Reviewed,
UniProtKB/Swiss-Prot Q9BSU3 (ARD1B_HUMAN)
Last modified
October 13, 2009.
Version 51.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: N-terminal acetyltransferase complex ARD1 subunit homolog B Short name=hARD2 EC=2.3.1.88 | ||||
| Gene names |
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| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 229 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | In complex with NARG1, displays alpha (N-terminal) acetyltransferase activity. Ref.2 |
| Catalytic activity | Acetyl-CoA + peptide = N(alpha)-acetylpeptide + CoA. |
| Subunit structure | Interacts with NARG1 and HIF1A. Ref.2 |
| Subcellular location | |
| Tissue specificity | Present in several cell lines, with highest levels in MCF-7 cells (at protein level). Ref.2 |
| Sequence similarities | Belongs to the acetyltransferase family. ARD1 subfamily. Contains 1 N-acetyltransferase domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Nucleus |
| Coding sequence diversity | Polymorphism |
| Molecular function | Acyltransferase Transferase |
| PTM | Acetylation |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleusInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | peptide alpha-N-acetyltransferase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 229 | 229 | N-terminal acetyltransferase complex ARD1 subunit homolog B | PRO_0000305009 | |||||
Regions | |||||||||
| Domain | 1 – 152 | 152 | N-acetyltransferase | ||||||
| Region | 1 – 58 | 58 | Interaction with NARG1 By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 136 | 1 | N6-acetyllysine Ref.3 | ||||||
Natural variations | |||||||||
| Natural variant | 6 | 1 | A → T: dbSNP rs3811765. | VAR_048164 | |||||
| Natural variant | 19 | 1 | L → F: dbSNP rs17003712. | VAR_048165 | |||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin. |
| [2] | "Characterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-alpha-acetyltransferase." Arnesen T., Betts M.J., Pendino F., Liberles D.A., Anderson D., Caro J., Kong X., Varhaug J.E., Lillehaug J.R. BMC Biochem. 7:13-13(2006) [PubMed: 16638120] [Abstract] Cited for: FUNCTION, INTERACTION WITH NARG1 AND HIF1A, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. |
| [3] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-136, MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| BC004552 mRNA. Translation: AAH04552.2. Different initiation. BC063623 mRNA. Translation: AAH63623.1. Different initiation. BC080651 mRNA. Translation: AAH80651.1. Different initiation. | |
| IPI | IPI00455623. |
| RefSeq | NP_116082.1. |
| UniGene | Hs.676048 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9BSU3. |
Proteomic databases | |
| PRIDE | Q9BSU3. |
Genome annotation databases | |
| Ensembl | ENST00000286794; ENSP00000286794; ENSG00000156269; Homo sapiens. [Genome view] |
| GeneID | 84779. |
| KEGG | hsa:84779. |
| UCSC | uc003hlt.2. human. |
Organism-specific databases | |
| CTD | 84779. |
| GeneCards | GC04M080456. |
| HGNC | HGNC:28125. ARD1B. |
| PharmGKB | PA142672595. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | Q9BSU3. |
Enzyme and pathway databases | |
| BRENDA | 2.3.1.88. 247. |
Gene expression databases | |
| ArrayExpress | Q9BSU3. |
| Bgee | Q9BSU3. |
| CleanEx | HS_ARD1B. |
| Genevestigator | Q9BSU3. |
Family and domain databases | |
| InterPro | IPR016181. Acyl_CoA_acyltransferase. IPR000182. GCN5-rel_AcTrfase. [Graphical view] |
| Gene3D | G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit. |
| Pfam | PF00583. Acetyltransf_1. 1 hit. [Graphical view] |
| PROSITE | PS51186. GNAT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 74933. |
Entry information
| Entry name | ARD1B_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9BSU3 Secondary accession number(s): Q66K19, Q6P479 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome 4 Human chromosome 4: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| SIMILARITY comments Index of protein domains and families |

Clusters with


