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Protein

Death-associated protein 1

Gene

DAP

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

Functioni

Negative regulator of autophagy. Involved in mediating interferon-gamma-induced cell death.1 Publication

GO - Molecular functioni

  1. death domain binding Source: UniProtKB

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  2. apoptotic process Source: MGI
  3. apoptotic signaling pathway Source: UniProtKB
  4. autophagy Source: UniProtKB-KW
  5. cellular response to amino acid starvation Source: UniProtKB
  6. negative regulation of autophagy Source: UniProtKB
  7. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  8. negative regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Autophagy

Names & Taxonomyi

Protein namesi
Recommended name:
Death-associated protein 1
Short name:
DAP-1
Gene namesi
Name:DAP
Synonyms:DAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:2672. DAP.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27140.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 102101Death-associated protein 1PRO_0000079782Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei3 – 31Phosphoserine; by MTOR2 Publications
Modified residuei29 – 291N6-acetyllysineBy similarity
Modified residuei49 – 491Phosphoserine3 Publications
Modified residuei51 – 511Phosphoserine; by MTOR5 Publications
Modified residuei91 – 911Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated. Phosphorylation by MTOR inhibits the suppressive activity of DAP toward autophagy.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP51397.
PaxDbiP51397.
PeptideAtlasiP51397.
PRIDEiP51397.

PTM databases

PhosphoSiteiP51397.

Expressioni

Gene expression databases

BgeeiP51397.
CleanExiHS_DAP.
ExpressionAtlasiP51397. baseline and differential.
GenevestigatoriP51397.

Interactioni

Protein-protein interaction databases

BioGridi107981. 5 interactions.
IntActiP51397. 1 interaction.
STRINGi9606.ENSP00000230895.

Structurei

3D structure databases

ProteinModelPortaliP51397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiNOG84666.
GeneTreeiENSGT00510000049345.
HOGENOMiHOG000039719.
HOVERGENiHBG005451.
InParanoidiP51397.
OMAiVEKLPHP.
OrthoDBiEOG757D0J.
PhylomeDBiP51397.
TreeFamiTF329716.

Family and domain databases

InterProiIPR024130. DAP1/DAPL1.
[Graphical view]
PANTHERiPTHR13177. PTHR13177. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51397-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSPPEGKLE TKAGHPPAVK AGGMRIVQKH PHTGDTKEEK DKDDQEWESP
60 70 80 90 100
SPPKPTVFIS GVIARGDKDF PPAAAQVAHQ KPHASMDKHP SPRTQHIQQP

RK
Length:102
Mass (Da):11,165
Last modified:January 23, 2007 - v3
Checksum:i52FBEFD23ABD182F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76105 mRNA. Translation: CAA53713.1.
CR542184 mRNA. Translation: CAG46981.1.
AY266680 Genomic DNA. Translation: AAO89078.1.
BC002726 mRNA. Translation: AAH02726.2.
CCDSiCCDS3880.1.
PIRiI37274.
RefSeqiNP_001278892.1. NM_001291963.1.
NP_004385.1. NM_004394.2.
UniGeneiHs.75189.

Genome annotation databases

EnsembliENST00000230895; ENSP00000230895; ENSG00000112977.
GeneIDi1611.
KEGGihsa:1611.
UCSCiuc003jez.4. human.

Polymorphism databases

DMDMi1706298.

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76105 mRNA. Translation: CAA53713.1.
CR542184 mRNA. Translation: CAG46981.1.
AY266680 Genomic DNA. Translation: AAO89078.1.
BC002726 mRNA. Translation: AAH02726.2.
CCDSiCCDS3880.1.
PIRiI37274.
RefSeqiNP_001278892.1. NM_001291963.1.
NP_004385.1. NM_004394.2.
UniGeneiHs.75189.

3D structure databases

ProteinModelPortaliP51397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107981. 5 interactions.
IntActiP51397. 1 interaction.
STRINGi9606.ENSP00000230895.

PTM databases

PhosphoSiteiP51397.

Polymorphism databases

DMDMi1706298.

Proteomic databases

MaxQBiP51397.
PaxDbiP51397.
PeptideAtlasiP51397.
PRIDEiP51397.

Protocols and materials databases

DNASUi1611.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000230895; ENSP00000230895; ENSG00000112977.
GeneIDi1611.
KEGGihsa:1611.
UCSCiuc003jez.4. human.

Organism-specific databases

CTDi1611.
GeneCardsiGC05M010679.
HGNCiHGNC:2672. DAP.
MIMi600954. gene.
neXtProtiNX_P51397.
PharmGKBiPA27140.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG84666.
GeneTreeiENSGT00510000049345.
HOGENOMiHOG000039719.
HOVERGENiHBG005451.
InParanoidiP51397.
OMAiVEKLPHP.
OrthoDBiEOG757D0J.
PhylomeDBiP51397.
TreeFamiTF329716.

Miscellaneous databases

ChiTaRSiDAP. human.
GeneWikiiDAP_(gene).
GenomeRNAii1611.
NextBioi6622.
PROiP51397.
SOURCEiSearch...

Gene expression databases

BgeeiP51397.
CleanExiHS_DAP.
ExpressionAtlasiP51397. baseline and differential.
GenevestigatoriP51397.

Family and domain databases

InterProiIPR024130. DAP1/DAPL1.
[Graphical view]
PANTHERiPTHR13177. PTHR13177. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel serine/threonine kinase and a novel 15-kD protein as potential mediators of the gamma interferon-induced cell death."
    Deiss L.P., Feinstein E., Berissi H., Cohen O., Kimchi A.
    Genes Dev. 9:15-30(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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 (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. NIEHS SNPs program
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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: Uterus.
  5. "Beyond linker histones and high mobility group proteins: global profiling of perchloric acid soluble proteins."
    Zougman A., Wisniewski J.R.
    J. Proteome Res. 5:925-934(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-8 AND 41-65, ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-3; SER-49 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-51 AND SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "DAP1, a novel substrate of mTOR, negatively regulates autophagy."
    Koren I., Reem E., Kimchi A.
    Curr. Biol. 20:1093-1098(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AUTOPHAGY, PHOSPHORYLATION AT SER-3 AND SER-51 BY MTOR.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-51 AND SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDAP1_HUMAN
AccessioniPrimary (citable) accession number: P51397
Secondary accession number(s): Q6FGC3, Q9BUC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 99 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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.