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Q9Y2J8 (PADI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PADI2
Synonyms:KIAA0994, PDI2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the deimination of arginine residues of proteins By similarity.

Catalytic activity

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

Cofactor

Calcium By similarity.

Subcellular location

Cytoplasm Ref.1.

Sequence similarities

Belongs to the protein arginine deiminase family.

Sequence caution

The sequence BAA76838.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCalcium
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin-mediated maintenance of transcription

Inferred from mutant phenotype PubMed 22853951. Source: UniProt

histone H3-R26 citrullination

Inferred from direct assay PubMed 22853951. Source: UniProt

intracellular estrogen receptor signaling pathway

Inferred from mutant phenotype PubMed 22853951. Source: UniProt

negative regulation of chemokine-mediated signaling pathway

Inferred from direct assay PubMed 18645041. Source: UniProt

negative regulation of lymphocyte chemotaxis

Inferred from direct assay PubMed 18645041. Source: UniProt

protein citrullination

Inferred from direct assay Ref.1PubMed 15629448. Source: UniProt

regulation of chromatin disassembly

Inferred from direct assay PubMed 22853951. Source: UniProt

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

transcriptionally active chromatin

Inferred from direct assay PubMed 22853951. Source: UniProt

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

estrogen receptor binding

Inferred from physical interaction PubMed 22853951. Source: UniProt

protein-arginine deiminase activity

Inferred from direct assay Ref.1PubMed 15629448PubMed 18645041PubMed 22853951. Source: UniProt

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 665665Protein-arginine deiminase type-2
PRO_0000220026

Experimental info

Sequence conflict6611W → L in BAA82557. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Y2J8 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 8D417A87A02D6839

FASTA66575,564
        10         20         30         40         50         60 
MLRERTVRLQ YGSRVEAVYV LGTYLWTDVY SAAPAGAQTF SLKHSEHVWV EVVRDGEAEE 

        70         80         90        100        110        120 
VATNGKQRWL LSPSTTLRVT MSQASTEASS DKVTVNYYDE EGSIPIDQAG LFLTAIEISL 

       130        140        150        160        170        180 
DVDADRDGVV EKNNPKKASW TWGPEGQGAI LLVNCDRETP WLPKEDCRDE KVYSKEDLKD 

       190        200        210        220        230        240 
MSQMILRTKG PDRLPAGYEI VLYISMSDSD KVGVFYVENP FFGQRYIHIL GRRKLYHVVK 

       250        260        270        280        290        300 
YTGGSAELLF FVEGLCFPDE GFSGLVSIHV SLLEYMAQDI PLTPIFTDTV IFRIAPWIMT 

       310        320        330        340        350        360 
PNILPPVSVF VCCMKDNYLF LKEVKNLVEK TNCELKVCFQ YLNRGDRWIQ DEIEFGYIEA 

       370        380        390        400        410        420 
PHKGFPVVLD SPRDGNLKDF PVKELLGPDF GYVTREPLFE SVTSLDSFGN LEVSPPVTVN 

       430        440        450        460        470        480 
GKTYPLGRIL IGSSFPLSGG RRMTKVVRDF LKAQQVQAPV ELYSDWLTVG HVDEFMSFVP 

       490        500        510        520        530        540 
IPGTKKFLLL MASTSACYKL FREKQKDGHG EAIMFKGLGG MSSKRITINK ILSNESLVQE 

       550        560        570        580        590        600 
NLYFQRCLDW NRDILKKELG LTEQDIIDLP ALFKMDEDHR ARAFFPNMVN MIVLDKDLGI 

       610        620        630        640        650        660 
PKPFGPQVEE ECCLEMHVRG LLEPLGLECT FIDDISAYHK FLGEVHCGTN VRRKPFTFKW 


WHMVP 

« Hide

References

« Hide 'large scale' references
[1]"Human peptidylarginine deiminase type II: molecular cloning, gene organization, and expression in human skin."
Ishigami A., Ohsawa T., Asaga H., Akiyama K., Kuramoto M., Maruyama N.
Arch. Biochem. Biophys. 407:25-31(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Tissue: Skin.
[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].
[3]"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB030176 mRNA. Translation: BAA82557.1.
AJ549502 Genomic DNA. Translation: CAE47740.1.
AB023211 mRNA. Translation: BAA76838.1. Different initiation.
AL049569 Genomic DNA. Translation: CAB96821.1.
CCDSCCDS177.1.
RefSeqNP_031391.2. NM_007365.2.
UniGeneHs.33455.

3D structure databases

ProteinModelPortalQ9Y2J8.
SMRQ9Y2J8. Positions 7-665.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116404. 1 interaction.
IntActQ9Y2J8. 1 interaction.
STRING9606.ENSP00000364635.

Chemistry

BindingDBQ9Y2J8.
ChEMBLCHEMBL1909487.
DrugBankDB00155. L-Citrulline.

PTM databases

PhosphoSiteQ9Y2J8.

Polymorphism databases

DMDM7531171.

Proteomic databases

MaxQBQ9Y2J8.
PaxDbQ9Y2J8.
PRIDEQ9Y2J8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375486; ENSP00000364635; ENSG00000117115.
GeneID11240.
KEGGhsa:11240.
UCSCuc001baf.3. human.

Organism-specific databases

CTD11240.
GeneCardsGC01M017393.
HGNCHGNC:18341. PADI2.
HPACAB012222.
MIM607935. gene.
neXtProtNX_Q9Y2J8.
PharmGKBPA32900.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42085.
HOGENOMHOG000220908.
HOVERGENHBG053016.
InParanoidQ9Y2J8.
KOK01481.
OMACLETHVR.
OrthoDBEOG7P5T09.
PhylomeDBQ9Y2J8.
TreeFamTF331952.

Enzyme and pathway databases

BioCycMetaCyc:HS04094-MONOMER.
BRENDA3.5.3.15. 2681.

Gene expression databases

ArrayExpressQ9Y2J8.
BgeeQ9Y2J8.
CleanExHS_PADI2.
GenevestigatorQ9Y2J8.

Family and domain databases

InterProIPR008972. Cupredoxin.
IPR004303. PAD.
IPR013530. PAD_C.
IPR013732. PAD_N.
IPR013733. Prot_Arg_deaminase_cen_dom.
IPR016296. Protein-arginine_deiminase_sub.
[Graphical view]
PANTHERPTHR10837. PTHR10837. 1 hit.
PfamPF03068. PAD. 1 hit.
PF08527. PAD_M. 1 hit.
PF08526. PAD_N. 1 hit.
[Graphical view]
PIRSFPIRSF001247. Protein-arginine_deiminase. 1 hit.
SUPFAMSSF110083. SSF110083. 1 hit.
SSF49503. SSF49503. 1 hit.
ProtoNetSearch...

Other

GeneWikiPADI2.
GenomeRNAi11240.
NextBio42778.
PROQ9Y2J8.
SOURCESearch...

Entry information

Entry namePADI2_HUMAN
AccessionPrimary (citable) accession number: Q9Y2J8
Secondary accession number(s): Q9UPN2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM