DAP1_HUMAN
ID DAP1_HUMAN Reviewed; 102 AA.
AC P51397; Q6FGC3; Q9BUC9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Death-associated protein 1;
DE Short=DAP-1;
GN Name=DAP; Synonyms=DAP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7828849; DOI=10.1101/gad.9.1.15;
RA Deiss L.P., Feinstein E., Berissi H., Cohen O., Kimchi A.;
RT "Identification of a novel serine/threonine kinase and a novel 15-kD
RT protein as potential mediators of the gamma interferon-induced cell
RT death.";
RL Genes Dev. 9:15-30(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-8 AND 41-65, ACETYLATION AT SER-2, PHOSPHORYLATION AT
RP SER-3; SER-49 AND SER-51, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16602700; DOI=10.1021/pr050415p;
RA Zougman A., Wisniewski J.R.;
RT "Beyond linker histones and high mobility group proteins: global profiling
RT of perchloric acid soluble proteins.";
RL J. Proteome Res. 5:925-934(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-51 AND SER-91, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP FUNCTION IN AUTOPHAGY, AND PHOSPHORYLATION AT SER-3 AND SER-51 BY MTOR.
RX PubMed=20537536; DOI=10.1016/j.cub.2010.04.041;
RA Koren I., Reem E., Kimchi A.;
RT "DAP1, a novel substrate of mTOR, negatively regulates autophagy.";
RL Curr. Biol. 20:1093-1098(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-51 AND SER-91, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Negative regulator of autophagy. Involved in mediating
CC interferon-gamma-induced cell death. {ECO:0000269|PubMed:20537536}.
CC -!- PTM: Phosphorylated. Phosphorylation by MTOR inhibits the suppressive
CC activity of DAP toward autophagy. {ECO:0000269|PubMed:16602700,
CC ECO:0000269|PubMed:20537536}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/dap/";
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DR EMBL; X76105; CAA53713.1; -; mRNA.
DR EMBL; CR542184; CAG46981.1; -; mRNA.
DR EMBL; AY266680; AAO89078.1; -; Genomic_DNA.
DR EMBL; BC002726; AAH02726.2; -; mRNA.
DR CCDS; CCDS3880.1; -.
DR PIR; I37274; I37274.
DR RefSeq; NP_001278892.1; NM_001291963.1.
DR RefSeq; NP_004385.1; NM_004394.2.
DR AlphaFoldDB; P51397; -.
DR BioGRID; 107981; 5.
DR IntAct; P51397; 2.
DR STRING; 9606.ENSP00000230895; -.
DR iPTMnet; P51397; -.
DR PhosphoSitePlus; P51397; -.
DR BioMuta; DAP; -.
DR DMDM; 1706298; -.
DR EPD; P51397; -.
DR jPOST; P51397; -.
DR MassIVE; P51397; -.
DR MaxQB; P51397; -.
DR PaxDb; P51397; -.
DR PeptideAtlas; P51397; -.
DR PRIDE; P51397; -.
DR ProteomicsDB; 56302; -.
DR TopDownProteomics; P51397; -.
DR Antibodypedia; 9394; 268 antibodies from 35 providers.
DR DNASU; 1611; -.
DR Ensembl; ENST00000230895.11; ENSP00000230895.7; ENSG00000112977.16.
DR GeneID; 1611; -.
DR KEGG; hsa:1611; -.
DR MANE-Select; ENST00000230895.11; ENSP00000230895.7; NM_004394.3; NP_004385.1.
DR UCSC; uc003jez.5; human.
DR CTD; 1611; -.
DR DisGeNET; 1611; -.
DR GeneCards; DAP; -.
DR HGNC; HGNC:2672; DAP.
DR HPA; ENSG00000112977; Low tissue specificity.
DR MIM; 600954; gene.
DR neXtProt; NX_P51397; -.
DR OpenTargets; ENSG00000112977; -.
DR PharmGKB; PA27140; -.
DR VEuPathDB; HostDB:ENSG00000112977; -.
DR eggNOG; ENOG502S4ST; Eukaryota.
DR GeneTree; ENSGT00940000154574; -.
DR HOGENOM; CLU_150759_2_0_1; -.
DR InParanoid; P51397; -.
DR OMA; PTHDARP; -.
DR OrthoDB; 1450599at2759; -.
DR PhylomeDB; P51397; -.
DR TreeFam; TF329716; -.
DR PathwayCommons; P51397; -.
DR SignaLink; P51397; -.
DR SIGNOR; P51397; -.
DR BioGRID-ORCS; 1611; 83 hits in 1078 CRISPR screens.
DR ChiTaRS; DAP; human.
DR GeneWiki; DAP_(gene); -.
DR GenomeRNAi; 1611; -.
DR Pharos; P51397; Tbio.
DR PRO; PR:P51397; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P51397; protein.
DR Bgee; ENSG00000112977; Expressed in body of pancreas and 172 other tissues.
DR ExpressionAtlas; P51397; baseline and differential.
DR Genevisible; P51397; HS.
DR GO; GO:0070513; F:death domain binding; IPI:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IGI:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IDA:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR InterPro; IPR024130; DAP1/DAPL1.
DR PANTHER; PTHR13177; PTHR13177; 1.
DR Pfam; PF15228; DAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Autophagy; Direct protein sequencing;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16602700"
FT CHAIN 2..102
FT /note="Death-associated protein 1"
FT /id="PRO_0000079782"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:16602700"
FT MOD_RES 3
FT /note="Phosphoserine; by MTOR"
FT /evidence="ECO:0000269|PubMed:16602700,
FT ECO:0000269|PubMed:20537536"
FT MOD_RES 29
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91XC8"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16602700,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT MOD_RES 51
FT /note="Phosphoserine; by MTOR"
FT /evidence="ECO:0000269|PubMed:16602700,
FT ECO:0000269|PubMed:20537536, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
SQ SEQUENCE 102 AA; 11165 MW; 52FBEFD23ABD182F CRC64;
MSSPPEGKLE TKAGHPPAVK AGGMRIVQKH PHTGDTKEEK DKDDQEWESP SPPKPTVFIS
GVIARGDKDF PPAAAQVAHQ KPHASMDKHP SPRTQHIQQP RK
