensembl; ENST00000628229; ENSP00000487021; ENSG00000280908.
GeneID; 23569; -.
KEGG; hsa:23569; -.
UCSC; uc001baj.3; human.
CTD; 23569; -.
DisGeNET; 23569; -.
EuPathDB; HostDB:ENSG00000159339.13; -.
GeneCards; PADI4; -.
H-InvDB; HIX0000182; -.
HGNC; HGNC:18368; PADI4.
HPA; HPA017007; -.
HPA; HPA042825; -.
MalaCards; PADI4; -.
MIM; 180300; phenotype.
MIM; 605347; gene.
neXtProt; NX_Q9UM07; -.
OpenTargets; ENSG00000159339; -.
PharmGKB; PA32903; -.
eggNOG; ENOG410IF3F; Eukaryota.
eggNOG; ENOG410ZKF3; LUCA.
GeneTree; ENSGT00390000008680; -.
HOGENOM; HOG000220908; -.
HOVERGEN; HBG053016; -.
InParanoid; Q9UM07; -.
KO; K01481; -.
OMA; RVFQATR; -.
OrthoDB; EOG091G02QG; -.
PhylomeDB; Q9UM07; -.
TreeFam; TF331952; -.
BioCyc; MetaCyc:HS08389-MONOMER; -.
BRENDA; 3.5.3.15; 2681.
Reactome; R-HSA-3247509; Chromatin modifying enzymes.
ChiTaRS; PADI4; human.
EvolutionaryTrace; Q9UM07; -.
GeneWiki; PADI4; -.
GenomeRNAi; 23569; -.
PRO; PR:Q9UM07; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000159339; -.
CleanEx; HS_PADI4; -.
ExpressionAtlas; Q9UM07; baseline and differential.
Genevisible; Q9UM07; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0034618; F:arginine binding; IMP:CAFA.
GO; GO:0016990; F:arginine deiminase activity; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
GO; GO:0004668; F:protein-arginine deiminase activity; IDA:UniProtKB.
GO; GO:0019546; P:arginine deiminase pathway; IMP:CAFA.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
GO; GO:0036414; P:histone citrullination; IDA:UniProtKB.
GO; GO:0036413; P:histone H3-R26 citrullination; IDA:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
GO; GO:0018101; P:protein citrullination; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.60.40.1700; -; 1.
InterPro; IPR008972; Cupredoxin.
InterPro; IPR004303; PAD.
InterPro; IPR013530; PAD_C.
InterPro; IPR036556; PAD_central_sf.
InterPro; IPR013732; PAD_N.
InterPro; IPR013733; Prot_Arg_deaminase_cen_dom.
PANTHER; PTHR10837; PTHR10837; 1.
Pfam; PF03068; PAD; 1.
Pfam; PF08527; PAD_M; 1.
Pfam; PF08526; PAD_N; 1.
PIRSF; PIRSF001247; Protein-arginine_deiminase; 1.
SUPFAM; SSF110083; SSF110083; 1.
SUPFAM; SSF49503; SSF49503; 1.
1: Evidence at protein level;
3D-structure; Calcium; Chromatin regulator; Citrullination;
Complete proteome; Cytoplasm; Hydrolase; Immunity; Innate immunity;
Metal-binding; Nucleus; Polymorphism; Reference proteome;
Transcription; Transcription regulation.
CHAIN 1 663 Protein-arginine deiminase type-4.
/FTId=PRO_0000220033.
ACT_SITE 350 350 {ECO:0000269|PubMed:15247907}.
ACT_SITE 471 471 {ECO:0000269|PubMed:15247907}.
ACT_SITE 473 473 {ECO:0000269|PubMed:15247907}.
ACT_SITE 645 645 {ECO:0000269|PubMed:15247907}.
METAL 153 153 Calcium 1. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 155 155 Calcium 1. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 155 155 Calcium 2. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 157 157 Calcium 1. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 157 157 Calcium 2. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 165 165 Calcium 1. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 165 165 Calcium 3; via carbonyl oxygen.
{ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 168 168 Calcium 3. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 170 170 Calcium 3; via carbonyl oxygen.
{ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 176 176 Calcium 1. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 179 179 Calcium 1. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 179 179 Calcium 2. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 349 349 Calcium 4. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 351 351 Calcium 5. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 353 353 Calcium 4. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 369 369 Calcium 5. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 370 370 Calcium 5; via carbonyl oxygen.
{ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 373 373 Calcium 5. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 388 388 Calcium 2. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 407 407 Calcium 4; via carbonyl oxygen.
{ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 410 410 Calcium 4; via carbonyl oxygen.
{ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
METAL 411 411 Calcium 4. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:17002273}.
BINDING 346 346 TDFA Inhibitor.
{ECO:0000269|PubMed:22004374}.
BINDING 369 369 TDFA Inhibitor.
{ECO:0000269|PubMed:22004374}.
BINDING 374 374 Substrate.
BINDING 374 374 TDFA Inhibitor.
{ECO:0000269|PubMed:22004374}.
BINDING 471 471 TDFA Inhibitor.
{ECO:0000269|PubMed:22004374}.
BINDING 473 473 TDFA Inhibitor.
{ECO:0000269|PubMed:22004374}.
BINDING 639 639 Substrate; via carbonyl oxygen.
BINDING 645 645 TDFA Inhibitor.
{ECO:0000269|PubMed:22004374}.
MOD_RES 205 205 Citrulline.
{ECO:0000269|PubMed:20201080}.
MOD_RES 212 212 Citrulline.
{ECO:0000269|PubMed:20201080}.
MOD_RES 218 218 Citrulline.
{ECO:0000269|PubMed:20201080}.
MOD_RES 372 372 Citrulline.
{ECO:0000269|PubMed:20201080}.
MOD_RES 374 374 Citrulline.
{ECO:0000269|PubMed:20201080}.
MOD_RES 383 383 Citrulline.
{ECO:0000269|PubMed:20201080}.
VARIANT 8 8 R -> H (in dbSNP:rs35381732).
/FTId=VAR_053560.
VARIANT 55 55 G -> S (does not catalytic activity;
dbSNP:rs11203366).
{ECO:0000269|PubMed:10488123,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:21245532}.
/FTId=VAR_020639.
VARIANT 79 79 T -> M (in dbSNP:rs35809521).
/FTId=VAR_053561.
VARIANT 82 82 V -> A (does not catalytic activity;
dbSNP:rs11203367).
{ECO:0000269|PubMed:10488123,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:21245532}.
/FTId=VAR_020640.
VARIANT 89 89 D -> N (in dbSNP:rs143187209).
{ECO:0000269|PubMed:15338034}.
/FTId=VAR_027401.
VARIANT 102 102 P -> T (in dbSNP:rs34309058).
{ECO:0000269|PubMed:15338034}.
/FTId=VAR_027402.
VARIANT 112 112 G -> A (does not catalytic activity;
dbSNP:rs874881).
{ECO:0000269|PubMed:10488123,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:21245532}.
/FTId=VAR_020641.
VARIANT 131 131 R -> T (in dbSNP:rs12733102).
{ECO:0000269|PubMed:15338034}.
/FTId=VAR_027403.
VARIANT 164 164 M -> T (in dbSNP:rs11588132).
/FTId=VAR_027404.
VARIANT 260 260 D -> N (in dbSNP:rs35903413).
/FTId=VAR_053562.
VARIANT 275 275 S -> F (in dbSNP:rs1748020).
{ECO:0000269|PubMed:15087120}.
/FTId=VAR_020642.
MUTAGEN 346 346 Q->A: Impaired binding of TDFA Inhibitor.
{ECO:0000269|PubMed:21882827}.
MUTAGEN 374 374 R->A: Strongly reduces enzymatic
activity. {ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:21882827}.
MUTAGEN 374 374 R->Q: Impaired binding of TDFA Inhibitor.
{ECO:0000269|PubMed:15247907,
ECO:0000269|PubMed:16567635,
ECO:0000269|PubMed:21882827}.
MUTAGEN 639 639 R->Q: Impaired binding of TDFA Inhibitor.
{ECO:0000269|PubMed:21882827}.
MUTAGEN 645 645 C->A: Abolishes enzymatic activity.
{ECO:0000269|PubMed:15247907}.
CONFLICT 149 149 I -> V (in Ref. 3; BAF83196).
{ECO:0000305}.
CONFLICT 247 247 M -> T (in Ref. 3; BAG37357).
{ECO:0000305}.
CONFLICT 657 657 K -> E (in Ref. 3; BAF83196).
{ECO:0000305}.
STRAND 4 8 {ECO:0000244|PDB:2DEW}.
STRAND 11 13 {ECO:0000244|PDB:2DEX}.
STRAND 15 20 {ECO:0000244|PDB:2DEW}.
STRAND 23 28 {ECO:0000244|PDB:2DEW}.
HELIX 30 32 {ECO:0000244|PDB:4X8C}.
STRAND 39 44 {ECO:0000244|PDB:2DEW}.
STRAND 48 51 {ECO:0000244|PDB:2DEW}.
STRAND 77 82 {ECO:0000244|PDB:2DEW}.
STRAND 85 88 {ECO:0000244|PDB:1WD8}.
STRAND 90 98 {ECO:0000244|PDB:2DEW}.
STRAND 101 118 {ECO:0000244|PDB:2DEW}.
STRAND 123 125 {ECO:0000244|PDB:5N0M}.
TURN 133 137 {ECO:0000244|PDB:4X8G}.
STRAND 148 150 {ECO:0000244|PDB:2DEW}.
STRAND 158 160 {ECO:0000244|PDB:3B1U}.
HELIX 165 167 {ECO:0000244|PDB:2DEW}.
STRAND 168 170 {ECO:0000244|PDB:2DEW}.
HELIX 174 179 {ECO:0000244|PDB:2DEW}.
STRAND 180 189 {ECO:0000244|PDB:2DEW}.
HELIX 193 195 {ECO:0000244|PDB:2DEW}.
STRAND 196 202 {ECO:0000244|PDB:2DEW}.
TURN 205 207 {ECO:0000244|PDB:2DEW}.
HELIX 208 210 {ECO:0000244|PDB:2DEW}.
STRAND 211 215 {ECO:0000244|PDB:2DEW}.
STRAND 226 230 {ECO:0000244|PDB:2DEW}.
STRAND 233 238 {ECO:0000244|PDB:2DEW}.
STRAND 242 253 {ECO:0000244|PDB:2DEW}.
STRAND 263 273 {ECO:0000244|PDB:2DEW}.
STRAND 277 279 {ECO:0000244|PDB:3B1U}.
STRAND 282 293 {ECO:0000244|PDB:2DEW}.
STRAND 305 310 {ECO:0000244|PDB:2DEW}.
HELIX 317 329 {ECO:0000244|PDB:2DEW}.
STRAND 333 336 {ECO:0000244|PDB:2DEW}.
HELIX 339 342 {ECO:0000244|PDB:2DEW}.
TURN 348 350 {ECO:0000244|PDB:2DEW}.
STRAND 351 359 {ECO:0000244|PDB:2DEW}.
STRAND 362 369 {ECO:0000244|PDB:2DEW}.
TURN 375 377 {ECO:0000244|PDB:2DEW}.
HELIX 378 383 {ECO:0000244|PDB:2DEW}.
STRAND 389 393 {ECO:0000244|PDB:2DEW}.
STRAND 397 399 {ECO:0000244|PDB:2DEW}.
HELIX 403 405 {ECO:0000244|PDB:2DEW}.
HELIX 407 409 {ECO:0000244|PDB:2DEW}.
STRAND 410 412 {ECO:0000244|PDB:2DEW}.
STRAND 415 418 {ECO:0000244|PDB:2DEW}.
STRAND 421 423 {ECO:0000244|PDB:2DEW}.
STRAND 428 432 {ECO:0000244|PDB:2DEW}.
HELIX 445 453 {ECO:0000244|PDB:2DEW}.
HELIX 455 457 {ECO:0000244|PDB:2DEX}.
STRAND 460 463 {ECO:0000244|PDB:2DEW}.
STRAND 467 469 {ECO:0000244|PDB:2DEW}.
HELIX 472 474 {ECO:0000244|PDB:2DEW}.
STRAND 476 480 {ECO:0000244|PDB:2DEW}.
STRAND 482 484 {ECO:0000244|PDB:1WD8}.
STRAND 486 493 {ECO:0000244|PDB:2DEW}.
HELIX 494 506 {ECO:0000244|PDB:2DEW}.
TURN 507 511 {ECO:0000244|PDB:5N0M}.
TURN 515 517 {ECO:0000244|PDB:2DEW}.
STRAND 519 521 {ECO:0000244|PDB:5N0M}.
HELIX 526 531 {ECO:0000244|PDB:2DEW}.
HELIX 533 557 {ECO:0000244|PDB:2DEW}.
HELIX 561 563 {ECO:0000244|PDB:2DEW}.
STRAND 564 568 {ECO:0000244|PDB:2DEW}.
STRAND 571 573 {ECO:0000244|PDB:2DEW}.
HELIX 575 577 {ECO:0000244|PDB:2DEW}.
STRAND 579 583 {ECO:0000244|PDB:2DEW}.
STRAND 586 588 {ECO:0000244|PDB:4X8C}.
STRAND 590 592 {ECO:0000244|PDB:2DEW}.
STRAND 595 599 {ECO:0000244|PDB:2DEW}.
STRAND 607 610 {ECO:0000244|PDB:2DEY}.
HELIX 611 620 {ECO:0000244|PDB:2DEW}.
HELIX 621 623 {ECO:0000244|PDB:2DEW}.
STRAND 626 630 {ECO:0000244|PDB:2DEW}.
TURN 633 636 {ECO:0000244|PDB:2DEW}.
HELIX 637 639 {ECO:0000244|PDB:2DEW}.
TURN 643 646 {ECO:0000244|PDB:2DEW}.
STRAND 647 651 {ECO:0000244|PDB:2DEW}.
HELIX 658 660 {ECO:0000244|PDB:2DEW}.
SEQUENCE 663 AA; 74079 MW; 79D7AF7B3D307A3B CRC64;
MAQGTLIRVT PEQPTHAVCV LGTLTQLDIC SSAPEDCTSF SINASPGVVV DIAHGPPAKK
KSTGSSTWPL DPGVEVTLTM KVASGSTGDQ KVQISYYGPK TPPVKALLYL TGVEISLCAD
ITRTGKVKPT RAVKDQRTWT WGPCGQGAIL LVNCDRDNLE SSAMDCEDDE VLDSEDLQDM
SLMTLSTKTP KDFFTNHTLV LHVARSEMDK VRVFQATRGK LSSKCSVVLG PKWPSHYLMV
PGGKHNMDFY VEALAFPDTD FPGLITLTIS LLDTSNLELP EAVVFQDSVV FRVAPWIMTP
NTQPPQEVYA CSIFENEDFL KSVTTLAMKA KCKLTICPEE ENMDDQWMQD EMEIGYIQAP
HKTLPVVFDS PRNRGLKEFP IKRVMGPDFG YVTRGPQTGG ISGLDSFGNL EVSPPVTVRG
KEYPLGRILF GDSCYPSNDS RQMHQALQDF LSAQQVQAPV KLYSDWLSVG HVDEFLSFVP
APDRKGFRLL LASPRSCYKL FQEQQNEGHG EALLFEGIKK KKQQKIKNIL SNKTLREHNS
FVERCIDWNR ELLKRELGLA ESDIIDIPQL FKLKEFSKAE AFFPNMVNML VLGKHLGIPK
PFGPVINGRC CLEEKVCSLL EPLGLQCTFI NDFFTYHIRH GEVHCGTNVR RKPFSFKWWN
MVP


Related products :

Catalog number Product name Quantity
EIAAB29710 Arginine deiminase-like protein,Egg and embryo abundant PAD,ePAD,Mouse,Mus musculus,Padi5,Padi6,Peptidylarginine deiminase VI,Protein-arginine deiminase type VI,Protein-arginine deiminase type-6
EIAAB29707 Padi4,PAD-R4,Pdi4,Peptidylarginine deiminase IV,Peptidylarginine deiminase type alpha,Protein-arginine deiminase type IV,Protein-arginine deiminase type-4,Rat,Rattus norvegicus
EIAAB29708 HL-60 PAD,Homo sapiens,Human,PADI4,PADI5,PDI5,Peptidylarginine deiminase IV,Protein-arginine deiminase type IV,Protein-arginine deiminase type-4
EIAAB29703 Homo sapiens,Human,KIAA0994,PAD-H19,PADI2,PDI2,Peptidylarginine deiminase II,Protein-arginine deiminase type II,Protein-arginine deiminase type-2
EIAAB29704 Homo sapiens,Human,PADI3,PDI3,Peptidylarginine deiminase III,Protein-arginine deiminase type III,Protein-arginine deiminase type-3
EIAAB29699 Homo sapiens,Human,PADI1,PDI1,Peptidylarginine deiminase I,Protein-arginine deiminase type I,Protein-arginine deiminase type-1
EIAAB29706 Padi3,Pdi3,Peptidylarginine deiminase III,Protein-arginine deiminase type III,Protein-arginine deiminase type-3,Rat,Rattus norvegicus
EIAAB29700 Padi1,PAD-R11,Pdi1,Peptidylarginine deiminase I,Protein-arginine deiminase type I,Protein-arginine deiminase type-1,Rat,Rattus norvegicus
EIAAB29701 Mouse,Mus musculus,Padi2,Pdi,Pdi2,Peptidylarginine deiminase II,Protein-arginine deiminase type II,Protein-arginine deiminase type-2
EIAAB29702 Padi2,Pdi,Pdi2,Peptidylarginine deiminase II,Protein-arginine deiminase type II,Protein-arginine deiminase type-2,Rat,Rattus norvegicus
EIAAB29711 Homo sapiens,Human,PADI6,Peptidylarginine deiminase VI,Protein-arginine deiminase type VI,Protein-arginine deiminase type-6
EIAAB29705 Mouse,Mus musculus,Padi3,Pdi3,Peptidylarginine deiminase III,Protein-arginine deiminase type III,Protein-arginine deiminase type-3
EIAAB29709 Mouse,Mus musculus,Padi4,Pdi4,Peptidylarginine deiminase IV,Protein-arginine deiminase type IV,Protein-arginine deiminase type-4
EIAAB29698 Mouse,Mus musculus,Padi1,Pdi1,Peptidylarginine deiminase I,Protein-arginine deiminase type I,Protein-arginine deiminase type-1
CF07 Protein-Arginine Deiminase Type-4 PADI4 500
EH2500 Protein-arginine deiminase type-2 Elisa Kit 96T
PSB7_RAT Rat ELISA Kit FOR Protein-arginine deiminase type-1 96T
CF07 Protein-Arginine Deiminase Type-4 PADI4 lmg
E0768h Rat ELISA Kit FOR Protein-arginine deiminase type-1 96T
E0110r Human ELISA Kit FOR Protein-arginine deiminase type-1 96T
E1644m Mouse ELISA Kit FOR Protein-arginine deiminase type-3 96T
G4552 Protein-arginine deiminase type-1 (PADI1), Rat, ELISA Kit 96T
G4555 Protein-arginine deiminase type-2 (PADI2), Rat, ELISA Kit 96T
C628 Human Protein-Arginine Deiminase Type-4 PADI4 50
G4558 Protein-arginine deiminase type-3 (PADI3), Rat, ELISA Kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur