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Protein

G2/M phase-specific E3 ubiquitin-protein ligase

Gene

G2e3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity). Required for prevention of apoptotic death in early embryogenesis.By similarity1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri80 – 12849PHD-type 1Add
BLAST
Zinc fingeri141 – 19555PHD-type 2; degenerateAdd
BLAST
Zinc fingeri237 – 28650PHD-type 3Add
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • blastocyst development Source: MGI
  • negative regulation of intrinsic apoptotic signaling pathway Source: MGI
  • protein polyubiquitination Source: MGI
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

BRENDAi6.3.2.19. 3474.
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:2444298. G2e3.

Subcellular locationi

  • Nucleusnucleolus By similarity
  • Cytoplasm By similarity

  • Note: Shuttles between the nucleus and the cytoplasm. In the nucleus, delocalizes from the nucleolus to the nucleoplasm in response to DNA damage (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryos die prior to implantation due to massive apoptosis resulting in blastocyst involution.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 716716G2/M phase-specific E3 ubiquitin-protein ligasePRO_0000248345Add
BLAST

Proteomic databases

EPDiQ5RJY2.
MaxQBiQ5RJY2.
PaxDbiQ5RJY2.
PRIDEiQ5RJY2.

PTM databases

iPTMnetiQ5RJY2.
PhosphoSiteiQ5RJY2.

Expressioni

Tissue specificityi

In the developing embryo, expressed predominantly in the central nervous system and early limb bud. In the adult, highest expression in Purkinje cell bodies and cells lining the ductus deferens.1 Publication

Gene expression databases

BgeeiQ5RJY2.
CleanExiMM_6030408C04RIK.
ExpressionAtlasiQ5RJY2. baseline and differential.
GenevisibleiQ5RJY2. MM.

Interactioni

Protein-protein interaction databases

IntActiQ5RJY2. 1 interaction.
STRINGi10090.ENSMUSP00000113270.

Structurei

3D structure databases

ProteinModelPortaliQ5RJY2.
SMRiQ5RJY2. Positions 14-126, 214-285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini369 – 696328HECTPROSITE-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 (By similarity).By similarity

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 fingeri141 – 19555PHD-type 2; degenerateAdd
BLAST
Zinc fingeri237 – 28650PHD-type 3Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IPTH. Eukaryota.
ENOG410ZNVY. LUCA.
GeneTreeiENSGT00390000005246.
HOGENOMiHOG000112684.
HOVERGENiHBG055656.
InParanoidiQ5RJY2.
OrthoDBiEOG78WKSC.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR000569. HECT_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00632. HECT. 1 hit.
[Graphical view]
SMARTiSM00119. HECTc. 1 hit.
SM00249. PHD. 3 hits.
[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.

Q5RJY2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNENKPDNSQ SLACVFCRKN DDCPNKYGEK KTYEKWNFSV HYYCLLMSSG
60 70 80 90 100
IWQRGKEEEG VYGFLIEDIR KEVQRASKLK CTVCKKNGAS IGCVVPTCKR
110 120 130 140 150
SYHLPCGLQK ECIFQFTDNF ASFCWKHRPV QAITSNKYSS SLPCTICLEF
160 170 180 190 200
VEPIPTYNIL QSPCCKNAWF HRDCLQVQAI NAGVFFFRCT LCNNTDIFQK
210 220 230 240 250
EMLRMGIHIP EKDASWELEE NAYQELLQSH DRCDIRRCHC KKGRDYNEPN
260 270 280 290 300
SKWEVKRCQS CGSSGTHLAC SSLQSWEQNW ECLDCRRITY TSDFQKAPKH
310 320 330 340 350
PLANSTNVTV TDCLLEESSS KLPRQSTVAQ HKELLRQGSK FRRDISTILI
360 370 380 390 400
ELGFQIKKKT KTLYINKANV WRSALEQFQS QKFNPSCSID VVYVNGNEVG
410 420 430 440 450
SQHLGSKQEF LSHLMHHLEN SSVFEGSLAK NLSLNSQAVK ENLYYEVGKM
460 470 480 490 500
LAISLVHGGP SPGFFSETLF NCLAYGPENT LPTLDDVSDI DVAQIIIKID
510 520 530 540 550
SATDLNILNS VISQHYNYLE VSGCLRLTTS LSDKFMLVKD ILFYHVINRV
560 570 580 590 600
KAPFESFKQG LKTLGVLEKI QTYPEAFYKI LCHKPENLSA KNLSDLFTIH
610 620 630 640 650
SVADVQTLRF WNSYLKAIED GKSATTMEDI LIFATGCSSV PPTGFKPSLS
660 670 680 690 700
VECLHVDFPV ADKYRNHLVL PATNTYEEFQ ENMDFTIRDT LRLEKEERSH
710
ILPRTLNVSS NEEMLI
Length:716
Mass (Da):81,784
Last modified:July 27, 2011 - v2
Checksum:i9A3B7CE4A9F53A52
GO

Sequence cautioni

The sequence BAC98142.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti675 – 6751T → A in AAH86455 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129332 mRNA. Translation: BAC98142.1. Different initiation.
AC161116 Genomic DNA. No translation available.
BC086455 mRNA. Translation: AAH86455.1.
AK084256 mRNA. Translation: BAC39150.1.
CCDSiCCDS25900.1.
RefSeqiNP_001015099.2. NM_001015099.2.
NP_001161435.1. NM_001167963.1.
NP_001161436.1. NM_001167964.1.
UniGeneiMm.253264.

Genome annotation databases

EnsembliENSMUST00000054308; ENSMUSP00000054474; ENSMUSG00000035293.
GeneIDi217558.
KEGGimmu:217558.
UCSCiuc007nml.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129332 mRNA. Translation: BAC98142.1. Different initiation.
AC161116 Genomic DNA. No translation available.
BC086455 mRNA. Translation: AAH86455.1.
AK084256 mRNA. Translation: BAC39150.1.
CCDSiCCDS25900.1.
RefSeqiNP_001015099.2. NM_001015099.2.
NP_001161435.1. NM_001167963.1.
NP_001161436.1. NM_001167964.1.
UniGeneiMm.253264.

3D structure databases

ProteinModelPortaliQ5RJY2.
SMRiQ5RJY2. Positions 14-126, 214-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5RJY2. 1 interaction.
STRINGi10090.ENSMUSP00000113270.

PTM databases

iPTMnetiQ5RJY2.
PhosphoSiteiQ5RJY2.

Proteomic databases

EPDiQ5RJY2.
MaxQBiQ5RJY2.
PaxDbiQ5RJY2.
PRIDEiQ5RJY2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000054308; ENSMUSP00000054474; ENSMUSG00000035293.
GeneIDi217558.
KEGGimmu:217558.
UCSCiuc007nml.2. mouse.

Organism-specific databases

CTDi55632.
MGIiMGI:2444298. G2e3.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IPTH. Eukaryota.
ENOG410ZNVY. LUCA.
GeneTreeiENSGT00390000005246.
HOGENOMiHOG000112684.
HOVERGENiHBG055656.
InParanoidiQ5RJY2.
OrthoDBiEOG78WKSC.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 3474.

Miscellaneous databases

ChiTaRSiG2e3. mouse.
PROiQ5RJY2.
SOURCEiSearch...

Gene expression databases

BgeeiQ5RJY2.
CleanExiMM_6030408C04RIK.
ExpressionAtlasiQ5RJY2. baseline and differential.
GenevisibleiQ5RJY2. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR000569. HECT_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00632. HECT. 1 hit.
[Graphical view]
SMARTiSM00119. HECTc. 1 hit.
SM00249. PHD. 3 hits.
[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. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Embryonic germ cell.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-356.
    Strain: C57BL/6J.
    Tissue: Eye.
  5. "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, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiG2E3_MOUSE
AccessioniPrimary (citable) accession number: Q5RJY2
Secondary accession number(s): E9QK24, Q6ZPT7, Q8BNA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.