Q921J4 (UBE2S_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Ubiquitin carrier protein S
Ubiquitin-conjugating enzyme E2-24 kDa
Ubiquitin-conjugating enzyme E2-EPF5
Ubiquitin-protein ligase S

Gene names

Name:	Ube2s
Synonyms:	E2epf

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	223 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes 'Lys-11'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by specifically elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit. Also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is however unclear whether UBE2D1/UBCH5 acts as a E2 enzyme for the APC/C in vivo. Also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination.
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Component of the APC/C complex. Interacts with CDC20, FZR1/CDH1 and VHL By similarity.
Post-translational modification	Autoubiquitinated by the APC/C complex during G1, leading to its degradation by the proteasome By similarity.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Ubl conjugation pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of anaphase-promoting complex activity Inferred from sequence or structural similarity. Source: UniProtKB anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW exit from mitosis Inferred from sequence or structural similarity. Source: UniProtKB free ubiquitin chain polymerization Inferred from sequence or structural similarity. Source: UniProtKB protein K11-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K27-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K29-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K6-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K63-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	anaphase-promoting complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 223	223	Ubiquitin-conjugating enzyme E2 S		PRO_0000082508
Sites
	Active site	95	1	Glycyl thioester intermediate By similarity
Experimental info
	Sequence conflict	213	1	K → N in BAC25019. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q921J4 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 10816CE4377BC406	FASTA	223	24,183
	10 20 30 40 50 60 MNSNVENLPP HIIRLVYKEV TTLTADPPDG IKVFPNEEDL TDLQVTIEGP EGTPYAGGLF 70 80 90 100 110 120 RMKLLLGKDF PASPPKGYFL TKIFHPNVGP NGEICVNVLK RDWTAELGIR HVLLTIKCLL 130 140 150 160 170 180 IHPNPESALN EEAGRLLLEN YEEYAARARL LTEIHGGACS TSSGRAEATQ DLASGASASS 190 200 210 220 ADPMIPGVLG GAEGPMAKKH AGERDKKLAA KKKLDKKRAL RRL

References

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J, DBA/2 and NOD. Tissue: Spleen and Thymus.
[2]	"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]. Strain: C57BL/6 and Czech II. Tissue: Mammary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK003078 mRNA. Translation: BAC25019.1. AK017648 mRNA. Translation: BAC25523.1. AK146276 mRNA. Translation: BAE27035.1. AK154026 mRNA. Translation: BAE32323.1. AK154067 mRNA. Translation: BAE32353.1. BC012255 mRNA. Translation: AAH12255.1. BC030171 mRNA. Translation: AAH30171.1. BC083323 mRNA. Translation: AAH83323.1.
IPI	IPI00121891.
RefSeq	NP_598538.1. NM_133777.2.
UniGene	Mm.389787.
3D structure databases
ProteinModelPortal	Q921J4.
SMR	Q921J4. Positions 6-156.
ModBase	Search...
PTM databases
PhosphoSite	Q921J4.
2D gel databases
REPRODUCTION-2DPAGE	Q921J4.
Proteomic databases
PaxDb	Q921J4.
PRIDE	Q921J4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000079496; ENSMUSP00000078459; ENSMUSG00000060860.
GeneID	77891.
KEGG	mmu:77891.
UCSC	uc009eyt.1. mouse.
Organism-specific databases
CTD	27338.
MGI	MGI:1925141. Ube2s.
Phylogenomic databases
eggNOG	COG5078.
GeneTree	ENSGT00680000099547.
HOGENOM	HOG000233455.
HOVERGEN	HBG063308.
InParanoid	Q8CF67.
KO	K10583.
OMA	PDLGIKH.
OrthoDB	EOG4KPTBW.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
Bgee	Q921J4.
CleanEx	MM_UBE2S.
Genevestigator	Q921J4.
GermOnline	ENSMUSG00000060860. 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	347761.
SOURCE	Search...

Entry information

Entry name

UBE2S_MOUSE

Accession

Primary (citable) accession number: Q921J4
Secondary accession number(s): Q3U4V7, Q8CF67

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	December 1, 2001
Last modified:	April 3, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program