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Protein

Protein-arginine deiminase type-2

Gene

PADI2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the deimination of arginine residues of proteins.2 Publications

Catalytic activityi

Protein L-arginine + H2O = protein L-citrulline + NH3.2 Publications

Cofactori

Ca2+2 PublicationsNote: Binding of Ca2+ triggers a conformation change that is essential for catalytic activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi123Calcium 1Combined sources1 Publication1
Metal bindingi125Calcium 1Combined sources1 Publication1
Metal bindingi127Calcium 1Combined sources1 Publication1
Metal bindingi129Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi131Calcium 1Combined sources1 Publication1
Metal bindingi154Calcium 2Combined sources1 Publication1
Metal bindingi156Calcium 2Combined sources1
Metal bindingi156Calcium 3Combined sources1 Publication1
Metal bindingi158Calcium 2Combined sources1
Metal bindingi158Calcium 3Combined sources1 Publication1
Metal bindingi166Calcium 2Combined sources1
Metal bindingi166Calcium 4; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi169Calcium 4Combined sources1 Publication1
Metal bindingi171Calcium 4; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi177Calcium 2Combined sources1
Metal bindingi180Calcium 2Combined sources1
Metal bindingi180Calcium 3Combined sources1 Publication1
Metal bindingi354Calcium 5Combined sources1 Publication1
Metal bindingi389Calcium 3Combined sources1 Publication1
Metal bindingi408Calcium 5; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi411Calcium 5; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi412Calcium 5Combined sources1 Publication1
Active sitei647Nucleophile1 Publication1

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionHydrolase
LigandCalcium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS04094-MONOMER
BRENDAi3.5.3.15 2681
ReactomeiR-HSA-3247509 Chromatin modifying enzymes
R-HSA-6798695 Neutrophil degranulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-arginine deiminase type-2 (EC:3.5.3.152 Publications)
Alternative name(s):
PAD-H19
Peptidylarginine deiminase II1 Publication
Protein-arginine deiminase type II
Gene namesi
Name:PADI2
Synonyms:KIAA0994, PAD2, PDI2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000117115.12
HGNCiHGNC:18341 PADI2
MIMi607935 gene
neXtProtiNX_Q9Y2J8

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi123D → N: Mildly reduced enzyme activity. 1 Publication1
Mutagenesisi125D → A: Mildly reduced enzyme activity. 1 Publication1
Mutagenesisi166D → A: Reduced enzyme activity. 1 Publication1
Mutagenesisi169D → A: Mildly reduced enzyme activity. 1 Publication1
Mutagenesisi177D → A: Reduced enzyme activity. 1 Publication1
Mutagenesisi348W → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi350Q → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi354E → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi370D → A: Reduced enzyme activity. 1 Publication1
Mutagenesisi373R → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi374D → A: Reduced enzyme activity. 1 Publication1
Mutagenesisi389D → A: Reduced enzyme activity. 1 Publication1
Mutagenesisi412E → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi647C → A: Loss of enzyme activity. 1 Publication1

Organism-specific databases

DisGeNETi11240
OpenTargetsiENSG00000117115
PharmGKBiPA32900

Chemistry databases

ChEMBLiCHEMBL1909487
DrugBankiDB00155 L-Citrulline

Polymorphism and mutation databases

BioMutaiPADI2
DMDMi7531171

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002200261 – 665Protein-arginine deiminase type-2Add BLAST665

Proteomic databases

EPDiQ9Y2J8
PaxDbiQ9Y2J8
PeptideAtlasiQ9Y2J8
PRIDEiQ9Y2J8
ProteomicsDBi85817

PTM databases

iPTMnetiQ9Y2J8
PhosphoSitePlusiQ9Y2J8

Expressioni

Tissue specificityi

Detected in keratinocytes in epidermis (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000117115 Expressed in 203 organ(s), highest expression level in medial globus pallidus
CleanExiHS_PADI2
ExpressionAtlasiQ9Y2J8 baseline and differential
GenevisibleiQ9Y2J8 HS

Organism-specific databases

HPAiHPA047735

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9Y2J8, 1 interactor
STRINGi9606.ENSP00000364635

Chemistry databases

BindingDBiQ9Y2J8

Structurei

Secondary structure

1665
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9Y2J8
SMRiQ9Y2J8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the protein arginine deiminase family.Curated

Phylogenomic databases

eggNOGiENOG410IF3F Eukaryota
ENOG410ZKF3 LUCA
GeneTreeiENSGT00390000008680
HOGENOMiHOG000220908
HOVERGENiHBG053016
InParanoidiQ9Y2J8
KOiK01481
OMAiCTFVDDI
OrthoDBiEOG091G02QG
PhylomeDBiQ9Y2J8
TreeFamiTF331952

Family and domain databases

Gene3Di2.60.40.1700, 1 hit
2.60.40.1860, 1 hit
InterProiView protein in InterPro
IPR008972 Cupredoxin
IPR004303 PAD
IPR013530 PAD_C
IPR036556 PAD_central_sf
IPR013732 PAD_N
IPR038685 PAD_N_sf
IPR013733 Prot_Arg_deaminase_cen_dom
PANTHERiPTHR10837 PTHR10837, 1 hit
PfamiView protein in Pfam
PF03068 PAD, 1 hit
PF08527 PAD_M, 1 hit
PF08526 PAD_N, 1 hit
PIRSFiPIRSF001247 Protein-arginine_deiminase, 1 hit
SUPFAMiSSF110083 SSF110083, 1 hit
SSF49503 SSF49503, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q9Y2J8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MLRERTVRLQ YGSRVEAVYV LGTYLWTDVY SAAPAGAQTF SLKHSEHVWV
60 70 80 90 100
EVVRDGEAEE VATNGKQRWL LSPSTTLRVT MSQASTEASS DKVTVNYYDE
110 120 130 140 150
EGSIPIDQAG LFLTAIEISL DVDADRDGVV EKNNPKKASW TWGPEGQGAI
160 170 180 190 200
LLVNCDRETP WLPKEDCRDE KVYSKEDLKD MSQMILRTKG PDRLPAGYEI
210 220 230 240 250
VLYISMSDSD KVGVFYVENP FFGQRYIHIL GRRKLYHVVK YTGGSAELLF
260 270 280 290 300
FVEGLCFPDE GFSGLVSIHV SLLEYMAQDI PLTPIFTDTV IFRIAPWIMT
310 320 330 340 350
PNILPPVSVF VCCMKDNYLF LKEVKNLVEK TNCELKVCFQ YLNRGDRWIQ
360 370 380 390 400
DEIEFGYIEA PHKGFPVVLD SPRDGNLKDF PVKELLGPDF GYVTREPLFE
410 420 430 440 450
SVTSLDSFGN LEVSPPVTVN GKTYPLGRIL IGSSFPLSGG RRMTKVVRDF
460 470 480 490 500
LKAQQVQAPV ELYSDWLTVG HVDEFMSFVP IPGTKKFLLL MASTSACYKL
510 520 530 540 550
FREKQKDGHG EAIMFKGLGG MSSKRITINK ILSNESLVQE NLYFQRCLDW
560 570 580 590 600
NRDILKKELG LTEQDIIDLP ALFKMDEDHR ARAFFPNMVN MIVLDKDLGI
610 620 630 640 650
PKPFGPQVEE ECCLEMHVRG LLEPLGLECT FIDDISAYHK FLGEVHCGTN
660
VRRKPFTFKW WHMVP
Length:665
Mass (Da):75,564
Last modified:May 30, 2000 - v2
Checksum:i8D417A87A02D6839
GO
Isoform 2 (identifier: Q9Y2J8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     438-665: Missing.

Note: No experimental confirmation available.
Show »
Length:437
Mass (Da):49,310
Checksum:i912B81FDA3DAC1A4
GO

Sequence cautioni

The sequence BAA76838 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti661W → L in BAA82557 (PubMed:12392711).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_056385438 – 665Missing in isoform 2. 1 PublicationAdd BLAST228

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB030176 mRNA Translation: BAA82557.1
AJ549502 Genomic DNA Translation: CAE47740.1
AB023211 mRNA Translation: BAA76838.1 Different initiation.
AL049569 Genomic DNA No translation available.
BC009701 mRNA Translation: AAH09701.1
CCDSiCCDS177.1 [Q9Y2J8-1]
RefSeqiNP_031391.2, NM_007365.2 [Q9Y2J8-1]
UniGeneiHs.33455

Genome annotation databases

EnsembliENST00000375481; ENSP00000364630; ENSG00000117115 [Q9Y2J8-2]
ENST00000375486; ENSP00000364635; ENSG00000117115 [Q9Y2J8-1]
GeneIDi11240
KEGGihsa:11240
UCSCiuc001baf.4 human [Q9Y2J8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB030176 mRNA Translation: BAA82557.1
AJ549502 Genomic DNA Translation: CAE47740.1
AB023211 mRNA Translation: BAA76838.1 Different initiation.
AL049569 Genomic DNA No translation available.
BC009701 mRNA Translation: AAH09701.1
CCDSiCCDS177.1 [Q9Y2J8-1]
RefSeqiNP_031391.2, NM_007365.2 [Q9Y2J8-1]
UniGeneiHs.33455

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4N20X-ray1.66A1-665[»]
4N22X-ray1.89A1-665[»]
4N24X-ray1.97A1-665[»]
4N25X-ray1.93A1-665[»]
4N26X-ray1.94A1-665[»]
4N28X-ray1.88A1-665[»]
4N2AX-ray1.70A1-665[»]
4N2BX-ray1.69A1-665[»]
4N2CX-ray3.02A1-665[»]
4N2DX-ray2.00A1-665[»]
4N2EX-ray1.86A1-665[»]
4N2FX-ray1.80A1-665[»]
4N2GX-ray1.85A1-665[»]
4N2HX-ray1.81A1-665[»]
4N2IX-ray1.90A1-665[»]
4N2KX-ray1.57A1-665[»]
4N2LX-ray2.10A1-665[»]
4N2MX-ray1.60A1-665[»]
4N2NX-ray1.80A1-665[»]
ProteinModelPortaliQ9Y2J8
SMRiQ9Y2J8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9Y2J8, 1 interactor
STRINGi9606.ENSP00000364635

Chemistry databases

BindingDBiQ9Y2J8
ChEMBLiCHEMBL1909487
DrugBankiDB00155 L-Citrulline

PTM databases

iPTMnetiQ9Y2J8
PhosphoSitePlusiQ9Y2J8

Polymorphism and mutation databases

BioMutaiPADI2
DMDMi7531171

Proteomic databases

EPDiQ9Y2J8
PaxDbiQ9Y2J8
PeptideAtlasiQ9Y2J8
PRIDEiQ9Y2J8
ProteomicsDBi85817

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375481; ENSP00000364630; ENSG00000117115 [Q9Y2J8-2]
ENST00000375486; ENSP00000364635; ENSG00000117115 [Q9Y2J8-1]
GeneIDi11240
KEGGihsa:11240
UCSCiuc001baf.4 human [Q9Y2J8-1]

Organism-specific databases

CTDi11240
DisGeNETi11240
EuPathDBiHostDB:ENSG00000117115.12
GeneCardsiPADI2
HGNCiHGNC:18341 PADI2
HPAiHPA047735
MIMi607935 gene
neXtProtiNX_Q9Y2J8
OpenTargetsiENSG00000117115
PharmGKBiPA32900
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF3F Eukaryota
ENOG410ZKF3 LUCA
GeneTreeiENSGT00390000008680
HOGENOMiHOG000220908
HOVERGENiHBG053016
InParanoidiQ9Y2J8
KOiK01481
OMAiCTFVDDI
OrthoDBiEOG091G02QG
PhylomeDBiQ9Y2J8
TreeFamiTF331952

Enzyme and pathway databases

BioCyciMetaCyc:HS04094-MONOMER
BRENDAi3.5.3.15 2681
ReactomeiR-HSA-3247509 Chromatin modifying enzymes
R-HSA-6798695 Neutrophil degranulation

Miscellaneous databases

ChiTaRSiPADI2 human
GeneWikiiPADI2
GenomeRNAii11240
PROiPR:Q9Y2J8
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000117115 Expressed in 203 organ(s), highest expression level in medial globus pallidus
CleanExiHS_PADI2
ExpressionAtlasiQ9Y2J8 baseline and differential
GenevisibleiQ9Y2J8 HS

Family and domain databases

Gene3Di2.60.40.1700, 1 hit
2.60.40.1860, 1 hit
InterProiView protein in InterPro
IPR008972 Cupredoxin
IPR004303 PAD
IPR013530 PAD_C
IPR036556 PAD_central_sf
IPR013732 PAD_N
IPR038685 PAD_N_sf
IPR013733 Prot_Arg_deaminase_cen_dom
PANTHERiPTHR10837 PTHR10837, 1 hit
PfamiView protein in Pfam
PF03068 PAD, 1 hit
PF08527 PAD_M, 1 hit
PF08526 PAD_N, 1 hit
PIRSFiPIRSF001247 Protein-arginine_deiminase, 1 hit
SUPFAMiSSF110083 SSF110083, 1 hit
SSF49503 SSF49503, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPADI2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2J8
Secondary accession number(s): Q96DA7, Q9UPN2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: October 10, 2018
This is version 149 of the entry and version 2 of the sequence. See 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
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Main funding by: National Institutes of Health

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