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Q9ULC6

- PADI1_HUMAN

UniProt

Q9ULC6 - PADI1_HUMAN

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Protein
Protein-arginine deiminase type-1
Gene
PADI1, PDI1
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Calcium 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: 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: UniProt
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-1
PRO_0000220023Add
BLAST

Proteomic databases

PaxDbiQ9ULC6.
PeptideAtlasiQ9ULC6.
PRIDEiQ9ULC6.

PTM databases

PhosphoSiteiQ9ULC6.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ9ULC6.
BgeeiQ9ULC6.
CleanExiHS_PADI1.
GenevestigatoriQ9ULC6.

Organism-specific databases

HPAiHPA028133.

Interactioni

Protein-protein interaction databases

BioGridi118980. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9ULC6.
SMRiQ9ULC6. Positions 6-663.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG42085.
HOGENOMiHOG000220908.
HOVERGENiHBG053016.
InParanoidiQ9ULC6.
KOiK01481.
OMAiNCDRDSL.
OrthoDBiEOG7P5T09.
PhylomeDBiQ9ULC6.
TreeFamiTF331952.

Family and domain databases

InterProiIPR008972. Cupredoxin.
IPR004303. PAD.
IPR013530. PAD_C.
IPR013732. PAD_N.
IPR013733. Prot_Arg_deaminase_cen_dom.
IPR016296. Protein-arginine_deiminase_sub.
[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

MAPKRVVQLS LKMPTHAVCV VGVEAHVDIH SDVPKGANSF RVSGSSGVEV    50
FMVYNRTRVK EPIGKARWPL DTDADMVVSV GTASKELKDF KVRVSYFGEQ 100
EDQALGRSVL YLTGVDISLE VDTGRTGKVK RSQGDKKTWR WGPEGYGAIL 150
LVNCDRDNHR SAEPDLTHSW LMSLADLQDM SPMLLSCNGP DKLFDSHKLV 200
LNVPFSDSKR VRVFCARGGN SLSDYKQVLG PQCLSYEVER QPGEQEIKFY 250
VEGLTFPDAD FLGLVSLSVS LVDPGTLPEV TLFTDTVGFR MAPWIMTPNT 300
QPPEELYVCR VMDTHGSNEK FLEDMSYLTL KANCKLTICP QVENRNDRWI 350
QDEMEFGYIE APHKSFPVVF DSPRNRGLKD FPYKRILGPD FGYVTREIPL 400
PGPSSLDSFG NLDVSPPVTV GGTEYPLGRI LIGSSFPKSG GRQMARAVRN 450
FLKAQQVQAP VELYSDWLSV GHVDEFLTFV PTSDQKGFRL LLASPSACLK 500
LFQEKKEEGY GEAAQFDGLK HQAKRSINEM LADRHLQRDN LHAQKCIDWN 550
RNVLKRELGL AESDIVDIPQ LFFLKNFYAE AFFPDMVNMV VLGKYLGIPK 600
PYGPIINGRC CLEEKVQSLL EPLGLHCIFI DDYLSYHELQ GEIHCGTNVR 650
RKPFPFKWWN MVP 663
Length:663
Mass (Da):74,666
Last modified:December 21, 2004 - v2
Checksum:i4674CEBC03A7E7CA
GO

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti420 – 4201V → G in BAA85771. 1 Publication
Sequence conflicti499 – 4991L → P in BAA85771. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS178.1.
RefSeqi NP_037490.2. NM_013358.2.
UniGenei Hs.412941.

3D structure databases

ProteinModelPortali Q9ULC6.
SMRi Q9ULC6. Positions 6-663.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118980. 1 interaction.

Chemistry

BindingDBi Q9ULC6.
ChEMBLi CHEMBL1909486.
DrugBanki DB00155. L-Citrulline.

PTM databases

PhosphoSitei Q9ULC6.

Polymorphism databases

DMDMi 56757695.

Proteomic databases

PaxDbi Q9ULC6.
PeptideAtlasi Q9ULC6.
PRIDEi Q9ULC6.

Protocols and materials databases

DNASUi 29943.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375471 ; ENSP00000364620 ; ENSG00000142623 .
GeneIDi 29943.
KEGGi hsa:29943.
UCSCi uc001bah.1. human.

Organism-specific databases

CTDi 29943.
GeneCardsi GC01P017531.
HGNCi HGNC:18367. PADI1.
HPAi HPA028133.
MIMi 607934. gene.
neXtProti NX_Q9ULC6.
PharmGKBi PA32899.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG42085.
HOGENOMi HOG000220908.
HOVERGENi HBG053016.
InParanoidi Q9ULC6.
KOi K01481.
OMAi NCDRDSL.
OrthoDBi EOG7P5T09.
PhylomeDBi Q9ULC6.
TreeFami TF331952.

Enzyme and pathway databases

BioCyci MetaCyc:HS06945-MONOMER.
BRENDAi 3.5.3.15. 2681.

Miscellaneous databases

GeneWikii PADI1.
GenomeRNAii 29943.
NextBioi 52603.
PROi Q9ULC6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9ULC6.
Bgeei Q9ULC6.
CleanExi HS_PADI1.
Genevestigatori Q9ULC6.

Family and domain databases

InterProi IPR008972. Cupredoxin.
IPR004303. PAD.
IPR013530. PAD_C.
IPR013732. PAD_N.
IPR013733. Prot_Arg_deaminase_cen_dom.
IPR016296. Protein-arginine_deiminase_sub.
[Graphical view ]
PANTHERi PTHR10837. PTHR10837. 1 hit.
Pfami PF03068. PAD. 1 hit.
PF08527. PAD_M. 1 hit.
PF08526. PAD_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF001247. Protein-arginine_deiminase. 1 hit.
SUPFAMi SSF110083. SSF110083. 1 hit.
SSF49503. SSF49503. 1 hit.
ProtoNeti Search...

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(2003) [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(2004) [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(2006) [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(2004) [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 11, 2001
Last sequence update: December 21, 2004
Last modified: September 3, 2014
This is version 106 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

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