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UniProtKB - Q9H8V3 (ECT2_HUMAN)

Entry version 159 (13 Feb 2019)
Sequence version 4 (16 Nov 2011)
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Protein

Protein ECT2

Gene

ECT2

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

Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)-induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells, thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death.14 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

  • GTPase activator activity Source: UniProtKB
  • guanyl-nucleotide exchange factor activity Source: Reactome
  • protein homodimerization activity Source: UniProtKB
  • Rho guanyl-nucleotide exchange factor activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 functionGuanine-nucleotide releasing factor
Biological processCell cycle, Cell division, Differentiation, Neurogenesis, Protein transport, Transport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-193648 NRAGE signals death through JNK
R-HSA-194840 Rho GTPase cycle
R-HSA-416482 G alpha (12/13) signalling events

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

More...SignaLinki		Q9H8V3

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q9H8V3

<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 ECT2
Alternative name(s):
Epithelial cell-transforming sequence 2 oncogene
<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:ECT2
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000114346.13

Human Gene Nomenclature Database

More...HGNCi		HGNC:3155 ECT2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		600586 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9H8V3

<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

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Nucleus, Tight junction

<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>Mutagenesisi184T → A: Inhibits interaction with RACGAP1. Abolishes targeting to the central spindle. 1 Publication1
Mutagenesisi226K → A: Inhibits interaction with RACGAP1. Abolishes targeting to the central spindle. 1 Publication1
Mutagenesisi336W → R: Inhibits homodimerization. Increases binding with RhoA and GEF activity. 1 Publication1
Mutagenesisi359T → A: Inhibits its phosphorylation and anchorage-independent growth and invasion in cancer cells. Does not inhibit its GEF activity. 1 Publication1
Mutagenesisi373T → A: Does not inhibit its Rho exchange activity. Increases interaction with RACGAP1. Does not inhibit anchorage-independent growth and invasion in cancer cells. 2 Publications1
Mutagenesisi373T → D: Does not inhibit subcellular localization or homodimerization. Enhances its Rho exchange activity. 2 Publications1
Mutagenesisi379 – 381KRR → AAA: Shows both nuclear and cytoplasmic localization and activates its transforming activity. 1 Publication3
Mutagenesisi402 – 404RKR → AKA: Shows both nuclear and cytoplasmic localization and activates its transforming activity. 1 Publication3
Mutagenesisi444T → A: Diminishes its phosphorylation status. Reduces its interaction with PLK1 and Rho exchange activity. Does not change its subcellular localization. Does not inhibit anchorage-independent growth and invasion in cancer cells. 1 Publication1
Mutagenesisi444T → D: Does not reduce its interaction with PLK1, change its subcellular localization and Rho exchange activity. 1 Publication1
Mutagenesisi596 – 599PVQR → AAAA: Inhibits activation of the transforming activity. 1 Publication4
Mutagenesisi846T → A: Diminishes its phosphorylation status. 1 Publication1

Keywords - Diseasei

Oncogene

Organism-specific databases

DisGeNET

More...DisGeNETi		1894

Open Targets

More...OpenTargetsi		ENSG00000114346

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27600

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ECT2

Domain mapping of disease mutations (DMDM)

More...DMDMi		357529579

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00000809382 – 914Protein ECT2Add BLAST913

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 residuei2N-acetylalanineCombined sources1
Modified residuei359Phosphothreonine; by PKC/PRKCICombined sources1 Publication1
Modified residuei367PhosphoserineCombined sources1
Modified residuei370PhosphoserineCombined sources1
Modified residuei373Phosphothreonine; by CDK1Combined sources1 Publication1
Modified residuei376PhosphoserineCombined sources1
Modified residuei444Phosphothreonine; by CDK11 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei716PhosphoserineCombined sources1
Modified residuei842PhosphoserineCombined sources1
Modified residuei846Phosphothreonine; by CDK1Combined sources1
Modified residuei861PhosphoserineCombined sources1
Modified residuei866PhosphoserineCombined 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 by PLK1 in vitro. Hyperphosphorylated during the G2 phase of the cell cycle. Phosphorylation at Thr-373 occurs during the G2/M phase, relieves its auto-inhibition status and stimulates its GEF activity. Phosphorylation at Thr-444 in G2/M phase is required for subsequent binding with PLK1 and Rho exchange activation. Dephosphorylated at the time of cytokinesis. Phosphorylation at Thr-359 is required for its transformation activity in cancer cells.4 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9H8V3

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9H8V3

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9H8V3

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

More...PaxDbi		Q9H8V3

PeptideAtlas

More...PeptideAtlasi		Q9H8V3

PRoteomics IDEntifications database

More...PRIDEi		Q9H8V3

ProteomicsDB human proteome resource

More...ProteomicsDBi		81243
81244 [Q9H8V3-2]
81245 [Q9H8V3-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9H8V3

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

More...PhosphoSitePlusi		Q9H8V3

<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

Expressed in lung epithelial cells (at protein level). Expressed in squamous cell carcinoma, primary non-small cell lung cancer tumors and lung adenocarcinoma.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by calcium in cells forming cell-cell contact sites. Up-regulated by DNA damaging agents like H2O2 or ionizing radiation (IR).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000114346 Expressed in 193 organ(s), highest expression level in secondary oocyte

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9H8V3 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9H8V3 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA036363
HPA053261

<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 NR1I3 (By similarity). Homodimer. Homooligomer. Found in the centralspindlin complex. Interacts (Thr-359 phosphorylated form) with PARD6A; the interaction is observed in cancer cells. Interacts (Thr-359 phosphorylated form) with PRKCI; the interaction is observed in cancer cells. Interacts with PKP4; the interaction is observed at the midbody. Interacts with RACGAP1; the interaction is direct, occurs in a microtubule-dependent manner, is inhibited in metaphase by phosphorylation of ECT2 on Thr-373 and is stimulated in early anaphase by dephosphorylation of ECT2 probably on Thr-373 through CDK1 activity. Interacts with PLK1; the interaction is stimulated upon its phosphorylation on Thr-444. Associates with RACGAP1 at anaphase and during cytokinesis. Interacts with KIF23, PARD3, PARD6A, PARD6B and PRKCQ.By similarity10 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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108223, 157 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9H8V3

Database of interacting proteins

More...DIPi		DIP-47496N

Protein interaction database and analysis system

More...IntActi		Q9H8V3, 21 interactors

Molecular INTeraction database

More...MINTi		Q9H8V3

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000232458

<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

1914
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3L46X-ray1.48A/B268-361[»]
4N40X-ray3.11A45-356[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q9H8V3

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

More...SMRi		Q9H8V3

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9H8V3

<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>Domaini171 – 260BRCT 1PROSITE-ProRule annotationAdd BLAST90
Domaini266 – 354BRCT 2PROSITE-ProRule annotationAdd BLAST89
Domaini452 – 641DHPROSITE-ProRule annotationAdd BLAST190
Domaini675 – 794PHAdd BLAST120

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>Motifi378 – 382Nuclear localization signal5
Motifi401 – 405Nuclear localization signal5

<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 BRCT domain 1 and 2 are required for the intramolecular interaction, but not for the intermolecular oligomerization. The BRCT domains negatively inhibit its GEF activity in interphase cells. The same BRCT domains may act as a positive regulatory motif for the completion of cytokinesis after the breakdown of nuclear membrane during mitosis.

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3524 Eukaryota
ENOG410XRV9 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156299

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000012876

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG005563

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9H8V3

KEGG Orthology (KO)

More...KOi		K20704

Identification of Orthologs from Complete Genome Data

More...OMAi		FKSPHGH

Database of Orthologous Groups

More...OrthoDBi		557169at2759

TreeFam database of animal gene trees

More...TreeFami		TF101161

Family and domain databases

Conserved Domains Database

More...CDDi		cd00027 BRCT, 2 hits
cd00160 RhoGEF, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.900.10, 1 hit
2.30.29.30, 1 hit
3.40.50.10190, 3 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR035899 DBL_dom_sf
IPR000219 DH-domain
IPR026817 Ect2
IPR001331 GDS_CDC24_CS
IPR011993 PH-like_dom_sf

The PANTHER Classification System

More...PANTHERi		PTHR16777 PTHR16777, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00533 BRCT, 1 hit
PF12738 PTCB-BRCT, 1 hit
PF00621 RhoGEF, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00292 BRCT, 2 hits
SM00325 RhoGEF, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48065 SSF48065, 1 hit
SSF52113 SSF52113, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50172 BRCT, 2 hits
PS00741 DH_1, 1 hit
PS50010 DH_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>Sequences (4+)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 <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 4 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9H8V3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
MAENSVLTST TGRTSLADSS IFDSKVTEIS KENLLIGSTS YVEEEMPQIE 
        60         70         80         90        100
TRVILVQEAG KQEELIKALK TIKIMEVPVI KIKESCPGKS DEKLIKSVIN 
       110        120        130        140        150
MDIKVGFVKM ESVEEFEGLD SPEFENVFVV TDFQDSVFND LYKADCRVIG 
       160        170        180        190        200
PPVVLNCSQK GEPLPFSCRP LYCTSMMNLV LCFTGFRKKE ELVRLVTLVH 
       210        220        230        240        250
HMGGVIRKDF NSKVTHLVAN CTQGEKFRVA VSLGTPIMKP EWIYKAWERR 
       260        270        280        290        300
NEQDFYAAVD DFRNEFKVPP FQDCILSFLG FSDEEKTNME EMTEMQGGKY 
       310        320        330        340        350
LPLGDERCTH LVVEENIVKD LPFEPSKKLY VVKQEWFWGS IQMDARAGET 
       360        370        380        390        400
MYLYEKANTP ELKKSVSMLS LNTPNSNRKR RRLKETLAQL SRETDVSPFP 
       410        420        430        440        450
PRKRPSAEHS LSIGSLLDIS NTPESSINYG DTPKSCTKSS KSSTPVPSKQ 
       460        470        480        490        500
SARWQVAKEL YQTESNYVNI LATIIQLFQV PLEEEGQRGG PILAPEEIKT 
       510        520        530        540        550
IFGSIPDIFD VHTKIKDDLE DLIVNWDESK SIGDIFLKYS KDLVKTYPPF 
       560        570        580        590        600
VNFFEMSKET IIKCEKQKPR FHAFLKINQA KPECGRQSLV ELLIRPVQRL 
       610        620        630        640        650
PSVALLLNDL KKHTADENPD KSTLEKAIGS LKEVMTHINE DKRKTEAQKQ 
       660        670        680        690        700
IFDVVYEVDG CPANLLSSHR SLVQRVETIS LGEHPCDRGE QVTLFLFNDC 
       710        720        730        740        750
LEIARKRHKV IGTFRSPHGQ TRPPASLKHI HLMPLSQIKK VLDIRETEDC 
       760        770        780        790        800
HNAFALLVRP PTEQANVLLS FQMTSDELPK ENWLKMLCRH VANTICKADA 
       810        820        830        840        850
ENLIYTADPE SFEVNTKDMD STLSRASRAI KKTSKKVTRA FSFSKTPKRA 
       860        870        880        890        900
LRRALMTSHG SVEGRSPSSN DKHVMSRLSS TSSLAGIPSP SLVSLPSFFE 
       910 
RRSHTLSRST THLI
Length:914
Mass (Da):103,505
Last modified:November 16, 2011 - v4
<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:iF40FC4F982FB8C78
GO
Isoform 2 (identifier: Q9H8V3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     44-44: Missing.
     71-101: Missing.

Show »
Length:882
Mass (Da):99,921
Checksum:iAAD4483A503D086C
GO
Isoform 3 (identifier: Q9H8V3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     886-914: GIPSPSLVSLPSFFERRSHTLSRSTTHLI → ITHSVSTSNV...SKSSLTFVKN

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.
Show »
Length:958
Mass (Da):108,529
Checksum:iF505EBBF2E1BBE23
GO
Isoform 4 (identifier: Q9H8V3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     71-101: Missing.

Show »
Length:883
Mass (Da):100,051
Checksum:iBAEFC693495C50E1
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 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7C3G1H7C3G1_HUMAN
Protein ECT2
ECT2
209Annotation 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>
C9JDB4C9JDB4_HUMAN
Protein ECT2
ECT2
204Annotation 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>
C9J1C4C9J1C4_HUMAN
Protein ECT2
ECT2
159Annotation 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>
H7C103H7C103_HUMAN
Protein ECT2
ECT2
298Annotation 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>
C9JTI2C9JTI2_HUMAN
Protein ECT2
ECT2
150Annotation 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>
C9JDV9C9JDV9_HUMAN
Protein ECT2
ECT2
110Annotation 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>
C9J0L6C9J0L6_HUMAN
Protein ECT2
ECT2
106Annotation 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>
C9JB41C9JB41_HUMAN
Protein ECT2
ECT2
18Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA91624 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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 conflicti66I → T in BAB14498 (PubMed:16641997).Curated1
Sequence conflicti276L → F in BAB14498 (PubMed:16641997).Curated1
Sequence conflicti393E → D in BAB14498 (PubMed:16641997).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_04706415S → T. Corresponds to variant dbSNP:rs34703432Ensembl.1
Natural variantiVAR_035975833T → P in a breast cancer sample; somatic mutation. 1 Publication1

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_04197644Missing in isoform 2. 4 Publications1
Alternative sequenceiVSP_04197771 – 101Missing in isoform 2 and isoform 4. 4 PublicationsAdd BLAST31
Alternative sequenceiVSP_041978886 – 914GIPSP…TTHLI → ITHSVSTSNVIGFTKHVYVQ RLNSTGGRSQYSWFQSVRHS AFRASFSEILEGNTDFSNFK KVLSKSSLTFVKN in isoform 3. 1 PublicationAdd BLAST29

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AY376439 mRNA Translation: AAQ83675.1
DQ847274 mRNA Translation: ABH10140.1
AK001323 mRNA Translation: BAA91624.1 Different initiation.
AK023267 mRNA Translation: BAB14498.1
AK314581 mRNA Translation: BAG37157.1
AC108667 Genomic DNA No translation available.
BC112086 mRNA Translation: AAI12087.1
AL137710 mRNA Translation: CAB70886.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS3220.1 [Q9H8V3-4]
CCDS58860.1 [Q9H8V3-1]
CCDS87168.1 [Q9H8V3-2]

NCBI Reference Sequences

More...RefSeqi		NP_001245244.1, NM_001258315.1 [Q9H8V3-1]
NP_001245245.1, NM_001258316.1 [Q9H8V3-4]
NP_060568.3, NM_018098.5 [Q9H8V3-4]
XP_011510816.1, XM_011512514.2 [Q9H8V3-3]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.518299

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000232458; ENSP00000232458; ENSG00000114346 [Q9H8V3-4]
ENST00000392692; ENSP00000376457; ENSG00000114346 [Q9H8V3-1]
ENST00000417960; ENSP00000415876; ENSG00000114346 [Q9H8V3-2]
ENST00000441497; ENSP00000412259; ENSG00000114346 [Q9H8V3-4]
ENST00000540509; ENSP00000443160; ENSG00000114346 [Q9H8V3-4]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1894

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:1894

UCSC genome browser

More...UCSCi		uc003fih.4 human [Q9H8V3-1]

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
AY376439 mRNA Translation: AAQ83675.1
DQ847274 mRNA Translation: ABH10140.1
AK001323 mRNA Translation: BAA91624.1 Different initiation.
AK023267 mRNA Translation: BAB14498.1
AK314581 mRNA Translation: BAG37157.1
AC108667 Genomic DNA No translation available.
BC112086 mRNA Translation: AAI12087.1
AL137710 mRNA Translation: CAB70886.1
CCDSiCCDS3220.1 [Q9H8V3-4]
CCDS58860.1 [Q9H8V3-1]
CCDS87168.1 [Q9H8V3-2]
RefSeqiNP_001245244.1, NM_001258315.1 [Q9H8V3-1]
NP_001245245.1, NM_001258316.1 [Q9H8V3-4]
NP_060568.3, NM_018098.5 [Q9H8V3-4]
XP_011510816.1, XM_011512514.2 [Q9H8V3-3]
UniGeneiHs.518299

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3L46X-ray1.48A/B268-361[»]
4N40X-ray3.11A45-356[»]
ProteinModelPortaliQ9H8V3
SMRiQ9H8V3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108223, 157 interactors
CORUMiQ9H8V3
DIPiDIP-47496N
IntActiQ9H8V3, 21 interactors
MINTiQ9H8V3
STRINGi9606.ENSP00000232458

PTM databases

iPTMnetiQ9H8V3
PhosphoSitePlusiQ9H8V3

Polymorphism and mutation databases

BioMutaiECT2
DMDMi357529579

Proteomic databases

EPDiQ9H8V3
jPOSTiQ9H8V3
MaxQBiQ9H8V3
PaxDbiQ9H8V3
PeptideAtlasiQ9H8V3
PRIDEiQ9H8V3
ProteomicsDBi81243
81244 [Q9H8V3-2]
81245 [Q9H8V3-3]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000232458; ENSP00000232458; ENSG00000114346 [Q9H8V3-4]
ENST00000392692; ENSP00000376457; ENSG00000114346 [Q9H8V3-1]
ENST00000417960; ENSP00000415876; ENSG00000114346 [Q9H8V3-2]
ENST00000441497; ENSP00000412259; ENSG00000114346 [Q9H8V3-4]
ENST00000540509; ENSP00000443160; ENSG00000114346 [Q9H8V3-4]
GeneIDi1894
KEGGihsa:1894
UCSCiuc003fih.4 human [Q9H8V3-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1894
DisGeNETi1894
EuPathDBiHostDB:ENSG00000114346.13

GeneCards: human genes, protein and diseases

More...GeneCardsi		ECT2
HGNCiHGNC:3155 ECT2
HPAiHPA036363
HPA053261
MIMi600586 gene
neXtProtiNX_Q9H8V3
OpenTargetsiENSG00000114346
PharmGKBiPA27600

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3524 Eukaryota
ENOG410XRV9 LUCA
GeneTreeiENSGT00940000156299
HOGENOMiHOG000012876
HOVERGENiHBG005563
InParanoidiQ9H8V3
KOiK20704
OMAiFKSPHGH
OrthoDBi557169at2759
TreeFamiTF101161

Enzyme and pathway databases

ReactomeiR-HSA-193648 NRAGE signals death through JNK
R-HSA-194840 Rho GTPase cycle
R-HSA-416482 G alpha (12/13) signalling events
SignaLinkiQ9H8V3
SIGNORiQ9H8V3

Miscellaneous databases

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

More...ChiTaRSi		ECT2 human
EvolutionaryTraceiQ9H8V3

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		ECT2

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

More...GenomeRNAii		1894

Protein Ontology

More...PROi		PR:Q9H8V3

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000114346 Expressed in 193 organ(s), highest expression level in secondary oocyte
ExpressionAtlasiQ9H8V3 baseline and differential
GenevisibleiQ9H8V3 HS

Family and domain databases

CDDicd00027 BRCT, 2 hits
cd00160 RhoGEF, 1 hit
Gene3Di1.20.900.10, 1 hit
2.30.29.30, 1 hit
3.40.50.10190, 3 hits
InterProiView protein in InterPro
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR035899 DBL_dom_sf
IPR000219 DH-domain
IPR026817 Ect2
IPR001331 GDS_CDC24_CS
IPR011993 PH-like_dom_sf
PANTHERiPTHR16777 PTHR16777, 1 hit
PfamiView protein in Pfam
PF00533 BRCT, 1 hit
PF12738 PTCB-BRCT, 1 hit
PF00621 RhoGEF, 1 hit
SMARTiView protein in SMART
SM00292 BRCT, 2 hits
SM00325 RhoGEF, 1 hit
SUPFAMiSSF48065 SSF48065, 1 hit
SSF52113 SSF52113, 2 hits
PROSITEiView protein in PROSITE
PS50172 BRCT, 2 hits
PS00741 DH_1, 1 hit
PS50010 DH_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 nameiECT2_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: Q9H8V3
Secondary accession number(s): Q0MT80
, Q2M269, Q6U836, Q9NSV8, Q9NVW9
<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: September 26, 2001
Last sequence update: November 16, 2011
Last modified: February 13, 2019
This is version 159 of the entry and version 4 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 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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