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Protein

Astrocytic phosphoprotein PEA-15

Gene

Pea15

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm. Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface (By similarity).By similarity1 Publication

GO - Molecular functioni

  • protein kinase C binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis, Sugar transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-112409. RAF-independent MAPK1/3 activation.
R-MMU-5673001. RAF/MAP kinase cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Astrocytic phosphoprotein PEA-15
Alternative name(s):
15 kDa phosphoprotein enriched in astrocytes
Gene namesi
Name:Pea15
Synonyms:Pea15a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:104799. Pea15a.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • microtubule associated complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi104 – 1041S → A: Abolishes inhibitory effect on FAS-mediated apoptosis. Does not change effect on TNFRSF1A-mediated apoptosis. 1 Publication
Mutagenesisi116 – 1161S → A: Abolishes inhibitory effect on FAS-mediated apoptosis. Does not change effect on TNFRSF1A-mediated apoptosis. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 130130Astrocytic phosphoprotein PEA-15PRO_0000191283Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611PhosphoserineBy similarity
Modified residuei90 – 901PhosphoserineCombined sources
Modified residuei104 – 1041Phosphoserine; by PKCCombined sources1 Publication
Modified residuei116 – 1161Phosphoserine; by CaMK2Combined sources1 Publication

Post-translational modificationi

Phosphorylated by protein kinase C and calcium-calmodulin-dependent protein kinase. These phosphorylation events are modulated by neurotransmitters or hormones.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ62048.
MaxQBiQ62048.
PaxDbiQ62048.
PRIDEiQ62048.

PTM databases

iPTMnetiQ62048.
PhosphoSiteiQ62048.

Expressioni

Tissue specificityi

Predominantly expressed in the brain. Low levels in some peripheral organs.

Gene expression databases

BgeeiQ62048.
CleanExiMM_PEA15A.
ExpressionAtlasiQ62048. baseline and differential.
GenevisibleiQ62048. MM.

Interactioni

Subunit structurei

Binds RPS6KA3, MAPK3 and MAPK1. Interacts with CASP8 and FADD (By similarity). Transient interaction with PLD1 and PLD2.By similarity1 Publication

GO - Molecular functioni

  • protein kinase C binding Source: MGI

Protein-protein interaction databases

BioGridi202103. 2 interactions.
DIPiDIP-60009N.
IntActiQ62048. 1 interaction.
MINTiMINT-4106963.
STRINGi10090.ENSMUSP00000013842.

Structurei

Secondary structure

1
130
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1413Combined sources
Helixi17 – 2610Combined sources
Turni27 – 304Combined sources
Helixi33 – 375Combined sources
Helixi42 – 5110Combined sources
Turni52 – 543Combined sources
Helixi61 – 699Combined sources
Helixi73 – 8917Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LS7NMR-A1-90[»]
ProteinModelPortaliQ62048.
SMRiQ62048. Positions 1-130.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8179DEDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 10710Microtubule-bindingSequence analysis
Regioni122 – 1298Microtubule-bindingSequence analysis

Sequence similaritiesi

Contains 1 DED (death effector) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
GeneTreeiENSGT00390000000230.
HOGENOMiHOG000049048.
HOVERGENiHBG053557.
InParanoidiQ62048.
OMAiSPVMAEY.
OrthoDBiEOG7D2FGM.
PhylomeDBiQ62048.
TreeFamiTF332405.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR001875. DED_dom.
IPR029546. PEA15.
[Graphical view]
PANTHERiPTHR15094:SF0. PTHR15094:SF0. 1 hit.
PfamiPF01335. DED. 1 hit.
[Graphical view]
SMARTiSM00031. DED. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50168. DED. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q62048-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAEYGTLLQD LTNNITLEDL EQLKSACKED IPSEKSEEIT TGSAWFSFLE
60 70 80 90 100
SHNKLDKDNL SYIEHIFEIS RRPDLLTMVV DYRTRVLKIS EEEELDTKLT
110 120 130
RIPSAKKYKD IIRQPSEEEI IKLAPPPKKA
Length:130
Mass (Da):15,054
Last modified:November 1, 1996 - v1
Checksum:i780F93A40B2834A8
GO
Isoform 2 (identifier: Q62048-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     36-57: Missing.
     58-58: D → N

Show »
Length:108
Mass (Da):12,544
Checksum:iBCF0527AE97E42AF
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei36 – 5722Missing in isoform 2. 1 PublicationVSP_007736Add
BLAST
Alternative sequencei58 – 581D → N in isoform 2. 1 PublicationVSP_007737

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86694 Genomic DNA. Translation: CAA60387.1.
AK089070 mRNA. Translation: BAC40734.1.
AK153141 mRNA. Translation: BAE31752.1.
AK153493 mRNA. Translation: BAE32041.1.
AK161635 mRNA. Translation: BAE36504.1.
AK161977 mRNA. Translation: BAE36662.1.
BC038282 mRNA. Translation: AAH38282.1.
CCDSiCCDS15510.1. [Q62048-1]
PIRiS55385.
RefSeqiNP_035193.1. NM_011063.2. [Q62048-1]
XP_006496765.1. XM_006496702.1. [Q62048-1]
UniGeneiMm.544.

Genome annotation databases

EnsembliENSMUST00000013842; ENSMUSP00000013842; ENSMUSG00000013698. [Q62048-1]
ENSMUST00000111247; ENSMUSP00000106878; ENSMUSG00000013698. [Q62048-2]
GeneIDi18611.
KEGGimmu:18611.
UCSCiuc007dpy.1. mouse. [Q62048-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86694 Genomic DNA. Translation: CAA60387.1.
AK089070 mRNA. Translation: BAC40734.1.
AK153141 mRNA. Translation: BAE31752.1.
AK153493 mRNA. Translation: BAE32041.1.
AK161635 mRNA. Translation: BAE36504.1.
AK161977 mRNA. Translation: BAE36662.1.
BC038282 mRNA. Translation: AAH38282.1.
CCDSiCCDS15510.1. [Q62048-1]
PIRiS55385.
RefSeqiNP_035193.1. NM_011063.2. [Q62048-1]
XP_006496765.1. XM_006496702.1. [Q62048-1]
UniGeneiMm.544.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LS7NMR-A1-90[»]
ProteinModelPortaliQ62048.
SMRiQ62048. Positions 1-130.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202103. 2 interactions.
DIPiDIP-60009N.
IntActiQ62048. 1 interaction.
MINTiMINT-4106963.
STRINGi10090.ENSMUSP00000013842.

PTM databases

iPTMnetiQ62048.
PhosphoSiteiQ62048.

Proteomic databases

EPDiQ62048.
MaxQBiQ62048.
PaxDbiQ62048.
PRIDEiQ62048.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000013842; ENSMUSP00000013842; ENSMUSG00000013698. [Q62048-1]
ENSMUST00000111247; ENSMUSP00000106878; ENSMUSG00000013698. [Q62048-2]
GeneIDi18611.
KEGGimmu:18611.
UCSCiuc007dpy.1. mouse. [Q62048-1]

Organism-specific databases

CTDi18611.
MGIiMGI:104799. Pea15a.

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
GeneTreeiENSGT00390000000230.
HOGENOMiHOG000049048.
HOVERGENiHBG053557.
InParanoidiQ62048.
OMAiSPVMAEY.
OrthoDBiEOG7D2FGM.
PhylomeDBiQ62048.
TreeFamiTF332405.

Enzyme and pathway databases

ReactomeiR-MMU-112409. RAF-independent MAPK1/3 activation.
R-MMU-5673001. RAF/MAP kinase cascade.

Miscellaneous databases

NextBioi294542.
PROiQ62048.
SOURCEiSearch...

Gene expression databases

BgeeiQ62048.
CleanExiMM_PEA15A.
ExpressionAtlasiQ62048. baseline and differential.
GenevisibleiQ62048. MM.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR001875. DED_dom.
IPR029546. PEA15.
[Graphical view]
PANTHERiPTHR15094:SF0. PTHR15094:SF0. 1 hit.
PfamiPF01335. DED. 1 hit.
[Graphical view]
SMARTiSM00031. DED. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50168. DED. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The major astrocytic phosphoprotein PEA-15 is encoded by two mRNAs conserved on their full length in mouse and human."
    Estelles A., Yokoyama M., Nothias F., Vincent J.-D., Glowinski J., Vernier P., Chneiweiss H.
    J. Biol. Chem. 271:14800-14806(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    Strain: SWR/J.
    Tissue: Astrocyte.
  2. "Identification of a novel, alternatively spliced isoform and single nucleotide polymorphisms in the murine Pea-15 gene."
    Underhill D.A., Vogan K.J., Underhill T.M., Gros P.
    Mamm. Genome 12:172-174(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Cerebellum and Thymus.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Retina.
  5. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 58-71, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  6. "The phosphoprotein protein PEA-15 inhibits Fas- but increases TNF-R1-mediated caspase-8 activity and apoptosis."
    Estelles A., Charlton C.A., Blau H.M.
    Dev. Biol. 216:16-28(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-104 AND SER-116, MUTAGENESIS OF SER-104 AND SER-116.
  7. "Regulation of expression of phospholipase D1 and D2 by PEA-15, a novel protein that interacts with them."
    Zhang Y., Redina O., Altshuller Y.M., Yamazaki M., Ramos J., Chneiweiss H., Kanaho Y., Frohman M.A.
    J. Biol. Chem. 275:35224-35232(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLD1 AND PLD2, SUBCELLULAR LOCATION.
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND SER-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPEA15_MOUSE
AccessioniPrimary (citable) accession number: Q62048
Secondary accession number(s): Q3U5N7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: March 16, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Increases PLD1 and PLD2 levels, possibly by stabilizing the protein.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.