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Protein

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

Gene

ALG10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

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.

Pathwayi

GO - Molecular functioni

  1. transferase activity, transferring hexosyl groups Source: InterPro

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
  3. post-translational protein modification Source: Reactome
  4. protein N-linked glycosylation via asparagine Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT59. Glycosyltransferase Family 59.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ALG10
Synonyms:ALG10A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:23162. ALG10.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2721HelicalSequence AnalysisAdd
BLAST
Topological domaini28 – 6437ExtracellularSequence AnalysisAdd
BLAST
Transmembranei65 – 8521HelicalSequence AnalysisAdd
BLAST
Topological domaini86 – 9712CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei98 – 11821HelicalSequence AnalysisAdd
BLAST
Topological domaini119 – 13012ExtracellularSequence AnalysisAdd
BLAST
Transmembranei131 – 15121HelicalSequence AnalysisAdd
BLAST
Transmembranei152 – 17221HelicalSequence AnalysisAdd
BLAST
Topological domaini173 – 1753ExtracellularSequence Analysis
Transmembranei176 – 19621HelicalSequence AnalysisAdd
BLAST
Topological domaini197 – 24953CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei250 – 27021HelicalSequence AnalysisAdd
BLAST
Topological domaini271 – 28313ExtracellularSequence AnalysisAdd
BLAST
Transmembranei284 – 30421HelicalSequence AnalysisAdd
BLAST
Topological domaini305 – 32319CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei324 – 34421HelicalSequence AnalysisAdd
BLAST
Topological domaini345 – 36723ExtracellularSequence AnalysisAdd
BLAST
Transmembranei368 – 38821HelicalSequence AnalysisAdd
BLAST
Topological domaini389 – 3924CytoplasmicSequence Analysis
Transmembranei393 – 41321HelicalSequence AnalysisAdd
BLAST
Topological domaini414 – 43623ExtracellularSequence AnalysisAdd
BLAST
Transmembranei437 – 45721HelicalSequence AnalysisAdd
BLAST
Topological domaini458 – 47316CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

Orphaneti101016. Romano-Ward syndrome.
PharmGKBiPA134732019.

Polymorphism and mutation databases

BioMutaiALG10.
DMDMi74736030.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferasePRO_0000215447Add
BLAST

Proteomic databases

MaxQBiQ5BKT4.
PaxDbiQ5BKT4.
PRIDEiQ5BKT4.

PTM databases

PhosphoSiteiQ5BKT4.

Expressioni

Gene expression databases

BgeeiQ5BKT4.
CleanExiHS_ALG10.
ExpressionAtlasiQ5BKT4. baseline and differential.
GenevestigatoriQ5BKT4.

Organism-specific databases

HPAiHPA043329.

Interactioni

Protein-protein interaction databases

BioGridi124356. 12 interactions.
STRINGi9606.ENSP00000266483.

Structurei

3D structure databases

ProteinModelPortaliQ5BKT4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALG10 glucosyltransferase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG236252.
GeneTreeiENSGT00390000012906.
HOGENOMiHOG000240902.
HOVERGENiHBG053222.
InParanoidiQ5BKT4.
KOiK03850.
OMAiFLLTWPY.
OrthoDBiEOG76HQ16.
PhylomeDBiQ5BKT4.
TreeFamiTF300150.

Family and domain databases

InterProiIPR016900. Alg10.
[Graphical view]
PANTHERiPTHR12989. PTHR12989. 1 hit.
PfamiPF04922. DIE2_ALG10. 1 hit.
[Graphical view]
PIRSFiPIRSF028810. Alpha1_2_glucosyltferase_Alg10. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5BKT4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQLEGYYFS AALSCTFLVS CLLFSAFSRA LREPYMDEIF HLPQAQRYCE
60 70 80 90 100
GHFSLSQWDP MITTLPGLYL VSIGVIKPAI WIFGWSEHVV CSIGMLRFVN
110 120 130 140 150
LLFSVGNFYL LYLLFCKVQP RNKAASSIQR VLSTLTLAVF PTLYFFNFLY
160 170 180 190 200
YTEAGSMFFT LFAYLMCLYG NHKTSAFLGF CGFMFRQTNI IWAVFCAGNV
210 220 230 240 250
IAQKLTEAWK TELQKKEDRL PPIKGPFAEF RKILQFLLAY SMSFKNLSML
260 270 280 290 300
LLLTWPYILL GFLFCAFVVV NGGIVIGDRS SHEACLHFPQ LFYFFSFTLF
310 320 330 340 350
FSFPHLLSPS KIKTFLSLVW KRRILFFVVT LVSVFLVWKF TYAHKYLLAD
360 370 380 390 400
NRHYTFYVWK RVFQRYETVK YLLVPAYIFA GWSIADSLKS KSIFWNLMFF
410 420 430 440 450
ICLFTVIVPQ KLLEFRYFIL PYVIYRLNIP LPPTSRLICE LSCYAVVNFI
460 470
TFFIFLNKTF QWPNSQDIQR FMW
Length:473
Mass (Da):55,606
Last modified:April 12, 2005 - v1
Checksum:i1860D4E61ACBC2A0
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841M → V in AAH70347 (PubMed:15489334).Curated
Sequence conflicti258 – 2581I → T in CAC41349 (PubMed:12200473).Curated
Sequence conflicti384 – 3841I → T in BAB55272 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ312278 mRNA. Translation: CAC41349.1.
BC070347 mRNA. Translation: AAH70347.1.
BC090948 mRNA. Translation: AAH90948.1.
AK027657 mRNA. Translation: BAB55272.1. Different initiation.
CCDSiCCDS41769.1.
RefSeqiNP_116223.3. NM_032834.3.
UniGeneiHs.102971.

Genome annotation databases

EnsembliENST00000266483; ENSP00000266483; ENSG00000139133.
GeneIDi84920.
KEGGihsa:84920.
UCSCiuc001rlm.3. human.

Polymorphism and mutation databases

BioMutaiALG10.

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ312278 mRNA. Translation: CAC41349.1.
BC070347 mRNA. Translation: AAH70347.1.
BC090948 mRNA. Translation: AAH90948.1.
AK027657 mRNA. Translation: BAB55272.1. Different initiation.
CCDSiCCDS41769.1.
RefSeqiNP_116223.3. NM_032834.3.
UniGeneiHs.102971.

3D structure databases

ProteinModelPortaliQ5BKT4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124356. 12 interactions.
STRINGi9606.ENSP00000266483.

Protein family/group databases

CAZyiGT59. Glycosyltransferase Family 59.

PTM databases

PhosphoSiteiQ5BKT4.

Polymorphism and mutation databases

BioMutaiALG10.
DMDMi74736030.

Proteomic databases

MaxQBiQ5BKT4.
PaxDbiQ5BKT4.
PRIDEiQ5BKT4.

Protocols and materials databases

DNASUi84920.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266483; ENSP00000266483; ENSG00000139133.
GeneIDi84920.
KEGGihsa:84920.
UCSCiuc001rlm.3. human.

Organism-specific databases

CTDi84920.
GeneCardsiGC12P034075.
H-InvDBHIX0036775.
HGNCiHGNC:23162. ALG10.
HPAiHPA043329.
neXtProtiNX_Q5BKT4.
Orphaneti101016. Romano-Ward syndrome.
PharmGKBiPA134732019.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG236252.
GeneTreeiENSGT00390000012906.
HOGENOMiHOG000240902.
HOVERGENiHBG053222.
InParanoidiQ5BKT4.
KOiK03850.
OMAiFLLTWPY.
OrthoDBiEOG76HQ16.
PhylomeDBiQ5BKT4.
TreeFamiTF300150.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

Miscellaneous databases

GenomeRNAii84920.
NextBioi75328.
PROiQ5BKT4.

Gene expression databases

BgeeiQ5BKT4.
CleanExiHS_ALG10.
ExpressionAtlasiQ5BKT4. baseline and differential.
GenevestigatoriQ5BKT4.

Family and domain databases

InterProiIPR016900. Alg10.
[Graphical view]
PANTHERiPTHR12989. PTHR12989. 1 hit.
PfamiPF04922. DIE2_ALG10. 1 hit.
[Graphical view]
PIRSFiPIRSF028810. Alpha1_2_glucosyltferase_Alg10. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiAG10A_HUMAN
AccessioniPrimary (citable) accession number: Q5BKT4
Secondary accession number(s): Q6NS98, Q96DU0, Q96SM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: April 12, 2005
Last modified: April 29, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.