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Protein

Protein-arginine deiminase type-6

Gene

PADI6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the deimination of arginine residues of proteins. May be involved in cytoskeletal reorganization in the egg and early embryo (By similarity).By similarity

Catalytic activityi

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

Cofactori

Ca2+By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciMetaCyc:G66-31585-MONOMER.
BRENDAi3.5.3.15. 2681.
ReactomeiR-HSA-3247509. Chromatin modifying enzymes.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-arginine deiminase type-6 (EC:3.5.3.15)
Alternative name(s):
Peptidyl arginine deiminase-like protein
Peptidylarginine deiminase VI
Short name:
hPADVI
Protein-arginine deiminase type VI
Gene namesi
Name:PADI6
Synonyms:PAD6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:20449. PADI6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134975206.

Chemistry

DrugBankiDB00155. L-Citrulline.

Polymorphism and mutation databases

BioMutaiPADI6.
DMDMi408360253.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 694694Protein-arginine deiminase type-6PRO_0000220036Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Phosphoserine1 Publication
Modified residuei446 – 4461Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation at Ser-10, possibly by RSK-type kinases, and Ser-446 creates binding sites for 14-3-3 proteins.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ6TGC4.

PTM databases

iPTMnetiQ6TGC4.

Expressioni

Tissue specificityi

Ovary, testis and peripheral blood leukocytes.1 Publication

Gene expression databases

CleanExiHS_PADI6.

Interactioni

Protein-protein interaction databases

IntActiQ6TGC4. 1 interaction.

Chemistry

BindingDBiQ6TGC4.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DATX-ray1.40B441-449[»]
4DAUX-ray2.00B1-13[»]
ProteinModelPortaliQ6TGC4.
SMRiQ6TGC4. Positions 13-694.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi501 – 5044Poly-Leu

Sequence similaritiesi

Belongs to the protein arginine deiminase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000008680.
HOVERGENiHBG053016.
InParanoidiQ6TGC4.
KOiK01481.
OMAiPLEVYLC.
PhylomeDBiQ6TGC4.

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.

Q6TGC4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSVEGRAMS FQSIIHLSLD SPVHAVCVLG TEICLDLSGC APQKCQCFTI
60 70 80 90 100
HGSGRVLIDV ANTVISEKED ATIWWPLSDP TYATVKMTSP SPSVDADKVS
110 120 130 140 150
VTYYGPNEDA PVGTAVLYLT GIEVSLEVDI YRNGQVEMSS DKQAKKKWIW
160 170 180 190 200
GPSGWGAILL VNCNPADVGQ QLEDKKTKKV IFSEEITNLS QMTLNVQGPS
210 220 230 240 250
CILKKYRLVL HTSKEESKKA RVYWPQKDNS STFELVLGPD QHAYTLALLG
260 270 280 290 300
NHLKETFYVE AIAFPSAEFS GLISYSVSLV EESQDPSIPE TVLYKDTVVF
310 320 330 340 350
RVAPCVFIPC TQVPLEVYLC RELQLQGFVD TVTKLSEKSN SQVASVYEDP
360 370 380 390 400
NRLGRWLQDE MAFCYTQAPH KTTSLILDTP QAADLDEFPM KYSLSPGIGY
410 420 430 440 450
MIQDTEDHKV ASMDSIGNLM VSPPVKVQGK EYPLGRVLIG SSFYPSAEGR
460 470 480 490 500
AMSKTLRDFL YAQQVQAPVE LYSDWLMTGH VDEFMCFIPT DDKNEGKKGF
510 520 530 540 550
LLLLASPSAC YKLFREKQKE GYGDALLFDE LRADQLLSNG REAKTIDQLL
560 570 580 590 600
ADESLKKQNE YVEKCIHLNR DILKTELGLV EQDIIEIPQL FCLEKLTNIP
610 620 630 640 650
SDQQPKRSFA RPYFPDLLRM IVMGKNLGIP KPFGPQIKGT CCLEEKICCL
660 670 680 690
LEPLGFKCTF INDFDCYLTE VGDICACANI RRVPFAFKWW KMVP
Length:694
Mass (Da):77,727
Last modified:October 3, 2012 - v3
Checksum:i5D56D6AFF5CE36AD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti487 – 4871F → S in AAS07634 (PubMed:15625577).Curated
Sequence conflicti517 – 5171K → N in AAS07634 (PubMed:15625577).Curated
Sequence conflicti623 – 6231M → I in AAR38850 (PubMed:15087120).Curated
Sequence conflicti686 – 6861A → T in AAR38850 (PubMed:15087120).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY443100 mRNA. Translation: AAS07634.1.
AY422079 mRNA. Translation: AAR38850.1.
AJ549502 Genomic DNA. Translation: CAD70706.1.
CCDSiCCDS72715.1.
RefSeqiNP_997304.3. NM_207421.4.
UniGeneiHs.531598.

Genome annotation databases

EnsembliENST00000619609; ENSP00000483125; ENSG00000276747.
ENST00000625380; ENSP00000485805; ENSG00000280949.
GeneIDi353238.
KEGGihsa:353238.
UCSCiuc031trf.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY443100 mRNA. Translation: AAS07634.1.
AY422079 mRNA. Translation: AAR38850.1.
AJ549502 Genomic DNA. Translation: CAD70706.1.
CCDSiCCDS72715.1.
RefSeqiNP_997304.3. NM_207421.4.
UniGeneiHs.531598.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DATX-ray1.40B441-449[»]
4DAUX-ray2.00B1-13[»]
ProteinModelPortaliQ6TGC4.
SMRiQ6TGC4. Positions 13-694.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6TGC4. 1 interaction.

Chemistry

BindingDBiQ6TGC4.
DrugBankiDB00155. L-Citrulline.

PTM databases

iPTMnetiQ6TGC4.

Polymorphism and mutation databases

BioMutaiPADI6.
DMDMi408360253.

Proteomic databases

PRIDEiQ6TGC4.

Protocols and materials databases

DNASUi353238.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000619609; ENSP00000483125; ENSG00000276747.
ENST00000625380; ENSP00000485805; ENSG00000280949.
GeneIDi353238.
KEGGihsa:353238.
UCSCiuc031trf.2. human.

Organism-specific databases

CTDi353238.
GeneCardsiPADI6.
HGNCiHGNC:20449. PADI6.
MIMi610363. gene.
neXtProtiNX_Q6TGC4.
PharmGKBiPA134975206.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000008680.
HOVERGENiHBG053016.
InParanoidiQ6TGC4.
KOiK01481.
OMAiPLEVYLC.
PhylomeDBiQ6TGC4.

Enzyme and pathway databases

BioCyciMetaCyc:G66-31585-MONOMER.
BRENDAi3.5.3.15. 2681.
ReactomeiR-HSA-3247509. Chromatin modifying enzymes.

Miscellaneous databases

GenomeRNAii353238.
NextBioi99747.
PROiQ6TGC4.
SOURCEiSearch...

Gene expression databases

CleanExiHS_PADI6.

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

  1. "cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type VI."
    Zhang J., Dai J., Zhao E., Lin Y., Zeng L., Chen J., Zheng H., Wang Y., Li X., Ying K., Xie Y., Mao Y.
    Acta Biochim. Pol. 51:1051-1058(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  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 / MRNA].
    Tissue: Ovary.
  3. "Identification and structural characterization of two 14-3-3 binding sites in the human peptidylarginine deiminase type VI."
    Rose R., Rose M., Ottmann C.
    J. Struct. Biol. 180:65-72(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-13 IN COMPLEX WITH SFN, X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 441-449 IN COMPLEX WITH SFN, PHOSPHORYLATION AT SER-10 AND SER-446.

Entry informationi

Entry nameiPADI6_HUMAN
AccessioniPrimary (citable) accession number: Q6TGC4
Secondary accession number(s): Q330K5, Q70SX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: October 3, 2012
Last modified: May 11, 2016
This is version 99 of the entry and version 3 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.