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Protein

Ubiquitin-conjugating enzyme E2 S

Gene

UBE2S

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.5 Publications

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.2 PublicationsPROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei95 – 951Glycyl thioester intermediate

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. small conjugating protein transferase activity Source: GO_Central
  4. ubiquitin conjugating enzyme activity Source: MGI
  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. cellular protein modification process Source: ProtInc
  5. exit from mitosis Source: UniProtKB
  6. free ubiquitin chain polymerization Source: UniProtKB
  7. protein K11-linked ubiquitination Source: UniProtKB
  8. protein K27-linked ubiquitination Source: UniProtKB
  9. protein K29-linked ubiquitination Source: UniProtKB
  10. protein K63-linked ubiquitination Source: UniProtKB
  11. protein K6-linked ubiquitination Source: UniProtKB
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

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ16763.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 S (EC:6.3.2.19)
Alternative name(s):
E2-EPF
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
ORF Names:OK/SW-cl.73
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:17895. UBE2S.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi95 – 951C → S: Loss of function. 2 Publications

Organism-specific databases

PharmGKBiPA134904441.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Ubiquitin-conjugating enzyme E2 SPRO_0000082507Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Post-translational modificationi

Autoubiquitinated by the APC/C complex during G1, leading to its degradation by the proteasome.1 Publication

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiQ16763.
PaxDbiQ16763.
PeptideAtlasiQ16763.
PRIDEiQ16763.

PTM databases

PhosphoSiteiQ16763.

Expressioni

Gene expression databases

BgeeiQ16763.
CleanExiHS_UBE2S.
ExpressionAtlasiQ16763. baseline.
GenevestigatoriQ16763.

Organism-specific databases

HPAiCAB015228.
HPA057150.

Interactioni

Subunit structurei

Component of the APC/C complex. Interacts with CDC20, FZR1/CDH1 and VHL.2 Publications

Protein-protein interaction databases

BioGridi118150. 51 interactions.
DIPiDIP-52784N.
IntActiQ16763. 7 interactions.
MINTiMINT-6774405.
STRINGi9606.ENSP00000264552.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2516Combined sources
Beta strandi31 – 355Combined sources
Beta strandi42 – 487Combined sources
Turni54 – 574Combined sources
Beta strandi59 – 657Combined sources
Turni68 – 725Combined sources
Beta strandi76 – 816Combined sources
Beta strandi92 – 943Combined sources
Helixi96 – 994Combined sources
Turni100 – 1023Combined sources
Helixi109 – 12113Combined sources
Helixi125 – 1273Combined sources
Helixi131 – 1399Combined sources
Helixi141 – 15515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZDNX-ray1.93A/B1-156[»]
ProteinModelPortaliQ16763.
SMRiQ16763. Positions 6-156.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16763.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110565.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ16763.
KOiK10583.
OrthoDBiEOG73JKXD.
PhylomeDBiQ16763.
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.

Q16763-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSNVENLPP HIIRLVYKEV TTLTADPPDG IKVFPNEEDL TDLQVTIEGP
60 70 80 90 100
EGTPYAGGLF RMKLLLGKDF PASPPKGYFL TKIFHPNVGA NGEICVNVLK
110 120 130 140 150
RDWTAELGIR HVLLTIKCLL IHPNPESALN EEAGRLLLEN YEEYAARARL
160 170 180 190 200
LTEIHGGAGG PSGRAEAGRA LASGTEASST DPGAPGGPGG AEGPMAKKHA
210 220
GERDKKLAAK KKTDKKRALR RL
Length:222
Mass (Da):23,845
Last modified:October 10, 2002 - v2
Checksum:i2842DC3DCD2AFCB5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti216 – 2161K → KRAL in AAA58446 (PubMed:1379239).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91670 mRNA. Translation: AAA58446.1.
AB062397 mRNA. Translation: BAB93484.1.
AC020922 Genomic DNA. No translation available.
BC004236 mRNA. Translation: AAH04236.1.
BC007554 mRNA. Translation: AAH07554.1.
BC065364 mRNA. Translation: AAH65364.1.
CCDSiCCDS33114.1.
RefSeqiNP_055316.2. NM_014501.2.
UniGeneiHs.396393.

Genome annotation databases

EnsembliENST00000264552; ENSP00000264552; ENSG00000108106.
GeneIDi27338.
KEGGihsa:27338.
UCSCiuc002qkx.1. human.

Polymorphism databases

DMDMi23829978.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91670 mRNA. Translation: AAA58446.1.
AB062397 mRNA. Translation: BAB93484.1.
AC020922 Genomic DNA. No translation available.
BC004236 mRNA. Translation: AAH04236.1.
BC007554 mRNA. Translation: AAH07554.1.
BC065364 mRNA. Translation: AAH65364.1.
CCDSiCCDS33114.1.
RefSeqiNP_055316.2. NM_014501.2.
UniGeneiHs.396393.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZDNX-ray1.93A/B1-156[»]
ProteinModelPortaliQ16763.
SMRiQ16763. Positions 6-156.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118150. 51 interactions.
DIPiDIP-52784N.
IntActiQ16763. 7 interactions.
MINTiMINT-6774405.
STRINGi9606.ENSP00000264552.

PTM databases

PhosphoSiteiQ16763.

Polymorphism databases

DMDMi23829978.

Proteomic databases

MaxQBiQ16763.
PaxDbiQ16763.
PeptideAtlasiQ16763.
PRIDEiQ16763.

Protocols and materials databases

DNASUi27338.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264552; ENSP00000264552; ENSG00000108106.
GeneIDi27338.
KEGGihsa:27338.
UCSCiuc002qkx.1. human.

Organism-specific databases

CTDi27338.
GeneCardsiGC19M055912.
H-InvDBHIX0039201.
HGNCiHGNC:17895. UBE2S.
HPAiCAB015228.
HPA057150.
MIMi610309. gene.
neXtProtiNX_Q16763.
PharmGKBiPA134904441.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110565.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ16763.
KOiK10583.
OrthoDBiEOG73JKXD.
PhylomeDBiQ16763.
TreeFamiTF101120.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ16763.

Miscellaneous databases

ChiTaRSiUBE2S. human.
EvolutionaryTraceiQ16763.
GenomeRNAii27338.
NextBioi50400.
PROiQ16763.
SOURCEiSearch...

Gene expression databases

BgeeiQ16763.
CleanExiHS_UBE2S.
ExpressionAtlasiQ16763. baseline.
GenevestigatoriQ16763.

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

« Hide 'large scale' publications
  1. "cDNA cloning of a novel human ubiquitin carrier protein. An antigenic domain specifically recognized by endemic pemphigus foliaceus autoantibodies is encoded in a secondary reading frame of this human epidermal transcript."
    Liu Z., Diaz L.A., Haas A.L., Giudice G.J.
    J. Biol. Chem. 267:15829-15835(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Foreskin.
  2. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
    Shichijo S., Itoh K.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon adenocarcinoma.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Colon and Skin.
  5. "E2-EPF UCP targets pVHL for degradation and associates with tumor growth and metastasis."
    Jung C.R., Hwang K.S., Yoo J., Cho W.K., Kim J.M., Kim W.H., Im D.S.
    Nat. Med. 12:809-816(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VHL.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "UBE2S elongates ubiquitin chains on APC/C substrates to promote mitotic exit."
    Garnett M.J., Mansfeld J., Godwin C., Matsusaka T., Wu J., Russell P., Pines J., Venkitaraman A.R.
    Nat. Cell Biol. 11:1363-1369(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
  9. "Identification of a physiological E2 module for the human anaphase-promoting complex."
    Williamson A., Wickliffe K.E., Mellone B.G., Song L., Karpen G.H., Rape M.
    Proc. Natl. Acad. Sci. U.S.A. 106:18213-18218(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH CDC20 AND FZR, UBIQUITINATION, MUTAGENESIS OF CYS-95.
  10. "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.
  11. "Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne."
    Bremm A., Freund S.M., Komander D.
    Nat. Struct. Mol. Biol. 17:939-947(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-95.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Crystal structure of human ubiquitin-conjugating enzyme E2S."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 1-156.

Entry informationi

Entry nameiUBE2S_HUMAN
AccessioniPrimary (citable) accession number: Q16763
Secondary accession number(s): Q9BTC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 10, 2002
Last modified: March 4, 2015
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.