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P61803 (DAD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1

Short name=Oligosaccharyl transferase subunit DAD1
EC=2.4.1.119
Alternative name(s):
Defender against cell death 1
Short name=DAD-1
Gene names
Name:DAD1
OrganismHomo sapiens (Human)
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

Component of the N-oligosaccharyl transferase enzyme 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-glycosyl linkage to protein L-asparagine.

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

Membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the DAD/OST2 family.

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

Transmembrane31 – 5121Helical; Potential
Transmembrane53 – 7321Helical; Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.9

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: 8413235] [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: 15489334] [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: 12665801] [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, 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: 21269460] [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.
IPIIPI00009407.
PIRA54437.
RefSeqNP_001335.1. NM_001344.2.
UniGeneHs.82890.

3D structure databases

ProteinModelPortalP61803.
ModBaseSearch...

Protein-protein interaction databases

IntActP61803. 1 interaction.
STRINGP61803.

PTM databases

PhosphoSiteP61803.

Polymorphism databases

DMDM48428858.

Proteomic databases

PRIDEP61803.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTD1603.
GeneCardsGC14M023033.
H-InvDBHIX0011517.
HGNCHGNC:2664. DAD1.
HPAHPA028882.
MIM600243. gene.
neXtProtNX_P61803.
PharmGKBPA27136.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG20630.
HOVERGENHBG004452.
InParanoidP61803.
OMAYCCLVGT.
OrthoDBEOG4G7C0W.
PhylomeDBP61803.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP61803.
BgeeP61803.
CleanExHS_DAD1.
GenevestigatorP61803.
GermOnlineENSG00000129562. Homo sapiens.

Family and domain databases

InterProIPR003038. DAD.
[Graphical view]
KOK12668.
PANTHERPTHR10705. DAD. 1 hit.
PfamPF02109. DAD. 1 hit.
[Graphical view]
PIRSFPIRSF005588. DAD. 1 hit.
ProtoNetSearch...

Other

NextBio6578.
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: January 25, 2012
This is version 79 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

Human chromosome 14

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families