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P17707

- DCAM_HUMAN

UniProt

P17707 - DCAM_HUMAN

Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

AMD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels By similarity.By similarity

    Catalytic activityi

    S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2.

    Cofactori

    Pyruvoyl group.

    Enzyme regulationi

    Both proenzyme processing and catalytic activity are stimulated by putrescine. Catalytic activity is inhibited by iodoacetic acid.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei7 – 71Substrate
    Active sitei8 – 81
    Active sitei11 – 111
    Sitei67 – 682Cleavage (non-hydrolytic); by autolysis
    Binding sitei67 – 671Substrate
    Active sitei68 – 681Schiff-base intermediate with substrate; via pyruvic acid
    Active sitei82 – 821Proton donor; for catalytic activity
    Binding sitei223 – 2231Substrate
    Active sitei229 – 2291Proton acceptor; for processing activity
    Active sitei243 – 2431Proton acceptor; for processing activity
    Binding sitei247 – 2471Substrate

    GO - Molecular functioni

    1. adenosylmethionine decarboxylase activity Source: UniProtKB

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. polyamine metabolic process Source: Reactome
    3. S-adenosylmethioninamine biosynthetic process Source: UniProtKB-UniPathway
    4. small molecule metabolic process Source: Reactome
    5. spermidine biosynthetic process Source: UniProtKB-KW
    6. spermine biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Polyamine biosynthesis, Spermidine biosynthesis

    Keywords - Ligandi

    Pyruvate, S-adenosyl-L-methionine, Schiff base

    Enzyme and pathway databases

    BRENDAi4.1.1.50. 2681.
    ReactomeiREACT_14820. Metabolism of polyamines.
    SABIO-RKP17707.
    UniPathwayiUPA00331; UER00451.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-adenosylmethionine decarboxylase proenzyme (EC:4.1.1.50)
    Short name:
    AdoMetDC
    Short name:
    SAMDC
    Cleaved into the following 2 chains:
    Gene namesi
    Name:AMD1
    Synonyms:AMD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:457. AMD1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71F → A: No effect. 2 Publications
    Mutagenesisi8 – 81E → Q: Loss of activity. Normal putrescine-stimulated processing. 1 Publication
    Mutagenesisi11 – 111E → Q: Loss of activity. Loss of putrescine-stimulated processing. 1 Publication
    Mutagenesisi15 – 151E → Q: Little effect. 1 Publication
    Mutagenesisi49 – 491C → A: Little effect. 1 Publication
    Mutagenesisi61 – 611E → Q: Little effect. 1 Publication
    Mutagenesisi67 – 671E → Q: Little effect. 1 Publication
    Mutagenesisi80 – 801K → A: Greatly reduced catalytic activity. No putrescine-stimulated processing. 1 Publication
    Mutagenesisi82 – 821C → A: Loss of activity. Greatly reduced putrescine-stimulated processing. 1 Publication
    Mutagenesisi223 – 2231F → A: No effect. 2 Publications
    Mutagenesisi226 – 2261C → A: Little effect. 1 Publication
    Mutagenesisi229 – 2291S → A: Loss of processing. 2 Publications
    Mutagenesisi229 – 2291S → C: Greatly reduced processing. 2 Publications
    Mutagenesisi229 – 2291S → T: Greatly reduced catalytic activity but little effect on processing. 2 Publications
    Mutagenesisi243 – 2431H → A: Greatly reduced catalytic activity and processing. 2 Publications
    Mutagenesisi243 – 2431H → E: Greatly reduced catalytic activity and processing. 2 Publications
    Mutagenesisi243 – 2431H → F: Loss of processing. 2 Publications
    Mutagenesisi243 – 2431H → Y: Loss of processing. 2 Publications
    Mutagenesisi247 – 2471E → Q: Little effect. 1 Publication
    Mutagenesisi249 – 2491E → Q: Little effect. 1 Publication

    Organism-specific databases

    PharmGKBiPA24763.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 6767S-adenosylmethionine decarboxylase beta chainPRO_0000029959Add
    BLAST
    Chaini68 – 334267S-adenosylmethionine decarboxylase alpha chainPRO_0000029960Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei68 – 681Pyruvic acid (Ser); by autocatalysis
    Modified residuei298 – 2981Phosphoserine1 Publication

    Post-translational modificationi

    Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.

    Keywords - PTMi

    Autocatalytic cleavage, Phosphoprotein, Zymogen

    Proteomic databases

    MaxQBiP17707.
    PaxDbiP17707.
    PRIDEiP17707.

    PTM databases

    PhosphoSiteiP17707.

    Miscellaneous databases

    PMAP-CutDBP17707.

    Expressioni

    Gene expression databases

    ArrayExpressiP17707.
    BgeeiP17707.
    CleanExiHS_AMD1.
    GenevestigatoriP17707.

    Organism-specific databases

    HPAiHPA029281.
    HPA029282.

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha and two beta chains.

    Protein-protein interaction databases

    BioGridi106759. 3 interactions.
    DIPiDIP-363N.
    STRINGi9606.ENSP00000357880.

    Structurei

    Secondary structure

    1
    334
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 198
    Helixi32 – 343
    Helixi37 – 459
    Turni46 – 483
    Beta strandi51 – 566
    Beta strandi58 – 658
    Beta strandi70 – 8112
    Helixi87 – 904
    Helixi91 – 10212
    Beta strandi106 – 11510
    Helixi120 – 1223
    Helixi130 – 1389
    Beta strandi142 – 1509
    Beta strandi157 – 1626
    Beta strandi175 – 1839
    Helixi186 – 1894
    Helixi190 – 1923
    Helixi200 – 2067
    Helixi209 – 2113
    Beta strandi212 – 2154
    Beta strandi217 – 2226
    Beta strandi224 – 2263
    Beta strandi228 – 2336
    Beta strandi239 – 2457
    Helixi248 – 2503
    Beta strandi252 – 2576
    Helixi265 – 27511
    Beta strandi278 – 28710
    Helixi291 – 2966
    Beta strandi305 – 31410
    Beta strandi316 – 32712

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I72X-ray2.00A68-334[»]
    B1-67[»]
    1I79X-ray2.01A68-334[»]
    B1-67[»]
    1I7BX-ray1.90A68-334[»]
    B1-67[»]
    1I7CX-ray2.40A68-334[»]
    B1-67[»]
    1I7MX-ray2.24A/C68-334[»]
    B/D1-67[»]
    1JENX-ray2.25A/C69-334[»]
    B/D1-67[»]
    1JL0X-ray1.50A/B1-334[»]
    1MSVX-ray1.75A/B1-334[»]
    3DZ2X-ray1.86A69-334[»]
    B1-67[»]
    3DZ3X-ray2.62A69-334[»]
    B1-67[»]
    3DZ4X-ray1.84A69-334[»]
    B1-67[»]
    3DZ5X-ray2.43A69-334[»]
    B1-67[»]
    3DZ6X-ray1.83A69-334[»]
    B1-67[»]
    3DZ7X-ray1.91A69-334[»]
    B1-67[»]
    3EP3X-ray1.84A69-328[»]
    B1-67[»]
    3EP4X-ray1.89A69-328[»]
    B1-67[»]
    3EP5X-ray1.99A69-328[»]
    B1-67[»]
    3EP6X-ray1.70A69-328[»]
    B1-67[»]
    3EP7X-ray2.00A69-328[»]
    B1-67[»]
    3EP8X-ray1.97A69-328[»]
    B1-67[»]
    3EP9X-ray2.35A69-328[»]
    B1-67[»]
    3EPAX-ray2.10A69-328[»]
    B1-67[»]
    3EPBX-ray1.75A69-328[»]
    B1-67[»]
    3H0VX-ray2.24A69-334[»]
    B1-67[»]
    3H0WX-ray1.81A69-334[»]
    B1-67[»]
    ProteinModelPortaliP17707.
    SMRiP17707. Positions 4-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17707.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the eukaryotic AdoMetDC family.Curated

    Phylogenomic databases

    eggNOGiNOG77566.
    HOGENOMiHOG000159915.
    HOVERGENiHBG000761.
    InParanoidiP17707.
    KOiK01611.
    OMAiTIPRFEW.
    OrthoDBiEOG780RMV.
    PhylomeDBiP17707.
    TreeFamiTF313561.

    Family and domain databases

    Gene3Di3.60.90.10. 1 hit.
    InterProiIPR001985. S-AdoMet_decarboxylase.
    IPR018167. S-AdoMet_decarboxylase_subgr.
    IPR016067. S-AdoMet_deCO2ase_core.
    IPR018166. S-AdoMet_deCO2ase_CS.
    [Graphical view]
    PANTHERiPTHR11570. PTHR11570. 1 hit.
    PfamiPF01536. SAM_decarbox. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001355. S-AdenosylMet_decarboxylase. 1 hit.
    SUPFAMiSSF56276. SSF56276. 1 hit.
    TIGRFAMsiTIGR00535. SAM_DCase. 1 hit.
    PROSITEiPS01336. ADOMETDC. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P17707-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEAAHFFEGT EKLLEVWFSR QQPDANQGSG DLRTIPRSEW DILLKDVQCS    50
    IISVTKTDKQ EAYVLSESSM FVSKRRFILK TCGTTLLLKA LVPLLKLARD 100
    YSGFDSIQSF FYSRKNFMKP SHQGYPHRNF QEEIEFLNAI FPNGAAYCMG 150
    RMNSDCWYLY TLDFPESRVI SQPDQTLEIL MSELDPAVMD QFYMKDGVTA 200
    KDVTRESGIR DLIPGSVIDA TMFNPCGYSM NGMKSDGTYW TIHITPEPEF 250
    SYVSFETNLS QTSYDDLIRK VVEVFKPGKF VTTLFVNQSS KCRTVLASPQ 300
    KIEGFKRLDC QSAMFNDYNF VFTSFAKKQQ QQQS 334
    Length:334
    Mass (Da):38,340
    Last modified:October 17, 2006 - v2
    Checksum:i1BB433AF412C9179
    GO
    Isoform 2 (identifier: P17707-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-148: Missing.

    Show »
    Length:186
    Mass (Da):21,301
    Checksum:iAB97D68DA1BDB447
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti146 – 1461A → G in AAA51716. (PubMed:2460457)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 148148Missing in isoform 2. 1 PublicationVSP_043209Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21154 mRNA. Translation: AAA51716.1.
    AL832698 mRNA. Translation: CAI46113.1.
    AL357515, AL365206 Genomic DNA. Translation: CAH73388.1.
    AL365206, AL357515 Genomic DNA. Translation: CAI23233.1.
    AL357515, AL365206 Genomic DNA. Translation: CAH73390.1.
    AL365206 Genomic DNA. Translation: CAI23235.1.
    CH471051 Genomic DNA. Translation: EAW48307.1.
    CH471051 Genomic DNA. Translation: EAW48308.1.
    CH471051 Genomic DNA. Translation: EAW48309.1.
    BC000171 mRNA. Translation: AAH00171.1.
    CCDSiCCDS5086.1. [P17707-1]
    PIRiA31786. DCHUDM.
    RefSeqiNP_001625.2. NM_001634.5. [P17707-1]
    UniGeneiHs.159118.

    Genome annotation databases

    EnsembliENST00000368882; ENSP00000357877; ENSG00000123505. [P17707-2]
    ENST00000368885; ENSP00000357880; ENSG00000123505. [P17707-1]
    GeneIDi262.
    KEGGihsa:262.
    UCSCiuc003puk.1. human. [P17707-1]

    Polymorphism databases

    DMDMi116241324.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21154 mRNA. Translation: AAA51716.1 .
    AL832698 mRNA. Translation: CAI46113.1 .
    AL357515 , AL365206 Genomic DNA. Translation: CAH73388.1 .
    AL365206 , AL357515 Genomic DNA. Translation: CAI23233.1 .
    AL357515 , AL365206 Genomic DNA. Translation: CAH73390.1 .
    AL365206 Genomic DNA. Translation: CAI23235.1 .
    CH471051 Genomic DNA. Translation: EAW48307.1 .
    CH471051 Genomic DNA. Translation: EAW48308.1 .
    CH471051 Genomic DNA. Translation: EAW48309.1 .
    BC000171 mRNA. Translation: AAH00171.1 .
    CCDSi CCDS5086.1. [P17707-1 ]
    PIRi A31786. DCHUDM.
    RefSeqi NP_001625.2. NM_001634.5. [P17707-1 ]
    UniGenei Hs.159118.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1I72 X-ray 2.00 A 68-334 [» ]
    B 1-67 [» ]
    1I79 X-ray 2.01 A 68-334 [» ]
    B 1-67 [» ]
    1I7B X-ray 1.90 A 68-334 [» ]
    B 1-67 [» ]
    1I7C X-ray 2.40 A 68-334 [» ]
    B 1-67 [» ]
    1I7M X-ray 2.24 A/C 68-334 [» ]
    B/D 1-67 [» ]
    1JEN X-ray 2.25 A/C 69-334 [» ]
    B/D 1-67 [» ]
    1JL0 X-ray 1.50 A/B 1-334 [» ]
    1MSV X-ray 1.75 A/B 1-334 [» ]
    3DZ2 X-ray 1.86 A 69-334 [» ]
    B 1-67 [» ]
    3DZ3 X-ray 2.62 A 69-334 [» ]
    B 1-67 [» ]
    3DZ4 X-ray 1.84 A 69-334 [» ]
    B 1-67 [» ]
    3DZ5 X-ray 2.43 A 69-334 [» ]
    B 1-67 [» ]
    3DZ6 X-ray 1.83 A 69-334 [» ]
    B 1-67 [» ]
    3DZ7 X-ray 1.91 A 69-334 [» ]
    B 1-67 [» ]
    3EP3 X-ray 1.84 A 69-328 [» ]
    B 1-67 [» ]
    3EP4 X-ray 1.89 A 69-328 [» ]
    B 1-67 [» ]
    3EP5 X-ray 1.99 A 69-328 [» ]
    B 1-67 [» ]
    3EP6 X-ray 1.70 A 69-328 [» ]
    B 1-67 [» ]
    3EP7 X-ray 2.00 A 69-328 [» ]
    B 1-67 [» ]
    3EP8 X-ray 1.97 A 69-328 [» ]
    B 1-67 [» ]
    3EP9 X-ray 2.35 A 69-328 [» ]
    B 1-67 [» ]
    3EPA X-ray 2.10 A 69-328 [» ]
    B 1-67 [» ]
    3EPB X-ray 1.75 A 69-328 [» ]
    B 1-67 [» ]
    3H0V X-ray 2.24 A 69-334 [» ]
    B 1-67 [» ]
    3H0W X-ray 1.81 A 69-334 [» ]
    B 1-67 [» ]
    ProteinModelPortali P17707.
    SMRi P17707. Positions 4-328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106759. 3 interactions.
    DIPi DIP-363N.
    STRINGi 9606.ENSP00000357880.

    Chemistry

    BindingDBi P17707.
    ChEMBLi CHEMBL4181.
    DrugBanki DB00118. S-Adenosylmethionine.

    PTM databases

    PhosphoSitei P17707.

    Polymorphism databases

    DMDMi 116241324.

    Proteomic databases

    MaxQBi P17707.
    PaxDbi P17707.
    PRIDEi P17707.

    Protocols and materials databases

    DNASUi 262.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368882 ; ENSP00000357877 ; ENSG00000123505 . [P17707-2 ]
    ENST00000368885 ; ENSP00000357880 ; ENSG00000123505 . [P17707-1 ]
    GeneIDi 262.
    KEGGi hsa:262.
    UCSCi uc003puk.1. human. [P17707-1 ]

    Organism-specific databases

    CTDi 262.
    GeneCardsi GC06P111195.
    HGNCi HGNC:457. AMD1.
    HPAi HPA029281.
    HPA029282.
    MIMi 180980. gene.
    neXtProti NX_P17707.
    PharmGKBi PA24763.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG77566.
    HOGENOMi HOG000159915.
    HOVERGENi HBG000761.
    InParanoidi P17707.
    KOi K01611.
    OMAi TIPRFEW.
    OrthoDBi EOG780RMV.
    PhylomeDBi P17707.
    TreeFami TF313561.

    Enzyme and pathway databases

    UniPathwayi UPA00331 ; UER00451 .
    BRENDAi 4.1.1.50. 2681.
    Reactomei REACT_14820. Metabolism of polyamines.
    SABIO-RK P17707.

    Miscellaneous databases

    ChiTaRSi AMD1. human.
    EvolutionaryTracei P17707.
    GenomeRNAii 262.
    NextBioi 1029.
    PMAP-CutDB P17707.
    PROi P17707.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17707.
    Bgeei P17707.
    CleanExi HS_AMD1.
    Genevestigatori P17707.

    Family and domain databases

    Gene3Di 3.60.90.10. 1 hit.
    InterProi IPR001985. S-AdoMet_decarboxylase.
    IPR018167. S-AdoMet_decarboxylase_subgr.
    IPR016067. S-AdoMet_deCO2ase_core.
    IPR018166. S-AdoMet_deCO2ase_CS.
    [Graphical view ]
    PANTHERi PTHR11570. PTHR11570. 1 hit.
    Pfami PF01536. SAM_decarbox. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001355. S-AdenosylMet_decarboxylase. 1 hit.
    SUPFAMi SSF56276. SSF56276. 1 hit.
    TIGRFAMsi TIGR00535. SAM_DCase. 1 hit.
    PROSITEi PS01336. ADOMETDC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and regulation of mammalian S-adenosylmethionine decarboxylase."
      Pajunen A., Crozat A., Jaenne O.A., Ihalainen R., Laitinen P.H., Stanley B., Madhubala R., Pegg A.E.
      J. Biol. Chem. 263:17040-17049(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, PYRUVATE FORMATION AT SER-68.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Heart.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [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] (ISOFORM 1).
      Tissue: Placenta.
    6. "Amino acid residues necessary for putrescine stimulation of human S-adenosylmethionine decarboxylase proenzyme processing and catalytic activity."
      Stanley B.A., Pegg A.E.
      J. Biol. Chem. 266:18502-18506(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    7. "Mechanistic studies of the processing of human S-adenosylmethionine decarboxylase proenzyme. Isolation of an ester intermediate."
      Xiong H., Pegg A.E.
      J. Biol. Chem. 274:35059-35066(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-229 AND HIS-243.
    8. "Role of cysteine-82 in the catalytic mechanism of human S-adenosylmethionine decarboxylase."
      Xiong H., Stanley B.A., Pegg A.E.
      Biochemistry 38:2462-2470(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IMPORTANCE OF CYS-82 IN CATALYTIC ACTIVITY, INHIBITION BY IODOACETIC ACID.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "The crystal structure of human S-adenosylmethionine decarboxylase at 2.25-A resolution reveals a novel fold."
      Ekstrom J.L., Mathews I.I., Stanley B.A., Pegg A.E., Ealick S.E.
      Structure 7:583-595(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
    11. "The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase."
      Tolbert W.D., Ekstrom J.L., Mathews I.I., Secrist J.A. III, Kapoor P., Pegg A.E., Ealick S.E.
      Biochemistry 40:9484-9494(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), REACTION MECHANISM, MUTAGENESIS OF PHE-7 AND PHE-223.

    Entry informationi

    Entry nameiDCAM_HUMAN
    AccessioniPrimary (citable) accession number: P17707
    Secondary accession number(s): E1P5F7
    , Q5VXN4, Q5VXN6, Q9BWK4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 163 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3