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InterPro: IPR006597 Sel1-like

Protein matchesHelp
UniProtKB
Matches:
4575 proteins
AccessionHelp IPR006597 Sel1-like
SecondaryHelp IPR013245
TypeHelp Repeat
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR011990 Tetratricopeptide-like helical
IPR017400 Elongation factor 2 kinase
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Sel1-like repeats are tetratricopeptide repeat sequences originally identified in a Caenorhabditis elegans receptor molecule which is a key negative regulator of the Notch pathway [1]. Mammalian homologues have since been identified although these mainly pancreatic proteins have yet to have a function assigned.

Structural linksHelp
SCOP: a.118.18.1
CATH: 1.25.40.10
Database linksHelp
Blocks: IPB006597
Pfam Clan: CL0020.21

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR006597 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
A6ZR53 Protein SHC1

O00418 Elongation factor 2 kinase

O01991 Elongation factor 2 kinase

O08796 Elongation factor 2 kinase

Q9W5N0 Hcp beta-lactamase-like protein CG13865

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR011009 Protein kinase-like domain
IPR004166 MHCK/EF2 kinase
IPR011990 Tetratricopeptide-like helical
IPR006597 Sel1-like
IPR017400 Elongation factor 2 kinase
SWISS-MODEL
ModBase

PublicationsHelp
1. Grant B, Greenwald I.
The Caenorhabditis elegans sel-1 gene, a negative regulator of lin-12 and glp-1, encodes a predicted extracellular protein.
Genetics 143 237-47 1996 [PubMed: 8722778]
http://intl.genetics.org/cgi/content/abstract/143/1/237

Additional ReadingHelp
Luthy L, Grutter MG, Mittl PR.
The crystal structure of Helicobacter cysteine-rich protein C at 2.0 A resolution: similar peptide-binding sites in TPR and SEL1-like repeat proteins.
J. Mol. Biol. 340 2004 829-41 [PubMed: 15223324]
http://dx.doi.org/10.1016/j.jmb.2004.04.055
Luthy L, Grutter MG, Mittl PR.
The crystal structure of Helicobacter pylori cysteine-rich protein B reveals a novel fold for a penicillin-binding protein.
J. Biol. Chem. 277 2002 10187-93 [PubMed: 11777911]
http://dx.doi.org/10.1074/jbc.M108993200
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InterPro 23.1