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Q16763 (UBE2S_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:UBE2S
Synonyms:E2EPF
ORF Names:OK/SW-cl.73
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.5 Ref.8 Ref.9 Ref.10 Ref.11

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine. Ref.8 Ref.9

Pathway

Protein modification; protein ubiquitination. Ref.8 Ref.9

Subunit structure

Component of the APC/C complex. Interacts with CDC20, FZR1/CDH1 and VHL. Ref.5 Ref.9

Post-translational modification

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

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Ubl conjugation pathway
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of anaphase-promoting complex activity

Inferred from direct assay Ref.8Ref.9. Source: UniProtKB

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.8Ref.9. Source: UniProtKB

cellular protein modification process

Traceable author statement Ref.1. Source: ProtInc

exit from mitosis

Inferred from direct assay Ref.8. Source: UniProtKB

free ubiquitin chain polymerization

Inferred from direct assay Ref.9. Source: UniProtKB

protein K11-linked ubiquitination

Inferred from direct assay Ref.9Ref.10Ref.11. Source: UniProtKB

protein K27-linked ubiquitination

Inferred from direct assay Ref.10. Source: UniProtKB

protein K29-linked ubiquitination

Inferred from direct assay Ref.10. Source: UniProtKB

protein K6-linked ubiquitination

Inferred from direct assay Ref.10. Source: UniProtKB

protein K63-linked ubiquitination

Inferred from direct assay Ref.10. Source: UniProtKB

   Cellular_componentanaphase-promoting complex

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein ligase activity

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 222222Ubiquitin-conjugating enzyme E2 S
PRO_0000082507

Sites

Active site951Glycyl thioester intermediate

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7

Experimental info

Mutagenesis951C → S: Loss of function. Ref.9 Ref.11
Sequence conflict2161K → KRAL in AAA58446. Ref.1

Secondary structure

............................ 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16763 [UniParc].

Last modified October 10, 2002. Version 2.
Checksum: 2842DC3DCD2AFCB5

FASTA22223,845
        10         20         30         40         50         60 
MNSNVENLPP HIIRLVYKEV TTLTADPPDG IKVFPNEEDL TDLQVTIEGP EGTPYAGGLF 

        70         80         90        100        110        120 
RMKLLLGKDF PASPPKGYFL TKIFHPNVGA NGEICVNVLK RDWTAELGIR HVLLTIKCLL 

       130        140        150        160        170        180 
IHPNPESALN EEAGRLLLEN YEEYAARARL LTEIHGGAGG PSGRAEAGRA LASGTEASST 

       190        200        210        220 
DPGAPGGPGG AEGPMAKKHA GERDKKLAAK KKTDKKRALR RL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_055316.2. NM_014501.2.
UniGeneHs.396393.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZDNX-ray1.93A/B1-156[»]
ProteinModelPortalQ16763.
SMRQ16763. Positions 6-156.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118150. 42 interactions.
IntActQ16763. 6 interactions.
MINTMINT-6774405.
STRING9606.ENSP00000264552.

PTM databases

PhosphoSiteQ16763.

Polymorphism databases

DMDM23829978.

Proteomic databases

PaxDbQ16763.
PeptideAtlasQ16763.
PRIDEQ16763.

Protocols and materials databases

DNASU27338.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264552; ENSP00000264552; ENSG00000108106.
GeneID27338.
KEGGhsa:27338.
UCSCuc002qkx.1. human.

Organism-specific databases

CTD27338.
GeneCardsGC19M055912.
H-InvDBHIX0039201.
HGNCHGNC:17895. UBE2S.
HPACAB015228.
HPA041197.
HPA057150.
MIM610309. gene.
neXtProtNX_Q16763.
PharmGKBPA134904441.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233455.
HOVERGENHBG063308.
InParanoidQ16763.
KOK10583.
OrthoDBEOG73JKXD.
PhylomeDBQ16763.
TreeFamTF101120.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ16763.
UniPathwayUPA00143.

Gene expression databases

BgeeQ16763.
CleanExHS_UBE2S.
GenevestigatorQ16763.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ16763.
GenomeRNAi27338.
NextBio50400.
PROQ16763.
SOURCESearch...

Entry information

Entry nameUBE2S_HUMAN
AccessionPrimary (citable) accession number: Q16763
Secondary accession number(s): Q9BTC1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 10, 2002
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM