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Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

AMD1

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

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

pyruvateNote: Binds 1 pyruvoyl group covalently per subunit.

Enzyme regulationi

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

Pathway: S-adenosylmethioninamine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes S-adenosylmethioninamine from S-adenosyl-L-methionine.
Proteins known to be involved in this subpathway in this organism are:
  1. S-adenosylmethionine decarboxylase proenzyme (DKFZp686G18136), S-adenosylmethionine decarboxylase proenzyme (AMD1)
This subpathway is part of the pathway S-adenosylmethioninamine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-adenosylmethioninamine from S-adenosyl-L-methionine, the pathway S-adenosylmethioninamine biosynthesis and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei7 – 71Substrate1 Publication
Active sitei8 – 81
Active sitei11 – 111
Sitei67 – 682Cleavage (non-hydrolytic); by autolysis
Binding sitei67 – 671Substrate1 Publication
Active sitei68 – 681Schiff-base intermediate with substrate; via pyruvic acid1 Publication
Active sitei82 – 821Proton donor; for catalytic activity2 Publications
Binding sitei223 – 2231Substrate1 Publication
Active sitei229 – 2291Proton acceptor; for processing activity1 Publication
Active sitei243 – 2431Proton acceptor; for processing activity1 Publication
Binding sitei247 – 2471Substrate1 Publication

GO - Molecular functioni

  • adenosylmethionine decarboxylase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:457. AMD1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71F → A: No effect. 1 Publication
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. 1 Publication
Mutagenesisi226 – 2261C → A: Little effect. 1 Publication
Mutagenesisi229 – 2291S → A: Loss of processing. 1 Publication
Mutagenesisi229 – 2291S → C: Greatly reduced processing. 1 Publication
Mutagenesisi229 – 2291S → T: Greatly reduced catalytic activity but little effect on processing. 1 Publication
Mutagenesisi243 – 2431H → A: Greatly reduced catalytic activity and processing. 1 Publication
Mutagenesisi243 – 2431H → E: Greatly reduced catalytic activity and processing. 1 Publication
Mutagenesisi243 – 2431H → F: Loss of processing. 1 Publication
Mutagenesisi243 – 2431H → Y: Loss of processing. 1 Publication
Mutagenesisi247 – 2471E → Q: Little effect. 1 Publication
Mutagenesisi249 – 2491E → Q: Little effect. 1 Publication

Organism-specific databases

PharmGKBiPA24763.

Chemistry

DrugBankiDB00118. S-Adenosylmethionine.

Polymorphism and mutation databases

DMDMi116241324.

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

BgeeiP17707.
CleanExiHS_AMD1.
ExpressionAtlasiP17707. baseline and differential.
GenevisibleiP17707. HS.

Organism-specific databases

HPAiHPA029281.
HPA029282.

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains.

Protein-protein interaction databases

BioGridi106759. 19 interactions.
DIPiDIP-363N.
IntActiP17707. 1 interaction.
STRINGi9606.ENSP00000357880.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000011776.
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. AlignAdd to basket

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

        10         20         30         40         50
MEAAHFFEGT EKLLEVWFSR QQPDANQGSG DLRTIPRSEW DILLKDVQCS
60 70 80 90 100
IISVTKTDKQ EAYVLSESSM FVSKRRFILK TCGTTLLLKA LVPLLKLARD
110 120 130 140 150
YSGFDSIQSF FYSRKNFMKP SHQGYPHRNF QEEIEFLNAI FPNGAAYCMG
160 170 180 190 200
RMNSDCWYLY TLDFPESRVI SQPDQTLEIL MSELDPAVMD QFYMKDGVTA
210 220 230 240 250
KDVTRESGIR DLIPGSVIDA TMFNPCGYSM NGMKSDGTYW TIHITPEPEF
260 270 280 290 300
SYVSFETNLS QTSYDDLIRK VVEVFKPGKF VTTLFVNQSS KCRTVLASPQ
310 320 330
KIEGFKRLDC QSAMFNDYNF VFTSFAKKQQ QQQS
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:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000368885; ENSP00000357880; ENSG00000123505. [P17707-1]
GeneIDi262.
KEGGihsa:262.
UCSCiuc003puk.1. human. [P17707-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi106759. 19 interactions.
DIPiDIP-363N.
IntActiP17707. 1 interaction.
STRINGi9606.ENSP00000357880.

Chemistry

BindingDBiP17707.
ChEMBLiCHEMBL4181.
DrugBankiDB00118. S-Adenosylmethionine.

PTM databases

PhosphoSiteiP17707.

Polymorphism and mutation databases

DMDMi116241324.

Proteomic databases

MaxQBiP17707.
PaxDbiP17707.
PRIDEiP17707.

Protocols and materials databases

DNASUi262.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368885; ENSP00000357880; ENSG00000123505. [P17707-1]
GeneIDi262.
KEGGihsa:262.
UCSCiuc003puk.1. human. [P17707-1]

Organism-specific databases

CTDi262.
GeneCardsiGC06P111195.
HGNCiHGNC:457. AMD1.
HPAiHPA029281.
HPA029282.
MIMi180980. gene.
neXtProtiNX_P17707.
PharmGKBiPA24763.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG77566.
GeneTreeiENSGT00390000011776.
HOGENOMiHOG000159915.
HOVERGENiHBG000761.
InParanoidiP17707.
KOiK01611.
OMAiTIPRFEW.
OrthoDBiEOG780RMV.
PhylomeDBiP17707.
TreeFamiTF313561.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiAMD1. human.
EvolutionaryTraceiP17707.
GenomeRNAii262.
NextBioi1029.
PMAP-CutDBP17707.
PROiP17707.
SOURCEiSearch...

Gene expression databases

BgeeiP17707.
CleanExiHS_AMD1.
ExpressionAtlasiP17707. baseline and differential.
GenevisibleiP17707. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 169 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

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.