Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P61803 (DAD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1

Short name=Oligosaccharyl transferase subunit DAD1
EC=2.4.99.18
Alternative name(s):
Defender against cell death 1
Short name=DAD-1
Gene names
Name:DAD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length113 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). Loss of the DAD1 protein triggers apoptosis By similarity.

Catalytic activity

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.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Component of the oligosaccharyltransferase (OST) complex. OST seems to exist in different forms which contain at least RPN1, RPN2, OST48, DAD1, OSTC, KRTCAP2 and either STT3A or STT3B. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the DAD/OST2 family.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

blastocyst development

Inferred from electronic annotation. Source: Ensembl

cellular protein metabolic process

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Traceable author statement Ref.1. Source: ProtInc

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Inferred by curator PubMed 15835887. Source: HGNC

protein glycosylation

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentendoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

oligosaccharyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functiondolichyl-diphosphooligosaccharide-protein glycotransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.9
Chain2 – 113112Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
PRO_0000124009

Regions

Topological domain2 – 3029Cytoplasmic Potential
Transmembrane31 – 5121Helical; Potential
Topological domain521Lumenal Potential
Transmembrane53 – 7321Helical; Potential
Topological domain74 – 9219Cytoplasmic Potential
Transmembrane93 – 11321Helical; Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.9 Ref.11

Natural variations

Natural variant831A → T. Ref.5
Corresponds to variant rs5742796 [ dbSNP | Ensembl ].
VAR_018825

Experimental info

Sequence conflict201T → I in AAH09798. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P61803 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 481983CADCEB2345

FASTA11312,497
        10         20         30         40         50         60 
MSASVVSVIS RFLEEYLSST PQRLKLLDAY LLYILLTGAL QFGYCLLVGT FPFNSFLSGF 

        70         80         90        100        110 
ISCVGSFILA VCLRIQINPQ NKADFQGISP ERAFADFLFA STILHLVVMN FVG 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of a human cDNA encoding a novel protein, DAD1, whose defect causes apoptotic cell death in hamster BHK21 cells."
Nakashima T., Sekiguchi T., Kuraoka A., Fukushima K., Shibata Y., Komiyama S., Nishimoto T.
Mol. Cell. Biol. 13:6367-6374(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Wang K., Lee I.Y., Hood L.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]NIEHS SNPs program
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-83.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 Skin.
[8]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11.
Tissue: Platelet.
[9]Bienvenut W.V.
Submitted (JUN-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-23, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D15057 mRNA. Translation: BAA03650.1.
U84213, U84212 Genomic DNA. Translation: AAB58540.1.
CR407682 mRNA. Translation: CAG28610.1.
CR542204 mRNA. Translation: CAG47001.1.
AY259117 Genomic DNA. Translation: AAO74827.1.
CH471078 Genomic DNA. Translation: EAW66252.1.
CH471078 Genomic DNA. Translation: EAW66253.1.
BC007403 mRNA. Translation: AAH07403.1.
BC009798 mRNA. Translation: AAH09798.1.
CCDSCCDS9571.1.
PIRA54437.
RefSeqNP_001335.1. NM_001344.3.
UniGeneHs.82890.

3D structure databases

ProteinModelPortalP61803.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107973. 6 interactions.
IntActP61803. 2 interactions.
STRING9606.ENSP00000250498.

PTM databases

PhosphoSiteP61803.

Polymorphism databases

DMDM48428858.

Proteomic databases

MaxQBP61803.
PaxDbP61803.
PRIDEP61803.

Protocols and materials databases

DNASU1603.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250498; ENSP00000250498; ENSG00000129562.
GeneID1603.
KEGGhsa:1603.
UCSCuc001wgl.2. human.

Organism-specific databases

CTD1603.
GeneCardsGC14M023033.
HGNCHGNC:2664. DAD1.
HPAHPA028882.
MIM600243. gene.
neXtProtNX_P61803.
PharmGKBPA27136.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG246737.
HOVERGENHBG004452.
InParanoidP61803.
KOK12668.
OMAQSLGKAY.
OrthoDBEOG7WT43N.
PhylomeDBP61803.
TreeFamTF312846.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressP61803.
BgeeP61803.
CleanExHS_DAD1.
GenevestigatorP61803.

Family and domain databases

InterProIPR003038. DAD/Ost2.
[Graphical view]
PANTHERPTHR10705. PTHR10705. 1 hit.
PfamPF02109. DAD. 1 hit.
[Graphical view]
PIRSFPIRSF005588. DAD. 1 hit.
ProtoNetSearch...

Other

ChiTaRSDAD1. human.
GeneWikiDAD1.
GenomeRNAi1603.
NextBio6578.
PROP61803.
SOURCESearch...

Entry information

Entry nameDAD1_HUMAN
AccessionPrimary (citable) accession number: P61803
Secondary accession number(s): D3DS25 expand/collapse secondary AC list , O08552, O70364, P46966, P46968, Q6FGA3, Q96GB7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 103 of the entry and version 3 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM