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Q16763

- UBE2S_HUMAN

UniProt

Q16763 - UBE2S_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 S

Gene

UBE2S

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (10 Oct 2002)
      Previous versions | rss
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    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. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    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 K63-linked ubiquitination Source: UniProtKB
    10. protein K6-linked ubiquitination Source: UniProtKB

    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

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

    Structurei

    Secondary structure

    1
    222
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16763.

    Family & Domainsi

    Sequence similaritiesi

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

    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

    Experimental Info

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

    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. 44 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

    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: October 1, 2014
    This is version 141 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