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Q16763

- UBE2S_HUMAN

UniProt

Q16763 - UBE2S_HUMAN

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Protein
Ubiquitin-conjugating enzyme E2 S
Gene
UBE2S, E2EPF, OK/SW-cl.73
Organism
Homo sapiens (Human)
Status
Reviewed - 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 Publications

Pathwayi

Sites

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. acid-amino acid ligase activity Source: InterPro
  3. 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. cellular protein modification process Source: ProtInc
  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 K6-linked ubiquitination Source: UniProtKB
  10. protein K63-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
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 S
PRO_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.

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiQ16763.
PaxDbiQ16763.
PeptideAtlasiQ16763.
PRIDEiQ16763.

PTM databases

PhosphoSiteiQ16763.

Expressioni

Gene expression databases

BgeeiQ16763.
CleanExiHS_UBE2S.
GenevestigatoriQ16763.

Organism-specific databases

HPAiCAB015228.
HPA041197.
HPA057150.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi118150. 42 interactions.
DIPiDIP-52784N.
IntActiQ16763. 6 interactions.
MINTiMINT-6774405.
STRINGi9606.ENSP00000264552.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZDNX-ray1.93A/B1-156[»]
ProteinModelPortaliQ16763.
SMRiQ16763. Positions 6-156.

Miscellaneous databases

EvolutionaryTraceiQ16763.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5078.
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

MNSNVENLPP HIIRLVYKEV TTLTADPPDG IKVFPNEEDL TDLQVTIEGP    50
EGTPYAGGLF RMKLLLGKDF PASPPKGYFL TKIFHPNVGA NGEICVNVLK 100
RDWTAELGIR HVLLTIKCLL IHPNPESALN EEAGRLLLEN YEEYAARARL 150
LTEIHGGAGG PSGRAEAGRA LASGTEASST DPGAPGGPGG AEGPMAKKHA 200
GERDKKLAAK KKTDKKRALR RL 222
Length:222
Mass (Da):23,845
Last modified:October 10, 2002 - v2
Checksum:i2842DC3DCD2AFCB5
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti216 – 2161K → KRAL in AAA58446. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS33114.1.
RefSeqi NP_055316.2. NM_014501.2.
UniGenei Hs.396393.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZDN X-ray 1.93 A/B 1-156 [» ]
ProteinModelPortali Q16763.
SMRi Q16763. Positions 6-156.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118150. 42 interactions.
DIPi DIP-52784N.
IntActi Q16763. 6 interactions.
MINTi MINT-6774405.
STRINGi 9606.ENSP00000264552.

PTM databases

PhosphoSitei Q16763.

Polymorphism databases

DMDMi 23829978.

Proteomic databases

MaxQBi Q16763.
PaxDbi Q16763.
PeptideAtlasi Q16763.
PRIDEi Q16763.

Protocols and materials databases

DNASUi 27338.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264552 ; ENSP00000264552 ; ENSG00000108106 .
GeneIDi 27338.
KEGGi hsa:27338.
UCSCi uc002qkx.1. human.

Organism-specific databases

CTDi 27338.
GeneCardsi GC19M055912.
H-InvDB HIX0039201.
HGNCi HGNC:17895. UBE2S.
HPAi CAB015228.
HPA041197.
HPA057150.
MIMi 610309. gene.
neXtProti NX_Q16763.
PharmGKBi PA134904441.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5078.
HOGENOMi HOG000233455.
HOVERGENi HBG063308.
InParanoidi Q16763.
KOi K10583.
OrthoDBi EOG73JKXD.
PhylomeDBi Q16763.
TreeFami TF101120.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinki Q16763.

Miscellaneous databases

EvolutionaryTracei Q16763.
GenomeRNAii 27338.
NextBioi 50400.
PROi Q16763.
SOURCEi Search...

Gene expression databases

Bgeei Q16763.
CleanExi HS_UBE2S.
Genevestigatori Q16763.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 140 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

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