Q5RFH3 (NDKB_PONAB) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 50.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Nucleoside diphosphate kinase B Short name=NDK B Short name=NDP kinase B EC=2.7.4.6 | ||
| Gene names |
| ||
| Organism | Pongo abelii (Sumatran orangutan) | ||
| Taxonomic identifier | 9601 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo |
Protein attributes
| Sequence length | 152 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Negatively regulates Rho activity by interacting with AKAP13/LBC. Exhibits histidine protein kinase activity By similarity. |
| Catalytic activity | ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. |
| Cofactor | Magnesium By similarity. |
| Subunit structure | Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3, A2B4, AB5, B6). Interacts with AKAP13 and CAPN8 By similarity. |
| Subcellular location | Cytoplasm. Cell membrane By similarity. |
| Sequence similarities | Belongs to the NDK family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 152 | 151 | Nucleoside diphosphate kinase B | PRO_0000250202 | |||||
Regions | |||||||||
| Region | 2 – 66 | 65 | Interaction with AKAP13 By similarity | ||||||
Sites | |||||||||
| Active site | 118 | 1 | Pros-phosphohistidine intermediate By similarity | ||||||
| Binding site | 12 | 1 | ATP By similarity | ||||||
| Binding site | 60 | 1 | ATP By similarity | ||||||
| Binding site | 88 | 1 | ATP By similarity | ||||||
| Binding site | 94 | 1 | ATP By similarity | ||||||
| Binding site | 105 | 1 | ATP By similarity | ||||||
| Binding site | 115 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 12 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 49 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 52 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 56 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 85 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 94 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 100 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 124 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 128 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR857184 mRNA. Translation: CAH89484.1. |
| RefSeq | NP_001127154.1. NM_001133682.1. |
| UniGene | Pab.9662. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1NUE based on UniProtKB P22392. |
| ProteinModelPortal | Q5RFH3. |
| SMR | Q5RFH3. Positions 2-152. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q5RFH3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 100174205. |
| KEGG | pon:100174205. |
Organism-specific databases | |
| CTD | 4831. |
Phylogenomic databases | |
| HOVERGEN | HBG000423. |
| InParanoid | Q5RFH3. |
Family and domain databases | |
| InterPro | IPR001564. Nucleoside_diP_kinase. IPR023005. Nucleoside_diP_kinase_AS. [Graphical view] |
| Gene3D | G3DSA:3.30.70.141. NDK. 1 hit. |
| KO | K00940. |
| PANTHER | PTHR11349. Nuc_diP_kinase_core. 1 hit. |
| Pfam | PF00334. NDK. 1 hit. [Graphical view] |
| PRINTS | PR01243. NUCDPKINASE. |
| SMART | SM00562. NDK. 1 hit. [Graphical view] |
| SUPFAM | SSF54919. NDK. 1 hit. |
| PROSITE | PS00469. NDP_KINASES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NDKB_PONAB | ||||||||
| Accession | Primary (citable) accession number: Q5RFH3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with