SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P17707

- DCAM_HUMAN

UniProt

P17707 - DCAM_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
S-adenosylmethionine decarboxylase proenzyme
Gene
AMD1, AMD
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2.1 Publication

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
Complete GO annotation...

GO - Biological processi

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

Organism-specific databases

HGNCiHGNC:457. AMD1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
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.
Mutagenesisi11 – 111E → Q: Loss of activity. Loss of putrescine-stimulated processing.
Mutagenesisi15 – 151E → Q: Little effect.
Mutagenesisi49 – 491C → A: Little effect.
Mutagenesisi61 – 611E → Q: Little effect.
Mutagenesisi67 – 671E → Q: Little effect.
Mutagenesisi80 – 801K → A: Greatly reduced catalytic activity. No putrescine-stimulated processing.
Mutagenesisi82 – 821C → A: Loss of activity. Greatly reduced putrescine-stimulated processing.
Mutagenesisi223 – 2231F → A: No effect. 1 Publication
Mutagenesisi226 – 2261C → A: Little effect.
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.
Mutagenesisi249 – 2491E → Q: Little effect.

Organism-specific databases

PharmGKBiPA24763.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6767S-adenosylmethionine decarboxylase beta chain
PRO_0000029959Add
BLAST
Chaini68 – 334267S-adenosylmethionine decarboxylase alpha chain
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP17707.

Family & Domainsi

Sequence similaritiesi

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 148148Missing in isoform 2.
VSP_043209Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461A → G in AAA51716. 1 Publication

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...

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

« 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: September 3, 2014
This is version 162 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