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Protein

Protein-arginine deiminase type-2

Gene

PADI2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the deimination of arginine residues of proteins.By similarity

Catalytic activityi

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

Cofactori

Ca2+By similarity

GO - Molecular functioni

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

GO - Biological processi

  • chromatin-mediated maintenance of transcription Source: UniProtKB
  • chromatin organization Source: Reactome
  • histone H3-R26 citrullination Source: UniProtKB
  • intracellular estrogen receptor signaling pathway Source: UniProtKB
  • negative regulation of chemokine-mediated signaling pathway Source: UniProtKB
  • negative regulation of lymphocyte chemotaxis Source: UniProtKB
  • protein citrullination Source: UniProtKB
  • regulation of chromatin disassembly Source: UniProtKB
  • substantia nigra development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciMetaCyc:HS04094-MONOMER.
ZFISH: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:3.5.3.15)
Alternative name(s):
PAD-H19
Peptidylarginine deiminase II
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

HGNCiHGNC:18341. PADI2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • transcriptionally active chromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

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

PaxDbiQ9Y2J8.
PeptideAtlasiQ9Y2J8.
PRIDEiQ9Y2J8.

PTM databases

iPTMnetiQ9Y2J8.
PhosphoSitePlusiQ9Y2J8.

Expressioni

Gene expression databases

BgeeiENSG00000117115.
CleanExiHS_PADI2.
ExpressionAtlasiQ9Y2J8. baseline and differential.
GenevisibleiQ9Y2J8. HS.

Organism-specific databases

HPAiHPA047735.

Interactioni

GO - Molecular functioni

  • estrogen receptor binding Source: UniProtKB

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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Beta strandi11 – 13Combined sources3
Beta strandi15 – 20Combined sources6
Beta strandi24 – 27Combined sources4
Beta strandi30 – 33Combined sources4
Beta strandi39 – 44Combined sources6
Beta strandi49 – 54Combined sources6
Beta strandi57 – 61Combined sources5
Beta strandi75 – 80Combined sources6
Beta strandi86 – 88Combined sources3
Beta strandi91 – 98Combined sources8
Beta strandi106 – 121Combined sources16
Beta strandi126 – 129Combined sources4
Turni135 – 138Combined sources4
Beta strandi149 – 151Combined sources3
Beta strandi162 – 164Combined sources3
Helixi166 – 168Combined sources3
Helixi175 – 178Combined sources4
Beta strandi181 – 193Combined sources13
Beta strandi198 – 203Combined sources6
Helixi207 – 210Combined sources4
Beta strandi212 – 216Combined sources5
Helixi220 – 222Combined sources3
Beta strandi226 – 231Combined sources6
Beta strandi236 – 239Combined sources4
Beta strandi243 – 254Combined sources12
Beta strandi264 – 274Combined sources11
Beta strandi283 – 294Combined sources12
Beta strandi306 – 312Combined sources7
Helixi318 – 329Combined sources12
Beta strandi334 – 338Combined sources5
Helixi340 – 343Combined sources4
Helixi348 – 351Combined sources4
Beta strandi353 – 360Combined sources8
Beta strandi363 – 370Combined sources8
Beta strandi375 – 377Combined sources3
Helixi383 – 386Combined sources4
Beta strandi391 – 394Combined sources4
Beta strandi398 – 400Combined sources3
Helixi404 – 406Combined sources3
Helixi408 – 410Combined sources3
Beta strandi411 – 413Combined sources3
Beta strandi417 – 419Combined sources3
Beta strandi422 – 424Combined sources3
Beta strandi429 – 433Combined sources5
Turni436 – 439Combined sources4
Helixi445 – 453Combined sources9
Beta strandi460 – 463Combined sources4
Beta strandi467 – 469Combined sources3
Helixi472 – 474Combined sources3
Beta strandi476 – 480Combined sources5
Beta strandi487 – 493Combined sources7
Helixi494 – 506Combined sources13
Turni507 – 511Combined sources5
Beta strandi513 – 515Combined sources3
Turni519 – 521Combined sources3
Helixi522 – 524Combined sources3
Helixi528 – 532Combined sources5
Helixi535 – 559Combined sources25
Helixi563 – 565Combined sources3
Beta strandi566 – 570Combined sources5
Beta strandi573 – 575Combined sources3
Beta strandi581 – 585Combined sources5
Beta strandi592 – 594Combined sources3
Beta strandi597 – 601Combined sources5
Helixi613 – 622Combined sources10
Helixi623 – 625Combined sources3
Beta strandi628 – 632Combined sources5
Helixi636 – 638Combined sources3
Beta strandi648 – 653Combined sources6
Helixi660 – 662Combined sources3

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...

Family & Domainsi

Sequence similaritiesi

Belongs to the protein arginine deiminase family.Curated

Phylogenomic databases

eggNOGiENOG410IF3F. Eukaryota.
ENOG410ZKF3. LUCA.
GeneTreeiENSGT00390000008680.
HOGENOMiHOG000220908.
HOVERGENiHBG053016.
InParanoidiQ9Y2J8.
KOiK01481.
OMAiCLETHVR.
OrthoDBiEOG091G02QG.
PhylomeDBiQ9Y2J8.
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.

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. Translation: CAB96821.1.
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

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. Translation: CAB96821.1.
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

PaxDbiQ9Y2J8.
PeptideAtlasiQ9Y2J8.
PRIDEiQ9Y2J8.

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.
GeneCardsiPADI2.
HGNCiHGNC:18341. PADI2.
HPAiHPA047735.
MIMi607935. gene.
neXtProtiNX_Q9Y2J8.
OpenTargetsiENSG00000117115.
PharmGKBiPA32900.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiPADI2. human.
GeneWikiiPADI2.
GenomeRNAii11240.
PROiQ9Y2J8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000117115.
CleanExiHS_PADI2.
ExpressionAtlasiQ9Y2J8. baseline and differential.
GenevisibleiQ9Y2J8. 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 nameiPADI2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2J8
Secondary accession number(s): Q96DA7, Q9UPN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: November 30, 2016
This is version 135 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.