SUPERFAMILY 1.75 HMM library and genome assignments server

Superfamily is undergoing a server migration - you are now browsing on the new server. Please contact us if you experience any problems.


N-terminal domain of cbl (N-cbl) superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   All alpha proteins [ 46456] (284)
Fold:   N-cbl like [ 47667] (5)
Superfamily:   N-terminal domain of cbl (N-cbl) [ 47668]
Families:   N-terminal domain of cbl (N-cbl) [ 47669]


Superfamily statistics
Genomes (139) Uniprot 2018_03 genome PDB chains (SCOP 1.75)
Domains 324 884 4
Proteins 324 882 4


Functional annotation
General category coiled coil
Detailed category The code refers to a 2-stranded_canonical_parallel_coiled_coils in the CC+ database. Please click on the link for more information and to visit the CC+ website.

Document:
Function annotation of SCOP domain superfamilies

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEC levelAnnotation (direct or inherited)
Enzyme Commission (EC)Aminoacyltransferases0Moderately InformativeDirect
Enzyme Commission (EC)RING-type E3 ubiquitin transferase0InformativeDirect

Document: EC annotation of SCOP domains

InterPro annotation
Cross references IPR003153 SSF47668 Protein matches
Abstract

Cbl adaptor proteins are RING-type E3 ubiquitin ligases. Cbl may be involved in the negative regulation of thymocyte development, targeting its substrate for ubiquitination [PubMed11864842]. The ubiquitin ligase activity of Cbl, and of its homologue Cbl-b, plays a role in the negative regulation of upstream kinases, such as Lck, Syk and PI3K, in T and B cells [PubMed12787751]. Cbl can interact with the EGF receptor (EGFR), causing the ubiquitination of the receptor following EGF ligand binding and Grb2 association. Ubiquitination is required for ligand-induced endocytosis of the EGFR [PubMed15194809].

The N-terminal region is composed of three evolutionarily conserved domains: an N-terminal four-helix bundle domain, an EF Hand-like domain and a SH2-like domain, which together are known to bind to phosphorylated tyrosine residues. This entry represents the N-terminal four-helical bundle domain.


InterPro database


PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) ]

Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.


Alignments of sequences to 3 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.


Browse and view proteins in genomes which have different domain combinations including a N-terminal domain of cbl (N-cbl) domain.


Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.


Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 3 hidden Markov models representing the N-terminal domain of cbl (N-cbl) superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.


Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Internal database links ]