Reviewed,
UniProtKB/Swiss-Prot Q5BKT4 (AG10A_HUMAN)
Last modified
November 3, 2009.
Version 51.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Alpha-1,2-glucosyltransferase ALG10-A EC=2.4.1.- Alternative name(s): Alpha-2-glucosyltransferase ALG10-A Asparagine-linked glycosylation protein 10 homolog A | ||||
| Gene names |
| ||||
| 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 | 473 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc2Man9GlcNAc(2)-PP-Dol. |
| Pathway | |
| Subcellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein. |
| Sequence similarities | Belongs to the ALG10 glucosyltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum Membrane |
| Domain | Transmembrane |
| Molecular function | Glycosyltransferase Transferase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Cellular component | endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | transferase activity, transferring hexosyl groups Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 473 | 473 | Alpha-1,2-glucosyltransferase ALG10-A | PRO_0000215447 | |||||
Regions | |||||||||
| Topological domain | 1 – 6 | 6 | Cytoplasmic Potential | ||||||
| Transmembrane | 7 – 27 | 21 | Potential | ||||||
| Topological domain | 28 – 64 | 37 | Extracellular Potential | ||||||
| Transmembrane | 65 – 85 | 21 | Potential | ||||||
| Topological domain | 86 – 97 | 12 | Cytoplasmic Potential | ||||||
| Transmembrane | 98 – 118 | 21 | Potential | ||||||
| Topological domain | 119 – 130 | 12 | Extracellular Potential | ||||||
| Transmembrane | 131 – 151 | 21 | Potential | ||||||
| Transmembrane | 152 – 172 | 21 | Potential | ||||||
| Topological domain | 173 – 175 | 3 | Extracellular Potential | ||||||
| Transmembrane | 176 – 196 | 21 | Potential | ||||||
| Topological domain | 197 – 249 | 53 | Cytoplasmic Potential | ||||||
| Transmembrane | 250 – 270 | 21 | Potential | ||||||
| Topological domain | 271 – 283 | 13 | Extracellular Potential | ||||||
| Transmembrane | 284 – 304 | 21 | Potential | ||||||
| Topological domain | 305 – 323 | 19 | Cytoplasmic Potential | ||||||
| Transmembrane | 324 – 344 | 21 | Potential | ||||||
| Topological domain | 345 – 367 | 23 | Extracellular Potential | ||||||
| Transmembrane | 368 – 388 | 21 | Potential | ||||||
| Topological domain | 389 – 392 | 4 | Cytoplasmic Potential | ||||||
| Transmembrane | 393 – 413 | 21 | Potential | ||||||
| Topological domain | 414 – 436 | 23 | Extracellular Potential | ||||||
| Transmembrane | 437 – 457 | 21 | Potential | ||||||
| Topological domain | 458 – 473 | 16 | Cytoplasmic Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 366 | 1 | Phosphotyrosine Ref.4 | ||||||
| Modified residue | 387 | 1 | Phosphoserine Ref.4 | ||||||
Experimental info | |||||||||
| Sequence conflict | 184 | 1 | M → V in AAH70347. Ref.2 | ||||||
| Sequence conflict | 258 | 1 | I → T in CAC41349. Ref.1 | ||||||
| Sequence conflict | 384 | 1 | I → T in BAB55272. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Common origin and evolution of glycosyltransferases using Dol-P-monosaccharides as donor substrate." Oriol R., Martinez-Duncker I., Chantret I., Mollicone R., Codogno P. Mol. Biol. Evol. 19:1451-1463(2002) [PubMed: 12200473] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Embryo. |
| [2] | "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: Brain and Lung. |
| [3] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-473. |
| [4] | "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-366 AND SER-387, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AJ312278 mRNA. Translation: CAC41349.1. BC070347 mRNA. Translation: AAH70347.1. BC090948 mRNA. Translation: AAH90948.1. AK027657 mRNA. Translation: BAB55272.1. Different initiation. | |
| IPI | IPI00414597. |
| RefSeq | NP_116223.3. |
| UniGene | Hs.714929 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q5BKT4. |
Protein family/group databases | |
| CAZy | GT59. Glycosyltransferase Family 59. |
PTM databases | |
| PhosphoSite | Q5BKT4. |
Proteomic databases | |
| PRIDE | Q5BKT4. |
Genome annotation databases | |
| Ensembl | ENST00000266483; ENSP00000266483; ENSG00000139133; Homo sapiens. [Genome view] |
| GeneID | 84920. |
| KEGG | hsa:84920. |
| UCSC | uc001rlm.1. human. |
Organism-specific databases | |
| CTD | 84920. |
| GeneCards | GC12P034066. |
| H-InvDB | HIX0010540. |
| HGNC | HGNC:23162. ALG10. |
| PharmGKB | PA134732019. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | Q5BKT4. |
| HOVERGEN | Q5BKT4. |
| OMA | WKFTYVH. |
Gene expression databases | |
| Bgee | Q5BKT4. |
| CleanEx | HS_ALG10. |
| Genevestigator | Q5BKT4. |
| GermOnline | ENSG00000139133. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR016900. Alpha1_2_glucosyltferase_Alg10. IPR007006. Glycosyltransferase_ALG10. [Graphical view] |
| PANTHER | PTHR12989. DIE2_ALG10. 1 hit. |
| Pfam | PF04922. DIE2_ALG10. 1 hit. [Graphical view] |
| PIRSF | PIRSF028810. Alpha1_2_glucosyltferase_Alg10. 1 hit. |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 75328. |
Entry information
| Entry name | AG10A_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q5BKT4 Secondary accession number(s): Q6NS98, Q96DU0, Q96SM6 | ||||||||
| Entry history |
| ||||||||
| 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 12 Human chromosome 12: entries, gene names and cross-references to MIM |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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