RBCC Red Blood Cell Collection

PEA15 [Confidence: low (only semi-automatic identification from reviews)]
Astrocytic phosphoprotein PEA-15 (15 kDa phosphoprotein enriched in astrocytes; Phosphoprotein enriched in diabetes; PED)
Note: presumably soluble (membrane word is not in UniProt keywords or features)

UniProt Q15121
ID PEA15_HUMAN Reviewed; 130 AA.
AC Q15121; O00511;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-JUL-2003, sequence version 2.
DT 22-JAN-2014, entry version 119.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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], 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
RT type 2 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 MRNA].
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
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 55-83 AND 89-98, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
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.,
RA Oriente F., Miele C., Caruso M., Formisano P., Beguinot F.;
RT "PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-
RT induced apoptosis.";
RL Oncogene 18:4409-4415(1999).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-116, AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
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 [10]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-116, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-116, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Blocks Ras-mediated inhibition of integrin activation
CC and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3
CC activities by retaining it in the cytoplasm (By similarity).
CC Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and
CC apoptosis. Regulates glucose transport by controlling both the
CC content of SLC2A1 glucose transporters on the plasma membrane and
CC the insulin-dependent trafficking of SLC2A4 from the cell interior
CC to the surface.
CC -!- SUBUNIT: Binds RPS6KA3, MAPK3 and MAPK1. Transient interaction
CC with PLD1 and PLD2 (By similarity). Interacts with CASP8 and FADD.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Associated with
CC microtubules.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Most abundant in
CC tissues such as heart, brain, muscle and adipose tissue which
CC utilize glucose as an energy source. Lower expression in glucose-
CC producing tissues. Higher levels of expression are found in
CC tissues from individuals with type 2 diabetes than in controls.
CC -!- PTM: Phosphorylated by protein kinase C and calcium-calmodulin-
CC dependent protein kinase. These phosphorylation events are
CC modulated by neurotransmitters or hormones.
CC -!- SIMILARITY: Contains 1 DED (death effector) domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PEA15ID46286ch1q21.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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; BC002426; AAH02426.1; -; mRNA.
DR EMBL; BC022554; AAH22554.1; -; mRNA.
DR EMBL; BT007252; AAP35916.1; -; mRNA.
DR PIR; S55384; S55384.
DR RefSeq; NP_003759.1; NM_003768.3.
DR RefSeq; XP_005245620.1; XM_005245563.1.
DR RefSeq; XP_005245621.1; XM_005245564.1.
DR UniGene; Hs.517216; -.
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 PDBsum; 4IZ5; -.
DR PDBsum; 4IZA; -.
DR ProteinModelPortal; Q15121; -.
DR SMR; Q15121; 1-130.
DR IntAct; Q15121; 9.
DR MINT; MINT-141556; -.
DR STRING; 9606.ENSP00000353660; -.
DR PhosphoSite; Q15121; -.
DR DMDM; 32470612; -.
DR PaxDb; Q15121; -.
DR PRIDE; Q15121; -.
DR DNASU; 8682; -.
DR Ensembl; ENST00000360472; ENSP00000353660; ENSG00000162734.
DR GeneID; 8682; -.
DR KEGG; hsa:8682; -.
DR UCSC; uc001fvk.3; human.
DR CTD; 8682; -.
DR GeneCards; GC01P160175; -.
DR HGNC; HGNC:8822; PEA15.
DR HPA; HPA028356; -.
DR MIM; 603434; gene.
DR neXtProt; NX_Q15121; -.
DR PharmGKB; PA33166; -.
DR eggNOG; NOG314638; -.
DR HOGENOM; HOG000049048; -.
DR HOVERGEN; HBG053557; -.
DR InParanoid; Q15121; -.
DR OrthoDB; EOG7D2FGM; -.
DR PhylomeDB; Q15121; -.
DR SignaLink; Q15121; -.
DR ChiTaRS; PEA15; human.
DR GeneWiki; PEA15; -.
DR GenomeRNAi; 8682; -.
DR NextBio; 32565; -.
DR PMAP-CutDB; Q15121; -.
DR PRO; PR:Q15121; -.
DR ArrayExpress; Q15121; -.
DR Bgee; Q15121; -.
DR CleanEx; HS_PEA15; -.
DR Genevestigator; Q15121; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005875; C:microtubule associated complex; NAS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
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:0043278; P:response to morphine; IEA:Ensembl.
DR GO; GO:0006810; P:transport; TAS:ProtInc.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom.
DR InterPro; IPR001875; 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; Apoptosis; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Sugar transport; Transport.
FT CHAIN 1 130 Astrocytic phosphoprotein PEA-15.
FT /FTId=PRO_0000191282.
FT DOMAIN 3 81 DED.
FT REGION 98 107 Microtubule-binding (Potential).
FT REGION 122 129 Microtubule-binding (Potential).
FT MOD_RES 61 61 Phosphoserine.
FT MOD_RES 104 104 Phosphoserine.
FT MOD_RES 116 116 Phosphoserine.
FT CONFLICT 2 2 A -> V (in Ref. 1; CAA60499).
FT CONFLICT 8 8 L -> F (in Ref. 1; CAA60499).
FT CONFLICT 62 62 Y -> I (in Ref. 1; CAA60499).
FT CONFLICT 124 124 A -> G (in Ref. 1; CAA60499).
FT HELIX 1 13
FT HELIX 17 27
FT TURN 28 30
FT HELIX 32 34
FT HELIX 42 51
FT HELIX 61 69
FT HELIX 73 90
SQ SEQUENCE 130 AA; 15040 MW; 8D0F93A40B299FB2 CRC64;
MAEYGTLLQD LTNNITLEDL EQLKSACKED IPSEKSEEIT TGSAWFSFLE SHNKLDKDNL
SYIEHIFEIS RRPDLLTMVV DYRTRVLKIS EEDELDTKLT RIPSAKKYKD IIRQPSEEEI
IKLAPPPKKA
//

MIM 603434
*RECORD*
*FIELD* NO
603434
*FIELD* TI
*603434 PHOSPHOPROTEIN ENRICHED IN ASTROCYTES, 15-KD; PEA15
;;PHOSPHOPROTEIN ENRICHED IN DIABETES; PED;;
read moreMAMMARY TRANSFORMING GENE 1, MOUSE, HOMOLOG OF; HMAT1;;
MAT1, MOUSE, HOMOLOG OF
*FIELD* TX

DESCRIPTION

PEA15 is a ubiquitously expressed 15-kD protein with broad antiapoptotic
function. By virtue of its death effector domain (DED), PEA15 binds
other DED-containing proteins, preventing formation of the
death-inducing signaling complex and inhibiting activation of the
caspase cascade (see CASP3; 600636) (summary by Trencia et al., 2004).

CLONING

Astrocytes are involved in a variety of functions, including storage of
glycogen and support for the migration and differentiation of neurons.
They express membrane receptors which allow them to respond to
extracellular signals. Activation of the receptors induces a cascade of
events, such as the stimulation of protein kinases and the subsequent
phosphorylation of target proteins. Araujo et al. (1993) identified a
unique 15-kD protein in astrocytes that exists as a nonphosphorylated
form and as 2 increasingly phosphorylated varieties. This protein, which
they called PEA15, contains a consensus site for protein kinase C (PKC;
e.g., 176960) and is an endogenous substrate for PKC.

Bera et al. (1994) isolated the mouse Mat1 gene and found that it can
transform NIH 3T3 cells and the mammary epithelial cell line TM3. Hwang
et al. (1997) noted that the HMAT1 gene (GenBank GENBANK L37385), the
human homolog of mouse Mat1, had been cloned. They stated that a 2.5-kb
HMAT1 transcript had been detected in normal mammary epithelial cells
and tumor cell lines; its expression levels were higher in breast cancer
cell lines than in normal mammary epithelial cells.

Estelles et al. (1996) cloned 2 forms of mouse Pea15 cDNA that differ in
the length of the 3-prime UTR; these likely represent transcripts
generated by alternative polyadenylation. The authors found that the
3-prime UTR of the longer Pea15 cDNA contains the Mat1 protooncogene
sequence. They proposed that the Mat1 cDNA is a partial sequence of the
Pea15 gene and does not encode a protein. Northern blot analysis of rat
tissues revealed 2 Pea15 transcripts which were expressed abundantly in
the central nervous system and at lower levels in peripheral tissues.
Estelles et al. (1996) also identified 2 forms of human PEA15 cDNA
(GenBank GENBANK X86809), which are the counterparts of the mouse Pea15
cDNAs. Northern blot analysis of human brain extracts detected both
PEA15 transcripts. Several regions between the human and mouse 3-prime
UTRs share more than 90% identity. The deduced 130-amino acid human and
mouse PEA15 proteins are 96% identical. Danziger et al. (1995) showed
that the Pea15 protein colocalizes with microtubules.

GENE FUNCTION

Using differential display to identify genes whose expressions are
altered in tissues derived from type II diabetes mellitus (125853)
patients compared with nondiabetic individuals, Condorelli et al. (1998)
cloned cDNAs encoding PEA15, which they named PED for 'phosphoprotein
enriched in diabetes.' The ubiquitously expressed 2.8-kb PED mRNA was
overexpressed in fibroblasts, skeletal muscle, and adipose tissue from
type II diabetics. Levels of the 15-kD PED phosphoprotein were also
elevated in type II diabetic tissues. The authors demonstrated that
transfection of a PED cDNA into differentiating L6 skeletal muscle cells
increases the content of glucose transporter-1 (GLUT1; 138140) on the
plasma membrane and inhibits insulin-stimulated glucose transport and
cell surface recruitment of glucose transporter-4 (GLUT4; 138190). These
effects were reversed by blocking PKC activity.

Wolford et al. (2000) demonstrated the PEA15 gene is not associated with
type II diabetes mellitus in Pima Indians.

Using expression cloning, Ramos et al. (1998) identified PEA15 in a
screen designed to isolate cDNAs that prevent Ras suppression of
integrin activation. The authors concluded that PEA15 inhibits
suppression downstream of MAP kinase via a pathway blocked by a
dominant-negative form of R-Ras (165090). Cotransfection experiments
showed that PEA15 mutants lacking the DED were unable to reverse Ras
suppression of integrin activation.

Kitsberg et al. (1999) investigated whether PEA15 expression could be
involved in astrocytic protection against deleterious effects of TNF
(191160). Using in vitro assays, Kitsberg et al. (1999) determined that
PEA15 interacts with 2 other DED-containing proteins, FADD (602457) and
caspase-8 (CASP8; 601763), known to be apical adaptors of TNF apoptotic
signaling. Using homologous recombination, Kitsberg et al. (1999)
generated PEA15 null mice. Based on the analysis of primary astrocyte
cultures from the PEA15 knockout mice, they concluded that PEA15
expression protects astrocytes from TNF-induced apoptosis.

Formstecher et al. (2001) reported that PEA15 blocks ERK (see
601795)-dependent transcription and proliferation by binding ERKs and
preventing their localization in the nucleus. In transfected cells, the
expression of PEA15 blocked the ability of ERK MAP kinase to
phosphorylate and activate the transcription factor ELK1 (311040).
Formstecher et al. (2001) concluded that the effect of PEA15 on ERK
signaling was due to the binding of PEA15 to ERKs and the inhibition of
their accumulation in the nucleus. Formstecher et al. (2001) identified
a nuclear export sequence in PEA15 that is required to anchor ERK in the
cytoplasm. They concluded that PEA15 can redirect the biologic outcome
of MAP kinase signaling by regulating the subcellular localization of
ERK MAP kinase.

Trencia et al. (2004) determined that the antiapoptotic effect of PEA15
was reversed by OMI (HTRA2; 606441)-mediated PEA15 degradation. OMI is a
mitochondrial intermembrane serine protease that is released from
mitochondria by apoptotic stimuli. OMI did not coprecipitate with PEA15
from HeLa cells under normal conditions. However, exposure of cells to
ultraviolet C radiation resulted in cytosolic relocalization of OMI,
interaction of OMI with PEA15, and PEA15 degradation. Pharmacologic
inhibition of OMI serine protease activity or overexpression of PEA15
reduced cell sensitivity to ultraviolet C. Trencia et al. (2004)
concluded that the caspase-independent cell death induced by cytoplasmic
release of OMI is mediated by PEA15 degradation.

Vaidyanathan et al. (2007) showed that PEA15 enhanced activation of
ribosomal S6 kinase-2 (RSK2, or RPS6KA3; 300075) by increasing its
association with ERK in a concentration-dependent manner. PEA15
increased RSK2 activity and CREB-mediated transcription, and this
process was regulated by PEA15 phosphorylation. Phorbol ester
stimulation of Pea15-null mouse lymphocytes resulted in impaired Rsk2
activation, which was rescued by exogenous Pea15 expression.
Vaidyanathan et al. (2007) concluded that PEA15 functions as a scaffold
to enhance ERK activation of RSK2, and that this activity is regulated
by PEA15 phosphorylation.

GENE STRUCTURE

Wolford et al. (2000) determined that the PEA15 gene contains 4 exons
and spans approximately 10.2 kb of genomic DNA flanked upstream by a
potentially expressed Alu element and downstream by the H326 gene.

MAPPING

By radiation hybrid mapping using STSs generated from PEA15 ESTs,
Condorelli et al. (1998) localized the human PEA15 gene to chromosome
1q21-q22 between markers D1S2635 and D1S484. Hwang et al. (1997) mapped
the HMAT1 gene to 1q21.1 by fluorescence in situ hybridization.

*FIELD* RF
1. Araujo, H.; Danziger, N.; Cordier, J.; Glowinski, J.; Chneiweiss,
H.: Characterization of PEA-15, a major substrate for protein kinase
C in astrocytes. J. Biol. Chem. 268: 5911-5920, 1993.

2. Bera, T. K.; Guzman, R. C.; Miyamoto, S.; Panda, D. K.; Sasaki,
M.; Hanyu, K.; Enami, J.; Nandi, S.: Identification of a mammary
transforming gene (MAT1) associated with mouse mammary carcinogenesis. Proc.
Nat. Acad. Sci. 91: 9789-9793, 1994.

3. Condorelli, G.; Vigliotta, G.; Iavarone, C.; Caruso, M.; Tocchetti,
C. G.; Andreozzi, F.; Cafieri, A.; Tecce, M. F.; Formisano, P.; Beguinot,
L.; Beguinot, F.: PED/PEA-15 gene controls glucose transport and
is overexpressed in type 2 diabetes mellitus. EMBO J. 17: 3858-3866,
1998.

4. Danziger, N.; Yokoyama, M.; Jay, T.; Cordier, J.; Glowinski, J.;
Chneiweiss, H.: Cellular expression, developmental regulation, and
phylogenic conservation of PEA-15, the astrocytic major phosphoprotein
and protein kinase C substrate. J. Neurochem. 64: 1016-1025, 1995.

5. Estelles, A.; Yokoyama, M.; Nothias, F.; Vincent, J.-D.; Glowinski,
J.; Vernier, P.; Chneiweiss, H.: The major astrocytic phosphoprotein
PEA-15 is encoded by two mRNAs conserved on their full length in mouse
and human. J. Biol. Chem. 271: 14800-14806, 1996.

6. Formstecher, E.; Ramos, J. W.; Fauquet, M.; Calderwood, D. A.;
Hsieh, J.-C.; Canton, B.; Nguyen, X.-T.; Barnier, J.-V.; Camonis,
J.; Ginsberg, M. H.; Chneiweiss, H.: PEA-15 mediates cytoplasmic
sequestration of ERK MAP kinase. Dev. Cell 1: 239-250, 2001.

7. Hwang, S.; Kuo, W.-L.; Cochran, J. F.; Guzman, R. C.; Tsukamoto,
T.; Bandyopadhyay, G.; Myambo, K.; Collins, C. C.: Assignment of
HMAT1, the human homolog of the murine mammary transforming gene (MAT1)
associated with tumorigenesis, to 1q21.1, a region frequently gained
in human breast cancers. Genomics 42: 540-542, 1997.

8. Kitsberg, D.; Formstecher, E.; Fauquet, M.; Kubes, M.; Cordier,
J.; Canton, B.; Pan, G.; Rolli, M.; Glowinski, J.; Chneiweiss, H.
: Knock-out of the neural death effector domain protein PEA-15 demonstrates
that its expression protects astrocytes from TNF-alpha-induced apoptosis. J.
Neurosci. 19: 8244-8251, 1999.

9. Ramos, J. W.; Kojima, T. K.; Hughes, P. E.; Fenczik, C. A.; Ginsberg,
M. H.: The death effector domain of PEA-15 is involved in its regulation
of integrin activation. J. Biol. Chem. 273: 33897-33900, 1998.

10. Trencia, A.; Fiory, F.; Maitan, M. A.; Vito, P.; Barbagallo, A.
P. M.; Perfetti, A.; Miele, C.; Ungaro, P.; Oriente, F.; Cilenti,
L.; Zervos, A. S.; Formisano, P.; Beguinot, F.: Omi/HtrA2 promotes
cell death by binding and degrading the anti-apoptotic protein ped/pea-15. J.
Biol. Chem. 279: 46566-46572, 2004.

11. Vaidyanathan, H.; Opoku-Ansah, J.; Pastorino, S.; Renganathan,
H.; Matter, M. L.; Ramos, J. W.: ERK MAP kinase is targeted to RSK2
by the phosphoprotein PEA-15. Proc. Nat. Acad. Sci. 104: 19837-19842,
2007.

12. Wolford, J. K.; Bogardus, C.; Ossowski, V.; Prochazka, M.: Molecular
characterization of the human PEA15 gene on 1q21-q22 and association
with type 2 diabetes mellitus in Pima Indians. Gene 241: 143-148,
2000.

*FIELD* CN
Patricia A. Hartz - updated: 11/21/2012
Patricia A. Hartz - updated: 1/29/2008
Dawn Watkins-Chow - updated: 5/20/2003
Ada Hamosh - updated: 2/1/2000
Patti M. Sherman - updated: 1/20/1999

*FIELD* CD
Sheryl A. Jankowski: 1/14/1999

*FIELD* ED
mgross: 12/11/2012
terry: 11/21/2012
mgross: 2/7/2008
terry: 1/29/2008
carol: 5/20/2003
alopez: 2/2/2000
terry: 2/1/2000
psherman: 1/20/1999
psherman: 1/15/1999