ID PEA15_HUMAN Reviewed; 130 AA. AC Q15121; B1AKZ3; O00511; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 03-JUL-2003, sequence version 2. DT 02-SEP-2026, entry version 199. DE RecName: Full=Astrocytic phosphoprotein PEA-15; DE AltName: Full=15 kDa phosphoprotein enriched in astrocytes; DE AltName: Full=Phosphoprotein enriched in diabetes; DE Short=PED; GN Name=PEA15; 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] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=8662970; DOI=10.1074/jbc.271.25.14800; RA Estelles A., Yokoyama M., Nothias F., Vincent J.-D., Glowinski J., RA Vernier P., Chneiweiss H.; RT "The major astrocytic phosphoprotein PEA-15 is encoded by two mRNAs RT conserved on their full length in mouse and human."; RL J. Biol. Chem. 271:14800-14806(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Heart; RX PubMed=9670003; DOI=10.1093/emboj/17.14.3858; RA Condorelli G., Vigliotta G., Iavarone C., Caruso M., Tocchetti C.G., RA Andreozzi F., Cafieri A., Tecce M.F., Formisano P., Beguinot L., RA Beguinot F.; RT "PED/PEA-15 gene controls glucose transport and is overexpressed in type 2 RT diabetes mellitus."; RL EMBO J. 17:3858-3866(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10607908; DOI=10.1016/s0378-1119(99)00455-2; RA Wolford J.K., Bogardus C., Ossowski V., Prochazka M.; RT "Molecular characterization of the human PEA15 gene on 1q21-q22 and RT association with type 2 diabetes mellitus in Pima Indians."; RL Gene 241:143-148(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Skin; 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 [9] RP PROTEIN SEQUENCE OF 55-83 AND 89-98, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [10] RP FUNCTION, AND INTERACTION WITH CASP8 AND FADD. RX PubMed=10442631; DOI=10.1038/sj.onc.1202831; RA Condorelli G., Vigliotta G., Cafieri A., Trencia A., Andalo P., Oriente F., RA Miele C., Caruso M., Formisano P., Beguinot F.; RT "PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced RT apoptosis."; RL Oncogene 18:4409-4415(1999). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-116, AND 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 [12] 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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-116, 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 [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-116, AND RP IDENTIFICATION BY 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-116, AND 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Blocks Ras-mediated inhibition of integrin activation and CC modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by CC retaining it in the cytoplasm (By similarity). Inhibits both CC TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates CC glucose transport by controlling both the content of SLC2A1 glucose CC transporters on the plasma membrane and the insulin-dependent CC trafficking of SLC2A4 from the cell interior to the surface. CC {ECO:0000250, ECO:0000269|PubMed:10442631, ECO:0000269|PubMed:9670003}. CC -!- SUBUNIT: Binds RPS6KA3, MAPK3 and MAPK1. Transient interaction with CC PLD1 and PLD2 (By similarity). Interacts with CASP8 and FADD. CC {ECO:0000250, ECO:0000269|PubMed:10442631}. CC -!- INTERACTION: CC Q15121; P28482: MAPK1; NbExp=12; IntAct=EBI-714410, EBI-959949; CC Q15121; P27361: MAPK3; NbExp=5; IntAct=EBI-714410, EBI-73995; CC Q15121; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-714410, EBI-750109; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Associated with microtubules. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q15121-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15121-2; Sequence=VSP_056174; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Most abundant in tissues CC such as heart, brain, muscle and adipose tissue which utilize glucose CC as an energy source. Lower expression in glucose-producing tissues. CC Higher levels of expression are found in tissues from individuals with CC type 2 diabetes than in controls. {ECO:0000269|PubMed:9670003}. CC -!- PTM: Phosphorylated by protein kinase C and calcium-calmodulin- CC dependent protein kinase. These phosphorylation events are modulated by CC neurotransmitters or hormones. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/46286/PEA15"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X86809; CAA60499.1; -; mRNA. DR EMBL; Y13736; CAA74076.1; -; mRNA. DR EMBL; AF153274; AAD56775.1; -; Genomic_DNA. DR EMBL; AF153273; AAD56775.1; JOINED; Genomic_DNA. DR EMBL; AK095879; BAG53155.1; -; mRNA. DR EMBL; AL121987; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL139011; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW52735.1; -; Genomic_DNA. DR EMBL; BC002426; AAH02426.1; -; mRNA. DR EMBL; BC022554; AAH22554.1; -; mRNA. DR EMBL; BT007252; AAP35916.1; -; mRNA. DR CCDS; CCDS1199.1; -. [Q15121-1] DR CCDS; CCDS72954.1; -. [Q15121-2] DR PIR; S55384; S55384. DR RefSeq; NP_001284505.1; NM_001297576.2. [Q15121-2] DR RefSeq; NP_001284506.1; NM_001297577.2. [Q15121-1] DR RefSeq; NP_001284507.1; NM_001297578.2. DR RefSeq; NP_003759.1; NM_003768.5. [Q15121-1] DR RefSeq; XP_047289347.1; XM_047433391.1. [Q15121-2] DR RefSeq; XP_054195371.1; XM_054339396.1. [Q15121-2] DR PDB; 4IZ5; X-ray; 3.19 A; E/F/G/H=1-130. DR PDB; 4IZA; X-ray; 1.93 A; B=1-96. DR PDB; 6P6B; NMR; -; A=1-90. DR PDB; 6P6C; NMR; -; A=1-130. DR AlphaFoldDB; Q15121; -. DR BMRB; Q15121; -. DR SMR; Q15121; -. DR BioGRID; 114230; 88. DR FunCoup; Q15121; 1453. DR IntAct; Q15121; 51. DR MINT; Q15121; -. DR NDEx; IQUERY-CP-PEA15; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000357055; -. DR GlyGen; Q15121; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q15121; -. DR MetOSite; Q15121; -. DR PhosphoSitePlus; Q15121; -. DR BioMuta; PEA15; -. DR DMDM; 32470612; -. DR jPOST; Q15121; -. DR MassIVE; Q15121; -. DR PaxDb; 9606-ENSP00000357055; -. DR PeptideAtlas; Q15121; -. DR ProteomicsDB; 60449; -. [Q15121-1] DR Pumba; Q15121; -. DR TopDownProteomics; Q15121-1; -. [Q15121-1] DR Antibodypedia; 20486; 496 antibodies from 37 providers. DR DNASU; 8682; -. DR Ensembl; ENST00000360472.9; ENSP00000353660.5; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000368076.1; ENSP00000357055.1; ENSG00000162734.14. [Q15121-2] DR Ensembl; ENST00000853680.1; ENSP00000523739.1; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000853683.1; ENSP00000523742.1; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000853684.1; ENSP00000523743.1; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000853685.1; ENSP00000523744.1; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000853686.1; ENSP00000523745.1; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000853687.1; ENSP00000523746.1; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000853688.1; ENSP00000523747.1; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000853689.1; ENSP00000523748.1; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000853690.1; ENSP00000523749.1; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000853692.1; ENSP00000523750.1; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000853693.1; ENSP00000523751.1; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000853694.1; ENSP00000523752.1; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000853696.1; ENSP00000523754.1; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000853698.1; ENSP00000523758.1; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000853701.1; ENSP00000523760.1; ENSG00000162734.14. [Q15121-1] DR Ensembl; ENST00000962148.1; ENSP00000632207.1; ENSG00000162734.14. [Q15121-1] DR GeneID; 8682; -. DR KEGG; hsa:8682; -. DR MANE-Select; ENST00000360472.9; ENSP00000353660.5; NM_003768.5; NP_003759.1. DR UCSC; uc001fvk.4; human. [Q15121-1] DR AGR; HGNC:8822; -. DR ClinPGx; PA33166; -. DR CTD; 8682; -. DR DisGeNET; 8682; -. DR GeneCards; PEA15; -. DR HGNC; HGNC:8822; PEA15. DR HPA; ENSG00000162734; Tissue enriched (brain). DR MIM; 603434; gene. DR OpenTargets; ENSG00000162734; -. DR VEuPathDB; HostDB:ENSG00000162734; -. DR eggNOG; KOG3573; Eukaryota. DR GeneTree; ENSGT00390000000230; -. DR InParanoid; Q15121; -. DR OMA; ATSKDWF; -. DR OrthoDB; 9931131at2759; -. DR PAN-GO; Q15121; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q15121; -. DR PathwayCommons; Q15121; -. DR Reactome; R-HSA-112409; RAF-independent MAPK1/3 activation. DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade. DR SignaLink; Q15121; -. DR SIGNOR; Q15121; -. DR Agora; ENSG00000162734; -. DR BioGRID-ORCS; 8682; 29 hits in 1161 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; PEA15; human. DR EvolutionaryTrace; Q15121; -. DR GeneWiki; PEA15; -. DR GenomeRNAi; 8682; -. DR Pharos; Q15121; Tbio. DR PRO; PR:Q15121; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q15121; protein. DR Bgee; ENSG00000162734; Expressed in dorsal motor nucleus of vagus nerve and 211 other cell types or tissues. DR ExpressionAtlas; Q15121; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005875; C:microtubule associated complex; NAS:UniProtKB. DR GO; GO:0000165; P:MAPK cascade; IEA:InterPro. DR GO; GO:0046325; P:negative regulation of D-glucose import across plasma membrane; IDA:UniProtKB. DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:UniProtKB. DR CDD; cd08338; DED_PEA15; 1. DR FunFam; 1.10.533.10:FF:000026; astrocytic phosphoprotein PEA-15 isoform X1; 1. DR Gene3D; 1.10.533.10; Death Domain, Fas; 1. DR InterPro; IPR011029; DEATH-like_dom_sf. DR InterPro; IPR001875; DED_dom. DR InterPro; IPR029546; PEA15_DED. DR PANTHER; PTHR48169:SF1; ASTROCYTIC PHOSPHOPROTEIN PEA-15; 1. DR PANTHER; PTHR48169; DED DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF01335; DED; 1. DR SMART; SM00031; DED; 1. DR SUPFAM; SSF47986; DEATH domain; 1. DR PROSITE; PS50168; DED; 1. DR PDBsum; 4IZ5; -. DR PDBsum; 4IZA; -. DR PDBsum; 6P6B; -. DR PDBsum; 6P6C; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm; KW Direct protein sequencing; Phosphoprotein; Proteomics identification; KW Reference proteome; Sugar transport; Transport. FT CHAIN 1..130 FT /note="Astrocytic phosphoprotein PEA-15" FT /id="PRO_0000191282" FT DOMAIN 3..81 FT /note="DED" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00065" FT REGION 98..107 FT /note="Microtubule-binding" FT /evidence="ECO:0000255" FT REGION 122..129 FT /note="Microtubule-binding" FT /evidence="ECO:0000255" FT MOD_RES 61 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 90 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62048" FT MOD_RES 104 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 116 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 1 FT /note="M -> MEDEGNKLCQAPPWPGQTSPVM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056174" FT CONFLICT 2 FT /note="A -> V (in Ref. 1; CAA60499)" FT /evidence="ECO:0000305" FT CONFLICT 8 FT /note="L -> F (in Ref. 1; CAA60499)" FT /evidence="ECO:0000305" FT CONFLICT 62 FT /note="Y -> I (in Ref. 1; CAA60499)" FT /evidence="ECO:0000305" FT CONFLICT 124 FT /note="A -> G (in Ref. 1; CAA60499)" FT /evidence="ECO:0000305" FT HELIX 1..13 FT /evidence="ECO:0007829|PDB:4IZA" FT HELIX 17..27 FT /evidence="ECO:0007829|PDB:4IZA" FT TURN 28..30 FT /evidence="ECO:0007829|PDB:4IZA" FT HELIX 32..34 FT /evidence="ECO:0007829|PDB:4IZA" FT HELIX 42..51 FT /evidence="ECO:0007829|PDB:4IZA" FT HELIX 61..69 FT /evidence="ECO:0007829|PDB:4IZA" FT HELIX 73..90 FT /evidence="ECO:0007829|PDB:4IZA" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:4IZ5" SQ SEQUENCE 130 AA; 15040 MW; 8D0F93A40B299FB2 CRC64; MAEYGTLLQD LTNNITLEDL EQLKSACKED IPSEKSEEIT TGSAWFSFLE SHNKLDKDNL SYIEHIFEIS RRPDLLTMVV DYRTRVLKIS EEDELDTKLT RIPSAKKYKD IIRQPSEEEI IKLAPPPKKA //