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Protein

G2/M phase-specific E3 ubiquitin-protein ligase

Gene

G2E3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

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 Componenti: 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

Complete GO annotation...

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. 1 Publication
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.

Polymorphism and mutation databases

BioMutaiG2E3.
DMDMi74738611.

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

BgeeiQ7L622.
CleanExiHS_KIAA1333.
ExpressionAtlasiQ7L622. baseline and differential.
GenevestigatoriQ7L622.

Organism-specific databases

HPAiHPA001601.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
RPS15P628413EBI-751757,EBI-372635

Protein-protein interaction databases

BioGridi120771. 4 interactions.
IntActiQ7L622. 5 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.
GeneTreeiENSGT00390000005246.
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

        10         20         30         40         50
MNESKPGDSQ NLACVFCRKH DDCPNKYGEK KTKEKWNLTV HYYCLLMSSG
60 70 80 90 100
IWQRGKEEEG VYGFLIEDIR KEVNRASKLK CCVCKKNGAS IGCVAPRCKR
110 120 130 140 150
SYHFPCGLQR ECIFQFTGNF ASFCWDHRPV QIITSNNYRE SLPCTICLEF
160 170 180 190 200
IEPIPSYNIL RSPCCKNAWF HRDCLQVQAI NAGVFFFRCT ICNNSDIFQK
210 220 230 240 250
EMLRMGIHIP EKDASWELEE NAYQELLQHY ERCDVRRCRC KEGRDYNAPD
260 270 280 290 300
SKWEIKRCQC CGSSGTHLAC SSLRSWEQNW ECLECRGIIY NSGEFQKAKK
310 320 330 340 350
HVLPNSNNVG ITDCLLEESS PKLPRQSPGS QSKDLLRQGS KFRRNVSTLL
360 370 380 390 400
IELGFQIKKK TKRLYINKAN IWNSALDAFR NRNFNPSYAI EVAYVIENDN
410 420 430 440 450
FGSEHPGSKQ EFLSLLMQHL ENSSLFEGSL SKNLSLNSQA LKENLYYEAG
460 470 480 490 500
KMLAISLVHG GPSPGFFSKT LFNCLVYGPE NTQPILDDVS DFDVAQIIIR
510 520 530 540 550
INTATTVADL KSIINECYNY LELIGCLRLI TTLSDKYMLV KDILGYHVIQ
560 570 580 590 600
RVHTPFESFK QGLKTLGVLE KIQAYPEAFC SILCHKPESL SAKILSELFT
610 620 630 640 650
VHTLPDVKAL GFWNSYLQAV EDGKSTTTME DILIFATGCS SIPPAGFKPT
660 670 680 690 700
PSIECLHVDF PVGNKCNNCL AIPITNTYKE FQENMDFTIR NTLRLEKEES

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

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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi120771. 4 interactions.
IntActiQ7L622. 5 interactions.
MINTiMINT-1441199.
STRINGi9606.ENSP00000206595.

PTM databases

PhosphoSiteiQ7L622.

Polymorphism and mutation databases

BioMutaiG2E3.
DMDMi74738611.

Proteomic databases

MaxQBiQ7L622.
PaxDbiQ7L622.
PRIDEiQ7L622.

Protocols and materials databases

DNASUi55632.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi55632.
GeneCardsiGC14P031028.
HGNCiHGNC:20338. G2E3.
HPAiHPA001601.
MIMi611299. gene.
neXtProtiNX_Q7L622.
PharmGKBiPA164720127.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG304942.
GeneTreeiENSGT00390000005246.
HOGENOMiHOG000112684.
HOVERGENiHBG055656.
InParanoidiQ7L622.
OrthoDBiEOG78WKSC.
PhylomeDBiQ7L622.
TreeFamiTF325426.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiG2E3. human.
GeneWikiiKIAA1333.
GenomeRNAii55632.
NextBioi60275.
PROiQ7L622.
SOURCEiSearch...

Gene expression databases

BgeeiQ7L622.
CleanExiHS_KIAA1333.
ExpressionAtlasiQ7L622. baseline and differential.
GenevestigatoriQ7L622.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 103 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.