Q9BQC3 · DPH2_HUMAN
- Protein2-(3-amino-3-carboxypropyl)histidine synthase subunit 2
- GeneDPH2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids489 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (PubMed:32576952).
DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase (By similarity).
Facilitates the reduction of the catalytic iron-sulfur cluster found in the DPH1 subunit (By similarity).
DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase (By similarity).
Facilitates the reduction of the catalytic iron-sulfur cluster found in the DPH1 subunit (By similarity).
Cofactor
Note: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the DPH1 subunit.
Pathway
Protein modification; peptidyl-diphthamide biosynthesis.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | protein-containing complex | |
Molecular Function | 2-(3-amino-3-carboxypropyl)histidine synthase activity | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Biological Process | protein histidyl modification to diphthamide |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name2-(3-amino-3-carboxypropyl)histidine synthase subunit 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BQC3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Involvement in disease
Developmental delay with short stature, dysmorphic facial features, and sparse hair 2 (DEDSSH2)
- Note
- DescriptionAn autosomal recessive syndrome characterized by developmental delay with variably impaired intellectual development and speech delay, short stature, abnormal head circumference, dysmorphic facial features, and sparse scalp hair. Affected individuals may have other abnormalities, including congenital cardiac defects and distal skeletal anomalies.
- See alsoMIM:620062
Natural variants in DEDSSH2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086299 | 201 | R>C | in DEDSSH2; severely impairs diphthamide modification of elongation factor 2; dbSNP:rs767455462 | |
VAR_086300 | 308-489 | missing | in DEDSSH2; severely impairs diphthamide modification of elongation factor 2; dbSNP:rs755058688 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_086299 | 201 | in DEDSSH2; severely impairs diphthamide modification of elongation factor 2; dbSNP:rs767455462 | |||
Sequence: R → C | ||||||
Natural variant | VAR_086300 | 308-489 | in DEDSSH2; severely impairs diphthamide modification of elongation factor 2; dbSNP:rs755058688 | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 580 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000307889 | 1-489 | UniProt | 2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 | |||
Sequence: MESMFSSPAEAALQRETGVPGLLTPLPDLDGVYELERVAGFVRDLGCERVALQFPDQLLGDAVAVAARLEETTGSKMFILGDTAYGSCCVDVLGAEQAGAQALIHFGPACLSPPARPLPVAFVLRQRSVALELCVKAFEAQNPDPKAPVVLLSEPACAHALEALATLLRPRYLDLLVSSPAFPQPVGSLSPEPMPLERFGRRFPLAPGRRLEEYGAFYVGGSKASPDPDLDPDLSRLLLGWAPGQPFSSCCPDTGKTQDEGARAGRLRARRRYLVERARDARVVGLLAGTLGVAQHREALAHLRNLTQAAGKRSYVLALGRPTPAKLANFPEVDVFVLLACPLGALAPQLSGSFFQPILAPCELEAACNPAWPPPGLAPHLTHYADLLPGSPFHVALPPPESELWETPDVSLITGDLRPPPAWKSSNDHGSLALTPRPQLELAESSPAASFLSSRSWQGLEPRLGQTPVTEAVSGRRGIAIAYEDEGSG | |||||||
Modified residue | 7 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 435 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 435 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 446 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 446 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 456 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 467 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 467 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 474 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 488 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 488 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Strongly expressed in skeletal muscle. Moderately expressed in heart, small intestine, liver, pancreas, testis and colon. Weakly expressed in brain, placenta, kidney, spleen, thymus, prostate, ovary and lymphocytes.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Component of the 2-(3-amino-3-carboxypropyl)histidine synthase complex composed of DPH1, DPH2, DPH3 and a NADH-dependent reductase (By similarity).
Interacts with DPH1 (By similarity).
Interacts with DPH1 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BQC3 | CRYGA Q24JT5 | 3 | EBI-10237931, EBI-10239205 | |
BINARY | Q9BQC3 | FARS2 O95363 | 3 | EBI-10237931, EBI-2513774 | |
BINARY | Q9BQC3 | IL17A Q16552 | 3 | EBI-10237931, EBI-10237926 | |
BINARY | Q9BQC3 | MAGOH P61326 | 3 | EBI-10237931, EBI-299134 | |
BINARY | Q9BQC3 | MISP Q8IVT2 | 3 | EBI-10237931, EBI-2555085 | |
BINARY | Q9BQC3 | NEK6 Q9HC98-4 | 3 | EBI-10237931, EBI-11750983 | |
BINARY | Q9BQC3 | TNK2 Q07912-2 | 3 | EBI-10237931, EBI-11994780 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9BQC3-1
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.
- Name1
- Length489
- Mass (Da)52,083
- Last updated2001-06-01 v1
- Checksum2908FB7E816E3AEF
Q9BQC3-2
- Name2
- Differences from canonical
- 162-389: Missing
Q9BQC3-3
- Name3
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_056052 | 1-26 | in isoform 3 | |||
Sequence: MESMFSSPAEAALQRETGVPGLLTPL → MLWLWLHDWRRRQGQRCSFWVTQPTA | ||||||
Alternative sequence | VSP_056053 | 27-161 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 125-153 | in Ref. 1; AAC18086 | ||||
Sequence: RQRSVALELCVKAFEAQNPDPKAPVVLLS → SSTFCGLGTLCQDLWGPKPRPQSACGAAG | ||||||
Alternative sequence | VSP_047151 | 162-389 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 266 | in Ref. 1; AAC18086 | ||||
Sequence: R → G | ||||||
Sequence conflict | 435 | in Ref. 1; AAC18086 | ||||
Sequence: T → N | ||||||
Sequence conflict | 449 | in Ref. 1; AAC18086 | ||||
Sequence: A → V |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF053003 EMBL· GenBank· DDBJ | AAC18086.1 EMBL· GenBank· DDBJ | mRNA | ||
AK297933 EMBL· GenBank· DDBJ | BAG60250.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315506 EMBL· GenBank· DDBJ | BAG37890.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007431 EMBL· GenBank· DDBJ | AAP36099.1 EMBL· GenBank· DDBJ | mRNA | ||
AL357079 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471059 EMBL· GenBank· DDBJ | EAX07070.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001389 EMBL· GenBank· DDBJ | AAH01389.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003181 EMBL· GenBank· DDBJ | AAH03181.1 EMBL· GenBank· DDBJ | mRNA | ||
BC016956 EMBL· GenBank· DDBJ | AAH16956.1 EMBL· GenBank· DDBJ | mRNA |