Q9UM07 (PADI4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PADI4
Synonyms:	PADI5, PDI5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	663 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the citrullination/deimination of arginine residues of proteins. Citrullinates histone H3 at 'Arg-8' and/or 'Arg-17' and histone H4 at 'Arg-3', which prevents their methylation by CARM1 and HRMT1L2/PRMT1 and represses transcription. Citrullinates EP300/P300 at 'Arg-2142', which favors its interaction with NCOA2/GRIP1. Ref.7 Ref.8
Catalytic activity	Protein L-arginine + H2O = protein L-citrulline + NH3.
Cofactor	Binds 5 calcium ions per subunit. Ref.9
Subcellular location	Cytoplasm. Nucleus. Cytoplasmic granule. Note: Cytoplasmic granules of eosinophils and neutrophils. Ref.5 Ref.9
Tissue specificity	Expressed in eosinophils and neutrophils, not expressed in peripheral monocytes or lymphocytes. Ref.5
Post-translational modification	Autocitrullination at Arg-372 and Arg-374 inactivates the enzyme.
Involvement in 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. Note: The gene represented in this entry may be involved in disease pathogenesis. It could play a role in increasing citrullination of proteins in rheumatoid arthritis synovial tissues, leading, in a cytokine-rich milieu, to a break in tolerance to citrullinated peptides processed and presented in the appropriate HLA context. Ref.6
Sequence similarities	Belongs to the protein arginine deiminase family.
Biophysicochemical properties	Kinetic parameters: KM=0.055 mM for fibrinogen Ref.9 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 dependence: Optimum pH is 6.5-9.0.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	Calcium Metal-binding
Molecular function	Chromatin regulator Hydrolase
PTM	Citrullination
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein modification process Traceable author statement Ref.1. Source: ProtInc chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-citrulline biosynthetic process from peptidyl-arginine Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro protein-arginine deiminase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 663

663

Protein-arginine deiminase type-4

PRO_0000220033

Sites

Active site

350

1

Active site

471

1

Active site

473

1

Active site

645

1

Metal binding

153

1

Calcium 1

Metal binding

155

1

Calcium 1

Metal binding

155

1

Calcium 2

Metal binding

157

1

Calcium 1

Metal binding

157

1

Calcium 2

Metal binding

165

1

Calcium 1

Metal binding

165

1

Calcium 3; via carbonyl oxygen

Metal binding

168

1

Calcium 3

Metal binding

170

1

Calcium 3; via carbonyl oxygen

Metal binding

176

1

Calcium 1

Metal binding

179

1

Calcium 1

Metal binding

179

1

Calcium 2

Metal binding

349

1

Calcium 4

Metal binding

351

1

Calcium 5

Metal binding

353

1

Calcium 4

Metal binding

369

1

Calcium 5

Metal binding

370

1

Calcium 5; via carbonyl oxygen

Metal binding

373

1

Calcium 5

Metal binding

388

1

Calcium 2

Metal binding

407

1

Calcium 4; via carbonyl oxygen

Metal binding

410

1

Calcium 4; via carbonyl oxygen

Metal binding

411

1

Calcium 4

Binding site

374

1

Substrate

Binding site

639

1

Substrate; via carbonyl oxygen

Amino acid modifications

Modified residue

205

1

Citrulline

Modified residue

212

1

Citrulline

Modified residue

218

1

Citrulline

Modified residue

372

1

Citrulline

Modified residue

374

1

Citrulline

Modified residue

383

1

Citrulline

Natural variations

Natural variant

8

1

R → H.
Corresponds to variant rs35381732 [ dbSNP | Ensembl ].

VAR_053560

Natural variant

55

1

G → S. Ref.1 Ref.4
Corresponds to variant rs11203366 [ dbSNP | Ensembl ].

VAR_020639

Natural variant

79

1

T → M.
Corresponds to variant rs35809521 [ dbSNP | Ensembl ].

VAR_053561

Natural variant

82

1

V → A. Ref.1 Ref.4
Corresponds to variant rs11203367 [ dbSNP | Ensembl ].

VAR_020640

Natural variant

89

1

D → N. Ref.13

VAR_027401

Natural variant

102

1

P → T. Ref.13
Corresponds to variant rs34309058 [ dbSNP | Ensembl ].

VAR_027402

Natural variant

112

1

G → A. Ref.1 Ref.4
Corresponds to variant rs874881 [ dbSNP | Ensembl ].

VAR_020641

Natural variant

131

1

R → T. Ref.13
Corresponds to variant rs12733102 [ dbSNP | Ensembl ].

VAR_027403

Natural variant

164

1

M → T.
Corresponds to variant rs11588132 [ dbSNP | Ensembl ].

VAR_027404

Natural variant

260

1

D → N.
Corresponds to variant rs35903413 [ dbSNP | Ensembl ].

VAR_053562

Natural variant

275

1

S → F. Ref.2
Corresponds to variant rs1748020 [ dbSNP | Ensembl ].

VAR_020642

Experimental info

Mutagenesis

374

1

R → A: Strongly reduces enzymatic activity. Ref.12

Mutagenesis

645

1

C → A: Abolishes enzymatic activity. Ref.12

Secondary structure

1

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663

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Beta strand

11 – 13

3

Beta strand

15 – 20

6

Beta strand

23 – 28

6

Beta strand

39 – 44

6

Beta strand

48 – 51

4

Beta strand

77 – 82

6

Beta strand

85 – 88

4

Beta strand

90 – 98

9

Beta strand

101 – 118

18

Beta strand

123 – 126

4

Beta strand

148 – 150

3

Beta strand

158 – 160

3

Helix

165 – 167

3

Beta strand

168 – 170

3

Helix

174 – 179

6

Beta strand

180 – 189

10

Helix

193 – 195

3

Beta strand

196 – 202

7

Turn

205 – 207

3

Helix

208 – 210

3

Beta strand

211 – 215

5

Beta strand

226 – 230

5

Beta strand

233 – 238

6

Beta strand

242 – 253

12

Beta strand

263 – 273

11

Beta strand

277 – 279

3

Beta strand

282 – 293

12

Beta strand

305 – 310

6

Helix

317 – 329

13

Beta strand

333 – 336

4

Helix

339 – 342

4

Turn

348 – 350

3

Beta strand

351 – 359

9

Beta strand

362 – 369

8

Turn

375 – 377

3

Helix

378 – 383

6

Beta strand

389 – 393

5

Beta strand

397 – 399

3

Helix

403 – 405

3

Helix

407 – 409

3

Beta strand

410 – 412

3

Beta strand

415 – 418

4

Beta strand

421 – 423

3

Beta strand

428 – 432

5

Helix

445 – 453

9

Helix

455 – 457

3

Beta strand

460 – 463

4

Beta strand

467 – 469

3

Helix

472 – 474

3

Beta strand

476 – 480

5

Beta strand

482 – 484

3

Beta strand

486 – 493

8

Helix

494 – 506

13

Turn

507 – 511

5

Turn

515 – 517

3

Beta strand

519 – 521

3

Helix

526 – 531

6

Helix

533 – 557

25

Helix

561 – 563

3

Beta strand

564 – 568

5

Beta strand

571 – 573

3

Helix

575 – 577

3

Beta strand

579 – 583

5

Beta strand

590 – 592

3

Beta strand

595 – 599

5

Beta strand

607 – 610

4

Helix

611 – 620

10

Helix

621 – 623

3

Beta strand

626 – 630

5

Turn

633 – 636

4

Helix

637 – 639

3

Turn

643 – 646

4

Beta strand

647 – 651

5

Helix

658 – 660

3

Sequences

	Sequence		Length	Mass (Da)
	Q9UM07 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 79D7AF7B3D307A3B	FASTA	663	74,079
	10 20 30 40 50 60 MAQGTLIRVT PEQPTHAVCV LGTLTQLDIC SSAPEDCTSF SINASPGVVV DIAHGPPAKK 70 80 90 100 110 120 KSTGSSTWPL DPGVEVTLTM KVASGSTGDQ KVQISYYGPK TPPVKALLYL TGVEISLCAD 130 140 150 160 170 180 ITRTGKVKPT RAVKDQRTWT WGPCGQGAIL LVNCDRDNLE SSAMDCEDDE VLDSEDLQDM 190 200 210 220 230 240 SLMTLSTKTP KDFFTNHTLV LHVARSEMDK VRVFQATRGK LSSKCSVVLG PKWPSHYLMV 250 260 270 280 290 300 PGGKHNMDFY VEALAFPDTD FPGLITLTIS LLDTSNLELP EAVVFQDSVV FRVAPWIMTP 310 320 330 340 350 360 NTQPPQEVYA CSIFENEDFL KSVTTLAMKA KCKLTICPEE ENMDDQWMQD EMEIGYIQAP 370 380 390 400 410 420 HKTLPVVFDS PRNRGLKEFP IKRVMGPDFG YVTRGPQTGG ISGLDSFGNL EVSPPVTVRG 430 440 450 460 470 480 KEYPLGRILF GDSCYPSNDS RQMHQALQDF LSAQQVQAPV KLYSDWLSVG HVDEFLSFVP 490 500 510 520 530 540 APDRKGFRLL LASPRSCYKL FQEQQNEGHG EALLFEGIKK KKQQKIKNIL SNKTLREHNS 550 560 570 580 590 600 FVERCIDWNR ELLKRELGLA ESDIIDIPQL FKLKEFSKAE AFFPNMVNML VLGKHLGIPK 610 620 630 640 650 660 PFGPVINGRC CLEEKVCSLL EPLGLQCTFI NDFFTYHIRH GEVHCGTNVR RKPFSFKWWN MVP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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].
[4]	"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.
[5]	"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.
[6]	"Functional haplotypes of PADI4, encoding citrullinating enzyme peptidylarginine deiminase 4, are associated with rheumatoid arthritis." 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. Nat. Genet. 34:395-402(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE.
[7]	"Histone deimination antagonizes arginine methylation." 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. Cell 118:545-553(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Human PAD4 regulates histone arginine methylation levels via demethylimination." 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. Science 306:279-283(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Comparison of enzymatic properties between hPADI2 and hPADI4." Nakayama-Hamada M., Suzuki A., Kubota K., Takazawa T., Ohsaka M., Kawaida R., Ono M., Kasuya A., Furukawa H., Yamada R., Yamamoto K. Biochem. Biophys. Res. Commun. 327:192-200(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
[10]	"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: CITRULLINATION OF EP300.
[11]	"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.
[12]	"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, MUTAGENESIS OF ARG-374 AND CYS-645.
[13]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB017919 mRNA. Translation: BAA84542.1.
AJ549502 Genomic DNA. Translation: CAE47743.1.
AL590644, AC004824 Genomic DNA. Translation: CAH73167.1.
BC025718 mRNA. Translation: AAH25718.1.

IPI

IPI00008307.

RefSeq

NP_036519.2. NM_012387.2.

UniGene

Hs.522969.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

DisProt

DP00321.

ProteinModelPortal

Q9UM07.

SMR

Q9UM07. Positions 2-663.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000364597.

PTM databases

PhosphoSite

Q9UM07.

Polymorphism databases

DMDM

296439260.

Proteomic databases

PaxDb

Q9UM07.

PRIDE

Q9UM07.

Protocols and materials databases

DNASU

23569.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375448; ENSP00000364597; ENSG00000159339.

GeneID

23569.

KEGG

hsa:23569.

UCSC

uc001baj.2. human.

Organism-specific databases

CTD

23569.

GeneCards

GC01P017634.

H-InvDB

HIX0000182.

HGNC

HGNC:18368. PADI4.

HPA

HPA017007.

MIM

180300. phenotype.
605347. gene.

neXtProt

NX_Q9UM07.

PharmGKB

PA32903.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG42085.

HOGENOM

HOG000220908.

HOVERGEN

HBG053016.

InParanoid

Q9UM07.

KO

K01481.

OMA

VERCIDW.

OrthoDB

EOG4SN1N9.

PhylomeDB

Q9UM07.

Enzyme and pathway databases

BioCyc

MetaCyc:HS08389-MONOMER.

BRENDA

3.5.3.15. 2681.

Gene expression databases

ArrayExpress

Q9UM07.

Bgee

Q9UM07.

CleanEx

HS_PADI4.

Genevestigator

Q9UM07.

GermOnline

ENSG00000159339. Homo sapiens.

Family and domain databases

InterPro

IPR008972. Cupredoxin.
IPR004303. PAD.
IPR013530. PAD_C.
IPR013732. PAD_N.
IPR013733. Prot_Arg_deaminase_cen_dom.
IPR016296. Protein-arginine_deiminase_sub.
[Graphical view]

PANTHER

PTHR10837. PTHR10837. 1 hit.

Pfam

PF03068. PAD. 1 hit.
PF08527. PAD_M. 1 hit.
PF08526. PAD_N. 1 hit.
[Graphical view]

PIRSF

PIRSF001247. Protein-arginine_deiminase. 1 hit.

SUPFAM

SSF49503. Cupredoxin. 1 hit.
SSF110083. PAD_central. 1 hit.

ProtoNet

Search...

Other

BindingDB

Q9UM07.

ChEMBL

CHEMBL6111.

DrugBank

DB00155. L-Citrulline.

EvolutionaryTrace

Q9UM07.

GenomeRNAi

23569.

NextBio

46172.

SOURCE

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Entry information

Entry name

PADI4_HUMAN

Accession

Primary (citable) accession number: Q9UM07
Secondary accession number(s): Q5VTZ8, Q70SX4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.