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Protein

Protein-arginine deiminase type-4

Gene

PADI4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 Ca2+ 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
  1. Vmax=33.2 µmol/h/mg enzyme toward fibrinogen1 Publication
  2. 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)DescriptionActionsGraphical viewLength
Metal bindingi153Calcium 13 Publications1
Metal bindingi155Calcium 13 Publications1
Metal bindingi155Calcium 23 Publications1
Metal bindingi157Calcium 13 Publications1
Metal bindingi157Calcium 23 Publications1
Metal bindingi165Calcium 13 Publications1
Metal bindingi165Calcium 3; via carbonyl oxygen3 Publications1
Metal bindingi168Calcium 33 Publications1
Metal bindingi170Calcium 3; via carbonyl oxygen3 Publications1
Metal bindingi176Calcium 13 Publications1
Metal bindingi179Calcium 13 Publications1
Metal bindingi179Calcium 23 Publications1
Binding sitei346TDFA Inhibitor1 Publication1
Metal bindingi349Calcium 43 Publications1
Active sitei3501 Publication1
Metal bindingi351Calcium 53 Publications1
Metal bindingi353Calcium 43 Publications1
Metal bindingi369Calcium 53 Publications1
Binding sitei369TDFA Inhibitor1 Publication1
Metal bindingi370Calcium 5; via carbonyl oxygen3 Publications1
Metal bindingi373Calcium 53 Publications1
Binding sitei374Substrate1
Binding sitei374TDFA Inhibitor1 Publication1
Metal bindingi388Calcium 23 Publications1
Metal bindingi407Calcium 4; via carbonyl oxygen3 Publications1
Metal bindingi410Calcium 4; via carbonyl oxygen3 Publications1
Metal bindingi411Calcium 43 Publications1
Active sitei4711 Publication1
Binding sitei471TDFA Inhibitor1 Publication1
Active sitei4731 Publication1
Binding sitei473TDFA Inhibitor1 Publication1
Binding sitei639Substrate; via carbonyl oxygen1
Active sitei6451 Publication1
Binding sitei645TDFA Inhibitor1 Publication1

GO - Molecular functioni

  • arginine deiminase activity Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • protein-arginine deiminase activity Source: UniProtKB

GO - Biological processi

  • cellular protein modification process Source: ProtInc
  • chromatin organization Source: UniProtKB
  • chromatin remodeling Source: UniProtKB
  • histone citrullination Source: UniProtKB
  • histone H3-R26 citrullination Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • nucleosome assembly Source: UniProtKB
  • protein citrullination Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • stem cell population maintenance Source: UniProtKB
  • 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.
ZFISH:HS08389-MONOMER.
BRENDAi3.5.3.15. 2681.
ReactomeiR-HSA-3247509. Chromatin modifying enzymes.

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:PAD4, PADI5, PDI5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18368. PADI4.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Rheumatoid arthritis (RA)1 Publication
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
Disease descriptionAn 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.
See also OMIM:180300

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi346Q → A: Impaired binding of TDFA Inhibitor. 1 Publication1
Mutagenesisi374R → A: Strongly reduces enzymatic activity. 3 Publications1
Mutagenesisi374R → Q: Impaired binding of TDFA Inhibitor. 3 Publications1
Mutagenesisi639R → Q: Impaired binding of TDFA Inhibitor. 1 Publication1
Mutagenesisi645C → A: Abolishes enzymatic activity. 1 Publication1

Organism-specific databases

DisGeNETi23569.
MalaCardsiPADI4.
MIMi180300. phenotype.
OpenTargetsiENSG00000159339.
ENSG00000280908.
PharmGKBiPA32903.

Chemistry databases

ChEMBLiCHEMBL6111.
DrugBankiDB00207. Azithromycin.
DB00254. Doxycycline.
DB00155. L-Citrulline.
DB01082. Streptomycin.
DB00759. Tetracycline.
GuidetoPHARMACOLOGYi2877.

Polymorphism and mutation databases

BioMutaiPADI4.
DMDMi296439260.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002200331 – 663Protein-arginine deiminase type-4Add BLAST663

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei205Citrulline1 Publication1
Modified residuei212Citrulline1 Publication1
Modified residuei218Citrulline1 Publication1
Modified residuei372Citrulline1 Publication1
Modified residuei374Citrulline1 Publication1
Modified residuei383Citrulline1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Citrullination

Proteomic databases

MaxQBiQ9UM07.
PaxDbiQ9UM07.
PeptideAtlasiQ9UM07.
PRIDEiQ9UM07.

PTM databases

iPTMnetiQ9UM07.
PhosphoSitePlusiQ9UM07.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000159339.
CleanExiHS_PADI4.
ExpressionAtlasiQ9UM07. baseline and differential.
GenevisibleiQ9UM07. HS.

Organism-specific databases

HPAiHPA017007.
HPA042825.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ANXA4Q6LES23EBI-1042511,EBI-10250835

Protein-protein interaction databases

BioGridi117111. 11 interactors.
DIPiDIP-50397N.
IntActiQ9UM07. 3 interactors.
STRINGi9606.ENSP00000364597.

Chemistry databases

BindingDBiQ9UM07.

Structurei

Secondary structure

1663
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Beta strandi11 – 13Combined sources3
Beta strandi15 – 20Combined sources6
Beta strandi23 – 28Combined sources6
Helixi30 – 32Combined sources3
Beta strandi39 – 44Combined sources6
Beta strandi48 – 51Combined sources4
Beta strandi77 – 82Combined sources6
Beta strandi85 – 88Combined sources4
Beta strandi90 – 98Combined sources9
Beta strandi101 – 118Combined sources18
Beta strandi123 – 126Combined sources4
Turni133 – 137Combined sources5
Beta strandi148 – 150Combined sources3
Beta strandi158 – 160Combined sources3
Helixi165 – 167Combined sources3
Beta strandi168 – 170Combined sources3
Helixi174 – 179Combined sources6
Beta strandi180 – 189Combined sources10
Helixi193 – 195Combined sources3
Beta strandi196 – 202Combined sources7
Turni205 – 207Combined sources3
Helixi208 – 210Combined sources3
Beta strandi211 – 215Combined sources5
Beta strandi226 – 230Combined sources5
Beta strandi233 – 238Combined sources6
Beta strandi242 – 253Combined sources12
Beta strandi263 – 273Combined sources11
Beta strandi277 – 279Combined sources3
Beta strandi282 – 293Combined sources12
Beta strandi305 – 310Combined sources6
Helixi317 – 329Combined sources13
Beta strandi333 – 336Combined sources4
Helixi339 – 342Combined sources4
Turni348 – 350Combined sources3
Beta strandi351 – 359Combined sources9
Beta strandi362 – 369Combined sources8
Turni375 – 377Combined sources3
Helixi378 – 383Combined sources6
Beta strandi389 – 393Combined sources5
Beta strandi397 – 399Combined sources3
Helixi403 – 405Combined sources3
Helixi407 – 409Combined sources3
Beta strandi410 – 412Combined sources3
Beta strandi415 – 418Combined sources4
Beta strandi421 – 423Combined sources3
Beta strandi428 – 432Combined sources5
Helixi445 – 453Combined sources9
Helixi455 – 457Combined sources3
Beta strandi460 – 463Combined sources4
Beta strandi467 – 469Combined sources3
Helixi472 – 474Combined sources3
Beta strandi476 – 480Combined sources5
Beta strandi482 – 484Combined sources3
Beta strandi486 – 493Combined sources8
Helixi494 – 506Combined sources13
Turni507 – 511Combined sources5
Turni515 – 517Combined sources3
Beta strandi519 – 521Combined sources3
Helixi526 – 531Combined sources6
Helixi533 – 557Combined sources25
Helixi561 – 563Combined sources3
Beta strandi564 – 568Combined sources5
Beta strandi571 – 573Combined sources3
Helixi575 – 577Combined sources3
Beta strandi579 – 583Combined sources5
Beta strandi586 – 588Combined sources3
Beta strandi590 – 592Combined sources3
Beta strandi595 – 599Combined sources5
Beta strandi607 – 610Combined sources4
Helixi611 – 620Combined sources10
Helixi621 – 623Combined sources3
Beta strandi626 – 630Combined sources5
Turni633 – 636Combined sources4
Helixi637 – 639Combined sources3
Turni643 – 646Combined sources4
Beta strandi647 – 651Combined sources5
Helixi658 – 660Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4X8CX-ray3.10A1-663[»]
4X8GX-ray3.29A1-663[»]
DisProtiDP00321.
ProteinModelPortaliQ9UM07.
SMRiQ9UM07.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UM07.

Family & Domainsi

Sequence similaritiesi

Belongs to the protein arginine deiminase family.Curated

Phylogenomic databases

eggNOGiENOG410IF3F. Eukaryota.
ENOG410ZKF3. LUCA.
GeneTreeiENSGT00390000008680.
HOGENOMiHOG000220908.
HOVERGENiHBG053016.
InParanoidiQ9UM07.
KOiK01481.
OMAiHVARSEM.
OrthoDBiEOG091G02QG.
PhylomeDBiQ9UM07.
TreeFamiTF331952.

Family and domain databases

InterProiIPR008972. Cupredoxin.
IPR004303. PAD.
IPR013530. PAD_C.
IPR013732. PAD_N.
IPR013733. Prot_Arg_deaminase_cen_dom.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti149I → V in BAF83196 (PubMed:14702039).Curated1
Sequence conflicti247M → T in BAG37357 (PubMed:14702039).Curated1
Sequence conflicti657K → E in BAF83196 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0535608R → H.Corresponds to variant rs35381732dbSNPEnsembl.1
Natural variantiVAR_02063955G → S Does not catalytic activity. 3 PublicationsCorresponds to variant rs11203366dbSNPEnsembl.1
Natural variantiVAR_05356179T → M.Corresponds to variant rs35809521dbSNPEnsembl.1
Natural variantiVAR_02064082V → A Does not catalytic activity. 3 PublicationsCorresponds to variant rs11203367dbSNPEnsembl.1
Natural variantiVAR_02740189D → N.1 PublicationCorresponds to variant rs143187209dbSNPEnsembl.1
Natural variantiVAR_027402102P → T.1 PublicationCorresponds to variant rs34309058dbSNPEnsembl.1
Natural variantiVAR_020641112G → A Does not catalytic activity. 3 PublicationsCorresponds to variant rs874881dbSNPEnsembl.1
Natural variantiVAR_027403131R → T.1 PublicationCorresponds to variant rs12733102dbSNPEnsembl.1
Natural variantiVAR_027404164M → T.Corresponds to variant rs11588132dbSNPEnsembl.1
Natural variantiVAR_053562260D → N.Corresponds to variant rs35903413dbSNPEnsembl.1
Natural variantiVAR_020642275S → F.1 PublicationCorresponds to variant rs1748020dbSNPEnsembl.1

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.
ENST00000628229; ENSP00000487021; ENSG00000280908.
GeneIDi23569.
KEGGihsa:23569.
UCSCiuc001baj.3. human.

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.
CCDSiCCDS180.1.
RefSeqiNP_036519.2. NM_012387.2.
UniGeneiHs.522969.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4X8CX-ray3.10A1-663[»]
4X8GX-ray3.29A1-663[»]
DisProtiDP00321.
ProteinModelPortaliQ9UM07.
SMRiQ9UM07.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117111. 11 interactors.
DIPiDIP-50397N.
IntActiQ9UM07. 3 interactors.
STRINGi9606.ENSP00000364597.

Chemistry databases

BindingDBiQ9UM07.
ChEMBLiCHEMBL6111.
DrugBankiDB00207. Azithromycin.
DB00254. Doxycycline.
DB00155. L-Citrulline.
DB01082. Streptomycin.
DB00759. Tetracycline.
GuidetoPHARMACOLOGYi2877.

PTM databases

iPTMnetiQ9UM07.
PhosphoSitePlusiQ9UM07.

Polymorphism and mutation databases

BioMutaiPADI4.
DMDMi296439260.

Proteomic databases

MaxQBiQ9UM07.
PaxDbiQ9UM07.
PeptideAtlasiQ9UM07.
PRIDEiQ9UM07.

Protocols and materials databases

DNASUi23569.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375448; ENSP00000364597; ENSG00000159339.
ENST00000628229; ENSP00000487021; ENSG00000280908.
GeneIDi23569.
KEGGihsa:23569.
UCSCiuc001baj.3. human.

Organism-specific databases

CTDi23569.
DisGeNETi23569.
GeneCardsiPADI4.
H-InvDBHIX0000182.
HGNCiHGNC:18368. PADI4.
HPAiHPA017007.
HPA042825.
MalaCardsiPADI4.
MIMi180300. phenotype.
605347. gene.
neXtProtiNX_Q9UM07.
OpenTargetsiENSG00000159339.
ENSG00000280908.
PharmGKBiPA32903.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF3F. Eukaryota.
ENOG410ZKF3. LUCA.
GeneTreeiENSGT00390000008680.
HOGENOMiHOG000220908.
HOVERGENiHBG053016.
InParanoidiQ9UM07.
KOiK01481.
OMAiHVARSEM.
OrthoDBiEOG091G02QG.
PhylomeDBiQ9UM07.
TreeFamiTF331952.

Enzyme and pathway databases

BioCyciMetaCyc:HS08389-MONOMER.
ZFISH:HS08389-MONOMER.
BRENDAi3.5.3.15. 2681.
ReactomeiR-HSA-3247509. Chromatin modifying enzymes.

Miscellaneous databases

ChiTaRSiPADI4. human.
EvolutionaryTraceiQ9UM07.
GeneWikiiPADI4.
GenomeRNAii23569.
PROiQ9UM07.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000159339.
CleanExiHS_PADI4.
ExpressionAtlasiQ9UM07. baseline and differential.
GenevisibleiQ9UM07. HS.

Family and domain databases

InterProiIPR008972. Cupredoxin.
IPR004303. PAD.
IPR013530. PAD_C.
IPR013732. PAD_N.
IPR013733. Prot_Arg_deaminase_cen_dom.
[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.
ProtoNetiSearch...

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 30, 2016
This is version 151 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.