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Reviewed, UniProtKB/Swiss-Prot Q5BKT4 (AG10A_HUMAN)

Last modified July 22, 2008. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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
Name: ALG10
Synonyms: ALG10A
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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 Glc(2)Man(9)GlcNAc(2)-PP-Dol.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the ALG10 glucosyltransferase family.

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Ontologies

Keywords

   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   Molecular functionGlycosyltransferase
Transferase
   PTMPhosphoprotein

Gene Ontology (GO)

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 473473Alpha-1,2-glucosyltransferase ALG10-A

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2721 Potential
Topological domain28 – 6437Extracellular Potential
Transmembrane65 – 8521 Potential
Topological domain86 – 9712Cytoplasmic Potential
Transmembrane98 – 11821 Potential
Topological domain119 – 13012Extracellular Potential
Transmembrane131 – 15121 Potential
Transmembrane152 – 17221 Potential
Topological domain173 – 1753Extracellular Potential
Transmembrane176 – 19621 Potential
Topological domain197 – 24953Cytoplasmic Potential
Transmembrane250 – 27021 Potential
Topological domain271 – 28313Extracellular Potential
Transmembrane284 – 30421 Potential
Topological domain305 – 32319Cytoplasmic Potential
Transmembrane324 – 34421 Potential
Topological domain345 – 36723Extracellular Potential
Transmembrane368 – 38821 Potential
Topological domain389 – 3924Cytoplasmic Potential
Transmembrane393 – 41321 Potential
Topological domain414 – 43623Extracellular Potential
Transmembrane437 – 45721 Potential
Topological domain458 – 47316Cytoplasmic Potential

Amino acid modifications

Modified residue3661Phosphotyrosine
Modified residue3871Phosphoserine

Experimental info

Sequence conflict1841M → V in AAH70347. Ref.2
Sequence conflict2581I → T in CAC41349. Ref.1
Sequence conflict3841I → T in BAB55272. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
Q5BKT4-1 [UniParc].

Last modified April 12, 2005. Version 1.
Checksum: 1860D4E61ACBC2A0

FASTA47355,606
        10         20         30         40         50         60 
MAQLEGYYFS AALSCTFLVS CLLFSAFSRA LREPYMDEIF HLPQAQRYCE GHFSLSQWDP 

        70         80         90        100        110        120 
MITTLPGLYL VSIGVIKPAI WIFGWSEHVV CSIGMLRFVN LLFSVGNFYL LYLLFCKVQP 

       130        140        150        160        170        180 
RNKAASSIQR VLSTLTLAVF PTLYFFNFLY YTEAGSMFFT LFAYLMCLYG NHKTSAFLGF 

       190        200        210        220        230        240 
CGFMFRQTNI IWAVFCAGNV IAQKLTEAWK TELQKKEDRL PPIKGPFAEF RKILQFLLAY 

       250        260        270        280        290        300 
SMSFKNLSML LLLTWPYILL GFLFCAFVVV NGGIVIGDRS SHEACLHFPQ LFYFFSFTLF 

       310        320        330        340        350        360 
FSFPHLLSPS KIKTFLSLVW KRRILFFVVT LVSVFLVWKF TYAHKYLLAD NRHYTFYVWK 

       370        380        390        400        410        420 
RVFQRYETVK YLLVPAYIFA GWSIADSLKS KSIFWNLMFF ICLFTVIVPQ KLLEFRYFIL 

       430        440        450        460        470 
PYVIYRLNIP LPPTSRLICE LSCYAVVNFI TFFIFLNKTF QWPNSQDIQR FMW

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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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., 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.

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Web resources

GGDB

GlycoGene database

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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.
RefSeqNP_116223.3.
UniGeneHs.102971

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ5BKT4.

Genome annotation databases

EnsemblENSG00000139133. Homo sapiens. [Contig view]
GeneID84920.
KEGGhsa:84920.

Organism-specific databases

H-InvDBHIX0010540.
HGNCHGNC:23162. ALG10.
PharmGKBPA134732019.
GenAtlasSearch...
GeneCardsSearch...
GeneLynxSearch...

Phylogenomic databases

HOGENOMQ5BKT4.
HOVERGENQ5BKT4.

Gene expression databases

CleanExHS_ALG10.
GermOnlineENSG00000139133. Homo sapiens.

Family and domain databases

InterProIPR016900. Alpha1_2_glucosyltferase_Alg10.
IPR007006. DIE2_ALG10.
[Graphical view]
PANTHERPTHR12989. DIE2_ALG10. 1 hit.
PfamPF04922. DIE2_ALG10. 1 hit.
[Graphical view]
PIRSFPIRSF028810. Alpha1_2_glucosyltferase_Alg10. 1 hit.
ProDomQ5BKT4.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

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Entry information

Entry nameAG10A_HUMAN
AccessionPrimary (citable) accession number: Q5BKT4
Secondary accession number(s): Q6NS98, Q96DU0, Q96SM6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: April 12, 2005
Last modified: July 22, 2008
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents