Type |
Details |
Score |
Publication |
First Author: |
Bairoch A |
Year: |
1999 |
Journal: |
Database Release |
Title: |
SWISS-PROT Annotated protein sequence database |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics |
Year: |
2010 |
Journal: |
Database Release |
Title: |
Protein Ontology Association Load. |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and loading genome assembly coordinates from NCBI annotations |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2009 |
Journal: |
Database Download |
Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Zimmermann J |
Year: |
2004 |
Journal: |
J Biomol NMR |
Title: |
1H, 13C and 15N resonance assignment of the human Spred2 EVH1 domain. |
Volume: |
29 |
Issue: |
3 |
Pages: |
435-6 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
The SPRE (also known as SPRED) proteins have the following domains: an N-terminal EVH1 domain, a unique KBD (c-Kit kinase binding) domain which is phosphorylated by the stem cell factor receptor c-Kit, and a C-terminal cysteine-rich SPR (Sprouty-related) domain which is involved in membrane localization. This entry represents the EVH1 domain of SPRE. Proteins containing this domaininclude Spred1 which interacts with both Ras and Raf through its SPR domain; Spred2 which is the most abundant isoform; and Spred3 which has a non-functional KBD and maintains the inhibitory action on Raf. Legius syndrome is caused by heterozygous mutations in Spred1. Both EVH1 and SPR domains are involved in the inhibition of the MAP kinase pathway by SPRE proteins. The specific function of the EVH1 domain is unknown and there are no known interacting proteins to date. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains [, , ]. |
|
•
•
•
•
•
|
Publication |
First Author: |
Harmer NJ |
Year: |
2005 |
Journal: |
FEBS Lett |
Title: |
1.15 A crystal structure of the X. tropicalis Spred1 EVH1 domain suggests a fourth distinct peptide-binding mechanism within the EVH1 family. |
Volume: |
579 |
Issue: |
5 |
Pages: |
1161-6 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
410
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
408
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
444
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
229
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
408
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
437
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Callebaut I |
Year: |
1998 |
Journal: |
FEBS Lett |
Title: |
EVH1/WH1 domains of VASP and WASP proteins belong to a large family including Ran-binding domains of the RanBP1 family. |
Volume: |
441 |
Issue: |
2 |
Pages: |
181-5 |
|
•
•
•
•
•
|