Reviewed, UniProtKB/Swiss-Prot P62253 (UB2G1_HUMAN)

Names and origin

Protein names

Recommended name:
    Ubiquitin-conjugating enzyme E2 G1
    EC=6.3.2.19
Alternative name(s):
    Ubiquitin-protein ligase G1
    Ubiquitin carrier protein G1
    E217K
    UBC7

Gene names

Name:	UBE2G1
Synonyms:	UBE2G

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	170 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins. May be involved in degradation of muscle-specific proteins.
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Tissue specificity	Widely expressed, mainly in skeletal muscle.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Molecular function	Ligase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	post-translational protein modification Inferred from electronic annotation. Source: InterPro regulation of protein metabolic process Inferred from electronic annotation. Source: InterPro ubiquitin-dependent protein catabolic process Ref.1 Traceable author statement. Source: ProtInc
Molecular function	ubiquitin-protein ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 170

169

Ubiquitin-conjugating enzyme E2 G1

PRO_0000082480

Sites

Active site

90

1

Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue

2

1

N-acetylthreonine

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

170

Helix Strand Turn

Details...

Helix

8 – 19

12

Beta strand

25 – 31

7

Beta strand

37 – 43

7

Turn

49 – 52

4

Beta strand

54 – 60

7

Turn

63 – 66

4

Beta strand

71 – 74

4

Helix

92 – 94

3

Helix

117 – 128

12

Sequences

	Sequence		Length	Mass (Da)
	P62253-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 36B61766D995B332	FASTA	170	19,509
	10 20 30 40 50 60 MTELQSALLL RRQLAELNKN PVEGFSAGLI DDNDLYRWEV LIIGPPDTLY EGGVFKAHLT 70 80 90 100 110 120 FPKDYPLRPP KMKFITEIWH PNVDKNGDVC ISILHEPGED KYGYEKPEER WLPIHTVETI 130 140 150 160 170 MISVISMLAD PNGDSPANVD AAKEWREDRN GEFKRKVARC VRKSQETAFE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of UBE2G, encoding a human skeletal muscle-specific ubiquitin-conjugating enzyme homologous to UBC7 of C. elegans." Watanabe T.K., Kawai A., Fujiwara T., Maekawa H., Hirai Y., Nakamura Y., Takahashi E. Cytogenet. Cell Genet. 74:146-148(1996) [PubMed: 8893823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Fetal brain.
[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 (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph and Prostate.
[4]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11, ACETYLATION AT THR-2. Tissue: Platelet.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

D78514 mRNA. Translation: BAA11410.1.
BT007416 mRNA. Translation: AAP36084.1.
BC002775 mRNA. Translation: AAH02775.1.
BC026288 mRNA. Translation: AAH26288.2. Different initiation.

RefSeq

NP_003333.1.

UniGene

Hs.462035

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AWF	X-ray	2.10	A	8-160	[»]

ModBase

Search...

PTM databases

PhosphoSite

P62253.

Proteomic databases

PeptideAtlas

P62253.

Genome annotation databases

Ensembl

ENSG00000132388. Homo sapiens. [Contig view]

GeneID

7326.

KEGG

hsa:7326.

Organism-specific databases

H-InvDB

HIX0013442.

HGNC

HGNC:12482. UBE2G1.

HPA

HPA013207.

MIM

601569. gene.

PharmGKB

PA37131.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P62253.

HOVERGEN

P62253.

Gene expression databases

ArrayExpress

P62253.

CleanEx

HS_UBE2G1.

GermOnline

ENSG00000132388. Homo sapiens.

Family and domain databases

InterPro

IPR016135. UBQ-conjugat/RWD-like.
IPR000608. UBQ-conjugat_E2.
[Graphical view]

Gene3D

G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.

PANTHER

PTHR11621. UBQ-conjugat_E2. 1 hit.

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

ProDom

PD000461. UBQ_conjugat. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00212. UBCc. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other Resources

LinkHub

P62253.

NextBio

28666.

SOURCE

Search...

Entry information

Entry name

UB2G1_HUMAN

Accession

Primary (citable) accession number: P62253
Secondary accession number(s): Q99462

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 52 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)