P51397 (DAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Death-associated protein 1
Short name=DAP-1

Gene names

Name:	DAP
Synonyms:	DAP1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	102 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Negative regulator of autophagy. Involved in mediating interferon-gamma-induced cell death. Ref.10
Post-translational modification	Phosphorylated. Phosphorylation by MTOR inhibits the suppressive activity of DAP1 toward autophagy. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Ontologies

Keywords
Biological process	Apoptosis Autophagy
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from mutant phenotype. Source: UniProtKB cellular response to amino acid starvation Inferred from direct assay Ref.10. Source: UniProtKB induction of apoptosis by extracellular signals Inferred from mutant phenotype Ref.1. Source: UniProtKB negative regulation of NF-kappaB transcription factor activity Inferred from mutant phenotype. Source: UniProtKB negative regulation of autophagy Inferred from mutant phenotype Ref.10. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from mutant phenotype. Source: UniProtKB
Molecular function	death domain binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 102	101	Death-associated protein 1		PRO_0000079782
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.5
	Modified residue	3	1	Phosphoserine; by MTOR Ref.5 Ref.9 Ref.10
	Modified residue	49	1	Phosphoserine Ref.5 Ref.8
	Modified residue	51	1	Phosphoserine; by MTOR Ref.5 Ref.6 Ref.8 Ref.10
	Modified residue	91	1	Phosphoserine Ref.7 Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P51397 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 52FBEFD23ABD182F	FASTA	102	11,165
	10 20 30 40 50 60 MSSPPEGKLE TKAGHPPAVK AGGMRIVQKH PHTGDTKEEK DKDDQEWESP SPPKPTVFIS 70 80 90 100 GVIARGDKDF PPAAAQVAHQ KPHASMDKHP SPRTQHIQQP RK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7828849] [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: 15489334] [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: 16602700] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8 AND 41-65, ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-3; SER-49 AND SER-51, 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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-51 AND SER-91, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"DAP1, a novel substrate of mTOR, negatively regulates autophagy." Koren I., Reem E., Kimchi A. Curr. Biol. 20:1093-1098(2010) [PubMed: 20537536] [Abstract] Cited for: FUNCTION IN AUTOPHAGY, PHOSPHORYLATION AT SER-3 AND SER-51 BY MTOR.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	X76105 mRNA. Translation: CAA53713.1. CR542184 mRNA. Translation: CAG46981.1. AY266680 Genomic DNA. Translation: AAO89078.1. BC002726 mRNA. Translation: AAH02726.2.
IPI	IPI00018117.
PIR	I37274.
RefSeq	NP_004385.1. NM_004394.2.
UniGene	Hs.75189.
3D structure databases
ProteinModelPortal	P51397.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51397. 1 interaction.
STRING	P51397.
PTM databases
PhosphoSite	P51397.
Polymorphism databases
DMDM	1706298.
Proteomic databases
PeptideAtlas	P51397.
PRIDE	P51397.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000230895; ENSP00000230895; ENSG00000112977.
GeneID	1611.
KEGG	hsa:1611.
UCSC	uc003jez.2. human.
Organism-specific databases
CTD	1611.
GeneCards	GC05M010679.
HGNC	HGNC:2672. DAP.
MIM	600954. gene.
neXtProt	NX_P51397.
PharmGKB	PA27140.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG19302.
GeneTree	ENSGT00390000008309.
HOVERGEN	HBG005451.
OMA	KDAEDCT.
OrthoDB	EOG41JZDS.
Gene expression databases
ArrayExpress	P51397.
Bgee	P51397.
CleanEx	HS_DAP.
Genevestigator	P51397.
GermOnline	ENSG00000112977. Homo sapiens.
Family and domain databases
InterPro	IPR024130. DAP1/DAPL1. [Graphical view]
PANTHER	PTHR13177. PTHR13177. 1 hit.
ProtoNet	Search...
Other
NextBio	6622.
SOURCE	Search...

Entry information

Entry name

DAP1_HUMAN

Accession

Primary (citable) accession number: P51397
Secondary accession number(s): Q6FGC3, Q9BUC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.