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Protein

Astrocytic phosphoprotein PEA-15

Gene

PEA15

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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). Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm.By similarity3 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis, Sugar transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Astrocytic phosphoprotein PEA-15
Alternative name(s):
15 kDa phosphoprotein enriched in astrocytes
Gene namesi
Name:PEA15
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

  • Cytoplasm

  • Note: Associated with microtubules.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141N → R: Reduces MAPK1 binding. 1 Publication
Mutagenesisi16 – 161T → R: Reduces MAPK1 binding. 1 Publication
Mutagenesisi18 – 181E → R: Slightly reduces MAPK1 binding. 1 Publication
Mutagenesisi71 – 711R → A: Reduces MAPK1 binding. 1 Publication
Mutagenesisi74 – 741D → A: Abolishes MAPK1 binding and the blocking of Ras-mediated inhibition of integrin activation. 2 Publications
Mutagenesisi121 – 1211I → A or R: Abolishes MAPK1 binding. 1 Publication
Mutagenesisi122 – 1221K → E: Reduces MAPK1 binding. 1 Publication
Mutagenesisi123 – 1231L → A or R: Abolishes MAPK1 binding. 1 Publication
Mutagenesisi128 – 1281K → A or E: Abolishes MAPK1 binding. 1 Publication
Mutagenesisi129 – 1291K → A or R: Abolishes MAPK1 binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 130130Astrocytic phosphoprotein PEA-15PRO_0000191281Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611PhosphoserineBy similarity
Modified residuei90 – 901PhosphoserineBy similarity
Modified residuei104 – 1041Phosphoserine; by PKCBy similarity
Modified residuei116 – 1161Phosphoserine; by CaMK2By similarity

Post-translational modificationi

Phosphorylated by protein kinase C and calcium-calmodulin-dependent protein kinase. These phosphorylation events are modulated by neurotransmitters or hormones (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Interacts with CASP8 and FADD. Transient interaction with PLD1 and PLD2 (By similarity). Binds RPS6KA3, MAPK1 and MAPK3.By similarity3 Publications

Structurei

Secondary structure

130
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1313Combined sources
Helixi17 – 2711Combined sources
Turni28 – 303Combined sources
Turni36 – 383Combined sources
Helixi42 – 5110Combined sources
Turni52 – 543Combined sources
Helixi61 – 699Combined sources
Helixi73 – 8513Combined sources
Turni86 – 883Combined sources
Beta strandi93 – 964Combined sources
Turni103 – 1053Combined sources
Beta strandi109 – 1113Combined sources
Helixi120 – 1234Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N3KNMR-A1-130[»]
4IZ7X-ray1.80B1-96[»]
ProteinModelPortaliQ9Z297.
SMRiQ9Z297. Positions 1-130.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Z297.

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

HOVERGENiHBG053557.

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]

Sequencei

Sequence statusi: Complete.

Q9Z297-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEYGTLLQD LTNNITLEDL EQLKSACKED IPSEKSEEIT TGSAWFSFLE
60 70 80 90 100
SHNKLDKDNL SYIEHIFEIS RRPDLLTMVV DYRTRVLKIS EEDELDTKLT
110 120 130
RIPSAKKYKD IIRQPSEEEI IKLAPPPKKA
Length:130
Mass (Da):15,040
Last modified:May 1, 1999 - v1
Checksum:i8D0F93A40B299FB2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF080001 mRNA. Translation: AAC97496.1.
RefSeqiNP_001231780.1. NM_001244851.1.

Genome annotation databases

GeneIDi100736554.
KEGGicge:100736554.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF080001 mRNA. Translation: AAC97496.1.
RefSeqiNP_001231780.1. NM_001244851.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N3KNMR-A1-130[»]
4IZ7X-ray1.80B1-96[»]
ProteinModelPortaliQ9Z297.
SMRiQ9Z297. Positions 1-130.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100736554.
KEGGicge:100736554.

Organism-specific databases

CTDi8682.

Phylogenomic databases

HOVERGENiHBG053557.

Miscellaneous databases

EvolutionaryTraceiQ9Z297.

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

  1. "The death effector domain of PEA-15 is involved in its regulation of integrin activation."
    Ramos J.W., Kojima T.K., Hughes P.E., Fenczik C.A., Ginsberg M.H.
    J. Biol. Chem. 273:33897-33900(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF ASP-74.
    Tissue: Ovary.
  2. "Death effector domain protein PEA-15 potentiates Ras activation of extracellular signal receptor-activated kinase by an adhesion-independent mechanism."
    Ramos J.W., Hughes P.E., Renshaw M.W., Schwartz M.A., Formstecher E., Chneiweiss H., Ginsberg M.H.
    Mol. Biol. Cell 11:2863-2872(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "RSK2 activity is regulated by its interaction with PEA-15."
    Vaidyanathan H., Ramos J.W.
    J. Biol. Chem. 278:32367-32372(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPS6KA3.
  4. "PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation."
    Chou F.-L., Hill J.M., Hsieh J.-C., Pouyssegur J., Brunet A., Glading A., Ueberall F., Ramos J.W., Werner M.H., Ginsberg M.H.
    J. Biol. Chem. 278:52587-52597(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAPK1 AND MAPK3.
  5. "Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain."
    Hill J.M., Vaidyanathan H., Ramos J.W., Ginsberg M.H., Werner M.H.
    EMBO J. 21:6494-6504(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, INTERACTION WITH MAPK1, MUTAGENESIS OF ASN-14; THR-16; GLU-18; ARG-71; ASP-74; ILE-121; LYS-122; LEU-123; LYS-128 AND LYS-129.

Entry informationi

Entry nameiPEA15_CRIGR
AccessioniPrimary (citable) accession number: Q9Z297
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 1999
Last modified: October 14, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.