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Q5BKT4 (AG10A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase

EC=2.4.1.256
Alternative name(s):
Alpha-1,2-glucosyltransferase ALG10-A
Alpha-2-glucosyltransferase ALG10-A
Asparagine-linked glycosylation protein 10 homolog A
Gene names
Name:ALG10
Synonyms:ALG10A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

Catalytic activity

Dolichyl beta-D-glucosyl phosphate + D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Glc-alpha-(1->2)-D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the ALG10 glucosyltransferase family.

Sequence caution

The sequence BAB55272.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase
PRO_0000215447

Regions

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

Experimental info

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

Sequences

Sequence LengthMass (Da)Tools
Q5BKT4 [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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-473.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ312278 mRNA. Translation: CAC41349.1.
BC070347 mRNA. Translation: AAH70347.1.
BC090948 mRNA. Translation: AAH90948.1.
AK027657 mRNA. Translation: BAB55272.1. Different initiation.
CCDSCCDS41769.1.
RefSeqNP_116223.3. NM_032834.3.
UniGeneHs.102971.

3D structure databases

ProteinModelPortalQ5BKT4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124356. 1 interaction.
STRING9606.ENSP00000266483.

Protein family/group databases

CAZyGT59. Glycosyltransferase Family 59.

PTM databases

PhosphoSiteQ5BKT4.

Polymorphism databases

DMDM74736030.

Proteomic databases

MaxQBQ5BKT4.
PaxDbQ5BKT4.
PRIDEQ5BKT4.

Protocols and materials databases

DNASU84920.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266483; ENSP00000266483; ENSG00000139133.
GeneID84920.
KEGGhsa:84920.
UCSCuc001rlm.3. human.

Organism-specific databases

CTD84920.
GeneCardsGC12P034075.
H-InvDBHIX0036775.
HGNCHGNC:23162. ALG10.
HPAHPA043329.
neXtProtNX_Q5BKT4.
Orphanet101016. Romano-Ward syndrome.
PharmGKBPA134732019.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236252.
HOGENOMHOG000240902.
HOVERGENHBG053222.
InParanoidQ5BKT4.
KOK03850.
OMAFLLTWPY.
OrthoDBEOG76HQ16.
PhylomeDBQ5BKT4.
TreeFamTF300150.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ5BKT4.
BgeeQ5BKT4.
CleanExHS_ALG10.
GenevestigatorQ5BKT4.

Family and domain databases

InterProIPR016900. Alg10.
[Graphical view]
PANTHERPTHR12989. PTHR12989. 1 hit.
PfamPF04922. DIE2_ALG10. 1 hit.
[Graphical view]
PIRSFPIRSF028810. Alpha1_2_glucosyltferase_Alg10. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi84920.
NextBio75328.
PROQ5BKT4.

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 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Human chromosome 12

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