P60604 (UB2G2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 G2
EC=6.3.2.19

Alternative name(s):
Ubiquitin carrier protein G2
Ubiquitin-protein ligase G2

Gene names

Name:

UBE2G2

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	165 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Involved in endoplasmic reticulum-associated degradation (ERAD). Ref.7 Ref.9
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from mutant phenotype Ref.9. Source: UniProtKB protein K48-linked ubiquitination Inferred from direct assay Ref.7. Source: UniProtKB protein N-linked glycosylation via asparagine Inferred from mutant phenotype Ref.9. Source: UniProtKB
Cellular_component	cytosol Inferred from direct assay PubMed 16780588. Source: UniProtKB endoplasmic reticulum Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P60604-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P60604-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 165

165

Ubiquitin-conjugating enzyme E2 G2

PRO_0000082483

Sites

Active site

89

1

Glycyl thioester intermediate

Natural variations

Alternative sequence

1 – 28

28

Missing in isoform 2.

VSP_046260

Experimental info

Sequence conflict

12

1

E → V in AAC32312. Ref.1

Sequence conflict

101 – 107

7

MGYESSA → HGLREQP in AAC32312. Ref.1

Secondary structure

1

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165

Helix Strand Turn

Details...

Helix

4 – 18

15

Beta strand

24 – 30

7

Beta strand

36 – 42

7

Turn

48 – 51

4

Beta strand

53 – 59

7

Turn

62 – 65

4

Beta strand

70 – 73

4

Beta strand

86 – 88

3

Helix

91 – 93

3

Helix

105 – 108

4

Helix

116 – 128

13

Helix

135 – 137

3

Helix

138 – 146

9

Helix

148 – 163

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 15, 2004. Version 1. Checksum: 74DEC732A79575E3	FASTA	165	18,566
	10 20 30 40 50 60 MAGTALKRLM AEYKQLTLNP PEGIVAGPMN EENFFEWEAL IMGPEDTCFE FGVFPAILSF 70 80 90 100 110 120 PLDYPLSPPK MRFTCEMFHP NIYPDGRVCI SILHAPGDDP MGYESSAERW SPVQSVEKIL 130 140 150 160 LSVVSMLAEP NDESGANVDA SKMWRDDREQ FYKIAKQIVQ KSLGL
	Isoform 2 [UniParc]. Checksum: FA95FDC41C3FCAD4	FASTA	137	15,614
	10 20 30 40 50 60 MNEENFFEWE ALIMGPEDTC FEFGVFPAIL SFPLDYPLSP PKMRFTCEMF HPNIYPDGRV 70 80 90 100 110 120 CISILHAPGD DPMGYESSAE RWSPVQSVEK ILLSVVSMLA EPNDESGANV DASKMWRDDR 130 EQFYKIAKQI VQKSLGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification, expression, and chromosomal localization of ubiquitin conjugating enzyme 7 (UBE2G2), a human homologue of the Saccharomyces cerevisiae UBC7 gene." Katsanis N., Fisher E.M.C. Genomics 51:128-131(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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] (ISOFORM 1). Tissue: Heart.
[4]	"The DNA sequence of human chromosome 21." Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L. Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORM 1). Tissue: Lung.
[7]	"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines." David Y., Ziv T., Admon A., Navon A. J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein." Sato T., Sako Y., Sho M., Momohara M., Suico M.A., Shuto T., Nishitoh H., Okiyoneda T., Kokame K., Kaneko M., Taura M., Miyata M., Chosa K., Koga T., Morino-Koga S., Wada I., Kai H. Mol. Cell 47:99-110(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ERAD PATHWAY.
[10]	"Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7)." Arai R., Yoshikawa S., Murayama K., Imai Y., Takahashi R., Shirouzu M., Yokoyama S. Acta Crystallogr. F 62:330-334(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF032456 mRNA. Translation: AAC32312.1.
BT006914 mRNA. Translation: AAP35560.1.
AK290629 mRNA. Translation: BAF83318.1.
AL163300 Genomic DNA. Translation: CAB90551.1.
CH471079 Genomic DNA. Translation: EAX09395.1.
CH471079 Genomic DNA. Translation: EAX09397.1.
CH471079 Genomic DNA. Translation: EAX09398.1.
CH471079 Genomic DNA. Translation: EAX09399.1.
BC001738 mRNA. Translation: AAH01738.1.
BC008351 mRNA. Translation: AAH08351.1.
BC011569 mRNA. Translation: AAH11569.1.

IPI

IPI00010142.
IPI00337747.

RefSeq

NP_001189418.1. NM_001202489.1.
NP_003334.2. NM_003343.5.
NP_872630.1. NM_182688.2.

UniGene

Hs.529420.
Hs.701398.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CYX	X-ray	2.56	A/B/C	1-165	[»]
2KLY	NMR	-	A	1-165	[»]
3H8K	X-ray	1.80	A	2-165	[»]

ProteinModelPortal

P60604.

ModBase

Search...

Protein-protein interaction databases

IntAct

P60604. 23 interactions.

STRING

9606.ENSP00000338348.

PTM databases

PhosphoSite

P60604.

Polymorphism databases

DMDM

45593583.

Proteomic databases

PaxDb

P60604.

PRIDE

P60604.

Protocols and materials databases

DNASU

7327.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000330942; ENSP00000331384; ENSG00000184787.
ENST00000345496; ENSP00000338348; ENSG00000184787.

GeneID

7327.

KEGG

hsa:7327.

UCSC

uc002zfx.3. human.

Organism-specific databases

CTD

7327.

GeneCards

GC21M046188.

HGNC

HGNC:12483. UBE2G2.

HPA

HPA003332.

MIM

603124. gene.

neXtProt

NX_P60604.

PharmGKB

PA37132.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5078.

HOGENOM

HOG000233454.

HOVERGEN

HBG063308.

KO

K04555.

OMA

RRLMAEY.

OrthoDB

EOG4GB77C.

PhylomeDB

P60604.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

SignaLink

P60604.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

P60604.

Bgee

P60604.

CleanEx

HS_UBE2G2.

Genevestigator

P60604.

GermOnline

ENSG00000184787. Homo sapiens.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

SUPFAM

SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

UBE2G2. human.

EvolutionaryTrace

P60604.

GenomeRNAi

7327.

NextBio

28670.

SOURCE

Search...

Entry information

Entry name

UB2G2_HUMAN

Accession

Primary (citable) accession number: P60604
Secondary accession number(s): A6NMQ7 , A8K3L4, D3DSL7, P56554

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	March 15, 2004
Last modified:	May 29, 2013
This is version 105 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.