P61082 (UBC12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NEDD8-conjugating enzyme Ubc12
EC=6.3.2.-

Alternative name(s):
NEDD8 carrier protein
NEDD8 protein ligase
Ubiquitin-conjugating enzyme E2 M

Gene names

Name:	Ube2m
Synonyms:	Ubc-rs2, Ubc12

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	183 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation By similarity.
Catalytic activity	ATP + NEDD8 + protein lysine = AMP + diphosphate + protein N-NEDD8yllysine.
Pathway	Protein modification; protein neddylation.
Subunit structure	Interacts with UBA3, DCN1L and RBX1 By similarity.
Domain	Both the N-terminal docking peptide and the catalytic core domain must bind the UBA3-NAE1 complex simultaneously for optimal transfer of NEDD8 By similarity.
Post-translational modification	The acetylation of Met-1 is cotranslational, and not regulatory. The N-acetylmethionine increases affinity for DCUN1D1 by about 2 orders of magnitude and is crucial for NEDD8 transfer to cullins By similarity.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family. UBC12 subfamily.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara protein neddylation Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NEDD8 ligase activity Inferred from sequence or structural similarity. Source: UniProtKB ribosomal S6-glutamic acid ligase activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-protein ligase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 183	183	NEDD8-conjugating enzyme Ubc12		PRO_0000082489
Regions
	Region	1 – 26	26	Interaction with UBA3 By similarity
	Region	27 – 57	31	Interaction with UBA3 By similarity
Sites
	Active site	111	1	Glycyl thioester intermediate By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	3	1	N6-acetyllysine By similarity
	Modified residue	50	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P61082 [UniParc]. Last modified April 26, 2004. Version 1. Checksum: E3C288CA6A98BC5C	FASTA	183	20,900
	10 20 30 40 50 60 MIKLFSLKQQ KKEEESAGGT KGSSKKASAA QLRIQKDINE LNLPKTCDIS FSDPDDLLNF 70 80 90 100 110 120 KLVICPDEGF YKSGKFVFSF KVGQGYPHDP PKVKCETMVY HPNIDLEGNV CLNILREDWK 130 140 150 160 170 180 PVLTINSIIY GLQYLFLEPN PEDPLNKEAA EVLQNNRRLF EQNVQRSMRG GYIGSTYFER CLK

References

[1]	"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: Kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC021792 mRNA. Translation: AAH21792.1.
IPI	IPI00169448.
RefSeq	NP_663553.1. NM_145578.3.
UniGene	Mm.196580.
3D structure databases
ProteinModelPortal	P61082.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000005714.
PTM databases
PhosphoSite	P61082.
2D gel databases
REPRODUCTION-2DPAGE	IPI00169448. P61082.
Proteomic databases
PaxDb	P61082.
PRIDE	P61082.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000005714; ENSMUSP00000005714; ENSMUSG00000005575.
GeneID	22192.
KEGG	mmu:22192.
UCSC	uc009ffd.1. mouse.
Organism-specific databases
CTD	9040.
MGI	MGI:108278. Ube2m.
Phylogenomic databases
eggNOG	COG5078.
GeneTree	ENSGT00630000089859.
HOGENOM	HOG000233456.
HOVERGEN	HBG098591.
InParanoid	P61082.
KO	K10579.
OrthoDB	EOG4TB4CC.
Enzyme and pathway databases
UniPathway	UPA00885.
Gene expression databases
ArrayExpress	P61082.
Bgee	P61082.
Genevestigator	P61082.
GermOnline	ENSMUSG00000005575. Mus musculus.
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
NextBio	302165.
SOURCE	Search...

Entry information

Entry name

UBC12_MOUSE

Accession

Primary (citable) accession number: P61082
Secondary accession number(s): O76069, Q8VC50

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	April 26, 2004
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program