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Q7L622

- G2E3_HUMAN

UniProt

Q7L622 - G2E3_HUMAN

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Protein
G2/M phase-specific E3 ubiquitin-protein ligase
Gene
G2E3, KIAA1333
Organism
Homo sapiens (Human)
Status
Reviewed - 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 1
Add
BLAST
Zinc fingeri143 – 19351PHD-type 2; degenerate
Add
BLAST
Zinc fingeri237 – 28650PHD-type 3
Add
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
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: Chromosome 14

Organism-specific databases

HGNCiHGNC:20338. G2E3.

Subcellular locationi

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

GO - Cellular componenti

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini371 – 698328HECT
Add
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

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.

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841V → A in BAA91095. 1 Publication
Sequence conflicti627 – 6271T → A in BAB14280. 1 Publication
Sequence conflicti665 – 6651K → E in BAA91095. 1 Publication

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

« 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: September 3, 2014
This is version 97 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

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