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Entry version 183 (18 Sep 2019)
Sequence version 3 (06 Feb 2007)
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Protein

E3 ubiquitin-protein ligase CBL-C

Gene

CBLC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Functionally coupled with the E2 ubiquitin-protein ligases UB2D1, UB2D2 and UB2D3. Regulator of EGFR mediated signal transduction; upon EGF activation, ubiquitinates EGFR. Isoform 1, but not isoform 2, inhibits EGF stimulated MAPK1 activation. Promotes ubiquitination of SRC phosphorylated at 'Tyr-419'. In collaboration with CD2AP may act as regulatory checkpoint for Ret signaling by modulating the rate of RET degradation after ligand activation; CD2AP converts it from an inhibitor to a promoter of RET degradation; the function limits the potency of GDNF on neuronal survival.5 Publications

Miscellaneous

This protein has one functional calcium-binding site.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Phosphorylation at Tyr-341 is necessary and sufficient for the activation of E3 activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei264Phosphotyrosine1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi199 – 210Add BLAST12
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri351 – 390RING-typePROSITE-ProRule annotationAdd BLAST40

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
Biological processUbl conjugation pathway
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q9ULV8

SIGNOR Signaling Network Open Resource

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SIGNORi
Q9ULV8

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
E3 ubiquitin-protein ligase CBL-C (EC:2.3.2.273 Publications)
Alternative name(s):
RING finger protein 57
RING-type E3 ubiquitin transferase CBL-CCurated
SH3-binding protein CBL-3
SH3-binding protein CBL-C
Signal transduction protein CBL-C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CBLC
Synonyms:CBL3, RNF57
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:15961 CBLC

Online Mendelian Inheritance in Man (OMIM)

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MIMi
608453 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9ULV8

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi244Y → A: Abolishes interaction with EGFR. Decreases interaction with SRC and abolishes SRC ubiquitination. 1 Publication1
Mutagenesisi244Y → F: No effect on interaction with EGFR and SRC as well as on SRC ubiquitination. 1 Publication1
Mutagenesisi264R → A: Abolishes interaction with EGFR. Decreases interaction with SRC and abolishes SRC ubiquitination. 1 Publication1
Mutagenesisi265P → L: Enhances interaction with EGFR and SRC as well as SRC ubiquitination. 1 Publication1
Mutagenesisi266S → A: Decreases interactions with EGFR and SRC as well as SRC ubiquitination. 1 Publication1
Mutagenesisi268T → A: Abolishes interaction with EGFR. Decreases interaction with and ubiquitination of SRC. 1 Publication1
Mutagenesisi276G → E: No effect on interaction with RET. Binds slightly to SRC, this interaction is independent of SRC phosphorylation. Strongly decreases SRC ubiquitination. Abolishes interaction with EGFR. 3 Publications1
Mutagenesisi341Y → E: Induces E3 activity and autoubiquitination. Releases ubiquitin-conjugating enzyme E2 UBE2D2 faster. 3 Publications1
Mutagenesisi341Y → F: Abolishes activation by EGF stimulation and enhancement by TGFB1I1 of E3 activity. 3 Publications1
Mutagenesisi341Missing : Abolishes E3 activity. 3 Publications1
Mutagenesisi351C → A: No effect on TGFB1I1 and SRC interactions. Abolishes SRC ubiquitination. Abolishes interaction with TGFB1I1; when associated with A-366. Abolishes interaction with RET and inhibition of RET degradation. 3 Publications1
Mutagenesisi366C → A: Abolishes interaction with TGFB1I1. Abolishes interaction with TGFB1I1; when associated with A-351. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
23624

Open Targets

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OpenTargetsi
ENSG00000142273

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26117

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CBLC

Domain mapping of disease mutations (DMDM)

More...
DMDMi
125987803

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000558661 – 474E3 ubiquitin-protein ligase CBL-CAdd BLAST474

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei341Phosphotyrosine; by SRC2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated on multiple tyrosine residues by SRC. Isoform 1, but not isoform 2, is phosphorylated on tyrosines by EGFR.
Autoubiquitinated when phosphorylated at Tyr-341, enhanced by SRC; suggesting proteasomal degradation.3 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9ULV8

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9ULV8

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9ULV8

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q9ULV8

PeptideAtlas

More...
PeptideAtlasi
Q9ULV8

PRoteomics IDEntifications database

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PRIDEi
Q9ULV8

ProteomicsDB human proteome resource

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ProteomicsDBi
85137 [Q9ULV8-1]
85138 [Q9ULV8-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9ULV8

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9ULV8

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000142273 Expressed in 77 organ(s), highest expression level in mucosa of transverse colon

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9ULV8 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9ULV8 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB008087
HPA035266

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with ubiquitin-conjugating enzyme E2 UBE2D2 and UBE2D3.

Isoform 1 interacts with EGFR (tyrosine phosphorylated).

Interacts with the SH3 domain proteins LYN and CRK.

Interacts (via RING-type zinc finger) with TGFB1I1 (via LIM zinc-binding domain 2); the interaction is direct and enhances the E3 activity.

Interacts directly with RET (inactive) and CD2AP; dissociates from RET upon RET activation by GDNF which also increases the interaction with CD2AP suggesting dissociation as CBLC:CD2AP complex.

Interacts with SRC; the interaction is enhanced when SRC is phosphorylated at 'Tyr-419'.

7 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
117156, 66 interactors

Protein interaction database and analysis system

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IntActi
Q9ULV8, 31 interactors

Molecular INTeraction database

More...
MINTi
Q9ULV8

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000270279

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1474
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9ULV8

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini7 – 321Cbl-PTBPROSITE-ProRule annotationAdd BLAST315

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni7 – 1454HAdd BLAST139
Regioni146 – 218EF-hand-likeAdd BLAST73
Regioni219 – 321SH2-likeAdd BLAST103
Regioni322 – 350LinkerAdd BLAST29
Regioni351 – 474Interaction with RET1 PublicationAdd BLAST124

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

EF-hand-like and Sh2-like domains are required for N-terminal inhibition of E3 activity.1 Publication
The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain.PROSITE-ProRule annotation1 Publication
The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri351 – 390RING-typePROSITE-ProRule annotationAdd BLAST40

Keywords - Domaini

Repeat, SH3-binding, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1785 Eukaryota
ENOG410YDNH LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000162336

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000294176

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9ULV8

KEGG Orthology (KO)

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KOi
K22518

Identification of Orthologs from Complete Genome Data

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OMAi
QWAVGYV

Database of Orthologous Groups

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OrthoDBi
540689at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9ULV8

TreeFam database of animal gene trees

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TreeFami
TF314210

Family and domain databases

Conserved Domains Database

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CDDi
cd09920 SH2_Cbl-b_TKB, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.930.20, 1 hit
3.30.40.10, 1 hit
3.30.505.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR024162 Adaptor_Cbl
IPR014741 Adaptor_Cbl_EF_hand-like
IPR036537 Adaptor_Cbl_N_dom_sf
IPR003153 Adaptor_Cbl_N_hlx
IPR014742 Adaptor_Cbl_SH2-like
IPR024159 Cbl_PTB
IPR011992 EF-hand-dom_pair
IPR036860 SH2_dom_sf
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS

The PANTHER Classification System

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PANTHERi
PTHR23007 PTHR23007, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02262 Cbl_N, 1 hit
PF02761 Cbl_N2, 1 hit
PF02762 Cbl_N3, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00184 RING, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47473 SSF47473, 1 hit
SSF47668 SSF47668, 1 hit
SSF55550 SSF55550, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51506 CBL_PTB, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9ULV8-1) [UniParc]FASTAAdd to basket
Also known as: Long

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MALAVAPWGR QWEEARALGR AVRMLQRLEE QCVDPRLSVS PPSLRDLLPR
60 70 80 90 100
TAQLLREVAH SRRAAGGGGP GGPGGSGDFL LIYLANLEAK SRQVAALLPP
110 120 130 140 150
RGRRSANDEL FRAGSRLRRQ LAKLAIIFSH MHAELHALFP GGKYCGHMYQ
160 170 180 190 200
LTKAPAHTFW RESCGARCVL PWAEFESLLG TCHPVEPGCT ALALRTTIDL
210 220 230 240 250
TCSGHVSIFE FDVFTRLFQP WPTLLKNWQL LAVNHPGYMA FLTYDEVQER
260 270 280 290 300
LQACRDKPGS YIFRPSCTRL GQWAIGYVSS DGSILQTIPA NKPLSQVLLE
310 320 330 340 350
GQKDGFYLYP DGKTHNPDLT ELGQAEPQQR IHVSEEQLQL YWAMDSTFEL
360 370 380 390 400
CKICAESNKD VKIEPCGHLL CSCCLAAWQH SDSQTCPFCR CEIKGWEAVS
410 420 430 440 450
IYQFHGQATA EDSGNSSDQE GRELELGQVP LSAPPLPPRP DLPPRKPRNA
460 470
QPKVRLLKGN SPPAALGPQD PAPA
Length:474
Mass (Da):52,456
Last modified:February 6, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i202634AEDE434544
GO
Isoform 2 (identifier: Q9ULV8-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     261-306: Missing.

Show »
Length:428
Mass (Da):47,418
Checksum:i7070EDF530032CA0
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2R8Y647A0A2R8Y647_HUMAN
E3 ubiquitin-protein ligase CBL-C
CBLC
182Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti234N → T in BAA86298 (PubMed:10571044).Curated1
Sequence conflicti413S → P in AAH28915 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_018298405H → Y2 PublicationsCorresponds to variant dbSNP:rs3208856Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_005732261 – 306Missing in isoform 2. 1 PublicationAdd BLAST46

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AB028645 mRNA Translation: BAA86298.1
AF117646 mRNA Translation: AAD34341.1
AF117647 mRNA Translation: AAD34342.1
BC028915 mRNA Translation: AAH28915.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS12643.1 [Q9ULV8-1]
CCDS46109.1 [Q9ULV8-2]

NCBI Reference Sequences

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RefSeqi
NP_001124324.1, NM_001130852.1 [Q9ULV8-2]
NP_036248.3, NM_012116.3 [Q9ULV8-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000341505; ENSP00000340250; ENSG00000142273 [Q9ULV8-2]
ENST00000647358; ENSP00000494162; ENSG00000142273 [Q9ULV8-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
23624

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:23624

UCSC genome browser

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UCSCi
uc002ozs.4 human [Q9ULV8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028645 mRNA Translation: BAA86298.1
AF117646 mRNA Translation: AAD34341.1
AF117647 mRNA Translation: AAD34342.1
BC028915 mRNA Translation: AAH28915.1
CCDSiCCDS12643.1 [Q9ULV8-1]
CCDS46109.1 [Q9ULV8-2]
RefSeqiNP_001124324.1, NM_001130852.1 [Q9ULV8-2]
NP_036248.3, NM_012116.3 [Q9ULV8-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OP0X-ray2.52A/B9-323[»]
3VRNX-ray1.64A1-323[»]
3VROX-ray1.80A1-323[»]
3VRPX-ray1.52A1-323[»]
3VRQX-ray2.39A/B1-323[»]
3VRRX-ray2.00A1-323[»]
SMRiQ9ULV8
ModBaseiSearch...

Protein-protein interaction databases

BioGridi117156, 66 interactors
IntActiQ9ULV8, 31 interactors
MINTiQ9ULV8
STRINGi9606.ENSP00000270279

PTM databases

iPTMnetiQ9ULV8
PhosphoSitePlusiQ9ULV8

Polymorphism and mutation databases

BioMutaiCBLC
DMDMi125987803

Proteomic databases

EPDiQ9ULV8
jPOSTiQ9ULV8
MassIVEiQ9ULV8
PaxDbiQ9ULV8
PeptideAtlasiQ9ULV8
PRIDEiQ9ULV8
ProteomicsDBi85137 [Q9ULV8-1]
85138 [Q9ULV8-2]

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
23624
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341505; ENSP00000340250; ENSG00000142273 [Q9ULV8-2]
ENST00000647358; ENSP00000494162; ENSG00000142273 [Q9ULV8-1]
GeneIDi23624
KEGGihsa:23624
UCSCiuc002ozs.4 human [Q9ULV8-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
23624
DisGeNETi23624

GeneCards: human genes, protein and diseases

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GeneCardsi
CBLC
HGNCiHGNC:15961 CBLC
HPAiCAB008087
HPA035266
MIMi608453 gene
neXtProtiNX_Q9ULV8
OpenTargetsiENSG00000142273
PharmGKBiPA26117

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1785 Eukaryota
ENOG410YDNH LUCA
GeneTreeiENSGT00940000162336
HOGENOMiHOG000294176
InParanoidiQ9ULV8
KOiK22518
OMAiQWAVGYV
OrthoDBi540689at2759
PhylomeDBiQ9ULV8
TreeFamiTF314210

Enzyme and pathway databases

SignaLinkiQ9ULV8
SIGNORiQ9ULV8

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
CBLC

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
23624

Pharos

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Pharosi
Q9ULV8

Protein Ontology

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PROi
PR:Q9ULV8

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000142273 Expressed in 77 organ(s), highest expression level in mucosa of transverse colon
ExpressionAtlasiQ9ULV8 baseline and differential
GenevisibleiQ9ULV8 HS

Family and domain databases

CDDicd09920 SH2_Cbl-b_TKB, 1 hit
Gene3Di1.20.930.20, 1 hit
3.30.40.10, 1 hit
3.30.505.10, 1 hit
InterProiView protein in InterPro
IPR024162 Adaptor_Cbl
IPR014741 Adaptor_Cbl_EF_hand-like
IPR036537 Adaptor_Cbl_N_dom_sf
IPR003153 Adaptor_Cbl_N_hlx
IPR014742 Adaptor_Cbl_SH2-like
IPR024159 Cbl_PTB
IPR011992 EF-hand-dom_pair
IPR036860 SH2_dom_sf
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PANTHERiPTHR23007 PTHR23007, 1 hit
PfamiView protein in Pfam
PF02262 Cbl_N, 1 hit
PF02761 Cbl_N2, 1 hit
PF02762 Cbl_N3, 1 hit
SMARTiView protein in SMART
SM00184 RING, 1 hit
SUPFAMiSSF47473 SSF47473, 1 hit
SSF47668 SSF47668, 1 hit
SSF55550 SSF55550, 1 hit
PROSITEiView protein in PROSITE
PS51506 CBL_PTB, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCBLC_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9ULV8
Secondary accession number(s): Q8N1E5, Q9Y5Z2, Q9Y5Z3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 6, 2007
Last modified: September 18, 2019
This is version 183 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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