Q01433 · AMPD2_HUMAN
- ProteinAMP deaminase 2
- GeneAMPD2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids825 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle.
Catalytic activity
- AMP + H+ + H2O = IMP + NH4+
Cofactor
Note: Binds 1 zinc ion per subunit.
Pathway
Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 364 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 366 | substrate | ||||
Sequence: H | ||||||
Binding site | 366 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 435-440 | substrate | ||||
Sequence: KFNAKY | ||||||
Binding site | 633 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 636 | substrate | ||||
Sequence: E | ||||||
Active site | 655 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 710 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 711-714 | substrate | ||||
Sequence: DPLQ |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | AMP deaminase activity | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Biological Process | AMP metabolic process | |
Biological Process | cyclic purine nucleotide metabolic process | |
Biological Process | energy homeostasis | |
Biological Process | IMP biosynthetic process | |
Biological Process | IMP salvage |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAMP deaminase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ01433
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Involvement in disease
Pontocerebellar hypoplasia 9 (PCH9)
- Note
- DescriptionA form of pontocerebellar hypoplasia, a disorder characterized by structural defects of the pons and cerebellum, evident upon brain imaging. PCH9 features include severely delayed psychomotor development, progressive microcephaly, spasticity, seizures, and brain abnormalities, including brain atrophy, thin corpus callosum, and delayed myelination.
- See alsoMIM:615809
Natural variants in PCH9
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_071158 | 620 | R>H | in PCH9; dbSNP:rs587777395 | |
VAR_071193 | 724 | E>D | in PCH9; dbSNP:rs587777392 | |
VAR_071159 | 739 | D>Y | in PCH9; dbSNP:rs587777394 |
Spastic paraplegia 63, autosomal recessive (SPG63)
- Note
- DescriptionA form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.
- See alsoMIM:615686
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_069105 | 468 | in dbSNP:rs201254826 | |||
Sequence: I → V | ||||||
Natural variant | VAR_071158 | 620 | in PCH9; dbSNP:rs587777395 | |||
Sequence: R → H | ||||||
Natural variant | VAR_071193 | 724 | in PCH9; dbSNP:rs587777392 | |||
Sequence: E → D | ||||||
Natural variant | VAR_071159 | 739 | in PCH9; dbSNP:rs587777394 | |||
Sequence: D → Y |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 912 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000194407 | 1-825 | UniProt | AMP deaminase 2 | |||
Sequence: MASYPSGSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAPCLKHFPLDLRTSMDGKCKEIAEELFTRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLRAKQDFLKTDSDSDLQLYKEQGEGQGDRSLRERDVLEREFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYEHCEPSTMPGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALITQAVQSEMLETIPEEAGITMSPGPQ | |||||||
Modified residue | 22 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 22 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 45 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 46 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 46 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 63 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 64 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 64 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 80 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 80 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 88 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 91 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 91 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 97 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 97 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 114 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 114 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 134 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 134 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 136 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 136 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 138 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 138 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 154 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 821 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in cerebellum.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homotetramer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q01433 | CCNDBP1 O95273 | 4 | EBI-8796759, EBI-748961 | |
BINARY | Q01433 | TERF1 P54274 | 2 | EBI-8796759, EBI-710997 | |
BINARY | Q01433-2 | AMPD1 P23109 | 3 | EBI-11957578, EBI-2959675 | |
BINARY | Q01433-2 | AMPD2 Q01433-2 | 3 | EBI-11957578, EBI-11957578 | |
BINARY | Q01433-2 | NTAQ1 Q96HA8 | 3 | EBI-11957578, EBI-741158 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-49 | Disordered | ||||
Sequence: MASYPSGSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPG |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q01433-1
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.
- NameEx1B-2-3
- Length825
- Mass (Da)94,890
- Last updated2023-09-13 v3
- ChecksumF79EAD41CBA771AC
Q01433-2
- NameEx1A-2-3
Q01433-4
- NameEx1B-3
- Differences from canonical
- 1-74: MASYPSGSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAPCLKHFPLDLRTSMDGKCKEIAE → MWQSQAPAGAAQTPPLSPPWSQPWHPIHLALASPRPNIPLRSGPACRPPLQLQ
Q01433-5
- Name5
- Differences from canonical
- 1-64: Missing
Computationally mapped potential isoform sequences
There are 14 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YF16 | H0YF16_HUMAN | AMPD2 | 719 | ||
H0YE32 | H0YE32_HUMAN | AMPD2 | 40 | ||
A0A7P0T999 | A0A7P0T999_HUMAN | AMPD2 | 118 | ||
A0A804CCZ3 | A0A804CCZ3_HUMAN | AMPD2 | 788 | ||
A0A804H2H4 | A0A804H2H4_HUMAN | AMPD2 | 625 | ||
A0A7P0TB79 | A0A7P0TB79_HUMAN | AMPD2 | 237 | ||
H0Y360 | H0Y360_HUMAN | AMPD2 | 836 | ||
A0A590UJY6 | A0A590UJY6_HUMAN | AMPD2 | 38 | ||
A0A590UJX5 | A0A590UJX5_HUMAN | AMPD2 | 469 | ||
A0A590UK85 | A0A590UK85_HUMAN | AMPD2 | 564 | ||
A0A590UJD1 | A0A590UJD1_HUMAN | AMPD2 | 75 | ||
E9PJF6 | E9PJF6_HUMAN | AMPD2 | 103 | ||
A0A7P0Z4H6 | A0A7P0Z4H6_HUMAN | AMPD2 | 628 | ||
E9PIJ1 | E9PIJ1_HUMAN | AMPD2 | 87 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_001271 | 1-27 | in isoform Ex1A-2-3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_045975 | 1-64 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_001273 | 1-74 | in isoform Ex1B-3 | |||
Sequence: MASYPSGSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAPCLKHFPLDLRTSMDGKCKEIAE → MWQSQAPAGAAQTPPLSPPWSQPWHPIHLALASPRPNIPLRSGPACRPPLQLQ | ||||||
Alternative sequence | VSP_001272 | 28-30 | in isoform Ex1A-2-3 | |||
Sequence: AAP → MAS | ||||||
Sequence conflict | 153 | in Ref. 1; AAA11725 | ||||
Sequence: R → G | ||||||
Sequence conflict | 757 | in Ref. 4; BAG59062 | ||||
Sequence: V → I |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M91029 EMBL· GenBank· DDBJ | AAA62126.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
M91029 EMBL· GenBank· DDBJ | AAA62127.1 EMBL· GenBank· DDBJ | Genomic RNA | Sequence problems. | |
S47833 EMBL· GenBank· DDBJ | AAA11725.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
U16267 EMBL· GenBank· DDBJ | AAC50306.1 EMBL· GenBank· DDBJ | mRNA | ||
U16268 EMBL· GenBank· DDBJ | AAC50307.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
U16269 EMBL· GenBank· DDBJ | AAB06511.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
U16270 EMBL· GenBank· DDBJ | AAC50308.1 EMBL· GenBank· DDBJ | mRNA | ||
U16272 EMBL· GenBank· DDBJ | AAC50309.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
U16271 EMBL· GenBank· DDBJ | AAC50309.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
U16272 EMBL· GenBank· DDBJ | AAD56302.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
U16271 EMBL· GenBank· DDBJ | AAD56302.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
U16272 EMBL· GenBank· DDBJ | AAD56303.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U16271 EMBL· GenBank· DDBJ | AAD56303.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK296394 EMBL· GenBank· DDBJ | BAG59062.1 EMBL· GenBank· DDBJ | mRNA | ||
AK302939 EMBL· GenBank· DDBJ | BAG64097.1 EMBL· GenBank· DDBJ | mRNA | ||
AL355310 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471122 EMBL· GenBank· DDBJ | EAW56396.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CH471122 EMBL· GenBank· DDBJ | EAW56399.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471122 EMBL· GenBank· DDBJ | EAW56401.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC007711 EMBL· GenBank· DDBJ | AAH07711.1 EMBL· GenBank· DDBJ | mRNA | ||
BC075844 EMBL· GenBank· DDBJ | AAH75844.1 EMBL· GenBank· DDBJ | mRNA |