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Q969T4

- UB2E3_HUMAN

UniProt

Q969T4 - UB2E3_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 E3

Gene

UBE2E3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (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. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest.2 Publications

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei145 – 1451Glycyl 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. protein K11-linked ubiquitination Source: UniProtKB
    2. protein K48-linked ubiquitination Source: UniProtKB
    3. protein K63-linked ubiquitination Source: UniProtKB
    4. regulation of growth Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Growth regulation, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiQ969T4.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 E3 (EC:6.3.2.19)
    Alternative name(s):
    UbcH9
    Ubiquitin carrier protein E3
    Ubiquitin-conjugating enzyme E2-23 kDa
    Ubiquitin-protein ligase E3
    Gene namesi
    Name:UBE2E3
    Synonyms:UBCE4, UBCH9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:12479. UBE2E3.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Shuttles between the nucleus and cytoplasm in a IPO11-dependent manner.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi145 – 1451C → S: Loss of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA37129.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 207206Ubiquitin-conjugating enzyme E2 E3PRO_0000082474Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei8 – 81Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ969T4.
    PaxDbiQ969T4.
    PRIDEiQ969T4.

    PTM databases

    PhosphoSiteiQ969T4.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed at low levels. Highly expressed in skeletal muscle.1 Publication

    Gene expression databases

    BgeeiQ969T4.
    CleanExiHS_UBE2E3.
    GenevestigatoriQ969T4.

    Organism-specific databases

    HPAiHPA003303.
    HPA030445.

    Interactioni

    Subunit structurei

    The ubiquitin-loaded form interacts specifically with importin-11 (IPO11), leading to its import into the nucleus By similarity. Interacts with NEDD4L.By similarity

    Protein-protein interaction databases

    BioGridi115740. 78 interactions.
    IntActiQ969T4. 55 interactions.
    MINTiMINT-1035070.
    STRINGi9606.ENSP00000307109.

    Structurei

    3D structure databases

    ProteinModelPortaliQ969T4.
    SMRiQ969T4. Positions 60-207.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    HOGENOMiHOG000233455.
    HOVERGENiHBG063308.
    KOiK06689.
    OMAiAKPNPKM.
    OrthoDBiEOG7PCJGX.
    PhylomeDBiQ969T4.
    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.

    Q969T4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSDRQRSDD ESPSTSSGSS DADQRDPAAP EPEEQEERKP SATQQKKNTK    50
    LSSKTTAKLS TSAKRIQKEL AEITLDPPPN CSAGPKGDNI YEWRSTILGP 100
    PGSVYEGGVF FLDITFSSDY PFKPPKVTFR TRIYHCNINS QGVICLDILK 150
    DNWSPALTIS KVLLSICSLL TDCNPADPLV GSIATQYLTN RAEHDRIARQ 200
    WTKRYAT 207
    Length:207
    Mass (Da):22,913
    Last modified:December 1, 2001 - v1
    Checksum:i821CB1382478DC9F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651R → K in AAP97266. 1 PublicationCurated
    Sequence conflicti91 – 911Y → C in AAP97266. 1 PublicationCurated
    Sequence conflicti101 – 1011P → L in AAP97266. 1 PublicationCurated
    Sequence conflicti134 – 1341Y → D in AAP97266. 1 PublicationCurated
    Sequence conflicti159 – 1591I → V in AAP97266. 1 PublicationCurated
    Sequence conflicti171 – 1711T → M in AAP97266. 1 PublicationCurated
    Sequence conflicti176 – 1761A → V in AAP97266. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti201 – 2011W → R.1 Publication
    Corresponds to variant rs2368192 [ dbSNP | Ensembl ].
    VAR_023392

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017644 mRNA. Translation: BAA76544.1.
    AF085362 mRNA. Translation: AAD40197.1.
    AF136176 mRNA. Translation: AAP97266.1.
    BT019345 mRNA. Translation: AAV38152.1.
    AK314145 mRNA. Translation: BAG36833.1.
    AC104076 Genomic DNA. Translation: AAY14882.1.
    CH471058 Genomic DNA. Translation: EAX10989.1.
    CH471058 Genomic DNA. Translation: EAX10990.1.
    BC003554 mRNA. Translation: AAH03554.1.
    BC092407 mRNA. Translation: AAH92407.1.
    CCDSiCCDS2282.1.
    RefSeqiNP_001265483.1. NM_001278554.1.
    NP_001265484.1. NM_001278555.1.
    NP_006348.1. NM_006357.3.
    NP_872619.1. NM_182678.2.
    XP_005246301.1. XM_005246244.2.
    UniGeneiHs.470804.
    Hs.567831.

    Genome annotation databases

    EnsembliENST00000392415; ENSP00000376215; ENSG00000170035.
    ENST00000410062; ENSP00000386788; ENSG00000170035.
    ENST00000602710; ENSP00000473623; ENSG00000170035.
    ENST00000602959; ENSP00000473639; ENSG00000170035.
    GeneIDi10477.
    KEGGihsa:10477.
    UCSCiuc002unq.1. human.

    Polymorphism databases

    DMDMi47606197.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017644 mRNA. Translation: BAA76544.1 .
    AF085362 mRNA. Translation: AAD40197.1 .
    AF136176 mRNA. Translation: AAP97266.1 .
    BT019345 mRNA. Translation: AAV38152.1 .
    AK314145 mRNA. Translation: BAG36833.1 .
    AC104076 Genomic DNA. Translation: AAY14882.1 .
    CH471058 Genomic DNA. Translation: EAX10989.1 .
    CH471058 Genomic DNA. Translation: EAX10990.1 .
    BC003554 mRNA. Translation: AAH03554.1 .
    BC092407 mRNA. Translation: AAH92407.1 .
    CCDSi CCDS2282.1.
    RefSeqi NP_001265483.1. NM_001278554.1.
    NP_001265484.1. NM_001278555.1.
    NP_006348.1. NM_006357.3.
    NP_872619.1. NM_182678.2.
    XP_005246301.1. XM_005246244.2.
    UniGenei Hs.470804.
    Hs.567831.

    3D structure databases

    ProteinModelPortali Q969T4.
    SMRi Q969T4. Positions 60-207.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115740. 78 interactions.
    IntActi Q969T4. 55 interactions.
    MINTi MINT-1035070.
    STRINGi 9606.ENSP00000307109.

    PTM databases

    PhosphoSitei Q969T4.

    Polymorphism databases

    DMDMi 47606197.

    Proteomic databases

    MaxQBi Q969T4.
    PaxDbi Q969T4.
    PRIDEi Q969T4.

    Protocols and materials databases

    DNASUi 10477.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000392415 ; ENSP00000376215 ; ENSG00000170035 .
    ENST00000410062 ; ENSP00000386788 ; ENSG00000170035 .
    ENST00000602710 ; ENSP00000473623 ; ENSG00000170035 .
    ENST00000602959 ; ENSP00000473639 ; ENSG00000170035 .
    GeneIDi 10477.
    KEGGi hsa:10477.
    UCSCi uc002unq.1. human.

    Organism-specific databases

    CTDi 10477.
    GeneCardsi GC02P181809.
    H-InvDB HIX0056142.
    HGNCi HGNC:12479. UBE2E3.
    HPAi HPA003303.
    HPA030445.
    MIMi 604151. gene.
    neXtProti NX_Q969T4.
    PharmGKBi PA37129.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233455.
    HOVERGENi HBG063308.
    KOi K06689.
    OMAi AKPNPKM.
    OrthoDBi EOG7PCJGX.
    PhylomeDBi Q969T4.
    TreeFami TF101117.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q969T4.

    Miscellaneous databases

    ChiTaRSi UBE2E3. human.
    GeneWikii UBE2E3.
    GenomeRNAii 10477.
    NextBioi 39740.
    PROi Q969T4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q969T4.
    CleanExi HS_UBE2E3.
    Genevestigatori Q969T4.

    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 UBE2E3 (alias UbcH9), encoding an N-terminally extended human ubiquitin-conjugating enzyme."
      Ito K., Kato S., Matsuda Y., Kimura M., Okano Y.
      Cytogenet. Cell Genet. 84:99-104(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, MUTAGENESIS OF CYS-145.
      Tissue: Gastric adenocarcinoma.
    2. "Human UbcM2 gene, complete cds."
      Shen Y., Ye M., Fu G., Zhou J., Zhang Q., Huang Q., Xu S., He K., Chen S., Mao M., Chen Z.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Umbilical cord blood.
    3. "Cloning of a new human cDNA homologous to Mus musculus ubiquitin-conjugating enzyme UbcM2."
      Xin Y.R., Yu L., Zhao S.Y.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-201.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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].
    6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Lung and PNS.
    9. "Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import."
      Plafker S.M., Plafker K.S., Weissman A.M., Macara I.G.
      J. Cell Biol. 167:649-659(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "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].
    11. "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.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUB2E3_HUMAN
    AccessioniPrimary (citable) accession number: Q969T4
    Secondary accession number(s): B2RAD6
    , D3DPG3, Q5U0R7, Q7Z4W4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 125 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3