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Protein

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1

Gene
N/A
Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains.UniRule annotation

Catalytic activityi

Dolichyl diphosphooligosaccharide + [protein]-L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.UniRule annotation

Pathway:iprotein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1UniRule annotation (EC:2.4.99.18UniRule annotation)
Short name:
Oligosaccharyl transferase subunit DAD1UniRule annotation
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Subcellular locationi

  • Endoplasmic reticulum membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei30 – 4920HelicalUniRule annotationAdd
BLAST
Transmembranei55 – 7319HelicalUniRule annotationAdd
BLAST
Transmembranei93 – 11220HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulumUniRule annotation, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27136.

PTM / Processingi

Proteomic databases

PRIDEiQ53G02.

Expressioni

Gene expression databases

GenevisibleiQ53G02. HS.

Interactioni

Subunit structurei

Component of the oligosaccharyltransferase (OST) complex.UniRule annotation

Protein-protein interaction databases

STRINGi9606.ENSP00000250498.

Family & Domainsi

Sequence similaritiesi

Belongs to the DAD/OST2 family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helixUniRule annotation

Phylogenomic databases

HOVERGENiHBG004452.
KOiK12668.

Family and domain databases

InterProiIPR003038. DAD/Ost2.
[Graphical view]
PANTHERiPTHR10705. PTHR10705. 1 hit.
PfamiPF02109. DAD. 1 hit.
[Graphical view]
PIRSFiPIRSF005588. DAD. 1 hit.

Sequencei

Sequence statusi: Fragment.

Q53G02-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASVVSVIS RFLEEYLSST PQRLKLLDAY LLYILLTGAL QFGYCLLVGT
60 70 80 90 100
FPFNSFLSGF ISCVGSFILA VCLRIQINPQ NKADFQGISP GRAFADFLFA
110
STILHLVVMN FVG
Length:113
Mass (Da):12,425
Last modified:May 24, 2005 - v1
Checksum:iCA1983CADCEB20F3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK223129 mRNA. Translation: BAD96849.1.
RefSeqiNP_001335.1. NM_001344.3.
UniGeneiHs.82890.

Genome annotation databases

GeneIDi1603.
KEGGihsa:1603.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK223129 mRNA. Translation: BAD96849.1.
RefSeqiNP_001335.1. NM_001344.3.
UniGeneiHs.82890.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000250498.

Proteomic databases

PRIDEiQ53G02.

Protocols and materials databases

DNASUi1603.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1603.
KEGGihsa:1603.

Organism-specific databases

CTDi1603.
PharmGKBiPA27136.

Phylogenomic databases

HOVERGENiHBG004452.
KOiK12668.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

GenomeRNAii1603.
NextBioi6578.

Gene expression databases

GenevisibleiQ53G02. HS.

Family and domain databases

InterProiIPR003038. DAD/Ost2.
[Graphical view]
PANTHERiPTHR10705. PTHR10705. 1 hit.
PfamiPF02109. DAD. 1 hit.
[Graphical view]
PIRSFiPIRSF005588. DAD. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides."
    Maruyama K., Sugano S.
    Gene 138:171-174(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library."
    Suzuki Y., Yoshitomo K., Maruyama K., Suyama A., Sugano S.
    Gene 200:149-156(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiQ53G02_HUMAN
AccessioniPrimary (citable) accession number: Q53G02
Entry historyi
Integrated into UniProtKB/TrEMBL: May 24, 2005
Last sequence update: May 24, 2005
Last modified: June 24, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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.

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.