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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

PTM databases

iPTMnetiQ9Z297.

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...

PTM databases

iPTMnetiQ9Z297.

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...

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: June 8, 2016
This is version 84 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.