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Protein

Protein CASC3

Gene

CASC3

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

Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Binds poly(G) and poly(U) RNA homopolymer.2 Publications

<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

  • enzyme binding Source: UniProtKB
  • identical protein binding Source: MGI
  • RNA binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

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 functionRNA-binding
Biological processmRNA processing, mRNA splicing, mRNA transport, Nonsense-mediated mRNA decay, Stress response, Translation regulation, Transport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-109688 Cleavage of Growing Transcript in the Termination Region
R-HSA-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.A.18.1.1 the nuclear mrna exporter (mrna-e) family

<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:
Protein CASC3
Alternative name(s):
Cancer susceptibility candidate gene 3 protein
Metastatic lymph node gene 51 protein1 Publication
Short name:
MLN 51
Protein barentsz
Short name:
Btz
<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:CASC3
Synonyms:MLN511 Publication
<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 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000108349.14

Human Gene Nomenclature Database

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HGNCi
HGNC:17040 CASC3

Online Mendelian Inheritance in Man (OMIM)

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MIMi
606504 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O15234

<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 projection, Cytoplasm, Nucleus

<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>Mutagenesisi181Y → A: Does not affect EJC formation. 1 Publication1
Mutagenesisi184 – 185RK → AA: Does not affect EJC formation. 1 Publication2
Mutagenesisi188F → A: Does not affect EJC formation. 1 Publication1
Mutagenesisi218W → A: Abolishes interaction with EIF4A3, EJC formation and localization in nucleus speckles. 1 Publication1
Mutagenesisi220 – 221HD → AA: Abolishes interaction with EIF4A3, EJC formation and localization in nucleus speckles. 1 Publication2
Mutagenesisi240 – 241YG → AA: Abolishes interaction with EIF4A3, EJC formation and localization in nucleus speckles. 1 Publication2

Organism-specific databases

DisGeNET

More...
DisGeNETi
22794

Open Targets

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OpenTargetsi
ENSG00000108349

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA134948596

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CASC3

<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_00000893241 – 703Protein CASC3Add BLAST703

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 residuei35PhosphoserineBy similarity1
Modified residuei117PhosphoserineCombined sources1
Modified residuei148PhosphoserineCombined sources1
Modified residuei265PhosphoserineCombined sources1
Modified residuei357PhosphothreonineCombined sources1
Modified residuei363PhosphoserineCombined sources1
Modified residuei373PhosphoserineCombined sources1
Modified residuei477PhosphoserineCombined 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

ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination.1 Publication
Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation.1 Publication

Keywords - PTMi

ADP-ribosylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O15234

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O15234

MaxQB - The MaxQuant DataBase

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MaxQBi
O15234

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

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PaxDbi
O15234

PeptideAtlas

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PeptideAtlasi
O15234

PRoteomics IDEntifications database

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PRIDEi
O15234

ProteomicsDB human proteome resource

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ProteomicsDBi
48528

Consortium for Top Down Proteomics

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TopDownProteomicsi
O15234

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O15234

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

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PhosphoSitePlusi
O15234

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
O15234

<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

Widely expressed. Overexpressed in breast cancers and metastasis, as well as in gastric cancers.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000108349 Expressed in 233 organ(s), highest expression level in middle frontal gyrus

CleanEx database of gene expression profiles

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CleanExi
HS_CASC3

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O15234 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O15234 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA024592
HPA050262

<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

Component of the mRNA splicing-dependent exon junction complex (EJC), which contains at least CASC3, EIF4A3, MAGOH, NXF1 and RBM8A/Y14 (PubMed:15166247, PubMed:16170325, PubMed:16314458, PubMed:16923391, PubMed:16931718, PubMed:19033377). Forms homooligomers (By similarity). Interacts with STAU in an RNA-dependent manner (By similarity).By similarity6 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
116475, 60 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1941 Exon junction core complex, MAGOH variant
CPX-682 Exon junction core complex, MAGOHB variant

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O15234

Database of interacting proteins

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DIPi
DIP-33288N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
O15234

Protein interaction database and analysis system

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IntActi
O15234, 33 interactors

Molecular INTeraction database

More...
MINTi
O15234

STRING: functional protein association networks

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STRINGi
9606.ENSP00000264645

<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

1703
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
2HYIX-ray2.30D/J170-246[»]
2J0QX-ray3.20I/T137-286[»]
2J0SX-ray2.21T137-286[»]
2J0UX-ray3.00T137-250[»]
2XB2X-ray3.40S/T137-286[»]
3EX7X-ray2.30D/I138-283[»]
5XJCelectron microscopy3.60x1-703[»]
5YZGelectron microscopy4.10x1-703[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O15234

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

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SMRi
O15234

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
O15234

<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

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>Regioni137 – 283Necessary for RNA-binding, interaction with MAGOH and localization in nucleus speckles1 PublicationAdd BLAST147
Regioni137 – 283Sufficient to form the EJCAdd BLAST147
Regioni377 – 703Necessary for localization in cytoplasmic stress granulesAdd BLAST327

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili95 – 131Sequence analysisAdd BLAST37

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi204 – 210Nuclear localization signal 1Sequence analysis7
Motifi254 – 262Nuclear localization signal 2Sequence analysis9
Motifi462 – 466Nuclear export signal5

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 biasi41 – 46Poly-Gly6
Compositional biasi392 – 395Poly-Pro4
Compositional biasi425 – 428Poly-Pro4
Compositional biasi643 – 648Poly-Pro6
Compositional biasi692 – 695Poly-Pro4

<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 coiled coil domain may be involved in oligomerization.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the CASC3 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4264 Eukaryota
ENOG410ZW5Y LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000006930

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000069997

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG050799

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O15234

KEGG Orthology (KO)

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KOi
K14323

Identification of Orthologs from Complete Genome Data

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OMAi
PAKTGNW

Database of Orthologous Groups

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OrthoDBi
486761at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O15234

TreeFam database of animal gene trees

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TreeFami
TF329663

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR018545 Btz_dom
IPR028544 CASC3

The PANTHER Classification System

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PANTHERi
PTHR13434 PTHR13434, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF09405 Btz, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01044 Btz, 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 3 potential isoforms that are computationally mapped.Show allAlign All

O15234-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADRRRQRAS QDTEDEESGA SGSDSGGSPL RGGGSCSGSA GGGGSGSLPS
60 70 80 90 100
QRGGRTGALH LRRVESGGAK SAEESECESE DGIEGDAVLS DYESAEDSEG
110 120 130 140 150
EEGEYSEEEN SKVELKSEAN DAVNSSTKEE KGEEKPDTKS TVTGERQSGD
160 170 180 190 200
GQESTEPVEN KVGKKGPKHL DDDEDRKNPA YIPRKGLFFE HDLRGQTQEE
210 220 230 240 250
EVRPKGRQRK LWKDEGRWEH DKFREDEQAP KSRQELIALY GYDIRSAHNP
260 270 280 290 300
DDIKPRRIRK PRYGSPPQRD PNWNGERLNK SHRHQGLGGT LPPRTFINRN
310 320 330 340 350
AAGTGRMSAP RNYSRSGGFK EGRAGFRPVE AGGQHGGRSG ETVKHEISYR
360 370 380 390 400
SRRLEQTSVR DPSPEADAPV LGSPEKEEAA SEPPAAAPDA APPPPDRPIE
410 420 430 440 450
KKSYSRARRT RTKVGDAVKL AEEVPPPPEG LIPAPPVPET TPTPPTKTGT
460 470 480 490 500
WEAPVDSSTS GLEQDVAQLN IAEQNWSPGQ PSFLQPRELR GMPNHIHMGA
510 520 530 540 550
GPPPQFNRME EMGVQGGRAK RYSSQRQRPV PEPPAPPVHI SIMEGHYYDP
560 570 580 590 600
LQFQGPIYTH GDSPAPLPPQ GMLVQPGMNL PHPGLHPHQT PAPLPNPGLY
610 620 630 640 650
PPPVSMSPGQ PPPQQLLAPT YFSAPGVMNF GNPSYPYAPG ALPPPPPPHL
660 670 680 690 700
YPNTQAPSQV YGGVTYYNPA QQQVQPKPSP PRRTPQPVTI KPPPPEVVSR

GSS
Length:703
Mass (Da):76,278
Last modified:August 14, 2001 - 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:i642A4C01C8DD3BE0
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3KSY7J3KSY7_HUMAN
Protein CASC3
CASC3
223Annotation 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>
J3QSC4J3QSC4_HUMAN
Protein CASC3
CASC3
129Annotation 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>
K7EQ38K7EQ38_HUMAN
Protein CASC3
CASC3
66Annotation 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>

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

More...
DDBJi
Links Updated
X80199 mRNA Translation: CAC27699.1
AK292425 mRNA Translation: BAF85114.1
AC068669 Genomic DNA No translation available.
BC044656 mRNA Translation: AAH44656.1
BC050526 mRNA Translation: AAH50526.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS11362.1

NCBI Reference Sequences

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RefSeqi
NP_031385.2, NM_007359.4
XP_005257220.1, XM_005257163.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.743287

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000264645; ENSP00000264645; ENSG00000108349

Database of genes from NCBI RefSeq genomes

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GeneIDi
22794

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:22794

UCSC genome browser

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UCSCi
uc002hue.4 human

<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
X80199 mRNA Translation: CAC27699.1
AK292425 mRNA Translation: BAF85114.1
AC068669 Genomic DNA No translation available.
BC044656 mRNA Translation: AAH44656.1
BC050526 mRNA Translation: AAH50526.1
CCDSiCCDS11362.1
RefSeqiNP_031385.2, NM_007359.4
XP_005257220.1, XM_005257163.1
UniGeneiHs.743287

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HYIX-ray2.30D/J170-246[»]
2J0QX-ray3.20I/T137-286[»]
2J0SX-ray2.21T137-286[»]
2J0UX-ray3.00T137-250[»]
2XB2X-ray3.40S/T137-286[»]
3EX7X-ray2.30D/I138-283[»]
5XJCelectron microscopy3.60x1-703[»]
5YZGelectron microscopy4.10x1-703[»]
ProteinModelPortaliO15234
SMRiO15234
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116475, 60 interactors
ComplexPortaliCPX-1941 Exon junction core complex, MAGOH variant
CPX-682 Exon junction core complex, MAGOHB variant
CORUMiO15234
DIPiDIP-33288N
ELMiO15234
IntActiO15234, 33 interactors
MINTiO15234
STRINGi9606.ENSP00000264645

Protein family/group databases

TCDBi3.A.18.1.1 the nuclear mrna exporter (mrna-e) family

PTM databases

iPTMnetiO15234
PhosphoSitePlusiO15234

Polymorphism and mutation databases

BioMutaiCASC3

Proteomic databases

EPDiO15234
jPOSTiO15234
MaxQBiO15234
PaxDbiO15234
PeptideAtlasiO15234
PRIDEiO15234
ProteomicsDBi48528
TopDownProteomicsiO15234

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264645; ENSP00000264645; ENSG00000108349
GeneIDi22794
KEGGihsa:22794
UCSCiuc002hue.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
22794
DisGeNETi22794
EuPathDBiHostDB:ENSG00000108349.14

GeneCards: human genes, protein and diseases

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GeneCardsi
CASC3
HGNCiHGNC:17040 CASC3
HPAiHPA024592
HPA050262
MIMi606504 gene
neXtProtiNX_O15234
OpenTargetsiENSG00000108349
PharmGKBiPA134948596

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG4264 Eukaryota
ENOG410ZW5Y LUCA
GeneTreeiENSGT00390000006930
HOGENOMiHOG000069997
HOVERGENiHBG050799
InParanoidiO15234
KOiK14323
OMAiPAKTGNW
OrthoDBi486761at2759
PhylomeDBiO15234
TreeFamiTF329663

Enzyme and pathway databases

ReactomeiR-HSA-109688 Cleavage of Growing Transcript in the Termination Region
R-HSA-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Miscellaneous databases

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

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ChiTaRSi
CASC3 human
EvolutionaryTraceiO15234

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
CASC3

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

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GenomeRNAii
22794
PMAP-CutDBiO15234

Protein Ontology

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PROi
PR:O15234

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000108349 Expressed in 233 organ(s), highest expression level in middle frontal gyrus
CleanExiHS_CASC3
ExpressionAtlasiO15234 baseline and differential
GenevisibleiO15234 HS

Family and domain databases

InterProiView protein in InterPro
IPR018545 Btz_dom
IPR028544 CASC3
PANTHERiPTHR13434 PTHR13434, 1 hit
PfamiView protein in Pfam
PF09405 Btz, 1 hit
SMARTiView protein in SMART
SM01044 Btz, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiCASC3_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: O15234
Secondary accession number(s): A8K8R0
<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: May 30, 2000
Last sequence update: August 14, 2001
Last modified: January 16, 2019
This is version 177 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. SIMILARITY comments
    Index of protein domains and families
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
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