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Q9H8V3

- ECT2_HUMAN

UniProt

Q9H8V3 - ECT2_HUMAN

Protein

Protein ECT2

Gene

ECT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 4 (16 Nov 2011)
      Previous versions | rss
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    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

    GO - Molecular functioni

    1. GTPase activator activity Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB
    4. Rho guanyl-nucleotide exchange factor activity Source: UniProtKB
    5. signal transducer activity Source: UniProtKB

    GO - Biological processi

    1. activation of protein kinase activity Source: UniProtKB
    2. activation of Rac GTPase activity Source: UniProtKB
    3. activation of Rho GTPase activity Source: UniProtKB
    4. apoptotic signaling pathway Source: Reactome
    5. cell morphogenesis Source: Ensembl
    6. cellular response to calcium ion Source: UniProtKB
    7. cellular response to hydrogen peroxide Source: UniProtKB
    8. cellular response to ionizing radiation Source: UniProtKB
    9. cytokinesis Source: UniProtKB
    10. neurotrophin TRK receptor signaling pathway Source: Reactome
    11. positive regulation of apoptotic process Source: UniProtKB
    12. positive regulation of Cdc42 GTPase activity Source: UniProtKB
    13. positive regulation of cytokinesis Source: UniProtKB
    14. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    15. positive regulation of neuron differentiation Source: UniProtKB
    16. positive regulation of protein import into nucleus Source: UniProtKB
    17. positive regulation of Rho GTPase activity Source: UniProtKB
    18. protein homooligomerization Source: UniProtKB
    19. protein transport Source: UniProtKB-KW
    20. regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
    21. regulation of protein kinase activity Source: UniProtKB
    22. regulation of small GTPase mediated signal transduction Source: Reactome
    23. small GTPase mediated signal transduction Source: Reactome
    24. tight junction assembly Source: UniProtKB

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Keywords - Biological processi

    Cell cycle, Cell division, Differentiation, Neurogenesis, Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_13638. NRAGE signals death through JNK.
    REACT_18407. G alpha (12/13) signalling events.
    SignaLinkiQ9H8V3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein ECT2
    Alternative name(s):
    Epithelial cell-transforming sequence 2 oncogene
    Gene namesi
    Name:ECT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:3155. ECT2.

    Subcellular locationi

    Nucleus. Cytoplasm. Cytoplasmcytoskeletonspindle. Cleavage furrow. Midbody. Cell junction. Cell junctiontight junction
    Note: Sequestered within the nucleus during interphase. Dispersed throughout the cytoplasm upon breakdown of the nuclear envelope during mitosis. Colocalizes with the centralspindlin complex to the mitotic spindles during anaphase/metaphase, the cleavage furrow during telophase and at the midbody at the end of cytokinesis. Colocalized with RhoA at the midbody. Its subcellular localization to tight junction is increased by calcium. Localized predominantly in the cytoplasm of numerous carcinoma cells.

    GO - Cellular componenti

    1. cell-cell junction Source: UniProtKB
    2. centralspindlin complex Source: UniProtKB
    3. cleavage furrow Source: UniProtKB
    4. cytoplasm Source: UniProtKB
    5. cytosol Source: Reactome
    6. midbody Source: UniProtKB
    7. mitotic spindle Source: UniProtKB
    8. nucleus Source: UniProtKB
    9. tight junction Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton, Nucleus, Tight junction

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi184 – 1841T → A: Inhibits interaction with RACGAP1. Abolishes targeting to the central spindle. 2 Publications
    Mutagenesisi226 – 2261K → A: Inhibits interaction with RACGAP1. Abolishes targeting to the central spindle. 2 Publications
    Mutagenesisi336 – 3361W → R: Inhibits homodimerization. Increases binding with RhoA and GEF activity. 2 Publications
    Mutagenesisi359 – 3591T → A: Inhibits its phosphorylation and anchorage-independent growth and invasion in cancer cells. Does not inhibit its GEF activity. 2 Publications
    Mutagenesisi373 – 3731T → A: Does not inhibit its Rho exchange activity. Increases interaction with RACGAP1. Does not inhibit anchorage-independent growth and invasion in cancer cells. 3 Publications
    Mutagenesisi373 – 3731T → D: Does not inhibit subcellular localization or homodimerization. Enhances its Rho exchange activity. 3 Publications
    Mutagenesisi379 – 3813KRR → AAA: Shows both nuclear and cytoplasmic localization and activates its transforming activity. 1 Publication
    Mutagenesisi402 – 4043RKR → AKA: Shows both nuclear and cytoplasmic localization and activates its transforming activity. 1 Publication
    Mutagenesisi444 – 4441T → 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. 2 Publications
    Mutagenesisi444 – 4441T → D: Does not reduce its interaction with PLK1, change its subcellular localization and Rho exchange activity. 2 Publications
    Mutagenesisi596 – 5994PVQR → AAAA: Inhibits activation of the transforming activity. 1 Publication
    Mutagenesisi846 – 8461T → A: Diminishes its phosphorylation status. 2 Publications

    Keywords - Diseasei

    Oncogene

    Organism-specific databases

    PharmGKBiPA27600.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 914913Protein ECT2PRO_0000080938Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei359 – 3591Phosphothreonine; by PKC/PRKCI4 Publications
    Modified residuei367 – 3671Phosphoserine2 Publications
    Modified residuei370 – 3701Phosphoserine2 Publications
    Modified residuei373 – 3731Phosphothreonine; by CDK13 Publications
    Modified residuei376 – 3761Phosphoserine2 Publications
    Modified residuei444 – 4441Phosphothreonine; by CDK12 Publications
    Modified residuei842 – 8421Phosphoserine2 Publications
    Modified residuei846 – 8461Phosphothreonine; by CDK12 Publications

    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.7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H8V3.
    PaxDbiQ9H8V3.
    PRIDEiQ9H8V3.

    PTM databases

    PhosphoSiteiQ9H8V3.

    Expressioni

    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

    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

    ArrayExpressiQ9H8V3.
    BgeeiQ9H8V3.
    CleanExiHS_ECT2.
    GenevestigatoriQ9H8V3.

    Organism-specific databases

    HPAiHPA053261.

    Interactioni

    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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCK1P163333EBI-1054039,EBI-389883

    Protein-protein interaction databases

    BioGridi108223. 139 interactions.
    DIPiDIP-47496N.
    IntActiQ9H8V3. 7 interactions.
    MINTiMINT-6166617.
    STRINGi9606.ENSP00000232458.

    Structurei

    Secondary structure

    1
    914
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni270 – 2734
    Beta strandi278 – 2803
    Helixi283 – 29513
    Beta strandi309 – 3135
    Turni315 – 3173
    Beta strandi318 – 3203
    Beta strandi330 – 3334
    Helixi334 – 34310
    Helixi349 – 3513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3L46X-ray1.48A/B268-361[»]
    ProteinModelPortaliQ9H8V3.
    SMRiQ9H8V3. Positions 176-361, 443-730.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H8V3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini171 – 26090BRCT 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini266 – 35489BRCT 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini452 – 641190DHPROSITE-ProRule annotationAdd
    BLAST
    Domaini675 – 794120PHAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi378 – 3825Nuclear localization signal
    Motifi401 – 4055Nuclear localization signal

    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.

    Sequence similaritiesi

    Contains 2 BRCT domains.PROSITE-ProRule annotation
    Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
    Contains 1 PH domain.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5422.
    HOGENOMiHOG000012876.
    HOVERGENiHBG005563.
    TreeFamiTF101161.

    Family and domain databases

    Gene3Di1.20.900.10. 1 hit.
    2.30.29.30. 1 hit.
    3.40.50.10190. 2 hits.
    InterProiIPR001357. BRCT_dom.
    IPR000219. DH-domain.
    IPR026817. Ect2.
    IPR001331. GDS_CDC24_CS.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PANTHERiPTHR16777. PTHR16777. 1 hit.
    PfamiPF00533. BRCT. 1 hit.
    PF12738. PTCB-BRCT. 1 hit.
    PF00621. RhoGEF. 1 hit.
    [Graphical view]
    SMARTiSM00292. BRCT. 2 hits.
    SM00233. PH. 1 hit.
    SM00325. RhoGEF. 1 hit.
    [Graphical view]
    SUPFAMiSSF48065. SSF48065. 1 hit.
    SSF52113. SSF52113. 2 hits.
    PROSITEiPS50172. BRCT. 2 hits.
    PS00741. DH_1. 1 hit.
    PS50010. DH_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    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

    MAENSVLTST TGRTSLADSS IFDSKVTEIS KENLLIGSTS YVEEEMPQIE    50
    TRVILVQEAG KQEELIKALK TIKIMEVPVI KIKESCPGKS DEKLIKSVIN 100
    MDIKVGFVKM ESVEEFEGLD SPEFENVFVV TDFQDSVFND LYKADCRVIG 150
    PPVVLNCSQK GEPLPFSCRP LYCTSMMNLV LCFTGFRKKE ELVRLVTLVH 200
    HMGGVIRKDF NSKVTHLVAN CTQGEKFRVA VSLGTPIMKP EWIYKAWERR 250
    NEQDFYAAVD DFRNEFKVPP FQDCILSFLG FSDEEKTNME EMTEMQGGKY 300
    LPLGDERCTH LVVEENIVKD LPFEPSKKLY VVKQEWFWGS IQMDARAGET 350
    MYLYEKANTP ELKKSVSMLS LNTPNSNRKR RRLKETLAQL SRETDVSPFP 400
    PRKRPSAEHS LSIGSLLDIS NTPESSINYG DTPKSCTKSS KSSTPVPSKQ 450
    SARWQVAKEL YQTESNYVNI LATIIQLFQV PLEEEGQRGG PILAPEEIKT 500
    IFGSIPDIFD VHTKIKDDLE DLIVNWDESK SIGDIFLKYS KDLVKTYPPF 550
    VNFFEMSKET IIKCEKQKPR FHAFLKINQA KPECGRQSLV ELLIRPVQRL 600
    PSVALLLNDL KKHTADENPD KSTLEKAIGS LKEVMTHINE DKRKTEAQKQ 650
    IFDVVYEVDG CPANLLSSHR SLVQRVETIS LGEHPCDRGE QVTLFLFNDC 700
    LEIARKRHKV IGTFRSPHGQ TRPPASLKHI HLMPLSQIKK VLDIRETEDC 750
    HNAFALLVRP PTEQANVLLS FQMTSDELPK ENWLKMLCRH VANTICKADA 800
    ENLIYTADPE SFEVNTKDMD STLSRASRAI KKTSKKVTRA FSFSKTPKRA 850
    LRRALMTSHG SVEGRSPSSN DKHVMSRLSS TSSLAGIPSP SLVSLPSFFE 900
    RRSHTLSRST THLI 914
    Length:914
    Mass (Da):103,505
    Last modified:November 16, 2011 - v4
    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

    Sequence cautioni

    The sequence BAA91624.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661I → T in BAB14498. (PubMed:16641997)Curated
    Sequence conflicti276 – 2761L → F in BAB14498. (PubMed:16641997)Curated
    Sequence conflicti393 – 3931E → D in BAB14498. (PubMed:16641997)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151S → T.
    Corresponds to variant rs34703432 [ dbSNP | Ensembl ].
    VAR_047064
    Natural varianti833 – 8331T → P in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035975

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei44 – 441Missing in isoform 2. 4 PublicationsVSP_041976
    Alternative sequencei71 – 10131Missing in isoform 2 and isoform 4. 4 PublicationsVSP_041977Add
    BLAST
    Alternative sequencei886 – 91429GIPSP…TTHLI → ITHSVSTSNVIGFTKHVYVQ RLNSTGGRSQYSWFQSVRHS AFRASFSEILEGNTDFSNFK KVLSKSSLTFVKN in isoform 3. 1 PublicationVSP_041978Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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]
    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_006713586.1. XM_006713523.1. [Q9H8V3-3]
    UniGeneiHs.518299.

    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. [Q9H8V3-1]
    GeneIDi1894.
    KEGGihsa:1894.
    UCSCiuc003fih.3. human. [Q9H8V3-2]
    uc003fil.2. human. [Q9H8V3-1]

    Polymorphism databases

    DMDMi357529579.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS3220.1. [Q9H8V3-4 ]
    CCDS58860.1. [Q9H8V3-1 ]
    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_006713586.1. XM_006713523.1. [Q9H8V3-3 ]
    UniGenei Hs.518299.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3L46 X-ray 1.48 A/B 268-361 [» ]
    ProteinModelPortali Q9H8V3.
    SMRi Q9H8V3. Positions 176-361, 443-730.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108223. 139 interactions.
    DIPi DIP-47496N.
    IntActi Q9H8V3. 7 interactions.
    MINTi MINT-6166617.
    STRINGi 9606.ENSP00000232458.

    PTM databases

    PhosphoSitei Q9H8V3.

    Polymorphism databases

    DMDMi 357529579.

    Proteomic databases

    MaxQBi Q9H8V3.
    PaxDbi Q9H8V3.
    PRIDEi Q9H8V3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000232458 ; ENSP00000232458 ; ENSG00000114346 . [Q9H8V3-4 ]
    ENST00000392692 ; ENSP00000376457 ; ENSG00000114346 . [Q9H8V3-1 ]
    ENST00000417960 ; ENSP00000415876 ; ENSG00000114346 . [Q9H8V3-2 ]
    ENST00000441497 ; ENSP00000412259 ; ENSG00000114346 . [Q9H8V3-4 ]
    ENST00000540509 ; ENSP00000443160 ; ENSG00000114346 . [Q9H8V3-1 ]
    GeneIDi 1894.
    KEGGi hsa:1894.
    UCSCi uc003fih.3. human. [Q9H8V3-2 ]
    uc003fil.2. human. [Q9H8V3-1 ]

    Organism-specific databases

    CTDi 1894.
    GeneCardsi GC03P172468.
    HGNCi HGNC:3155. ECT2.
    HPAi HPA053261.
    MIMi 600586. gene.
    neXtProti NX_Q9H8V3.
    PharmGKBi PA27600.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5422.
    HOGENOMi HOG000012876.
    HOVERGENi HBG005563.
    TreeFami TF101161.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_13638. NRAGE signals death through JNK.
    REACT_18407. G alpha (12/13) signalling events.
    SignaLinki Q9H8V3.

    Miscellaneous databases

    ChiTaRSi ECT2. human.
    EvolutionaryTracei Q9H8V3.
    GeneWikii ECT2.
    GenomeRNAii 1894.
    NextBioi 7725.
    PROi Q9H8V3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H8V3.
    Bgeei Q9H8V3.
    CleanExi HS_ECT2.
    Genevestigatori Q9H8V3.

    Family and domain databases

    Gene3Di 1.20.900.10. 1 hit.
    2.30.29.30. 1 hit.
    3.40.50.10190. 2 hits.
    InterProi IPR001357. BRCT_dom.
    IPR000219. DH-domain.
    IPR026817. Ect2.
    IPR001331. GDS_CDC24_CS.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    PANTHERi PTHR16777. PTHR16777. 1 hit.
    Pfami PF00533. BRCT. 1 hit.
    PF12738. PTCB-BRCT. 1 hit.
    PF00621. RhoGEF. 1 hit.
    [Graphical view ]
    SMARTi SM00292. BRCT. 2 hits.
    SM00233. PH. 1 hit.
    SM00325. RhoGEF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48065. SSF48065. 1 hit.
    SSF52113. SSF52113. 2 hits.
    PROSITEi PS50172. BRCT. 2 hits.
    PS00741. DH_1. 1 hit.
    PS50010. DH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human ECT2 is an exchange factor for Rho GTPases, phosphorylated in G2/M phases, and involved in cytokinesis."
      Tatsumoto T., Xie X., Blumenthal R., Okamoto I., Miki T.
      J. Cell Biol. 147:921-928(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    2. "Rho exchange factor ECT2 is induced by growth factors and regulates cytokinesis through the N-terminal cell cycle regulator-related domains."
      Saito S., Tatsumoto T., Lorenzi M.V., Chedid M., Kapoor V., Sakata H., Rubin J.S., Miki T.
      J. Cell. Biochem. 90:819-836(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "The armadillo protein p0071 regulates Rho signalling during cytokinesis."
      Wolf A., Keil R., Gotzl O., Mun A., Schwarze K., Lederer M., Huttelmaier S., Hatzfeld M.
      Nat. Cell Biol. 8:1432-1440(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PKP4, SUBCELLULAR LOCATION.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Teratocarcinoma and Testis.
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Lung.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 662-914 (ISOFORM 3).
      Tissue: Testis.
    8. "Deregulation and mislocalization of the cytokinesis regulator ECT2 activate the Rho signaling pathways leading to malignant transformation."
      Saito S., Liu X.F., Kamijo K., Raziuddin R., Tatsumoto T., Okamoto I., Chen X., Lee C.C., Lorenzi M.V., Ohara N., Miki T.
      J. Biol. Chem. 279:7169-7179(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HOMODIMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF 379-ARG--ARG-381; 402-ARG--ARG-404 AND 596-PRO--ARG-599.
    9. "Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity."
      Liu X.F., Ishida H., Raziuddin R., Miki T.
      Mol. Cell. Biol. 24:6665-6675(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PARD3; PARD6A; PARD6B AND PRKCQ, INDUCTION, SUBCELLULAR LOCATION.
    10. "The tandem BRCT domains of Ect2 are required for both negative and positive regulation of Ect2 in cytokinesis."
      Kim J.E., Billadeau D.D., Chen J.
      J. Biol. Chem. 280:5733-5739(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HOMODIMERIZATION, HOMOOLIGOMERIZATION, MUTAGENESIS OF TRP-336.
    11. "Ect2 and MgcRacGAP regulate the activation and function of Cdc42 in mitosis."
      Oceguera-Yanez F., Kimura K., Yasuda S., Higashida C., Kitamura T., Hiraoka Y., Haraguchi T., Narumiya S.
      J. Cell Biol. 168:221-232(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. "An ECT2-centralspindlin complex regulates the localization and function of RhoA."
      Yuce O., Piekny A., Glotzer M.
      J. Cell Biol. 170:571-582(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RACGAP1, MUTAGENESIS OF THR-373, SUBCELLULAR LOCATION.
    13. "MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis."
      Zhao W.-M., Fang G.
      Proc. Natl. Acad. Sci. U.S.A. 102:13158-13163(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RACGAP1.
    14. "Nucleotide exchange factor ECT2 regulates epithelial cell polarity."
      Liu X.F., Ohno S., Miki T.
      Cell. Signal. 18:1604-1615(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    15. "Dissecting the role of Rho-mediated signaling in contractile ring formation."
      Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T.
      Mol. Biol. Cell 17:43-55(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, INTERACTION WITH KIF23 AND RACGAP1, SUBCELLULAR LOCATION.
    16. "Cytokinesis regulator ECT2 changes its conformation through phosphorylation at Thr-341 in G2/M phase."
      Hara T., Abe M., Inoue H., Yu L.R., Veenstra T.D., Kang Y.H., Lee K.S., Miki T.
      Oncogene 25:566-578(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HOMODIMERIZATION, PHOSPHORYLATION AT THR-373, MUTAGENESIS OF THR-373.
    17. "Phosphorylation of the cytokinesis regulator ECT2 at G2/M phase stimulates association of the mitotic kinase Plk1 and accumulation of GTP-bound RhoA."
      Niiya F., Tatsumoto T., Lee K.S., Miki T.
      Oncogene 25:827-837(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-444, INTERACTION WITH PLK1, MUTAGENESIS OF THR-444 AND THR-846.
    18. "Sequential Cyk-4 binding to ECT2 and FIP3 regulates cleavage furrow ingression and abscission during cytokinesis."
      Simon G.C., Schonteich E., Wu C.C., Piekny A., Ekiert D., Yu X., Gould G.W., Glotzer M., Prekeris R.
      EMBO J. 27:1791-1803(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB11FIP3.
    19. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-370; THR-373; SER-376; SER-842 AND THR-846, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Centrosome/spindle pole-associated protein regulates cytokinesis via promoting the recruitment of MyoGEF to the central spindle."
      Asiedu M., Wu D., Matsumura F., Wei Q.
      Mol. Biol. Cell 20:1428-1440(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "Ect2 links the PKCiota-Par6alpha complex to Rac1 activation and cellular transformation."
      Justilien V., Fields A.P.
      Oncogene 28:3597-3607(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PARD6A AND PRKCI, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    23. "Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation."
      Wolfe B.A., Takaki T., Petronczki M., Glotzer M.
      PLoS Biol. 7:E1000110-E1000110(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KIF23 AND RACGAP1, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-184 AND LYS-226.
    24. "Plk1 self-organization and priming phosphorylation of HsCYK-4 at the spindle midzone regulate the onset of division in human cells."
      Burkard M.E., Maciejowski J., Rodriguez-Bravo V., Repka M., Lowery D.M., Clauser K.R., Zhang C., Shokat K.M., Carr S.A., Yaffe M.B., Jallepalli P.V.
      PLoS Biol. 7:E1000111-E1000111(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RACGAP1.
    25. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. "Oncogenic activity of Ect2 is regulated through protein kinase C iota-mediated phosphorylation."
      Justilien V., Jameison L., Der C.J., Rossman K.L., Fields A.P.
      J. Biol. Chem. 286:8149-8157(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-359, MUTAGENESIS OF THR-359, IDENTIFICATION BY MASS SPECTROMETRY.
    28. "The nuclear guanine nucleotide exchange factors Ect2 and Net1 regulate RhoB-mediated cell death after DNA damage."
      Srougi M.C., Burridge K.
      PLoS ONE 6:E17108-E17108(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    29. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    31. "Crystal structure of the second BRCT domain of epithelial cell transforming 2 (ECT2)."
      Structural genomics consortium (SGC)
      Submitted (JAN-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 268-361.
    32. Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-833.

    Entry informationi

    Entry nameiECT2_HUMAN
    AccessioniPrimary (citable) accession number: Q9H8V3
    Secondary accession number(s): Q0MT80
    , Q2M269, Q6U836, Q9NSV8, Q9NVW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: November 16, 2011
    Last modified: October 1, 2014
    This is version 118 of the entry and version 4 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3