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Q7L622

- G2E3_HUMAN

UniProt

Q7L622 - G2E3_HUMAN

Protein

G2/M phase-specific E3 ubiquitin-protein ligase

Gene

G2E3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Essential in early embryonic development to prevent apoptotic death.1 Publication

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri80 – 12849PHD-type 1Add
    BLAST
    Zinc fingeri143 – 19351PHD-type 2; degenerateAdd
    BLAST
    Zinc fingeri237 – 28650PHD-type 3Add
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. ubiquitin-protein transferase activity Source: Ensembl
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. blastocyst development Source: Ensembl
    3. negative regulation of intrinsic apoptotic signaling pathway Source: Ensembl
    4. protein polyubiquitination Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein, Ligase

    Keywords - Biological processi

    Apoptosis, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    G2/M phase-specific E3 ubiquitin-protein ligase (EC:6.3.2.-)
    Gene namesi
    Name:G2E3
    Synonyms:KIAA1333
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:20338. G2E3.

    Subcellular locationi

    Nucleusnucleolus 1 Publication. Cytoplasm 1 Publication
    Note: Shuttles between the nucleus and the cytoplasm. In the nucleus, delocalizes from the nucleolus to the nucleoplasm in response to DNA damage.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleolus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi30 – 312KK → AA: Loss of nucleolar localization. No effect on nuclear localization.
    Mutagenesisi84 – 841C → A: Strong activity; when associated with A-258; A-261 and A-666. Strong activity; when associated with A-147 and A-666. No activity; when associated with A-147; A-258 and A-261. 1 Publication
    Mutagenesisi147 – 1471C → A: Strong activity; when associated with A-84 and A-666. No activity; when associated with A-258; A-261 and A-666. No activity; when associated with A-84; A-258 and A-261. 1 Publication
    Mutagenesisi258 – 2581C → A: Strong activity; when associated with A-84; A-261 and A-666. No activity; when associated with A-147; A-261 and A-666. No activity; when associated with A-84; A-147 and A-261. 1 Publication
    Mutagenesisi261 – 2611C → A: Strong activity; when associated with A-84; A-258 and A-666. No activity; when associated with A-84; A-147 and A-258. No activity; when associated with A-147; A-258 and A-666. 1 Publication
    Mutagenesisi666 – 6661C → A: No effect on subcellular location. Strong activity; when associated with A-84; A-258 and A261. Strong activity; when associated with A-84 and A-147. No activity; when associated with A-147; A-258 and A-261. 2 Publications

    Organism-specific databases

    PharmGKBiPA164720127.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 706706G2/M phase-specific E3 ubiquitin-protein ligasePRO_0000248343Add
    BLAST

    Proteomic databases

    MaxQBiQ7L622.
    PaxDbiQ7L622.
    PRIDEiQ7L622.

    PTM databases

    PhosphoSiteiQ7L622.

    Expressioni

    Tissue specificityi

    Predominantly expressed in brain, liver, kidney, testes and ovary.1 Publication

    Inductioni

    Up-regulated approximately 4-fold in G2 when compared to S phase. Down-regulated approximately 3-fold by gamma-irradiation.1 Publication

    Gene expression databases

    ArrayExpressiQ7L622.
    BgeeiQ7L622.
    CleanExiHS_KIAA1333.
    GenevestigatoriQ7L622.

    Organism-specific databases

    HPAiHPA001601.

    Interactioni

    Protein-protein interaction databases

    BioGridi120771. 3 interactions.
    IntActiQ7L622. 4 interactions.
    MINTiMINT-1441199.
    STRINGi9606.ENSP00000206595.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7L622.
    SMRiQ7L622. Positions 14-127, 214-285.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini371 – 698328HECTPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    Ubiquitin ligase activity is mediated by two distinct domains, PHD-type zinc fingers 2 and 3. The use of these distinct domains may allow ubiquitination of different targets by each domain. The HECT domain is catalytically inactive and does not contribute to this activity.1 Publication

    Sequence similaritiesi

    Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
    Contains 3 PHD-type zinc fingers.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri80 – 12849PHD-type 1Add
    BLAST
    Zinc fingeri143 – 19351PHD-type 2; degenerateAdd
    BLAST
    Zinc fingeri237 – 28650PHD-type 3Add
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG304942.
    HOGENOMiHOG000112684.
    HOVERGENiHBG055656.
    InParanoidiQ7L622.
    OrthoDBiEOG78WKSC.
    PhylomeDBiQ7L622.
    TreeFamiTF325426.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR000569. HECT.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF00632. HECT. 1 hit.
    [Graphical view]
    SMARTiSM00249. PHD. 2 hits.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF56204. SSF56204. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEiPS50237. HECT. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q7L622-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNESKPGDSQ NLACVFCRKH DDCPNKYGEK KTKEKWNLTV HYYCLLMSSG    50
    IWQRGKEEEG VYGFLIEDIR KEVNRASKLK CCVCKKNGAS IGCVAPRCKR 100
    SYHFPCGLQR ECIFQFTGNF ASFCWDHRPV QIITSNNYRE SLPCTICLEF 150
    IEPIPSYNIL RSPCCKNAWF HRDCLQVQAI NAGVFFFRCT ICNNSDIFQK 200
    EMLRMGIHIP EKDASWELEE NAYQELLQHY ERCDVRRCRC KEGRDYNAPD 250
    SKWEIKRCQC CGSSGTHLAC SSLRSWEQNW ECLECRGIIY NSGEFQKAKK 300
    HVLPNSNNVG ITDCLLEESS PKLPRQSPGS QSKDLLRQGS KFRRNVSTLL 350
    IELGFQIKKK TKRLYINKAN IWNSALDAFR NRNFNPSYAI EVAYVIENDN 400
    FGSEHPGSKQ EFLSLLMQHL ENSSLFEGSL SKNLSLNSQA LKENLYYEAG 450
    KMLAISLVHG GPSPGFFSKT LFNCLVYGPE NTQPILDDVS DFDVAQIIIR 500
    INTATTVADL KSIINECYNY LELIGCLRLI TTLSDKYMLV KDILGYHVIQ 550
    RVHTPFESFK QGLKTLGVLE KIQAYPEAFC SILCHKPESL SAKILSELFT 600
    VHTLPDVKAL GFWNSYLQAV EDGKSTTTME DILIFATGCS SIPPAGFKPT 650
    PSIECLHVDF PVGNKCNNCL AIPITNTYKE FQENMDFTIR NTLRLEKEES 700
    SHYIGH 706
    Length:706
    Mass (Da):80,504
    Last modified:July 5, 2004 - v1
    Checksum:i4B46ACF8782F941A
    GO

    Sequence cautioni

    The sequence BAA92571.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB14280.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti184 – 1841V → A in BAA91095. (PubMed:14702039)Curated
    Sequence conflicti627 – 6271T → A in BAB14280. (PubMed:14702039)Curated
    Sequence conflicti665 – 6651K → E in BAA91095. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti232 – 2321R → H.
    Corresponds to variant rs17096934 [ dbSNP | Ensembl ].
    VAR_027273

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037754 mRNA. Translation: BAA92571.1. Different initiation.
    AK000340 mRNA. Translation: BAA91095.1.
    AK022867 mRNA. Translation: BAB14280.1. Different initiation.
    BC000973 mRNA. Translation: AAH00973.2.
    CCDSiCCDS9638.1.
    RefSeqiNP_060239.2. NM_017769.3.
    UniGeneiHs.509008.
    Hs.605081.

    Genome annotation databases

    EnsembliENST00000206595; ENSP00000206595; ENSG00000092140.
    GeneIDi55632.
    KEGGihsa:55632.
    UCSCiuc001wqk.2. human.

    Polymorphism databases

    DMDMi74738611.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037754 mRNA. Translation: BAA92571.1 . Different initiation.
    AK000340 mRNA. Translation: BAA91095.1 .
    AK022867 mRNA. Translation: BAB14280.1 . Different initiation.
    BC000973 mRNA. Translation: AAH00973.2 .
    CCDSi CCDS9638.1.
    RefSeqi NP_060239.2. NM_017769.3.
    UniGenei Hs.509008.
    Hs.605081.

    3D structure databases

    ProteinModelPortali Q7L622.
    SMRi Q7L622. Positions 14-127, 214-285.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120771. 3 interactions.
    IntActi Q7L622. 4 interactions.
    MINTi MINT-1441199.
    STRINGi 9606.ENSP00000206595.

    PTM databases

    PhosphoSitei Q7L622.

    Polymorphism databases

    DMDMi 74738611.

    Proteomic databases

    MaxQBi Q7L622.
    PaxDbi Q7L622.
    PRIDEi Q7L622.

    Protocols and materials databases

    DNASUi 55632.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000206595 ; ENSP00000206595 ; ENSG00000092140 .
    GeneIDi 55632.
    KEGGi hsa:55632.
    UCSCi uc001wqk.2. human.

    Organism-specific databases

    CTDi 55632.
    GeneCardsi GC14P031028.
    HGNCi HGNC:20338. G2E3.
    HPAi HPA001601.
    MIMi 611299. gene.
    neXtProti NX_Q7L622.
    PharmGKBi PA164720127.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG304942.
    HOGENOMi HOG000112684.
    HOVERGENi HBG055656.
    InParanoidi Q7L622.
    OrthoDBi EOG78WKSC.
    PhylomeDBi Q7L622.
    TreeFami TF325426.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    GeneWikii KIAA1333.
    GenomeRNAii 55632.
    NextBioi 60275.
    PROi Q7L622.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7L622.
    Bgeei Q7L622.
    CleanExi HS_KIAA1333.
    Genevestigatori Q7L622.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR000569. HECT.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF00632. HECT. 1 hit.
    [Graphical view ]
    SMARTi SM00249. PHD. 2 hits.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56204. SSF56204. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEi PS50237. HECT. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "G2E3 is a nucleo-cytoplasmic shuttling protein with DNA damage responsive localization."
      Brooks W.S., Banerjee S., Crawford D.F.
      Exp. Cell Res. 313:665-676(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, MUTAGENESIS OF 30-LYS-LYS-31 AND CYS-666.
    2. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY.
      Tissue: Brain.
    3. "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].
      Tissue: Hepatoma and Teratocarcinoma.
    4. "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].
      Tissue: Placenta.
    5. "The G(2) DNA damage checkpoint delays expression of genes encoding mitotic regulators."
      Crawford D.F., Piwnica-Worms H.
      J. Biol. Chem. 276:37166-37177(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    6. "G2E3 is a dual function ubiquitin ligase required for early embryonic development."
      Brooks W.S., Helton E.S., Banerjee S., Venable M., Johnson L., Schoeb T.R., Kesterson R.A., Crawford D.F.
      J. Biol. Chem. 283:22304-22315(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, MUTAGENESIS OF CYS-84; CYS-147; CYS-258; CYS-261 AND CYS-666.

    Entry informationi

    Entry nameiG2E3_HUMAN
    AccessioniPrimary (citable) accession number: Q7L622
    Secondary accession number(s): Q9BVR2
    , Q9H9E9, Q9NXC0, Q9P2L3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3