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Protein

Protein-arginine deiminase type-1

Gene

PADI1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 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

  1. calcium ion binding Source: InterPro
  2. protein-arginine deiminase activity Source: UniProtKB-EC

GO - Biological processi

  1. protein citrullination Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciMetaCyc:HS06945-MONOMER.
BRENDAi3.5.3.15. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-arginine deiminase type-1 (EC:3.5.3.15)
Alternative name(s):
Peptidylarginine deiminase I
Protein-arginine deiminase type I
Gene namesi
Name:PADI1
Synonyms:PDI1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18367. PADI1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32899.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 663663Protein-arginine deiminase type-1PRO_0000220023Add
BLAST

Proteomic databases

MaxQBiQ9ULC6.
PaxDbiQ9ULC6.
PeptideAtlasiQ9ULC6.
PRIDEiQ9ULC6.

PTM databases

PhosphoSiteiQ9ULC6.

Expressioni

Tissue specificityi

Epidermis, prostate, testis, placenta, spleen and thymus.1 Publication

Gene expression databases

BgeeiQ9ULC6.
CleanExiHS_PADI1.
ExpressionAtlasiQ9ULC6. baseline and differential.
GenevestigatoriQ9ULC6.

Organism-specific databases

HPAiHPA062294.

Interactioni

Protein-protein interaction databases

BioGridi118980. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9ULC6.
SMRiQ9ULC6. Positions 6-663.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the protein arginine deiminase family.Curated

Phylogenomic databases

eggNOGiNOG42085.
GeneTreeiENSGT00390000008680.
HOGENOMiHOG000220908.
HOVERGENiHBG053016.
InParanoidiQ9ULC6.
KOiK01481.
OMAiDIPQLFF.
OrthoDBiEOG7P5T09.
PhylomeDBiQ9ULC6.
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.

Q9ULC6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPKRVVQLS LKMPTHAVCV VGVEAHVDIH SDVPKGANSF RVSGSSGVEV
60 70 80 90 100
FMVYNRTRVK EPIGKARWPL DTDADMVVSV GTASKELKDF KVRVSYFGEQ
110 120 130 140 150
EDQALGRSVL YLTGVDISLE VDTGRTGKVK RSQGDKKTWR WGPEGYGAIL
160 170 180 190 200
LVNCDRDNHR SAEPDLTHSW LMSLADLQDM SPMLLSCNGP DKLFDSHKLV
210 220 230 240 250
LNVPFSDSKR VRVFCARGGN SLSDYKQVLG PQCLSYEVER QPGEQEIKFY
260 270 280 290 300
VEGLTFPDAD FLGLVSLSVS LVDPGTLPEV TLFTDTVGFR MAPWIMTPNT
310 320 330 340 350
QPPEELYVCR VMDTHGSNEK FLEDMSYLTL KANCKLTICP QVENRNDRWI
360 370 380 390 400
QDEMEFGYIE APHKSFPVVF DSPRNRGLKD FPYKRILGPD FGYVTREIPL
410 420 430 440 450
PGPSSLDSFG NLDVSPPVTV GGTEYPLGRI LIGSSFPKSG GRQMARAVRN
460 470 480 490 500
FLKAQQVQAP VELYSDWLSV GHVDEFLTFV PTSDQKGFRL LLASPSACLK
510 520 530 540 550
LFQEKKEEGY GEAAQFDGLK HQAKRSINEM LADRHLQRDN LHAQKCIDWN
560 570 580 590 600
RNVLKRELGL AESDIVDIPQ LFFLKNFYAE AFFPDMVNMV VLGKYLGIPK
610 620 630 640 650
PYGPIINGRC CLEEKVQSLL EPLGLHCIFI DDYLSYHELQ GEIHCGTNVR
660
RKPFPFKWWN MVP
Length:663
Mass (Da):74,666
Last modified:December 20, 2004 - v2
Checksum:i4674CEBC03A7E7CA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti420 – 4201V → G in BAA85771 (PubMed:12416996).Curated
Sequence conflicti499 – 4991L → P in BAA85771 (PubMed:12416996).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti649 – 6491V → M.
Corresponds to variant rs16824215 [ dbSNP | Ensembl ].
VAR_053557

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB033768 mRNA. Translation: BAA85771.1.
AJ549502 Genomic DNA. Translation: CAE47741.1.
AL590644 Genomic DNA. Translation: CAH73165.1.
CH471134 Genomic DNA. Translation: EAW94833.1.
BC130574 mRNA. Translation: AAI30575.1.
BC136402 mRNA. Translation: AAI36403.1.
CCDSiCCDS178.1.
RefSeqiNP_037490.2. NM_013358.2.
UniGeneiHs.412941.

Genome annotation databases

EnsembliENST00000375471; ENSP00000364620; ENSG00000142623.
GeneIDi29943.
KEGGihsa:29943.
UCSCiuc001bah.1. human.

Polymorphism databases

DMDMi56757695.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB033768 mRNA. Translation: BAA85771.1.
AJ549502 Genomic DNA. Translation: CAE47741.1.
AL590644 Genomic DNA. Translation: CAH73165.1.
CH471134 Genomic DNA. Translation: EAW94833.1.
BC130574 mRNA. Translation: AAI30575.1.
BC136402 mRNA. Translation: AAI36403.1.
CCDSiCCDS178.1.
RefSeqiNP_037490.2. NM_013358.2.
UniGeneiHs.412941.

3D structure databases

ProteinModelPortaliQ9ULC6.
SMRiQ9ULC6. Positions 6-663.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118980. 1 interaction.

Chemistry

BindingDBiQ9ULC6.
ChEMBLiCHEMBL1909486.
DrugBankiDB00155. L-Citrulline.

PTM databases

PhosphoSiteiQ9ULC6.

Polymorphism databases

DMDMi56757695.

Proteomic databases

MaxQBiQ9ULC6.
PaxDbiQ9ULC6.
PeptideAtlasiQ9ULC6.
PRIDEiQ9ULC6.

Protocols and materials databases

DNASUi29943.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375471; ENSP00000364620; ENSG00000142623.
GeneIDi29943.
KEGGihsa:29943.
UCSCiuc001bah.1. human.

Organism-specific databases

CTDi29943.
GeneCardsiGC01P017531.
HGNCiHGNC:18367. PADI1.
HPAiHPA062294.
MIMi607934. gene.
neXtProtiNX_Q9ULC6.
PharmGKBiPA32899.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42085.
GeneTreeiENSGT00390000008680.
HOGENOMiHOG000220908.
HOVERGENiHBG053016.
InParanoidiQ9ULC6.
KOiK01481.
OMAiDIPQLFF.
OrthoDBiEOG7P5T09.
PhylomeDBiQ9ULC6.
TreeFamiTF331952.

Enzyme and pathway databases

BioCyciMetaCyc:HS06945-MONOMER.
BRENDAi3.5.3.15. 2681.

Miscellaneous databases

GeneWikiiPADI1.
GenomeRNAii29943.
NextBioi52603.
PROiQ9ULC6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ULC6.
CleanExiHS_PADI1.
ExpressionAtlasiQ9ULC6. baseline and differential.
GenevestigatoriQ9ULC6.

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...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I."
    Guerrin M., Ishigami A., Mechin M.-C., Nachat R., Valmary S., Sebbag M., Simon M., Senshu T., Serre G.
    Biochem. J. 370:167-174(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Epidermis.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiPADI1_HUMAN
AccessioniPrimary (citable) accession number: Q9ULC6
Secondary accession number(s): A1L4K6, Q70SX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2001
Last sequence update: December 20, 2004
Last modified: March 31, 2015
This is version 112 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.