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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)DescriptionActionsGraphical viewLength
Mutagenesisi14N → R: Reduces MAPK1 binding. 1 Publication1
Mutagenesisi16T → R: Reduces MAPK1 binding. 1 Publication1
Mutagenesisi18E → R: Slightly reduces MAPK1 binding. 1 Publication1
Mutagenesisi71R → A: Reduces MAPK1 binding. 1 Publication1
Mutagenesisi74D → A: Abolishes MAPK1 binding and the blocking of Ras-mediated inhibition of integrin activation. 2 Publications1
Mutagenesisi121I → A or R: Abolishes MAPK1 binding. 1 Publication1
Mutagenesisi122K → E: Reduces MAPK1 binding. 1 Publication1
Mutagenesisi123L → A or R: Abolishes MAPK1 binding. 1 Publication1
Mutagenesisi128K → A or E: Abolishes MAPK1 binding. 1 Publication1
Mutagenesisi129K → A or R: Abolishes MAPK1 binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001912811 – 130Astrocytic phosphoprotein PEA-15Add BLAST130

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei61PhosphoserineBy similarity1
Modified residuei90PhosphoserineBy similarity1
Modified residuei104Phosphoserine; by PKCBy similarity1
Modified residuei116Phosphoserine; by CaMK2By similarity1

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

Proteomic databases

PRIDEiQ9Z297.

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

1130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 13Combined sources13
Helixi17 – 27Combined sources11
Turni28 – 30Combined sources3
Turni36 – 38Combined sources3
Helixi42 – 51Combined sources10
Turni52 – 54Combined sources3
Helixi61 – 69Combined sources9
Helixi73 – 85Combined sources13
Turni86 – 88Combined sources3
Beta strandi93 – 96Combined sources4
Turni103 – 105Combined sources3
Beta strandi109 – 111Combined sources3
Helixi120 – 123Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9Z297.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 81DEDPROSITE-ProRule annotationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni98 – 107Microtubule-bindingSequence analysis10
Regioni122 – 129Microtubule-bindingSequence analysis8

Sequence similaritiesi

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

Phylogenomic databases

HOVERGENiHBG053557.

Family and domain databases

CDDicd08338. DED_PEA15. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N3KNMR-A1-130[»]
4IZ7X-ray1.80B1-96[»]
ProteinModelPortaliQ9Z297.
SMRiQ9Z297.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ9Z297.

Proteomic databases

PRIDEiQ9Z297.

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

CDDicd08338. DED_PEA15. 1 hit.
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: November 2, 2016
This is version 86 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.