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Protein

Ubiquitin-conjugating enzyme E2 S

Gene

Ube2s

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei95 – 951Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. ubiquitin conjugating enzyme activity Source: MGI
  4. ubiquitin-like protein transferase activity Source: GO_Central
  5. ubiquitin protein ligase activity Source: GO_Central
  6. ubiquitin protein ligase binding Source: GO_Central
  7. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. activation of anaphase-promoting complex activity Source: UniProtKB
  2. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  3. cell division Source: UniProtKB-KW
  4. exit from mitosis Source: UniProtKB
  5. free ubiquitin chain polymerization Source: UniProtKB
  6. protein K11-linked ubiquitination Source: UniProtKB
  7. protein K27-linked ubiquitination Source: UniProtKB
  8. protein K29-linked ubiquitination Source: UniProtKB
  9. protein K63-linked ubiquitination Source: UniProtKB
  10. protein K6-linked ubiquitination Source: UniProtKB
  11. protein polyubiquitination Source: GO_Central
  12. ubiquitin-dependent protein catabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Ube2s
Synonyms:E2epf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1925141. Ube2s.

Subcellular locationi

GO - Cellular componenti

  1. anaphase-promoting complex Source: UniProtKB
  2. cytoplasm Source: GO_Central
  3. nucleus Source: GO_Central
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 223223Ubiquitin-conjugating enzyme E2 SPRO_0000082508Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Post-translational modificationi

Autoubiquitinated by the APC/C complex during G1, leading to its degradation by the proteasome.By similarity

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiQ921J4.
PaxDbiQ921J4.
PRIDEiQ921J4.

2D gel databases

REPRODUCTION-2DPAGEQ921J4.

PTM databases

PhosphoSiteiQ921J4.

Expressioni

Gene expression databases

BgeeiQ921J4.
CleanExiMM_UBE2S.
GenevestigatoriQ921J4.

Interactioni

Subunit structurei

Component of the APC/C complex. Interacts with CDC20, FZR1/CDH1 and VHL (By similarity).By similarity

Protein-protein interaction databases

IntActiQ921J4. 1 interaction.
MINTiMINT-8178472.

Structurei

3D structure databases

ProteinModelPortaliQ921J4.
SMRiQ921J4. Positions 6-156.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110565.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ921J4.
KOiK10583.
OMAiGHKGEIC.
OrthoDBiEOG73JKXD.
PhylomeDBiQ921J4.
TreeFamiTF101120.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q921J4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSNVENLPP HIIRLVYKEV TTLTADPPDG IKVFPNEEDL TDLQVTIEGP
60 70 80 90 100
EGTPYAGGLF RMKLLLGKDF PASPPKGYFL TKIFHPNVGP NGEICVNVLK
110 120 130 140 150
RDWTAELGIR HVLLTIKCLL IHPNPESALN EEAGRLLLEN YEEYAARARL
160 170 180 190 200
LTEIHGGACS TSSGRAEATQ DLASGASASS ADPMIPGVLG GAEGPMAKKH
210 220
AGERDKKLAA KKKLDKKRAL RRL
Length:223
Mass (Da):24,183
Last modified:November 30, 2001 - v1
Checksum:i10816CE4377BC406
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti213 – 2131K → N in BAC25019 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS39743.1.
RefSeqiNP_598538.1. NM_133777.2.
UniGeneiMm.389787.

Genome annotation databases

EnsembliENSMUST00000079496; ENSMUSP00000078459; ENSMUSG00000060860.
GeneIDi77891.
KEGGimmu:77891.
UCSCiuc009eyt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS39743.1.
RefSeqiNP_598538.1. NM_133777.2.
UniGeneiMm.389787.

3D structure databases

ProteinModelPortaliQ921J4.
SMRiQ921J4. Positions 6-156.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ921J4. 1 interaction.
MINTiMINT-8178472.

PTM databases

PhosphoSiteiQ921J4.

2D gel databases

REPRODUCTION-2DPAGEQ921J4.

Proteomic databases

MaxQBiQ921J4.
PaxDbiQ921J4.
PRIDEiQ921J4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000079496; ENSMUSP00000078459; ENSMUSG00000060860.
GeneIDi77891.
KEGGimmu:77891.
UCSCiuc009eyt.1. mouse.

Organism-specific databases

CTDi27338.
MGIiMGI:1925141. Ube2s.

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110565.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ921J4.
KOiK10583.
OMAiGHKGEIC.
OrthoDBiEOG73JKXD.
PhylomeDBiQ921J4.
TreeFamiTF101120.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

NextBioi347761.
PROiQ921J4.
SOURCEiSearch...

Gene expression databases

BgeeiQ921J4.
CleanExiMM_UBE2S.
GenevestigatoriQ921J4.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and Czech II.
    Tissue: Mammary gland.

Entry informationi

Entry nameiUBE2S_MOUSE
AccessioniPrimary (citable) accession number: Q921J4
Secondary accession number(s): Q3U4V7, Q8CF67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 9, 2002
Last sequence update: November 30, 2001
Last modified: March 31, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.