Q9Y2J8 (PADI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PADI2
Synonyms:	KIAA0994, PDI2

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	665 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm
Ligand	Calcium
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-citrulline biosynthetic process from peptidyl-arginine Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro protein-arginine deiminase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 665	665	Protein-arginine deiminase type-2		PRO_0000220026
Experimental info
	Sequence conflict	661	1	W → L in BAA82557. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9Y2J8 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 8D417A87A02D6839	FASTA	665	75,564
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00294187.
RefSeq	NP_031391.2. NM_007365.2.
UniGene	Hs.33455.
3D structure databases
ProteinModelPortal	Q9Y2J8.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y2J8. 1 interaction.
STRING	9606.ENSP00000364635.
PTM databases
PhosphoSite	Q9Y2J8.
Polymorphism databases
DMDM	7531171.
Proteomic databases
PaxDb	Q9Y2J8.
PRIDE	Q9Y2J8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000375486; ENSP00000364635; ENSG00000117115.
GeneID	11240.
KEGG	hsa:11240.
UCSC	uc001baf.3. human.
Organism-specific databases
CTD	11240.
GeneCards	GC01M017393.
HGNC	HGNC:18341. PADI2.
HPA	CAB012222.
MIM	607935. gene.
neXtProt	NX_Q9Y2J8.
PharmGKB	PA32900.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG42085.
HOGENOM	HOG000220908.
HOVERGEN	HBG053016.
InParanoid	Q9Y2J8.
KO	K01481.
OMA	CLETHVR.
OrthoDB	EOG4X3H10.
PhylomeDB	Q9Y2J8.
Enzyme and pathway databases
BioCyc	MetaCyc:HS04094-MONOMER.
BRENDA	3.5.3.15. 2681.
Gene expression databases
ArrayExpress	Q9Y2J8.
Bgee	Q9Y2J8.
CleanEx	HS_PADI2.
Genevestigator	Q9Y2J8.
GermOnline	ENSG00000117115. 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	Q9Y2J8.
ChEMBL	CHEMBL1909487.
DrugBank	DB00155. L-Citrulline.
GenomeRNAi	11240.
NextBio	42778.
SOURCE	Search...

Entry information

Entry name

PADI2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 103 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.