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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pyruvate1 PublicationNote: Binds 1 pyruvoyl group covalently per subunit.1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: S-adenosylmethioninamine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes S-adenosylmethioninamine from S-adenosyl-L-methionine.6 Publications
Proteins known to be involved in this subpathway in this organism are:
  1. S-adenosylmethionine decarboxylase proenzyme (AMD1), S-adenosylmethionine decarboxylase proenzyme (DKFZp686G18136)
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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei7Substrate1 Publication1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei81 Publication1
Active sitei111 Publication1
Binding sitei67Substrate1 Publication1
Active sitei68Schiff-base intermediate with substrate; via pyruvic acid1 Publication1
Active sitei82Proton donor; for catalytic activity2 Publications1
Binding sitei223Substrate1 Publication1
Active sitei229Proton acceptor; for processing activity1 Publication1
Active sitei243Proton acceptor; for processing activity1 Publication1
Binding sitei247Substrate1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • adenosylmethionine decarboxylase activity Source: GO_Central
  • putrescine binding Source: GO_Central

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDecarboxylase, Lyase
Biological processPolyamine biosynthesis, Spermidine biosynthesis
LigandPyruvate, S-adenosyl-L-methionine, Schiff base

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.1.1.50 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-351202 Metabolism of polyamines

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P17707

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00331;UER00451

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
S-adenosylmethionine decarboxylase proenzyme (EC:4.1.1.506 Publications)
Short name:
AdoMetDC
Short name:
SAMDC
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:AMD1
Synonyms:AMD
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000123505.14

Human Gene Nomenclature Database

More...
HGNCi
HGNC:457 AMD1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
180980 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P17707

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi7F → A: No effect. 1 Publication1
Mutagenesisi8E → Q: Loss of activity. Normal putrescine-stimulated processing. 2 Publications1
Mutagenesisi11E → Q: Loss of activity. Loss of putrescine-stimulated processing. 1 Publication1
Mutagenesisi15E → Q: Little effect. 1 Publication1
Mutagenesisi49C → A: Little effect. 1 Publication1
Mutagenesisi50S → A: 17 percent decrease in catalytic activity. No effect on processing. 1 Publication1
Mutagenesisi61E → Q: Little effect. 1 Publication1
Mutagenesisi66S → A: 38 percent decrease in catalytic activity. Slight reduction in processing. 1 Publication1
Mutagenesisi67E → Q: Little effect. 1 Publication1
Mutagenesisi68 – 69SS → II: Loss of catalytic activity and processing. 1 Publication2
Mutagenesisi68S → A: Loss of catalytic activity and processing. 1 Publication1
Mutagenesisi69S → A: 24 percent decrease in catalytic activity. Slight reduction in processing. 1 Publication1
Mutagenesisi80K → A: Greatly reduced catalytic activity. No putrescine-stimulated processing. 1 Publication1
Mutagenesisi82C → A: Loss of activity. Greatly reduced putrescine-stimulated processing. 1 Publication1
Mutagenesisi223F → A: No effect. 1 Publication1
Mutagenesisi226C → A: Little effect. 1 Publication1
Mutagenesisi229S → A: Loss of processing. 1 Publication1
Mutagenesisi229S → C: Greatly reduced processing. 1 Publication1
Mutagenesisi229S → T: Greatly reduced catalytic activity but little effect on processing. 1 Publication1
Mutagenesisi243H → A: Greatly reduced catalytic activity and processing. 1 Publication1
Mutagenesisi243H → E: Greatly reduced catalytic activity and processing. 1 Publication1
Mutagenesisi243H → F: Loss of processing. 1 Publication1
Mutagenesisi243H → Y: Loss of processing. 1 Publication1
Mutagenesisi247E → Q: Little effect. 1 Publication1
Mutagenesisi249E → Q: Little effect. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
262

Open Targets

More...
OpenTargetsi
ENSG00000123505

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA24763

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4181

Drug and drug target database

More...
DrugBanki
DB08163 5'-{[4-(aminooxy)butyl](methyl)amino}-5'-deoxy-8-ethenyladenosine
DB01917 Putrescine
DB00118 S-Adenosylmethionine
DB03754 Tris

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
AMD1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
116241324

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000299591 – 67S-adenosylmethionine decarboxylase beta chainAdd BLAST67
ChainiPRO_000002996068 – 334S-adenosylmethionine decarboxylase alpha chainAdd BLAST267

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei68Pyruvic acid (Ser); by autocatalysis2 Publications1
Modified residuei298PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei67 – 68Cleavage (non-hydrolytic); by autolysis2 Publications2

Keywords - PTMi

Autocatalytic cleavage, Phosphoprotein, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P17707

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P17707

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P17707

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P17707

PeptideAtlas

More...
PeptideAtlasi
P17707

PRoteomics IDEntifications database

More...
PRIDEi
P17707

ProteomicsDB human proteome resource

More...
ProteomicsDBi
53510
53511 [P17707-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P17707

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P17707

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P17707

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000123505 Expressed in 233 organ(s), highest expression level in prostate gland

CleanEx database of gene expression profiles

More...
CleanExi
HS_AMD1

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P17707 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P17707 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA029281
HPA029282

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterotetramer of two alpha and two beta chains.1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
106759, 36 interactors

Database of interacting proteins

More...
DIPi
DIP-363N

Protein interaction database and analysis system

More...
IntActi
P17707, 3 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000357880

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P17707

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1334
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB 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[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P17707

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P17707

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P17707

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the eukaryotic AdoMetDC family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0788 Eukaryota
ENOG410XRN0 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000011776

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000159915

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG000761

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P17707

KEGG Orthology (KO)

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KOi
K01611

Identification of Orthologs from Complete Genome Data

More...
OMAi
RTDMQCC

Database of Orthologous Groups

More...
OrthoDBi
932490at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P17707

TreeFam database of animal gene trees

More...
TreeFami
TF313561

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001985 S-AdoMet_decarboxylase
IPR016067 S-AdoMet_deCO2ase_core
IPR018166 S-AdoMet_deCO2ase_CS

The PANTHER Classification System

More...
PANTHERi
PTHR11570 PTHR11570, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01536 SAM_decarbox, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001355 S-AdenosylMet_decarboxylase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56276 SSF56276, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00535 SAM_DCase, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01336 ADOMETDC, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B4DZ60B4DZ60_HUMAN
S-adenosylmethionine decarboxylase ...
AMD1
214Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5VXN5Q5VXN5_HUMAN
S-adenosylmethionine decarboxylase ...
AMD1
265Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F6R5I9F6R5I9_HUMAN
S-adenosylmethionine decarboxylase ...
AMD1
48Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti146A → G in AAA51716 (PubMed:2460457).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0432091 – 148Missing in isoform 2. 1 PublicationAdd BLAST148

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M21154 mRNA Translation: AAA51716.1
AL832698 mRNA Translation: CAI46113.1
AL357515 Genomic DNA No translation available.
AL365206 Genomic DNA No translation available.
CH471051 Genomic DNA Translation: EAW48307.1
CH471051 Genomic DNA Translation: EAW48308.1
CH471051 Genomic DNA Translation: EAW48309.1
BC000171 mRNA Translation: AAH00171.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS5086.1 [P17707-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A31786 DCHUDM

NCBI Reference Sequences

More...
RefSeqi
NP_001625.2, NM_001634.5 [P17707-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.159118

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000368885; ENSP00000357880; ENSG00000123505 [P17707-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
262

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:262

UCSC genome browser

More...
UCSCi
uc003puk.3 human [P17707-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21154 mRNA Translation: AAA51716.1
AL832698 mRNA Translation: CAI46113.1
AL357515 Genomic DNA No translation available.
AL365206 Genomic DNA No translation available.
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
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106759, 36 interactors
DIPiDIP-363N
IntActiP17707, 3 interactors
STRINGi9606.ENSP00000357880

Chemistry databases

BindingDBiP17707
ChEMBLiCHEMBL4181
DrugBankiDB08163 5'-{[4-(aminooxy)butyl](methyl)amino}-5'-deoxy-8-ethenyladenosine
DB01917 Putrescine
DB00118 S-Adenosylmethionine
DB03754 Tris

PTM databases

iPTMnetiP17707
PhosphoSitePlusiP17707

Polymorphism and mutation databases

BioMutaiAMD1
DMDMi116241324

Proteomic databases

EPDiP17707
jPOSTiP17707
MaxQBiP17707
PaxDbiP17707
PeptideAtlasiP17707
PRIDEiP17707
ProteomicsDBi53510
53511 [P17707-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
262
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368885; ENSP00000357880; ENSG00000123505 [P17707-1]
GeneIDi262
KEGGihsa:262
UCSCiuc003puk.3 human [P17707-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
262
DisGeNETi262
EuPathDBiHostDB:ENSG00000123505.14

GeneCards: human genes, protein and diseases

More...
GeneCardsi
AMD1
HGNCiHGNC:457 AMD1
HPAiHPA029281
HPA029282
MIMi180980 gene
neXtProtiNX_P17707
OpenTargetsiENSG00000123505
PharmGKBiPA24763

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0788 Eukaryota
ENOG410XRN0 LUCA
GeneTreeiENSGT00390000011776
HOGENOMiHOG000159915
HOVERGENiHBG000761
InParanoidiP17707
KOiK01611
OMAiRTDMQCC
OrthoDBi932490at2759
PhylomeDBiP17707
TreeFamiTF313561

Enzyme and pathway databases

UniPathwayi
UPA00331;UER00451

BRENDAi4.1.1.50 2681
ReactomeiR-HSA-351202 Metabolism of polyamines
SABIO-RKiP17707

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
AMD1 human
EvolutionaryTraceiP17707

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
262
PMAP-CutDBiP17707

Protein Ontology

More...
PROi
PR:P17707

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000123505 Expressed in 233 organ(s), highest expression level in prostate gland
CleanExiHS_AMD1
ExpressionAtlasiP17707 baseline and differential
GenevisibleiP17707 HS

Family and domain databases

InterProiView protein in InterPro
IPR001985 S-AdoMet_decarboxylase
IPR016067 S-AdoMet_deCO2ase_core
IPR018166 S-AdoMet_deCO2ase_CS
PANTHERiPTHR11570 PTHR11570, 1 hit
PfamiView protein in Pfam
PF01536 SAM_decarbox, 1 hit
PIRSFiPIRSF001355 S-AdenosylMet_decarboxylase, 1 hit
SUPFAMiSSF56276 SSF56276, 1 hit
TIGRFAMsiTIGR00535 SAM_DCase, 1 hit
PROSITEiView protein in PROSITE
PS01336 ADOMETDC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDCAM_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P17707
Secondary accession number(s): E1P5F7
, Q5VXN4, Q5VXN6, Q9BWK4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 17, 2006
Last modified: January 16, 2019
This is version 198 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
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