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Protein

E3 ubiquitin-protein ligase CBL

Gene

CBL

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

Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. 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. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation. Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis. Essential for osteoclastic bone resorption. The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity).By similarity9 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 the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei294PhosphotyrosineBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi227 – 240Add BLAST14
<p>This subsection of the ‘Function’ 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 fingeri381 – 420RING-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

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.3.2.B10 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1059683 Interleukin-6 signaling
R-HSA-1236382 Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants
R-HSA-1295596 Spry regulation of FGF signaling
R-HSA-1433559 Regulation of KIT signaling
R-HSA-182971 EGFR downregulation
R-HSA-2173789 TGF-beta receptor signaling activates SMADs
R-HSA-5637810 Constitutive Signaling by EGFRvIII
R-HSA-5654726 Negative regulation of FGFR1 signaling
R-HSA-5654727 Negative regulation of FGFR2 signaling
R-HSA-5654732 Negative regulation of FGFR3 signaling
R-HSA-5654733 Negative regulation of FGFR4 signaling
R-HSA-6807004 Negative regulation of MET activity
R-HSA-8849469 PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
R-HSA-8856825 Cargo recognition for clathrin-mediated endocytosis
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-8875360 InlB-mediated entry of Listeria monocytogenes into host cell
R-HSA-912631 Regulation of signaling by CBL

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

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SignaLinki
P22681

SIGNOR Signaling Network Open Resource

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SIGNORi
P22681

UniPathway: a resource for the exploration and annotation of metabolic pathways

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UniPathwayi
UPA00143

<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 (EC:2.3.2.273 Publications)
Alternative name(s):
Casitas B-lineage lymphoma proto-oncogene
Proto-oncogene c-Cbl
RING finger protein 55
RING-type E3 ubiquitin transferase CBLCurated
Signal transduction protein CBL
<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:CBL
Synonyms:CBL2, RNF55
<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 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000110395.5

Human Gene Nomenclature Database

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HGNCi
HGNC:1541 CBL

Online Mendelian Inheritance in Man (OMIM)

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MIMi
165360 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P22681

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Golgi apparatus, Membrane

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Noonan syndrome-like disorder with or without juvenile myelomonocytic leukemia (NSLL)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by a phenotype reminiscent of Noonan syndrome. Clinical features are highly variable, including facial dysmorphism, short neck, developmental delay, hyperextensible joints and thorax abnormalities with widely spaced nipples. The facial features consist of triangular face with hypertelorism, large low-set ears, ptosis, and flat nasal bridge. Some patients manifest cardiac defects. Some have an increased risk for certain malignancies, particularly juvenile myelomonocytic leukemia.
See also OMIM:613563
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_064332367Q → P in NSLL. 1 PublicationCorresponds to variant dbSNP:rs267606704EnsemblClinVar.1
Natural variantiVAR_064333382K → E in NSLL; dominant-negative; impairs CBL-mediated ubiquitination, internalization and degradation of the EGF receptor/EGFR; decreases the ability to negatively regulate EGFR signaling. 1 PublicationCorresponds to variant dbSNP:rs267606705EnsemblClinVar.1
Natural variantiVAR_064334390D → Y in NSLL; dominant-negative; impairs CBL-mediated ubiquitination, internalization and degradation of the EGF receptor/EGFR; decreases the ability to negatively regulate EGFR signaling. 2 PublicationsCorresponds to variant dbSNP:rs267606707EnsemblClinVar.1
Natural variantiVAR_064335420R → Q in NSLL; dominant-negative; impairs CBL-mediated ubiquitination, internalization and degradation of the EGF receptor/EGFR; decreases the ability to negatively regulate EGFR signaling. 2 PublicationsCorresponds to variant dbSNP:rs267606708EnsemblClinVar.1

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>Mutagenesisi80S → D: Abolishes interaction with ZAP70. 1 Publication1
Mutagenesisi82P → A: Abolishes interaction with ZAP70. 1 Publication1
Mutagenesisi229D → Q: Abolishes interaction with ZAP70. 1 Publication1
Mutagenesisi240E → S: Abolishes interaction with ZAP70. 1 Publication1
Mutagenesisi294R → K: Abolishes interaction with ZAP70. 1 Publication1
Mutagenesisi306G → E: Abolishes interaction with ZAP70 and EPHB1, but does not affect interaction with SLA. 2 Publications1
Mutagenesisi371Y → F: Strongly reduces tyrosine phosphorylation by INSR; when associated with F-700 and F-774. 1 Publication1
Mutagenesisi381C → A: Loss of ubiquitin ligase activity. 1 Publication1
Mutagenesisi700Y → F: Strongly reduces tyrosine phosphorylation by INSR; when associated with F-371 and F-774. 1 Publication1
Mutagenesisi731Y → F: No effect on tyrosine phosphorylation by INSR. Loss of phosphorylation by SRC. Inhibition of bone resorption. Abolishes interaction with PIK3R1. 2 Publications1
Mutagenesisi774Y → F: Strongly reduces tyrosine phosphorylation by INSR; when associated with F-371 and F-700. 1 Publication1

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNET

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DisGeNETi
867

MalaCards human disease database

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MalaCardsi
CBL
MIMi613563 phenotype

Open Targets

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OpenTargetsi
ENSG00000110395

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
86834 Juvenile myelomonocytic leukemia
363972 Noonan syndrome-like disorder with juvenile myelomonocytic leukemia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26115

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CBL

Domain mapping of disease mutations (DMDM)

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DMDMi
251757253

<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_00000558581 – 906E3 ubiquitin-protein ligase CBLAdd BLAST906

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 residuei371Phosphotyrosine; by INSR1 Publication1
Modified residuei439PhosphoserineCombined sources1
Modified residuei452PhosphoserineCombined sources1
Modified residuei483PhosphoserineCombined sources1
Modified residuei619PhosphoserineBy similarity1
Modified residuei642PhosphoserineBy similarity1
Modified residuei668PhosphoserineBy similarity1
Modified residuei669PhosphoserineCombined sources1
Modified residuei674Phosphotyrosine1 Publication1
Modified residuei700Phosphotyrosine; by ABL13 Publications1
Modified residuei731Phosphotyrosine; by SRC1 Publication1
Modified residuei774Phosphotyrosine2 Publications1
Modified residuei900PhosphoserineCombined sources1

<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 tyrosine residues by ALK, EGFR, SYK, FYN and ZAP70 (By similarity). Phosphorylated on tyrosine residues in response to FLT1 and KIT signaling. Phosphorylated on tyrosine residues by INSR and FGR. Phosphorylated on several tyrosine residues by constitutively activated FGFR3. Not phosphorylated at Tyr-731 by FGFR3. Phosphorylated on tyrosine residues by activated CSF1R, PDGFRA and PDGFRB. Phosphorylated on tyrosine residues by HCK.By similarity14 Publications
Ubiquitinated, leading to its degradation via the proteasome (PubMed:11896602, PubMed:20094046). Ubiquitination is negatively regulated by IFT20 (PubMed:29237719).3 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P22681

MaxQB - The MaxQuant DataBase

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MaxQBi
P22681

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

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PaxDbi
P22681

PeptideAtlas

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PeptideAtlasi
P22681

PRoteomics IDEntifications database

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PRIDEi
P22681

ProteomicsDB human proteome resource

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ProteomicsDBi
54017

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P22681

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

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PhosphoSitePlusi
P22681

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P22681

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000110395 Expressed in 210 organ(s), highest expression level in blood

CleanEx database of gene expression profiles

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CleanExi
HS_CBL

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P22681 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P22681 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004350
HPA027956

<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

Forms homodimers; IFT20 promotes the formation of stable homodimers (PubMed:29237719). Interacts (phosphorylated at Tyr-731) with PIK3R1. Associates with NCK via its SH3 domain. The phosphorylated C-terminus interacts with CD2AP via its second SH3 domain. Binds to UBE2L3. Interacts with adapters SLA, SLA2 and with the phosphorylated C-terminus of SH2B2. Interacts with EGFR, SYK and ZAP70 via the highly conserved Cbl-N region. Also interacts with SORBS1 and INPPL1/SHIP2. Interacts with phosphorylated LAT2 (By similarity). Interacts with CBLB (PubMed:29237719). Interacts with ALK, AXL, BLK, FGR and FGFR2. Interacts with CSF1R, EPHB1, FLT1, KDR, PDGFRA and PDGFRB; regulates receptor degradation through ubiquitination. Interacts with HCK and LYN. Interacts with TEK/TIE2 (tyrosine phosphorylated). Interacts with SH3KBP1 and this interaction is inhibited in the presence of SHKBP1 (By similarity). Interacts with SIGLEC10 (By similarity). Interacts with IFT20 (PubMed:29237719).By similarity29 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107315, 256 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P22681

Database of interacting proteins

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DIPi
DIP-189N

Protein interaction database and analysis system

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IntActi
P22681, 93 interactors

Molecular INTeraction database

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MINTi
P22681

STRING: functional protein association networks

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STRINGi
9606.ENSP00000264033

<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

1906
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P22681

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

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SMRi
P22681

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P22681

<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>Domaini47 – 351Cbl-PTBPROSITE-ProRule annotationAdd BLAST305
Domaini856 – 895UBAPROSITE-ProRule annotationAdd BLAST40

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>Regioni1 – 357Sufficient for interaction with EPHB11 PublicationAdd BLAST357
Regioni47 – 1754HAdd BLAST129
Regioni176 – 248EF-hand-likeAdd BLAST73
Regioni249 – 351SH2-likeAdd BLAST103
Regioni352 – 380LinkerAdd BLAST29
Regioni648 – 906Interaction with CD2AP1 PublicationAdd BLAST259

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi357 – 476Asp/Glu-rich (acidic)Add BLAST120
Compositional biasi477 – 688Pro-richAdd BLAST212
Compositional biasi689 – 834Asp/Glu-rich (acidic)Add BLAST146

<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

The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.
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.

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri381 – 420RING-typePROSITE-ProRule annotationAdd BLAST40

Keywords - Domaini

Repeat, 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
ENSGT00940000155772

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000294176

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005255

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P22681

KEGG Orthology (KO)

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KOi
K04707

Identification of Orthologs from Complete Genome Data

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OMAi
KTVEKCW

Database of Orthologous Groups

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OrthoDBi
EOG091G0GPE

Database for complete collections of gene phylogenies

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PhylomeDBi
P22681

TreeFam database of animal gene trees

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TreeFami
TF314210

Family and domain databases

Conserved Domains Database

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CDDi
cd16709 RING-HC_Cbl-b, 1 hit
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
IPR039520 CBL-B_RING-HC
IPR024159 Cbl_PTB
IPR011992 EF-hand-dom_pair
IPR036860 SH2_dom_sf
IPR015940 UBA
IPR009060 UBA-like_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
PF00627 UBA, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00184 RING, 1 hit
SM00165 UBA, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF46934 SSF46934, 1 hit
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
PS50030 UBA, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)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 has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

P22681-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAGNVKKSSG AGGGSGSGGS GSGGLIGLMK DAFQPHHHHH HHLSPHPPGT
60 70 80 90 100
VDKKMVEKCW KLMDKVVRLC QNPKLALKNS PPYILDLLPD TYQHLRTILS
110 120 130 140 150
RYEGKMETLG ENEYFRVFME NLMKKTKQTI SLFKEGKERM YEENSQPRRN
160 170 180 190 200
LTKLSLIFSH MLAELKGIFP SGLFQGDTFR ITKADAAEFW RKAFGEKTIV
210 220 230 240 250
PWKSFRQALH EVHPISSGLE AMALKSTIDL TCNDYISVFE FDIFTRLFQP
260 270 280 290 300
WSSLLRNWNS LAVTHPGYMA FLTYDEVKAR LQKFIHKPGS YIFRLSCTRL
310 320 330 340 350
GQWAIGYVTA DGNILQTIPH NKPLFQALID GFREGFYLFP DGRNQNPDLT
360 370 380 390 400
GLCEPTPQDH IKVTQEQYEL YCEMGSTFQL CKICAENDKD VKIEPCGHLM
410 420 430 440 450
CTSCLTSWQE SEGQGCPFCR CEIKGTEPIV VDPFDPRGSG SLLRQGAEGA
460 470 480 490 500
PSPNYDDDDD ERADDTLFMM KELAGAKVER PPSPFSMAPQ ASLPPVPPRL
510 520 530 540 550
DLLPQRVCVP SSASALGTAS KAASGSLHKD KPLPVPPTLR DLPPPPPPDR
560 570 580 590 600
PYSVGAESRP QRRPLPCTPG DCPSRDKLPP VPSSRLGDSW LPRPIPKVPV
610 620 630 640 650
SAPSSSDPWT GRELTNRHSL PFSLPSQMEP RPDVPRLGST FSLDTSMSMN
660 670 680 690 700
SSPLVGPECD HPKIKPSSSA NAIYSLAARP LPVPKLPPGE QCEGEEDTEY
710 720 730 740 750
MTPSSRPLRP LDTSQSSRAC DCDQQIDSCT YEAMYNIQSQ APSITESSTF
760 770 780 790 800
GEGNLAAAHA NTGPEESENE DDGYDVPKPP VPAVLARRTL SDISNASSSF
810 820 830 840 850
GWLSLDGDPT TNVTEGSQVP ERPPKPFPRR INSERKAGSC QQGSGPAASA
860 870 880 890 900
ATASPQLSSE IENLMSQGYS YQDIQKALVI AQNNIEMAKN ILREFVSISS

PAHVAT
Length:906
Mass (Da):99,633
Last modified:July 7, 2009 - v2
<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:i1AA6BF67377322CA
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 are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0U1RR39A0A0U1RR39_HUMAN
E3 ubiquitin-protein ligase CBL
CBL
862Annotation score:

Annotation score:2 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>
A0A0U1RQX8A0A0U1RQX8_HUMAN
E3 ubiquitin-protein ligase CBL
CBL
882Annotation 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>
A0A1B0GW38A0A1B0GW38_HUMAN
E3 ubiquitin-protein ligase CBL
CBL
869Annotation 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>
A0A0U1RRJ5A0A0U1RRJ5_HUMAN
E3 ubiquitin-protein ligase CBL
CBL
89Annotation 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 conflicti15S → T in CAA40393 (PubMed:2030914).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071040287K → R Found in patients with acute myeloid leukemia; unknown pathological significance. 1 Publication1
Natural variantiVAR_071041365Q → QSK Found in patients with acute myeloid leukemia; unknown pathological significance; loss of the ability to negatively regulate signaling pathways; promotes cell cycle progression; decreases apoptosis. 1
Natural variantiVAR_064332367Q → P in NSLL. 1 PublicationCorresponds to variant dbSNP:rs267606704EnsemblClinVar.1
Natural variantiVAR_071042371Y → H Found in patients with acute myeloid leukemia; unknown pathological significance; loss of the ability to negatively regulate signaling pathways; promotes cell cycle progression; decreases apoptosis. 1 PublicationCorresponds to variant dbSNP:rs267606706EnsemblClinVar.1
Natural variantiVAR_064333382K → E in NSLL; dominant-negative; impairs CBL-mediated ubiquitination, internalization and degradation of the EGF receptor/EGFR; decreases the ability to negatively regulate EGFR signaling. 1 PublicationCorresponds to variant dbSNP:rs267606705EnsemblClinVar.1
Natural variantiVAR_064334390D → Y in NSLL; dominant-negative; impairs CBL-mediated ubiquitination, internalization and degradation of the EGF receptor/EGFR; decreases the ability to negatively regulate EGFR signaling. 2 PublicationsCorresponds to variant dbSNP:rs267606707EnsemblClinVar.1
Natural variantiVAR_064335420R → Q in NSLL; dominant-negative; impairs CBL-mediated ubiquitination, internalization and degradation of the EGF receptor/EGFR; decreases the ability to negatively regulate EGFR signaling. 2 PublicationsCorresponds to variant dbSNP:rs267606708EnsemblClinVar.1
Natural variantiVAR_071043499R → L Found in patients with acute myeloid leukemia; unknown pathological significance. 1 Publication1
Natural variantiVAR_057211620L → F. Corresponds to variant dbSNP:rs2227988EnsemblClinVar.1
Natural variantiVAR_057212782P → L. Corresponds to variant dbSNP:rs2229073EnsemblClinVar.1
Natural variantiVAR_057213904V → I. Corresponds to variant dbSNP:rs17122769EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X57110 mRNA Translation: CAA40393.1
AP002956 Genomic DNA No translation available.
BC132733 mRNA Translation: AAI32734.1
BC136463 mRNA Translation: AAI36464.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS8418.1

Protein sequence database of the Protein Information Resource

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PIRi
A43817

NCBI Reference Sequences

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RefSeqi
NP_005179.2, NM_005188.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.504096

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000264033; ENSP00000264033; ENSG00000110395

Database of genes from NCBI RefSeq genomes

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GeneIDi
867

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:867

UCSC genome browser

More...
UCSCi
uc001pwe.5 human

Keywords - Coding sequence diversityi

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
X57110 mRNA Translation: CAA40393.1
AP002956 Genomic DNA No translation available.
BC132733 mRNA Translation: AAI32734.1
BC136463 mRNA Translation: AAI36464.1
CCDSiCCDS8418.1
PIRiA43817
RefSeqiNP_005179.2, NM_005188.3
UniGeneiHs.504096

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
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
1B47X-ray2.20A/B/C47-350[»]
1FBVX-ray2.90A47-434[»]
1YVHX-ray2.05A25-351[»]
2CBLX-ray2.10A47-351[»]
2JUJNMR-A851-906[»]
2K4DNMR-A358-437[»]
2OO9X-ray2.10A/B/C856-895[»]
2Y1MX-ray2.67A/B/C/D/E/F47-435[»]
2Y1NX-ray2.00A/C47-435[»]
3BUMX-ray2.00B25-351[»]
3BUNX-ray2.00B25-351[»]
3BUOX-ray2.60B/D25-351[»]
3BUWX-ray1.45B/D25-351[»]
3BUXX-ray1.35B/D25-351[»]
3OB1X-ray2.20B25-351[»]
3OB2X-ray2.10B25-351[»]
3PLFX-ray1.92B/D25-351[»]
4A49X-ray2.21A354-435[»]
4A4BX-ray2.79A47-435[»]
4A4CX-ray2.70A47-435[»]
4GPLX-ray3.00B47-351[»]
5HKWX-ray2.25A/B/C47-351[»]
5HKXX-ray1.85A47-435[»]
5HKYX-ray1.80A47-351[»]
5HKZX-ray1.80A47-351[»]
5HL0X-ray2.20A47-351[»]
5J3XX-ray2.82A/B/C/D/E/F47-435[»]
5O76X-ray2.47A/C47-435[»]
ProteinModelPortaliP22681
SMRiP22681
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107315, 256 interactors
CORUMiP22681
DIPiDIP-189N
IntActiP22681, 93 interactors
MINTiP22681
STRINGi9606.ENSP00000264033

PTM databases

iPTMnetiP22681
PhosphoSitePlusiP22681

Polymorphism and mutation databases

BioMutaiCBL
DMDMi251757253

Proteomic databases

EPDiP22681
MaxQBiP22681
PaxDbiP22681
PeptideAtlasiP22681
PRIDEiP22681
ProteomicsDBi54017

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264033; ENSP00000264033; ENSG00000110395
GeneIDi867
KEGGihsa:867
UCSCiuc001pwe.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
867
DisGeNETi867
EuPathDBiHostDB:ENSG00000110395.5

GeneCards: human genes, protein and diseases

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GeneCardsi
CBL
HGNCiHGNC:1541 CBL
HPAiCAB004350
HPA027956
MalaCardsiCBL
MIMi165360 gene
613563 phenotype
neXtProtiNX_P22681
OpenTargetsiENSG00000110395
Orphaneti86834 Juvenile myelomonocytic leukemia
363972 Noonan syndrome-like disorder with juvenile myelomonocytic leukemia
PharmGKBiPA26115

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1785 Eukaryota
ENOG410YDNH LUCA
GeneTreeiENSGT00940000155772
HOGENOMiHOG000294176
HOVERGENiHBG005255
InParanoidiP22681
KOiK04707
OMAiKTVEKCW
OrthoDBiEOG091G0GPE
PhylomeDBiP22681
TreeFamiTF314210

Enzyme and pathway databases

UniPathwayi
UPA00143

BRENDAi2.3.2.B10 2681
ReactomeiR-HSA-1059683 Interleukin-6 signaling
R-HSA-1236382 Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants
R-HSA-1295596 Spry regulation of FGF signaling
R-HSA-1433559 Regulation of KIT signaling
R-HSA-182971 EGFR downregulation
R-HSA-2173789 TGF-beta receptor signaling activates SMADs
R-HSA-5637810 Constitutive Signaling by EGFRvIII
R-HSA-5654726 Negative regulation of FGFR1 signaling
R-HSA-5654727 Negative regulation of FGFR2 signaling
R-HSA-5654732 Negative regulation of FGFR3 signaling
R-HSA-5654733 Negative regulation of FGFR4 signaling
R-HSA-6807004 Negative regulation of MET activity
R-HSA-8849469 PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
R-HSA-8856825 Cargo recognition for clathrin-mediated endocytosis
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-8875360 InlB-mediated entry of Listeria monocytogenes into host cell
R-HSA-912631 Regulation of signaling by CBL
SignaLinkiP22681
SIGNORiP22681

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
CBL human
EvolutionaryTraceiP22681

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
CBL_(gene)

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

More...
GenomeRNAii
867
PMAP-CutDBiP22681

Protein Ontology

More...
PROi
PR:P22681

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000110395 Expressed in 210 organ(s), highest expression level in blood
CleanExiHS_CBL
ExpressionAtlasiP22681 baseline and differential
GenevisibleiP22681 HS

Family and domain databases

CDDicd16709 RING-HC_Cbl-b, 1 hit
cd09920 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
IPR039520 CBL-B_RING-HC
IPR024159 Cbl_PTB
IPR011992 EF-hand-dom_pair
IPR036860 SH2_dom_sf
IPR015940 UBA
IPR009060 UBA-like_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
PF00627 UBA, 1 hit
SMARTiView protein in SMART
SM00184 RING, 1 hit
SM00165 UBA, 1 hit
SUPFAMiSSF46934 SSF46934, 1 hit
SSF47473 SSF47473, 1 hit
SSF47668 SSF47668, 1 hit
SSF55550 SSF55550, 1 hit
PROSITEiView protein in PROSITE
PS51506 CBL_PTB, 1 hit
PS50030 UBA, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiCBL_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: P22681
Secondary accession number(s): A3KMP8
<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: August 1, 1991
Last sequence update: July 7, 2009
Last modified: December 5, 2018
This is version 225 of the entry and version 2 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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