PEA15_HUMAN
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 03-AUG-2022, entry version 180.
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=4; IntAct=EBI-714410, EBI-959949;
CC Q15121; P27361: MAPK3; NbExp=4; 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="http://atlasgeneticsoncology.org/Genes/PEA15ID46286ch1q21.html";
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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_001297576.1. [Q15121-2]
DR RefSeq; NP_001284506.1; NM_001297577.1. [Q15121-1]
DR RefSeq; NP_001284507.1; NM_001297578.1.
DR RefSeq; NP_003759.1; NM_003768.4. [Q15121-1]
DR RefSeq; XP_006711662.1; XM_006711599.2. [Q15121-1]
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 PDBsum; 4IZ5; -.
DR PDBsum; 4IZA; -.
DR PDBsum; 6P6B; -.
DR PDBsum; 6P6C; -.
DR AlphaFoldDB; Q15121; -.
DR BMRB; Q15121; -.
DR SMR; Q15121; -.
DR BioGRID; 114230; 81.
DR IntAct; Q15121; 15.
DR MINT; Q15121; -.
DR STRING; 9606.ENSP00000357055; -.
DR iPTMnet; Q15121; -.
DR MetOSite; Q15121; -.
DR PhosphoSitePlus; Q15121; -.
DR BioMuta; PEA15; -.
DR DMDM; 32470612; -.
DR EPD; Q15121; -.
DR jPOST; Q15121; -.
DR MassIVE; Q15121; -.
DR MaxQB; Q15121; -.
DR PaxDb; Q15121; -.
DR PeptideAtlas; Q15121; -.
DR PRIDE; Q15121; -.
DR ProteomicsDB; 60449; -. [Q15121-1]
DR TopDownProteomics; Q15121-1; -. [Q15121-1]
DR Antibodypedia; 20486; 508 antibodies from 35 providers.
DR DNASU; 8682; -.
DR Ensembl; ENST00000360472.9; ENSP00000353660.5; ENSG00000162734.13. [Q15121-1]
DR Ensembl; ENST00000368076.1; ENSP00000357055.1; ENSG00000162734.13. [Q15121-2]
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 CTD; 8682; -.
DR DisGeNET; 8682; -.
DR GeneCards; PEA15; -.
DR HGNC; HGNC:8822; PEA15.
DR HPA; ENSG00000162734; Tissue enhanced (brain, choroid plexus).
DR MIM; 603434; gene.
DR neXtProt; NX_Q15121; -.
DR OpenTargets; ENSG00000162734; -.
DR PharmGKB; PA33166; -.
DR VEuPathDB; HostDB:ENSG00000162734; -.
DR eggNOG; KOG3573; Eukaryota.
DR GeneTree; ENSGT00390000000230; -.
DR InParanoid; Q15121; -.
DR OMA; VEYRTTV; -.
DR PhylomeDB; Q15121; -.
DR TreeFam; TF332405; -.
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 BioGRID-ORCS; 8682; 28 hits in 1080 CRISPR screens.
DR ChiTaRS; PEA15; human.
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 209 other tissues.
DR ExpressionAtlas; Q15121; baseline and differential.
DR Genevisible; Q15121; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005875; C:microtubule associated complex; NAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IEA:InterPro.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:UniProtKB.
DR GO; GO:0046325; P:negative regulation of glucose import; IDA:UniProtKB.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0043278; P:response to morphine; IEA:Ensembl.
DR CDD; cd08338; DED_PEA15; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR001875; DED_dom.
DR InterPro; IPR029546; PEA15_DED.
DR Pfam; PF01335; DED; 1.
DR SMART; SM00031; DED; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50168; DED; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW 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"
SQ SEQUENCE 130 AA; 15040 MW; 8D0F93A40B299FB2 CRC64;
MAEYGTLLQD LTNNITLEDL EQLKSACKED IPSEKSEEIT TGSAWFSFLE SHNKLDKDNL
SYIEHIFEIS RRPDLLTMVV DYRTRVLKIS EEDELDTKLT RIPSAKKYKD IIRQPSEEEI
IKLAPPPKKA
