Q7L622 (G2E3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
G2/M phase-specific E3 ubiquitin-protein ligase
EC=6.3.2.-

Gene names

Name:	G2E3
Synonyms:	KIAA1333

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	706 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6
Pathway	Protein modification; protein ubiquitination.
Subcellular location	Nucleus › nucleolus. Cytoplasm. Note: Shuttles between the nucleus and the cytoplasm. In the nucleus, delocalizes from the nucleolus to the nucleoplasm in response to DNA damage. Ref.1
Tissue specificity	Predominantly expressed in brain, liver, kidney, testes and ovary. Ref.2
Induction	Up-regulated approximately 4-fold in G2 when compared to S phase. Down-regulated approximately 3-fold by gamma-irradiation. Ref.5
Domain	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. Ref.6
Sequence similarities	Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain. Contains 3 PHD-type zinc fingers.
Sequence caution	The sequence BAA92571.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB14280.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Apoptosis Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Developmental protein Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW blastocyst development Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara protein polyubiquitination Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ubiquitin-protein ligase activity Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 706	706	G2/M phase-specific E3 ubiquitin-protein ligase		PRO_0000248343
Regions
	Domain	371 – 698	328	HECT
	Zinc finger	80 – 128	49	PHD-type 1
	Zinc finger	143 – 193	51	PHD-type 2; degenerate
	Zinc finger	237 – 286	50	PHD-type 3
Natural variations
	Natural variant	232	1	R → H. Corresponds to variant rs17096934 [ dbSNP | Ensembl ].		VAR_027273
Experimental info
	Mutagenesis	30 – 31	2	KK → AA: Loss of nucleolar localization. No effect on nuclear localization.
	Mutagenesis	84	1	C → 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. Ref.6
	Mutagenesis	147	1	C → 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. Ref.6
	Mutagenesis	258	1	C → 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. Ref.6
	Mutagenesis	261	1	C → 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. Ref.6
	Mutagenesis	666	1	C → 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. Ref.1 Ref.6
	Sequence conflict	184	1	V → A in BAA91095. Ref.3
	Sequence conflict	627	1	T → A in BAB14280. Ref.3
	Sequence conflict	665	1	K → E in BAA91095. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q7L622 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 4B46ACF8782F941A	FASTA	706	80,504
	10 20 30 40 50 60 MNESKPGDSQ NLACVFCRKH DDCPNKYGEK KTKEKWNLTV HYYCLLMSSG IWQRGKEEEG 70 80 90 100 110 120 VYGFLIEDIR KEVNRASKLK CCVCKKNGAS IGCVAPRCKR SYHFPCGLQR ECIFQFTGNF 130 140 150 160 170 180 ASFCWDHRPV QIITSNNYRE SLPCTICLEF IEPIPSYNIL RSPCCKNAWF HRDCLQVQAI 190 200 210 220 230 240 NAGVFFFRCT ICNNSDIFQK EMLRMGIHIP EKDASWELEE NAYQELLQHY ERCDVRRCRC 250 260 270 280 290 300 KEGRDYNAPD SKWEIKRCQC CGSSGTHLAC SSLRSWEQNW ECLECRGIIY NSGEFQKAKK 310 320 330 340 350 360 HVLPNSNNVG ITDCLLEESS PKLPRQSPGS QSKDLLRQGS KFRRNVSTLL IELGFQIKKK 370 380 390 400 410 420 TKRLYINKAN IWNSALDAFR NRNFNPSYAI EVAYVIENDN FGSEHPGSKQ EFLSLLMQHL 430 440 450 460 470 480 ENSSLFEGSL SKNLSLNSQA LKENLYYEAG KMLAISLVHG GPSPGFFSKT LFNCLVYGPE 490 500 510 520 530 540 NTQPILDDVS DFDVAQIIIR INTATTVADL KSIINECYNY LELIGCLRLI TTLSDKYMLV 550 560 570 580 590 600 KDILGYHVIQ RVHTPFESFK QGLKTLGVLE KIQAYPEAFC SILCHKPESL SAKILSELFT 610 620 630 640 650 660 VHTLPDVKAL GFWNSYLQAV EDGKSTTTME DILIFATGCS SIPPAGFKPT PSIECLHVDF 670 680 690 700 PVGNKCNNCL AIPITNTYKE FQENMDFTIR NTLRLEKEES SHYIGH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB037754 mRNA. Translation: BAA92571.1. Different initiation. AK000340 mRNA. Translation: BAA91095.1. AK022867 mRNA. Translation: BAB14280.1. Different initiation. BC000973 mRNA. Translation: AAH00973.2.
IPI	IPI00479641.
RefSeq	NP_060239.2. NM_017769.3.
UniGene	Hs.509008. Hs.605081.
3D structure databases
ProteinModelPortal	Q7L622.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q7L622. 4 interactions.
MINT	MINT-1441199.
STRING	9606.ENSP00000206595.
PTM databases
PhosphoSite	Q7L622.
Polymorphism databases
DMDM	74738611.
Proteomic databases
PaxDb	Q7L622.
PRIDE	Q7L622.
Protocols and materials databases
DNASU	55632.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000206595; ENSP00000206595; ENSG00000092140.
GeneID	55632.
KEGG	hsa:55632.
UCSC	uc001wqk.2. human.
Organism-specific databases
CTD	55632.
GeneCards	GC14P031028.
HGNC	HGNC:20338. G2E3.
HPA	HPA001601.
MIM	611299. gene.
neXtProt	NX_Q7L622.
PharmGKB	PA164720127.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG304942.
HOGENOM	HOG000112684.
HOVERGEN	HBG055656.
InParanoid	Q7L622.
OrthoDB	EOG4R23T7.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q7L622.
Bgee	Q7L622.
CleanEx	HS_KIAA1333.
Genevestigator	Q7L622.
GermOnline	ENSG00000092140. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	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]
Pfam	PF00632. HECT. 1 hit. [Graphical view]
SMART	SM00249. PHD. 2 hits. SM00184. RING. 1 hit. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 1 hit. SSF56204. HECT. 1 hit.
PROSITE	PS50237. HECT. 1 hit. PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	55632.
NextBio	60275.
SOURCE	Search...

Entry information

Entry name

G2E3_HUMAN

Accession

Primary (citable) accession number: Q7L622
Secondary accession number(s): Q9BVR2 , Q9H9E9, Q9NXC0, Q9P2L3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	July 5, 2004
Last modified:	May 29, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.