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Q96LR5

- UB2E2_HUMAN

UniProt

Q96LR5 - UB2E2_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 E2

Gene

UBE2E2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Catalyzes the ISGylation of influenza A virus NS1 protein.3 Publications

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei139 – 1391Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ISG15 ligase activity Source: HGNC
    3. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. ISG15-protein conjugation Source: HGNC
    2. protein K11-linked ubiquitination Source: UniProtKB
    3. protein K48-linked ubiquitination Source: UniProtKB
    4. protein K63-linked ubiquitination Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiQ96LR5.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 E2 (EC:6.3.2.19)
    Alternative name(s):
    UbcH8
    Ubiquitin carrier protein E2
    Ubiquitin-protein ligase E2
    Gene namesi
    Name:UBE2E2
    Synonyms:UBCH8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:12478. UBE2E2.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37128.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 201200Ubiquitin-conjugating enzyme E2 E2PRO_0000082472Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei19 – 191Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96LR5.
    PRIDEiQ96LR5.

    PTM databases

    PhosphoSiteiQ96LR5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96LR5.
    BgeeiQ96LR5.
    CleanExiHS_UBE2E2.
    GenevestigatoriQ96LR5.

    Organism-specific databases

    HPAiHPA003303.
    HPA028872.
    HPA030445.

    Interactioni

    Protein-protein interaction databases

    BioGridi113173. 63 interactions.
    DIPiDIP-52704N.
    IntActiQ96LR5. 37 interactions.
    STRINGi9606.ENSP00000379931.

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi55 – 6915
    Beta strandi75 – 828
    Beta strandi86 – 927
    Turni98 – 1014
    Beta strandi103 – 1097
    Turni112 – 1154
    Beta strandi120 – 1256
    Helixi141 – 1433
    Turni144 – 1463
    Helixi153 – 16513
    Helixi175 – 1839
    Helixi185 – 19915

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Y6LX-ray1.85A/B/C55-201[»]
    ProteinModelPortaliQ96LR5.
    SMRiQ96LR5. Positions 54-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96LR5.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000233455.
    HOVERGENiHBG063308.
    InParanoidiQ96LR5.
    KOiK06689.
    OMAiCNINSHG.
    OrthoDBiEOG7PCJGX.
    PhylomeDBiQ96LR5.
    TreeFamiTF101117.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q96LR5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTEAQRVDD SPSTSGGSSD GDQRESVQQE PEREQVQPKK KEGKISSKTA    50
    AKLSTSAKRI QKELAEITLD PPPNCSAGPK GDNIYEWRST ILGPPGSVYE 100
    GGVFFLDITF SPDYPFKPPK VTFRTRIYHC NINSQGVICL DILKDNWSPA 150
    LTISKVLLSI CSLLTDCNPA DPLVGSIATQ YMTNRAEHDR MARQWTKRYA 200
    T 201
    Length:201
    Mass (Da):22,255
    Last modified:December 1, 2001 - v1
    Checksum:i3286FB51E2B9CD3E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK057886 mRNA. Translation: BAB71605.1.
    BC022332 mRNA. Translation: AAH22332.1.
    CCDSiCCDS2637.1.
    RefSeqiNP_689866.1. NM_152653.3.
    XP_005265489.1. XM_005265432.1.
    UniGeneiHs.475688.
    Hs.595802.

    Genome annotation databases

    EnsembliENST00000396703; ENSP00000379931; ENSG00000182247.
    ENST00000425792; ENSP00000401053; ENSG00000182247.
    GeneIDi7325.
    KEGGihsa:7325.
    UCSCiuc003ccg.2. human.

    Polymorphism databases

    DMDMi47606201.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK057886 mRNA. Translation: BAB71605.1 .
    BC022332 mRNA. Translation: AAH22332.1 .
    CCDSi CCDS2637.1.
    RefSeqi NP_689866.1. NM_152653.3.
    XP_005265489.1. XM_005265432.1.
    UniGenei Hs.475688.
    Hs.595802.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Y6L X-ray 1.85 A/B/C 55-201 [» ]
    ProteinModelPortali Q96LR5.
    SMRi Q96LR5. Positions 54-201.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113173. 63 interactions.
    DIPi DIP-52704N.
    IntActi Q96LR5. 37 interactions.
    STRINGi 9606.ENSP00000379931.

    PTM databases

    PhosphoSitei Q96LR5.

    Polymorphism databases

    DMDMi 47606201.

    Proteomic databases

    MaxQBi Q96LR5.
    PRIDEi Q96LR5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000396703 ; ENSP00000379931 ; ENSG00000182247 .
    ENST00000425792 ; ENSP00000401053 ; ENSG00000182247 .
    GeneIDi 7325.
    KEGGi hsa:7325.
    UCSCi uc003ccg.2. human.

    Organism-specific databases

    CTDi 7325.
    GeneCardsi GC03P023221.
    HGNCi HGNC:12478. UBE2E2.
    HPAi HPA003303.
    HPA028872.
    HPA030445.
    MIMi 602163. gene.
    neXtProti NX_Q96LR5.
    PharmGKBi PA37128.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000233455.
    HOVERGENi HBG063308.
    InParanoidi Q96LR5.
    KOi K06689.
    OMAi CNINSHG.
    OrthoDBi EOG7PCJGX.
    PhylomeDBi Q96LR5.
    TreeFami TF101117.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q96LR5.

    Miscellaneous databases

    ChiTaRSi UBE2E2. human.
    EvolutionaryTracei Q96LR5.
    GeneWikii UBE2E2.
    GenomeRNAii 7325.
    NextBioi 28662.
    PROi Q96LR5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96LR5.
    Bgeei Q96LR5.
    CleanExi HS_UBE2E2.
    Genevestigatori Q96LR5.

    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, characterization, and chromosome mapping of UBE2E2 encoding a human ubiquitin-conjugating E2 enzyme."
      Kimura M., Hattori T., Matsuda Y., Yoshioka T., Sumi N., Umeda Y., Nakashima S., Okano Y.
      Cytogenet. Cell Genet. 78:107-111(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "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: Prostate.
    4. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    5. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    6. "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.
    7. "ISG15 conjugation system targets the viral NS1 protein in influenza A virus-infected cells."
      Zhao C., Hsiang T.Y., Kuo R.L., Krug R.M.
      Proc. Natl. Acad. Sci. U.S.A. 107:2253-2258(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUB2E2_HUMAN
    AccessioniPrimary (citable) accession number: Q96LR5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 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 3
      Human chromosome 3: 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