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Showing toxin card for Palladium(II) acetate (T3D1575)

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Version 1.0
Creation Date 2009-06-19 21:58:59
Update Date 2010-03-18 21:54:37
Accession Number T3D1575
Name Palladium(II) acetate
Compound Type
  • Organic Compound
  • Organometallic
  • Palladium Compound
Description Palladium acetate is a chemical compound of palladium. It is used as a catalyst for many organic reactions and as a precursor to other palladium(II) compounds. Palladium is a chemical element with the chemical symbol Pd and an atomic number of 46. It is found as a free metal alloyed with gold and other platinum group metals and in the rare minerals cooperite and polarite. (S058, S070)
Synonyms
  1. Acetic Acid palladium salt
  2. Acetic Acid, palladium salt
  3. Acetic Acid, palladium(2+) salt
  4. Bis(acetato)palladium
  5. Bisacetylpalladium
  6. Diacetatopalladium
  7. Diacetoxypalladium
  8. Palladium acetate
  9. Palladium diacetate
  10. Palladium(2+) acetate
  11. Palladous acetate
Chemical IUPAC Name (acetyloxy)palladio acetate
Chemical Formula C4H6O4Pd
Chemical Structure Structure
CAS Registry Number 3375-31-3
InChI Identifier InChI=1S/2C2H4O2.Pd/c2*1-2(3)4;/h2*1H3,(H,3,4);/q;;+2/p-2
InChI Key InChIKey=YJVFFLUZDVXJQI-UHFFFAOYSA-L
PubChem Compound ID 167845 Link Image
KEGG ID Not Available
UniProt ID Not Available
OMIM ID Not Available
ChEBI ID Not Available
BioCyc ID Not Available
SuperToxic ID Not Available
CTD ID Not Available
Stitch ID Palladium(II) acetate Link Image
DrugBank ID Not Available
PDB ID Not Available
ACToR ID Not Available
Wikipedia Link Not Available
Monoisotopic Mass 223.930092
MOL File Show
PDB File Show
SDF File Show
SMILES CC(=O)O[Pd]OC(C)=O
Appearance Brown solid.
Melting Point 205 °C (478 K), decomposes
Solubility Not Available
Predicted LogP -0.1134
Route of Exposure Not Available
Mechanism of Action Due to their ability to form strong complexes with both inorganic and organic ligands, palladium ions can disturb cellular equilibria, replace other essential ions, and interact with functional groups of macromolecules, such as proteins or DNA. Palladium complexes binding to DNA and RNA leads to strand breakage. Palladium ions are able to inhibit most major cellular functions, including DNA and RNA synthesis. Palladium compounds have been shown to bind to and inhibit various enzymes, including creatine kinase and prolyl hydroxylase. (S062)
Metabolism Palladium may be absorbed through oral, dermal, and inhalation exposure. Once in the body it distributes to the kidney, liver, spleen, lymph nodes, adrenal gland, lung and bone. Palladium's ability to form complexes allows it the bind to amino acids, proteins, DNA, and other macromolecules. Palladium and its metabolites are excreted in the urine and faeces. (R062)
Toxicity Values Not Available
Lethal Dose Not Available
Carcinogenicity (IARC Classification) Not Available
Uses/Sources Palladium acetate is used as a catalyst for many organic reactions and as a precursor to other palladium(II) compounds. (S070)
Minimum Risk Level Not Available
Health Effects Contact with palladium may cause palladium sensitivity and allergy. Animal studies have shown that palladium may damage the liver and kidney. (S062)
Symptoms Skin contact with palladium may cause contact dermatitis, erythema, and oedema. (S062)
Treatment Not Available
General References
  • S062 - International Programme on Chemical Safety (IPCS) INCHEM (2002). Environmental Health Criteria for Palladium.
  • S058 - Wikipedia. Palladium. Last Updated 14 June 2009.
  • R062 - Smith DR, Kahng MW, Quintala-Vega B, Fowler BA: High-affinity renal lead-binding proteins in environmentally-exposed humans. Chem Biol Interact. 1998 Aug 14;115(1):39-52. [PubMed Link Image]
  • S070 - Wikipedia. Palladium(II) acetate. Last Updated 22 January 2009.
Targets
  1. Creatine kinase M-type
  2. Prolyl 4-hydroxylase subunit alpha-1
  3. Prolyl 4-hydroxylase subunit alpha-2
  4. Prolyl 4-hydroxylase subunit alpha-3
  5. Transmembrane prolyl 4-hydroxylase
Target 1 [top]
Target 1 ID 560
Target 1 Name Creatine kinase M-type
Target 1 Mechanism of Action Palladium inhibits creatine kinase by forming a complex with its essential SH groups. (S066)
Target 1 Description Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa
Target 1 Synonyms
  1. Creatine kinase M chain; M-CK
Target 1 Gene Name CKM
Target 1 Protein Sequence >Creatine kinase M-type 
MPFGNTHNKFKLNYKPEEEYPDLSKHNNHMAKVLTLELYKKLRDKETPSGFTVDDVIQTG
VDNPGHPFIMTVGCVAGDEESYEVFKELFDPIISDRHGGYKPTDKHKTDLNHENLKGGDD
LDPNYVLSSRVRTGRSIKGYTLPPHCSRGERRAVEKLSVEALNSLTGEFKGKYYPLKSMT
EKEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKSFLVWVNEEDHLRVISM
EKGGNMKEVFRRFCVGLQKIEEIFKKAGHPFMWNQHLGYVLTCPSNLGTGLRGGVHVKLA
HLSKHPKFEEILTRLRLQKRGTGGVDTAAVGSVFDVSNADRLGSSEVEQVQLVVDGVKLM
VEMEKKLEKGQSIDDMIPAQK
Target 1 Number of Residues 381
Target 1 Molecular Weight 43100.9
Target 1 Theoretical pI 7.28
Target 1 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
Process
Not Available
Component
Not Available
Target 1 General Function Involved in ATP binding
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non Essential
Target 1 Domain Function PF00217:ATP-gua_Ptrans PF02807:ATP-gua_PtransN
Target 1 GenBank ID Protein Not Available
Target 1 UniProtKB ID P06732 Link Image
Target 1 Cellular Location Cytoplasm
Target 1 Gene Sequence >1146 bp 
CCCAGCCCAGCCAGGTCTCCTTACACCGCCACCATGCCATTCGGTAACACCCACAACAAG
TTCAAGCTGAATTACAAGCCTGAGGAGGAGTACCCCGACCTCAGCAAACATAACAACCAC
ATGGCCAAGGTACTGACCCTTGAACTCTACAAGAAGCTGCGGGACAAGGAGATCCCATCT
GGCTTCACTGTAGACGATGTCATCCAGACAGGAGTGGACAACCCAGGTCACCCCTTCATC
ATGACCGTGGGCTGCGTGGCTGGTGATGAGGAGTCCTACGAAGTTTTCAAGGAACTCTTT
GACCCCATCATCTCGGATCGCCACGGGGGCTACAAACCCACTGACAAGCACAAGACTGAC
CTCAACCATGAAAACCTCAAGGGTGGAGACGACCTGGACCCCAACTACGTGCTCAGCAGC
CCGGTCCGCACTGGCCGCAGCATCAAGGGCTACACGTTGCCCCCACACTGCTCCCGTGGC
GAGCGCCGGGCGGTGGAGAAGCTCTCTGTGGAAGCTCTCAACAGCCTGACGGGCGAGTTC
AAAGGGAAGTACTACCCTCTGAAGAGCATGACGGAGAAGGAGCAGCAGCAGCTCATCGAT
GACCACTTCCAGTTCGACAAGCCCGTGTCCCCGCTGCTGCTGGCCTCAGGCATGGCCCGC
CACTGGCCCGACGCCCCTGGCATCTGGCACAATGACAACAAGAGCTTCCTGGTGTGGGTG
AACGAGGAGGATCACCTCCGGGTCATCTCCATGGAGAAGGGGGGCAACATGAAGGAGGTT
TTCCGCCGCTTCTGCGTAGGGCTGCAGAAGATTGAGGAGATCTTTAAGAAAGCTGGCCAC
CCCTTCATGTGGAACCAGCACCTGGGCTACGTGCTCACCTGCCCATCCAACCTGGGCACT
GGGCTGCGTGGAGGCGTGCATGTGAAGCTGGCGCACCTGAGCAAGCACCCCAAGTTCGAG
GAGATCCTCACCCGCCTGCGTCTGCAGAAGAGGGGTACAGGTGCGGTGGACACAGCTGCC
GTGGGCTCAGTATTTGACGTGTCCAACGCTGATCGGCTGGGCTCGTCCGAAGTAGAACAG
GTGCAGCTGGTGGTGGATGGTGTGAAGCTCATGGTGGAAATGGAGAAGAAGTTGGAGAAA
GGCCAG
Target 1 GenBank Gene ID Not Available
Target 1 GeneCard ID CKM Link Image
Target 1 GenAtlas ID CKM Link Image
Target 1 HGNC ID HGNC:1994 Link Image
Target 1 Chromosome Location Chromosome:19
Target 1 Locus 19q13.2-q13.3
Target 1 SNPs SNPJam Report Link Image
Target 1 Toxin References
  • S066 - Liu TZ, Khayam-Bashi H, Bhatnagar RS: Inhibition of creatine kinase activity and alterations in electrophoretic mobility by palladium ions. J Environ Pathol Toxicol. 1979 Jan-Feb;2(3):907-16. [PubMed Link Image]
Target 1 General References 3778496; 2903158; 15057824; 15489334; 3031982; 1690725; 10089465
Target 2 [top]
Target 2 ID 697
Target 2 Name Prolyl 4-hydroxylase subunit alpha-1
Target 2 Mechanism of Action Palladium irreversibly inhibits prolyl hydroxylase by replacing Fe2+ in the active site, forming a strong complex with the enzyme. (S067)
Target 2 Description Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins
Target 2 Synonyms
  1. 4-PH alpha-1; Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1
Target 2 Gene Name P4HA1
Target 2 Protein Sequence >Prolyl 4-hydroxylase subunit alpha-1 
MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWA
EKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQY
FPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADY
YHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQR
ANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKM
TPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRL
RRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANY
GVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKG
TAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE
Target 2 Number of Residues 534
Target 2 Molecular Weight 61048.8
Target 2 Theoretical pI 5.84
Target 2 GO Classification
Function
binding
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
Not Available
Target 2 General Function Involved in iron ion binding
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Signals
  • 1-17
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non Essential
Target 2 Domain Function PF03171:2OG-FeII_Oxy PF08336:P4Ha_N
Target 2 GenBank ID Protein Not Available
Target 2 UniProtKB ID P13674 Link Image
Target 2 Cellular Location Endoplasmic reticulum lumen
Target 2 Gene Sequence >1605 bp 
ATGATCTGGTATATATTAATTATAGGAATTCTGCTTCCCCAGTCTTTGGCTCATCCAGGC
TTTTTTACTTCAATTGGTCAGATGACTGATTTGATCCATACTGAGAAAGATCTGGTGACT
TCTCTGAAAGATTATATTAAGGCAGAAGAGGACAAGTTAGAACAAATAAAAAAATGGGCA
GAGAAGTTAGATCGGCTAACTAGTACAGCGACAAAAGATCCAGAAGGATTTGTTGGGCAT
CCAGTAAATGCATTCAAATTAATGAAACGTCTGAATACTGAGTGGAGTGAGTTGGAGAAT
CTGGTCCTTAAGGATATGTCAGATGGCTTTATCTCTAACCTAACCATTCAGAGACCAGTA
CTTTCTAATGATGAAGATCAGGTTGGGGCAGCCAAAGCTCTGTTACGTCTCCAGGATACC
TACAATTTGGATACAGATACCATCTCAAAGGGTAATCTTCCAGGAGTGAAACACAAATCT
TTTCTAACGGCTGAGGACTGCTTTGAGTTGGGCAAAGTGGCCTATACAGAAGCAGATTAT
TACCATACGGAACTGTGGATGGAACAAGCCCTAAGGCAACTGGATGAAGGCGAGATTTCT
ACCATAGATAAAGTCTCTGTTCTAGATTATTTGAGCTATGCGGTATATCAGCAGGGAGAC
CTGGATAAGGCACTTTTGCTCACAAAGAAGCTTCTTGAACTAGATCCTGAACATCAGAGA
GCTAATGGTAACTTAAAATATTTTGAGTATATAATGGCTAAAGAAAAAGATGTCAATAAG
TCTGCTTCAGATGACCAATCTGATCAGAAAACTACACCAAAGAAAAAAGGGGTTGCTGTG
GATTACCTGCCAGAGAGACAGAAGTACGAAATGCTGTGCCGTGGGGAGGGTATCAAAATG
ACCCCTCGGAGACAGAAAAAACTCTTTTGCCGCTACCATGATGGAAACCGTAATCCTAAA
TTTATTCTGGCTCCAGCTAAACAGGAGGATGAATGGGACAAGCCTCGTATTATTCGCTTC
CATGATATTATTTCTGATGCAGAAATTGAAATCGTCAAAGACCTAGCAAAACCAAGGCTG
AGCCGAGCTACAGTACATGACCCTGAGACTGGAAAATTGACCACAGCACAGTACAGAGTA
TCTAAGAGTGCCTGGCTCTCTGGCTATGAAAATCCTGTGGTGTCTCGAATTAATATGAGA
ATACAAGATCTAACAGGACTAGATGTTTCCACAGCAGAGGAATTACAGGTAGCAAATTAT
GGAGTTGGAGGACAGTATGAACCCCATTTTGACTTTGCACGGAAAGATGAGCCAGATGCT
TTCAAAGAGCTGGGGACAGGAAATAGAATTGCTACATGGCTGTTTTATATGAGTGATGTG
TCTGCAGGAGGAGCCACTGTTTTTCCTGAAGTTGGAGCTAGTGTTTGGCCCAAAAAAGGA
ACTGCTGTTTTCTGGTATAATCTGTTTGCCAGTGGAGAAGGAGATTATAGTACACGGCAT
GCAGCCTGTCCAGTGCTAGTTGGCAACAAATGGGTATCCAATAAATGGCTCCATGAACGT
GGACAAGAATTTCGAAGACCTTGTACGTTGTCAGAATTGGAATGA
Target 2 GenBank Gene ID Not Available
Target 2 GeneCard ID P4HA1 Link Image
Target 2 GenAtlas ID P4HA1 Link Image
Target 2 HGNC ID HGNC:8546 Link Image
Target 2 Chromosome Location Chromosome:10
Target 2 Locus 10q21.3-q23.1
Target 2 SNPs SNPJam Report Link Image
Target 2 Toxin References
  • S067 - Rapaka RS, Sorensen KR, Lee SD, Bhatnagar RS: Inhibition of hydroxyproline synthesis by palladium ions. Biochim Biophys Acta. 1976 Mar 11;429(1):63-71. [PubMed Link Image]
Target 2 General References 2543975; 7961714; 15164054; 15489334; 19159218; 15456751
Target 3 [top]
Target 3 ID 698
Target 3 Name Prolyl 4-hydroxylase subunit alpha-2
Target 3 Mechanism of Action Palladium irreversibly inhibits prolyl hydroxylase by replacing Fe2+ in the active site, forming a strong complex with the enzyme. (S067)
Target 3 Description Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins
Target 3 Synonyms
  1. 4-PH alpha-2; Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-2
Target 3 Gene Name P4HA2
Target 3 Protein Sequence >Prolyl 4-hydroxylase subunit alpha-2 
MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKS
WANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQR
QFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVDDCFGMGRSAYNEG
DYYHTVLWMEQVLKQLDAGEEATTTKSQVLDYLSYAVFQLGDLHRALELTRRLLSLDPSH
ERAGGNLRYFEQLLEEEREKTLTNQTEAELATPEGIYERPVDYLPERDVYESLCRGEGVK
LTPRRQKRLFCRYHHGNRAPQLLIAPFKEEDEWDSPHIVRYYDVMSDEEIERIKEIAKPK
LARATVRDPKTGVLTVASYRVSKSSWLEEDDDPVVARVNRRMQHITGLTVKTAELLQVAN
YGVGGQYEPHFDFSRNDERDTFKHLGTGNRVATFLNYMSDVEAGGATVFPDLGAAIWPKK
GTAVFWYNLLRSGEGDYRTRHAACPVLVGCKWVSNKWFHERGQEFLRPCGSTEVD
Target 3 Number of Residues 535
Target 3 Molecular Weight 60901.4
Target 3 Theoretical pI 5.43
Target 3 GO Classification
Function
binding
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
Not Available
Target 3 General Function Involved in electron carrier activity
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Signals
  • 1-21
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non Essential
Target 3 Domain Function PF03171:2OG-FeII_Oxy PF08336:P4Ha_N
Target 3 GenBank ID Protein Not Available
Target 3 UniProtKB ID O15460 Link Image
Target 3 Cellular Location Endoplasmic reticulum lumen
Target 3 Gene Sequence >1608 bp 
ATGAAACTCTGGGTGTCTGCATTGCTGATGGCCTGGTTTGGTGTCCTGAGCTGTGTGCAG
GCCGAATTCTTCACCTCTATTGGGCACATGACTGACCTGATTTATGCAGAGAAAGAGCTG
GTGCAGTCTCTGAAAGAGTACATCCTTGTGGAGGAAGCCAAGCTTTCCAAGATTAAGAGC
TGGGCCAACAAAATGGAAGCCTTGACTAGCAAGTCAGCTGCTGATGCTGAGGGCTACCTG
GCTCACCCTGTGAATGCCTACAAACTGGTGAAGCGGCTAAACACAGACTGGCCTGCGCTG
GAGGACCTTGTCCTGCAGGACTCAGCTGCAGGTTTTATCGCCAACCTCTCTGTGCAGCGG
CAGTTCTTCCCCACTGATGAGGACGAGATAGGAGCTGCCAAAGCCCTGATGAGACTTCAG
GACACATACAGGCTGGACCCAGGCACAATTTCCAGAGGGGAACTTCCAGGAACCAAGTAC
CAGGCAATGCTGAGTGTGGATGACTGCTTTGGGATGGGCCGCTCGGCCTACAATGAAGGG
GACTATTATCATACGGTGTTGTGGATGGAGCAGGTGCTAAAGCAGCTTGATGCCGGGGAG
GAGGCCACCACAACCAAGTCACAGGTGCTGGACTACCTCAGCTATGCTGTCTTCCAGTTG
GGTGATCTGCACCGTGCCCTGGAGCTCACCCGCCGCCTGCTCTCCCTTGACCCAAGCCAC
GAACGAGCTGGAGGGAATCTGCGGTACTTTGAGCAGTTATTGGAGGAAGAGAGAGAAAAA
ACGTTAACAAATCAGACAGAAGCTGAGCTAGCAACCCCAGAAGGCATCTATGAGAGGCCT
GTGGACTACCTGCCTGAGAGGGATGTTTACGAGAGCCTCTGTCGTGGGGAGGGTGTCAAA
CTGACACCCCGTAGACAGAAGAGGCTTTTCTGTAGGTACCACCATGGCAACAGGGCCCCA
CAGCTGCTCATTGCCCCCTTCAAAGAGGAGGACGAGTGGGACAGCCCGCACATCGTCAGG
TACTACGATGTCATGTCTGATGAGGAAATCGAGAGGATCAAGGAGATCGCAAAACCTAAA
CTTGCACGAGCCACCGTTCGTGATCCCAAGACAGGAGTCCTCACTGTCGCCAGCTACCGG
GTTTCCAAAAGCTCCTGGCTAGAGGAAGATGATGACCCTGTTGTGGCCCGAGTAAATCGT
CGGATGCAGCATATCACAGGGTTAACAGTAAAGACTGCAGAATTGTTACAGGTTGCAAAT
TATGGAGTGGGAGGACAGTATGAACCGCACTTCGACTTCTCTAGGAATGATGAGCGAGAT
ACTTTCAAGCATTTAGGGACGGGGAATCGTGTGGCTACTTTCTTAAACTACATGAGTGAT
GTAGAAGCTGGTGGTGCCACCGTCTTCCCTGATCTGGGGGCTGCAATTTGGCCTAAGAAG
GGTACAGCTGTGTTCTGGTACAACCTCTTGCGGAGCGGGGAAGGTGACTACCGAACAAGA
CATGCTGCCTGCCCTGTGCTTGTGGGCTGCAAGTGGGTCTCCAATAAGTGGTTCCATGAA
CGAGGACAGGAGTTCTTGAGACCTTGTGGATCAACAGAAGTTGACTGA
Target 3 GenBank Gene ID Not Available
Target 3 GeneCard ID P4HA2 Link Image
Target 3 GenAtlas ID P4HA2 Link Image
Target 3 HGNC ID HGNC:8547 Link Image
Target 3 Chromosome Location Not Available
Target 3 Locus 5q31
Target 3 SNPs SNPJam Report Link Image
Target 3 Toxin References
  • S067 - Rapaka RS, Sorensen KR, Lee SD, Bhatnagar RS: Inhibition of hydroxyproline synthesis by palladium ions. Biochim Biophys Acta. 1976 Mar 11;429(1):63-71. [PubMed Link Image]
Target 3 General References 9211872; 11606192; 12975309; 15489334
Target 4 [top]
Target 4 ID 699
Target 4 Name Prolyl 4-hydroxylase subunit alpha-3
Target 4 Mechanism of Action Palladium irreversibly inhibits prolyl hydroxylase by replacing Fe2+ in the active site, forming a strong complex with the enzyme. (S067)
Target 4 Description Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins
Target 4 Synonyms
  1. 4-PH alpha-3; Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-3
Target 4 Gene Name P4HA3
Target 4 Protein Sequence >Prolyl 4-hydroxylase subunit alpha-3 
MGPGARLAALLAVLALGTGDPERAAARGDTFSALTSVARALAPERRLLGLLRRYLRGEEA
RLRDLTRFYDKVLSLHEDSTTPVANPLLAFTLIKRLQSDWRNVVHSLEASENIRALKDGY
EKVEQDLPAFEDLEGAARALMRLQDVYMLNVKGLARGVFQRVTGSAITDLYSPKRLFSLT
GDDCFQVGKVAYDMGDYYHAIPWLEEAVSLFRGSYGEWKTEDEASLEDALDHLAFAYFRA
GNVSCALSLSREFLLYSPDNKRMARNVLKYERLLAESPNHVVAEAVIQRPNIPHLQTRDT
YEGLCQTLGSQPTLYQIPSLYCSYETNSNAYLLLQPIRKEVIHLEPYIALYHDFVSDSEA
QKIRELAEPWLQRSVVASGEKQLQVEYRISKSAWLKDTVDPKLVTLNHRIAALTGLDVRP
PYAEYLQVVNYGIGGHYEPHFDHATSPSSPLYRMKSGNRVATFMIYLSSVEAGGATAFIY
ANLSVPVVRNAALFWWNLHRSGEGDSDTLHAGCPVLVGDKWVANKWIHEYGQEFRRPCSS
SPED
Target 4 Number of Residues 544
Target 4 Molecular Weight 61125.7
Target 4 Theoretical pI 6.46
Target 4 GO Classification
Function
binding
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
Not Available
Target 4 General Function Involved in iron ion binding
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Signals
  • 1-19
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non Essential
Target 4 Domain Function PF03171:2OG-FeII_Oxy PF08336:P4Ha_N
Target 4 GenBank ID Protein Not Available
Target 4 UniProtKB ID Q7Z4N8 Link Image
Target 4 Cellular Location Endoplasmic reticulum lumen (Probable)
Target 4 Gene Sequence >1635 bp 
ATGGGTCCTGGGGCGCGGCTGGCGGCGCTGCTGGCGGTGCTGGCGCTCGGGACAGGAGAC
CCAGAAAGGGCTGCGGCTCGGGGCGACACGTTCTCGGCGCTGACCAGCGTGGCGCGCGCC
CTGGCGCCCGAGCGCCGGCTGCTGGGGCTGCTGAGGCGGTACCTGCGCGGGGAGGAGGCG
CGGCTGCGGGACCTGACTAGATTCTACGACAAGGTACTTTCTTTGCATGAGGATTCAACA
ACCCCTGTGGCTAACCCTCTGCTTGCATTTACTCTCATCAAACGCCTGCAGTCTGACTGG
AGGAATGTGGTACATAGTCTGGAGGCCAGTGAGAACATCCGAGCTCTGAAGGATGGCTAT
GAGAAGGTGGAGCAAGACCTTCCAGCCTTTGAGGACCTTGAGGGAGCAGCAAGGGCCCTG
ATGCGGCTGCAGGACGTGTACATGCTCAATGTGAAAGGCCTGGCCCGAGGTGTCTTTCAG
AGAGTCACTGGCTCTGCCATCACTGACCTGTACAGCCCCAAACGGCTCTTTTCTCTCACA
GGGGATGACTGCTTCCAAGTTGGCAAGGTGGCCTATGACATGGGGGATTATTACCATGCC
ATTCCATGGCTGGAGGAGGCTGTCAGTCTCTTCCGAGGATCTTACGGAGAGTGGAAGACA
GAGGATGAGGCAAGTCTAGAAGATGCCTTGGATCACTTGGCCTTTGCTTATTTCCGGGCA
GGAAATGTTTCGTGTGCCCTCAGCCTCTCTCGGGAGTTTCTTCTCTACAGCCCAGATAAT
AAGAGGATGGCCAGGAATGTCTTGAAATATGAAAGGCTCTTGGCAGAGAGCCCCAACCAC
GTGGTAGCTGAGGCTGTCATCCAGAGGCCCAATATACCCCACCTGCAGACCAGAGACACC
TACGAGGGGCTATGTCAGACCCTGGGTTCCCAGCCCACTCTCTACCAGATCCCTAGCCTC
TACTGTTCCTATGAGACCAATTCCAACGCCTACCTGCTGCTCCAGCCCATCCGGAAGGAG
GTCATCCACCTGGAGCCCTACATTGCTCTCTACCATGACTTCGTCAGTGACTCAGAGGCT
CAGAAAATTAGAGAACTTGCAGAACCATGGCTACAGAGGTCAGTGGTGGCATCAGGGGAG
AAGCAGTTACAAGTGGAGTACCGCATCAGCAAAAGTGCCTGGCTGAAGGACACTGTTGAC
CCAAAACTGGTGACCCTCAACCACCGCATTGCTGCCCTCACAGGCCTTGATGTCCGGCCT
CCCTATGCAGAGTATCTGCAGGTGGTGAACTATGGCATCGGAGGACACTATGAGCCTCAC
TTTGACCATGCTACGTCACCAAGCAGCCCCCTCTACAGAATGAAGTCAGGAAACCGAGTT
GCAACATTTATGATCTATCTGAGCTCGGTGGAAGCTGGAGGAGCCACAGCCTTCATCTAT
GCCAACCTCAGCGTGCCTGTGGTTAGGAATGCAGCACTGTTTTGGTGGAACCTGCACAGG
AGTGGTGAAGGGGACAGTGACACACTTCATGCTGGCTGTCCTGTCCTGGTGGGAGATAAG
TGGGTGGCCAACAAGTGGATACATGAGTATGGACAGGAATTCCGCAGACCCTGCAGCTCC
AGCCCTGAAGACTGA
Target 4 GenBank Gene ID Not Available
Target 4 GeneCard ID P4HA3 Link Image
Target 4 GenAtlas ID P4HA3 Link Image
Target 4 HGNC ID HGNC:30135 Link Image
Target 4 Chromosome Location Chromosome:11
Target 4 Locus 11q13.4
Target 4 SNPs SNPJam Report Link Image
Target 4 Toxin References
  • S067 - Rapaka RS, Sorensen KR, Lee SD, Bhatnagar RS: Inhibition of hydroxyproline synthesis by palladium ions. Biochim Biophys Acta. 1976 Mar 11;429(1):63-71. [PubMed Link Image]
Target 4 General References 14500733; 12874193; 12975309; 17974005; 15489334
Target 5 [top]
Target 5 ID 696
Target 5 Name Transmembrane prolyl 4-hydroxylase
Target 5 Mechanism of Action Palladium irreversibly inhibits prolyl hydroxylase by replacing Fe2+ in the active site, forming a strong complex with the enzyme. (S067)
Target 5 Description Catalyzes the post-translational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex
Target 5 Synonyms
  1. P4H-TM; HIF-prolyl hydroxylase PH-4; Hypoxia-inducible factor prolyl 4-hydroxylase
Target 5 Gene Name P4HTM
Target 5 Protein Sequence >Transmembrane prolyl 4-hydroxylase 
MAAAAVTGQRPETAAAEEASRPQWAPPDHCQAQAAAGLGDGEDAPVRPLCKPRGICSRAY
FLVLMVFVHLYLGNVLALLLFVHYSNGDESSDPGPQHRAQGPGPEPTLGPLTRLEGIKVG
HERKVQLVTDRDHFIRTLSLKPLLFEIPGFLTDEECRLIIHLAQMKGLQRSQILPTEEYE
EAMSTMQVSQLDLFRLLDQNRDGHLQLREVLAQTRLGNGWWMTPESIQEMYAAIKADPDG
DGVLSLQEFSNMDLRDFHKYMRSHKAESSELVRNSHHTWLYQGEGAHHIMRAIRQRVLRL
TRLSPEIVELSEPLQVVRYGEGGHYHAHVDSGPVYPETICSHTKLVANESVPFETSCRYM
TVLFYLNNVTGGGETVFPVADNRTYDEMSLIQDDVDLRDTRRHCDKGNLRVKPQQGTAVF
WYNYLPDGQGWVGDVDDYSLHGGCLVTRGTKWIANNWINVDPSRARQALFQQEMARLARE
GGTDSQPEWALDRAYRDARVEL
Target 5 Number of Residues 502
Target 5 Molecular Weight 56660.5
Target 5 Theoretical pI 5.99
Target 5 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
binding
ion binding
cation binding
calcium ion binding
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
Component
Not Available
Target 5 General Function Involved in calcium ion binding
Target 5 Pathways Not Available
Target 5 Reactions Not Available
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • 61-81
Target 5 Essentiality Non Essential
Target 5 Domain Function PF03171:2OG-FeII_Oxy
Target 5 GenBank ID Protein Not Available
Target 5 UniProtKB ID Q9NXG6 Link Image
Target 5 Cellular Location Endoplasmic reticulum membrane
Target 5 Gene Sequence Not Available
Target 5 GenBank Gene ID Not Available
Target 5 GeneCard ID P4HTM Link Image
Target 5 GenAtlas ID P4HTM Link Image
Target 5 HGNC ID HGNC:28858 Link Image
Target 5 Chromosome Location Not Available
Target 5 Locus 3p21.31
Target 5 SNPs SNPJam Report Link Image
Target 5 Toxin References
  • S067 - Rapaka RS, Sorensen KR, Lee SD, Bhatnagar RS: Inhibition of hydroxyproline synthesis by palladium ions. Biochim Biophys Acta. 1976 Mar 11;429(1):63-71. [PubMed Link Image]
Target 5 General References 12163023; 17974005; 15489334; 14702039; 17726031

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government.